Sf_category,Sf_framecode,Entry_ID,Sf_ID,ID,Name,Class,CAS_abstract_code,MEDLINE_UI_code,PubMed_ID,DOI,Full_citation,Title,Status,Type,Journal_abbrev,Journal_name_full,Journal_volume,Journal_issue,Journal_ASTM,Journal_ISSN,Journal_CSD,Book_title,Book_chapter_title,Book_volume,Book_series,Book_publisher,Book_publisher_city,Book_ISBN,Conference_title,Conference_site,Conference_state_province,Conference_country,Conference_start_date,Conference_end_date,Conference_abstract_number,Thesis_institution,Thesis_institution_city,Thesis_institution_country,WWW_URL,Page_first,Page_last,Year,Details citations,entry_citation,1000,2,1,,entry citation,,,,,"Roy, Melinda, Lee, Robert W.-K., Kaarsholm, Niels C., Thogersen, Henning, Brange, Jens, Dunn, M.F., ""Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin,"" Biochim. Biophys. Acta 1053, 63-73 (1990).","Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin",published,journal,Biochim. Biophys. Acta,,1053,,,,,,,,,,,,,,,,,,,,,,,63,73,1990, citations,citation_1,10001,16,1,,entry citation,,,16714348,,,"Structure of Tightly Membrane-Bound Mastoparan-X, a G-protein-Activating Peptide, Determined by Solid-State NMR",published,journal,Biophys. J.,Biophys. Journal,91,4,,,,,,,,,,,,,,,,,,,,,,1368,1379,2006, citations,citation_2,10001,17,2,,reference citation,,,12810033,,,Chemical shift referencing in MAS solid state NMR.,published,journal,J. Magn. Reson.,Journal of Magnetic Resonance,162,2,,,,,,,,,,,,,,,,,,,,,,479,486,2003, citations,TSR_article,10002,35,1,,entry citation,,,16736493,,,Solution structures of the first and fourth TSR domains of F-spondin,published,journal,Proteins,,64,3,,,,,,,,,,,,,,,,,,,,,,665,672,2006, citations,citation_1,10004,48,1,,entry citation,,,16456701,,,"1H, 13C and 15N resonance assignments of the 2'-5' RNA ligase-like protein from Pyrococcus furiosus",published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,16,16,2006, citations,citation_1,10005,73,1,,entry citation,,,16567413,,,"Identification of the Substrate Interaction Region of the Chitin-Binding Domain of Streptomyces griseus Chitinase C",published,journal,J. Biochem.,,139,3,,,,,,,,,,,,,,,,,,,,,,483,493,2006, citations,citation_1,10006,102,1,,entry citation,,,,,,Solution structure of fibronectin type III domain of mouse hypothetical protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10008,121,1,,entry citation,,,,,,"Solution structure of C-terminal fibronectin type III domain of mouse 1700129L13Rik protein",in preparation,journal,not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10009,140,1,,entry citation,,,,,,Solution structure of SH3 domain of mouse Kalirin-9a protein,in preparation,journal,not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1001,159,1,,entry citation,,,,,"Roy, Melinda, Lee, Robert W.-K., Kaarsholm, Niels C., Thogersen, Henning, Brange, Jens, Dunn, M.F., ""Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin,"" Biochim. Biophys. Acta 1053, 63-73 (1990).","Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin",published,journal,Biochim. Biophys. Acta,,1053,,,,,,,,,,,,,,,,,,,,,,,63,73,1990, citations,citation_1,10010,173,1,,entry citation,,,16368109,,,"Dynamics and Mechanism of the Tanford Transition of Bovine beta-Lactoglobulin Studied using Heteronuclear NMR Spectroscopy",published,journal,J. Mol. Biol.,,356,2,,,,,,,,,,,,,,,,,,,,,,483,496,2006, citations,citation_2,10010,174,2,,reference citation,,,9514124,,"Kim, T.-R., Goto, Y., Hirota, N., Kuwata, K., Denton, H., Wu, S.-Y., Sawyer, L., and Batt, C.A. (1997) High-level expression of bovine beta-lactoglobulin in Pichia pastoris and characterization of its physical properties. Protein Eng. 10:1339-1345.","High-level expression of bovine beta-lactoglobulin in Pichia pastoris and characterization of its physical properties.",published,journal,Protein Eng.,,10,11,,,,,,,,,,,,,,,,,,,,,,1339,1345,1997, citations,citation_3,10010,175,3,,reference citation,,,9790836,,"Kuwata, K., Hoshino, M., Era, S., Batt, C.A., and Goto, Y. (1998) alpha to beta Transition of beta-lactoglobulin as evidenced by heteronuclear NMR. J. Mol. Biol. 283: 731-739.",alpha to beta Transition of beta-lactoglobulin as evidenced by heteronuclear NMR.,published,journal,J. Mol. Biol.,,283,4,,,,,,,,,,,,,,,,,,,,,,731,739,1998, citations,citation_4,10010,176,4,,reference citation,,,9729790,,"Uhrinova, S., Uhrin, D., Denton, H., Smith, M., Sawyer, L., and Barlow, P.N. (1998) Complete assignment of 1H, 13C and 15N chemical shifts for bovine beta-lactoglobulin: Secondary structure and topology of the native state is retained in a partially unfolded form. J. Biomol. NMR 12: 89-107.","Complete assignment of 1H, 13C and 15N chemical shifts for bovine beta-lactoglobulin: Secondary structure and topology of the native state is retained in a partially unfolded form.",published,journal,J. Biomol. NMR,,12,1,,,,,,,,,,,,,,,,,,,,,,89,107,1998, citations,citation_1,10011,194,1,,entry citation,,,16531230,,,Solution structure of the SWIRM domain of human histone demethylase LSD1,published,journal,Structure,,14,3,,,,,,,,,,,,,,,,,,,,,,457,468,2006, citations,citation_1,10012,214,1,,entry citation,,,16061251,,,"Structural Basis for Ca(2+)-regulated Muscle Relaxation at Interaction Sites of Troponin with Actin and Tropomyosin",published,journal,J. Mol. Biol.,Journal of molecular biology,352,1,JMOBAK,0022-2836,0353,,,,,,,,,,,,,,,,,,,178,201,2005, citations,citation_1,10013,232,1,,entry citation,,,,,,Solution Structure of the RING Finger Domain of the Human KIAA1045 Protein,in preparation,journal,not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10014,253,1,,entry citation,,,16838833,,,"Solution structure of a GAAG tetraloop in helix 6 of SRP RNA from Pyrococcus furiosus",published,journal,Nucleos. Nucleot. Nucl.,"Nucleosides, Nucleotides & Nucleic Acids",25,4-6,,,,,,,,,,,,,,,,,,,,,,383,395,2006, citations,citation_1,10015,273,1,,entry citation,,,16672276,,,"Structural Analysis of a Mutant of the HIV-1 Integrase Zinc Finger Domain That Forms a Single Conformation",published,journal,J. Biochem. (Tokyo),,139,4,,,,,,,,,,,,,,,,,,,,,,753,759,2006, citations,citation_1,10016,297,1,,entry citation,,,16791740,,,"Heteronuclear multidimensional NMR and homology modelling studies of the C-terminal nucleotide-binding domain of the human mitochondrial ABC transporter ABCB6",published,journal,J. Biomol. NMR,,35,1,,,,,,,,,,,,,,,,,,,,,,53,71,2006, citations,citation_1,10017,321,1,,entry citation,,,16791740,,,"Heteronuclear multidimensional NMR and homology modelling studies of the C-terminal nucleotide-binding domain of the human mitochondrial ABC transporter ABCB6",published,journal,J. Biomol. NMR,,35,1,,,,,,,,,,,,,,,,,,,,,,53,71,2006, citations,citiation_1,10018,347,1,,entry citation,,,17000640,,,Solution structure and functional importance of a conserved RNA hairpin of eel LINE UnaL2,published,journal,Nucleic Acids Res.,,34,18,,,,,,,,,,,,,,,,,,,,,,5184,5193,2006, citations,1,10019,370,1,,entry citation,,,,,,"1H and 15N Assigned Chemical Shifts for GSPT1/eRF3a(PAM2-1) and 1H, 13C and 15N Assigned Chemical Shifts for PABC",in preparation,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1002,395,1,,entry citation,,,,,"Roy, Melinda, Lee, Robert W.-K., Kaarsholm, Niels C., Thogersen, Henning, Brange, Jens, Dunn, M.F., ""Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin,"" Biochim. Biophys. Acta 1053, 63-73 (1990).","Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin",published,journal,Biochim. Biophys. Acta,,1053,,,,,,,,,,,,,,,,,,,,,,,63,73,1990, citations,citation_1,10050,1015,1,,entry citation,,,,,,"Solution structure of N-terminal ubiquitin-like domain of human NEDD8 ultimate buster-1",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,16610,51671,1,,entry citation,,,,,,TBD,in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10021,409,1,,entry citation,,,17080295,,"Signal assignment and secondary structure analysis of a uniformly [13C, 15N]-labeled membrane protein, H +-ATP synthase subunit c, by magic-angle spinning solid-state NMR.","13C and 15N chemical shift assignment of H+-ATP synthase subunit c in the solid state",published,journal,J. Biomol. NMR,,36,4,,,,,,,,,,,,,,,,,,,,,,279,293,2006, citations,citation_1,10022,430,1,,entry citation,,,17108084,,,"3D Structure of amyloid protofibrils of beta2-microglobulin fragment probed by solid-state NMR",published,journal,Proc. Natl. Acad. Sci. U.S.A.,,103,48,,,,,,,,,,,,,,,,,,,,,,18119,18124,2006, citations,1,10023,451,1,,entry citation,,,17122952,,,"Resonance assignments of the alpha subunit of human eukaryotic initiation factor 2 (heIF2alpha)",published,journal,J. Biomol. NMR,,38,2,,,,,,,,,,,,,,,,,,,,,,173,173,2007, citations,citation_1,10024,472,1,,entry citation,,,17335288,,,"Solution structure of the Rhodobacter sphaeroides PufX membrane protein: implications for the quinone exchange and protein-protein interactions.",published,journal,Biochemistry,,46,12,,,,,,,,,,,,,,,,,,,,,,3635,3642,2007, citations,citation_1,10025,491,1,,entry citation,,,17075132,,,"Solution structure of the kinase-associated domain 1 of mouse microtubule-associated protein/microtubule affinity-regulating kinase 3",published,journal,Protein Sci.,Protein Science,15,11,,,,,,,,,,,,,,,,,,,,,,2534,2543,2006, citations,citation_1,10026,509,1,,entry citation,,,17075132,,,Solution structure of the kinase-associated domain 1 of mouse microtubule-associated protein/microtubule affinity-regulating kinase 3,published,journal,Protein Sci.,,15,11,,,,,,,,,,,,,,,,,,,,,,2534,2543,2006, citations,Citation_1,10027,528,1,,entry citation,,,19636826,,,"Assignment of 1H, 13C and 15N resonances of N-terminal domain of DnaA protein",published,journal,Biomol. NMR Assignments,,1,1,,,,,,,,,,,,,,,,,,,,,,57,59,2007, citations,citation_1,10028,557,1,,entry citation,,,17239860,,,"Solution structure of an atypical WW domain in a novel beta-clam-like dimeric form",published,journal,Febs Lett.,FEBS Letters,581,3,,,,,,,,,,,,,,,,,,,,,,462,468,2007, citations,citation_1,10029,575,1,,entry citation,,,,,,"Solution structure of the fifth PDZ domain of human membrane associated guanylate kinase inverted-2 (KIAA0705 protein)",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1003,594,1,,entry citation,,,,,"Roy, Melinda, Lee, Robert W.-K., Kaarsholm, Niels C., Thogersen, Henning, Brange, Jens, Dunn, M.F., ""Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin,"" Biochim. Biophys. Acta 1053, 63-73 (1990).","Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin",published,journal,Biochim. Biophys. Acta,,1053,,,,,,,,,,,,,,,,,,,,,,,63,73,1990, citations,citation_1,10030,607,1,,entry citation,,,,,,Solution structure of the forth CH domain from human plastin 3 T-isoform,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10031,626,1,,entry citation,,,,,,Solution structure of the 2nd mbt domain from human KIAA1617 protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10032,645,1,,entry citation,,,,,,Solution structure of the first mbt domain from human KIAA1798 protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10033,664,1,,entry citation,,,,,,Solution Structure of J-domain of mouse DnaJ like protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10034,683,1,,entry citation,,,,,,"Solution structure of Fibronectin type III domain derived from human KIAA0970 protein",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10035,702,1,,entry citation,,,,,,"Solution structure of Lectin C-type domain derived from a hypothetical protein from C. elegans",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10036,721,1,,entry citation,,,,,,Solution structure of mouse CGI-38 protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10037,740,1,,entry citation,,,,,,Solution structure of the third mbt domain from human KIAA1798 protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10038,759,1,,entry citation,,,,,,Solution structure of zf-C2H2 domains from human Zinc finger protein 295,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10039,780,1,,entry citation,,,,,,"Solution Structure of the Pleckstrin Homology Domain of Mouse Ethanol Decreased 4 Protein",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1004,799,1,,entry citation,,,,,"Roy, Melinda, Lee, Robert W.-K., Kaarsholm, Niels C., Thogersen, Henning, Brange, Jens, Dunn, M.F., ""Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin,"" Biochim. Biophys. Acta 1053, 63-73 (1990).","Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin",published,journal,Biochim. Biophys. Acta,,1053,,,,,,,,,,,,,,,,,,,,,,,63,73,1990, citations,citation_1,10040,812,1,,entry citation,,,,,,Solution Structure of the RA Domain of Human Grb7 Protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10041,831,1,,entry citation,,,,,,"Solution Structure of the Tudor Domain from Mouse Hypothetical Protein Homologous to Histone Acetyltransferase",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10042,850,1,,entry citation,,,,,,Solution Structure of the CS Domain of Human KIAA1068 Protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10043,869,1,,entry citation,,,,,,"Solution Structure of the N-terminal Domain of Mouse Putative Signal Recoginition Particle 54 (SRP54)",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10044,888,1,,entry citation,,,,,,"Solution structure of homeobox domain of Arabidopsisthaliana zinc finger homeobox family protein",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10045,907,1,,entry citation,,,,,,"Solution structure of homeobox domain of Arabidopsis thaliana hypothetical protein F22K18.140",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10046,926,1,,entry citation,,,,,,"Solution structure of the PB1 domain of mouse mitogen activated protein kinase kinase 5 (MAP2K5)",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10047,945,1,,entry citation,,,,,,"Solution Structure of the Homeobox Domain of Human Homeodomain Leucine Zipper-Encoding Gene (Homez)",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10048,964,1,,entry citation,,,,,,Solution Structure of the UBA Domain of Human Tudor Domain Containing Protein 3,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10049,983,1,,entry citation,,,,,,"Solution structure of the N-terminal Domain I of mouse transcription elongation factor S-II protein 3",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1005,1002,1,,entry citation,,,,,"Roy, Melinda, Lee, Robert W.-K., Kaarsholm, Niels C., Thogersen, Henning, Brange, Jens, Dunn, M.F., ""Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin,"" Biochim. Biophys. Acta 1053, 63-73 (1990).","Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin",published,journal,Biochim. Biophys. Acta,,1053,,,,,,,,,,,,,,,,,,,,,,,63,73,1990, citations,citation_1,10051,1034,1,,entry citation,,,17237976,,,Improving cell-free protein synthesis for stable-isotope labeling,published,journal,J. Biomol. NMR,,37,3,,,,,,,,,,,,,,,,,,,,,,225,229,2007, citations,citation_1,10052,1054,1,,entry citation,,,17309236,,,"Characterization of the denatured structure of pyrrolidone carboxyl peptidase from a hyperthermophile under non-denaturing conditions: Role of the C-terminal a-helix of the protein in folding and stability",published,journal,Biochemistry,,46,12,,,,,,,,,,,,,,,,,,,,,,3664,3672,2007, citations,citation_2,10052,1055,2,,reference citation,,,15362877,,,"Unusually slow denaturation and refolding processes of pyrrolidone carboxyl peptidase from a hyperthermophile are highly cooperative: Real-time NMR studies",published,journal,Biochemistry,,43,37,,,,,,,,,,,,,,,,,,,,,,11906,11915,2004, citations,citation_1,10053,1078,1,,entry citation,,,19636820,,,"Backbone 1H, 13C and 15N assignments of a 59 kDa Salmonella typhimurium periplasmic oligopeptide binding protein, OppA",published,journal,Biomol. NMR Assignments,,1,1,,,,,,,,,,,,,,,,,,,,,,37,39,2007, citations,citation_1,10054,1104,1,,entry citation,,,,,,"Solution structure of the first cold-shock domain of the human KIAA0885 protein (UNR protein)",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10055,1123,1,,entry citation,,,,,,Solution Structure of Glia Maturation Factor-gamma from Mus Musculus,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10056,1142,1,,entry citation,,,,,,Solution structure of the Ras-binding domain of mouse RGS14,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10057,1161,1,,entry citation,,,,,,Solution structure of Iron-sulfur cluster protein U (IscU),in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10058,1182,1,,entry citation,,,,,,"Solution Structure of the PICOT homology 2 domain of the mouse PKC-interacting cousin of thioredoxin protein",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10059,1201,1,,entry citation,,,,,,Solution Structure of the Band 7 Domain of the mouse Flotillin 2 Protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1006,1220,1,,entry citation,,,,,"Roy, Melinda, Lee, Robert W.-K., Kaarsholm, Niels C., Thogersen, Henning, Brange, Jens, Dunn, M.F., ""Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin,"" Biochim. Biophys. Acta 1053, 63-73 (1990).","Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin",published,journal,Biochim. Biophys. Acta,,1053,,,,,,,,,,,,,,,,,,,,,,,63,73,1990, citations,citation_1,10060,1233,1,,entry citation,,,,,,Solution structure of hypothetical protein C330018D20Rik from Mus musculus,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10061,1252,1,,entry citation,,,,,,Solution structure of PDZ domain of mouse Cypher protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10062,1271,1,,entry citation,,,17206147,,,"Direct interactions between Nedd8 and ubiquitin E2 conjugating enzymes upregulate cullin-based E3 ligase activity",published,journal,Nat. Struct. Mol. Biol.,,14,2,,,,,,,,,,,,,,,,,,,,,,167,168,2007, citations,citation_1,10063,1289,1,,entry citation,,,,,,Solution structure of the fourth SH3 domain of human intersectin 2 (KIAA1256),in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10064,1308,1,,entry citation,,,,,,"Solution Structure of The forth PDZ Domain of Human Atrophin-1 Interacting Protein 1 (KIAA0705 Protein)",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10065,1328,1,,entry citation,,,,,,"Solution structure of the SAND domain of the putative nuclear protein homolog (5830484A20Rik)",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10066,1347,1,,entry citation,,,,,,Solution structure of the third PDZ domain of human KIAA1526 protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10067,1366,1,,entry citation,,,,,,Solution Structure of The FHA Domain of Arabidopsis thaliana Hypothetical Protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10068,1385,1,,entry citation,,,,,,Solution Structure of the CH domain from Mouse Trangelin,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10069,1404,1,,entry citation,,,,,,"Solution structure of the Villin headpiece domain of human actin-binding LIM protein homologue (KIAA0843 protein)",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1007,1423,1,,entry citation,,,,,"Roy, Melinda, Lee, Robert W.-K., Kaarsholm, Niels C., Thogersen, Henning, Brange, Jens, Dunn, M.F., ""Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin,"" Biochim. Biophys. Acta 1053, 63-73 (1990).","Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin",published,journal,Biochim. Biophys. Acta,,1053,,,,,,,,,,,,,,,,,,,,,,,63,73,1990, citations,citation_1,10070,1436,1,,entry citation,,,,,,Solution structure of RRM domain in heterogeneous nuclear ribonucleoprotein H',in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10071,1455,1,,entry citation,,,,,,Solution structure of RRM domain in RNA-binding protein NP_057951,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10072,1474,1,,entry citation,,,,,,Solution structure of RRM domain in HNRPC protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10073,1493,1,,entry citation,,,,,,C2 domain-containing protein from putative elicitor-responsive gene,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10074,1513,1,,entry citation,,,,,,The first C2 domain of human synaptotagmin XIII,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10075,1532,1,,entry citation,,,,,,The fourth FN3 domain of human sidekick-2,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10076,1552,1,,entry citation,,,,,,The eighth FN3 domain of human sidekick-2,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10077,1571,1,,entry citation,,,,,,Solution structure of the RNA binding domain of eukaryotic initiation factor 4B,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10078,1592,1,,entry citation,,,19636845,,,Backbone resonance assignments for the periplasmic chaperone LolA from Escherichia coli,published,journal,Biomol. NMR Assignments,,1,1,,,,,,,,,,,,,,,,,,,,,,125,127,2007, citations,citation_1,10079,1615,1,,entry citation,,,,,,Solution structure of putative domain of human KIAA0561 protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1008,1634,1,,entry citation,,,,,"Roy, Melinda, Lee, Robert W.-K., Kaarsholm, Niels C., Thogersen, Henning, Brange, Jens, Dunn, M.F., ""Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin,"" Biochim. Biophys. Acta 1053, 63-73 (1990).","Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin",published,journal,Biochim. Biophys. Acta,,1053,,,,,,,,,,,,,,,,,,,,,,,63,73,1990, citations,citation_1,10080,1647,1,,entry citation,,,,,,Solution structure of mouse putative 42-9-9 protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10081,1666,1,,entry citation,,,,,,Solution structure of the PDZ domain of mouse Rhophilin-2,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10082,1685,1,,entry citation,,,,,,Solution structure of RRM domain in calcipressin 1,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10083,1704,1,,entry citation,,,,,,PDZ domain of human RIM2B,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10084,1723,1,,entry citation,,,,,,Nuclear move domain of nuclear distribution gene C homolog,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10085,1743,1,,entry citation,,,,,,"Solution structure of the first RRM domain in heterogeneous nuclear ribonucleoprotein H",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10086,1762,1,,entry citation,,,,,,RA domain of guanine nucleotide exchange factor for Rap1,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10087,1781,1,,entry citation,,,,,,"Solution structure of C-terminal ubiquitin like domain of human 2'-5'-oligoadenylate synthetase-like protain (p59 OASL)",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10088,1800,1,,entry citation,,,,,,Solution structure of the second PDZ domain of human scribble (KIAA0147 protein),in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10089,1819,1,,entry citation,,,,,,Solution structure of phosphotyrosine interaction domain of mouse Numb protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1009,1838,1,,entry citation,,,,,"Roy, Melinda, Lee, Robert W.-K., Kaarsholm, Niels C., Thogersen, Henning, Brange, Jens, Dunn, M.F., ""Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin,"" Biochim. Biophys. Acta 1053, 63-73 (1990).","Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin",published,journal,Biochim. Biophys. Acta,,1053,,,,,,,,,,,,,,,,,,,,,,,63,73,1990, citations,citation_1,10090,1851,1,,entry citation,,,,,,Solution structure of hypothetical protein F20O9.120 from Arabidopsis thaliana,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10091,1870,1,,entry citation,,,,,,"Solution structure of the C-terminal ubiquitin-like domain of mouse tubulin-specific chaperone e",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10092,1889,1,,entry citation,,,,,,"Solution structure of the DEATH domain of Interleukin-1 receptor-associated kinase4 (IRAK4) from Mus musculus",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10093,1909,1,,entry citation,,,,,,Solution structure of the second CUT domain of human Homeobox protein Cux-2,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10094,1929,1,,entry citation,,,,,,Solution structure of the third CUT domain of human Homeobox protein Cux-2,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10095,1949,1,,entry citation,,,,,,Solution structure of the KH domain of human ribosomal protein S3,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10096,1969,1,,entry citation,,,19636844,,,Backbone resonance assignment for the outer membrane lipoprotein receptor LolB from Escherichia coli,published,journal,Biomol. NMR Assignments,,1,1,,,,,,,,,,,,,,,,,,,,,,121,123,2007, citations,citation_1,10097,1990,1,,entry citation,,,,,,Solution Structure of the SH3 Domain Binding Glutamic Acid-rich Protein Like 3,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10098,2010,1,,entry citation,,,,,,Solution Structure of The C1 Domain of The Human Diacylglycerol Kinase Delta,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10099,2031,1,,entry citation,,,,,,"Solution Structure of the First Fibronectin Type III domain of human KIAA1568 Protein",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1010,2051,1,,entry citation,,,,,"Roy, Melinda, Lee, Robert W.-K., Kaarsholm, Niels C., Thogersen, Henning, Brange, Jens, Dunn, M.F., ""Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin,"" Biochim. Biophys. Acta 1053, 63-73 (1990).","Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin",published,journal,Biochim. Biophys. Acta,,1053,,,,,,,,,,,,,,,,,,,,,,,63,73,1990, citations,citation_1,10100,2064,1,,entry citation,,,,,,"Solution Structure of The Third PDZ Domain of Human Atrophin-1 Interacting Protein 1 (KIAA0705 Protein)",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10101,2084,1,,entry citation,,,,,,"Solution structure of four helical up-and-down bundle domain of the hypothetical protein 2610208M17Rik similar to the protein FLJ12806",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10102,2103,1,,entry citation,,,,,,"Solution structure of the second fibronectin Type III domain of human KIAA1568 protein",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10103,2125,1,,entry citation,,,,,,Solution structure of the fourth PDZ domain of human scribble (KIAA0147 protein),in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10104,2144,1,,entry citation,,,,,,"The forkhead associated (FHA) domain like structure from mouse polynucleotide kinase 3'-phosphatase",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10105,2162,1,,entry citation,,,,,,"Solution structure of the SWIB/MDM2 domain of the hypothetical protein At5g14170 from Arabidopsis thaliana",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10106,2181,1,,entry citation,,,,,,"Solution structure of the SWIB/MDM2 domain of the hypothetical protein At5g08430 from Arabidopsis thaliana",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10107,2200,1,,entry citation,,,,,,Solution structure of the CH domain from mouse EB-1,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10108,2219,1,,entry citation,,,,,,"Solution Structure of DC1 Domain of PDI-like Hypothetical Protein from Arabidopsis thaliana",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10109,2239,1,,entry citation,,,,,,"Solution Structure of the PDZ Domain from Mouse Glutamate Receptor Interacting Protein 1A-L (GRIP1) Homolog",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1011,2257,1,,entry citation,,,,,"Roy, Melinda, Lee, Robert W.-K., Kaarsholm, Niels C., Thogersen, Henning, Brange, Jens, Dunn, M.F., ""Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin,"" Biochim. Biophys. Acta 1053, 63-73 (1990).","Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin",published,journal,Biochim. Biophys. Acta,,1053,,,,,,,,,,,,,,,,,,,,,,,63,73,1990, citations,citation_1,10110,2270,1,,entry citation,,,,,,Solution Structure of the Gas2 Domain of the Growth Arrest Specific 2 Protein,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10111,2290,1,,entry citation,,,,,,Solution structure of the 6th HMG box of mouse UBF1,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10112,2308,1,,entry citation,,,,,,Solution structure of the ubiquitin domain from mouse D7Wsu128e protein,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10113,2326,1,,entry citation,,,,,,Solution Structure of the Pleckstrin Homology Domain of Mouse APS,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10114,2345,1,,entry citation,,,,,,"Solution Structure of the C-terminal Pleckstrin Homology Domain of Sbf1 from Mouse",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10115,2364,1,,entry citation,,,,,,"Solution Structure of the Pleckstrin Homology Domain of Oxysterol-Binding Protein-Related Protein 8 (KIAA1451 Protein)",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10116,2383,1,,entry citation,,,17979195,,,"The confirmation of the denatured structure of pyrrolidone carboxyl peptidase under nondenaturing conditions: difference in helix propensity of two synthetic peptides with single amino acid substitution.",published,journal,Proteins,,71,2,,,,,,,,,,,,,,,,,,,,,,737,742,2008, citations,citation_2,10116,2384,2,,reference citation,,,17309236,,,"Characterization of the denatured structure of pyrrolidone carboxyl peptidase from a hyperthermophile under nondenaturing conditions: role of the C-terminal alpha-helix of the protein in folding and stability.",published,journal,Biochemistry,,46,12,,,,,,,,,,,,,,,,,,,,,,3664,3672,2007, citations,citation_1,10117,2401,1,,entry citation,,,17979195,,,"The confirmation of the denatured structure of pyrrolidone carboxyl peptidase under nondenaturing conditions: difference in helix propensity of two synthetic peptides with single amino acid substitution.",published,journal,Proteins,,71,2,,,,,,,,,,,,,,,,,,,,,,737,742,2008, citations,citation_2,10117,2402,2,,reference citation,,,17309236,,,"Characterization of the denatured structure of pyrrolidone carboxyl peptidase from a hyperthermophile under nondenaturing conditions: role of the C-terminal alpha-helix of the protein in folding and stability.",published,journal,Biochemistry,,46,12,,,,,,,,,,,,,,,,,,,,,,3664,3672,2007, citations,citation_1,10118,2419,1,,entry citation,,,18687870,,,The solution structure of the C-terminal domain of NfeD reveals a novel membrane-anchored OB-fold,published,journal,Protein Sci.,,17,11,,,,,,,,,,,,,,,,,,,,,,1915,1924,2008, citations,citation_1,10119,2447,1,,entry citation,,,,,,Solution structure of DnaJ domain of human KIAA0730 protein,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1012,2465,1,,entry citation,,,,,"Roy, Melinda, Lee, Robert W.-K., Kaarsholm, Niels C., Thogersen, Henning, Brange, Jens, Dunn, M.F., ""Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin,"" Biochim. Biophys. Acta 1053, 63-73 (1990).","Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin",published,journal,Biochim. Biophys. Acta,,1053,,,,,,,,,,,,,,,,,,,,,,,63,73,1990, citations,citation_1,10120,2478,1,,entry citation,,,,,,Solution structure of immunoglobulin like domain of mouse nuclear lamin,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10121,2497,1,,entry citation,,,,,,Solution structure of a peptidyl-tRNA hydrolase domain of a hypothetical protein,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10122,2516,1,,entry citation,,,,,,Solution structure of the second SH3 domain of human intersectin 2 (KIAA1256),in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10123,2535,1,,entry citation,,,15689505,,,"Solution structure of the PWWP domain of the hepatoma-derived growth factor family.",published,journal,Protein Sci.,Protein Science,14,3,,,,,,,,,,,,,,,,,,,,,,756,764,2005, citations,citation_1,10124,2554,1,,entry citation,,,,,,"Solution structure of the second PDZ domain of human membrane associated guanylate kinase inverted-2 (MAGI-2)",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10125,2573,1,,entry citation,,,,,,Solution structure of the dsRBD from hypothetical protein BAB26260,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10126,2590,1,,entry citation,,,,,,Solution structure of the R3H domain from human hypothetical protein BAA76846,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10127,2607,1,,entry citation,,,,,,Solution structure of the alpha-helical domain from mouse hypothetical PNPase,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10128,2624,1,,entry citation,,,,,,Solution structure of the second FNIII domain of DSCAML1 protein,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10129,2642,1,,entry citation,,,,,,Solution structure of the first Fn3 domain of Sidekick-2 protein,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1013,2660,1,,entry citation,,,,,"Roy, Melinda, Lee, Robert W.-K., Kaarsholm, Niels C., Thogersen, Henning, Brange, Jens, Dunn, M.F., ""Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin,"" Biochim. Biophys. Acta 1053, 63-73 (1990).","Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin",published,journal,Biochim. Biophys. Acta,,1053,,,,,,,,,,,,,,,,,,,,,,,63,73,1990, citations,citation_1,10130,2673,1,,entry citation,,,,,,"Solution structure of a novel beta-grasp fold like domain of Hypothetical protein (Arabidopsis thaliana)",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10131,2691,1,,entry citation,,,,,,"Solution Structure of the N-terminal Pleckstrin Homology Domain Of TAPP2 from Mouse",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10132,2709,1,,entry citation,,,17658890,,,"Local conformational transition of Hydrogenobacter thermophilus cytochrome c552 relevant to its redox potential.",published,journal,Biochemistry,,46,32,,,,,,,,,,,,,,,,,,,,,,9215,9224,2007, citations,citation_1,10133,2724,1,,entry citation,,,17658890,,,"Local conformational transition of Hydrogenobacter thermophilus cytochrome c552 relevant to its redox potential.",published,journal,Biochemistry,,46,32,,,,,,,,,,,,,,,,,,,,,,9215,9224,2007, citations,citation_1,10134,2739,1,,entry citation,,,17658890,,,"Local conformational transition of Hydrogenobacter thermophilus cytochrome c552 relevant to its redox potential.",published,journal,Biochemistry,,46,32,,,,,,,,,,,,,,,,,,,,,,9215,9224,2007, citations,citation_1,10135,2754,1,,entry citation,,,17658890,,,"Local conformational transition of Hydrogenobacter thermophilus cytochrome c552 relevant to its redox potential.",published,journal,Biochemistry,,46,32,,,,,,,,,,,,,,,,,,,,,,9215,9224,2007, citations,citation_1,10136,2769,1,,entry citation,,,,,,Solution structure of the first SH3 domain of human intersectin2 (KIAA1256),in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,L-PGDS_citation,10137,2787,1,,entry citation,,,17715133,,,"NMR solution structure of lipocalin-type prostaglandin D synthase: evidence for partial overlapping of catalytic pocket and retinoic acid-binding pocket within the central cavity.",published,journal,J. Biol. Chem.,,282,43,,,,,,,,,,,,,,,,,,,,,,31373,31379,2007, citations,citation_1,10138,2800,1,,entry citation,,,17616598,,,"Structural characterization of the ribosome maturation protein, RimM",published,journal,J. Bacteriol.,,189,17,,,,,,,,,,,,,,,,,,,,,,,6397,6406,2007 citations,citation_1,10139,2821,1,,entry citation,,,17616598,,,"Structural characterization of the ribosome maturation protein, RimM",published,journal,J. Bacteriol.,,189,17,,,,,,,,,,,,,,,,,,,,,,,6397,6406,2007 citations,entry_citation,1014,2846,1,,entry citation,,,,,"Roy, Melinda, Lee, Robert W.-K., Kaarsholm, Niels C., Thogersen, Henning, Brange, Jens, Dunn, M.F., ""Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin,"" Biochim. Biophys. Acta 1053, 63-73 (1990).","Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin",published,journal,Biochim. Biophys. Acta,,1053,,,,,,,,,,,,,,,,,,,,,,,63,73,1990, citations,citation_1,10140,2859,1,,entry citation,,,17616598,,,"Structural characterization of the ribosome maturation protein, RimM",published,journal,J. Bacteriol.,,189,17,,,,,,,,,,,,,,,,,,,,,,,6397,6406,2007 citations,citation_1,10141,2881,1,,entry citation,,,,,,"Solution structure of the alpha adaptinC2 domain from human Adapter-related protein complex 1 gamma 2 subunit",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10142,2899,1,,entry citation,,,,,,"Solution structure of the N-terminal extended 20th Filamin domain from human Filamin-B",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10143,2917,1,,entry citation,,,,,,Solution structure of the 14th filamin domain from human Filamin-B,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10144,2935,1,,entry citation,,,,,,"Solution structure of the RhoGAP domain from human Rho GTPase activating protein 5 variant",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10145,2955,1,,entry citation,,,,,,"Solution structure of the N-teruminus extended RhoGAP domain from human Rho GTPase activating protein 5 variant",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10146,2975,1,,entry citation,,,,,,Solution structure of the 21th filamin domain from human Filamin-B,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10147,2993,1,,entry citation,,,,,,Solution structure of the CH domain from human Sperm flagellar protein 1,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10148,3011,1,,entry citation,,,,,,"Solution structure of three zf-C2H2 domains from mouse protein odd-skipped-related 2 splicing isoform 2",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10149,3031,1,,entry citation,,,,,,Solution structure of the CH domain from human MICAL-2,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1015,3049,1,,entry citation,,,,,"Roy, Melinda, Lee, Robert W.-K., Kaarsholm, Niels C., Thogersen, Henning, Brange, Jens, Dunn, M.F., ""Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin,"" Biochim. Biophys. Acta 1053, 63-73 (1990).","Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin",published,journal,Biochim. Biophys. Acta,,1053,,,,,,,,,,,,,,,,,,,,,,,63,73,1990, citations,citation_1,10150,3062,1,,entry citation,,,,,,Solution structure of the SANT domain of fission yeast SPCC24B10.08c protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10151,3080,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 887-919) of human Zinc finger protein 268",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10152,3100,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 495-525) of human Zinc finger protein 268",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10153,3120,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 519-551) of human Zinc finger protein 484",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10154,3140,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 557-589) of human Zinc finger protein 473",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10155,3160,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 603-635) of human Zinc finger protein 484",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10156,3180,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 715-747) of human Zinc finger protein 484",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10157,3200,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 626-654) of human B-cell lymphoma 6 protein",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10158,3220,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 370-400) of human Zinc finger protein 473",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10159,3240,1,,entry citation,,,,,,Solution structure of the 16th filamin domain from human Filamin-B,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1016,3258,1,,entry citation,,,,,"Roy, Melinda, Lee, Robert W.-K., Kaarsholm, Niels C., Thogersen, Henning, Brange, Jens, Dunn, M.F., ""Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin,"" Biochim. Biophys. Acta 1053, 63-73 (1990).","Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin",published,journal,Biochim. Biophys. Acta,,1053,,,,,,,,,,,,,,,,,,,,,,,63,73,1990, citations,citation_1,10160,3271,1,,entry citation,,,,,,Solution structure of the 17th filamin domain from human Filamin-B,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10161,3289,1,,entry citation,,,,,,Solution structure of the 22th filamin domain from human Filamin-B,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10162,3307,1,,entry citation,,,,,,Solution structure of the 23th filamin domain from human Filamin-B,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10163,3325,1,,entry citation,,,,,,Solution structure of the 24th filamin domain from human Filamin-B,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10164,3343,1,,entry citation,,,,,,Solution structure of the A1pp domain from human protein C6orf130,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10165,3361,1,,entry citation,,,,,,"Solution structure of the CBM_21 domain from human protein phosphatase 1, regulatory (inhibitor) subunit 3B",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10166,3379,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 637-667) of human Zinc finger protein 268",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10167,3399,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 584-616) of human Zinc finger protein 28 homolog",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10168,3419,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 640-672) of human Zinc finger protein 28 homolog",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10169,3439,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 171-203) of human Zinc finger protein 224",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10226,4656,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 273-303) of human Zinc finger protein 268",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1017,3459,1,,entry citation,,,,,"Roy, Melinda, Lee, Robert W.-K., Kaarsholm, Niels C., Thogersen, Henning, Brange, Jens, Dunn, M.F., ""Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin,"" Biochim. Biophys. Acta 1053, 63-73 (1990).","Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin",published,journal,Biochim. Biophys. Acta,,1053,,,,,,,,,,,,,,,,,,,,,,,63,73,1990, citations,citation_1,10170,3472,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 415-447) of human Zinc finger protein 28 homolog",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10171,3492,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 311-343) of human Zinc finger protein 224",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10172,3512,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 395-427) of human Zinc finger protein 224",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10173,3532,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 592-624) of human Zinc finger protein 347",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10174,3552,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 340-372) of human Zinc finger protein 347",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10175,3572,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 556-588) of human Zinc finger protein 28 homolog",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10176,3592,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 696-728) of human Zinc finger protein 28 homolog",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10177,3612,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 687-719) of human Zinc finger protein 484",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10178,3632,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 204-236) of human Zinc finger protein 473",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10179,3652,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 724-756) of human Zinc finger protein 28 homolog",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1018,3672,1,,entry citation,,,,,"Roy, Melinda, Lee, Robert W.-K., Kaarsholm, Niels C., Thogersen, Henning, Brange, Jens, Dunn, M.F., ""Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin,"" Biochim. Biophys. Acta 1053, 63-73 (1990).","Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin",published,journal,Biochim. Biophys. Acta,,1053,,,,,,,,,,,,,,,,,,,,,,,63,73,1990, citations,citation_1,10180,3685,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 339-371) of human Zinc finger protein 224",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10181,3705,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 367-399) of human Zinc finger protein 224",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10182,3725,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 725-757) of human Zinc finger protein 473",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10183,3745,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 379-411) of human Zinc finger protein 484",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10184,3765,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 463-495) of human Zinc finger protein 484",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10185,3785,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 607-639) of human Zinc finger protein 268",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10186,3805,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 369-401) of human Zinc finger protein 95 homolog",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10187,3825,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 479-511) of human Zinc finger protein 224",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10188,3845,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 564-596) of human Zinc finger protein 347",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10189,3865,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 341-373) of human Zinc finger protein 95 homolog",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1019,3885,1,,entry citation,,,,,"Roy, Melinda, Lee, Robert W.-K., Kaarsholm, Niels C., Thogersen, Henning, Brange, Jens, Dunn, M.F., ""Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin,"" Biochim. Biophys. Acta 1053, 63-73 (1990).","Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin",published,journal,Biochim. Biophys. Acta,,1053,,,,,,,,,,,,,,,,,,,,,,,63,73,1990, citations,citation_1,10190,3898,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 425-457) of human Zinc finger protein 95 homolog",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10191,3918,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 719-751) of human Zinc finger protein 268",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10192,3938,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 283-315) of human Zinc finger protein 224",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10193,3958,1,,entry citation,,,,,,Solution structure of the Myb-like DNA-binding domain of human ZZZ3 protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10194,3976,1,,entry citation,,,,,,Solution structure of the SH3 domain of mouse RUN and TBC1 domain containing 3,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10195,3994,1,,entry citation,,,,,,Solution structure of the second SH3 domain of human Vinexin,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10196,4012,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 768-800) of human Zinc finger protein 95 homolog",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10197,4032,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 199-231) of human Zinc finger protein 224",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10198,4052,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 423-455) of human Zinc finger protein 224",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10199,4072,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 312-344) of human Zinc finger protein 347",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,102,4092,1,,entry citation,,,,,"Koyama, Satoshi, Kobayashi, Yuji, Norioka, Shigemi, Kyogoku, Yoshimasa, Ikenaka, Tokuji, ""Conformational Studies by 1H Nuclear Magnetic Resonance of the Trypsin-Chymotrypsin Inhibitor B-III from Peanuts and Its Enzymatically Modified Derivative,"" Biochemistry 25, 8076-8082 (1986).","Conformational Studies by 1H Nuclear Magnetic Resonance of the Trypsin-Chymotrypsin Inhibitor B-III from Peanuts and Its Enzymatically Modified Derivative",published,journal,Biochemistry,,25,,,,,,,,,,,,,,,,,,,,,,,8076,8082,1986, citations,entry_citation,1020,4105,1,,entry citation,,,,,"Roy, Melinda, Lee, Robert W.-K., Kaarsholm, Niels C., Thogersen, Henning, Brange, Jens, Dunn, M.F., ""Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin,"" Biochim. Biophys. Acta 1053, 63-73 (1990).","Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin",published,journal,Biochim. Biophys. Acta,,1053,,,,,,,,,,,,,,,,,,,,,,,63,73,1990, citations,citation_1,10200,4118,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 342-372) of human Zinc finger protein 473",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10201,4138,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 641-673) of human Zinc finger protein 473",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10202,4158,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 491-523) of human Zinc finger protein 484",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10203,4178,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 547-579) of human Zinc finger protein 484",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10204,4198,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 612-644) of human Zinc finger protein 28 homolog",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10205,4218,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 668-70) of human Zinc finger protein 28 homolog",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10206,4238,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 780-812) of human Zinc finger protein 28 homolog",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10207,4258,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 368-400) of human Zinc finger protein 347",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10208,4278,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 315-345) of human Zinc finger protein 473",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10209,4298,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 809-841) of human Zinc finger protein 473",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1021,4318,1,,entry citation,,,,,"Roy, Melinda, Lee, Robert W.-K., Kaarsholm, Niels C., Thogersen, Henning, Brange, Jens, Dunn, M.F., ""Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin,"" Biochim. Biophys. Acta 1053, 63-73 (1990).","Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin",published,journal,Biochim. Biophys. Acta,,1053,,,,,,,,,,,,,,,,,,,,,,,63,73,1990, citations,citation_1,10210,4331,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 528-560) of human Zinc finger protein 28 homolog",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10211,4351,1,,entry citation,,,,,,Solution structure of the SH3 domain of human Tyrosine-protein kinase ITK/TSK,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10212,4369,1,,entry citation,,,,,,"Solution structure of the SH3 domain of the human SRC-like adopter protein (SLAP)",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10213,4387,1,,entry citation,,,18615715,,,"Solution structure of the GUCT domain from human RNA helicase II/Gubeta reveals the RRM fold, but implausible RNA interactions.",published,journal,Proteins,Proteins,74,1,,,,,,,,,,,,,,,,,,,,,,133,144,2008, citations,citation_1,10214,4407,1,,entry citation,,,18562638,,,"Structural basis for controlling the dimerization and stability of the WW domains of an atypical subfamily.",published,journal,Protein Sci.,Protein Science,17,9,,,,,,,,,,,,,,,,,,,,,,1531,1541,2008, citations,citation_1,10215,4425,1,,entry citation,,,18562638,,,"Structural basis for controlling the dimerization and stability of the WW domains of an atypical subfamily.",published,journal,Protein Sci.,Protein Science,17,9,,,,,,,,,,,,,,,,,,,,,,1531,1541,2008, citations,citation_1,10216,4443,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 411-441) of human Zinc finger protein 268",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10217,4463,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 693-723) of human Zinc finger protein 268",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10218,4483,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 355-385) of human Zinc finger protein 268",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10219,4503,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 441-469) of human Zinc finger protein 268",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1022,4523,1,,entry citation,,,,,"Roy, Melinda, Lee, Robert W.-K., Kaarsholm, Niels C., Thogersen, Henning, Brange, Jens, Dunn, M.F., ""Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin,"" Biochim. Biophys. Acta 1053, 63-73 (1990).","Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin",published,journal,Biochim. Biophys. Acta,,1053,,,,,,,,,,,,,,,,,,,,,,,63,73,1990, citations,citation_1,10220,4536,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 397-429) of human Zinc finger protein 95 homolog",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10221,4556,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 255-287) of human Zinc finger protein 224",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10222,4576,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 775-807) of human Zinc finger protein 268",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10223,4596,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 760-792) of human Zinc finger protein 347",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10224,4616,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 859-889) of human Zinc finger protein 268",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10225,4636,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 301-331) of human Zinc finger protein 268",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10227,4676,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 551-583) of human Zinc finger protein 268",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10228,4696,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 628-660) of human Zinc finger protein 95 homolog",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10229,4716,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 385-413) of human Zinc finger protein 268",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1023,4736,1,,entry citation,,,,,"Roy, Melinda, Lee, Robert W.-K., Kaarsholm, Niels C., Thogersen, Henning, Brange, Jens, Dunn, M.F., ""Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin,"" Biochim. Biophys. Acta 1053, 63-73 (1990).","Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin",published,journal,Biochim. Biophys. Acta,,1053,,,,,,,,,,,,,,,,,,,,,,,63,73,1990, citations,citation_1,10230,4749,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 563-595) of human Zinc finger protein 224",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10231,4769,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 598-626) of human B-cell lymphoma 6 protein",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10232,4789,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 796-828) of human Zinc finger protein 95 homolog",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10233,4809,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 284-316) of human Zinc finger protein 347",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10234,4829,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 648-680) of human Zinc finger protein 347",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10235,4849,1,,entry citation,,,18650440,,,"Structure of the C-terminal PID Domain of Fe65L1 Complexed with the Cytoplasmic Tail of APP Reveals a Novel Peptide Binding Mode",published,journal,J. Biol. Chem.,Journal of Biological Chemistry,283,40,,,,,,,,,,,,,,,,,,,,,,27165,27178,2008, citations,citation_1,10236,4867,1,,entry citation,,,18650440,,,"Structure of the C-terminal PID Domain of Fe65L1 Complexed with the Cytoplasmic Tail of APP Reveals a Novel Peptide Binding Mode",published,journal,J. Biol. Chem.,Journal of Biological Chemistry,283,40,,,,,,,,,,,,,,,,,,,,,,27165,27178,2008, citations,citation_1,10237,4886,1,,entry citation,,,18650440,,,"Structure of the C-terminal PID Domain of Fe65L1 Complexed with the Cytoplasmic Tail of APP Reveals a Novel Peptide Binding Mode",published,journal,J. Biol. Chem.,Journal of Biological Chemistry,283,40,,,,,,,,,,,,,,,,,,,,,,27165,27178,2008, citations,citation_1,10238,4904,1,,entry citation,,,18650440,,,"Structure of the C-terminal PID Domain of Fe65L1 Complexed with the Cytoplasmic Tail of APP Reveals a Novel Peptide Binding Mode",published,journal,J. Biol. Chem.,Journal of Biological Chemistry,283,40,,,,,,,,,,,,,,,,,,,,,,27165,27178,2008, citations,citation_1,10239,4922,1,,entry citation,,,18650440,,,"Structure of the C-terminal PID Domain of Fe65L1 Complexed with the Cytoplasmic Tail of APP Reveals a Novel Peptide Binding Mode",published,journal,J. Biol. Chem.,Journal of Biological Chemistry,283,40,,,,,,,,,,,,,,,,,,,,,,27165,27178,2008, citations,entry_citation,1024,4940,1,,entry citation,,,,,"Roy, Melinda, Lee, Robert W.-K., Kaarsholm, Niels C., Thogersen, Henning, Brange, Jens, Dunn, M.F., ""Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin,"" Biochim. Biophys. Acta 1053, 63-73 (1990).","Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin",published,journal,Biochim. Biophys. Acta,,1053,,,,,,,,,,,,,,,,,,,,,,,63,73,1990, citations,citation_1,10240,4954,1,,entry citation,,,,,,Solution structures of the SH3 domain of human Src substrate cortactin,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10241,4972,1,,entry citation,,,,,,"Solution structures of the SH3 domain of human rho guanine exchange factor (GEF) 16",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10242,4990,1,,entry citation,,,,,,Solution structures of the PDZ domain of human Interleukin-16,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10243,5008,1,,entry citation,,,,,,"Solution structures of the C2H2 type zinc finger domain of human Zinc finger protein 24",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10244,5028,1,,entry citation,,,,,,"Solution structures of the C2H2 type zinc finger domain of human Zinc finger protein 462",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10245,5048,1,,entry citation,,,,,,"Solution structures of the SH3 domain of human megakaryocyte-associated tyrosine-protein kinase.",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10246,5066,1,,entry citation,,,,,,"Solution structures of the C2H2 type zinc finger domain of human Transcriptional repressor CTCF",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10247,5086,1,,entry citation,,,,,,"Solution structures of the LIM domain of human NEDD9 interacting protein with calponin homology and LIM domains",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10248,5106,1,,entry citation,,,,,,Solution Structure of the HMG_box Domain of Murine Bobby Sox Homolog,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10249,5124,1,,entry citation,,,,,,Solution structure of the C-terminal PH domain of human pleckstrin,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1025,5142,1,,entry citation,,,,,"Roy, Melinda, Lee, Robert W.-K., Kaarsholm, Niels C., Thogersen, Henning, Brange, Jens, Dunn, M.F., ""Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin,"" Biochim. Biophys. Acta 1053, 63-73 (1990).","Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin",published,journal,Biochim. Biophys. Acta,,1053,,,,,,,,,,,,,,,,,,,,,,,63,73,1990, citations,citation_1,10250,5155,1,,entry citation,,,,,,Solution structure of the PH domain of human Docking protein BRDG1,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10251,5173,1,,entry citation,,,,,,Solution structure of the C-terminal PH domain of human pleckstrin 2,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10252,5191,1,,entry citation,,,,,,"Solution structure of the HMG_box domain of thymus high mobility group box protein TOX from mouse",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10253,5209,1,,entry citation,,,,,,"Solution structure of the PH domain of protein kinase C, D2 type from human",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10254,5227,1,,entry citation,,,,,,"Solution structure of the C-terminal PH domain of FYVE, RhoGEF and PH domain containing protein 3 (FGD3) from human",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10255,5245,1,,entry citation,,,,,,Solution structure of the N-terminal PH domain of ARAP2 protein from human,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10256,5263,1,,entry citation,,,,,,"Solution structure of the C-terminal PH domain of hypothetical protein KIAA1914 from human",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10257,5281,1,,entry citation,,,,,,"Solution structures of the C2H2 type zinc finger domain of human zinc finger BED domain containing protein 2",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10258,5301,1,,entry citation,,,,,,Solution structures of the fn3 domain of human ephrin type-B receptor 1,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10259,5319,1,,entry citation,,,,,,Solution structures of the PDZ domain of human unnamed protein product,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10260,5337,1,,entry citation,,,,,,"Solution structures of the fn3 domain of human receptor-type tyrosine-protein phosphatase F",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10261,5355,1,,entry citation,,,,,,Solution structures of the WHEP-TRS domain of human methionyl-tRNA synthetase,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10262,5373,1,,entry citation,,,,,,Solution structures of the fn3 domain of human collagen alpha-1(XX) chain,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10263,5391,1,,entry citation,,,,,,"Solution structures of the 6th fn3 domain of human receptor-type tyrosine-protein phosphatase F",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10264,5409,1,,entry citation,,,,,,"The solution structure of the VHS domain of human Signal transducing adaptor molecule 2",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10265,5427,1,,entry citation,,,,,,"Solution structures of the fn3 domain of human receptor-type tyrosine-protein phosphatase F",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10266,5445,1,,entry citation,,,,,,"Solution structures of the fn3 domain of human receptor-type tyrosine-protein phosphatase F",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10267,5463,1,,entry citation,,,,,,"Solution structures of the PDZ domain of mus musculus PDZ domain-containing protein 1",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10268,5481,1,,entry citation,,,,,,Solution structures of the CA domain of human protocadherin 9,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10269,5499,1,,entry citation,,,,,,"Solution structures of the Chromo domain of human chromodomain helicase-DNA-binding protein 4",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1027,5517,1,,entry citation,,,,,"Hauksson, Jon B., La Mar, Gerd N., Pandey, Ravindra K., Rezzano, Irene N., Smith, Kevin M., ""1H NMR Study of the Role of Individual Heme Propionates in Modulating Structural and Dynamic Properties of the Heme Pocket in Myoglobin,"" J. Am. Chem. Soc. 112, 6198-6205 (1990).","1H NMR Study of the Role of Individual Heme Propionates in Modulating Structural and Dynamic Properties of the Heme Pocket in Myoglobin",published,journal,J. Am. Chem. Soc.,,112,,,,,,,,,,,,,,,,,,,,,,,6198,6205,1990, citations,citation_1,10270,5530,1,,entry citation,,,,,,Solution structures of the fn3 domain of human contactin 1,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10271,5548,1,,entry citation,,,,,,Solution structures of the fn3 domain of human collagen alpha-1(XX) chain,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10272,5566,1,,entry citation,,,,,,Solution structures of the SH3 domain of human KIAA0418,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10273,5584,1,,entry citation,,,,,,"Solution structures of the TGS domain of human developmentally-regulated GTP-binding protein 1",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10274,5602,1,,entry citation,,,,,,Solution structures of the fn3 domain of human collagen alpha-1(XX) chain,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10275,5620,1,,entry citation,,,,,,"Solution structures of the PAAD_DAPIN domain of mus musculus interferon-activatable protein 205",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10276,5638,1,,entry citation,,,,,,"Solution structure of the Tudor domain of Tudor domain containing protein 3 from mouse",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10277,5656,1,,entry citation,,,,,,Solution structure of the Chromo domain of chromobox homolog 2 from human,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10278,5674,1,,entry citation,,,,,,"Solution structure of the PH domain of Pleckstrin homology domain-containing protein family B member 1 from mouse",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10279,5692,1,,entry citation,,,,,,Solution structure of the PH domain of Docking protein 2 from human,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1028,5710,1,,entry citation,,,,,"Hauksson, Jon B., La Mar, Gerd N., Pandey, Ravindra K., Rezzano, Irene N., Smith, Kevin M., ""1H NMR Study of the Role of Individual Heme Propionates in Modulating Structural and Dynamic Properties of the Heme Pocket in Myoglobin,"" J. Am. Chem. Soc. 112, 6198-6205 (1990).","1H NMR Study of the Role of Individual Heme Propionates in Modulating Structural and Dynamic Properties of the Heme Pocket in Myoglobin",published,journal,J. Am. Chem. Soc.,,112,,,,,,,,,,,,,,,,,,,,,,,6198,6205,1990, citations,citation_1,10280,5723,1,,entry citation,,,,,,"Solution structure of the PH domain of Oxysterol binding protein-related protein 11 from human",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10281,5741,1,,entry citation,,,,,,Solution structure of the homeobox domain of the human paired box protein Pax-6,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10282,5759,1,,entry citation,,,,,,"Solution structure of the homeobox domain of the human hypothetical protein FLJ21616",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10283,5777,1,,entry citation,,,,,,"Solution structure of the first homeobox domain of AT-binding transcription factor 1 (ATBF1)",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10284,5795,1,,entry citation,,,,,,"Solution structure of the second homeobox domain of AT-binding transcription factor 1 (ATBF1)",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10285,5813,1,,entry citation,,,,,,"Solution structure of the third homeobox domain of AT-binding transcription factor 1 (ATBF1)",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10286,5831,1,,entry citation,,,,,,"Solution structure of the homeobox domain of the hypothetical protein, DKFZp686K21156",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10287,5849,1,,entry citation,,,,,,"Solution structure of the second homeobox domain of Zinc fingers and homeoboxes protein 3 (Triple homeobox 1 protein)",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10288,5867,1,,entry citation,,,,,,"Solution structure of the homeobox domain of Hepatocyte nuclear factor 1-beta (HNF-1beta)",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10289,5885,1,,entry citation,,,,,,"Solution structure of the homeobox domain of Zinc finger homeobox protein 1b (Smad interacting protein 1)",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1029,5903,1,,entry citation,,,,,"Hauksson, Jon B., La Mar, Gerd N., Pandey, Ravindra K., Rezzano, Irene N., Smith, Kevin M., ""1H NMR Study of the Role of Individual Heme Propionates in Modulating Structural and Dynamic Properties of the Heme Pocket in Myoglobin,"" J. Am. Chem. Soc. 112, 6198-6205 (1990).","1H NMR Study of the Role of Individual Heme Propionates in Modulating Structural and Dynamic Properties of the Heme Pocket in Myoglobin",published,journal,J. Am. Chem. Soc.,,112,,,,,,,,,,,,,,,,,,,,,,,6198,6205,1990, citations,citation_1,10290,5916,1,,entry citation,,,,,,The solution structure of the homeobox domain of human Homeobox protein DLX-5,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10291,5934,1,,entry citation,,,,,,The solution structure of the homeobox domain of human homeobox protein TGIF2LX,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10292,5952,1,,entry citation,,,,,,"Solution structure of the third homeobox domain of Zinc fingers and homeoboxes protein 2",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10293,5970,1,,entry citation,,,,,,Solution structure of the homeobox domain of LIM/homeobox protein Lhx9,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10294,5988,1,,entry citation,,,,,,Solution structure of the homeobox domain of Homeobox protein OTX2,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10295,6006,1,,entry citation,,,,,,Solution structure of the homeobox domain of Homeobox protein BarH-like 1,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10296,6024,1,,entry citation,,,,,,Solution structure of the homeobox domain of Homeobox protein goosecoid,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10297,6042,1,,entry citation,,,,,,"Solution structure of the homeobox domain from human NIL-2-A zinc finger protein, transcription factor 8",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10298,6060,1,,entry citation,,,,,,"structure of the third Homeodomain from the human homeobox and leucine zipper protein, Homez",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10299,6078,1,,entry citation,,,,,,Solution structures of the fn3 domain of human Tripartite motif protein 9,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,103,6096,1,,entry citation,,,,,"Koyama, Satoshi, Kobayashi, Yuji, Norioka, Shigemi, Kyogoku, Yoshimasa, Ikenaka, Tokuji, ""Conformational Studies by 1H Nuclear Magnetic Resonance of the Trypsin-Chymotrypsin Inhibitor B-III from Peanuts and Its Enzymatically Modified Derivative,"" Biochemistry 25, 8076-8082 (1986).","Conformational Studies by 1H Nuclear Magnetic Resonance of the Trypsin-Chymotrypsin Inhibitor B-III from Peanuts and Its Enzymatically Modified Derivative",published,journal,Biochemistry,,25,,,,,,,,,,,,,,,,,,,,,,,8076,8082,1986, citations,entry_citation,1030,6109,1,,entry citation,,,,,"Hauksson, Jon B., La Mar, Gerd N., Pandey, Ravindra K., Rezzano, Irene N., Smith, Kevin M., ""1H NMR Study of the Role of Individual Heme Propionates in Modulating Structural and Dynamic Properties of the Heme Pocket in Myoglobin,"" J. Am. Chem. Soc. 112, 6198-6205 (1990).","1H NMR Study of the Role of Individual Heme Propionates in Modulating Structural and Dynamic Properties of the Heme Pocket in Myoglobin",published,journal,J. Am. Chem. Soc.,,112,,,,,,,,,,,,,,,,,,,,,,,6198,6205,1990, citations,citation_1,10300,6122,1,,entry citation,,,,,,"Solution structures of the fn3 domain of human Proto-oncogene tyrosine-protein kinase MER precursor",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10301,6140,1,,entry citation,,,,,,Solution structures of the SH3 domain of human Crk-like protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10302,6158,1,,entry citation,,,,,,"Solution structures of the SH3 domain of human SH3-containing GRB2-like protein 2",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10303,6176,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 752-784) of human Zinc finger protein 28 homolog",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10304,6196,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 544-576) of human Zinc finger protein 95 homolog",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10305,6216,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 536-568) of human Zinc finger protein 347",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10306,6236,1,,entry citation,,,,,,"Solution structure of the 1st zf-C2H2 domain from Human B-cell lymphoma 6 protein",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10307,6256,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 426-458) of human Zinc finger protein 473",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10308,6276,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 484-512) of human Zinc finger protein 473",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10309,6296,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 771-803) of human Zinc finger protein 484",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1031,6316,1,,entry citation,,,,,"Hauksson, Jon B., La Mar, Gerd N., Pandey, Ravindra K., Rezzano, Irene N., Smith, Kevin M., ""1H NMR Study of the Role of Individual Heme Propionates in Modulating Structural and Dynamic Properties of the Heme Pocket in Myoglobin,"" J. Am. Chem. Soc. 112, 6198-6205 (1990).","1H NMR Study of the Role of Individual Heme Propionates in Modulating Structural and Dynamic Properties of the Heme Pocket in Myoglobin",published,journal,J. Am. Chem. Soc.,,112,,,,,,,,,,,,,,,,,,,,,,,6198,6205,1990, citations,citation_1,10310,6329,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 396-428) of human Zinc finger protein 347",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10311,6349,1,,entry citation,,,,,,Solution structure of the PH domain of PEPP-3 from human,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10312,6367,1,,entry citation,,,,,,"Solution structure of the PH domain of Protein kinase C, nu type from human",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10313,6385,1,,entry citation,,,,,,"Solution structure of the PH domain of PIP2-dependent ARF1 GTPase-activating protein from human",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10314,6403,1,,entry citation,,,,,,Solution structure of the PH domain of Evectin-2 from mouse,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10315,6421,1,,entry citation,,,,,,"Solution structure of the PH domain of Rho GTPase activating protein 21 from human",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10316,6439,1,,entry citation,,,,,,"Solution structure of the PH domain of TBC1 domain family member 2 protein from human",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10317,6457,1,,entry citation,,,,,,"Solution structure of the PH domain of pleckstrin homology domain-containing protein family A member 5 from human""",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10318,6475,1,,entry citation,,,,,,Solution structure of the PTB domain of KIAA1075 protein from human,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10319,6493,1,,entry citation,,,,,,Solution structure of the PH domain of KIAA0640 protein from human,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1032,6511,1,,entry citation,,,,,"Hauksson, Jon B., La Mar, Gerd N., Pandey, Ravindra K., Rezzano, Irene N., Smith, Kevin M., ""1H NMR Study of the Role of Individual Heme Propionates in Modulating Structural and Dynamic Properties of the Heme Pocket in Myoglobin,"" J. Am. Chem. Soc. 112, 6198-6205 (1990).","1H NMR Study of the Role of Individual Heme Propionates in Modulating Structural and Dynamic Properties of the Heme Pocket in Myoglobin",published,journal,J. Am. Chem. Soc.,,112,,,,,,,,,,,,,,,,,,,,,,,6198,6205,1990, citations,citation_1,10320,6524,1,,entry citation,,,,,,Solution structure of the 9th filamin domain from human Filamin-B,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10321,6542,1,,entry citation,,,,,,Solution structure of the 11th filamin domain from human Filamin-B,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10322,6560,1,,entry citation,,,,,,Solution structure of the 12th filamin domain from human Filamin-B,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10323,6578,1,,entry citation,,,,,,Solution structure of the 13th filamin domain from human Filamin-B,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10324,6596,1,,entry citation,,,,,,Solution structure of the 20th Filamin domain from human Filamin-B,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10325,6614,1,,entry citation,,,,,,Solution structure of the 15th Filamin domain from human Filamin-B,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10326,6632,1,,entry citation,,,,,,Solution structure of the 18th Filamin domain from human Filamin-B,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10327,6650,1,,entry citation,,,,,,Solution structure of the filamin domain from human tripartite motif protein 45,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10328,6668,1,,entry citation,,,,,,Solution structure of the 14th Filamin domain from human Filamin C,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10329,6686,1,,entry citation,,,,,,Solution structure of the 16th Filamin domain from human Filamin C,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1033,6704,1,,entry citation,,,,,"Hauksson, Jon B., La Mar, Gerd N., Pandey, Ravindra K., Rezzano, Irene N., Smith, Kevin M., ""1H NMR Study of the Role of Individual Heme Propionates in Modulating Structural and Dynamic Properties of the Heme Pocket in Myoglobin,"" J. Am. Chem. Soc. 112, 6198-6205 (1990).","1H NMR Study of the Role of Individual Heme Propionates in Modulating Structural and Dynamic Properties of the Heme Pocket in Myoglobin",published,journal,J. Am. Chem. Soc.,,112,,,,,,,,,,,,,,,,,,,,,,,6198,6205,1990, citations,citation_1,10330,6717,1,,entry citation,,,,,,Solution structure of the 17th Filamin domain from human Filamin C,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10331,6735,1,,entry citation,,,,,,Solution structure of the 22th Filamin domain from human Filamin C,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10332,6753,1,,entry citation,,,,,,Solution structure of the 23th Filamin domain from human Filamin C,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10333,6771,1,,entry citation,,,,,,Solution structure of the filamin domain from human BK158_1 protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10334,6789,1,,entry citation,,,,,,Solution structure of the 19th filamin domain from human Filamin-B,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10335,6807,1,,entry citation,,,,,,Solution structure of the 10th filamin domain from human Filamin-B,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10336,6825,1,,entry citation,,,20455272,,,Solution structure of the C-terminal DUF1000 domain of the human thioredoxin-like 1 protein,published,journal,Proteins,,78,9,,,,,,,,,,,,,,,,,,,,,,2176,2180,2010, citations,citation_1,10337,6859,1,,entry citation,,,,,,Solution structure of SH3 domain in Suppressor of T-cell receptor signaling 1,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,10338,6877,1,,entry citation,,,,,,"Solution Structure of the First UBA Domain in the Human Ubiquitin Specific Protease 5 (Isopeptidase 5)",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1037,6895,1,,entry citation,,,,,"Billeter, Martin, Qian, Yan-qiu, Otting, Gottfried, Muller, Martin, Gehring, Walter, Wuthrich, Kurt, ""Determination of the Three-dimensional Structure of the Antennapedia Homeodomain from Drosophila in Solution by 1H Nuclear Magnetic Resonance Spectroscopy,"" J. Mol. Biol. 214, 183-197 (1990).","Determination of the Three-dimensional Structure of the Antennapedia Homeodomain from Drosophila in Solution by 1H Nuclear Magnetic Resonance Spectroscopy",published,journal,J. Mol. Biol.,,214,,,,,,,,,,,,,,,,,,,,,,,183,197,1990, citations,entry_citation,1039,6908,1,,entry citation,,,,,"Snyder, Grayson H., Rowan, Robert, III, Karplus, Susan, Sykes, Brian D., ""Complete Tyrosine Assignments in the High Field 1H Nuclear Magnetic Resonance Spectrum of the Bovine Pancreatic Trypsin Inhibitor,"" Biochemistry 14, 3765-3777 (1975).","Complete Tyrosine Assignments in the High Field 1H Nuclear Magnetic Resonance Spectrum of the Bovine Pancreatic Trypsin Inhibitor",published,journal,Biochemistry,,14,,,,,,,,,,,,,,,,,,,,,,,3765,3777,1975, citations,entry_citation,104,6921,1,,entry citation,,,,,"Koyama, Satoshi, Kobayashi, Yuji, Norioka, Shigemi, Kyogoku, Yoshimasa, Ikenaka, Tokuji, ""Conformational Studies by 1H Nuclear Magnetic Resonance of the Trypsin-Chymotrypsin Inhibitor B-III from Peanuts and Its Enzymatically Modified Derivative,"" Biochemistry 25, 8076-8082 (1986).","Conformational Studies by 1H Nuclear Magnetic Resonance of the Trypsin-Chymotrypsin Inhibitor B-III from Peanuts and Its Enzymatically Modified Derivative",published,journal,Biochemistry,,25,,,,,,,,,,,,,,,,,,,,,,,8076,8082,1986, citations,entry_citation,1042,6934,1,,entry citation,,,,,"Ming, Li-June, Valentine, Joan Selverstone, ""NMR Studies of Nickle(II)-Substituted Derivatives of Bovine Copper-Zinc Superoxide Dismutase with Nickle(II) Bound in the Copper Site,"" J. Am. Chem. Soc. 112, 6374-6383 (1990).","NMR Studies of Nickle(II)-Substituted Derivatives of Bovine Copper-Zinc Superoxide Dismutase with Nickle(II) Bound in the Copper Site",published,journal,J. Am. Chem. Soc.,,112,,,,,,,,,,,,,,,,,,,,,,,6374,6383,1990, citations,entry_citation,1043,6948,1,,entry citation,,,,,"Ming, Li-June, Valentine, Joan Selverstone, ""NMR Studies of Nickle(II)-Substituted Derivatives of Bovine Copper-Zinc Superoxide Dismutase with Nickle(II) Bound in the Copper Site,"" J. Am. Chem. Soc. 112, 6374-6383 (1990).","NMR Studies of Nickle(II)-Substituted Derivatives of Bovine Copper-Zinc Superoxide Dismutase with Nickle(II) Bound in the Copper Site",published,journal,J. Am. Chem. Soc.,,112,,,,,,,,,,,,,,,,,,,,,,,6374,6383,1990, citations,entry_citation,1044,6962,1,,entry citation,,,,,"Ming, Li-June, Valentine, Joan Selverstone, ""NMR Studies of Nickle(II)-Substituted Derivatives of Bovine Copper-Zinc Superoxide Dismutase with Nickle(II) Bound in the Copper Site,"" J. Am. 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Chem.,,250,16,,,,,,,,,,,,,,,,,,,,,,6381,6402,1975, citations,citation_1,11140,9973,1,,entry citation,,,,,,Solution structure of the 4th KH type I domain from human Vigilin,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11141,9991,1,,entry citation,,,,,,Solution structure of the CH domain from human Vav-3 protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11142,10009,1,,entry citation,,,,,,Solution structure of the CH domain from human Smoothelin splice isoform L2,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11143,10027,1,,entry citation,,,,,,Solution structure of the CH domain from human MICAL-3 protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11144,10045,1,,entry citation,,,,,,"Solution structure of the DnaJ domain from human Williams-Beuren syndrome chromosome region 18 protein",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11145,10063,1,,entry citation,,,,,,Solution structure of the CH domain from human EH domain binding protein 1,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11146,10081,1,,entry citation,,,,,,"Solution structure of the eIF-5_eIF-2B domain from human Eukaryotic translation initiation factor 5",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11147,10101,1,,entry citation,,,,,,"Solution structure of the tandem HMG box domain from Human High mobility group protein B1",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11148,10119,1,,entry citation,,,,,,"Solution structure of the TIG domain from Human Nuclear factor of activated T-cells, cytoplasmic 4",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,11149,10137,1,,entry citation,,,,,,Structural study of the UBA domain of p62 and its interaction with ubiquitin,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1115,10153,1,,entry citation,,,,,"Oldfield, Eric, Norton, Raymond S., Allerhand, Adam, ""Studies of Individual Carbon Sites of Proteins in Solution by Natural Abundance Carbon 13 Nuclear Magnetic Resonance Spectroscopy,"" J. Biol. Chem. 250 (16), 6381-6402 (1975).","Studies of Individual Carbon Sites of Proteins in Solution by Natural Abundance Carbon 13 Nuclear Magnetic Resonance Spectroscopy",published,journal,J. Biol. Chem.,,250,16,,,,,,,,,,,,,,,,,,,,,,6381,6402,1975, citations,citation_1,11150,10169,1,,entry citation,,,,,,"Solution structure of the Somatomedin B domain of human Ectonucleotide pyrophosphatase/phosphodiesterase family member",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11151,10187,1,,entry citation,,,,,,"Solution structure of the first Phorbol esters/diacylglycerol binding domain of human Protein kinase C, delta",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11152,10207,1,,entry citation,,,,,,Solution structure of the fibronectin type III domain of human Integrin beta-4,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11153,10225,1,,entry citation,,,,,,"Solution structure of the SH3 domain of 130 kDa phosphatidylinositol 4,5-biphosphate-dependent ARF1 GTPase-activating protein",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11154,10243,1,,entry citation,,,,,,"Solution structure of the SH3 domain of Sorbin and SH3 domain-containing protein 1",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11155,10261,1,,entry citation,,,,,,Solution structure of the SH3 domain of Abl interactor 2 (Abelson interactor 2),in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11156,10278,1,,entry citation,,,,,,Solution structure of the SH3 domain of human Nostrin,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11157,10296,1,,entry citation,,,,,,"Solution structure of the BTK motif of human Cytoplasmic tyrosine-protein kinase BMX",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11158,10316,1,,entry citation,,,,,,Solution structure of the HMG box of human Transcription factor SOX-17,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11159,10334,1,,entry citation,,,,,,Solution structure of the Ring finger of human Retinoblastoma-binding protein 6,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1116,10354,1,,entry citation,,,,,"Oldfield, Eric, Norton, Raymond S., Allerhand, Adam, ""Studies of Individual Carbon Sites of Proteins in Solution by Natural Abundance Carbon 13 Nuclear Magnetic Resonance Spectroscopy,"" J. 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Chem.,,250,16,,,,,,,,,,,,,,,,,,,,,,6381,6402,1975, citations,citation_1,11160,10370,1,,entry citation,,,,,,"Solution structure of the HMG box of human Myeloid/lymphoid or mixed-lineage leukemia protein 3 homolog",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11161,10388,1,,entry citation,,,,,,"Solution structure of the Zinc finger, C3HC4 type (RING finger) domain Tripartite motif protein 30",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11162,10408,1,,entry citation,,,,,,"Solution structure of the Zinc finger, C3HC4 type (RING finger) domain of RING finger protein 126",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11163,10428,1,,entry citation,,,,,,"Solution structure of the Zinc finger, C3HC4 type (RING finger) domain of Tripartite motif-containing protein 5",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11164,10448,1,,entry citation,,,,,,"Solution structure of the Zinc finger, C3HC4 type (RING finger) domain of TNF receptor-associated factor 3",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11165,10468,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 329-359) of human Zinc finger protein 268",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11166,10488,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 581-609) of human Zinc finger protein 268",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11167,10508,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 508-540) of human Zinc finger protein 347",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11168,10528,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 732-764) of human Zinc finger protein 347",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11169,10548,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc finger (region 435-467) of human Zinc finger protein 484",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1117,10568,1,,entry citation,,,,,"Oldfield, Eric, Norton, Raymond S., Allerhand, Adam, ""Studies of Individual Carbon Sites of Proteins in Solution by Natural Abundance Carbon 13 Nuclear Magnetic Resonance Spectroscopy,"" J. 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Chem.,The Journal of biological chemistry,286,8,,,,,,,,,,,,,,,,,,,,,,6720,6732,2011, citations,citation_1,11178,10709,1,,entry citation,,,,,,"Solution structure of the SH3 domain of human olygophrein-1 like protein (KIAA0621)",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11179,10727,1,,entry citation,,,,,,Solution structure of the SH3 domain of SH3-domain kinase binding protein 1,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11180,10745,1,,entry citation,,,,,,Solution structure of the first SH3 domain of KIAA0318 protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11181,10763,1,,entry citation,,,,,,Solution structure of the fourth fn3 domain of KIAA1496 protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11182,10781,1,,entry citation,,,,,,Solution structure of the PDZ domain of human KIAA0340 protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11183,10800,1,,entry citation,,,,,,Solution structure of the FNIII domain of human RIM-binding protein 2,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11184,10818,1,,entry citation,,,,,,Solution structure of the second SH3 domain of human RIM-binding protein 2,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11185,10836,1,,entry citation,,,,,,Solution structure of the third SH3 domain of human RIM-binding protein 2,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11186,10854,1,,entry citation,,,,,,Solution structure of the fifth PDZ domain of InaD-like protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11187,10872,1,,entry citation,,,,,,Solution structure of the 7th PDZ domain of InaD-like protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11188,10890,1,,entry citation,,,,,,Solution structure of the first PDZ domain of InaD-like protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11189,10908,1,,entry citation,,,,,,Solution structure of the second PDZ domain of human InaD-like protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11190,10926,1,,entry citation,,,,,,Solution structure of the third PDZ domain of human InaD-like protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11191,10945,1,,entry citation,,,,,,Solution structure of the eighth PDZ domain of human InaD-like protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11192,10963,1,,entry citation,,,,,,"Solution structure of the Ig-like domain(433 - 525) of murine myosin-binding protein C, fast-type",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11193,10981,1,,entry citation,,,,,,Solution structure of the first SH3 domain from human KIAA0418 protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11194,10999,1,,entry citation,,,,,,Solution structure of the fifth SH3 domain from human KIAA0418 protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11195,11017,1,,entry citation,,,,,,"Solution structure of the PDZ domain of human Rho guanine nucleotide exchange factor 11",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11196,11035,1,,entry citation,,,,,,Solution structure of the third SH3 domain from human KIAA1666 protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11197,11053,1,,entry citation,,,,,,Solution structure of the sixth PDZ domain of human InaD-like protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11198,11071,1,,entry citation,,,,,,Solution structure of the third PDZ domain of synapse-associated protein 102,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11199,11089,1,,entry citation,,,,,,Solution structure of the PDZ domain of Enigma homologue protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,112,11107,1,,entry citation,,,,,"Koyama, Satoshi, Kobayashi, Yuji, Norioka, Shigemi, Kyogoku, Yoshimasa, Ikenaka, Tokuji, ""Conformational Studies by 1H Nuclear Magnetic Resonance of the Trypsin-Chymotrypsin Inhibitor B-III from Peanuts and Its Enzymatically Modified Derivative,"" Biochemistry 25, 8076-8082 (1986).","Conformational Studies by 1H Nuclear Magnetic Resonance of the Trypsin-Chymotrypsin Inhibitor B-III from Peanuts and Its Enzymatically Modified Derivative",published,journal,Biochemistry,,25,,,,,,,,,,,,,,,,,,,,,,,8076,8082,1986, citations,entry_citation,1120,11120,1,,entry citation,,,,,"Torigoe, Hidetaka, Shimada, Ichio, Saito, Akiko, Sato, Moriyuki, Arata, Yoji, ""Sequential 1H NMR Assignments and Secondary Structure of the B Domain of Staphylococcal Protein A: Structural Changes between the Free B Domain in Solution and the Fc-Bound B Domain in Crystal,"" Biochemistry 29, 8787-8793 (1990).","Sequential 1H NMR Assignments and Secondary Structure of the B Domain of Staphylococcal Protein A: Structural Changes between the Free B Domain in Solution and the Fc-Bound B Domain in Crystal",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,8787,8793,1990, citations,citation_1,11200,11133,1,,entry citation,,,,,,Solution structure of the PDZ domain of Pals1 protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11201,11151,1,,entry citation,,,,,,Solution structure of the fourth PDZ domain of KIAA1095 protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11202,11169,1,,entry citation,,,,,,Solution structure of the PDZ domain of Spinophilin/NeurabinII protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11203,11187,1,,entry citation,,,,,,"Solution structure of the core domain of calcyclin binding protein; siah-interacting protein (SIP)",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11204,11205,1,,entry citation,,,,,,Solution structure of the second PDZ domain of harmonin protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11205,11223,1,,entry citation,,,,,,"Solution structure of the first and second zf-C2H2 domain of Zinc finger protein 435",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11206,11243,1,,entry citation,,,,,,"Solution structure of the fourth PDZ domain of Glutamate receptor interacting protein 2",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11207,11262,1,,entry citation,,,,,,Solution structure of the first PDZ domain of scribble homolog protein (hScrib),in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11208,11281,1,,entry citation,,,,,,Solution structure of the second fn3 domain of Eph receptor A8 protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11209,11300,1,,entry citation,,,,,,Solution structure of the SH3 domain of Endophilin B1 (Sh3g1b1),in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11210,11318,1,,entry citation,,,,,,"Solution structure of the first PDZ domain of amyloid beta A4 precursor protein-binding family A, member 1",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11211,11336,1,,entry citation,,,,,,"Solution structure of the third ig-like domain of Myosin-dinding protein C, slow-type",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11212,11355,1,,entry citation,,,,,,"Solution structure of the first ig-like domain of Myosin-binding protein C, slow-type",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11213,11374,1,,entry citation,,,,,,Solution structure of the SH3 domain of Hypothetical protein SH3YL1,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11214,11392,1,,entry citation,,,,,,Solution structure of the SH3 domain of Fyn-related kinase,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11215,11410,1,,entry citation,,,,,,"Solution structure of the PDZ domain of T-cell lymphoma invasion and metastasis 1 varian",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11216,11428,1,,entry citation,,,,,,Solution structure of the third PDZ domain of PDZ domain containing protein 1,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11217,11447,1,,entry citation,,,,,,Solution structure of the first SH3 domain of Stac protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11218,11465,1,,entry citation,,,,,,Solution structure of the CIDE-N domain of human cell death activator CIDE-A,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11219,11483,1,,entry citation,,,,,,"Solution structure of the first SH3 domain of human sorbin and Sh3 domain-containing protein 1",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11220,11502,1,,entry citation,,,,,,Solution structure of the second SH3 domain of human KIAA0769 protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11221,11520,1,,entry citation,,,,,,"Solution structure of the Ig-like domain (615-713) from human Obscurin-like protein 1",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11222,11538,1,,entry citation,,,,,,Solution structure of the first SH3 domain of human KIAA0769 protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11223,11556,1,,entry citation,,,,,,"Solution structure of the Ig-like domain of human Leucine-rich repeat-containing protein 4",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11224,11574,1,,entry citation,,,,,,"Solution structure of the SH3 domain from Phospholipase C, gamma 2",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11225,11592,1,,entry citation,,,,,,"Solution structure of the SH3 domain of human SLIT-ROBO Rho GTPase-activating protein 2",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11226,11610,1,,entry citation,,,,,,Solution structure of the PDZ domain from Human MAGUK p55 subfamily member 2,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11227,11628,1,,entry citation,,,,,,Solution structure of the second fn3 domain from human Ephrin type-B receptor 4,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11228,11646,1,,entry citation,,,,,,"Solution structure of the SH3 domain from Rho guanine nucleotide exchange factor 9",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11229,11664,1,,entry citation,,,,,,"Solution structure of the Ig-like domain (714-804) from human Obscurin-like protein 1",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11230,11682,1,,entry citation,,,,,,Solution structure of the 6th Ig-like domain from human KIAA1556,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11231,11700,1,,entry citation,,,,,,Solution structure of the PKD domain from KIAA 1837 protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11232,11719,1,,entry citation,,,,,,Solution structure of the PKD domain (329-428) from human KIAA0319,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11233,11737,1,,entry citation,,,,,,Solution structure of the SH3 domain of human KIAA1783 protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11234,11755,1,,entry citation,,,,,,"Solution structure of the RING domain (1-66) from tripartite motif-containing protein 31",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11235,11775,1,,entry citation,,,,,,"Solution structure of the 6th Ig-like domain from human Myosin-binding protein C, fast-type",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11236,11793,1,,entry citation,,,,,,"Solution structure of the fourth Ig-like domain from myosin light chain kinase, smooth muscle",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11237,11811,1,,entry citation,,,,,,"Solution structure of the first and second PHD domain from Myeloid/lymphoid or mixed-lineage leukemia protein 3 homolog",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11238,11832,1,,entry citation,,,,,,"Solution structure of the C2H2-type zinc finger domain (699-729) from zinc finger protein 473",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11239,11852,1,,entry citation,,,,,,"Solution structure of the C2H2-type zinc finger domain (781-813) from zinc finger protein 473",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11240,11872,1,,entry citation,,,,,,"Solution structure of the e3_binding domain of dihydrolipoamide branched chaintransacylase",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11242,11890,1,,entry citation,,,,,,Solution structure of the first SH3 domain of human vinexin,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11244,11908,1,,entry citation,,,,,,"Solution structure of the first SANT domain from human nuclear receptor corepressor 1",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11245,11926,1,,entry citation,,,,,,"Solution Structure of the murine ubiquitin-like 5 protein from RIKEN cDNA 0610031K06",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11246,11944,1,,entry citation,,,,,,Solution structure of the FHA domain of mouse Afadin 6,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11247,11962,1,,entry citation,,,,,,Solution structure of the FHA domain of human ubiquitin ligase protein RNF8,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11248,11981,1,,entry citation,,,,,,Solution structure of the PDZ domain from mouse LIM domain kinase,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,11249,11999,1,,entry citation,,,21086077,,,"1H, 13C, and 15N resonance assignments of reduced GrxS14 from Populus tremula tremuloides.",published,journal,Biomol. 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Biochem.,The Journal of Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11253,12078,1,,entry citation,,,,,,"Solution Structure of the Ubiquitin-like Domain from Mouse Hypothetical 1700011N24Rik Protein",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11254,12096,1,,entry citation,,,,,,"Solution Structure of a N-terminal Ubiquitin-like Domain in Mouse Tubulin-specific Chaperone B",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11255,12114,1,,entry citation,,,,,,"Solution Structure of Anticodon Binding Domain from Nuclear Receptor Coactivator 5 (Human KIAA1637 Protein)",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11256,12132,1,,entry citation,,,,,,"Solution Structure of the N-terminal Ubiquitin-like Domain of Mouse Ubiquitin Specific Protease 14 (USP14)",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11257,12150,1,,entry citation,,,,,,Solution Structure of Mouse Ubiquitin-like 3 Protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11258,12168,1,,entry citation,,,,,,Solution Structure of Mouse Hypothetical Protein 2900073H19RIK,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11259,12186,1,,entry citation,,,,,,"Solution Structure of CUE domain in the C-terminal of Human Toll-interacting Protein (Tollip)",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11260,12204,1,,entry citation,,,,,,Solution Structure of UBA domain of Human Ubiquitin Associated Protein 1 (UBAP1),in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11261,12222,1,,entry citation,,,,,,"Solution Structure of the N-terminal Ubiquitin-like Domain in the Human Ubiquilin 3 (UBQLN3)",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11262,12240,1,,entry citation,,,,,,"Solution Structure of the N-terminal Ubiquitin-like Domain in the 4931431F19Rik Protein",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11263,12258,1,,entry citation,,,,,,"Solution Structure of the N-terminal Ubiquitin-like Domain in the Human BAT3 Protein",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11264,12276,1,,entry citation,,,,,,Solution Structure of Ras-binding Domain in Mouse AF-6 Protein,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11265,12294,1,,entry citation,,,,,,"Solution Structure of the N-terminal Ras-binding Domain (RBD) in Human a-Raf Kinase",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11266,12312,1,,entry citation,,,,,,"Solution Structure of the N-terminal Ubiquitin-like Domain in Human Np95/ICBP90-like Ring Finger Protein (NIRF)",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11267,12330,1,,entry citation,,,,,,"Solution Structure of Human SUMO-2 (SMT3B), a Ubiquitin-like Protein",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11268,12348,1,,entry citation,,,,,,"Solution Structure of the N-terminal Ubiquitin-like Domain in Mouse Ubiquitin-like Protein SB132",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11269,12366,1,,entry citation,,,,,,"Solution Structure of the N-terminal CUE Domain in the Human Mitogen-activated Protein Kinase Kinase Kinase 7 Interacting Protein 2 (MAP3K7IP2)",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1127,12384,1,,entry citation,,,,,"Haruyama, Hideyuki, Qian, Yan-qiu, Wuthrich, Kurt, ""Static and Transient Hydrogen-Bonding Interactions in Recombinant Desulfatohirudin Studied by 1H Nuclear Magnetic Resonance Measurements of Amide Proton Exchange Rates and pH-Dependent Chemical Shifts,"" Biochemistry 28, 4312-4317 (1989).","Static and Transient Hydrogen-Bonding Interactions in Recombinant Desulfatohirudin Studied by 1H Nuclear Magnetic Resonance Measurements of Amide Proton Exchange Rates and pH-Dependent Chemical Shifts",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,4312,4317,1989, citations,citation_1,11270,12397,1,,entry citation,,,,,,"Solution Structure of the Novel Identified Ubiquitin-like Domain in the Human Hypothetical Protein FLJ35834",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11271,12415,1,,entry citation,,,,,,Solution Structure of the C-terminal UBA Domain in the Human Ubiquilin 3,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11272,12433,1,,entry citation,,,,,,"Solution Structure of the Novel Identified Ubiquitin-like Domain in the Human COBL-like 1 Protein",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11273,12451,1,,entry citation,,,,,,"Solution Structure of the Novel Identified UBA-like Domain in the N-terminal of Human Fas Associated Factor 1 Protein",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11274,12469,1,,entry citation,,,,,,"Solution Structure of the Novel Identified UBA-like Domain in the N-terminal of Human ETEA Protein",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11275,12487,1,,entry citation,,,,,,"Solution Structure of the RRM Domain in the Human Poly (ADP-ribose) Polymerase Family, Member 10 Variant",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11276,12505,1,,entry citation,,,,,,"Solution Structure of the CUE Domain in the Human CUE Domain Containing Protein 1 (CUEDC1)",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11277,12523,1,,entry citation,,,,,,"Solution Structure of the RA Domain in the Human Link Guanine Nucleotide Exchange Factor II (Link-GEFII)",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11278,12541,1,,entry citation,,,,,,"Solution Structure of the CUE Domain in the Human Activating Signal Cointegrator 1 Complex Subunit 2 (ASCC2)",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11279,12559,1,,entry citation,,,,,,"2DZI/Solution Structure of the N-terminal Ubiquitin-like Domain in Human Ubiquitin-like Protein 4A (GDX)",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1128,12577,1,,entry citation,,,,,"Haruyama, Hideyuki, Wuthrich, Kurt, ""Conformation of Recombinant Desulfatohirudin in Aqueous Solution Determined by Nuclear Magnetic Resonance,"" Biochemistry 28, 4301-4312 (1989).","Conformation of Recombinant Desulfatohirudin in Aqueous Solution Determined by Nuclear Magnetic Resonance",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,4301,4312,1989, citations,citation_1,11280,12590,1,,entry citation,,,,,,"2DZJ/Solution Structure of the N-terminal Ubiquitin-like Domain in Human Synaptic Glycoprotein SC2",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11281,12608,1,,entry citation,,,,,,Structure of the UBX domain in Mouse UBX Domain-Containing Protein 2,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11282,12626,1,,entry citation,,,,,,Solution Structure of the UBA domain in Human Protein FAM100B,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11283,12644,1,,entry citation,,,,,,"Solution Structure of the Ubiquitin-like Domain in Human FAS-associated factor 1 (hFAF1)",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11284,12662,1,,entry citation,,,,,,Solution structure of the SH3 domain of human hypothetical protein FLJ21522,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11285,12680,1,,entry citation,,,,,,Solution structure of the SH3 domain of mouse peroxisomal biogenesis factor 13,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11286,12698,1,,entry citation,,,,,,Solution structure of the BSD domain of human Synapse associated protein 1,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11287,12716,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc-binding domain of human zinc finger protein 292",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11288,12736,1,,entry citation,,,,,,"Solution structure of the fibronectin type-III domain of human fibronectin type-III domain containing protein 3a",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11289,12754,1,,entry citation,,,,,,Solution structure of the LIM domain of human Leupaxin,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1129,12774,1,,entry citation,,,,,"Haruyama, Hideyuki, Wuthrich, Kurt, ""Conformation of Recombinant Desulfatohirudin in Aqueous Solution Determined by Nuclear Magnetic Resonance,"" Biochemistry 28, 4301-4312 (1989).","Conformation of Recombinant Desulfatohirudin in Aqueous Solution Determined by Nuclear Magnetic Resonance",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,4301,4312,1989, citations,citation_1,11290,12787,1,,entry citation,,,,,,"Solution structure of the fibronectin type-III domain of human fibronectin type III domain containing protein 3",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11291,12805,1,,entry citation,,,,,,"Solution structure of the fibronectin type-III domain of mouse myosin-binding protein C, Fast-type homolog",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11292,12823,1,,entry citation,,,,,,"Solution structure of the fibronectin type-III domain of human protein tyrosine phosphatase, receptor type, D isoform 4 variant",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11293,12841,1,,entry citation,,,,,,Solution structure of the LIM domain of human Cysteine-rich protein 2,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11294,12861,1,,entry citation,,,,,,Solution structure of the RWD domain of human RWD omain containing protein 2,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11295,12879,1,,entry citation,,,,,,Solution structure of the RWD domain of human protein C21orf6,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11296,12897,1,,entry citation,,,,,,Solution structure of the RWD domain of human ring finger protein 25,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11297,12915,1,,entry citation,,,,,,Solusion structure of the Todor domain of human Lamin-B receptor,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11298,12933,1,,entry citation,,,,,,"Solution structure of the BSD domain of human TFIIH basal transcription factor complex p62 subunit",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11299,12951,1,,entry citation,,,,,,"Solution structure of the SH3 domain of the human 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structure of the Fibronectin type-III domain of human Neural cell adhesion molecule 2",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11305,13061,1,,entry citation,,,,,,Solution Structure of the LIM Domain of the Human Actin Binding LIM Protein 2,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11306,13081,1,,entry citation,,,,,,Solution Structure of the Ring-H2 Finger Domain of Mouse Deltex Protein 2,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11307,13101,1,,entry citation,,,,,,"Solution Structure of the RING finger Domain of the human UbcM4-interacting Protein 4",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11308,13121,1,,entry citation,,,,,,"Solution structure of the C2H2 zinc finger domain of the protein arginine N-methyltransferase 3 from Mus musculus",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11309,13141,1,,entry citation,,,,,,"Solution structure of the N-terminal zinc finger domain of mouse cell growth regulating nucleolar protein LYAR",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11310,13161,1,,entry citation,,,,,,"Solution structure of the C-terminal domain of mouse phosphoacetylglucosamine mutase (PAGM)",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11311,13179,1,,entry citation,,,,,,"Solution structure of the FAS1 domain of human transforming growth factor-beta induced protein IG-H3",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11312,13197,1,,entry citation,,,,,,"Solution structure of the C2H2 type zinc-binding domain of human zinc finger protein 64, isoforms 1 and 2",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11313,13217,1,,entry citation,,,,,,Solution structure of the RING domain of the Zinc finger protein 183-like 1,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, 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citations,citation_1,11357,14108,1,,entry citation,,,,,,Solution structure of WW domain in transcription elongation regulator 1,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,11358,14126,1,,entry citation,,,20826339,,,Structural insight into the zinc finger CW domain as a histone modification reader.,published,journal,Structure,"Structure (London, England : 1993)",18,9,,,,,,,,,,,,,,,,,,,,,,1127,1139,2010, citations,citation_1,11359,14147,1,,entry citation,,,20826339,,,Structural insight into the zinc finger CW domain as a histone modification reader.,published,journal,Structure,"Structure (London, England : 1993)",18,9,,,,,,,,,,,,,,,,,,,,,,1127,1139,2010, citations,entry_citation,1136,14169,1,,entry citation,,,,,"Torigoe, Hidetaka, Shimada, Ichio, Waelchli, Markus, Saito, Akiko, Sato, Moriyuki, Arata, Yoji, ""15N nuclear magnetic resonance studies of the B domain of Staphylococcal protein A: Sequence specific assignments of the imide 15N resonances of the 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Biochemistry 29, 8998-9006 (1990).","Conformational Requirement of Signal Sequences Functioning in Yeast: Circular Dichroism and 1H Nuclear Magnetic Resonance Studies of Synthetic Peptides",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,8998,9006,1990, citations,citation_1,11370,14399,1,,entry citation,,,18500819,,,Solution structure of the second RNA recognition motif (RRM) domain of murine T cell intracellular antigen-1 (TIA-1) and its RNA recognition mode.,published,journal,Biochemistry,Biochemistry,47,24,,,,,,,,,,,,,,,,,,,,,,6437,6450,2008, citations,citation_1,11371,14413,1,,entry citation,,,18500819,,,Solution structure of the second RNA recognition motif (RRM) domain of murine T cell intracellular antigen-1 (TIA-1) and its RNA recognition mode.,published,journal,Biochemistry,Biochemistry,47,24,,,,,,,,,,,,,,,,,,,,,,6437,6450,2008, citations,citation_1,11372,14427,1,,entry citation,,,18500819,,,Solution structure of the second RNA recognition motif (RRM) domain of murine 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J.,Biophysical journal,104,10,,0006-3495,,,,,,,,,,,,,,,,,,,,2222,2234,2013, citations,entry_citation,11512,16870,1,,entry citation,,,23271376,,,Secondary structural analysis of proteins based on (13)C chemical shift assignments in unresolved solid-state NMR spectra enhanced by fragmented structure database,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,55,2,,1573-5001,,,,,,,,,,,,,,,,,,,,189,200,2013, citations,entry_citation,11513,16885,1,,entry citation,,,,,,Chitosan-binding modules derived from Paenibacillus fukuinensis D1 : binding mode and specificity evaluated from NMR spectroscopy,in preparation,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,reference,11513,16886,2,,reference citation,,,11854270,,,Biochemical and genetic properties of Paenibacillus glycosyl hydrolase having chitosanase activity and discoidin domain.,published,journal,J. Biol. 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Chem.,The Journal of biological chemistry,288,20,,1083-351X,,,,,,,,,,,,,,,,,,,,14408,14416,2013, citations,entry_citation,11516,16928,1,,entry citation,,,,,,THE SOLUTION STRUCTURE OF THE C-TERMINAL DOMAIN OF HUMAN ACTIVATOR OF 90 KDA HEAT SHOCK PROTEIN ATPASE HOMOLOG 1,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,11519,16946,1,,entry citation,,,,,,Reduced native state stability in crowded cellular environment due to protein-protein interactions,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1152,16963,1,,entry citation,,,,,"Miura, Shigetoshi, Ichikawa, Yoshiyuki, ""Conformational Change of Adrenodoxin Induced by Reduction of Iron-Sulfur Cluster,"" J. Biol. Chem. 266 (10), 6252-6258 (1991).",Conformational Change of Adrenodoxin Induced by Reduction of Iron-Sulfur Cluster,published,journal,J. Biol. Chem.,,266,10,,,,,,,,,,,,,,,,,,,,,,6252,6258,1991, citations,entry_citation,11520,16976,1,,entry citation,,,,,,Reduced native state stability in crowded cellular environment due to protein-protein interactions,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,11521,16993,1,,entry citation,,,,,,Reduced native state stability in crowded cellular environment due to protein-protein interactions,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,11522,17010,1,,entry citation,,,23708873,,,"1H, 13C and 15N backbone resonance assignments of the monomeric human M-ficolin fibrinogen-like domain secreted by Brevibacillus choshinensis",published,journal,Biomol NMR Assign.,Biomolecular NMR Assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,11523,17026,1,,entry citation,,,23770370,,,"Structure of the second RRM domain of Nrd1, a fission yeast MAPK target RNA binding protein, and implication for its RNA recognition and regulation",published,journal,Biochem. 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Commun.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,11534,17224,1,,entry citation,,,24322300,,,Identification of residues required for stalled-ribosome rescue in the codon-independent release factor YaeJ,published,journal,Nucleic Acids Res.,,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,11535,17243,1,,entry citation,,,24425781,,,Experimental conversion of a defensin into a neurotoxin: implications for origin of toxic function,published,journal,Mol. Biol. 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Acta,,1019,,,,,,,,,,,,,,,,,,,,,,,283,292,1990, citations,entry_citation,1211,19317,1,,entry citation,,,,,"van de Kamp, Mart, Hali, Frits C., Rosato, Nicola, Finazzi Agro, Alessandro, Canters, Gerard W., ""Purification and characterization of a non-reconstitutable azurin, obtained by heterologous expression of the Pseudomonas aeruginosa azu gene in Escherichia coli,"" Biochim. Biophys. Acta 1019, 283-292 (1990).","Purification and characterization of a non-reconstitutable azurin, obtained by heterologous expression of the Pseudomonas aeruginosa azu gene in Escherichia coli",published,journal,Biochim. Biophys. Acta,,1019,,,,,,,,,,,,,,,,,,,,,,,283,292,1990, citations,entry_citation,1212,19330,1,,entry citation,,,,,"van de Kamp, Mart, Hali, Frits C., Rosato, Nicola, Finazzi Agro, Alessandro, Canters, Gerard W., ""Purification and characterization of a non-reconstitutable azurin, obtained by heterologous expression of the Pseudomonas aeruginosa azu gene in Escherichia coli,"" Biochim. Biophys. Acta 1019, 283-292 (1990).","Purification and characterization of a non-reconstitutable azurin, obtained by heterologous expression of the Pseudomonas aeruginosa azu gene in Escherichia coli",published,journal,Biochim. Biophys. Acta,,1019,,,,,,,,,,,,,,,,,,,,,,,283,292,1990, citations,entry_citation,1213,19343,1,,entry citation,,,,,"van de Kamp, Mart, Hali, Frits C., Rosato, Nicola, Finazzi Agro, Alessandro, Canters, Gerard W., ""Purification and characterization of a non-reconstitutable azurin, obtained by heterologous expression of the Pseudomonas aeruginosa azu gene in Escherichia coli,"" Biochim. Biophys. Acta 1019, 283-292 (1990).","Purification and characterization of a non-reconstitutable azurin, obtained by heterologous expression of the Pseudomonas aeruginosa azu gene in Escherichia coli",published,journal,Biochim. Biophys. Acta,,1019,,,,,,,,,,,,,,,,,,,,,,,283,292,1990, citations,entry_citation,1214,19356,1,,entry citation,,,,,"van de Kamp, Mart, Hali, Frits C., Rosato, Nicola, Finazzi Agro, Alessandro, Canters, Gerard W., ""Purification and characterization of a non-reconstitutable azurin, obtained by heterologous expression of the Pseudomonas aeruginosa azu gene in Escherichia coli,"" Biochim. Biophys. Acta 1019, 283-292 (1990).","Purification and characterization of a non-reconstitutable azurin, obtained by heterologous expression of the Pseudomonas aeruginosa azu gene in Escherichia coli",published,journal,Biochim. Biophys. Acta,,1019,,,,,,,,,,,,,,,,,,,,,,,283,292,1990, citations,entry_citation,1215,19369,1,,entry citation,,,,,"van de Kamp, Mart, Hali, Frits C., Rosato, Nicola, Finazzi Agro, Alessandro, Canters, Gerard W., ""Purification and characterization of a non-reconstitutable azurin, obtained by heterologous expression of the Pseudomonas aeruginosa azu gene in Escherichia coli,"" Biochim. Biophys. Acta 1019, 283-292 (1990).","Purification and characterization of a non-reconstitutable azurin, obtained by heterologous expression of the Pseudomonas aeruginosa azu gene in Escherichia coli",published,journal,Biochim. Biophys. Acta,,1019,,,,,,,,,,,,,,,,,,,,,,,283,292,1990, citations,entry_citation,15008,20899,1,,entry citation,,,17350627,,,Predominantly buried residues in the response regulator Spo0F influence specific sensor kinase recognition,published,journal,FEBS Lett.,,581,7,,,,,,,,,,,,,,,,,,,,,,1425,1429,2007, citations,entry_citation,1216,19382,1,,entry citation,,,,,"van de Kamp, Mart, Hali, Frits C., Rosato, Nicola, Finazzi Agro, Alessandro, Canters, Gerard W., ""Purification and characterization of a non-reconstitutable azurin, obtained by heterologous expression of the Pseudomonas aeruginosa azu gene in Escherichia coli,"" Biochim. Biophys. Acta 1019, 283-292 (1990).","Purification and characterization of a non-reconstitutable azurin, obtained by heterologous expression of the Pseudomonas aeruginosa azu gene in Escherichia coli",published,journal,Biochim. Biophys. Acta,,1019,,,,,,,,,,,,,,,,,,,,,,,283,292,1990, citations,entry_citation,1217,19395,1,,entry citation,,,,,"van de Kamp, Mart, Hali, Frits C., Rosato, Nicola, Finazzi Agro, Alessandro, Canters, Gerard W., ""Purification and characterization of a non-reconstitutable azurin, obtained by heterologous expression of the Pseudomonas aeruginosa azu gene in Escherichia coli,"" Biochim. Biophys. Acta 1019, 283-292 (1990).","Purification and characterization of a non-reconstitutable azurin, obtained by heterologous expression of the Pseudomonas aeruginosa azu gene in Escherichia coli",published,journal,Biochim. Biophys. Acta,,1019,,,,,,,,,,,,,,,,,,,,,,,283,292,1990, citations,entry_citation,1218,19408,1,,entry citation,,,,,"van de Kamp, Mart, Hali, Frits C., Rosato, Nicola, Finazzi Agro, Alessandro, Canters, Gerard W., ""Purification and characterization of a non-reconstitutable azurin, obtained by heterologous expression of the Pseudomonas aeruginosa azu gene in Escherichia coli,"" Biochim. Biophys. Acta 1019, 283-292 (1990).","Purification and characterization of a non-reconstitutable azurin, obtained by heterologous expression of the Pseudomonas aeruginosa azu gene in Escherichia coli",published,journal,Biochim. Biophys. Acta,,1019,,,,,,,,,,,,,,,,,,,,,,,283,292,1990, citations,entry_citation,1219,19421,1,,entry citation,,,,,"van de Kamp, Mart, Hali, Frits C., Rosato, Nicola, Finazzi Agro, Alessandro, Canters, Gerard W., ""Purification and characterization of a non-reconstitutable azurin, obtained by heterologous expression of the Pseudomonas aeruginosa azu gene in Escherichia coli,"" Biochim. Biophys. Acta 1019, 283-292 (1990).","Purification and characterization of a non-reconstitutable azurin, obtained by heterologous expression of the Pseudomonas aeruginosa azu gene in Escherichia coli",published,journal,Biochim. Biophys. Acta,,1019,,,,,,,,,,,,,,,,,,,,,,,283,292,1990, citations,entry_citation,122,19434,1,,entry citation,,,,,"Driscoll, Paul C., Hill, H. Allen O., Redfield, Christina, ""1H-NMR sequential assignments and cation-binding studies of spinach plastocyanin,"" Eur. J. Biochem. 170, 279-292 (1987).",1H-NMR sequential assignments and cation-binding studies of spinach plastocyanin,published,journal,Eur. J. Biochem.,,170,,,,,,,,,,,,,,,,,,,,,,,279,292,1987, citations,entry_citation,1220,19447,1,,entry citation,,,,,"Bushuev, V., Tonevitskii, A., ""High Mobility of N-Terminal Parts of A and B Subunits of Ricin,"" J. Biomol. Struct. Dyn. 6 (6), 1061-1070 (1989).",High Mobility of N-Terminal Parts of A and B Subunits of Ricin,published,journal,J. Biomol. Struct. Dyn.,,6,6,,,,,,,,,,,,,,,,,,,,,,1061,1070,1989, citations,entry_citation,1221,19460,1,,entry citation,,,,,"Bushuev, V., Tonevitskii, A., ""High Mobility of N-Terminal Parts of A and B Subunits of Ricin,"" J. Biomol. Struct. Dyn. 6 (6), 1061-1070 (1989).",High Mobility of N-Terminal Parts of A and B Subunits of Ricin,published,journal,J. Biomol. Struct. Dyn.,,6,6,,,,,,,,,,,,,,,,,,,,,,1061,1070,1989, citations,entry_citation,1222,19473,1,,entry citation,,,,,"Hincke, Maxwell T., Sykes, Brian D., Kay, Cyril M., ""Laser Photochemically Induced Dynamic Nuclear Polarization Proton Nuclear Magnetic Resonance Studies on Three Homologous Calcium Binding Proteins: Cardiac Troponin-C, Skeletal Troponin-C, and Calmodulin,"" Biochemistry 20, 4185-4193 (1981).","Laser Photochemically Induced Dynamic Nuclear Polarization Proton Nuclear Magnetic Resonance Studies on Three Homologous Calcium Binding Proteins: Cardiac Troponin-C, Skeletal Troponin-C, and Calmodulin",published,journal,Biochemistry,,20,,,,,,,,,,,,,,,,,,,,,,,4185,4193,1981, citations,entry_citation,1225,19486,1,,entry citation,,,,,"Seamon, Kenneth B., Hartshorne, David J., Bothner-By, Aksel A., ""Ca2+ and Mg2+ Dependent Conformations of Troponin C as Determined by 1H and 19F Nuclear Magnetic Resonance,"" Biochemistry 16 (18), 4039-4046 (1977).","Ca2+ and Mg2+ Dependent Conformations of Troponin C as Determined by 1H and 19F Nuclear Magnetic Resonance",published,journal,Biochemistry,,16,18,,,,,,,,,,,,,,,,,,,,,,4039,4046,1977, citations,entry_citation,1226,19499,1,,entry citation,,,,,"Seamon, Kenneth B., Hartshorne, David J., Bothner-By, Aksel A., ""Ca2+ and Mg2+ Dependent Conformations of Troponin C as Determined by 1H and 19F Nuclear Magnetic Resonance,"" Biochemistry 16 (18), 4039-4046 (1977).","Ca2+ and Mg2+ Dependent Conformations of Troponin C as Determined by 1H and 19F Nuclear Magnetic Resonance",published,journal,Biochemistry,,16,18,,,,,,,,,,,,,,,,,,,,,,4039,4046,1977, citations,entry_citation,1227,19512,1,,entry citation,,,,,"Birnbaum, Edward R., Sykes, Brian D., ""Nuclear Magnetic Resonance Studied of a Ca2+-Binding Fragment of Troponin C.,"" Biochemistry 17 (23), 4965-4971 (1978).",Nuclear Magnetic Resonance Studied of a Ca2+-Binding Fragment of Troponin C.,published,journal,Biochemistry,,17,23,,,,,,,,,,,,,,,,,,,,,,4965,4971,1978, citations,entry_citation,1228,19525,1,,entry citation,,,,,"Birnbaum, Edward R., Sykes, Brian D., ""Nuclear Magnetic Resonance Studied of a Ca2+-Binding Fragment of Troponin C.,"" Biochemistry 17 (23), 4965-4971 (1978).",Nuclear Magnetic Resonance Studied of a Ca2+-Binding Fragment of Troponin C.,published,journal,Biochemistry,,17,23,,,,,,,,,,,,,,,,,,,,,,4965,4971,1978, citations,entry_citation,123,19538,1,,entry citation,,,,,"Widmer, Hans, Wagner, Gerhard, Schweitz, Hugues, Lazdunski, Michel, Wuthrich, Kurt, ""The Secondary Structure of the Toxin ATX Ia from Anemonia sulcata in Aqueous Solution Determined on the Basis of Complete Sequence-specific 1H NMR Assignments,"" Eur. J. Biochem. 171, 177-192 (1988).","The Secondary Structure of the Toxin ATX Ia from Anemonia sulcata in Aqueous Solution Determined on the Basis of Complete Sequence-specific 1H NMR Assignments",published,journal,Eur. J. Biochem.,,171,,,,,,,,,,,,,,,,,,,,,,,177,192,1988, citations,entry_citation,1230,19551,1,,entry citation,,,,,"Falzone, Christopher J., Benkovic, Stephen J., Wright, Peter E., ""Partial 1H NMR Assignments of the Escherichia coli Dihydrofolate Reductase Complex with Folate: Evidence for a Unique Conformation of Bound Folate,"" Biochemistry 29 (41), 9667-9677 (1990).","Partial 1H NMR Assignments of the Escherichia coli Dihydrofolate Reductase Complex with Folate: Evidence for a Unique Conformation of Bound Folate",published,journal,Biochemistry,,29,41,,,,,,,,,,,,,,,,,,,,,,9667,9677,1990, citations,entry_citation,126,19564,1,,entry citation,,,,,"Saito, Takeshi, Wormald, M.R., Williams, Robert J. P., ""Some structural features of the iron-uptake regulation protein,"" Eur. J. Biochem. 197, 29-38 (1991).",Some structural features of the iron-uptake regulation protein,published,journal,Eur. J. Biochem.,,197,,,,,,,,,,,,,,,,,,,,,,,29,38,1991, citations,entry_citation,1480,20593,1,,entry citation,,,,,"Barlow, P. N., Baron, Martin, Norman, David G., Day, A. J., Willis, Antony, Sim, R. B., Campbell, Iain D., ""Secondary Structure of a Complement Control Protein Module by Two-Dimensional 1H NMR,"" Biochemistry 30 (4), 997-1004 (1991).","Secondary Structure of a Complement Control Protein Module by Two-Dimensional 1H NMR",published,journal,Biochemistry,,30,4,,,,,,,,,,,,,,,,,,,,,,997,1004,1991, citations,entry_citation,127,19577,1,,entry citation,,,,,"Zuiderweg, Erik R. P., Kaptein, Robert, Wuthrich, Kurt, ""Sequence-specific resonance assignments in the 1H nuclear-magnetic-resonance spectrum of the Lac repressor DNA-binding domain 1-51 from Escherichia coli by two-dimensional spectroscopy,"" Eur. J. Biochem. 137, 279-292 (1983).","Sequence-specific resonance assignments in the 1H nuclear-magnetic-resonance spectrum of the Lac repressor DNA-binding domain 1-51 from Escherichia coli by two-dimensional spectroscopy",published,journal,Eur. J. Biochem.,,137,,,,,,,,,,,,,,,,,,,,,,,279,292,1983, citations,entry_citation,131,19590,1,,entry citation,,,,,"Pielak, Gary J., Boyd, Jonathan, Moore, Geoffrey R., Williams, Robert J. P., ""Proton-NMR studies show that the Thr-102 mutant of yeast iso-1-cytochrome is a typical member of the eukaryotic cytochrome c family,"" Eur. J. Biochem. 177, 167-177 (1988).","Proton-NMR studies show that the Thr-102 mutant of yeast iso-1-cytochrome is a typical member of the eukaryotic cytochrome c family",published,journal,Eur. J. Biochem.,,177,,,,,,,,,,,,,,,,,,,,,,,167,177,1988, citations,entry_citation,132,19606,1,,entry citation,,,,,"Labhardt, Alexander M., Hunziker-Kwik, Eng-Hiang, Wuthrich, Kurt, ""Secondary structure determination for alpha-neurotoxin from Dendroaspis polylepis polylepis based on sequence-specific 1H-nuclear-magnetic-resonance assignments,"" Eur. J. Biochem. 177, 295-305 (1988).","Secondary structure determination for alpha-neurotoxin from Dendroaspis polylepis polylepis based on sequence-specific 1H-nuclear-magnetic-resonance assignments",published,journal,Eur. J. Biochem.,,177,,,,,,,,,,,,,,,,,,,,,,,295,305,1988, citations,entry_citation,1323,19619,1,,entry citation,,,,,"Veitch, Nigel C., Concar, David W., Williams, Robert J. P., Whitford, David, ""Investigation of the solution structures and mobility of oxidised and reduced cytochrome b5 by 2D NMR spectroscopy,"" FEBS Lett. 238 (1), 49-55 (1988).","Investigation of the solution structures and mobility of oxidised and reduced cytochrome b5 by 2D NMR spectroscopy",published,journal,FEBS Lett.,,238,1,,,,,,,,,,,,,,,,,,,,,,49,55,1988, citations,entry_citation,1324,19632,1,,entry citation,,,,,"Veitch, Nigel C., Concar, David W., Williams, Robert J. P., Whitford, David, ""Investigation of the solution structures and mobility of oxidised and reduced cytochrome b5 by 2D NMR spectroscopy,"" FEBS Lett. 238 (1), 49-55 (1988).","Investigation of the solution structures and mobility of oxidised and reduced cytochrome b5 by 2D NMR spectroscopy",published,journal,FEBS Lett.,,238,1,,,,,,,,,,,,,,,,,,,,,,49,55,1988, citations,entry_citation,133,19645,1,,entry citation,,,,,"Hoffmann, Eberhard, Ruterjans, Heinz, ""Two-dimensional 1H-NMR investigation of ribonuclease T1 (Resonance assignments, secondary and low-resolution tertiary structures of ribonuclease T1),"" Eur. J. Biochem. 177, 539-560 (1988).","Two-dimensional 1H-NMR investigation of ribonuclease T1 (Resonance assignments, secondary and low-resolution tertiary structures of ribonuclease T1)",published,journal,Eur. J. Biochem.,,177,,,,,,,,,,,,,,,,,,,,,,,539,560,1988, citations,entry_citation,1333,19658,1,,entry citation,,,,,"Detlefsen, David J., Thanabal, V., Pecoraro, V. L., Wagner, Gerhard, ""Sequential 1H NMR Assignments of Iron(II) Cytochrome c551 from Pseudomonas aeruginosa,"" Biochemistry 29 (40), 9377-9386 (1990).","Sequential 1H NMR Assignments of Iron(II) Cytochrome c551 from Pseudomonas aeruginosa",published,journal,Biochemistry,,29,40,,,,,,,,,,,,,,,,,,,,,,9377,9386,1990, citations,entry_citation,1334,19671,1,,entry citation,,,,,"Detlefsen, David J., Thanabal, V., Pecoraro, V. L., Wagner, Gerhard, ""Sequential 1H NMR Assignments of Iron(II) Cytochrome c551 from Pseudomonas aeruginosa,"" Biochemistry 29 (40), 9377-9386 (1990).","Sequential 1H NMR Assignments of Iron(II) Cytochrome c551 from Pseudomonas aeruginosa",published,journal,Biochemistry,,29,40,,,,,,,,,,,,,,,,,,,,,,9377,9386,1990, citations,entry_citation,1336,19684,1,,entry citation,,,,,"Omichinski, James G., Clore, G. Marius, Appella, Ettore, Sakaguchi, Kazuyasu, Gronenborn, Angela M., ""High-Resolution Three-Dimensional Structure of a Single Zinc Finger from a Human Enhancer Binding Protein Solution,"" Biochemistry 29 (40), 9324-9334 (1990).","High-Resolution Three-Dimensional Structure of a Single Zinc Finger from a Human Enhancer Binding Protein Solution",published,journal,Biochemistry,,29,40,,,,,,,,,,,,,,,,,,,,,,9324,9334,1990, citations,entry_citation,1337,19697,1,,entry citation,,,,,"Omichinski, James G., Clore, G. Marius, Appella, Ettore, Sakaguchi, Kazuyasu, Gronenborn, Angela M., ""High-Resolution Three-Dimensional Structure of a Single Zinc Finger from a Human Enhancer Binding Protein Solution,"" Biochemistry 29 (40), 9324-9334 (1990).","High-Resolution Three-Dimensional Structure of a Single Zinc Finger from a Human Enhancer Binding Protein Solution",published,journal,Biochemistry,,29,40,,,,,,,,,,,,,,,,,,,,,,9324,9334,1990, citations,entry_citation,1338,19710,1,,entry citation,,,,,"Kotani, Susumu, Kawai, Gota, Yokoyama, Shigeyuki, Murofushi, Hiromu, ""Interaction Mechanism between Microtubule-Associated Proteins and Microtubules. A Proton Nuclear Resonance Analysis on the Binding of Synthetic Peptide to Tubulin,"" Biochemistry 29 (43), 10049-10054 (1990).","Interaction Mechanism between Microtubule-Associated Proteins and Microtubules. A Proton Nuclear Resonance Analysis on the Binding of Synthetic Peptide to Tubulin",published,journal,Biochemistry,,29,43,,,,,,,,,,,,,,,,,,,,,,10049,10054,1990, citations,entry_citation,1339,19723,1,,entry citation,,,,,"Kotani, Susumu, Kawai, Gota, Yokoyama, Shigeyuki, Murofushi, Hiromu, ""Interaction Mechanism between Microtubule-Associated Proteins and Microtubules. A Proton Nuclear Resonance Analysis on the Binding of Synthetic Peptide to Tubulin,"" Biochemistry 29 (43), 10049-10054 (1990).","Interaction Mechanism between Microtubule-Associated Proteins and Microtubules. A Proton Nuclear Resonance Analysis on the Binding of Synthetic Peptide to Tubulin",published,journal,Biochemistry,,29,43,,,,,,,,,,,,,,,,,,,,,,10049,10054,1990, citations,entry_citation,1343,19736,1,,entry citation,,,,,"Karslake, Christine, Piotto, Martial E., Pak, Youngmi K., Weiner, Henry, Gorenstein, David G., ""2D NMR and Structural Model for a Mitochondrial Signal Peptide Bound to a Micelle,"" Biochemistry 29 (42), 9872-9878 (1990).","2D NMR and Structural Model for a Mitochondrial Signal Peptide Bound to a Micelle",published,journal,Biochemistry,,29,42,,,,,,,,,,,,,,,,,,,,,,9872,9878,1990, citations,entry_citation,1344,19749,1,,entry citation,,,,,"Hua, Qingxin and Weiss, Michael, A., ""Toward the Solution Structure of Human Insulin: Sequential 2D 1H NMR Assignment of a Des-pentapeptide Analogue and Comparison with Crystal Structure,"" Biochemistry 29 (46), 10545-10555 (1990).","Toward the Solution Structure of Human Insulin: Sequential 2D 1H NMR Assignment of a Des-pentapeptide Analogue and Comparison with Crystal Structure",published,journal,Biochemistry,,29,46,,,,,,,,,,,,,,,,,,,,,,10545,10555,1990, citations,entry_citation,1346,19762,1,,entry citation,,,,,"Birdsall, B., Tendler, Saul J. B., Arnold, J.R.P., Feeney, J., Griffin, R. J., Carr, Mark D., Thomas, Janette A., Roberts, G.C.K., Stevens, M. F. G., ""NMR Studies of Multiple Conformations in Complexes of Lactobacillus casei Dihydrofolate Reductase with Analogues of Pyrimethamine,"" Biochemistry 29 (41), 9660-9667 (1990).","NMR Studies of Multiple Conformations in Complexes of Lactobacillus casei Dihydrofolate Reductase with Analogues of Pyrimethamine",published,journal,Biochemistry,,29,41,,,,,,,,,,,,,,,,,,,,,,9660,9667,1990, citations,entry_citation,1347,19775,1,,entry citation,,,,,"Birdsall, B., Tendler, Saul J. B., Arnold, J.R.P., Feeney, J., Griffin, R. J., Carr, Mark D., Thomas, Janette A., Roberts, G.C.K., Stevens, M. F. G., ""NMR Studies of Multiple Conformations in Complexes of Lactobacillus casei Dihydrofolate Reductase with Analogues of Pyrimethamine,"" Biochemistry 29 (41), 9660-9667 (1990).","NMR Studies of Multiple Conformations in Complexes of Lactobacillus casei Dihydrofolate Reductase with Analogues of Pyrimethamine",published,journal,Biochemistry,,29,41,,,,,,,,,,,,,,,,,,,,,,9660,9667,1990, citations,entry_citation,1348,19788,1,,entry citation,,,,,"Birdsall, B., Tendler, Saul J. B., Arnold, J.R.P., Feeney, J., Griffin, R. J., Carr, Mark D., Thomas, Janette A., Roberts, G.C.K., Stevens, M. F. G., ""NMR Studies of Multiple Conformations in Complexes of Lactobacillus casei Dihydrofolate Reductase with Analogues of Pyrimethamine,"" Biochemistry 29 (41), 9660-9667 (1990).","NMR Studies of Multiple Conformations in Complexes of Lactobacillus casei Dihydrofolate Reductase with Analogues of Pyrimethamine",published,journal,Biochemistry,,29,41,,,,,,,,,,,,,,,,,,,,,,9660,9667,1990, citations,entry_citation,1358,19801,1,,entry citation,,,,,"Nieto, Jose Luis, Rico, Manuel, Santoro, Jorge, Bermejo, J., ""NH resonances of Ribonuclease S-peptide in aqueous solution,"" Int. J. Pept. Protein Res. 25, 47-55 (1985).",NH resonances of Ribonuclease S-peptide in aqueous solution,published,journal,Int. J. Pept. Protein Res.,,25,,,,,,,,,,,,,,,,,,,,,,,47,55,1985, citations,entry_citation,136,19814,1,,entry citation,,,,,"Torchia, Dennis A., Sparks, Steven W., Bax, Ad, ""NMR Signal Assignments of Amide Protons in the alpha-Helical Domains of Staphylococcal Nuclease,"" Biochemistry 27 (14), 5135-5141 (1988).","NMR Signal Assignments of Amide Protons in the alpha-Helical Domains of Staphylococcal Nuclease",published,journal,Biochemistry,,27,14,,,,,,,,,,,,,,,,,,,,,,5135,5141,1988, citations,entry_citation,1360,19827,1,,entry citation,,,,,"Nieto, Jose Luis, Rico, Manuel, Santoro, Jorge, Bermejo, J., ""NH resonances of Ribonuclease S-peptide in aqueous solution,"" Int. J. Pept. Protein Res. 25, 47-55 (1985).",NH resonances of Ribonuclease S-peptide in aqueous solution,published,journal,Int. J. Pept. Protein Res.,,25,,,,,,,,,,,,,,,,,,,,,,,47,55,1985, citations,entry_citation,1374,19840,1,,entry citation,,,,,"Rhyu, Gyung Ihm, Markley, John L., ""Two-Dimensional NMR Studies of Kazal Proteinase Inhibitors. 2. Sequence-Specific Assignments and Secondary Structure of Reactive Site Modified Turkey Ovomucoid Third Domain,"" Biochemistry 27, 2529-2539 (1988).","Two-Dimensional NMR Studies of Kazal Proteinase Inhibitors. 2. Sequence-Specific Assignments and Secondary Structure of Reactive Site Modified Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,27,,,,,,,,,,,,,,,,,,,,,,,2529,2539,1988, citations,entry_citation,1375,19853,1,,entry citation,,,,,"Robertson, Andrew D., Rhyu, Gyung Ihm, Westler, William M., Markley, John L., ""Assignment of the 13C-NMR Spectra of Virgin and Reactive-Site Modified Turkey Ovomucoid Third Domain,"" Biopolymers 29, 461-467 (1990).","Assignment of the 13C-NMR Spectra of Virgin and Reactive-Site Modified Turkey Ovomucoid Third Domain",published,journal,Biopolymers,,29,,,,,,,,,,,,,,,,,,,,,,,461,467,1990, citations,entry_citation,1376,19866,1,,entry citation,,,,,"Otting, Gottfried, Steinmetz, Wayne E., Bougis, Pierre E., Rochat, Herve, Wuthrich, Kurt, ""Sequence-specific 1H-NMR assignments and determination of the secondary structure in aqueous solution of the cardiotoxins CTXIIa and CTXIIb from Naja mossambica mossambica,"" Eur. J. Biochem. 168, 609-620 (1987).","Sequence-specific 1H-NMR assignments and determination of the secondary structure in aqueous solution of the cardiotoxins CTXIIa and CTXIIb from Naja mossambica mossambica",published,journal,Eur. J. Biochem.,,168,,,,,,,,,,,,,,,,,,,,,,,609,620,1987, citations,entry_citation,1377,19879,1,,entry citation,,,,,"Cooke, Robert M., Tappin, Michael J., Campbell, Iain D., Kohda, Daisuke, Miyake, Tetsuo, Fuwa, Toru, Miyazawa, Tatsuo, Inagaki, Fuyuhiko, ""Nuclear-magnetic-resonance studies of human epidermal growth factor,"" Eur. J. Biochem. 193, 807-815 (1990).",Nuclear-magnetic-resonance studies of human epidermal growth factor,published,journal,Eur. J. Biochem.,,193,,,,,,,,,,,,,,,,,,,,,,,807,815,1990, citations,entry_citation,1378,19892,1,,entry citation,,,,,"Cooke, Robert M., Tappin, Michael J., Campbell, Iain D., Kohda, Daisuke, Miyake, Tetsuo, Fuwa, Toru, Miyazawa, Tatsuo, Inagaki, Fuyuhiko, ""Nuclear-magnetic-resonance studies of human epidermal growth factor,"" Eur. J. Biochem. 193, 807-815 (1990).",Nuclear-magnetic-resonance studies of human epidermal growth factor,published,journal,Eur. J. Biochem.,,193,,,,,,,,,,,,,,,,,,,,,,,807,815,1990, citations,entry_citation,1379,19905,1,,entry citation,,,,,"van Mierlo, Carlo P.M., van der Sanden, Boudewijn P. J., van Woensel, Peter, Muller, Franz, Vervoort, Jacques, ""A two-dimensional 1H-NMR study on Megasphaera elsdenii flavodoxin in the oxidized state and some comparisons with the two-electron-reduced state,"" Eur. J. Biochem. 194, 199-216 (1990).","A two-dimensional 1H-NMR study on Megasphaera elsdenii flavodoxin in the oxidized state and some comparisons with the two-electron-reduced state",published,journal,Eur. J. Biochem.,,194,,,,,,,,,,,,,,,,,,,,,,,199,216,1990, citations,entry_citation,1381,19918,1,,entry citation,,,,,"Yu, Chin, Lee, Chang-Shin, Chuang, Li-Chin, Shei, You-Rhon, Wang, Chi Ying, ""Two-dimensional NMR studies and secondary structure of cobrotoxin in aqueous solution,"" Eur. J. Biochem. 193, 789-799 (1990).","Two-dimensional NMR studies and secondary structure of cobrotoxin in aqueous solution",published,journal,Eur. J. Biochem.,,193,,,,,,,,,,,,,,,,,,,,,,,789,799,1990, citations,entry_citation,139,19931,1,,entry citation,,,,,"Gariepy, Jean, Lane, Andrew, Prigent, Yann, Wilbur, David, Robien, Wolfgang, Schoolnik, Gary K., Jardetzky, Oleg, ""Structure of the Toxic Domain of the Escherichia coli Heat-Stable Enterotoxin ST I,"" Biochemistry 25, 7854-7866 (1986).","Structure of the Toxic Domain of the Escherichia coli Heat-Stable Enterotoxin ST I",published,journal,Biochemistry,,25,,,,,,,,,,,,,,,,,,,,,,,7854,7866,1986, citations,entry_citation,1393,19944,1,,entry citation,,,,,"Saudek, Vladimir, Atkinson, R. Andrew, Williams, Robert J. P., Ramponi, G., ""Identification and Description of alpha-Helical Regions in Horse Muscle Acylphosphatase by 1H Nuclear Magnetic Resonance Spectroscopy,"" J. Mol. Biol. 205, 229-239 (1989).","Identification and Description of alpha-Helical Regions in Horse Muscle Acylphosphatase by 1H Nuclear Magnetic Resonance Spectroscopy",published,journal,J. Mol. Biol.,,205,,,,,,,,,,,,,,,,,,,,,,,229,239,1989, citations,entry_citation,1394,19958,1,,entry citation,,,,,"Saudek, Vladimir, Boyd, Jonathan, Williams, Robert J. P., Stefani, M., Ramponi, G., ""The sequence-specific assignment of the 1H-NMR spectrum of an enzyme, horse-muscle acylphosphatase,"" Eur. J. Biochem. 182, 85-93 (1989).","The sequence-specific assignment of the 1H-NMR spectrum of an enzyme, horse-muscle acylphosphatase",published,journal,Eur. J. Biochem.,,182,,,,,,,,,,,,,,,,,,,,,,,85,93,1989, citations,entry_citation,1396,19972,1,,entry citation,,,,,"Saudek, Vladimir, Pastore, Annalisa, Castiglione Morelli, Maria Antoinetta, Frank, Rainer, Gausepohl, Heinrich, Gibson, Toby, Weih, Falk, Rosch, Paul, ""Solution structure of the DNA-binding domain of the yeast transcriptional activator protein GCN4,"" Protein Eng. 4 (1), 3-10 (1990).","Solution structure of the DNA-binding domain of the yeast transcriptional activator protein GCN4",published,journal,Protein Eng.,,4,1,,,,,,,,,,,,,,,,,,,,,,3,10,1990, citations,entry_citation,1397,19985,1,,entry citation,,,,,"Saudek, Vladimir, Pastore, Annalisa, Castiglione Morelli, Maria Antoinetta, Frank, Rainer, Gausepohl, Heinrich, Gibson, Toby, Weih, Falk, Rosch, Paul, ""Solution structure of the DNA-binding domain of the yeast transcriptional activator protein GCN4,"" Protein Eng. 4 (1), 3-10 (1990).","Solution structure of the DNA-binding domain of the yeast transcriptional activator protein GCN4",published,journal,Protein Eng.,,4,1,,,,,,,,,,,,,,,,,,,,,,3,10,1990, citations,entry_citation,1398,19998,1,,entry citation,,,,,"Saudek, Vladimir, Pastore, Annalisa, Castiglione Morelli, Maria Antoinetta, Frank, Rainer, Gausepohl, Heinrich, Gibson, Toby, Weih, Falk, Rosch, Paul, ""Solution structure of the DNA-binding domain of the yeast transcriptional activator protein GCN4,"" Protein Eng. 4 (1), 3-10 (1990).","Solution structure of the DNA-binding domain of the yeast transcriptional activator protein GCN4",published,journal,Protein Eng.,,4,1,,,,,,,,,,,,,,,,,,,,,,3,10,1990, citations,entry_citation,1399,20011,1,,entry citation,,,,,"Saudek, Vladimir, Pastore, Annalisa, Castiglione Morelli, Maria Antoinetta, Frank, Rainer, Gausepohl, Heinrich, Gibson, Toby, Weih, Falk, Rosch, Paul, ""Solution structure of the DNA-binding domain of the yeast transcriptional activator protein GCN4,"" Protein Eng. 4 (1), 3-10 (1990).","Solution structure of the DNA-binding domain of the yeast transcriptional activator protein GCN4",published,journal,Protein Eng.,,4,1,,,,,,,,,,,,,,,,,,,,,,3,10,1990, citations,entry_citation,140,20024,1,,entry citation,,,,,"Gronenborn, Angela M., Boverman, Gunter, Clore, G. Marius, ""A 1H-NMR study of the solution conformation of secretin Resonance assignment and secondary structure,"" FEBS Lett. 215 (1), 88-94 (1987).","A 1H-NMR study of the solution conformation of secretin Resonance assignment and secondary structure",published,journal,FEBS Lett.,,215,1,,,,,,,,,,,,,,,,,,,,,,88,94,1987, citations,entry_citation,1400,20037,1,,entry citation,,,,,"Forman-Kay, Julie D., Clore, G. Marius, Driscoll, Paul C., Wingfield, Paul, Richards, Frederic M., Gronenborn, Angela M., ""A Proton Nuclear Magnetic Resonance Assignment and Secondary Structure Determination of Recombinant Human Thioredoxin,"" Biochemistry 28, 7088-7097 (1989).","A Proton Nuclear Magnetic Resonance Assignment and Secondary Structure Determination of Recombinant Human Thioredoxin",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,7088,7097,1989, citations,entry_citation,1403,20050,1,,entry citation,,,,,"Breeze, Alexander L., Harvey, Timothy S., Bazzo, Renzo, Campbell, Iain D., ""Solution Structure of Human Calcitonin Gene-Related Peptide by 1H NMR and Distance Geometry with Restrained Molecular Dynamics,"" Biochemistry 30 (2), 575-582 (1991).","Solution Structure of Human Calcitonin Gene-Related Peptide by 1H NMR and Distance Geometry with Restrained Molecular Dynamics",published,journal,Biochemistry,,30,2,,,,,,,,,,,,,,,,,,,,,,575,582,1991, citations,entry_citation,1404,20062,1,,entry citation,,,,,"Gao, Yuan, Boyd, Jonathan, Williams, Robert J. P., ""A systematic approach towards the complete assignment of 13C resonances for horse ferrocytochrome c,"" Eur. J. Biochem. 194, 355-365 (1990).","A systematic approach towards the complete assignment of 13C resonances for horse ferrocytochrome c",published,journal,Eur. J. Biochem.,,194,,,,,,,,,,,,,,,,,,,,,,,355,365,1990, citations,entry_citation,141,20078,1,,entry citation,,,,,"Holak, Tadeusz A., Engstrom, Ake, Kraulis, Per J., Lindeberg, Gunnar, Bennich, Hans, Jones, Alwyn, Gronenborn, Angela M., Clore, G. Marius, ""The Solution Conformation of the Antibacterial Peptide Cecropin A: A Nuclear Magnetic Resonance and Dynamical Simulated Annealing Study,"" Biochemistry 27, 7620-7629 (1988).","The Solution Conformation of the Antibacterial Peptide Cecropin A: A Nuclear Magnetic Resonance and Dynamical Simulated Annealing Study",published,journal,Biochemistry,,27,,,,,,,,,,,,,,,,,,,,,,,7620,7629,1988, citations,entry_citation,1413,20091,1,,entry citation,,,,,"Yu, Liping P., La Mar, Gerd N., Rajarathnam, Krishnakumar, ""1H NMR Resonance Assignment of the Active Site Residues of Paramagnetic Proteins by 2D Bond Correlation Spectroscopy: Metcyanomyoglobin,"" J. Am. Chem. Soc. 112, 9527-9534 (1990).","1H NMR Resonance Assignment of the Active Site Residues of Paramagnetic Proteins by 2D Bond Correlation Spectroscopy: Metcyanomyoglobin",published,journal,J. Am. Chem. Soc.,,112,,,,,,,,,,,,,,,,,,,,,,,9527,9534,1990, citations,entry_citation,1414,20104,1,,entry citation,,,,,"Pastore, Annalisa, De Francesco, Raffaele, Barbato, Gaetano, Castiglione Morelli, Maria Antoinetta, Motta, Andrea, Cortese, Riccardo, ""1H Resonance Assignment and Secondary Structure Determination of the Dimerization Domain of Transcription Factor LFB1,"" Biochemistry 30 (1), 148-153 (1991).","1H Resonance Assignment and Secondary Structure Determination of the Dimerization Domain of Transcription Factor LFB1",published,journal,Biochemistry,,30,1,,,,,,,,,,,,,,,,,,,,,,148,153,1991, citations,entry_citation,1416,20117,1,,entry citation,,,,,"Nall, Barry T., Zuniga, Efrain H., ""Rates and Energetics of Tyrosine Ring Flips in Yeast Iso-2-cytochrome c,"" Biochemistry 29, 7576-7584 (1990).",Rates and Energetics of Tyrosine Ring Flips in Yeast Iso-2-cytochrome c,published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,7576,7584,1990, citations,entry_citation,142,20131,1,,entry citation,,,,,"Olejniczak, E.T., Gampe, Robert T., Jr., Rockway, T. W., Fesik, Stephen W., ""NMR Study of the Solution Conformation of Rat Atrial Natriuretic Factor 7-23 in Sodium Dodecyl Sulfate Micelles,"" Biochemistry 27 (18), 7124-7131 (1988).","NMR Study of the Solution Conformation of Rat Atrial Natriuretic Factor 7-23 in Sodium Dodecyl Sulfate Micelles",published,journal,Biochemistry,,27,18,,,,,,,,,,,,,,,,,,,,,,7124,7131,1988, citations,entry_citation,1439,20144,1,,entry citation,,,,,"Skjeldal, Lars, Westler, William M., Oh, Byung-Ha, Krezel, Andrzej M., Holden, Hazel M., Jacobson, Bruce L., Rayment, Ivan, Markley, John L., ""Two-Dimensional Magnetization Exchange Spectroscopy of Anabaena 7120 Ferredoxin. Nuclear Overhauser Effect and Electron Self Exchange Cross Peaks from Amino Acid Residues Surrounding the 2Fe-2S, Cluster,"" Biochemistry 30 (30), 7363-7368 (1991).","Two-Dimensional Magnetization Exchange Spectroscopy of Anabaena 7120 Ferredoxin. Nuclear Overhauser Effect and Electron Self Exchange Cross Peaks from Amino Acid Residues Surrounding the 2Fe-2S, Cluster",published,journal,Biochemistry,,30,30,,,,,,,,,,,,,,,,,,,,,,7363,7368,1991, citations,entry_citation,144,20157,1,,entry citation,,,,,"Padilla, Andre, Cave, Adrien, Parello, Joseph, ""Two-dimensional 1H Nuclear Magnetic Resonance Study of Pike pI 5.0 Parvalbumin (Esox lucius) Sequential Resonance Assignments and Folding of the Polypeptide Chain,"" J. Mol. Biol. 204, 995-1017 (1988).","Two-dimensional 1H Nuclear Magnetic Resonance Study of Pike pI 5.0 Parvalbumin (Esox lucius) Sequential Resonance Assignments and Folding of the Polypeptide Chain",published,journal,J. Mol. Biol.,,204,,,,,,,,,,,,,,,,,,,,,,,995,1017,1988, citations,entry_citation,1457,20383,1,,entry citation,,,,,"Hauksson, Jon B., La Mar, Gerd N., Pande, Usha, Pandey, Ravindra K., Parish, Daniel W., Singh, Jai P., Smith, Kevin M., ""1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers,"" Biochim. Biophys. Acta 1041, 186-194 (1990).","1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers",published,journal,Biochim. Biophys. Acta,,1041,,,,,,,,,,,,,,,,,,,,,,,186,194,1990, citations,entry_citation,1440,20171,1,,entry citation,,,,,"Skjeldal, Lars, Westler, William M., Oh, Byung-Ha, Krezel, Andrzej M., Holden, Hazel M., Jacobson, Bruce L., Rayment, Ivan, Markley, John L., ""Two-Dimensional Magnetization Exchange Spectroscopy of Anabaena 7120 Ferredoxin. Nuclear Overhauser Effect and Electron Self Exchange Cross Peaks from Amino Acid Residues Surrounding the 2Fe-2S, Cluster,"" Biochemistry 30 (30), 7363-7368 (1991).","Two-Dimensional Magnetization Exchange Spectroscopy of Anabaena 7120 Ferredoxin. Nuclear Overhauser Effect and Electron Self Exchange Cross Peaks from Amino Acid Residues Surrounding the 2Fe-2S, Cluster",published,journal,Biochemistry,,30,30,,,,,,,,,,,,,,,,,,,,,,7363,7368,1991, citations,entry_citation,1441,20184,1,,entry citation,,,,,"Skjeldal, Lars, Westler, William M., Oh, Byung-Ha, Krezel, Andrzej M., Holden, Hazel M., Jacobson, Bruce L., Rayment, Ivan, Markley, John L., ""Two-Dimensional Magnetization Exchange Spectroscopy of Anabaena 7120 Ferredoxin. Nuclear Overhauser Effect and Electron Self Exchange Cross Peaks from Amino Acid Residues Surrounding the 2Fe-2S, Cluster,"" Biochemistry 30 (30), 7363-7368 (1991).","Two-Dimensional Magnetization Exchange Spectroscopy of Anabaena 7120 Ferredoxin. Nuclear Overhauser Effect and Electron Self Exchange Cross Peaks from Amino Acid Residues Surrounding the 2Fe-2S, Cluster",published,journal,Biochemistry,,30,30,,,,,,,,,,,,,,,,,,,,,,7363,7368,1991, citations,entry_citation,1442,20197,1,,entry citation,,,,,"Higgins, Kerry A., Craik, David J., Hall, Jon G., ""2D 1H NMR Studies of Monomeric Insulin,"" Biochem. Int. 22 (4), 627-637 (1990).",2D 1H NMR Studies of Monomeric Insulin,published,journal,Biochem. Int.,,22,4,,,,,,,,,,,,,,,,,,,,,,627,637,1990, citations,entry_citation,1443,20210,1,,entry citation,,,,,"Higgins, Kerry A., Craik, David J., Hall, Jon G., ""2D 1H NMR Studies of Monomeric Insulin,"" Biochem. Int. 22 (4), 627-637 (1990).",2D 1H NMR Studies of Monomeric Insulin,published,journal,Biochem. Int.,,22,4,,,,,,,,,,,,,,,,,,,,,,627,637,1990, citations,entry_citation,1444,20223,1,,entry citation,,,,,"Higgins, Kerry A., Craik, David J., Hall, Jon G., ""2D 1H NMR Studies of Monomeric Insulin,"" Biochem. Int. 22 (4), 627-637 (1990).",2D 1H NMR Studies of Monomeric Insulin,published,journal,Biochem. Int.,,22,4,,,,,,,,,,,,,,,,,,,,,,627,637,1990, citations,entry_citation,1445,20236,1,,entry citation,,,,,"Bradley, Erin K., Thomason, John F., Cohen, Fred E., ""Studies of Synthetic Helical Peptides Using Circular Dichroism and Nuclear Magnetic Resonance,"" J. Mol. Biol. 215, 607-622 (1990).","Studies of Synthetic Helical Peptides Using Circular Dichroism and Nuclear Magnetic Resonance",published,journal,J. Mol. Biol.,,215,,,,,,,,,,,,,,,,,,,,,,,607,622,1990, citations,entry_citation,1446,20251,1,,entry citation,,,,,"Bradley, Erin K., Thomason, John F., Cohen, Fred E., ""Studies of Synthetic Helical Peptides Using Circular Dichroism and Nuclear Magnetic Resonance,"" J. Mol. Biol. 215, 607-622 (1990).","Studies of Synthetic Helical Peptides Using Circular Dichroism and Nuclear Magnetic Resonance",published,journal,J. Mol. Biol.,,215,,,,,,,,,,,,,,,,,,,,,,,607,622,1990, citations,entry_citation,1447,20266,1,,entry citation,,,,,"Saudek, Vladimir, Pasley, H. S., Gibson, Toby, Gausepohl, Heinrich, Frank, Rainer, Pastore, Annalisa, ""Solution Structure of the Basic Region from the Transcriptional Activator GCN4,"" Biochemistry 30, 1310-1317 (1991).",Solution Structure of the Basic Region from the Transcriptional Activator GCN4,published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,1310,1317,1991, citations,entry_citation,1448,20279,1,,entry citation,,,,,"Saudek, Vladimir, Pasley, H. S., Gibson, Toby, Gausepohl, Heinrich, Frank, Rainer, Pastore, Annalisa, ""Solution Structure of the Basic Region from the Transcriptional Activator GCN4,"" Biochemistry 30, 1310-1317 (1991).",Solution Structure of the Basic Region from the Transcriptional Activator GCN4,published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,1310,1317,1991, citations,entry_citation,1449,20292,1,,entry citation,,,,,"Saudek, Vladimir, Pasley, H. S., Gibson, Toby, Gausepohl, Heinrich, Frank, Rainer, Pastore, Annalisa, ""Solution Structure of the Basic Region from the Transcriptional Activator GCN4,"" Biochemistry 30, 1310-1317 (1991).",Solution Structure of the Basic Region from the Transcriptional Activator GCN4,published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,1310,1317,1991, citations,entry_citation,1450,20305,1,,entry citation,,,,,"Saudek, Vladimir, Pasley, H. S., Gibson, Toby, Gausepohl, Heinrich, Frank, Rainer, Pastore, Annalisa, ""Solution Structure of the Basic Region from the Transcriptional Activator GCN4,"" Biochemistry 30, 1310-1317 (1991).",Solution Structure of the Basic Region from the Transcriptional Activator GCN4,published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,1310,1317,1991, citations,entry_citation,1451,20318,1,,entry citation,,,,,"Saudek, Vladimir, Pasley, H. S., Gibson, Toby, Gausepohl, Heinrich, Frank, Rainer, Pastore, Annalisa, ""Solution Structure of the Basic Region from the Transcriptional Activator GCN4,"" Biochemistry 30, 1310-1317 (1991).",Solution Structure of the Basic Region from the Transcriptional Activator GCN4,published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,1310,1317,1991, citations,entry_citation,1452,20331,1,,entry citation,,,,,"Saudek, Vladimir, Pasley, H. S., Gibson, Toby, Gausepohl, Heinrich, Frank, Rainer, Pastore, Annalisa, ""Solution Structure of the Basic Region from the Transcriptional Activator GCN4,"" Biochemistry 30, 1310-1317 (1991).",Solution Structure of the Basic Region from the Transcriptional Activator GCN4,published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,1310,1317,1991, citations,entry_citation,1453,20344,1,,entry citation,,,,,"Saudek, Vladimir, Pasley, H. S., Gibson, Toby, Gausepohl, Heinrich, Frank, Rainer, Pastore, Annalisa, ""Solution Structure of the Basic Region from the Transcriptional Activator GCN4,"" Biochemistry 30, 1310-1317 (1991).",Solution Structure of the Basic Region from the Transcriptional Activator GCN4,published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,1310,1317,1991, citations,entry_citation,1454,20357,1,,entry citation,,,,,"Saudek, Vladimir, Pasley, H. S., Gibson, Toby, Gausepohl, Heinrich, Frank, Rainer, Pastore, Annalisa, ""Solution Structure of the Basic Region from the Transcriptional Activator GCN4,"" Biochemistry 30, 1310-1317 (1991).",Solution Structure of the Basic Region from the Transcriptional Activator GCN4,published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,1310,1317,1991, citations,entry_citation,1455,20370,1,,entry citation,,,,,"Hauksson, Jon B., La Mar, Gerd N., Pande, Usha, Pandey, Ravindra K., Parish, Daniel W., Singh, Jai P., Smith, Kevin M., ""1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers,"" Biochim. Biophys. Acta 1041, 186-194 (1990).","1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers",published,journal,Biochim. Biophys. Acta,,1041,,,,,,,,,,,,,,,,,,,,,,,186,194,1990, citations,entry_citation,148,20580,1,,entry citation,,,,,"Gooley, Paul R., Norton, Raymond S., ""Specific assignment of resonances in the 1H nuclear magnetic resonance spectrum of the polypeptide cardiac stimulant anthopleurin-A,"" Eur. J. Biochem. 153, 529-539 (1985).","Specific assignment of resonances in the 1H nuclear magnetic resonance spectrum of the polypeptide cardiac stimulant anthopleurin-A",published,journal,Eur. J. Biochem.,,153,,,,,,,,,,,,,,,,,,,,,,,529,539,1985, citations,entry_citation,1459,20396,1,,entry citation,,,,,"Hauksson, Jon B., La Mar, Gerd N., Pande, Usha, Pandey, Ravindra K., Parish, Daniel W., Singh, Jai P., Smith, Kevin M., ""1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers,"" Biochim. Biophys. Acta 1041, 186-194 (1990).","1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers",published,journal,Biochim. Biophys. Acta,,1041,,,,,,,,,,,,,,,,,,,,,,,186,194,1990, citations,entry_citation,146,20409,1,,entry citation,,,,,"Strop, Petr, Wider, Gerhard, Wuthrich, Kurt, ""Assignment of the 1H Nuclear Magnetic Resonance Spectrum of the Proteinase Inhibitor IIA from Bull Seminal Plasma by Two-dimensional Nuclear Magnetic Resonance at 500 MHz,"" J. Mol. Biol. 166, 641-667 (1983).","Assignment of the 1H Nuclear Magnetic Resonance Spectrum of the Proteinase Inhibitor IIA from Bull Seminal Plasma by Two-dimensional Nuclear Magnetic Resonance at 500 MHz",published,journal,J. Mol. Biol.,,166,,,,,,,,,,,,,,,,,,,,,,,641,667,1983, citations,entry_citation,1461,20423,1,,entry citation,,,,,"Hauksson, Jon B., La Mar, Gerd N., Pande, Usha, Pandey, Ravindra K., Parish, Daniel W., Singh, Jai P., Smith, Kevin M., ""1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers,"" Biochim. Biophys. Acta 1041, 186-194 (1990).","1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers",published,journal,Biochim. Biophys. Acta,,1041,,,,,,,,,,,,,,,,,,,,,,,186,194,1990, citations,entry_citation,1463,20436,1,,entry citation,,,,,"Hauksson, Jon B., La Mar, Gerd N., Pande, Usha, Pandey, Ravindra K., Parish, Daniel W., Singh, Jai P., Smith, Kevin M., ""1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers,"" Biochim. Biophys. Acta 1041, 186-194 (1990).","1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers",published,journal,Biochim. Biophys. Acta,,1041,,,,,,,,,,,,,,,,,,,,,,,186,194,1990, citations,entry_citation,1465,20449,1,,entry citation,,,,,"Hauksson, Jon B., La Mar, Gerd N., Pande, Usha, Pandey, Ravindra K., Parish, Daniel W., Singh, Jai P., Smith, Kevin M., ""1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers,"" Biochim. Biophys. Acta 1041, 186-194 (1990).","1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers",published,journal,Biochim. Biophys. Acta,,1041,,,,,,,,,,,,,,,,,,,,,,,186,194,1990, citations,entry_citation,1467,20462,1,,entry citation,,,,,"Hauksson, Jon B., La Mar, Gerd N., Pande, Usha, Pandey, Ravindra K., Parish, Daniel W., Singh, Jai P., Smith, Kevin M., ""1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers,"" Biochim. Biophys. Acta 1041, 186-194 (1990).","1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers",published,journal,Biochim. Biophys. Acta,,1041,,,,,,,,,,,,,,,,,,,,,,,186,194,1990, citations,entry_citation,1469,20475,1,,entry citation,,,,,"Hauksson, Jon B., La Mar, Gerd N., Pande, Usha, Pandey, Ravindra K., Parish, Daniel W., Singh, Jai P., Smith, Kevin M., ""1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers,"" Biochim. Biophys. Acta 1041, 186-194 (1990).","1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers",published,journal,Biochim. Biophys. Acta,,1041,,,,,,,,,,,,,,,,,,,,,,,186,194,1990, citations,entry_citation,1471,20488,1,,entry citation,,,,,"Hauksson, Jon B., La Mar, Gerd N., Pande, Usha, Pandey, Ravindra K., Parish, Daniel W., Singh, Jai P., Smith, Kevin M., ""1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers,"" Biochim. Biophys. Acta 1041, 186-194 (1990).","1H-NMR study of the mechanism of assembly and equilibrium heme orientation of sperm whale myoglobin reconstituted with protohemin type-isomers",published,journal,Biochim. Biophys. Acta,,1041,,,,,,,,,,,,,,,,,,,,,,,186,194,1990, citations,entry_citation,1474,20501,1,,entry citation,,,,,"Constantine, Keith L., Ramesh, Vasudevan, Banyai, Laszlo, Trexler, Maria, Patthy, Laszlo, Llinas, M., ""Sequence-specific 1H NMR Assignments and Structural Characterization of Bovine Seminal Fluid Protein PDC-109 Domain b,"" Biochemistry 30, 1663-1672 (1991).","Sequence-specific 1H NMR Assignments and Structural Characterization of Bovine Seminal Fluid Protein PDC-109 Domain b",published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,1663,1672,1991, citations,entry_citation,1475,20514,1,,entry citation,,,,,"Fesik, Stephen W., Gampe, Robert T., Jr., Holzman, Thomas F., Egan, D. A., Edalji, Rohinton P., Luly, Jay R., Simmer, R., Helfrich, R., Kishore, V., Rich, D. H., ""Isotope-Edited NMR of Cyclosporin A Bound to Cyclophilin: Evidence for a Trans 9,10 Amide Bond,"" Science 250, 1406-1409 (1990).","Isotope-Edited NMR of Cyclosporin A Bound to Cyclophilin: Evidence for a Trans 9,10 Amide Bond",published,journal,Science,,250,,,,,,,,,,,,,,,,,,,,,,,1406,1409,1990, citations,entry_citation,1476,20528,1,,entry citation,,,,,"Byeon, In-Ja L., Kelley, Robert F., Llinas, M., ""1H NMR Structure Characterization of a Recombinant Kringle 2 Domain from Human Tissue-Type Plasminogen Activator,"" Biochemistry 28, 9350-9360 (1989).","1H NMR Structure Characterization of a Recombinant Kringle 2 Domain from Human Tissue-Type Plasminogen Activator",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,9350,9360,1989, citations,entry_citation,1477,20541,1,,entry citation,,,,,"Byeon, In-Ja L., Kelley, Robert F., Llinas, M., ""1H NMR Structure Characterization of a Recombinant Kringle 2 Domain from Human Tissue-Type Plasminogen Activator,"" Biochemistry 28, 9350-9360 (1989).","1H NMR Structure Characterization of a Recombinant Kringle 2 Domain from Human Tissue-Type Plasminogen Activator",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,9350,9360,1989, citations,entry_citation,1478,20554,1,,entry citation,,,,,"Darbon, H., Weber, C., Braun, Werner, ""Two-Dimensional 1H Nuclear Magnetic Resonance Study of AaH IT, an Anti-Insect Toxin from the Scorpion Androctonus australis Hector. Sequential Resonance Assignments and Folding of the Polypeptide Chain,"" Biochemistry 30, 1836-1845 (1991).","Two-Dimensional 1H Nuclear Magnetic Resonance Study of AaH IT, an Anti-Insect Toxin from the Scorpion Androctonus australis Hector. Sequential Resonance Assignments and Folding of the Polypeptide Chain",published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,1836,1845,1991, citations,entry_citation,1479,20567,1,,entry citation,,,,,"Barlow, P. N., Baron, Martin, Norman, David G., Day, A. J., Willis, Antony, Sim, R. B., Campbell, Iain D., ""Secondary Structure of a Complement Control Protein Module by Two-Dimensional 1H NMR,"" Biochemistry 30 (4), 997-1004 (1991).","Secondary Structure of a Complement Control Protein Module by Two-Dimensional 1H NMR",published,journal,Biochemistry,,30,4,,,,,,,,,,,,,,,,,,,,,,997,1004,1991, citations,entry_citation,1481,20606,1,,entry citation,,,,,"Meadows, Robert P., Nikonowicz, Edward P., Jones, Claude R., Bastian, James W., Gorenstein, David G., ""Two-Dimensional NMR and Structure Determination of Salmon Calcitonin in Methanol,"" Biochemistry 30, 1247-1254 (1991).",Two-Dimensional NMR and Structure Determination of Salmon Calcitonin in Methanol,published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,1247,1254,1991, citations,entry_citation,1482,20620,1,,entry citation,,,,,"Meadows, Robert P., Nikonowicz, Edward P., Jones, Claude R., Bastian, James W., Gorenstein, David G., ""Two-Dimensional NMR and Structure Determination of Salmon Calcitonin in Methanol,"" Biochemistry 30, 1247-1254 (1991).",Two-Dimensional NMR and Structure Determination of Salmon Calcitonin in Methanol,published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,1247,1254,1991, citations,entry_citation,1483,20634,1,,entry citation,,,,,"Ishitsuka, Midori O., Kusumi, Takenori, Kakisawa, Hiroshi, Kaya, Kunimitsu, Watanabe, Makoto M., ""Microviridin: A Novel Tricyclic Depsipeptide from the Toxic Cyanobacterium Microcystis viridis,"" J. Am. Chem. Soc. 112 (22), 8180-8182 (1990).","Microviridin: A Novel Tricyclic Depsipeptide from the Toxic Cyanobacterium Microcystis viridis",published,journal,J. Am. Chem. Soc.,,112,22,,,,,,,,,,,,,,,,,,,,,,8180,8182,1990, citations,entry_citation,1484,20647,1,,entry citation,,,,,"Hinck, Andrew P., Loh, Stewart N., Wang, Jinfeng, Markley, John L., ""Histidine 121 of Staphylococcal Nuclease. Correlation of the Hdelta2 1H NMR Assignment and Reinterpretation of the Role This Residue Plays in Conformational Heterogeneity of the Protein,"" J. Am. Chem. Soc. 112 (25), 9031-9034 (1990).","Histidine 121 of Staphylococcal Nuclease. Correlation of the Hdelta2 1H NMR Assignment and Reinterpretation of the Role This Residue Plays in Conformational Heterogeneity of the Protein",published,journal,J. Am. Chem. Soc.,,112,25,,,,,,,,,,,,,,,,,,,,,,9031,9034,1990, citations,entry_citation,1485,20660,1,,entry citation,,,,,"Hinck, Andrew P., Loh, Stewart N., Wang, Jinfeng, Markley, John L., ""Histidine 121 of Staphylococcal Nuclease. Correlation of the Hdelta2 1H NMR Assignment and Reinterpretation of the Role This Residue Plays in Conformational Heterogeneity of the Protein,"" J. Am. Chem. Soc. 112 (25), 9031-9034 (1990).","Histidine 121 of Staphylococcal Nuclease. Correlation of the Hdelta2 1H NMR Assignment and Reinterpretation of the Role This Residue Plays in Conformational Heterogeneity of the Protein",published,journal,J. Am. Chem. Soc.,,112,25,,,,,,,,,,,,,,,,,,,,,,9031,9034,1990, citations,entry_citation,1486,20673,1,,entry citation,,,,,"Banci, Lucia, Bertini, Ivano, Miyano, Hiroshi, Hallewell, Robert A., Tung, James W., Viezzoli, Maria Silvia, ""A characterization of copper/zinc superoxide dismutase mutants at position 124,"" Eur. J. Biochem. 196, 123-128 (1991).",A characterization of copper/zinc superoxide dismutase mutants at position 124,published,journal,Eur. J. Biochem.,,196,,,,,,,,,,,,,,,,,,,,,,,123,128,1991, citations,entry_citation,1487,20687,1,,entry citation,,,,,"Banci, Lucia, Bertini, Ivano, Miyano, Hiroshi, Hallewell, Robert A., Tung, James W., Viezzoli, Maria Silvia, ""A characterization of copper/zinc superoxide dismutase mutants at position 124,"" Eur. J. Biochem. 196, 123-128 (1991).",A characterization of copper/zinc superoxide dismutase mutants at position 124,published,journal,Eur. J. Biochem.,,196,,,,,,,,,,,,,,,,,,,,,,,123,128,1991, citations,entry_citation,149,20701,1,,entry citation,,,,,"Gooley, Paul R., Norton, Raymond S., ""Specific assignment of resonances in the 1H nuclear magnetic resonance spectrum of the polypeptide cardiac stimulant anthopleurin-A,"" Eur. J. Biochem. 153, 529-539 (1985).","Specific assignment of resonances in the 1H nuclear magnetic resonance spectrum of the polypeptide cardiac stimulant anthopleurin-A",published,journal,Eur. J. Biochem.,,153,,,,,,,,,,,,,,,,,,,,,,,529,539,1985, citations,entry_citation,1494,20714,1,,entry citation,,,,,"Lamerichs, R.M.J.N., Boelens, Rolf, van der Marel, G.A., van Boom, J.H., Kaptein, Robert, ""Assignment of the 1H-NMR spectrum of a lac repressor headpiece-operator complex in H2O and identification of NOEs,"" Eur. J. Biochem. 194, 629-637 (1990).","Assignment of the 1H-NMR spectrum of a lac repressor headpiece-operator complex in H2O and identification of NOEs",published,journal,Eur. J. 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NMR Assignments,,1,1,,,,,,,,,,,,,,,,,,,,,,69,71,2007, citations,citation_1,15094,22337,1,,entry citation,,,17847095,,,Protonless (13)C direct detection NMR: characterization of the 37 kiloDalton trimeric protein CutA1,published,journal,Proteins,,70,4,,,,,,,,,,,,,,,,,,,,,,1196,1205,2008, citations,entry_citation,15095,22356,1,,entry citation,,,19762560,,,Interaction with synphilin-1 promotes inclusion formation of alpha-synuclein: mechanistic insights and pathological implication.,published,journal,FASEB J.,The FASEB journal : official publication of the Federation of American Societies for Experimental Biology,24,1,,,,,,,,,,,,,,,,,,,,,,196,205,2010, citations,entry_citation,15097,22374,1,,entry citation,,,17547371,,,"The Isolated Sixth Gelsolin Repeat and Headpiece Domain of Villin Bundle F-Actin in the Presence of Calcium and Are Linked by a 40-Residue Unstructured Sequence",published,journal,Biochemistry,,46,25,,,,,,,,,,,,,,,,,,,,,,7488,7496,2007, citations,citations,15098,22395,1,,entry citation,,,,,,"Solution Structures of the Brk Domains of the Human Chromo Helicase Domain 7 and 8, Reveals Structural Similarity with Gyf Domain Suggesting a Role in Protein Interaction",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15099,22410,1,,entry citation,,,17397158,,,Mapping the orientation of helices in micelle-bound peptides by paramagnetic relaxation waves,published,journal,J. 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Biol.,,368,3,,,0353,,,,,,,,,,,,,,,,,,,718,728,2007, citations,citations,15105,22527,1,,entry citation,,,17880110,,,The solution structure of clip domains from Manduca sexta prophenoloxidase activating proteinase-2,published,journal,Biochemistry,,46,41,,,0353,,,,,,,,,,,,,,,,,,,11431,11439,2007, citations,citations,15106,22544,1,,entry citation,,,17880110,,,The solution structure of clip domains from Manduca sexta prophenoloxidase activating proteinase-2,in preparation,journal,Biochemistry,,46,41,,,0353,,,,,,,,,,,,,,,,,,,11431,11439,2007, citations,citations,15107,22561,1,,entry citation,,,18473359,,,Understanding the roles of amino acid residues in tertiary structure formation of chignolin by using molecular dynamics simulation,published,journal,Proteins,,73,3,,,0353,,,,,,,,,,,,,,,,,,,621,631,2008, citations,citations,15108,22578,1,,entry citation,,,17488723,,,"Infectious bursal disease virus, a non-enveloped virus, possesses a capsid-associated peptide that deforms and perforates biological membranes",published,journal,J. 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Chem.,,282,15,,,,,,,,,,,,,,,,,,,,,,11300,11307,2007, citations,citations,15110,22614,1,,entry citation,,,17302442,,,An engineered second disulfide bond restricts lymphotactin/XCL1 to a chemokine-like conformation with XCR1 agonist activity,published,journal,Biochemistry,,46,10,,,0353,,,,,,,,,,,,,,,,,,,2564,2573,2007, citations,entry_citation,15111,22633,1,,entry citation,,,18596201,,,Differential Ubiquitin Binding of the UBA Domains from Human c-Cbl and Cbl-b: NMR Structural and Biochemical Insights,published,journal,Protein Sci.,,17,10,,,,,,,,,,,,,,,,,,,,,,1805,1814,2008, citations,citation_1,15112,22650,1,,entry citation,,,19636828,,,"NMR assignment of reduced form of copper, zinc superoxide dismutase from Salmonella enterica",published,journal,Biomol. 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Biol.,,366,2,,,0353,,,,,,,,,,,,,,,,,,,574,585,2007, citations,1,15117,22754,1,,entry citation,,,17475623,,,"Conserved surface features form the double-stranded RNA binding site of non-structural protein 1 (NS1) from influenza A and B viruses.",published,journal,J. Biol. Chem.,,282,28,,,,,,,,,,,,,,,,,,,,,,20584,20592,2007, citations,citations,15118,22773,1,,entry citation,,,17469802,,,"High-resolution solution structure of a designed peptide bound to lipopolysaccharide: transferred nuclear Overhauser effects, micelle selectivity, and anti-endotoxic activity",published,journal,Biochemistry,,48,20,,,0353,,,,,,,,,,,,,,,,,,,5864,5874,2007, citations,MMP3-NNGH,15120,22788,1,,entry citation,,,17710450,,,Matrix metalloproteinase-inhibitor interaction: the solution structure of the catalytic domain of human matrix metalloproteinase-3 with different inhibitors,published,journal,J. Biol. Inorg. 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J.,,93,4,,,,,,,,,,,,,,,,,,,,,,1264,1276,2007, citations,entry_citation,15138,23126,1,,entry citation,,,17279748,,,"Filamentous phage studied by magic-angle spinning NMR: resonance assignment and secondary structure of the coat protein in Pf1.",published,journal,J. Am. Chem. Soc.,,129,8,,,,,,,,,,,,,,,,,,,,,,2338,2344,2007, citations,entry_citation,15139,23147,1,,entry citation,,,,,,NMR structure of E.coli NirD.,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,Citation_1,15140,23181,1,,entry citation,,,17628674,,,"NMR structure of mussel mytilin, and antiviral-antibacterial activities of derived synthetic peptides.",published,journal,Dev. Comp. 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Biol.,,216,,,,,,,,,,,,,,,,,,,,,,,883,895,1990, citations,entry_citation,15180,23943,1,,entry citation,,,17279777,,,Structural basis for spinophilin-neurabin receptor interaction,published,journal,Biochemistry,,46,9,,,,,,,,,,,,,,,,,,,,,,2333,2344,2007, citations,primary_citation,15183,23959,1,,reference citation,,,16846216,,,Conformational dynamics of calmodulin in complex with the calmodulin-dependent kinase kinase alpha calmodulin-binding domain.,published,journal,Biochemistry,,45,29,,,,,,,,,,,,,,,,,,,,,,8732,8741,2006, citations,citation_2,15183,23960,2,,entry citation,,,17637663,,,Conformational entropy in molecular recognition by proteins,published,journal,Nature,,448,7151,,,,,,,,,,,,,,,,,,,,,,325,329,2007, citations,entry_citation,15184,23981,1,,reference citation,,,,,,"Characterization of the backbone and side chain dynamics of the CaM-CaMKIp complex reveals microscopic contributions to protein conformational entropy",published,journal,Biochemistry,,45,32,,,,,,,,,,,,,,,,,,,,,,9841,9848,2006, citations,entry_citation_2,15184,23982,2,,entry citation,,,17637663,,,Conformational entropy in molecular recognition by proteins,published,journal,Nature,,448,7151,,,,,,,,,,,,,,,,,,,,,,325,329,2007, citations,entry_citation,15185,24001,1,,entry citation,,,17637663,,,Conformational entropy in molecular recognition by proteins,published,journal,Nature,,448,7151,,,,,,,,,,,,,,,,,,,,,,325,329,2007, citations,entry_citation_2,15185,24002,2,,reference citation,,,,,,Characterization of the backbone and side chain dynamics of the CaM:eNOSp complex reveals microscopic contributions to protein conformational entropy,in preparation,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15186,24021,1,,entry citation,,,17637663,,,Conformational entropy in molecular recognition by proteins,published,journal,Nature,,448,7151,,,,,,,,,,,,,,,,,,,,,,325,329,2007, citations,entry_citation,15213,24546,1,,entry citation,,,18001133,,,DNA recognition via mutual-induced fit by the core-binding domain of bacteriophage lambda integrase.,published,journal,Biochemistry,,46,49,,,,,,,,,,,,,,,,,,,,,,13939,13947,2007, citations,entry_citation_2,15186,24022,2,,reference citation,,,,,,Characterization of the Backbone and Side Chain Dynamics of the CaM-CaMKIp Complex Reveals Microscopic Contributions to Protein Conformational Entropy,published,journal,Biochemistry,,45,32,,,,,,,,,,,,,,,,,,,,,,9841,9848,2006, citations,primary_citation,15187,24041,1,,reference citation,,,,,,Conformational dynamics of calmodulin in complex with the phosphodiesterase1A calmodulin-binding domain.,in preparation,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_2,15187,24042,2,,entry citation,,,17637663,,,Conformational entropy in molecular recognition by proteins,published,journal,Nature,,448,7151,,,,,,,,,,,,,,,,,,,,,,325,329,2007, citations,entry_citation,15188,24062,1,,entry citation,,,17637663,,,Conformational entropy in molecular recognition by proteins,published,journal,Nature,,448,7151,,,,,,,,,,,,,,,,,,,,,,325,329,2007, citations,entry_citation,15189,24080,1,,entry citation,,,18339402,,,Three-dimensional solution structure and conformational plasticity of the N-terminal scavenger receptor cysteine-rich domain of human CD5,published,journal,J. Mol. Biol.,Journal of Molecular Biology,378,1,,,,,,,,,,,,,,,,,,,,,,129,144,2008, citations,entry_citation,1519,24101,1,,entry citation,,,,,"Brewer, S., Tolley, M., Trayer, I. P., Barr, G. C., Dorman, C. J., Hannavy, K., Higgins, C. F., Evans, J. S., Levine, B.A., Wormald, M.R., ""Structure and Function of X-Pro Dipeptide Repeats in the TonB Proteins of Salmonella typhimurium and Escherichia coli,"" J. Mol. Biol. 216, 883-895 (1990).","Structure and Function of X-Pro Dipeptide Repeats in the TonB Proteins of Salmonella typhimurium and Escherichia coli",published,journal,J. Mol. Biol.,,216,,,,,,,,,,,,,,,,,,,,,,,883,895,1990, citations,entry_citation,15190,24115,1,,entry citation,,,,,,Solution Structure of Protein HP0495 from H. pylori,in preparation,BMRB only,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation_1,15191,24144,1,,entry citation,,,17637663,,,Conformational entropy in molecular recognition by proteins,published,journal,Nature,,448,7151,,,,,,,,,,,,,,,,,,,,,,325,329,2007, citations,entry_citation,15192,24161,1,,entry citation,,,17590019,,,"NMR solution structure, stability, and interaction of the recombinant bovine fibrinogen alphaC-domain fragment.",published,journal,Biochemistry,Biochemistry,46,29,,,,,,,,,,,,,,,,,,,,,,8550,8560,2007, citations,entry_citation,15193,24175,1,,entry citation,,,19636847,,,"NMR assignments of 1H, 13C and 15N spectra of methionine sulfoxide reductase B1 from Mus musculus",published,journal,Biomol. NMR Assignments,,1,1,,,,,,,,,,,,,,,,,,,,,,131,133,2007, citations,citation_1,15194,24191,1,,entry citation,,,19636839,,,"1H, 13C and 15N resonance assignment of truncated SUMO from Trypanosoma brucei",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,1,1,,,,,,,,,,,,,,,,,,,,,,103,104,2007, citations,citations,15195,24205,1,,entry citation,,,17437523,,,Solution Structure of an M-1 Conotoxin with a novel disulfide linkage,published,journal,FEBS J.,,274,10,,,0353,,,,,,,,,,,,,,,,,,,2596,2602,2007, citations,citations,15196,24224,1,,entry citation,,,17202191,,,RNA recognition mechanism of the minimal active domain of the human immunodeficiency virus type-2 nucleocapsid protein,published,journal,J. Biochem.,,141,2,,,0353,,,,,,,,,,,,,,,,,,,269,277,2007, citations,1,15197,24240,1,,entry citation,,,19636832,,,"1H, 15N, and 13C chemical shift assignments of calcium-binding protein 1 (CaBP1)",published,journal,Biomol. NMR Assignments,,1,1,,,,,,,,,,,,,,,,,,,,,,77,79,2007, citations,entry_citation,15198,24254,1,,entry citation,,,16258828,,,Heterologous expression of hen egg white lysozyme and resonance assignment of tryptophan side chains in its non-native states,published,journal,J. Biomol. NMR,,33,2,,,,,,,,,,,,,,,,,,,,,,95,104,2005, citations,entry_citation,15199,24271,1,,entry citation,,,19636852,,,"Sequence-specific (1)H, (13)C, and (15)N backbone assignment of the 28 kDa PDZ2/PDZ3 tandem domain of the protein tyrosine phosphatase PTP-BL",published,journal,Biomol. NMR Assignments,,1,2,,,,,,,,,,,,,,,,,,,,,,151,153,2007, citations,entry_citation,1520,24285,1,,entry citation,,,,,"Harding, Margaret M., Williams, Dudley H., Woolfson, Derek N., ""Characterization of a Partially Denatured State of a Protein by Two-Dimensional NMR: Reduction of the Hydrophobic Interactions in Ubiquitin,"" Biochemistry 30 (12), 3120-3128 (1991).","Characterization of a Partially Denatured State of a Protein by Two-Dimensional NMR: Reduction of the Hydrophobic Interactions in Ubiquitin",published,journal,Biochemistry,,30,12,,,,,,,,,,,,,,,,,,,,,,3120,3128,1991, citations,citation_1,15200,24298,1,,entry citation,,,19636833,,,NMR assignment of the apo-form of a Desulfovibrio gigas protein containing a novel Mo-Cu cluster,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,1,1,,,,,,,,,,,,,,,,,,,,,,81,83,2007, citations,entry_citation,15201,24317,1,,entry citation,,,14744128,,,Nonrandom Structure in the Urea-Unfolded Escherichia coli Outer Membrane Protein X (OmpX),published,journal,Biochemistry,,43,4,,,,,,,,,,,,,,,,,,,,,,860,869,2004, citations,entry_citation,15202,24331,1,,entry citation,,,19636840,,,"Sequence-specific 1H, 13C, and 15N backbone assignment of the activated 21 kDa GTPase rRheb",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,1,1,,,,,,,,,,,,,,,,,,,,,,105,108,2007, citations,entry_citation,15203,24352,1,,entry citation,,,,,,NMR structure of Clostridium perfringens protein CPE0013.,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,1,15204,24388,1,,entry citation,,,19636836,,,"Assignment of 1H, 13C and 15N resonances of the reduced human IgG1 C(H)3 domain",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,1,1,,,,,,,,,,,,,,,,,,,,,,93,94,2007, citations,entry_citation,15206,24403,1,,entry citation,,,17617421,,,"Differences in the electrostatic surfaces of the type III secretion needle proteins PrgI, BsaL, and MxiH.",published,journal,J. Mol. Biol.,,371,5,,,,,,,,,,,,,,,,,,,,,,1304,1314,2007, citations,entry_citation,15207,24420,1,,entry citation,,,19636835,,,"1H, 13C and 15N resonance assignments of YajG, an Escherichia coli protein of unknown structure and function",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,1,1,,,,,,,,,,,,,,,,,,,,,,89,91,2007, citations,entry_citation,15208,24442,1,,entry citation,,,17610897,,,"Embryonic Neural Inducing Factor Churchill is not a DNA-Binding Zinc Finger Protein: Solution Structure Reveals a Solvent-Exposed Beta-Sheet and Zinc Binuclear Cluster",published,journal,J. Mol. Biol.,,371,5,,,,,,,,,,,,,,,,,,,,,,1274,1289,2007, citations,citations,15209,24466,1,,entry citation,,,,,,Solution Structure of the hDLG/SAP97 PDZ2 domain and its mechanism for interaction with HPV-18 papillomavirus E6 protein,published,journal,Biochemistry,,46,38,,,0353,,,,,,,,,,,,,,,,,,,10864,10874,2007, citations,entry_citation,15210,24488,1,,entry citation,,,,,,"NMR Structure of 50S Ribosomal Protein L14e from Sulfolobus Solfataricus; Northeast Structural Genomics Consortium Target SSR105.",published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15211,24510,1,,entry citation,,,,,,"Solution NMR structure of protein, Northeastprotein yxeF Structural Genomics Consortium target Sr500a",in preparation,journal,Protein Sci.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15212,24530,1,,entry citation,,,19636870,,,"1H, 13C and 15N Resonance assignments of the first N-terminal RNA recognition motif (RRM) of the human heterogeneous nuclear ribonucleoprotein H (hnRNP H)",published,journal,Biomol. NMR Assignments,,1,2,,,,,,,,,,,,,,,,,,,,,,221,223,2007, citations,entry_citation,15214,24561,1,,entry citation,,,17827155,,,"Identification of the MxiH needle protein residues responsible for anchoring invasion plasmid antigen D to the type III secretion needle tip",published,journal,J. Biol. Chem.,Journal of Biological Chemistry,282,44,,,,,,,,,,,,,,,,,,,,,,32144,32151,2007, citations,citations,15215,24575,1,,entry citation,,,17302442,,,An engineered second disulfide bond restricts lymphotactin/XCL1 to a chemokine-like conformation with XCR1 agonist activity,published,journal,Biochemistry,,46,10,,,0353,,,,,,,,,,,,,,,,,,,2564,2573,2007, citations,citations,15217,24596,1,,entry citation,,,,,,NMR Solution Structure of Ykvr Protein from Bacillus Subtilis: Northeast Structural Genomics Consortium Target SR358,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15218,24629,1,,entry citation,,,17983687,,,"Structure-function analysis of the antiangiogenic ATWLPPR peptide inhibiting VEGF(165) binding to neuropilin-1 and molecular dynamics simulations of the ATWLPPR/neuropilin-1 complex.",published,journal,Peptides,,28,12,,,,,,,,,,,,,,,,,,,,,,2397,2402,2007, citations,citation_1,15219,24647,1,,entry citation,,,18088598,,,The RXRalpha C-terminus T462 is a NMR sensor for coactivator peptide binding,published,journal,Biochem. 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NMR Assignments,,1,2,,,,,,,,,,,,,,,,,,,,,,209,211,2007, citations,entry_citation,15252,25186,1,,entry citation,,,17878153,,,Crystallographic and NMR analyses of UvsW and UvsW.1 from bacteriophage T4,published,journal,J. Biol. Chem.,,282,47,,,,,,,,,,,,,,,,,,,,,,34392,34400,2007, citations,entry_citation,15253,25207,1,,entry citation,,,18825778,,,NMR-derived folate-bound structure of dihydrofolate reductase 1 from the halophile Haloferax volcanii,published,journal,Biopolymers,,91,2,,,,,,,,,,,,,,,,,,,,,,140,4,2009, citations,entry_citation,15254,25224,1,,entry citation,,,17976643,,,"Backbone dynamics in an intramolecular prolylpeptide-SH3 complex from the diphtheria toxin repressor, DtxR",published,journal,J. Mol. Biol.,,374,4,,,,,,,,,,,,,,,,,,,,,,977,992,2007, citations,DtxR_SH3,15255,25243,1,,entry citation,,,17976643,,,"Backbone dynamics in an intramolecular prolylpeptide-SH3 complex from the diphtheria toxin repressor, DtxR",published,journal,J. Mol. Biol.,,374,4,,,,,,,,,,,,,,,,,,,,,,977,992,2007, citations,entry_citation,15256,25261,1,,entry citation,,,17884092,,,"Structural basis of ligand binding and release in insect pheromone-binding proteins: NMR structure of Antheraea polyphemus PBP1 at pH 4.5",published,journal,J. Mol. Biol.,,373,4,JMOBAK UK,0022-2836,,,,,,,,,,,,,,,,,,,,811,819,2007, citations,entry_citation,15257,25281,1,,entry citation,,,17704818,,,Molecular basis of messenger RNA recognition by the specific bacterial repressing clamp RsmA/CsrA.,published,journal,Nat. Struct. Mol. Biol.,,14,9,,,,,,,,,,,,,,,,,,,,,,807,813,2007, citations,entry_citation,15258,25305,1,,entry citation,,,,,,Solution NMR structure of Vibrio parahaemolyticus VP2129. 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Biol.,,376,4,,,,,,,,,,,,,,,,,,,,,,1048,1059,2008, citations,entry_citation,15264,25420,1,,entry citation,,,17919953,,,Protein assignments without peak lists using higher-order spectra,published,journal,J. Magn. Reson.,,189,2,,,,,,,,,,,,,,,,,,,,,,173,181,2007, citations,entry_citation,15265,25440,1,,entry citation,,,,,,"solution structure of NESG target SsR10, Orf c02003 protein",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15266,25464,1,,entry citation,,,19636853,,,"(1)H, (13)C, and (15)N backbone resonance assignments of the carboxyl terminal domain of Connexin40",published,journal,Biomol. NMR Assignments,,1,2,,,,,,,,,,,,,,,,,,,,,,155,157,2007, citations,citation_1,15267,25479,1,,entry citation,,,17927950,,,Structural biology of membrane-acting peptides: Conformational plasticity of anticoccidial peptide PW2 probed by solution NMR,published,journal,Biochim. Biophys. 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Chem.,,283,25,,,,,,,,,,,,,,,,,,,,,,17416,17427,2008, citations,entry_citation,15269,25517,1,,entry citation,,,,,,Solution Structure of a protein (ATC2521)of unknow function from Agrobacterium tumefaciens,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15270,25541,1,,entry citation,,,,,,Solution structure of a Se-C motif containing protein from Rhodopseudomonas palustris,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15271,25567,1,,entry citation,,,17766387,,,Solution structure of recombinant Somatomedin B domain from vitronectin produced in Pichia pastoris,published,journal,Protein Sci.,,16,9,,,,,,,,,,,,,,,,,,,,,,1934,1945,2007, citations,citation_1,15272,25586,1,,entry citation,,,18355315,,,"Purification and structural characterization of a D-amino acid-containing conopeptide, conomarphin, from Conus marmoreus",published,journal,FEBS J.,,275,9,,,,,,,,,,,,,,,,,,,,,,1976,1987,2008, citations,entry_citation,15273,25607,1,,entry citation,,,18355315,,,"Purification and structural characterization of a D-amino acid-containing conopeptide, conomarphin, from Conus marmoreus",published,journal,FEBS J.,,275,9,,,,,,,,,,,,,,,,,,,,,,1976,1987,2008, citations,entry_citation,15274,25627,1,,entry citation,,,18809412,,,Intrinsically Unstructured Domains of Arf and Hdm2 Form Bimolecular Oligomeric Structures In Vitro and In Vivo,published,journal,J. Mol. Biol.,Journal of Molecular Biology,384,1,,,,,,,,,,,,,,,,,,,,,,240,254,2008, citations,entry_citation,15275,25644,1,,entry citation,,,18618268,,,A. fulgidus SRP54 M-domain,published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,41,4,,,,,,,,,,,,,,,,,,,,,,241,248,2008, citations,entry_citation,15276,25664,1,,entry citation,,,19636854,,,"1H, 13C and 15N resonance assignment of 6aJL2(R25G), a highly fibrillogenic lamdaVI light chain variable domain.",published,journal,Biomol. NMR Assignments,,1,2,,,,,,,,,,,,,,,,,,,,,,159,161,2007, citations,entry_citation,15277,25683,1,,entry citation,,,17897674,,,Investigating the substrate specificity and oligomerisation of the leader protease of foot and mouth disease virus using NMR,published,journal,J. Mol. Biol.,,373,4,,,,,,,,,,,,,,,,,,,,,,1071,1087,2007, citations,entry_citation,15278,25705,1,,entry citation,,,17897674,,,Investigating the substrate specificity and oligomerisation of the leader protease of foot and mouth disease virus using NMR,published,journal,J. Mol. Biol.,,373,4,,,,,,,,,,,,,,,,,,,,,,1071,1087,2007, citations,entry_citation,15279,25728,1,,entry citation,,,17899392,,,EH domain of EHD1,published,journal,J. Biomol. NMR,,39,4,,,,,,,,,,,,,,,,,,,,,,323,329,2007, citations,entry_citation,15280,25746,1,,entry citation,,,19636850,,,"1H, 13C and 15N resonance assignment of the oxidized form (Cys(67)-Cys (70)) of the N-terminal domain of PilB from Neisseria meningitidis",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,1,1,,,,,,,,,,,,,,,,,,,,,,143,145,2007, citations,citation_1,15281,25761,1,,entry citation,,,,,,Solution NMR structure of CC0527 from Caulobacter crescentus. Northeast Structural Genomics target CcR55.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,N-Me-Phe5_citation,15282,25805,1,,entry citation,,,19164290,,,Rapid optimization of a peptide inhibitor of malaria parasite invasion by comprehensive N-methyl scanning.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,284,14,,,,,,,,,,,,,,,,,,,,,,9361,9371,2009, citations,citation_1,15283,25820,1,,entry citation,,,19636843,,,"13C and 15N chemical shift assignments and secondary structure of the B3 immunoglobulin-binding domain of streptococcal protein G by magic-angle spinning solid-state NMR spectroscopy",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,1,1,,,,,,,,,,,,,,,,,,,,,,117,120,2007, citations,N-Me-Leu8_citation,15284,25836,1,,entry citation,,,19164290,,,Rapid optimization of a peptide inhibitor of malaria parasite invasion by comprehensive N-methyl scanning.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,284,14,,,,,,,,,,,,,,,,,,,,,,9361,9371,2009, citations,N-Me-Lys11_citation,15285,25852,1,,entry citation,,,19164290,,,Rapid optimization of a peptide inhibitor of malaria parasite invasion by comprehensive N-methyl scanning.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,284,14,,,,,,,,,,,,,,,,,,,,,,9361,9371,2009, citations,entry_citation,15286,25867,1,,entry citation,,,,,,chemical shift values for Bungatoxin,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,N-Me-Phe12_citation,15287,25882,1,,entry citation,,,19164290,,,Rapid optimization of a peptide inhibitor of malaria parasite invasion by comprehensive N-methyl scanning.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,284,14,,,,,,,,,,,,,,,,,,,,,,9361,9371,2009, citations,entry_citation,15288,25897,1,,entry citation,,,,,,NMR solution structure of Bacillus subtilis YobA 21-120,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15289,25918,1,,entry citation,,,18073205,,,"Structure-Function Analysis of the THAP Zinc Finger of THAP1, a Large C2CH DNA-binding Module Linked to Rb/E2F Pathways.",published,journal,J. Biol. Chem.,,283,7,,,,,,,,,,,,,,,,,,,,,,4352,4363,2008, citations,entry_citation,15290,25939,1,,entry citation,,,17565980,,,Structural analysis of Conserved Oligomeric Golgi complex subunit 2,published,journal,J. Biol. Chem.,Journal of Biological Chemistry,282,32,,,,,,,,,,,,,,,,,,,,,,23418,23426,2007, citations,N-Me-Gly13_citation,15291,25963,1,,entry citation,,,19164290,,,Rapid optimization of a peptide inhibitor of malaria parasite invasion by comprehensive N-methyl scanning.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,284,14,,,,,,,,,,,,,,,,,,,,,,9361,9371,2009, citations,N-Me-Ser14_citation,15292,25978,1,,entry citation,,,19164290,,,Rapid optimization of a peptide inhibitor of malaria parasite invasion by comprehensive N-methyl scanning.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,284,14,,,,,,,,,,,,,,,,,,,,,,9361,9371,2009, citations,N-Me-Leu8_N-Me-Ser14_citation,15293,25993,1,,entry citation,,,19164290,,,Rapid optimization of a peptide inhibitor of malaria parasite invasion by comprehensive N-methyl scanning.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,284,14,,,,,,,,,,,,,,,,,,,,,,9361,9371,2009, citations,N-Me-Val1_N-Me-Leu8_N-Me-Ser14_citation,15294,26009,1,,entry citation,,,19164290,,,Rapid optimization of a peptide inhibitor of malaria parasite invasion by comprehensive N-methyl scanning.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,284,14,,,,,,,,,,,,,,,,,,,,,,9361,9371,2009, citations,citations,15295,26026,1,,entry citation,,,18214976,,,Solution structure of At3g28950 from Arabidopsis thaliana,published,journal,Proteins,,71,2,,,,,,,,,,,,,,,,,,,,,,546,551,2008, citations,entry_citation,15296,26046,1,,entry citation,,,18089560,,,"S100A1 binds to the calmodulin-binding site of ryanodine receptor and modulates skeletal muscle excitation-contraction coupling",published,journal,J. Biol. Chem.,,283,8,,,,,,,,,,,,,,,,,,,,,,5046,5057,2008, citations,entry_citation,15298,26064,1,,entry citation,,,17681539,,,"Structural characterization of the intrinsically unfolded protein beta-synuclein, a natural negative regulator of alpha-Synuclein aggregation",published,journal,J. Mol. Biol.,,372,3,,,,,,,,,,,,,,,,,,,,,,708,722,2007, citations,entry_citation,15299,26079,1,,entry citation,,,18042681,,,"Chemical synthesis and 1H-NMR 3D structure determination of AgTx2-MTX chimera, a new potential blocker for Kv1.2 channel, derived from MTX and AgTx2 scorpion toxins",published,journal,Protein Sci.,,17,1,,,,,,,,,,,,,,,,,,,,,,107,118,2008, citations,entry_citation,15300,26094,1,,entry citation,,,18073205,,,"Structure-Function Analysis of the THAP Zinc Finger of THAP1, a Large C2CH DNA-binding Module Linked to Rb/E2F Pathways.",published,journal,J. Biol. Chem.,,283,7,,,,,,,,,,,,,,,,,,,,,,4352,4363,2008, citations,entry_citation,15301,26115,1,,entry citation,,,18439013,,,Dynamics in a pure encounter complex of two proteins studied by solution scattering and paramagnetic NMR spectroscopy,published,journal,J. Am. Chem. Soc.,,130,20,,,,,,,,,,,,,,,,,,,,,,6395,6403,2008, citations,Reference1,15301,26116,2,,reference citation,,,,,,HIGH-RESOLUTION REFINEMENT OF YEAST ISO-1-CYTOCHROME C AND COMPARISONS WITH OTHER EUKARYOTIC CYTOCHROMES C,published,journal,J. Mol. Biol.,,214,2,,,,,,,,,,,,,,,,,,,,,,527,555,1990, citations,Reference2,15301,26117,3,,reference citation,,,9551550,,,"New aspects of electron transfer revealed by the crystal structure of a truncated bovine adrenodoxin, Adx(4-1080",published,journal,Structure,,6,3,,,,,,,,,,,,,,,,,,,,,,269,280,1998, citations,entry_citation,15302,26143,1,,entry citation,,,18584053,,,Odorranalectin is a small peptide lectin with potential for drug delivery and targeting.,published,journal,PLoS ONE,PLoS ONE,3,6,,,,,,,,,,,,,,,,,,,,,,e2381,e2381,2008, citations,citation_1,15303,26158,1,,entry citation,,,19636846,,,"1H, 13C and 15N resonance assignments of the bb' domains of human protein disulfide isomerase",published,journal,Biomol. NMR Assignments,,1,1,,,,,,,,,,,,,,,,,,,,,,129,130,2007, citations,citations,15304,26175,1,,entry citation,,,17927700,,,"The solution structure of the periplasmic domain of the TonB system ExbD protein reveals an unexpected structural homology with siderophore binding proteins.",published,journal,Mol. Microbiol.,,66,4,,,0353,,,,,,,,,,,,,,,,,,,872,889,2007, citations,entry_citation,15305,26192,1,,entry citation,,,17918958,,,Role of glycosphingolipid conformational change in membrane pore forming activity of cobra cardiotoxin,published,journal,Biochemistry,,46,43,,,,,,,,,,,,,,,,,,,,,,12111,12123,2007, citations,entry_citation,15306,26211,1,,entry citation,,,17719543,,,Auto-inhibition of the HECT-type ubiquitin ligase Smurf2 through its C2 domain,published,journal,Cell,,130,4,,,,,,,,,,,,,,,,,,,,,,651,662,2007, citations,entry_citation,15309,26229,1,,entry citation,,,17918958,,,Role of glycosphingolipid conformational change in membrane pore forming activity of cobra cardiotoxin,published,journal,Biochemistry,,46,43,,,,,,,,,,,,,,,,,,,,,,12111,12123,2007, citations,entry_citation,15312,26247,1,,entry citation,,,18177898,,,Structural biophysics of the NusB:NusE antitermination complex,published,journal,J. Mol. Biol.,,376,3,,,,,,,,,,,,,,,,,,,,,,705,720,2008, citations,entry_citation,15313,26264,1,,entry citation,,,19636848,,,"1H, 15N and 13C backbone and side chain chemical shifts of human ASC (apoptosis-associated speck-like protein containing a CARD domain)",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,1,1,,,,,,,,,,,,,,,,,,,,,,135,137,2007, citations,entry_citation,15314,26280,1,,entry citation,,,,,,"Solution structure of the DNA binding domain of a nucleoid-associated protein, H-NS, from the phytopathogen Xylella fastidiosa.",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15315,26300,1,,entry citation,,,17703188,,,Structural basis of the collagen-binding mode of discoidin domain receptor 2,published,journal,EMBO J.,,26,18,,,,,,,,,,,,,,,,,,,,,,4168,4176,2007, citations,entry_citation,15316,26319,1,,entry citation,,,17920624,,,Electrostatic contributions to the stability of the GCN4 leucine zipper structure.,published,journal,J. Mol. Biol.,,374,1,,,,,,,,,,,,,,,,,,,,,,206,219,2007, citations,entry_citation,15317,26333,1,,entry citation,,,,,,Solution NMR structure of Colwellia psychrerythraea protein CPS_2611. Northeast Structural Genomics target CsR4.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,15318,26386,1,,entry citation,,,18341335,,,"Structure, self-assembly, and dual role of a beta-defensin-like peptide from the Chinese soft-shelled turtle eggshell matrix",published,journal,J. Am. Chem. Soc.,,130,14,,,,,,,,,,,,,,,,,,,,,,4660,4668,2008, citations,entry_citation,15319,26402,1,,entry citation,,,18473483,,,Anticodon domain modifications contribute order to tRNA for ribosome-mediated codon binding,published,journal,Biochemistry,,47,23,,,,,,,,,,,,,,,,,,,,,,6117,6129,2008, citations,entry_citation,15320,26423,1,,entry citation,,,,,,Solution structure of UPF0350 protein VC_2471: Northeast Structural Genomics Target VcR36,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15322,26446,1,,entry citation,,,17631272,,,Solution structure of the bacterial chemotaxis adaptor protein CheW from Escherichia coli,published,journal,Biochem. Biophys. Res. Commun.,,360,4,,,,,,,,,,,,,,,,,,,,,,863,867,2007, citations,entry_citation,15323,26460,1,,entry citation,,,18265434,,,"Solution structure, antibacterial activity, and expression profile of Manduca sexta moricin",published,journal,J. Pept. Sci.,,14,7,,,,,,,,,,,,,,,,,,,,,,855,863,2008, citations,entry_citation,15324,26475,1,,entry citation,,,,,,A novel domain-swapped solution NMR structure of protein RPA2121 from Rhodopseudomonas palustris,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15325,26497,1,,entry citation,,,17569664,,,Identification and solution structure of a highly conserved C-terminal domain within ORF1p required for retrotransposition of long interspersed nuclear element-1,published,journal,J. Biol. Chem.,,282,34,,,,,,,,,,,,,,,,,,,,,,24893,24904,2007, citations,entry_citation,15326,26512,1,,entry citation,,,19636857,,,"NMR assignment of human chemerin, a novel chemoattractant",published,journal,Biomol. NMR Assignments,,1,2,,,,,,,,,,,,,,,,,,,,,,171,173,2007, citations,entry_citation,15327,26528,1,,entry citation,,,,,,Solution NMR Structure of protein YqcC from E. coli,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,15329,26546,1,,entry citation,,,TBA,,,Solution NMR structure of Tubulin polymerization-promoting protein family member 3 from Homo sapiens. Northeast Structural Genomics target HR387.,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15330,26571,1,,entry citation,,,19917307,,,Caenopore-5: the three-dimensional structure of an antimicrobial protein from Caenorhabditis elegans.,published,journal,Dev. Comp. Immunol.,Developmental and comparative immunology,34,3,,,,,,,,,,,,,,,,,,,,,,323,330,2010, citations,entry_citation,15331,26587,1,,entry citation,,,18473483,,,Anticodon domain modifications contribute order to tRNA for ribosome-mediated codon binding,published,journal,Biochemistry,,47,23,,,,,,,,,,,,,,,,,,,,,,6117,6129,2008, citations,entry_citation,15332,26610,1,,entry citation,,,17985933,,,Insight into the Binding Properties of MEKK3 PB1 to MEK5 PB1 from Its Solution Structure,published,journal,Biochemistry,,46,47,,,,,,,,,,,,,,,,,,,,,,13478,13489,2007, citations,entry_citation,15333,26626,1,,entry citation,,,19043414,,,Molecular basis of Pirh2-mediated p53 ubiquitylation,published,journal,Nat. Struct. Mol. Biol.,,15,12,,,,,,,,,,,,,,,,,,,,,,1334,1342,2008, citations,NtrC4Ra,15334,26650,1,,entry citation,,,12885241,,,High-resolution solution structure of the beryllofluoride-activated NtrC receiver domain.,published,journal,Biochemistry,Biochemistry,42,30,,,,,,,,,,,,,,,,,,,,,,9081,9090,2003, citations,entry_citation,15335,26673,1,,entry citation,,,18951393,,,Structural elucidation of the Cys-His-Glu-Asn proteolytic relay in the secreted CHAP domain enzyme from the human pathogen Staphylococcus saprophyticus.,published,journal,Proteins,,74,2,,,,,,,,,,,,,,,,,,,,,,515,9,2009, citations,entry_citation,15336,26721,1,,entry citation,,,17660831,,,CFTR regulatory region interacts with NBD1 predominantly via multiple transient helices.,published,journal,Nat. Struct. Mol. Biol.,,14,8,,,,,,,,,,,,,,,,,,,,,,738,745,2007, citations,citation_1,15337,26735,1,,entry citation,,,,,,Solution Structure of SO0334 from Shewanella Oneidensis. Northeast Structural Genomics Consortium target SoR75,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15338,26763,1,,entry citation,,,,,,NMR Structure of Protein YfgJ from Salmonella Typhimurium.,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,15339,26805,1,,entry citation,,,TBA,,,"Solution NMR Structure of Ribosome Modulation Factor VP1593 from Vibrio parahaemolyticus",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15340,26846,1,,entry citation,,,17660831,,,CFTR regulatory region interacts with NBD1 predominantly via multiple transient helices.,published,journal,Nat. Struct. Mol. Biol.,,14,8,,,,,,,,,,,,,,,,,,,,,,738,745,2007, citations,citation_1,15341,26860,1,,entry citation,,,,,,NMR solution Structure of Q5LLS5 from Silicibacter pomeroyi.Northeast Structural Genomics Consortium target SiR90,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15342,26902,1,,entry citation,,,18473483,,,Anticodon domain modifications contribute order to tRNA for ribosome-mediated codon binding,published,journal,Biochemistry,,47,23,,,,,,,,,,,,,,,,,,,,,,6117,6129,2008, citations,entry_citation,15343,26924,1,,entry citation,,,,,,Solution NMR Structure of CAPER RRM2 Domain. Northeast Structural Genomics Target HR4730A.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15344,26954,1,,entry citation,,,,,,"The solution structure of the protein coded by gene RHOS4_12090 of R. sphaeroides. Northeast structural genomics target RhR5",in preparation,journal,Proteins,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15345,26975,1,,entry citation,,,18684949,,,"Nuclear Magnetic Resonance Structure and IgE Epitopes of Blo t 5, a Major Dust Mite Allergen",published,journal,J. Immunol.,The Journal of Immunology,181,4,,,,,,,,,,,,,,,,,,,,,,2586,2596,2008, citations,entry_citation,15346,26992,1,,entry citation,,,,,,NMR Chemical Shift Assignments of E. coli YejL protein,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15347,27012,1,,entry citation,,,,,,Chemical Shift Assignments of protein NE0084 from Nitrosomonas europea: Northeast Structural Genomics Consortium Target NeT6,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15348,27033,1,,entry citation,,,19636912,,,"Backbone and sidechain 1H, 13C and 15N resonance assignments of the Bright/ARID domain from the human JARID1C (SMCX) protein",published,journal,Biomol. NMR Assignments,,2,1,,,,,,,,,,,,,,,,,,,,,,9,11,2008, citations,citations,15349,27057,1,,entry citation,,,18269246,,,Specificity Determinants of a Novel Nck Interaction with the Juxtamembrane Domain of the Epidermal Growth Factor Receptor,published,journal,Biochemistry,,47,10,,,,,,,,,,,,,,,,,,,,,,3096,3108,2008, citations,entry_citation,15350,27076,1,,entry citation,,,,,,"NMR Structure of the Bacillus subtilis Protein YvfG, Northeast Structural Genomics Target SR478",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,15351,27112,1,,entry citation,,,18269246,,,Specificity Determinants of a Novel Nck Interaction with the Juxtamembrane Domain of the Epidermal Growth Factor Receptor,published,journal,Biochemistry,,47,10,,,,,,,,,,,,,,,,,,,,,,3096,3108,2008, citations,NMR_Structure_of_protein_Q6N9A4_RHOPA,15352,27131,1,,entry citation,,,,,,NMR Structure of protein Q6N9A4_RHOPA,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15353,27153,1,,entry citation,,,,,,NMR Solution Structure of Bordetella bronchiseptica protein BB2007,in preparation,journal,Proteins: Struct. Funct. Genet.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,NMR_Structure_of_Q60C73_METCA,15354,27178,1,,entry citation,,,,,,NMR Structure of protein Q60C73_METCA,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,15355,27198,1,,entry citation,,,17985933,,,Insight into the binding properties of MEKK3 PB1 to MEK5 PB1 from its solution structure,published,journal,Biochemistry,,46,47,,,,,,,,,,,,,,,,,,,,,,13478,13489,2007, citations,entry_citation,15356,27216,1,,entry citation,,,,,,Solution NMR Structure of Human Myeloid Differentiation Primary Response (MyD88). Northeast Structural Genomics target HR2869A.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15357,27246,1,,entry citation,,,19658434,,,The native-like interactions between SNase121 and SNase(111-143) fragments induce the recovery of their native-like structures and the ability to degrade DNA.,published,journal,Biochemistry,Biochemistry,48,36,,,,,,,,,,,,,,,,,,,,,,8692,8703,2009, citations,entry_citation,15358,27260,1,,entry citation,,,19917307,,,Caenopore-5: the three-dimensional structure of an antimicrobial protein from Caenorhabditis elegans.,published,journal,Dev. Comp. Immunol.,Developmental and comparative immunology,34,3,,,,,,,,,,,,,,,,,,,,,,323,330,2010, citations,entry_citation,15359,27276,1,,entry citation,,,17935487,,,Structure and mode of action of the antimicrobial peptide arenicin,published,journal,Biochem. J.,,410,1,,,,,,,,,,,,,,,,,,,,,,113,122,2008, citations,citations,15360,27292,1,,entry citation,,,17497831,,,"Solution structures of a DNA dodecamer duplex with and without a cisplatin 1,2-d(GG) intrastrand cross-link: comparison with the same DNA duplex containing an oxaliplatin 1,2-d(GG) intrastrand cross-link",published,journal,Biochemistry,,46,22,,,,,,,,,,,,,,,,,,,,,,6477,6487,2007, citations,entry_citation,15361,27310,1,,entry citation,,,17869250,,,"Catalytic domain of MMP20 (Enamelysin) - the NMR structure of a new matrix metalloproteinase.",published,journal,FEBS Lett.,,518,24,,,,,,,,,,,,,,,,,,,,,,4723,4726,2007, citations,entry_citation,15362,27339,1,,entry citation,,,18473483,,,Anticodon domain modifications contribute order to tRNA for ribosome-mediated codon binding,published,journal,Biochemistry,,47,23,,,,,,,,,,,,,,,,,,,,,,6117,6129,2008, citations,citations,15363,27361,1,,entry citation,,,18355315,,,"Purification and structural characterization of a D-amino acid-containing conopeptide, conomarphin, from Conus marmoreus",published,journal,FEBS. J.,,275,9,,,,,,,,,,,,,,,,,,,,,,1976,1987,2008, citations,citations,15364,27382,1,,entry citation,,,17202191,,,RNA recognition mechanism of the minimal active domain of the human immunodeficiency virus type-2 nucleocapsid protein,published,journal,J. Biochem.,,141,2,,,0353,,,,,,,,,,,,,,,,,,,269,277,2007, citations,citation_1,15366,27404,1,,entry citation,,,19636860,,,NMR assignments of the C-terminal domain of human polypeptide release factor eRF1,published,journal,Biomol. NMR Assignments,,1,2,,,,,,,,,,,,,,,,,,,,,,183,185,2007, citations,citation_1,15367,27428,1,,entry citation,,,18295795,,,"alpha-RgIA, a Novel Conotoxin That Blocks the alpha9alpha10 nAChR: Structure and Identification of Key Receptor-Binding Residues",published,journal,J. Mol. Biol.,,377,4,,,,,,,,,,,,,,,,,,,,,,1216,1227,2008, citations,entry_citation,15368,27442,1,,entry citation,,,18295795,,,"alpha-RgIA, a Novel Conotoxin That Blocks the alpha9alpha10 nAChR: Structure and Identification of Key Receptor-Binding Residues",published,journal,J. Mol. Biol.,,377,4,,,,,,,,,,,,,,,,,,,,,,1216,1227,2008, citations,entry_citation,15369,27457,1,,entry citation,,,19636861,,,"(1)H, (13)C and (15)N backbone and side chain resonance assignments of a 28 kDa active mutant of maize ribosome-inactivating protein (MOD)",published,journal,Biomol. NMR Assignments,,1,2,,,,,,,,,,,,,,,,,,,,,,187,189,2007, citations,entry_citation,15370,27471,1,,entry citation,,,19200043,,,Solution Structure of Synbindin Atypical PDZ Domain and Interaction with Syndecan-2,published,journal,Protein Pept. Lett.,Protein and Peptide Letters,16,2,,,,,,,,,,,,,,,,,,,,,,189,195,2009, citations,citation_1,15371,27490,1,,entry citation,,,17686460,,,First structure of the polymyxin resistance proteins,published,journal,Biochem. Biophys. Res. Commun.,Biochemical and Biophysical Research Communications,361,4,,,,,,,,,,,,,,,,,,,,,,1033,1037,2007, citations,entry_citation,15372,27509,1,,entry citation,,,18558717,,,"The NMR Structure and Dynamics of the Two-Domain Tick Carboxypeptidase Inhibitor Reveal Flexibility in Its Free Form and Stiffness upon Binding to Human Carboxypeptidase B",published,journal,Biochemistry,,47,27,,,,,,,,,,,,,,,,,,,,,,7066,7078,2008, citations,entry_citation,15373,27531,1,,entry citation,,,17956987,,,"The prokaryotic Cys2His2 zinc finger adopts a novel fold as revealed by the NMR structure of A.tumefaciens Ros DNA binding domain",published,journal,Proc. Natl. Acad. Sci. U.S.A.,,104,44,,,,,,,,,,,,,,,,,,,,,,17341,17346,2007, citations,entry_citation,15374,27558,1,,entry citation,,,19997764,,,An NMR structural study of nickel-substituted rubredoxin.,published,journal,J. Biol. Inorg. Chem.,Journal of biological inorganic chemistry,15,3,,,,,,,,,,,,,,,,,,,,,,409,420,2010, citations,entry_citation,15375,27580,1,,entry citation,,,19997764,,,An NMR structural study of nickel-substituted rubredoxin.,published,journal,J. Biol. Inorg. 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Chem.,The Journal of biological chemistry,285,41,,,,,,,,,,,,,,,,,,,,,,31682,31693,2010, citations,entry_citation,15395,28000,1,,entry citation,,,17710450,,,"Matrix metalloproteinase-inhibitor interaction: the solution structure of the catalytic domain of human matrix metalloproteinase-3 with different inhibitors.",published,journal,J. Biol. Inorg. Chem.,,12,8,,,,,,,,,,,,,,,,,,,,,,1197,1206,2007, citations,entry_citation,15396,28020,1,,entry citation,,,17710450,,,"Matrix metalloproteinase-inhibitor interaction: the solution structure of the catalytic domain of human matrix metalloproteinase-3 with different inhibitors.",published,journal,J. Biol. Inorg. Chem.,,12,8,,,,,,,,,,,,,,,,,,,,,,1197,1206,2007, citations,entry_citation,15397,28040,1,,entry citation,,,18177052,,,"NMR Relaxation Study of the Complex Formed Between CBP and the Activation Domain of the Nuclear Hormone Receptor Coactivator ACTR",published,journal,Biochemistry,,47,5,,,,,,,,,,,,,,,,,,,,,,1299,1308,2008, citations,entry_citation,15398,28056,1,,entry citation,,,18177052,,,"NMR Relaxation Study of the Complex Formed Between CBP and the Activation Domain of the Nuclear Hormone Receptor Coactivator ACTR",published,journal,Biochemistry,,47,5,,,,,,,,,,,,,,,,,,,,,,1299,1308,2008, citations,entry_citation,15399,28072,1,,entry citation,,,20949107,,,Solution Structure and Dynamics of the I214V Mutant of the Rabbit Prion Protein.,published,journal,PLoS ONE,PloS one,5,10,,,,,,,,,,,,,,,,,,,,,,e13273,,2010, citations,entry_citation,15400,28087,1,,entry citation,,,16131667,,,"Effects of Phe-to-Trp mutation and fluorotryptophan incorporation on the solution structure of cardiac troponin C, and analysis of its suitability as a potential probe for in situ NMR studies",published,journal,Protein Sci.,,14,9,,,,,,,,,,,,,,,,,,,,,,2447,2460,2005, citations,citations,15401,28106,1,,entry citation,,,21330362,,,Structures of Anabaena Calcium-binding Protein CcbP: INSIGHTS INTO CA2+ SIGNALING DURING HETEROCYST DIFFERENTIATION.,published,journal,J. 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NMR Assignments,,1,2,,,,,,,,,,,,,,,,,,,,,,175,177,2007, citations,entry_citation,15404,28160,1,,entry citation,,,18361504,,,Structural features responsible for the biological stability of Histoplasma's virulence factor CBP,published,journal,Biochemistry,,47,15,,,,,,,,,,,,,,,,,,,,,,4427,4438,2008, citations,entry_citation,15405,28179,1,,entry citation,,,17585879,,,The NMR Solution Structure of Recombinant RGD-hirudin,published,journal,Biochem. Biophys. Res. Commun.,,360,1,,,,,,,,,,,,,,,,,,,,,,103,108,2007, citations,citations,15406,28195,1,,entry citation,,,17109885,,,"Solution structure of E.coli PapI, a key regulator of the pap pili phase variation",published,journal,J. Mol. Biol.,,365,4,,,0353,,,,,,,,,,,,,,,,,,,1130,1142,2007, citations,entry_citation,15407,28213,1,,entry citation,,,17922258,,,The high resolution NMR structure of the third SH3 domain of CD2AP,published,journal,J. Biomol. 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Biol.,,373,3,,,,,,,,,,,,,,,,,,,,,,652,663,2007, citations,entry_citation,15418,28399,1,,entry citation,,,18803400,,,"Structure of the S100A6 complex with a fragment from the C-terminal domain of Siah-1 interacting protein: a novel mode for S100 protein target recognition",published,journal,Biochemistry,,47,41,,,,,,,,,,,,,,,,,,,,,,10921,10932,2008, citations,entry_citation,15419,28423,1,,entry citation,,,,,,"Solution Structure of protein RPA3401, Northeast Structural Genomics Consortium Target RpT7, Ontario Center for Structural Proteomics Target RP3384",in preparation,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1542,28446,1,,entry citation,,,,,"Lecomte, Juliette T.J., De Marco, A., Llinas, M., ""Analysis of the Methyl 1H-NMR Spectrum of Crambin, a Hydrophobic Protein,"" Biochim. Biophys. Acta 703, 223-230 (1982).","Analysis of the Methyl 1H-NMR Spectrum of Crambin, a Hydrophobic Protein",published,journal,Biochim. Biophys. Acta,,703,,,,,,,,,,,,,,,,,,,,,,,223,230,1982, citations,entry_citation,15420,28459,1,,entry citation,,,23300835,,,Recombinant expression of margatoxin and agitoxin-2 in Pichia pastoris: an efficient method for production of KV1.3 channel blockers.,published,journal,PLoS ONE,PloS one,7,12,,,,,,,,,,,,,,,,,,,,,,e52965,e52965,2012, citations,entry_citation,15421,28475,1,,entry citation,,,23300835,,,Recombinant expression of margatoxin and agitoxin-2 in Pichia pastoris: an efficient method for production of KV1.3 channel blockers.,published,journal,PLoS ONE,PloS one,7,12,,,,,,,,,,,,,,,,,,,,,,e52965,e52965,2012, citations,entry_citation,15422,28491,1,,entry citation,,,18458082,,,NMR Analysis of KChIP4a Reveals Structural Basis for Control of Surface Expression of Kv4 Channel Complexes,published,journal,J. Biol. Chem.,,283,27,,,,,,,,,,,,,,,,,,,,,,18937,18946,2008, citations,citation_1,15423,28510,1,,entry citation,,,,,,"Structure, Folding and Stability of FimA",in preparation,journal,J. Mol. Biol.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15424,28525,1,,entry citation,,,19636871,,,"NMR assignment of Cdc42(T35A), an active Switch I mutant of Cdc42",published,journal,Biomol. NMR Assignments,,1,2,,,,,,,,,,,,,,,,,,,,,,225,227,2007, citations,entry_citation,15425,28539,1,,entry citation,,,18458082,,,NMR Analysis of KChIP4a Reveals Structural Basis for Control of Surface Expression of Kv4 Channel Complexes,published,journal,J. Biol. Chem.,,283,27,,,,,,,,,,,,,,,,,,,,,,18937,18946,2008, citations,entry_citation,15426,28558,1,,entry citation,,,17911261,,,Structure of outer membrane protein G by solution NMR spectroscopy.,pbulished,journal,Proc. Natl. Acad. Sci. 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Natl. Acad. Sci. U. S. A.,,105,5,,,,,,,,,,,,,,,,,,,,,,1505,1510,2008, citations,entry_citation,15431,28650,1,,entry citation,,,19636863,,,NMR assignment of the periplasmic oxidoreductase DsbH from Chlamydia,published,journal,Biomol. NMR Assignments,,1,2,,,,,,,,,,,,,,,,,,,,,,195,196,2007, citations,entry_citation,15433,28664,1,,entry citation,,,17927211,,,Solution-state molecular structure of apo and oleate-liganded liver fatty acid-binding protein,published,journal,Biochemistry,,46,44,,,,,,,,,,,,,,,,,,,,,,12543,12556,2007, citations,entry_citation,15434,28691,1,,entry citation,,,17927211,,,Solution-state molecular structure of apo and oleate-liganded liver fatty acid-binding protein,published,journal,Biochemistry,,46,44,,,,,,,,,,,,,,,,,,,,,,12543,12556,2007, citations,entry_citation,15435,28722,1,,entry citation,,,18295795,,,"alpha-RgIA, a Novel Conotoxin That Blocks the alpha9alpha10 nAChR: Structure and Identification of Key Receptor-Binding Residues.",published,journal,J. Mol. Biol.,,377,4,,,,,,,,,,,,,,,,,,,,,,1216,1227,2008, citations,entry_citation,15436,28738,1,,entry citation,,,18295795,,,"alpha-RgIA, a Novel Conotoxin That Blocks the alpha9alpha10 nAChR: Structure and Identification of Key Receptor-Binding Residues.",published,journal,J. Mol. Biol.,,337,4,,,,,,,,,,,,,,,,,,,,,,1216,1227,2008, citations,structure_and_dynamics,15437,28752,1,,reference citation,,,,,,Structure and Dynamics of Proteins from Designed Combinatorial Libraries,in preparation,journal,Protein Sci.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,sequential_assignment,15437,28753,2,,entry citation,,,19636868,,,NMR assignment of S836: a de novo protein from a designed superfamily,published,journal,Biomol. NMR Assignments,,1,2,,,,,,,,,,,,,,,,,,,,,,213,215,2007, citations,entry_citation,15438,28781,1,,entry citation,,,18037438,,,Restriction endonuclease inhibitor IPI* of bacteriophage T4: a novel structure for a dedicated target,published,journal,J. Mol. Biol.,,375,3,,,,,,,,,,,,,,,,,,,,,,720,734,2008, citations,BMC,15439,28796,1,,entry citation,,,18536009,,,"Solution structure of the yeast URN1 splicing factor FF domain: Comparative analysis of charge distributions in FF domain structures-FFs and SURPs, two domains with a similar fold",published,journal,Proteins,,73,4,,,,,,,,,,,,,,,,,,,,,,1001,1009,2008, citations,entry_citation,1544,28815,1,,entry citation,,,,,"Motta, Andrea, Temussi, Piero Andrea, Wuensch, Erich, Boverman, Gunter, ""A 1H NMR Study of Human Calcitonin in Solution,"" Biochemistry 30 (9), 2364-2371 (1991).",A 1H NMR Study of Human Calcitonin in Solution,published,journal,Biochemistry,,30,9,,,,,,,,,,,,,,,,,,,,,,2364,2371,1991, citations,citation_1,15440,28828,1,,entry citation,,,19636864,,,"(1)H, (13)C and (15)N resonance assignments of the C-terminal domain of HasB, a specific TonB like protein, from Serratia marcescens",published,journal,Biomol. NMR Assignments,,1,2,,,,,,,,,,,,,,,,,,,,,,197,199,2007, citations,entry_citation,15441,28843,1,,entry citation,,,17919953,,,Protein Assignments without Peak Lists Using Higher-Order Spectra,published,journal,J. Magn. Reson.,,189,2,,,,,,,,,,,,,,,,,,,,,,173,181,2007, citations,entry_citation,15442,28860,1,,entry citation,,,18066054,,,Multienzyme docking in hybrid megasynthetases,published,journal,Nat. Chem. Biol.,,4,1,,,,,,,,,,,,,,,,,,,,,,75,81,2008, citations,entry_citation,15443,28878,1,,entry citation,,,18846567,,,"Structural Study of Ac-Phe-[Orn-Pro-dCha-Trp-Arg], a Potent C5a Receptor Antagonist, by NMR",published,journal,Biopolymers,,90,6,,,,,,,,,,,,,,,,,,,,,,803,815,2008, citations,citations,15444,28897,1,,entry citation,,,18367475,,,"Structure of the DNA-binding domain of NgTRF1 reveals unique features of plant telomere-binding proteins",published,journal,Nucleic Acids Res.,Nucleic Acids Research,36,8,,,,,,,,,,,,,,,,,,,,,,2739,2755,2008, citations,entry_citation,15445,28919,1,,entry citation,,,18044964,,,Functional implications for a prototypical K-turn binding protein from structural and dynamical studies of 15.5K,published,journal,Biochemistry,,46,51,,,,,,,,,,,,,,,,,,,,,,14979,14986,2007, citations,entry_citation,15446,28944,1,,entry citation,,,19636869,,,"Assignment of (1)H, (13)C, and (15)N resonances of YgiT, a putative DNA interacting protein from E. coli, containing one HTH and two CxxC motifs",published,journal,Biomol. NMR Assignments,,1,2,,,,,,,,,,,,,,,,,,,,,,217,219,2007, citations,entry_citation,15447,28960,1,,entry citation,,,17921136,,,The role of the fibronectin IGD motif in stimulating fibroblast migration,published,journal,J. Biol. Chem.,,282,49,,,,,,,,,,,,,,,,,,,,,,35530,35535,2007, citations,entry_citation,15448,28979,1,,entry citation,,,,,,NMR structural investigations of the ClpS protein from Xanthomonas axonopodis pv citri,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,15449,28995,1,,entry citation,,,17971456,,,A Mammalian Type I fatty acid synthase acyl carrier protein domain does not bind acyl chains,published,journal,J. Biol. Chem.,,283,1,,,,,,,,,,,,,,,,,,,,,,518,528,2008, citations,entry_citation,1545,29012,1,,entry citation,,,,,"Motta, Andrea, Temussi, Piero Andrea, Wuensch, Erich, Boverman, Gunter, ""A 1H NMR Study of Human Calcitonin in Solution,"" Biochemistry 30 (9), 2364-2371 (1991).",A 1H NMR Study of Human Calcitonin in Solution,published,journal,Biochemistry,,30,9,,,,,,,,,,,,,,,,,,,,,,2364,2371,1991, citations,entry_citation,15450,29025,1,,entry citation,,,17884811,,,"The A-Chain of insulin contacts the insert domain of the insulin receptor. Photo-cross-linking and mutagenesis of a diabetes-related crevice.",published,journal,J. Biol. Chem.,,282,48,,,,,,,,,,,,,,,,,,,,,,35337,35349,2007, citations,entry_citation,15451,29048,1,,entry citation,,,18295234,,,Identification and structural characterization of a CBP/p300-binding domain from the ETS family transcription factor GABP alpha,published,journal,J. Mol. Biol.,,377,3,,,,,,,,,,,,,,,,,,,,,,636,646,2008, citations,entry_citation,15452,29077,1,,entry citation,,,19636866,,,"Backbone and sidechain (1)H, (15)N and (13)C assignments of the human G-actin binding protein profilin IIa",published,journal,Biomol. NMR Assignments,,1,2,,,,,,,,,,,,,,,,,,,,,,205,207,2007, citations,FBP28WW2-PPLIPPPP_complex,15453,29094,1,,entry citation,,,17915251,,,Structural characterization of a new binding motif and a novel binding mode in group 2 WW domains,published,journal,J. Mol. Biol.,,373,5,,,,,,,,,,,,,,,,,,,,,,1255,1268,2007, citations,entry_citation,15454,29116,1,,entry citation,,,17884811,,,The A-chain of insulin contacts the insert domain of the insulin receptor. Photo-cross-linking and mutagenesis of a diabetes-related crevice,published,journal,J. Biol. Chem.,,282,48,,,,,,,,,,,,,,,,,,,,,,35337,35349,2007, citations,entry_citation,15455,29141,1,,entry citation,,,17884811,,,The A-chain of insulin contacts the insert domain of the insulin receptor. 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NMR Assignments,,2,1,,,,,,,,,,,,,,,,,,,,,,17,19,2008, citations,entry_citation,15458,29218,1,,entry citation,,,,,,The NMR structure of the F0F1 double domain from the Talin Ferm domain,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15459,29239,1,,entry citation,,,18269247,,,The periplasmic domain of TolR from Haemophilus influenzae forms a dimer with a large hydrophobic groove: NMR solution structure and comparison to SAXS data,published,journal,Biochemistry,,47,10,,,,,,,,,,,,,,,,,,,,,,3131,3142,2008, citations,citation_2,15489,29810,2,,reference citation,,,,,,Isoloation and identification of a Paenibacillus polymyxa Strain that coproduces a novel lantibiotic and polymyxin,published,journal,Applied and Environmental Microbiology,,73,1,,,,,,,,,,,,,,,,,,,,,,168,178,2007, citations,entry_citation,1546,29253,1,,entry citation,,,,,"Motta, Andrea, Temussi, Piero Andrea, Wuensch, Erich, Boverman, Gunter, ""A 1H NMR Study of Human Calcitonin in Solution,"" Biochemistry 30 (9), 2364-2371 (1991).",A 1H NMR Study of Human Calcitonin in Solution,published,journal,Biochemistry,,30,9,,,,,,,,,,,,,,,,,,,,,,2364,2371,1991, citations,entry_citation,15460,29266,1,,entry citation,,,18844294,,,"Lipopolysaccharide bound structures of the active fragments of fowlicidin-1, a cathelicidin family of antimicrobial and antiendotoxic peptide from chicken, determined by transferred nuclear overhauser effect spectroscopy",published,journal,Biopolymers,,92,1,,,,,,,,,,,,,,,,,,,,,,9,22,2009, citations,entry_citation,15461,29280,1,,entry citation,,,17961510,,,Interaction of the two soluble metal-binding domains of yeast Ccc2 with copper(I)-Atx1,published,journal,Biochem. Biophys. Res. Commun.,,364,3,,,,,,,,,,,,,,,,,,,,,,645,649,2007, citations,entry_citation,15462,29297,1,,entry citation,,,,,,Solution NMR Structure of HI0947 from Haemophilus influenzae.,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,15463,29319,1,,entry citation,,,18293934,,,Three-dimensional structure/hydrophobicity of latarcins specifies their mode of membrane activity,published,journal,Biochemistry,,47,11,,,,,,,,,,,,,,,,,,,,,,3525,3533,2008, citations,entry_citation,15464,29337,1,,entry citation,,,18040865,,,Structure of human insulin monomer in water/acetonitrile solution,published,journal,J. Biomol. NMR,,40,1,,,,,,,,,,,,,,,,,,,,,,55,64,2008, citations,citations,15465,29352,1,,entry citation,,,,,,The Solution Structure of Ph1500-N,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,15466,29371,1,,entry citation,,,18503784,,,"Structural characterisation of PinA WW domain and a comparison with other Group IV WW domains, Pin1 and Ess1",published,journal,Biochim. Biophys. Acta,Biochimica et Biophysica Acta,1784,9,,,,,,,,,,,,,,,,,,,,,,1208,1214,2008, citations,entry_citation,15467,29390,1,,entry citation,,,18318536,,,Anionic charge is prioritized over geometry in aluminum and magnesium fluoride transition state analogs of phosphoryl transfer enzymes.,published,journal,J. Am. Chem. Soc.,,130,12,,,,,,,,,,,,,,,,,,,,,,3952,3958,2008, citations,entry_citation,15468,29412,1,,entry citation,,,,,,Solution NMR structure of protein NE1242 from N. europaea. Northeast Structural Genomics Target NeT4,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15469,29433,1,,entry citation,,,19636862,,,NMR assignment of the domain 513-651 from the SARS-CoV nonstructural protein nsp3,published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,1,2,,,,,,,,,,,,,,,,,,,,,,191,194,2007, citations,citation1,15470,29451,1,,entry citation,,,20013162,,,"(1)H, (13)C and (15)N resonance assignments of the Calmodulin-Munc13-1 peptide complex.",published,journal,Biomol. NMR assignments,Biomolecular NMR assignments,4,1,,,,,,,,,,,,,,,,,,,,,,45,48,2009, citations,entry_citation,15471,29479,1,,entry citation,,,18247350,,,NMR structure of the peptidyl-tRNA hydrolase domain from Pseudomonas syringae expands the structural coverage of the hydrolysis domains of class 1 peptide chain release factors,published,journal,Proteins,,71,2,,,,,,,,,,,,,,,,,,,,,,1027,1031,2008, citations,entry_citation,15473,29502,1,,entry citation,,,19636913,,,"1H, 15N, 13C resonance assignment of folded and 8 M urea-denatured state of SUMO from Drosophila melanogaster",published,journal,Biomol. NMR Assignments,,2,1,,,,,,,,,,,,,,,,,,,,,,13,15,2008, citations,entry_citation,15474,29517,1,,entry citation,,,19053416,,,Extensive formation of off-pathway species during folding of an alpha-beta parallel protein is due to docking of (non)native structure elements in unfolded molecules,published,journal,J. Am. Chem. Soc.,,130,50,,,,,,,,,,,,,,,,,,,,,,16914,16920,2008, citations,entry_citation,15475,29534,1,,entry citation,,,18696230,,,Solution Structure of the Soluble Domain of the NfeD Protein YuaF from Bacillus subtilis,published,journal,J. Biomol. NMR,,42,1,,,,,,,,,,,,,,,,,,,,,,69,76,2008, citations,entry_citation,15476,29553,1,,entry citation,,,18431750,,,Solution NMR structure of the SOS response protein YnzC from Bacillus subtilis,published,journal,Proteins,,72,1,,,,,,,,,,,,,,,,,,,,,,526,530,2008, citations,entry_citation,15477,29581,1,,entry citation,,,19771161,,,"Solution structure and phylogenetics of Prod1, a member of the three-finger protein superfamily implicated in salamander limb regeneration.",published,journal,PLoS One,,4,9,,,,,,,,,,,,,,,,,,,,,,7123,,2009, citations,entry_citation,15478,29602,1,,entry citation,,,18498106,,,The NMR solution structure of the artificial protein M7 matches the computationally designed model,published,journal,Proteins,,72,3,,,,,,,,,,,,,,,,,,,,,,1104,1107,2008, citations,citation_1,15478,29603,2,,reference citation,,,,,,A tetrapeptide fragment-based design method results in highly stable artificial proteins,published,journal,Proteins,,68,4,,,,,,,,,,,,,,,,,,,,,,839,849,2007, citations,entry_citation,15479,29622,1,,entry citation,,,18035040,,,Structural characterization of the transmembrane and cytoplasmic domains of human CD4.,published,journal,Biochim. Biophys. Acta,,1768,12,,,,,,,,,,,,,,,,,,,,,,2949,2960,2007, citations,entry_citation,15480,29637,1,,entry citation,,,18395224,,,"The controlling roles of Trp60 and Trp95 in beta2-microglobulin function, folding and amyloid aggregation properties",published,journal,J. Mol. Biol.,,378,4,,,,,,,,,,,,,,,,,,,,,,885,895,2008, citations,entry_citation,15481,29651,1,,entry citation,,,,,,15N and 1HN assignments of the EVH1 domain of human HOMER3A,in preparation,journal,Biomol. NMR Assignments,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15482,29669,1,,entry citation,,,,,,Solution NMR Structure of R. sphaeroides protein RHOS4_26430: Northeast Structural Genomics Consortium Target RhR95,in preparation,journal,Proteins: Struct. Funct. Genet.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15483,29711,1,,entry citation,,,20538608,,,Solution Structure of the Squash Aspartic Acid Proteinase Inhibitor (SQAPI) and Mutational Analysis of Pepsin Inhibition.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,285,35,,,,,,,,,,,,,,,,,,,,,,27019,27025,2010, citations,citation_1,15485,29727,1,,entry citation,,,17936301,,,Improved segmental isotope labeling methods for the NMR study of multidomain or large proteins: application to the RRMs of Npl3p and hnRNP L.,published,journal,J. Mol. Biol.,,375,1,,,,,,,,,,,,,,,,,,,,,,151,164,2008, citations,entry_citation,15486,29747,1,,entry citation,,,18001134,,,The high-precision solution structure of Yersinia modulating protein YmoA provides insight into interaction with H-NS,published,journal,Biochemistry,,46,49,,,,,,,,,,,,,,,,,,,,,,13975,13982,2007, citations,citation_1,15487,29766,1,,entry citation,,,17936301,,,Improved segmental isotope labeling methods for the NMR study of multidomain or large proteins: application to the RRMs of Npl3p and hnRNP L,published,journal,J. Mol. Biol.,,375,1,,,,,,,,,,,,,,,,,,,,,,151,164,2008, citations,citation_1,15488,29787,1,,entry citation,,,19636920,,,Backbone NMR resonance assignment of the Abelson kinase domain in complex with imatinib,published,journal,Biomol. NMR Assignments,,2,1,,,,,,,,,,,,,,,,,,,,,,41,42,2008, citations,citiation_1,15489,29809,1,,entry citation,,,18625234,,,"N-terminal acetylation in paenibacillin, a novel lantibiotic",published,journal,FEBS Lett.,FEBS Letters,582,18,,,,,,,,,,,,,,,,,,,,,,2787,2792,2008, citations,citation_1,19247,102231,1,,entry citation,,,,,,Dynamics between plastocyanin and tetralysine peptides,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15490,29833,1,,entry citation,,,19500594,,,"Two structurally independent domains of E. coli NusG create regulatory plasticity via distinct interactions with RNA polymerase and regulators.",published,journal,J. Mol. Biol.,Journal of molecular biology,391,2,,,,,,,,,,,,,,,,,,,,,,341,358,2009, citations,entry_citation,15491,29849,1,,entry citation,,,,,,Solution NMR structure of uncharacterized protein Q5E7H1 from Vibrio fischeri. Northeast Structural Genomics target VfR117.,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15492,29875,1,,entry citation,,,19636875,,,Backbone chemical shift assignment of a glutamate receptor ligand binding domain in complexes with five partial agonists,published,journal,Biomol. NMR Assignments,,1,2,,,,,,,,,,,,,,,,,,,,,,241,243,2007, citations,entry_citation,15493,29892,1,,entry citation,,,19636875,,,Backbone chemical shift assignment of a glutamate receptor ligand binding domain in complexes with five partial agonists,published,journal,Biomol. NMR Assignments,,1,2,,,,,,,,,,,,,,,,,,,,,,241,243,2007, citations,entry_citation,15494,29909,1,,entry citation,,,19636875,,,Backbone chemical shift assignment of a glutamate receptor ligand binding domain in complexes with five partial agonists,published,journal,Biomol. NMR Assignments,,1,2,,,,,,,,,,,,,,,,,,,,,,241,243,2007, citations,entry_citation,15495,29926,1,,entry citation,,,19636875,,,Backbone chemical shift assignment of a glutamate receptor ligand binding domain in complexes with five partial agonists,published,journal,Biomol. NMR Assignments,,1,2,,,,,,,,,,,,,,,,,,,,,,241,243,2007, citations,entry_citation,15496,29943,1,,entry citation,,,19636875,,,Backbone chemical shift assignment of a glutamate receptor ligand binding domain in complexes with five partial agonists,published,journal,Biomol. NMR Assignments,,1,2,,,,,,,,,,,,,,,,,,,,,,241,243,2007, citations,citation_1,15497,29960,1,,entry citation,,,18940609,,,"Structural characterization of the type-III pilot-secretin complex from Shigella flexneri",published,journal,Structure,,16,10,,,,,,,,,,,,,,,,,,,,,,1544,1554,2008, citations,entry_citation,15498,29976,1,,entry citation,,,19636915,,,"1H, 13C and 15N resonance assignments for the human E2 conjugating enzyme, UbcH7",published,journal,Biomol. NMR Assignments,,2,1,,,,,,,,,,,,,,,,,,,,,,21,23,2008, citations,entry_citation,15499,29991,1,,entry citation,,,18313693,,,Solution Structure of NEMO Zinc Finger and Impact of an Anhidrotic Ectodermal Dysplasia with Immunodeficiency-related Point Mutation,published,journal,J. Mol. Biol.,,377,5,,,,,,,,,,,,,,,,,,,,,,1419,1432,2008, citations,entry_citation,15500,30010,1,,entry citation,,,18313693,,,Solution Structure of NEMO Zinc Finger and Impact of an Anhidrotic Ectodermal Dysplasia with Immunodeficiency-related Point Mutation,published,journal,J. Mol. Biol.,,377,5,,,,,,,,,,,,,,,,,,,,,,1419,1432,2008, citations,entry_citation,15501,30029,1,,entry citation,,,,,,Backbone Assignment of human Proliferating Cell Nuclear Antigen,published,journal,Biomol. NMR Assignments,,1,2,,,,,,,,,,,,,,,,,,,,,,245,247,2007, citations,entry_citation,15502,30049,1,,entry citation,,,17988686,,,Mapping intramolecular interactions between domains in HMGB1 using a tail-truncation approach,published,journal,J. Mol. Biol.,,374,5,,,,,,,,,,,,,,,,,,,,,,1286,1297,2007, citations,entry_citation,15503,30064,1,,entry citation,,,18940609,,,"Structural characterization of the type-III pilot-secretin complex from Shigella flexneri",published,journal,Structure,,16,10,,,,,,,,,,,,,,,,,,,,,,1544,1554,2008, citations,entry_citation,15504,30079,1,,entry citation,,,18940609,,,"Structural characterization of the type-III pilot-secretin complex from Shigella flexneri",published,journal,Structure,,16,10,,,,,,,,,,,,,,,,,,,,,,1544,1554,2008, citations,entry_citation,15505,30096,1,,entry citation,,,17855358,,,Structural and functional characterization of the interaction between cyclophilin B and a heparin-derived oligosaccharide.,published,journal,J. Biol. Chem.,,282,47,,,,,,,,,,,,,,,,,,,,,,34148,34158,2007, citations,entry_citation,15506,30114,1,,entry citation,,,18573254,,,Self-recognition by an intrinsically disordered protein.,published,journal,FEBS Lett.,,582,17,,,,,,,,,,,,,,,,,,,,,,2673,2677,2008, citations,entry_citation,15507,30128,1,,entry citation,,,18366641,,,Solution structure of the Legionella pneumophila Mip-rapamycin complex,published,journal,BMC Struct. Biol.,,8,17,,,,,,,,,,,,,,,,,,,,,,,,2008, citations,entry_citation,15508,30148,1,,entry citation,,,10913250,,,Restricted motion of the lipoyl-lysine swinging arm in the pyruvate dehydrogenase complex of Escherichia coli,published,journal,Biochemistry,,39,29,,,,,,,,,,,,,,,,,,,,,,8448,8459,2000, citations,entry_citation,15509,30162,1,,entry citation,,,,,,NMR Solution Structure of PARC CPH Domain,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1551,30178,1,,entry citation,,,,,"Pochapsky, Thomas C., Ye, Xiao Mei, ""1H NMR Identification of a B-Sheet Structure and Description of Folding Topology in Putidaredoxin,"" Biochemistry 30, 3850-3856 (1991).","1H NMR Identification of a B-Sheet Structure and Description of Folding Topology in Putidaredoxin",published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,3850,3856,1991, citations,entry_citation,15510,30191,1,,entry citation,,,18955169,,,Interaction between the N-terminal SH3 domain of Nckalpha and CD3varepsilon-derived peptides: Non-canonical and canonical recognition motifs.,published,journal,Biochim. Biophys. Acta,,1794,1,,,,,,,,,,,,,,,,,,,,,,110,117,2009, citations,entry_citation,15511,30217,1,,entry citation,,,18561946,,,Solution Structure of the C-terminal Dimerization Domain of SARS Coronavirus Nucleocapsid Protein Solved by the SAIL-NMR Method,published,journal,J. Mol. Biol.,,380,4,,,,,,,,,,,,,,,,,,,,,,608,622,2008, citations,entry_citation,15512,30233,1,,entry citation,,,19636923,,,"1H, 15N, and 13C NMR chemical shift assignments for the Ig3 domain of palladin",published,journal,Biomol. NMR Assignments,,2,1,,,,,,,,,,,,,,,,,,,,,,51,53,2008, citations,entry_citation,15513,30248,1,,entry citation,,,18186541,,,Structural consequences of phosphorylation of two serine residues in the cytoplasmic domain of HIV-1 VpU,published,journal,J. Pept. Sci.,,14,7,,,,,,,,,,,,,,,,,,,,,,804,810,2008, citations,entry_citation,15514,30263,1,,entry citation,,,19636873,,,"Assignment of backbone (1)H, (13)C and (15)N resonances of human IgG1 Fc (51.4 kDa)",published,journal,Biomol. NMR Assignments,,1,2,,,,,,,,,,,,,,,,,,,,,,233,235,2007, citations,citations,15515,30278,1,,entry citation,,,17945184,,,NMR structural studies of the antibiotic lipopeptide daptomycin in DHPC micelles,published,journal,Biochim. Biophys. Acta,,1768,12,VIER,0005-2736,,,,,,,,,,,,,,,,,,,,3116,3126,2007, citations,citation_1,15517,30302,1,,entry citation,,,18218708,,,Solution structure of Ca2+-free rat alpha-parvalbumin,published,journal,Protein Sci.,,17,3,,,,,,,,,,,,,,,,,,,,,,431,438,2008, citations,citation_1,15518,30319,1,,entry citation,,,17980149,,,Effect of Heterodimer Partner RXRalpha on PPARgamma Activation Function-2 Helix in Solution,published,journal,Biochem. Biophys. Res. Commun.,,365,1,,,,,,,,,,,,,,,,,,,,,,42,46,2008, citations,opn_citation,15519,30336,1,,entry citation,,,19636917,,,"Backbone assignment of osteopontin, a cytokine and cell attachment protein implicated in tumorigenesis.",published,journal,Biomol. 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NMR Assignments,,2,1,,,,,,,,,,,,,,,,,,,,,,5,7,2008, citations,entry_citation,15532,30593,1,,entry citation,,,17716689,,,Structure of the Wilms' Tumor Suppressor Protein Zinc Finger Domain Bound to DNA,published,journal,J. Mol. Biol.,,372,5,,,,,,,,,,,,,,,,,,,,,,1227,1245,2007, citations,entry_citation,15533,30611,1,,entry citation,,,17716689,,,Structure of the Wilms Tumor Suppressor Protein Zinc Finger Domain Bound to DNA,published,journal,J. Mol. Biol.,,372,5,,,,,,,,,,,,,,,,,,,,,,1227,1245,2007, citations,citations,15534,30631,1,,entry citation,,,18596201,,,Differential Ubiquitin Binding of the UBA Domains from Human c-Cbl and Cbl-b: NMR Structural and Biochemical Insights,published,journal,Protein Sci.,,17,10,,,,,,,,,,,,,,,,,,,,,,1805,1814,2008, citations,entry_citation,15535,30647,1,,entry citation,,,18796611,,,NMR structures of two designed proteins with high sequence identity but different fold and function,published,journal,Proc. Natl. Acad. Sci. 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NMR Assignments,,2,1,,,,,,,,,,,,,,,,,,,,,,25,28,2008, citations,entry_citation,15540,30742,1,,entry citation,,,19636919,,,"1H, 13C and 15N resonance assignments of the C-terminal domain of the 43 kDa subunit of the chloroplast signal recognition particle",published,journal,Biomol. 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Biophys. Res. Commun.,Biochemical and Biophysical Research Communications,369,3,,,,,,,,,,,,,,,,,,,,,,853,857,2008, citations,entry_citation,15545,30850,1,,entry citation,,,19636918,,,NMR assignment of the N-terminal TRAF-like RING zinc finger domain of human FLN29,published,journal,Biomol. 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Biol.,,375,2,,,,,,,,,,,,,,,,,,,,,,487,498,2007, citations,entry_citation,15549,30926,1,,entry citation,,,,,,Solution Structure of Human C6orf115 protein,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15550,30944,1,,entry citation,,,,,,"1H, 13C, and 15N resonance assignments of hPCIF1 WW domain",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15551,30963,1,,entry citation,,,18156175,,,"An integrin phosphorylation switch: the effect of beta3 integrin tail phosphorylation on DOK1 and talin binding.",published,journal,J. Biol. Chem.,,283,9,,,,,,,,,,,,,,,,,,,,,,5420,5426,2008, citations,entry_citation,15552,30977,1,,entry citation,,,18156175,,,An integrin phosphorylation switch: the effect of beta3 integrin tail phosphorylation on DOK1 and talin binding,published,journal,J. Biol. Chem.,,283,9,,,,,,,,,,,,,,,,,,,,,,5420,5426,2008, citations,entry_citation,15553,30997,1,,entry citation,,,18547526,,,Solution structure and sugar-binding mechanism of mouse latrophilin-1 RBL: a 7TM receptor-attached lectin-like domain,published,journal,Structure,,16,6,,,,,,,,,,,,,,,,,,,,,,944,953,2008, citations,Citation_bmrb,15554,31018,1,,entry citation,,,19636924,,,"1H, 13C, and 15N chemical shift assignments for the Eps15-EH2-stonin 2 complex",published,journal,Biomol. 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Biol.,Journal of molecular biology,391,1,,,,,,,,,,,,,,,,,,,,,,136,148,2009, citations,entry_citation,15564,31192,1,,entry citation,,,18273680,,,GFT projection NMR based resonance assignment of membrane proteins: application to subunit C of E. coli F(1)F (0) ATP synthase in LPPG micelles,published,journal,J. Biomol. NMR,,40,3,,,,,,,,,,,,,,,,,,,,,,157,163,2008, citations,entry_citation,15565,31208,1,,entry citation,,,19674102,,,Conformational stability of neuroglobin helix F--possible effects on the folding pathway within the globin family,published,journal,FEBS J.,,276,18,,,,,,,,,,,,,,,,,,,,,,5177,5190,2009, citations,citations,15566,31234,1,,entry citation,,,18585102,,,A comparison of BRCT domains involved in nonhomologous end-joining: Introducing the solution structure of the BRCT domain of polymerase lambda,published,journal,DNA Repair (Amst).,,7,8,,,,,,,,,,,,,,,,,,,,,,1340,1351,2008, citations,Citation_1,15567,31255,1,,entry citation,,,19446522,,,Autoinhibitory interactions between the PDZ2 and C-terminal domains in the scaffolding protein NHERF-1,published,journal,Structure,Structure,17,5,,0969-2126,,,,,,,,,,,,,,,,,,,,660,669,2009, citations,entry_citation,15568,31274,1,,entry citation,,,,,,Solution NMR Structure of Uncharacterized Lipoprotein B from Nitrosomona europaea. 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J.,The Open Magnetic Resonance Journal,1,,,,,,,,,,,,,,,,,,,,,,,16,28,2008, citations,entry_citation,15595,31802,1,,entry citation,,,,,,A Novel solution NMR structure of protein yst0336 from Saccharomyces cerevisiae/North Structural Genomics Consortium Target YT51/Ontario Center for Structural Proteomics Target yst0336,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,Citation_1,15596,31826,1,,entry citation,,,18086840,,,"Human macrophage inflammatory protein 3alpha: protein and peptide nuclear magnetic resonance solution structures, dimerization, dynamics, and anti-infective properties",published,journal,Antimicrob. Agents Chemother.,,52,3,,,,,,,,,,,,,,,,,,,,,,883,894,2008, citations,entry_citation,15597,31845,1,,entry citation,,,19636927,,,"1H, 13C, and 15N assignment of the oxidized and reduced forms of T. brucei glutathione peroxidase-type tryparedoxin peroxidase",published,journal,Biomol. NMR Assignments,,2,1,,,,,,,,,,,,,,,,,,,,,,65,68,2008, citations,entry_citation,15598,31866,1,,entry citation,,,19636927,,,"1H, 13C, and 15N assignment of the oxidized and reduced forms of T. brucei glutathione peroxidase-type tryparedoxin peroxidase""",published,journal,Biomol. NMR Assignments,,2,1,,,,,,,,,,,,,,,,,,,,,,65,68,2008, citations,entry_citation,15599,31886,1,,entry citation,,,18991813,,,Solution structure and catalytic mechanism of human protein histidine phosphatase 1.,published,journal,Biochemistry,,418,2,,,,,,,,,,,,,,,,,,,,,,337,344,2008, citations,entry_citation,15601,31901,1,,entry citation,,,19636880,,,"1H, 15N, and 13C Chemical shift assignments of the navel orange worm pheromone-binding protein-1 (Atra-PBP1)",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,2,2,,,,,,,,,,,,,,,,,,,,,,105,106,2008, citations,entry_citation,15602,31915,1,,entry citation,,,18452307,,,Domain C of Human Poly(ADP-ribose) Polymerase-1 is Important for Enzyme Activity and Contains a Novel Zinc-ribbon Motif,published,journal,Biochemistry,,47,21,,,,,,,,,,,,,,,,,,,,,,5804,5813,2008, citations,entry_citation,15603,31931,1,,entry citation,,,18715016,,,Solution NMR Structure of the NlpC/P60 Domain of Lipoprotein Spr from Escherichia coli: Structural Evidence for a Novel Cysteine Peptidase Catalytic Triad,published,journal,Biochemistry,,47,37,,,,,,,,,,,,,,,,,,,,,,9715,9717,2008, citations,entry_citation,15604,31981,1,,entry citation,,,,,,Solution NMR structure of Ssl0352 protein from Synechocystis sp.,in preparation,journal,Proteins: Struct. Funct. 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NMR,,30,3,,,,,,,,,,,,,,,,,,,,,,357,358,2004, citations,entry_citation,15609,32090,1,,entry citation,,,,,,solution structure of 50S ribosomal protein L28 from Thermotoga maritima: Northeast Structural Genomics consortium target VR97,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15610,32110,1,,entry citation,,,,,,Solution NMR Structure of BH09830 from Bartonella henselae Modeled with One Zn+2 Bound.,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,EwR120_protein_citation,15611,32146,1,,entry citation,,,,,,Solution NMR structure of Nitrite reductase [NAD(P)H] small subunit from Erwinia carotovora,in preparation,journal,J. Biomol. NMR,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15612,32176,1,,entry citation,,,18184587,,,"Extended polypeptide linkers establish the spatial architecture of a pyruvate dehydrogenase multienzyme complex",published,journal,Structure,,16,1,,,,,,,,,,,,,,,,,,,,,,93,103,2008, citations,entry_citation1,15613,32190,1,,entry citation,,,17397227,,,"Parallel Synthesis of a Novel C2-Aryl Pyrrolo[2,1-c][1,4]benzodiazepine (PBD) Library",published,journal,J. Comb. 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NMR Assignments,,2,1,,,,,,,,,,,,,,,,,,,,,,85,87,2008, citations,manuscript,15628,32458,1,,entry citation,,,19309529,,,Solution structure of the parvulin-type PPIase domain of Staphylococcus aureus PrsA--implications for the catalytic mechanism of parvulins.,published,journal,BMC Struct. 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Signal.,Science Signaling,1,37,,,,,,,,,,,,,,,,,,,,,,ra4,ra4,2008, citations,entry_citation,15634,32550,1,,entry citation,,,22580893,,,NMR structure note: the ferrous iron transport protein C (FeoC) from Klebsiella pneumoniae,published,journal,J. Biomol. NMR,,53,2,,,,,,,,,,,,,,,,,,,,,,161,165,2012, citations,citations,15635,32565,1,,entry citation,,,18799424,,,Structural basis of CXCR4 sulfotyrosine recognition by the chemokine SDF-1/CXCL12,published,journal,Sci. Signal.,Science Signaling,1,37,,,,,,,,,,,,,,,,,,,,,,ra4,ra4,2008, citations,citations,15636,32588,1,,entry citation,,,18799424,,,Structural basis of CXCR4 sulfotyrosine recognition by the chemokine SDF-1/CXCL12,published,journal,Sci. Signal.,Science Signaling,1,37,,,,,,,,,,,,,,,,,,,,,,ra4,ra4,2008, citations,citations,15637,32610,1,,entry citation,,,18799424,,,Structural basis of CXCR4 sulfotyrosine recognition by the chemokine SDF-1/CXCL12,published,journal,Sci. Signal.,Science Signaling,1,37,,,,,,,,,,,,,,,,,,,,,,ra4,ra4,2008, citations,citations,15638,32633,1,,entry citation,,,19636922,,,"1H, 15N and 13C backbone resonance assignment of Rv1567c, an integral membrane protein from Mycobacterium tuberculosis",published,journal,Biomol. NMR Assignments,,2,1,,,,,,,,,,,,,,,,,,,,,,47,49,2008, citations,entry_citation,15639,32651,1,,entry citation,,,18361918,,,A circular loop of the sixteen-residue repeating unit in ice nucleation protein,published,journal,Biochem. Biophys. Res. Commun.,,371,1,,,,,,,,,,,,,,,,,,,,,,5,9,2008, citations,entry_citation,15640,32668,1,,entry citation,,,18361918,,,A circular loop of the sixteen-residue repeating unit in ice nucleation protein,published,journal,Biochem. Biophys. Res. Commun.,,371,1,,,,,,,,,,,,,,,,,,,,,,5,9,2008, citations,entry_citation,15641,32685,1,,entry citation,,,18361918,,,A circular loop of the sixteen-residue repeating unit in ice nucleation protein,published,journal,Biochem. Biophys. Res. Commun.,,371,1,,,,,,,,,,,,,,,,,,,,,,5,9,2008, citations,entry_citation,15642,32700,1,,entry citation,,,19500594,,,"Two structurally independent domains of E. coli NusG create regulatory plasticity via distinct interactions with RNA polymerase and regulators.",published,journal,J. Mol. Biol.,Journal of molecular biology,391,2,,,,,,,,,,,,,,,,,,,,,,341,358,2009, citations,citation_1,15643,32716,1,,entry citation,,,19636932,,,Backbone assignments of the 34 kDa ketopantoate reductase from E. coli,published,journal,Biomol. NMR Assignments,,2,1,,,,,,,,,,,,,,,,,,,,,,93,96,2008, citations,entry_citation,15644,32731,1,,entry citation,,,18621724,,,Solution structure of the U2 snRNP protein Rds3p reveals a knotted zinc-finger motif,published,journal,Proc. Natl. Acad. Sci. U. S. A.,,105,28,,,,,,,,,,,,,,,,,,,,,,9621,9626,2008, citations,entry_citation,15645,32753,1,,entry citation,,,19651139,,,Amino acid insertion reveals a necessary three-helical intermediate in the folding pathway of the colicin E7 immunity protein Im7.,published,journal,J. Mol. Biol.,Journal of molecular biology,392,4,,,,,,,,,,,,,,,,,,,,,,1074,1086,2009, citations,entry_citation,15646,32778,1,,entry citation,,,18458823,,,NMR analysis of the closed conformation of syntaxin-1,published,journal,J. Biomol. NMR,,41,1,,,,,,,,,,,,,,,,,,,,,,43,54,2008, citations,gH626-644_peptide,15647,32796,1,,entry citation,,,18678872,,,Analysis of a membrane interacting region of herpes simplex virus type 1 glycoprotein H,published,journal,J. Biol. Chem.,The Journal of Biological Chemistry,283,44,,,,,,,,,,,,,,,,,,,,,,29993,30009,2008, citations,R642S__gH626-644_peptide,15648,32810,1,,entry citation,,,18678872,,,Analysis of a membrane interacting region of herpes simplex virus type 1 glycoprotein H,published,journal,J. Biol. Chem.,The Journal of Biological Chemistry,283,44,,,,,,,,,,,,,,,,,,,,,,29993,30009,2008, citations,L627S__gH626-644_peptide,15649,32825,1,,entry citation,,,18678872,,,Analysis of a membrane interacting region of herpes simplex virus type 1 glycoprotein H,published,journal,J. Biol. Chem.,The Journal of Biological Chemistry,283,44,,,,,,,,,,,,,,,,,,,,,,29993,30009,2008, citations,entry_citation,15650,32840,1,,entry citation,,,19317469,,,Accurate solution structures of proteins from X-ray data and a minimal set of NMR data: calmodulin-peptide complexes as examples,published,journal,J. Am. Chem. Soc.,,131,14,,,,,,,,,,,,,,,,,,,,,,5134,5144,2009, citations,entry_citation,15651,32862,1,,entry citation,,,18952100,,,"Solution State NMR Structure and Dynamics of KpOmpA, a 210 Residue Transmembrane Domain Possessing a High Potential for Immunological Applications",published,journal,J. Mol. Biol.,,385,1,,,,,,,,,,,,,,,,,,,,,,117,130,2009, citations,entry_citation,15652,32884,1,,entry citation,,,,,,Solution NMR structure of the uncharacterized protein from Rhodospirillum rubrum gene locus Rru_A0810. Northeast Structural Genomics Target RrR43.,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15653,32926,1,,entry citation,,,19636928,,,"Backbone 1H, 13C, and 15N NMR assignments of the tail domain of vinculin",published,journal,Biomol. NMR Assignments,,2,1,,,,,,,,,,,,,,,,,,,,,,69,71,2008, citations,entry_citation,15654,32948,1,,entry citation,,,19056307,,,Insulin-like growth factor-I (IGF-I): Solution properties and NMR chemical shift assignments near physiological pH.,published,journal,Growth Horm. IGF Res.,,19,3,,,,,,,,,,,,,,,,,,,,,,226,231,2009, citations,entry_citation,15655,32963,1,,entry citation,,,18533181,,,"Molecular structure and metal-binding properties of the periplasmic CopK protein expressed in Cupriavidus metallidurans CH34 during copper challenge",published,journal,J. Mol. Biol.,,380,2,,,,,,,,,,,,,,,,,,,,,,386,403,2008, citations,reference_1,15655,32964,2,,reference citation,,,16735739,,,Transcriptomic and proteomic analyses of the pMOL30-encoded copper resistance in Cupriavidus metallidurans strain CH3,published,journal,Microbiology,,152,,,,,,,,,,,,,,,,,,,,,,,1765,,, citations,entry_citation,15656,32996,1,,entry citation,,,19636894,,,"1H, 13C and 15N NMR assignments of Duck HBV apical stem loop of the epsilon encapsidation signal",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,2,2,,,,,,,,,,,,,,,,,,,,,,159,162,2008, citations,entry_citation,15658,33022,1,,entry citation,,,18770515,,,An ACP Structural Switch: Conformational Differences between the Apo and Holo Forms of the Actinorhodin Polyketide Synthase Acyl Carrier Protein,published,journal,ChemBioChem,,9,15,,,,,,,,,,,,,,,,,,,,,,2424,2432,2008, citations,entry_citation,15659,33038,1,,entry citation,,,18770515,,,An ACP Structural Switch: Conformational Differences between the Apo and Holo Forms of the Actinorhodin Polyketide Synthase Acyl Carrier Protein,published,journal,ChemBioChem,,9,15,,,,,,,,,,,,,,,,,,,,,,2424,2432,2008, citations,entry_citation,1566,33052,1,,entry citation,,,,,"Falzone, Christopher J., Wright, Peter E., Benkovic, Stephen J., ""Evidence for Two Interconverting Protein Isomers in the Methotrexate Complex of Dihydrofolate Reductase from Escherichia coli,"" Biochemistry 30, 2184-2191 (1991).","Evidence for Two Interconverting Protein Isomers in the Methotrexate Complex of Dihydrofolate Reductase from Escherichia coli",published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,2184,2191,1991, citations,entry_citation,15660,33065,1,,entry citation,,,20212144,,,Structural characterization of the Z RING-eIF4E complex reveals a distinct mode of control for eIF4E,published,journal,Proc. Natl. Acad. Sci. U. S. A.,,107,12,,,,,,,,,,,,,,,,,,,,,,5441,5446,2010, citations,entry_citation_2,15660,33066,2,,reference citation,,,18958179,,,NMR assignment of the arenaviral protein Z from Lassa fever virus,published,journal,Biomol. NMR Assignments,,2,1,,,,,,,,,,,,,,,,,,,,,,81,84,2008, citations,entry_citation,15661,33085,1,,entry citation,,,,,,"Solution NMR structure of protein hp1203 from helicobacter pyloric 26695/Northeast Structure Genomics Consortium (NESG) target PT1/Ontario Center for Structural Proteomics target hp1203",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15662,33109,1,,entry citation,,,19081741,,,"1H, 13C, and 15N resonance assignments of murine amelogenin, an essential enamel biomineralization protein",published,journal,Biomol. NMR Assignments,,2,1,,,,,,,,,,,,,,,,,,,,,,89,91,2008, citations,citation_1,15663,33135,1,,entry citation,,,19636930,,,"Sequence specific 1H, 13C and 15N resonance assignments of a calmodulin-like calcium-binding protein from the protozoan parasite Entamoeba histolytica (EhCaM)",published,journal,Biomol. NMR Assignments,,2,1,,,,,,,,,,,,,,,,,,,,,,77,79,2008, citations,citation_1,15664,33154,1,,entry citation,,,19138386,,,Evolution of prokaryotic SPFH proteins.,published,journal,BMC Evol. Biol.,BMC evolutionary biology,9,,,,,,,,,,,,,,,,,,,,,,,10,10,2009, citations,entry_citation,15665,33173,1,,entry citation,,,18387372,,,"Conformational analysis of the broad-spectrum antibacterial peptide, ranatuerin-2CSa: Identification of a full length helix-turn-helix motif.",published,journal,Biochim. Biophys. Acta,,1784,6,,,,,,,,,,,,,,,,,,,,,,924,929,2008, citations,entry_citation,15666,33191,1,,entry citation,,,19651139,,,Amino acid insertion reveals a necessary three-helical intermediate in the folding pathway of the colicin E7 immunity protein Im7.,published,journal,J. Mol. Biol.,Journal of molecular biology,392,4,,,,,,,,,,,,,,,,,,,,,,1074,1086,2009, citations,entry_citation,15667,33207,1,,entry citation,,,18844294,,,"Lipopolysaccharide bound structures of the active fragments of fowlicidin-1, a cathelicidin family of antimicrobial and antiendotoxic peptide from chicken, determined by transferred nuclear overhauser effect spectroscopy",published,journal,Biopolymers,,92,1,,,,,,,,,,,,,,,,,,,,,,9,22,2009, citations,entry_citation,15669,33221,1,,entry citation,,,19636878,,,"Sequence-specific 1H, 13C, and 15N resonance assignments of the GRP1 PH domain",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,2,2,,,,,,,,,,,,,,,,,,,,,,97,99,2008, citations,entry_citation,1567,33237,1,,entry citation,,,,,"Falzone, Christopher J., Wright, Peter E., Benkovic, Stephen J., ""Evidence for Two Interconverting Protein Isomers in the Methotrexate Complex of Dihydrofolate Reductase from Escherichia coli,"" Biochemistry 30, 2184-2191 (1991).","Evidence for Two Interconverting Protein Isomers in the Methotrexate Complex of Dihydrofolate Reductase from Escherichia coli",published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,2184,2191,1991, citations,entry_citation,15670,33250,1,,entry citation,,,18682226,,,Structural Insight into the Recognition of the H3K4me3 Mark by the TFIID Subunit TAF3,published,journal,Structure,Structure,16,8,,,,,,,,,,,,,,,,,,,,,,1245,1256,2008, citations,entry_citation,15671,33272,1,,entry citation,,,18682226,,,Structural Insight into the Recognition of the H3K4me3 Mark by the TFIID Subunit TAF3,published,journal,Structure,Structure,16,8,,,,,,,,,,,,,,,,,,,,,,1245,1256,2008, citations,entry_citation,15672,33296,1,,entry citation,,,18382677,,,The p12 domain is unstructured in a murine leukemia virus p12-CA(N) Gag construct,published,journal,PLoS. ONE.,,3,4,,,,,,,,,,,,,,,,,,,,,,1902,1902,2008, citations,citation_1,15673,33311,1,,entry citation,,,18500825,,,"Nuclear magnetic resonance solution structure of PisI, a group B immunity protein that provides protection against the type IIa bacteriocin piscicolin 126, PisA.",published,journal,Biochemistry,,47,24,,,,,,,,,,,,,,,,,,,,,,6427,6436,2008, citations,entry_citation,15674,33331,1,,entry citation,,,,,,Solution NMR structure of the chromobox protein homolog 7,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,15676,33349,1,,entry citation,,,,,,Null,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15677,33363,1,,entry citation,,,18948596,,,NMR studies of a channel protein without membranes: structure and dynamics of water-solubilized KcsA,published,journal,Proc. Natl. Acad. Sci. U. S. A.,,105,43,,,,,,,,,,,,,,,,,,,,,,16537,16542,2008, citations,entry_citation,15678,33384,1,,entry citation,,,20589905,,,Three-dimensional structure of the weakly associated protein homodimer SeR13 using RDCs and paramagnetic surface mapping.,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,19,9,,,,,,,,,,,,,,,,,,,,,,1673,1685,2010, citations,entry_citation,15679,33405,1,,entry citation,,,21297165,,,Structure and interactions of myosin-binding protein C domain C0: cardiac-specific regulation of myosin at its neck?,published,journal,J. Biol. Chem.,The Journal of biological chemistry,286,14,,,,,,,,,,,,,,,,,,,,,,12650,12658,2011, citations,Citation_1,15680,33424,1,,entry citation,,,19636879,,,"Sequence-specific 1H, 13C and 15N backbone resonance assignments of the 34 kDa catalytic domain of human PTPN7",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,2,2,,,,,,,,,,,,,,,,,,,,,,101,103,2008, citations,entry_citation,15681,33442,1,,entry citation,,,19636883,,,"NMR assignment of PN2-3, a tubulin interaction subdomain of the CPAP protein",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,2,2,,,,,,,,,,,,,,,,,,,,,,115,117,2008, citations,entry_citation,15682,33456,1,,entry citation,,,19636901,,,Complete NMR assignments for the second EGF domain of MIC6 from Toxoplasma gondii and re-assignment in complex with the galectin-like domain of MIC1,published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,2,2,,,,,,,,,,,,,,,,,,,,,,187,189,2008, citations,entry_citation,15683,33470,1,,entry citation,,,,,,Solution NMR Structure of the folded C-terminal fragment of YiaD from Escherichia coli. Northeast Structural Genomics Consortium Target ER553.,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15684,33517,1,,entry citation,,,19636955,,,"Backbone and side-chain 1H, 13C, 15N resonance assignments of rat lipocalin2",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,3,1,,,,,,,,,,,,,,,,,,,,,,95,97,2009, citations,entry_citation,15685,33532,1,,entry citation,,,19636901,,,Complete NMR assignments for the second EGF domain of MIC6 from Toxoplasma gondii and re-assignment in complex with the galectin-like domain of MIC1,published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,2,2,,,,,,,,,,,,,,,,,,,,,,187,189,2008, citations,entry_citation,15687,33551,1,,entry citation,,,,,,The Automated Suite for Protein Structure Determination by NMR Spectroscopy,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15688,33566,1,,entry citation,,,,,,The Automated Suite for Protein Structure by NMR Spectroscopy,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15689,33580,1,,entry citation,,,,,,The Automated Suite for Protein Structure by NMR Spectroscopy,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,15690,33594,1,,entry citation,,,19453293,,,Copper(I)-mediated protein-protein interactions result from suboptimal interaction surfaces.,published,journal,Biochem. J.,The Biochemical journal,422,1,,,,,,,,,,,,,,,,,,,,,,37,42,2009, citations,citation_1,15691,33624,1,,entry citation,,,18501926,,,Structural mechanism of transcriptional autorepression of the Escherichia coli RelB/RelE antitoxin/toxin module,published,journal,J. Mol. Biol.,,380,1,,,,,,,,,,,,,,,,,,,,,,107,119,2008, citations,entry_citation,15692,33643,1,,entry citation,,,19636898,,,Complete resonance assignment of the galectin-like domain of MIC1 from Toxoplasma gondii in complex with the second EGF domain from MIC6 and the backbone assignment in complex with the third EGF domain,published,journal,Biomol. NMR Assignments,,2,2,,,,,,,,,,,,,,,,,,,,,,175,177,2008, citations,citation_1,15693,33659,1,,entry citation,,,18829450,,,The solution structure of DNA-free Pax-8 Paired Box domain accounts for redox regulation of transcriptional activity in Pax protein family,published,journal,J. Biol. Chem.,,283,48,,,,,,,,,,,,,,,,,,,,,,33321,33328,2008, citations,entry_citation,15694,33681,1,,entry citation,,,19636884,,,"Complete resonance assignment of the first and second apple domains of MIC4 from Toxoplasma gondii, using a new NMRView-based assignment aid",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,2,2,,,,,,,,,,,,,,,,,,,,,,119,121,2008, citations,entry_citation,15695,33695,1,,entry citation,,,,,,Solution NMR structure of the chromobox protein homolog 4,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15697,33716,1,,entry citation,,,,,,"Mutational and Structural Analysis of Stem-loop IIId of the Hepatitis C Virus and GB Virus B Internal Ribosome Entry Sites",in preparation,journal,J. Virology,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15698,33731,1,,entry citation,,,20104876,,,Solution structure of the Apo C-terminal domain of the Lethocerus F1 troponin C isoform.,published,journal,Biochemistry,Biochemistry,49,8,,,,,,,,,,,,,,,,,,,,,,1719,1726,2010, citations,entry_citation,15700,33751,1,,entry citation,,,19043414,,,Molecular basis of Pirh2-mediated p53 ubiquitylation,published,journal,Nat. Struct. Mol. Biol.,,15,12,,,,,,,,,,,,,,,,,,,,,,1334,1342,2008, citations,entry_citation,15701,33778,1,,entry citation,,,19043414,,,Molecular basis of Pirh2-mediated p53 ubiquitylation,published,journal,Nat. Struct. Mol. Biol.,,15,12,,,,,,,,,,,,,,,,,,,,,,1334,1342,2008, citations,citation_1,15702,33806,1,,entry citation,,,,,,Solution structure of Bordatella pertussis protein BP2786,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation,15703,33829,1,,entry citation,,,18959746,,,"Soluble recombinant CD69 receptors optimized to have an exceptional physical and chemical stability display prolonged circulation and remain intact in the blood of mice",published,journal,FEBS J.,,275,22,,,,,,,,,,,,,,,,,,,,,,5589,5606,2008, citations,entry_citation,15704,33850,1,,entry citation,,,18650434,,,S100A1 and calmodulin compete for the same binding site on ryanodine receptor,published,journal,J. Biol. Chem.,The Journal of Biological Chemistry,,283,39,,,,,,,,,,,,,,,,,,,,,26676,26683,2008, citations,entry_citation,15705,33868,1,,entry citation,,,18413860,,,Structure determination of a Galectin-3-carbohydrate complex using paramagnetism-based NMR constraints,published,journal,Protein Sci.,,17,7,,,,,,,,,,,,,,,,,,,,,,1220,1231,2008, citations,entry_citation,15706,33887,1,,entry citation,,,19636887,,,Backbone NMR assignments of DFP-inhibited mature subtilisin E,published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,2,2,,,,,,,,,,,,,,,,,,,,,,131,133,2008, citations,citations,15707,33909,1,,entry citation,,,18728011,,,rac regulates its effector phospholipase Cgamma2 through interaction with a split pleckstrin homology domain,published,journal,J. Biol. 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U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,106,43,,,,,,,,,,,,,,,,,,,,,,18273,18278,2009, citations,entry_citation,15712,33992,1,,entry citation,,,19828437,,,Transient structural distortion of metal-free Cu/Zn superoxide dismutase triggers aberrant oligomerization.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,106,43,,,,,,,,,,,,,,,,,,,,,,18273,18278,2009, citations,entry_citation,15713,34007,1,,entry citation,,,19828437,,,Transient structural distortion of metal-free Cu/Zn superoxide dismutase triggers aberrant oligomerization.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,106,43,,,,,,,,,,,,,,,,,,,,,,18273,18278,2009, citations,entry_citation,15714,34022,1,,entry citation,,,19828437,,,Transient structural distortion of metal-free Cu/Zn superoxide dismutase triggers aberrant oligomerization.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,106,43,,,,,,,,,,,,,,,,,,,,,,18273,18278,2009, citations,entry_citation,15715,34037,1,,entry citation,,,19636904,,,"1H, 15N and 13C NMR assignments of mouse methionine sulfoxide reductase B2",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,2,2,,,,,,,,,,,,,,,,,,,,,,199,201,2008, citations,entry_citation,15716,34057,1,,entry citation,,,19636885,,,"1H, 15N, 13C resonance assignment of the AlgE6R1 subunit from the Azotobacter vinelandii mannuronan C5-epimerase",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,2,2,,,,,,,,,,,,,,,,,,,,,,123,125,2008, citations,citations,15717,34076,1,,entry citation,,,18762196,,,SOLUTION STRUCTURE OF A CYANOBACTERIAL PHYTOCHROME GAF DOMAIN IN THE RED LIGHT-ABSORBING GROUND STATE,published,journal,J. Mol. Biol.,,383,2,,,,,,,,,,,,,,,,,,,,,,403,413,2008, citations,Entry_Citation,15718,34108,1,,entry citation,,,18495154,,,Solution structure of the inner DysF domain of myoferlin and implications for limb girdle muscular dystrophy type 2b,published,journal,J. Mol. Biol.,,379,5,,,,,,,,,,,,,,,,,,,,,,981,990,2008, citations,reference_1,15719,34129,1,,entry citation,,,21463585,,,The calponin regulatory region is intrinsically unstructured: novel insight into actin-calponin and calmodulin-calponin interfaces using NMR spectroscopy.,published,journal,Biophys. J.,Biophysical journal,100,7,,,,,,,,,,,,,,,,,,,,,,1718,1728,2011, citations,citations,15720,34145,1,,entry citation,,,19326460,,,Structures of two Arabidopsis thaliana major latex proteins represent novel helix-grip folds,published,journal,Proteins,,76,1,,,,,,,,,,,,,,,,,,,,,,237,243,2009, citations,entry_citation,15721,34168,1,,entry citation,,,,,,Solution structure of protein Atu1203 from Agrobacterium tumefaciens,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15722,34190,1,,entry citation,,,19636886,,,"1H, 13C and 15N resonance assignments of Ca2+ bound collagen-binding domain derived from a clostridial collagenase",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,2,2,,,,,,,,,,,,,,,,,,,,,,127,129,2008, citations,entry_citation,15723,34209,1,,entry citation,,,19636888,,,NMR assignment of the nonstructural protein nsp3(1066-1181) from SARS-CoV,published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,2,2,,,,,,,,,,,,,,,,,,,,,,135,138,2008, citations,entry_citation,15724,34227,1,,entry citation,,,,,,Self-consistent 3J coupling analysis for the joint calibration of Karplus coefficients and evaluation of torsion angles,published,journal,J. Biomol. NMR,,14,1,,,,,,,,,,,,,,,,,,,,,,1,12,1999, citations,Billeter_et_al_1992,15724,34228,2,,reference citation,,,1392569,,,"Precise vicinal coupling constants 3JHNa in proteins from nonlinear fits of J-modulated [15N,1H]-COSY-experiments",published,journal,J. Biomol. NMR,,2,,,,,,,,,,,,,,,,,,,,,,,257,274,1992, citations,Kuboniwa_et_al_1994,15724,34229,3,,reference citation,,,7812158,,,"Measurement of HN,Ha J-couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods",published,journal,J. Biomol. 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Reson.,,102,,,,,,,,,,,,,,,,,,,,,,,228,231,1993, citations,Grzesiek_et_al_1995,15725,34260,5,,reference citation,,,,,,Multiple-quantum line narrowing for measurement of Ha-Hb J couplings in isotopically enriched proteins,published,journal,J. Am. Chem. Soc.,,117,,,,,,,,,,,,,,,,,,,,,,,5312,5315,1995, citations,Hu_&_Bax_1996,15725,34261,6,,reference citation,,,,,,Measurement of three-bond 13C-13C J couplings between carbonyl and carbonyl/carboxyl carbons in isotopically enriched proteins,published,journal,J. Am. Chem. Soc.,,118,,,,,,,,,,,,,,,,,,,,,,,8170,8171,1996, citations,Schmidt_et_al_1996,15725,34262,7,,reference citation,,,8616270,,,"Heteronuclear relayed E.COSY applied to the determination of accurate 3J(HN,C') and 3J(H beta,C') coupling constants in Desulfovibrio vulgaris flavodoxin",published,journal,J. Biomol. NMR,,7,2,,,,,,,,,,,,,,,,,,,,,,142,152,1996, citations,Hu_&_Bax_1997a,15725,34263,8,,reference citation,,,9204558,,,Chi1 angle information from a simple two-dimensional NMR experiment that identifies trans 3JNCg couplings in isotopically enriched proteins,published,journal,J. Biomol. NMR,,9,,,,,,,,,,,,,,,,,,,,,,,323,328,1997, citations,Hu_&_Bax_1997b,15725,34264,9,,reference citation,,,,,,Determination of phi and chi1 angles in proteins from 13C-13C three-bond J couplings measured by three-dimensional heteronuclear NMR. How planar is the peptide bond?,published,journal,J. Am. Chem. Soc.,,119,,,,,,,,,,,,,,,,,,,,,,,6360,6368,1997, citations,Konrat_et_al_1997,15725,34265,10,,reference citation,,,9255945,,,"Pulse schemes for the measurement of 3JC'C gamma and 3JNC gamma scalar couplings in 15N,13C uniformly labeled proteins",published,journal,J. Biomol. NMR,,9,,,,,,,,,,,,,,,,,,,,,,,409,422,1997, citations,Pervushin_et_al_1997,15725,34266,11,,reference citation,,,9356455,,,Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,94,,,,,,,,,,,,,,,,,,,,,,,12366,12371,1997, citations,Cordier_&_Grzesiek_1999,15725,34267,12,,reference citation,,,,,,Direct observation of hydrogen bonds in proteins by interresidue 3hJNC scalar couplings,published,journal,J. Am. Chem. Soc.,,121,,,,,,,,,,,,,,,,,,,,,,,1601,1602,1999, citations,Cornilescu_et_al_1999,15725,34268,13,,reference citation,,,,,,Identification of the hydrogen bonding network in a protein by scalar couplings,published,journal,J. Am. Chem. Soc.,,121,,,,,,,,,,,,,,,,,,,,,,,2949,2950,1999, citations,Lohr_et_al_1999a,15725,34269,14,,reference citation,,,,,,"Simultaneous measurement of 3JHN,Ha and 3JHa,Hb coupling constants in 13C,15N-labeled proteins",published,journal,J. Am. Chem. Soc.,,121,,,,,,,,,,,,,,,,,,,,,,,11821,11826,1999, citations,Lohr_et_al_1999b,15725,34270,15,,reference citation,,,,,,Recording heteronuclear quantitative J-correlation spectra with internal reference peaks,published,journal,Bull. Magn. Reson.,,20,,,,,,,,,,,,,,,,,,,,,,,9,14,1999, citations,Yang_et_al_1999,15725,34271,16,,reference citation,,,,,,"TROSY-based HNCO pulse sequence for the measurement of 1HN-15N, 15N-13CO, 1HN-13CO, 13CO-13Ca and 1HN-13Ca dipolar couplings in 15N, 13C, 2H-labeled proteins",published,journal,J. Biomol. NMR,,14,,,,,,,,,,,,,,,,,,,,,,,333,343,1999, citations,Lohr_et_al_2000,15725,34272,17,,reference citation,,,11061224,,,"Heteronuclear relayed E.COSY revisited: determination of 3J(H(alpha),C(gamma)) couplings in Asx and aromatic residues in proteins",published,journal,J. Biomol. NMR,,18,1,,,,,,,,,,,,,,,,,,,,,,13,22,2000, citations,Lohr_&_Ruterjans_2000,15725,34273,18,,reference citation,,,10968965,,,"Efficient measurement of (3)J(N,Cgamma) and (3)J(C',Cgamma) coupling constants of aromatic residues in (13)C, (15)N-labeled proteins",published,journal,J. Magn. Reson.,,146,1,,,,,,,,,,,,,,,,,,,,,,126,131,2000, citations,La_NTD_apo_and_with_U4,15726,34296,1,,entry citation,,,19636881,,,NMR assignment of the N-terminal region of human La free and in complex with RNA,published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,2,2,,,,,,,,,,,,,,,,,,,,,,107,109,2008, citations,La_NTD_apo_and_with_U4,15727,34317,1,,entry citation,,,19636881,,,NMR assignment of the N-terminal region of human La free and in complex with RNA,published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,2,2,,,,,,,,,,,,,,,,,,,,,,107,109,2008, citations,entry_citation,15728,34339,1,,entry citation,,,18728013,,,Spatial structure and pH-dependent conformational diversity of dimeric transmembrane domain of the receptor tyrosine kinase EphA1,published,journal,J. Biol. Chem.,,283,43,,,,,,,,,,,,,,,,,,,,,,29385,29395,2008, citations,entry_citation,15729,34365,1,,entry citation,,,18558717,,,The NMR structure and dynamics of the two-domain tick carboxypeptidase inhibitor reveal flexibility in its free form and stiffness upon binding to human carboxypeptidase B,published,journal,Biochemistry,,47,27,,,,,,,,,,,,,,,,,,,,,,7066,7078,2008, citations,entry_citation,1573,34381,1,,entry citation,,,,,"Wu, Jia-zhen, La Mar, Gerd N., Yu, Liping P., Lee, Kang-Bong, Walker, F. Ann, Chiu, Mark L., Sligar, Stephen G., ""1H NMR Study of the Solution Molecular and Electronic Structure of Escherichia coli Ferricytochrome b562: Evidence for S = 1/2 <=> S = 5/2 Spin Equilibrium for Intact His/Met Ligation,"" Biochemistry 30 (8), 2156-2165 (1991).","1H NMR Study of the Solution Molecular and Electronic Structure of Escherichia coli Ferricytochrome b562: Evidence for S = 1/2 <=> S = 5/2 Spin Equilibrium for Intact His/Met Ligation",published,journal,Biochemistry,,30,8,,,,,,,,,,,,,,,,,,,,,,2156,2165,1991, citations,entry_citation,15784,35418,1,,entry citation,,,18929573,,,Structural basis of the role of the NikA ribbon-helix-helix domain in initiating bacterial conjugation.,published,journal,J. Mol. Biol.,,384,3,,,,,,,,,,,,,,,,,,,,,,690,701,2008, citations,entry_citation,15730,34394,1,,entry citation,,,18558717,,,The NMR structure and dynamics of the two-domain tick carboxypeptidase inhibitor reveal flexibility in its free form and stiffness upon binding to human carboxypeptidase B,published,journal,Biochemistry,,47,27,,,,,,,,,,,,,,,,,,,,,,7066,7078,2008, citations,entry_citation,15731,34410,1,,entry citation,,,18558717,,,The NMR structure and dynamics of the two-domain tick carboxypeptidase inhibitor reveal flexibility in its free form and stiffness upon binding to human carboxypeptidase B,in preparation,journal,Biochemistry,,47,27,,,,,,,,,,,,,,,,,,,,,,7066,7078,2008, citations,citation_1,15732,34426,1,,entry citation,,,19636953,,,"1H, 13C, 15N backbone and side-chain resonance assignments of the Bright/ARID domain from the human histone demethylase JARID1B",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,3,1,,,,,,,,,,,,,,,,,,,,,,85,87,2009, citations,citations,15733,34440,1,,entry citation,,,22052904,,,Solution structure and molecular interactions of lamin B receptor Tudor domain,published,journal,J. Biol. Chem.,,287,2,,,,,,,,,,,,,,,,,,,,,,1032,1042,2012, citations,entry_citation,15734,34456,1,,entry citation,,,18534985,,,"Solution Structure of the cGMP Binding GAF Domain from Phosphodiesterase 5: INSIGHTS INTO NUCLEOTIDE SPECIFICITY, DIMERIZATION, AND cGMP-DEPENDENT CONFORMATIONAL CHANGE",published,journal,J. Biol. Chem.,,283,33,,,,,,,,,,,,,,,,,,,,,,22749,22759,2008, citations,entry_citation,15735,34486,1,,entry citation,,,19154179,,,NMR structure determination of a segmentally labeled glycoprotein using in vitro glycosylation,published,journal,J. Am. Chem. Soc.,,131,3,,,,,,,,,,,,,,,,,,,,,,1274,1281,2009, citations,entry_citation,15736,34508,1,,entry citation,,,,,,"1H, C13, 15N Resonace assignments for full-length human frataxin",in preparation,journal,J. Biomol. NMR,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15737,34522,1,,entry citation,,,19154179,,,NMR structure determination of a segmentally labeled glycoprotein using in vitro glycosylation,published,journal,J. Am. Chem. Soc.,,131,3,,,,,,,,,,,,,,,,,,,,,,1274,1281,2009, citations,entry_citation,15738,34547,1,,entry citation,,,,,,Structural Characterization and DNA Binding Sequence Selection of the CsrA Protein from Helicobacter pylori,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15739,34563,1,,entry citation,,,19019828,,,Hydramacin-1: Structure and antibacterial activity of a protein from the basal metazoan hydra,published,journal,J. Biol. Chem.,The Journal of biological chemistry,284,3,,,,,,,,,,,,,,,,,,,,,,1896,1905,2009, citations,entry_citation,1574,34578,1,,entry citation,,,,,"Lecomte, Juliette T.J., Kaplan, David, Llinas, M., Thunberg, Eva, Samuelsson, Gunnar, ""Proton magnetic resonance characterization of phoratoxins and homologous proteins related to crambin,"" Biochemistry 26, 1187-1194 (1987).","Proton magnetic resonance characterization of phoratoxins and homologous proteins related to crambin",published,journal,Biochemistry,,26,,,,,,,,,,,,,,,,,,,,,,,1187,1194,1987, citations,entry_citation,15740,34591,1,,entry citation,,,18845156,,,Poxvirus K7 protein adopts a Bcl-2 fold: Biochemical mapping of its interactions with human DEAD box RNA helicase DDX3,published,journal,J. Mol. Biol.,,385,3,,,,,,,,,,,,,,,,,,,,,,843,853,2009, citations,entry_citation,15741,34615,1,,entry citation,,,19636909,,,"1H, 15N and 13C resonance assignment of imidazole glycerol phosphate (IGP) synthase protein HisF from Thermotoga maritima",published,journal,Biomol. NMR Assignments,,2,2,,,,,,,,,,,,,,,,,,,,,,219,221,2008, citations,entry_citation,15742,34629,1,,entry citation,,,18652828,,,The three-dimensional structure of CsmA: A small antenna protein from the green sulfur bacterium Chlorobium tepidum,published,journal,FEBS Lett.,,582,19,,,,,,,,,,,,,,,,,,,,,,2869,2874,2008, citations,citation_1,15743,34646,1,,entry citation,,,19636892,,,"Sequence specific 1H, 13C, and 15N resonance assignments of Hahellin from Hahella chejuensis, a putative member of the betagamma-crystallin superfamily",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,2,2,,,,,,,,,,,,,,,,,,,,,,151,153,2008, citations,entry_citation,15744,34664,1,,entry citation,,,19636906,,,A complete backbone spectral assignment of lipid-free human apolipoprotein E (apoE),published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,2,2,,,,,,,,,,,,,,,,,,,,,,207,210,2008, citations,entry_citation,15745,34678,1,,entry citation,,,18263618,,,"Solution structure of stem-loop alpha of the hepatitis B virus post-transcriptional regulatory element",published,journal,Nucleic Acids Research,,36,5,,,,,,,,,,,,,,,,,,,,,,1681,1689,2008, citations,entry_citation,15746,34698,1,,entry citation,,,,,,Solution structure of a domain of a type three secretion system secretory protein BPP 3783 from Bordetella pertusis,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15747,34716,1,,entry citation,,,18508767,,,Structural and Functional Characterization of TM IX of the NHE1 Isoform of the Na+/H+ Exchanger,published,journal,J. Biol. Chem.,,283,32,,,,,,,,,,,,,,,,,,,,,,22018,22030,2008, citations,JACS_Article,15748,34735,1,,entry citation,,,19784965,,,"Engineering a beta-Helical d,l-Peptide for Folding in Polar Media",published,journal,Chemistry,,15,44,,,,,,,,,,,,,,,,,,,,,,11867,11877,2009, citations,JACS_Article,15749,34753,1,,entry citation,,,19784965,,,"Engineering a beta-Helical d,l-Peptide for Folding in Polar Media",published,journal,Chemistry,,15,44,,,,,,,,,,,,,,,,,,,,,,11867,11877,2009, citations,entry_citation,1575,34771,1,,entry citation,,,,,"Lecomte, Juliette T.J., Kaplan, David, Llinas, M., Thunberg, Eva, Samuelsson, Gunnar, ""Proton magnetic resonance characterization of phoratoxins and homologous proteins related to crambin,"" Biochemistry 26, 1187-1194 (1987).","Proton magnetic resonance characterization of phoratoxins and homologous proteins related to crambin",published,journal,Biochemistry,,26,,,,,,,,,,,,,,,,,,,,,,,1187,1194,1987, citations,entry_citation,15750,34784,1,,entry citation,,,,,,Solution NMR structure of the folded 79 residue fragment of Lin0334 from Listeria innocua. Northeast Structural Genomics Consortium target LkR15.,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15751,34812,1,,entry citation,,,18930922,,,"Synthesis, structure and activities of an oral mucosal alpha-defensin from rhesus macaque",published,journal,J. Biol. Chem.,,283,51,,,,,,,,,,,,,,,,,,,,,,35869,35877,2008, citations,entry_citation,15752,34827,1,,entry citation,,,18003615,,,Structure of a glycosylphosphatidylinositol-anchored domain from a trypanosome variant surface glycoprotein,published,journal,J. Biol. Chem.,,283,6,,,,,,,,,,,,,,,,,,,,,,3584,3593,2008, citations,entry_citation,15753,34843,1,,entry citation,,,18003615,,,Structure of a glycosylphosphatidylinositol-anchored domain from a trypanosome variant surface glycoprotein,published,journal,J. Biol. Chem.,,283,6,,,,,,,,,,,,,,,,,,,,,,3584,3593,2008, citations,entry_citation,15755,34859,1,,entry citation,,,19857500,,,"Structure, dynamics and thermodynamics of the human centrin 2/hSfi1 complex.",published,journal,J. Mol. Biol.,Journal of molecular biology,395,1,,,,,,,,,,,,,,,,,,,,,,191,204,2010, citations,entry_citation,15756,34879,1,,entry citation,,,19366708,,,Motogenic sites in human fibronectin are masked by long range interactions,published,journal,J. Biol. Chem.,,284,23,,,,,,,,,,,,,,,,,,,,,,15668,15675,2009, citations,entry_citation,16149,42504,1,,entry citation,,,19538999,,,Three-dimensional structure of the two-peptide bacteriocin plantaricin JK,published,journal,Peptides,,30,9,,,,,,,,,,,,,,,,,,,,,,1613,1621,2009, citations,entry_citation,15757,34895,1,,entry citation,,,19189375,,,"The (1)H, (13)C, (15)N resonance assignment, solution structure, and residue level stability of eosinophil cationic protein/RNase 3 determined by NMR spectroscopy.",published,journal,Biopolymers,Biopolymers,91,12,,,,,,,,,,,,,,,,,,,,,,1018,1028,2009, citations,entry_citation,15758,34911,1,,entry citation,,,19366708,,,Motogenic sites in human fibronectin are masked by long range interactions,published,journal,J. Biol. Chem.,,284,23,,,,,,,,,,,,,,,,,,,,,,15668,15675,2009, citations,entry_citation,15759,34927,1,,entry citation,,,19366708,,,Motogenic sites in human fibronectin are masked by long range interactions,published,journal,J. Biol. Chem.,,284,23,,,,,,,,,,,,,,,,,,,,,,15668,15675,2009, citations,entry_citation,1576,34943,1,,entry citation,,,,,"Lecomte, Juliette T.J., Kaplan, David, Llinas, M., Thunberg, Eva, Samuelsson, Gunnar, ""Proton magnetic resonance characterization of phoratoxins and homologous proteins related to crambin,"" Biochemistry 26, 1187-1194 (1987).","Proton magnetic resonance characterization of phoratoxins and homologous proteins related to crambin",published,journal,Biochemistry,,26,,,,,,,,,,,,,,,,,,,,,,,1187,1194,1987, citations,entry_citation,15760,34956,1,,entry citation,,,18508764,,,"The structure of alpha-parvin CH2-paxillin LD1 complex reveals a novel modular recognition for focal adhesion assembly",published,journal,J. Biol. Chem.,,283,30,,,,,,,,,,,,,,,,,,,,,,21113,21119,2008, citations,entry_citation,15761,34971,1,,entry citation,,,18623065,,,Structure of HP0564 from Helicobacter pylori identifies it as a new transcriptional regulator,published,journal,Proteins,,73,1,,,,,,,,,,,,,,,,,,,,,,265,268,2008, citations,entry_citation,15762,34992,1,,entry citation,,,,,,NMR STRUCTURE OF PROTEIN YIIS FROM SHIGELLA FLEXNERI: NORTHEAST STRUCTURAL GENOMICS TARGET SFR90,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,15763,35015,1,,entry citation,,,19182799,,,MIA40 is an oxidoreductase that catalyzes oxidative protein folding in mitochondria,published,journal,Nat. Struct. Mol. Biol.,,16,2,,,,,,,,,,,,,,,,,,,,,,198,206,2009, citations,entry_citation,15764,35039,1,,entry citation,,,18280495,,,Structure and Dynamics of Ca2+-Binding Domain 1 of the Na+/Ca2+ Exchanger in the Presence and in the Absence of Ca2+,published,journal,J. Mol. Biol.,,377,3,,,,,,,,,,,,,,,,,,,,,,945,955,2008, citations,entry_citation,15765,35053,1,,entry citation,,,18950243,,,The Solution Structure of a Tetraheme Cytochrome from Shewanella frigidimarina Reveals a Novel Family Structural Motif,published,journal,Biochemistry,,47,46,,,,,,,,,,,,,,,,,,,,,,11973,11980,2008, citations,entry_citation,15766,35078,1,,entry citation,,,18537264,,,"Local Structural Preferences of Calpastatin, the Intrinsically Unstructured Protein Inhibitor of Calpain",published,journal,Biochemistry,,47,26,,,,,,,,,,,,,,,,,,,,,,6936,6945,2008, citations,entry_citation,15767,35094,1,,entry citation,,,18992225,,,Structure and dynamics of the N-terminal half of hepatitis C virus core protein: an intrinsically unstructured protein,published,journal,Biochem. Biophys. Res. Commun.,Biochemical and Biophysical Research Communications,378,1,,,,,,,,,,,,,,,,,,,,,,27,31,2009, citations,entry_citation,15768,35108,1,,entry citation,,,,,,Structure and dynamics of the N-terminal half of hepatitis C virus core protein: an intrinsically unstructured protein,submitted,journal,Biochem. Cell Biol.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15769,35122,1,,entry citation,,,19636891,,,"1H, 13C, and 15N resonance assignment of the ubiquitin-like domain from Dsk2p",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,2,2,,,,,,,,,,,,,,,,,,,,,,147,149,2008, citations,entry_citation,1577,35140,1,,entry citation,,,,,"Lecomte, Juliette T.J., Kaplan, David, Llinas, M., Thunberg, Eva, Samuelsson, Gunnar, ""Proton magnetic resonance characterization of phoratoxins and homologous proteins related to crambin,"" Biochemistry 26, 1187-1194 (1987).","Proton magnetic resonance characterization of phoratoxins and homologous proteins related to crambin",published,journal,Biochemistry,,26,,,,,,,,,,,,,,,,,,,,,,,1187,1194,1987, citations,entry_citation,15770,35153,1,,entry citation,,,19636942,,,"1H, 13C and 15N backbone and side chain resonance assignments of a Myxococcus xanthus anti-repressor with no known sequence homologues",published,journal,Biomol. NMR Assignments,,3,1,,,,,,,,,,,,,,,,,,,,,,37,40,2009, citations,entry_citation,15773,35174,1,,entry citation,,,18652486,,,Analysis of Site-specific Histidine Protonation in Human Prolactin,published,journal,Biochemistry,,47,33,,,,,,,,,,,,,,,,,,,,,,8638,8647,2008, citations,entry_citation,15774,35199,1,,entry citation,,,19177358,,,Backbone structure of a small helical integral membrane protein: A unique structural characterization,published,journal,Protein Sci.,,18,1,,,,,,,,,,,,,,,,,,,,,,134,146,2009, citations,entry_citation,15775,35230,1,,entry citation,,,18702528,,,Structural Studies of the Transmembrane C-Terminal Domain of the Amyloid Precursor Protein (APP): Does APP Function as a Cholesterol Sensor?,published,journal,Biochemistry,,47,36,,,,,,,,,,,,,,,,,,,,,,9428,9446,2008, citations,Pfu_Rpp21,15776,35244,1,,entry citation,,,18922021,,,"Solution structure of Pyrococcus furiosus RPP21, a component of the archaeal RNase P holoenzyme, and interactions with its RPP29 protein partner",published,journal,Biochemistry,,47,45,,,,,,,,,,,,,,,,,,,,,,11704,11710,2008, citations,entry_citation,15777,35266,1,,entry citation,,,19293932,,,Molecular basis of filamin A-FilGAP interaction and its impairment in congenital disorders associated with filamin A mutations,published,journal,PLoS ONE,,4,3,,,,,,,,,,,,,,,,,,,,,,4928,4928,2009, citations,entry_citation,15778,35285,1,,entry citation,,,19251703,,,Structure of the tyrosine-sulfated C5a receptor N-terminus in complex with chemotaxis inhibitory protein of Staphylococcus aureus,published,journal,J. 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Chem.,,284,18,,,,,,,,,,,,,,,,,,,,,,12363,12372,2009, citations,entry_citation,15779,35320,1,,entry citation,,,19603485,,,Crystal structure of ginkbilobin-2 with homology to the extracellular domain of plant cysteine-rich receptor-like kinases,published,journal,Proteins,Proteins,77,1,,,,,,,,,,,,,,,,,,,,,,247,251,2009, citations,entry_citation,1578,35334,1,,entry citation,,,,,"Lecomte, Juliette T.J., Kaplan, David, Llinas, M., Thunberg, Eva, Samuelsson, Gunnar, ""Proton magnetic resonance characterization of phoratoxins and homologous proteins related to crambin,"" Biochemistry 26, 1187-1194 (1987).","Proton magnetic resonance characterization of phoratoxins and homologous proteins related to crambin",published,journal,Biochemistry,,26,,,,,,,,,,,,,,,,,,,,,,,1187,1194,1987, citations,entry_citation,15780,35347,1,,entry citation,,,18399645,,,Bulged adenosine influence on the RNA duplex conformation in solution.,published,journal,Biochemistry,Biochemistry,47,18,,,,,,,,,,,,,,,,,,,,,,5059,5067,2008, citations,entry_citation,15781,35367,1,,entry citation,,,18399645,,,Bulged adenosine influence on the RNA duplex conformation in solution.,published,journal,Biochemistry,Biochemistry,47,18,,,,,,,,,,,,,,,,,,,,,,5059,5067,2008, citations,entry_citation,15782,35387,1,,entry citation,,,19636893,,,NMR assignments of the sylvatic dengue 1 virus envelope protein domain III,published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,2,2,,,,,,,,,,,,,,,,,,,,,,155,157,2008, citations,citations,15783,35402,1,,entry citation,,,19723500,,,A residue-level investigation of the equilibrium unfolding of the C2A domain of synaptotagmin 1.,published,journal,Arch. Biochem. Biophys.,Archives of biochemistry and biophysics,490,2,,,,,,,,,,,,,,,,,,,,,,158,162,2009, citations,citations,15785,35437,1,,entry citation,,,19723500,,,A residue-level investigation of the equilibrium unfolding of the C2A domain of synaptotagmin 1.,published,journal,Arch. Biochem. Biophys.,Archives of biochemistry and biophysics,490,2,,,,,,,,,,,,,,,,,,,,,,158,162,2009, citations,entry_citation,15786,35453,1,,entry citation,,,19636890,,,"1H, 13C and 15N NMR assignments of Duck HBV primer loop of the encapsidation signal epsilon",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,2,2,,,,,,,,,,,,,,,,,,,,,,143,145,2008, citations,entry_citation,15787,35479,1,,entry citation,,,19636947,,,"Backbone assignment of HINT1 protein, a mouse histidine triad nucleotide binding protein",published,journal,Biomol. NMR Assignments,,3,1,,,,,,,,,,,,,,,,,,,,,,57,59,2009, citations,citation_1,15788,35495,1,,entry citation,,,18605699,,,X-ray Crystallographic and Solution State Nuclear Magnetic Resonance Spectroscopic Investigations of NADP(+) Binding to Ferredoxin NADP Reductase from Pseudomonas aeruginosa,published,journal,Biochemistry,,47,31,,,,,,,,,,,,,,,,,,,,,,8080,8093,2008, citations,entry_citation,15789,35515,1,,entry citation,,,18590741,,,New insights into multiple coagulation factor deficiency from the solution structure of human MCFD2,published,journal,J. Mol. Biol.,,381,4,,,,,,,,,,,,,,,,,,,,,,941,955,2008, citations,entry_citation,15790,35537,1,,entry citation,,,18687679,,,NMR STRUCTURE OF THE N-TERMINAL COILED COIL DOMAIN OF THE ANDES HANTAVIRUS NUCLEOCAPSID PROTEIN,published,journal,J. Biol. Chem.,,283,42,,,,,,,,,,,,,,,,,,,,,,28297,28304,2008, citations,citation_1,15791,35556,1,,entry citation,,,TBA,,,Solution NMR Structure of UPF0339 Protein SO3888 from Shewanella Oneidensis.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15792,35583,1,,entry citation,,,18614051,,,Structural basis for the autoinhibition of talin in regulating integrin activation,published,journal,Mol. Cell,,31,1,,,,,,,,,,,,,,,,,,,,,,124,133,2008, citations,entry_citation,15793,35597,1,,entry citation,,,18837698,,,"The copper-responsive repressor CopR of Lactococcus lactis is a 'winged helix' protein",published,journal,Biochem. J.,The Biochemical Journal,,417,2,,,,,,,,,,,,,,,,,,,,,493,499,2009, citations,entry_citation,15795,35618,1,,entry citation,,,19137618,,,Solution structure of the C-terminal domain of multiprotein bridging factor 1 (MBF1) of Trichoderma reesei,published,journal,Proteins,,75,2,,,,,,,,,,,,,,,,,,,,,,518,523,2009, citations,citation_1,15796,35637,1,,entry citation,,,18996392,,,E2-c-Cbl recognition is necessary but not sufficient for ubiquitination activity,published,journal,J. Mol. Biol.,,385,2,,,,,,,,,,,,,,,,,,,,,,507,519,2008, citations,entry_citation,15797,35657,1,,entry citation,,,19636900,,,Reversible conformational switch revealed by the redox structures of Bacillus subtilis thiol peroxidase,published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,2,2,,,,,,,,,,,,,,,,,,,,,,183,186,2008, citations,reference_citation,15797,35658,2,,reference citation,,,18588855,,,Reversible conformational switch revealed by the redox structures of Bacillus subtilis thiol peroxidase,published,journal,Biochem. Biophys. Res. Commun.,,373,3,,,,,,,,,,,,,,,,,,,,,,414,418,2008, citations,entry_citation,15798,35677,1,,entry citation,,,19636900,,,"1H, 13C, and 15N resonance assignments of the reduced and oxidized forms of Bacillus subtilis thiol peroxidase",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,2,2,,,,,,,,,,,,,,,,,,,,,,183,186,2008, citations,reference_citation,15798,35678,2,,reference citation,,,18588855,,,Reversible conformational switch revealed by the redox structures of Bacillus subtilis thiol peroxidase,published,journal,Biochem. Biophys. Res. Commun.,,373,3,,,,,,,,,,,,,,,,,,,,,,414,418,2008, citations,entry_citation,15799,35697,1,,entry citation,,,19254034,,,Structural Studies of HIV-1 Gag p6ct and Its Interaction with Vpr Determined by Solution Nuclear Magnetic Resonance,published,journal,Biochemistry,,48,11,,,,,,,,,,,,,,,,,,,,,,2355,2367,2009, citations,entry_citation,1580,35711,1,,entry citation,,,,,"Stockman, Brian J., Krezel, Andrzej M., Markley, John L., Leonhardt, Karin G., Straus, Neil A., ""Hydrogen-1, Carbon-13, Nitrogen-15 NMR Spectroscopy of Anabaena 7120 Flavodoxin: Assignment of beta-Sheet and Flavin Binding Site Resonances and Analysis of Protein-Flavin Interactions,"" Biochemistry 29 (41), 9600-9609 (1990).","Hydrogen-1, Carbon-13, Nitrogen-15 NMR Spectroscopy of Anabaena 7120 Flavodoxin: Assignment of beta-Sheet and Flavin Binding Site Resonances and Analysis of Protein-Flavin Interactions",published,journal,Biochemistry,,29,41,,,,,,,,,,,,,,,,,,,,,,9600,9609,1990, citations,entry_citation,15800,35724,1,,entry citation,,,19636905,,,"1H, 13C, and 15N backbone and side-chain chemical shift assignments for the 29 kDa human galectin-1 protein dimer",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,2,2,,,,,,,,,,,,,,,,,,,,,,203,205,2008, citations,entry_citation,15801,35741,1,,entry citation,,,19117956,,,Structural analysis of the DNA-binding domain of the Helicobacter pylori response regulator ArsR.,published,journal,J. Biol. Chem.,,284,10,,,,,,,,,,,,,,,,,,,,,,6536,6545,2009, citations,entry_citation,15802,35763,1,,entry citation,,,19636895,,,"1H, 13C, and 15N resonance assignments of a general stress protein GSP13 from Bacillus subtilis",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,2,2,,,,,,,,,,,,,,,,,,,,,,163,165,2008, citations,entry_citation,15803,35781,1,,entry citation,,,19636899,,,"1H, 13C and 15N resonance assignments for the active conformation of the small G proteins RalB in complex with its effector RLIP76",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,2,2,,,,,,,,,,,,,,,,,,,,,,179,182,2008, citations,entry_citation,15804,35801,1,,entry citation,,,,,,"Solution NMR Structure of M. thermoautotrophicum protein MTH_1000, Northeast Structural Genomics Consortium Target TR8",in preparation,journal,Proteins: Struct. Funct. Genet.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15805,35831,1,,entry citation,,,,,,Solution-State NMR Structure of protein PF0246 from Pyrococcus Furiosis,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15806,35851,1,,entry citation,,,18956887,,,NMR Solution Structure of the Neurotrypsin Kringle Domain,published,journal,Biochemistry,Biochemistry,47,47,BICHAW,0006-2960,0033,,,,,,,,,,,,,,,,,,,12290,12298,2008, citations,entry_citation,15807,35871,1,,entry citation,,,19251647,,,"The phage lambda major tail protein structure reveals a common evolution for long-tailed phages and the type VI bacterial secretion system",published,journal,Proc. Natl. Acad. Sci. USA,Proceedings of the National Academy of Science of the United States of America,106,11,,,,,,,,,,,,,,,,,,,,,,4160,4165,2009, citations,entry_citation,15808,35889,1,,entry citation,,,19636903,,,"Assignment of the 1H, 13C and 15N resonances of the calponin homology-2 domain of alpha-actinin-4",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,2,2,,,,,,,,,,,,,,,,,,,,,,195,197,2008, citations,entry_citation,15809,35909,1,,entry citation,,,19141284,,,Structure and Membrane Interaction of Myristoylated ARF1,published,journal,Structure,,17,1,,,,,,,,,,,,,,,,,,,,,,79,87,2009, citations,entry_citation,15837,36616,1,,entry citation,,,,,,"NMR CHEMICAL SHIFT ASSIGNMENTS OF IRON(II) TRANSPORT PROTEIN A FROM CLOSTRIDIUM THERMOCELLUM , NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET VR131",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1581,35934,1,,entry citation,,,,,"Baldisseri, Donna M., Torchia, Dennis A., Poole, Leslie B., Gerlt, John A., ""Deletion of the omega-loop in the Active Site of Staphylococcal Nuclease 2. Effects on Protein Structure and Dynamics,"" Biochemistry 30, 3628-3633 (1991).","Deletion of the omega-loop in the Active Site of Staphylococcal Nuclease 2. Effects on Protein Structure and Dynamics",published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,3628,3633,1991, citations,entry_citation,15810,35947,1,,entry citation,,,,,,Solution structure of uncharacterized protein PA1076 from Pseudomonas aeruginosa.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15811,35972,1,,entry citation,,,,,,Solution structure of 30S ribosomal protein S27A from Thermoplasma acidophilum/Northeast Structural Genomics Consortium Target TaT88/Ontario Center for Structural Proteomics target ta1093,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15812,35997,1,,entry citation,,,,,,NMR Structure of FeoA-like protein from Clostridium acetobutylicum: Northeast Structural Genomics Consortium Target CaR178,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,Entry,15813,36019,1,,entry citation,,,19636937,,,"1H, 15N and 13C assignments of the dimeric ribosome binding domain of trigger factor from Escherichia coli",published,journal,Biomol. NMR Assignments,,3,1,,,,,,,,,,,,,,,,,,,,,,17,20,2009, citations,1P9Y,15813,36020,2,,reference citation,,,14656439,,,Chaperone binding at the ribosomal exit tunnel,published,journal,Structure,,11,12,,,,,,,,,,,,,,,,,,,,,,1547,1556,2003, citations,Entry,15814,36036,1,,entry citation,,,19636940,,,"1H, 15N and 13C assignments of domain 5 of Dictyostelium discoideum gelation factor (ABP-120) in its native and 8M urea-denatured states",published,journal,Biomol. NMR Assignments,,3,1,,,,,,,,,,,,,,,,,,,,,,29,31,2009, citations,entry_citation,15816,36054,1,,entry citation,,,,,,Solution NMR Structure of the IscA-like Protein DsrR Involved in Sulfur Oxidation in Allochromatium vinosum,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15817,36075,1,,entry citation,,,19053456,,,Solid-State NMR on a Type III Antifreeze Protein in the Presence of Ice,published,journal,J. Am. Chem. Soc.,,130,51,,,,,,,,,,,,,,,,,,,,,,17394,17399,2008, citations,entry_citation,15818,36090,1,,entry citation,,,19053456,,,Solid-State NMR on a Type III Antifreeze Protein in the Presence of Ice,published,journal,J. Am. Chem. Soc.,,130,51,,,,,,,,,,,,,,,,,,,,,,17394,17399,2008, citations,entry_citation,15819,36106,1,,entry citation,,,,,,"Solution NMR Structure of the replication Factor A Related Protein from Methanobacterium thermoautotrophicum. Northeast Structural Genomics Target TR91A.",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1582,36155,1,,entry citation,,,,,"Baldisseri, Donna M., Torchia, Dennis A., Poole, Leslie B., Gerlt, John A., ""Deletion of the omega-loop in the Active Site of Staphylococcal Nuclease 2. Effects on Protein Structure and Dynamics,"" Biochemistry 30, 3628-3633 (1991).","Deletion of the omega-loop in the Active Site of Staphylococcal Nuclease 2. Effects on Protein Structure and Dynamics",published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,3628,3633,1991, citations,entry_citation,15820,36168,1,,entry citation,,,19100700,,,Memory T cell RNA rearrangement programmed by heterogeneous nuclear ribonucleoprotein hnRNPLL,published,journal,Immunity,,29,6,,,,,,,,,,,,,,,,,,,,,,863,875,2008, citations,entry_citation,15821,36184,1,,entry citation,,,,,,"Structure of uncharacterized protein MJ1198 from Methanocaldococcus jannaschii. Northeast Structural Genomics Target MjR117B",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15822,36233,1,,entry citation,,,,,,NMR Solution Structure of A3DK08 protein from Clostridium thermocellum: Northeast Structural Genomics Consortium Target CmR9,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15823,36261,1,,entry citation,,,,,,Solution structure of protein ATC0727 from Agrobacterium Tumefaciens.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15824,36284,1,,entry citation,,,18773909,,,NMR Structure of the Bank Vole Prion Protein at 20 degrees C Contains a Structured Loop of Residues 165-171,published,journal,J. Mol. Biol.,,383,2,,,,,,,,,,,,,,,,,,,,,,306,312,2008, citations,entry_citation,15825,36305,1,,entry citation,,,,,,"Solution NMR Structure of Putative Lipoprotein from Pseudomonas syringae Gene Locus PSPTO2350. Northeast Structural Genomics Target PsR76A",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,Entry,15826,36352,1,,entry citation,,,19636949,,,"1H, 15N and 13C assignments of yellow fluorescent protein (YFP) Venus",published,journal,Biomol. NMR Assignments,,3,1,,,,,,,,,,,,,,,,,,,,,,67,72,2009, citations,entry_citation,15827,36375,1,,entry citation,,,19180607,,,Helical hairpin structure of a potent antimicrobial peptide MSI-594 in lipopolysaccharide micelles by NMR spectroscopy,published,journal,Chemistry,,15,9,,,,,,,,,,,,,,,,,,,,,,2036,2040,2009, citations,NMR_structure_of_PF0385,15828,36389,1,,entry citation,,,,,,NMR structure of PF0385,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15829,36407,1,,entry citation,,,,,,SOLUTION NMR STRUCTURE OF SAG0934 from Streptococcus agalactiae. NORTHEAST STRUCTURAL GENOMICS TARGET SaR32[1-108].,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1583,36457,1,,entry citation,,,,,"Baldisseri, Donna M., Torchia, Dennis A., Poole, Leslie B., Gerlt, John A., ""Deletion of the omega-loop in the Active Site of Staphylococcal Nuclease 2. Effects on Protein Structure and Dynamics,"" Biochemistry 30, 3628-3633 (1991).","Deletion of the omega-loop in the Active Site of Staphylococcal Nuclease 2. Effects on Protein Structure and Dynamics",published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,3628,3633,1991, citations,entry_citation,15830,36470,1,,entry citation,,,19125388,,,Properties of the N-terminal domains from Y receptors probed by NMR spectroscopy.,published,journal,J. Pept. Sci.,,15,3,,,,,,,,,,,,,,,,,,,,,,184,191,2009, citations,entry_citation,15831,36487,1,,entry citation,,,19125388,,,Properties of the N-terminal domains from Y receptors probed by NMR spectroscopy.,published,journal,J. Pept. Sci.,,15,3,,,,,,,,,,,,,,,,,,,,,,184,191,2009, citations,entry_citation,15832,36503,1,,entry citation,,,19125388,,,Properties of the N-terminal domains from Y receptors probed by NMR spectroscopy.,published,journal,J. Pept. Sci.,,15,3,,,,,,,,,,,,,,,,,,,,,,184,191,2009, citations,entry_citation,15833,36521,1,,entry citation,,,,,,N.A.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15834,36545,1,,entry citation,,,,,,Solution NMR structure of FeoA protein from Chlorobium tepidum. Northeast Structural Genomics Consortium target CtR121,in preparation,journal,Proteins: Struct. Funct. Genet.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15835,36571,1,,entry citation,,,,,,"Solution NMR structure of protein encoded by gene BPP1335 from Bordetella parapertussis: Northeast Structural Genomics Target BpR195",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15836,36595,1,,entry citation,,,,,,Solution NMR structure of protein encoded by MTH693 from Methanobacterium thermoautotrophicum: Northeast Structural Genomics Consortium target tt824a,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15839,36642,1,,entry citation,,,,,,Solution structure of protein yiiF from Shigella flexneri serotype 5b (strain 8401) . Northeast Structural Genomics Consortium target sft1,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1584,36662,1,,entry citation,,,,,"Baldisseri, Donna M., Torchia, Dennis A., Poole, Leslie B., Gerlt, John A., ""Deletion of the omega-loop in the Active Site of Staphylococcal Nuclease 2. Effects on Protein Structure and Dynamics,"" Biochemistry 30, 3628-3633 (1991).","Deletion of the omega-loop in the Active Site of Staphylococcal Nuclease 2. Effects on Protein Structure and Dynamics",published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,3628,3633,1991, citations,entry_citation,15840,36675,1,,entry citation,,,,,,Solution Structure of RhR2,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15841,36696,1,,entry citation,,,,,,"Solution NMR Structure of Protein FeoA from Clostridium thermocellum, Northeast Structural Genomics Consortium Target CmR17",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15843,36720,1,,entry citation,,,,,,NMR Structure of the Putative Cold Shock Protein from Erwinia carotovora: Northeast Structural Genomics Consortium Target EwR156a,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15844,36747,1,,entry citation,,,,,,NMR Solution Structure of a Thiamine Biosynthesis Protein from Geobacter Metallireducens: Northeast Structural Genomics Consortium Target GmR137,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15845,36786,1,,entry citation,,,18773909,,,NMR Structure of the Bank Vole Prion Protein at 20 degrees C Contains a Structured Loop of Residues 165-171,published,journal,J. Mol. Biol.,,383,2,,,,,,,,,,,,,,,,,,,,,,306,312,2008, citations,entry_citation,15846,36805,1,,entry citation,,,,,,NMR solution Structure of Membrane associated protein from Bacillus cereus: Northeast Structural Genomics Consortium Target: BcR97A,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,15847,36839,1,,entry citation,,,TBA,,,"Solution NMR Structure of XF2673 from Xylella fastidiosa. Northeast Structural Genomics Consortium Target XfR39",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15848,36863,1,,entry citation,,,,,,Solution NMR Structure of Putative N-Acetyl Transferase YhhK from E. coli Bound to Coenzyme A,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15849,36885,1,,entry citation,,,,,,SOLUTION NMR STRUCTURE OF the second OB-fold domain of replication protein A from Methanococcus maripaludis. NORTHEAST STRUCTURAL GENOMICS TARGET MrR110B.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1585,36931,1,,entry citation,,,,,"Kristensen, Soren M., Jorgensen, Anne Marie M., Led, Jens J., Balschmidt, Per, Hansen, Finn B., ""Proton Nuclear Magnetic Resonance Study of the B9(Asp)Mutant of Human Insulin Sequential Assignment and Secondary Structure,"" J. Mol. Biol. 218, 221-231 (1991).","Proton Nuclear Magnetic Resonance Study of the B9(Asp)Mutant of Human Insulin Sequential Assignment and Secondary Structure",published,journal,J. Mol. Biol.,,218,,,,,,,,,,,,,,,,,,,,,,,221,231,1991, citations,entry_citation,15850,36942,1,,entry citation,,,,,,Solution NMR Structure of Putative Lipoprotein from Bacillus cereus Ordered Locus BC_2438. Northeast Structural Genomics Target BcR103A.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,15851,36973,1,,entry citation,,,18854159,,,Structural and Mechanistic Insights into STIM1-Mediated Initiation of Store-Operated Calcium Entry,published,journal,Cell,,135,1,,,,,,,,,,,,,,,,,,,,,,110,122,2008, citations,entry_citation,15852,36997,1,,entry citation,,,19317469,,,Accurate Solution Structures of Proteins from X-ray Data and a Minimal Set of NMR Data: Calmodulin-Peptide Complexes As Examples,published,journal,J. Am. Chem. Soc.,,131,14,,,,,,,,,,,,,,,,,,,,,,5134,5144,2009, citations,entry_citation,15853,37020,1,,entry citation,,,17945182,,,Local and global structure of the monomeric subunit of the potassium channel KcsA probed by NMR,published,journal,Biochim. Biophys. Acta.,,1768,12,,,,,,,,,,,,,,,,,,,,,,3260,3270,2007, citations,citation_1,15854,37040,1,,entry citation,,,18939814,,,"Solution structure of the supramolecular adduct between a liver cytosolic bile acid binding protein and a bile acid-based gadolinium(III)-chelate, a potential hepatospecific magnetic resonance imaging contrast agent",published,journal,J. Med. Chem.,Journal of Medicinal Chemistry,51,21,,,,,,,,,,,,,,,,,,,,,,6782,6792,2008, citations,citations_1,15855,37057,1,,entry citation,,,19636889,,,NMR assignment and secondary structure of human growth arrest and DNA damage alpha protein (Gadd45 alpha),published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,2,2,,,,,,,,,,,,,,,,,,,,,,139,142,2008, citations,entry_citation,15856,37082,1,,entry citation,,,,,,Solution structure of the 5'-splice site of a group II intron ribozyme,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15857,37115,1,,entry citation,,,,,,Solution structure of the 5'-splice site of a group II intron ribozyme,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15858,37145,1,,entry citation,,,,,,Solution structure of the 5'-splice site of a group II intron ribozyme,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15859,37169,1,,entry citation,,,,,,Solution structure of the 5'-splice site of a group II intron ribozyme,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1586,37195,1,,entry citation,,,,,"Kristensen, Soren M., Jorgensen, Anne Marie M., Led, Jens J., Balschmidt, Per, Hansen, Finn B., ""Proton Nuclear Magnetic Resonance Study of the B9(Asp)Mutant of Human Insulin Sequential Assignment and Secondary Structure,"" J. Mol. Biol. 218, 221-231 (1991).","Proton Nuclear Magnetic Resonance Study of the B9(Asp)Mutant of Human Insulin Sequential Assignment and Secondary Structure",published,journal,J. Mol. Biol.,,218,,,,,,,,,,,,,,,,,,,,,,,221,231,1991, citations,entry_citation,15860,37208,1,,entry citation,,,,,,Solution structure at different pHs of a DNA hairpin containing artificial nucleotides,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,15863,37234,1,,entry citation,,,18674544,,,"The Cys3-Cys4 loop of the hydrophobin EAS is not required for rodlet formation and surface activity",published,journal,J. Mol. Biol.,Journal of molecular biology,382,3,,,,,,,,,,,,,,,,,,,,,,708,720,2008, citations,entry_citation,15864,37255,1,,entry citation,,,19358820,,,Structure-function correlation of human programmed cell death 5 protein,published,journal,Arch. Biochem. Biophys.,Archives of Biochemistry and Biophysics,486,2,,,,,,,,,,,,,,,,,,,,,,141,149,2009, citations,entry_citation,15865,37272,1,,entry citation,,,18954090,,,Detailed Structural Characterization of Unbound Protein Phosphatase 1 Inhibitors,published,journal,Biochemistry,,47,47,,,,,,,,,,,,,,,,,,,,,,12346,12356,2008, citations,entry_citation,15866,37288,1,,entry citation,,,18680311,,,Interactions between the three CIN85 SH3 domains and ubiquitin: implications for CIN85 ubiquitination.,published,journal,Biochemistry,,47,34,,,,,,,,,,,,,,,,,,,,,,8937,8949,2008, citations,entry_citation,15910,38256,1,,entry citation,,,19361434,,,Structural and motional contributions of the Bacillus subtilis ClpC N-domain to adaptor protein interactions,published,journal,J. Mol. Biol.,,387,3,,,,,,,,,,,,,,,,,,,,,,639,652,2009, citations,entry_citation,15867,37305,1,,entry citation,,,19636936,,,"1H, 15N, 13C resonance assignment of 9.7 M urea-denatured state of the GTPase effector domain (GED) of dynamin",publshed,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,3,1,,,,,,,,,,,,,,,,,,,,,,13,16,2009, citations,GED97UREA,15867,37306,2,,reference citation,,,19026983,,,"1H, 13C and 15N resonance assignment of urea-denatured GED of dynamin",publshed,journal,Arch. Biochem. Biophys.,Archives of Biochemistry and Biophysics,481,2,,,,,,,,,,,,,,,,,,,,,,169,176,2009, citations,Guanidine-denatured_GED,15868,37323,1,,entry citation,,,17910478,,,Pockets of short-range transient order and restricted topological heterogeneity in the guanidine-denatured state ensemble of GED of dynamin,published,journal,Biochemistry,,46,42,,,,,,,,,,,,,,,,,,,,,,11819,11832,2007, citations,entry_1,15869,37339,1,,entry citation,,,19636896,,,NMR Assignments of HIV-2 TAR RNA,published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,2,2,,,,,,,,,,,,,,,,,,,,,,167,169,2008, citations,entry_citation,1587,37359,1,,entry citation,,,,,"Kristensen, Soren M., Jorgensen, Anne Marie M., Led, Jens J., Balschmidt, Per, Hansen, Finn B., ""Proton Nuclear Magnetic Resonance Study of the B9(Asp)Mutant of Human Insulin Sequential Assignment and Secondary Structure,"" J. Mol. Biol. 218, 221-231 (1991).","Proton Nuclear Magnetic Resonance Study of the B9(Asp)Mutant of Human Insulin Sequential Assignment and Secondary Structure",published,journal,J. Mol. Biol.,,218,,,,,,,,,,,,,,,,,,,,,,,221,231,1991, citations,citations,15870,37372,1,,entry citation,,,19580766,,,Domain features of the peripheral stalk subunit H of the methanogenic A1AO ATP synthase and the NMR solution structure of H(1-47).,published,journal,Biophys. J.,Biophysical journal,97,1,,,,,,,,,,,,,,,,,,,,,,286,294,2009, citations,entry_citation,15871,37389,1,,entry citation,,,20060909,,,A new member of the ribbon-helix-helix transcription factor superfamily from the plant pathogen Xanthomonas axonopodis pv.citri.,published,journal,J. Struct. Biol.,Journal of structural biology,170,1,,,,,,,,,,,,,,,,,,,,,,21,31,2010, citations,Solution_Structure_of_Supervillin_Headpiece,15873,37409,1,,entry citation,,,19683541,,,How to Arm a Supervillin: Designing F-Actin Binding Activity into Supervillin Headpiece,published,journal,J. Mol. Biol.,Journal of molecular biology,393,3,,,,,,,,,,,,,,,,,,,,,,608,618,2009, citations,Solution_Structure_of_Supervillin_Headpiece,15874,37433,1,,entry citation,,,19683541,,,How to arm a supervillin: designing F-actin binding activity into supervillin headpiece.,published,journal,J. Mol. Biol.,Journal of molecular biology,393,3,,,,,,,,,,,,,,,,,,,,,,608,618,2009, citations,citation_1,15875,37457,1,,entry citation,,,19462967,,,"Kinetic, Dynamic, Ligand Binding Properties, and Structural Models of a Dual-Substrate Specific Nudix Hydrolase from Schizosaccharomyces pombe",published,journal,Biochemistry,Biochemistry,48,26,,,,,,,,,,,,,,,,,,,,,,6224,6239,2009, citations,entry_citation,15876,37476,1,,entry citation,,,18818205,,,Structures of human host defense cathelicidin LL-37 and its smallest antimicrobial peptide KR-12 in lipid micelles,published,journal,J. Biol. 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Soc.,,123,,,,,,,,,,,,,,,,,,,,,,,2858,2864,2001, citations,Brutscher_2002,15909,38213,8,,reference citation,,,12081454,,,Intraresidue HNCA and COHNCA experiments for protein backbone resonance assignment,published,journal,J. Magn. Reson.,,156,,,,,,,,,,,,,,,,,,,,,,,155,159,2002, citations,Nietlispach_et_al_2002,15909,38214,9,,reference citation,,,12224968,,,A novel approach for the sequential backbone assignment of larger proteins: Selective intra-HNCA and DQ-HNCA,published,journal,J. Am. Chem. Soc.,,124,,,,,,,,,,,,,,,,,,,,,,,11199,11207,2002, citations,Permi_2002,15909,38215,10,,reference citation,,,12238592,,,Intraresidual HNCA: An experiment for correlating only intraresidual backbone resonances,published,journal,J. Biomol. NMR,,23,,,,,,,,,,,,,,,,,,,,,,,201,209,2002, citations,Hu_et_al_2003,15909,38216,11,,reference citation,,,,,,A high sensitivity 3D experiment for measuring Calpha-Halpha residual dipolar coupling constants,published,journal,J. Magn. 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Biol.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15911,38283,1,,entry citation,,,19159328,,,"The periplasmic loop P2 of the MalF subunit of the maltose ATP binding cassette transporter is sufficient to bind the maltose binding protein MalE",published,journal,Biochemistry,,48,10,,,,,,,,,,,,,,,,,,,,,,2216,2225,2009, citations,entry_citation,15912,38298,1,,entry citation,,,19361414,,,Proline isomerization preorganizes the Itk SH2 domian for binding to the Itk SH3 domain,published,journal,J. Mol. Biol.,Journal of Molecular Biology,387,3,,,,,,,,,,,,,,,,,,,,,,726,743,2009, citations,entry_citation,15913,38321,1,,entry citation,,,18715872,,,The IsdC protein from Staphylococcus aureus uses a flexible binding pocket to capture heme,published,journal,J. Biol. Chem.,,283,46,,,,,,,,,,,,,,,,,,,,,,31591,31600,2008, citations,entry_citation,15914,38344,1,,entry citation,,,18981177,,,The structure of binder of Arl2 (BART) reveals a novel G protein binding domain: Implications for function.,published,journal,J. Biol. Chem.,,284,2,,,,,,,,,,,,,,,,,,,,,,992,999,2009, citations,1,15915,38365,1,,entry citation,,,19324888,,,"The structure of the human tRNALys3 anticodon bound to the HIV genome is stabilized by modified nucleosides and adjacent mismatch base pairs",published,journal,Nucleic Acids Res.,Nucleic Acids Research,37,10,,,,,,,,,,,,,,,,,,,,,,3342,3353,2009, citations,entry_citation,15916,38395,1,,entry citation,,,,,,Solution structure of protein ATC0223 from Agrobacterium Tumefaciens.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15917,38421,1,,entry citation,,,21425229,,,Engineering an allosteric binding site for aminoglycosides into TEM1-beta-Lactamase,published,journal,Chembiochem,,12,6,,,,,,,,,,,,,,,,,,,,,,904,913,2011, citations,citation_1,15918,38440,1,,entry citation,,,19636958,,,"Complete backbone assignment of a Ca2+-binding protein of the betagamma-crystallin superfamily from Methanosarcina acetivorans, at two denaturant concentrations",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,3,1,,,,,,,,,,,,,,,,,,,,,,107,110,2009, citations,entry_citation,15919,38458,1,,entry citation,,,19215094,,,"NMR structure of a complex formed by the carboxyl-terminal domain of human RAP74 and a phosphorylated peptide from the central domain of the FCP1 Phosphatase",published,journal,Biochemistry,Biochemistry,48,9,,,,,,,,,,,,,,,,,,,,,,1964,1974,2009, citations,entry_citation,1592,38479,1,,entry citation,,,,,"Fry, David C., Kuby, Stephen A., Mildvan, Albert S., ""NMR Studies of the MgATP Binding Site of Adenylate Kinase and of a 45-Residue Peptide Fragment of the Enzyme,"" Biochemistry 24, 4680-4694 (1985).","NMR Studies of the MgATP Binding Site of Adenylate Kinase and of a 45-Residue Peptide Fragment of the Enzyme",published,journal,Biochemistry,,24,,,,,,,,,,,,,,,,,,,,,,,4680,4694,1985, citations,entry_citation,15921,38492,1,,entry citation,,,18937032,,,"Biosynthesis and NMR-studies of a double transmembrane domain from the Y4 receptor, a human GPCR",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,42,4,,,,,,,,,,,,,,,,,,,,,,257,269,2008, citations,citations,15922,38507,1,,entry citation,,,20007319,,,A large intrinsically disordered region in SKIP and its disorder-order transition induced by PPIL1 binding revealed by NMR.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,285,7,,,,,,,,,,,,,,,,,,,,,,4951,4963,2010, citations,entry_citation,15923,38521,1,,entry citation,,,18949447,,,Refinement of the solution structure and dynamic properties of Ca2+-bound rat S100B,published,journal,J. Biomol. NMR,,42,4,,,,,,,,,,,,,,,,,,,,,,279,286,2008, citations,FLNa16-17structure,15924,38543,1,,entry citation,,,19636946,,,"1H, 13C and 15N resonance assignments of the human filamin A tandem immunoglobulin-like domains 16-17 and 18-19",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,3,1,,,,,,,,,,,,,,,,,,,,,,53,56,2009, citations,FLNa18-19structure,15925,38563,1,,entry citation,,,19636946,,,"1H, 13C and 15N resonance assignments of the human filamin A tandem immunoglobulin-like domains 16-17 and 18-19",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,3,1,,,,,,,,,,,,,,,,,,,,,,53,56,2009, citations,citation_1,15926,38584,1,,entry citation,,,19255093,,,A novel zinc-binding fold in the helicase interaction domain of the Bacillus subtilis DnaI helicase loader,published,journal,Nucleic Acids Res.,,37,7,,,,,,,,,,,,,,,,,,,,,,2395,2404,2009, citations,entry_citation,15927,38607,1,,entry citation,,,19636934,,,"1H, 13C, and 15N NMR assignments of the actinoporin Sticholysin I",published,journal,Biomol. NMR Assignments,,3,1,,,,,,,,,,,,,,,,,,,,,,5,7,2009, citations,citation_1,15928,38624,1,,entry citation,,,19196990,,,ARNT PAS-B has a fragile native state structure with an alternative {beta}-sheet register nearby in sequence space.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,106,8,,1091-6490,,,,,,,,,,,,,,,,,,,,2617,2622,2009, citations,citation_2,15928,38625,2,,reference citation,,,16181639,,,Structural Basis of ARNT PAS-B Dimerization: Use of a Common Beta-sheet Interface for Hetero- and Homodimerization,published,journal,J. Mol. Biol.,,353,3,,,,,,,,,,,,,,,,,,,,,,664,677,2005, citations,entry_citation,15930,38643,1,,entry citation,,,19847776,,,Backbone dynamics of TFE-induced native-like fold of region 4 of Escherichia coli RNA polymerase sigma70 subunit.,published,journal,Proteins,Proteins,78,3,,,,,,,,,,,,,,,,,,,,,,754,768,2010, citations,entry_citation,15931,38660,1,,entry citation,,,19679089,,,A surface loop directs conformational switching of a lipoyl domain between a folded and a novel misfolded structure,published,journal,Structure,,17,8,,,,,,,,,,,,,,,,,,,,,,1117,1127,2009, citations,citation_1,15932,38674,1,,entry citation,,,19278658,,,Structural and Biochemical Studies on Procaspase-8: New Insights on Initiator Caspase Activation,published,journal,Structure,,17,3,,,,,,,,,,,,,,,,,,,,,,438,448,2009, citations,NOGO66,15933,38693,1,,entry citation,,,20351248,,,"Protein folding at the membrane interface, the structure of Nogo-66 requires interactions with a phosphocholine surface.",published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,107,15,,,,,,,,,,,,,,,,,,,,,,6847,6851,2010, citations,citation_1,15934,38709,1,,entry citation,,,19636958,,,"Complete backbone assignment of a Ca2+-binding protein of the betagamma-crystallin superfamily from Methanosarcina acetivorans, at two denaturant concentrations",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,3,1,,,,,,,,,,,,,,,,,,,,,,107,110,2009, citations,citation_1,15935,38726,1,,entry citation,,,,,,Pfu RPP29d17-RPP21V14 complex,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15936,38758,1,,entry citation,,,19847776,,,Backbone dynamics of TFE-induced native-like fold of region 4 of Escherichia coli RNA polymerase sigma70 subunit.,published,journal,Proteins,Proteins,78,3,,,,,,,,,,,,,,,,,,,,,,754,768,2010, citations,entry_citation,15937,38791,1,,entry citation,,,20015412,,,Solution structure of the equine infectious anemia virus p9 protein: a rationalization of its different ALIX binding requirements compared to the analogous HIV-p6 protein.,published,journal,BMC Struct. Biol.,BMC structural biology,9,,,,,,,,,,,,,,,,,,,,,,,74,74,2009, citations,entry_citation,15938,38805,1,,entry citation,,,19393245,,,NMR structural studies on human p190-A RhoGAPFF1 revealed that domain phosphorylation by the PDGF-receptor alpha requires its previous unfolding,published,journal,J. Mol. Biol.,Journal of Molecular Biology,389,2,,,,,,,,,,,,,,,,,,,,,,230,237,2009, citations,entry_citation,15939,38823,1,,entry citation,,,18824006,,,Biochemical and structural characterization of an intramolecular interaction in FOXO3a and its binding with p53,published,journal,J. Mol. Biol.,Journal of molecular biology,384,3,,,,,,,,,,,,,,,,,,,,,,590,603,2008, citations,citations,15940,38846,1,,entry citation,,,19344662,,,Assembly of subunit d (Vma6p) and G (Vma10p) and the NMR solution structure of subunit G (G(1-59)) of the Saccharomyces cerevisiae V(1)V(O) ATPase,published,journal,Biochim. Biophys Acta.,,1787,4,,,,,,,,,,,,,,,,,,,,,,242,251,2009, citations,entry_citation,15941,38863,1,,entry citation,,,21219456,,,Structure-function relationship in an archaebacterial methionine sulphoxide reductase B.,published,journal,Mol. Microbiol.,Molecular microbiology,79,2,,,,,,,,,,,,,,,,,,,,,,342,358,2011, citations,entry_citation,15942,38884,1,,entry citation,,,,,,Solution structure of RRM2 domain of PABP1,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,15943,38898,1,,entry citation,,,,,,Solution structure of protein yegP from Escherichia Coli.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15944,38921,1,,entry citation,,,19217391,,,Structural Basis for p300 Taz2-p53 TAD1 Binding and Modulation by Phosphorylation,published,journal,Structure,,17,2,,,,,,,,,,,,,,,,,,,,,,202,210,2009, citations,citation,15945,38948,1,,entry citation,,,18959403,,,Analysis of chemical shift changes reveals the binding modes of isoindolinone inhibitors of the MDM2-p53 interaction,published,journal,J. Am. Chem. Soc.,,130,47,,,,,,,,,,,,,,,,,,,,,,16038,16044,2008, citations,citations_1,15946,38963,1,,entry citation,,,19284291,,,"The solution structure of pGolemi, a high affinity Mena EVH1 binding miniature protein, suggests explanations for paralog-specific binding to Ena/VASP homology (EVH) 1 domains",published,journal,Biol. Chem.,,390,5-6,,,,,,,,,,,,,,,,,,,,,,417,26,2009, citations,citations_2,15946,38964,2,,reference citation,,,14709031,,,"Miniature protein ligands for EVH1 domains: interplay between affinity, specificity, and cell motility",published,journal,J. Am. Chem. Soc.,,126,1,,,,,,,,,,,,,,,,,,,,,,4,5,2004, citations,citations_3,15946,38965,3,,reference citation,,,17973491,,,"Miniature Protein Ligands for EVH1 Domains: Interplay between Affinity, Specificity, and Cell Motility",published,journal,Biochemistry,,46,47,,,,,,,,,,,,,,,,,,,,,,13541,13553,2007, citations,entry_citation,15948,38980,1,,entry citation,,,19032943,,,High yield expression and NMR characterization of Arkadia E3 ubiquitin ligase RING-H2 finger domain,published,journal,Biochem. Biophys. Res. Commun.,,378,3,,,,,,,,,,,,,,,,,,,,,,498,502,2009, citations,citations,15949,38996,1,,entry citation,,,19636948,,,"1H, 15N, 13C resonance assignments of the reduced and active form of human Protein Tyrosine Phosphatase, PRL-1.",published,journal,Biomol. NMR Assignments,,3,1,,,,,,,,,,,,,,,,,,,,,,61,65,2009, citations,entry_citation,15950,39014,1,,entry citation,,,19356587,,,"NMR Solution Structure of SlyD from Escherichia coli: Spatial Separation of Prolyl Isomerase and Chaperone Function",published,journal,J. Mol. Biol.,Journal of Molecular Biology,387,2,,,,,,,,,,,,,,,,,,,,,,295,305,2009, citations,entry_citation,15951,39029,1,,entry citation,,,20667830,,,NMR Structure and Ion Channel Activity of the p7 Protein from Hepatitis C Virus.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,285,41,,,,,,,,,,,,,,,,,,,,,,31446,31461,2010, citations,reference_citation,15951,39030,2,,reference citation,,,19009258,,,Structural and functional analysis of the HCV p7 protein.,published,journal,Methods Mol. Biol.,Methods in molecular biology,510,,,,,,,,,,,,,,,,,,,,,,,125,43,2009, citations,S100A13-C2A,15952,39045,1,,entry citation,,,19284995,,,"S100A13-C2A binary complex structure-a key component in the acidic fibroblast growth factor for the non-classical pathway",published,journal,Biochem. Biophys. Res. Commun.,Biochemical and Biophysical Research Communications,380,3,,,,,,,,,,,,,,,,,,,,,,514,519,2009, citations,entry_citation,15953,39063,1,,entry citation,,,18942858,,,"Differences in Dynamic Structure of LC8 Monomer, Dimer and Dimer-Peptide Complexes.",published,journal,Biochemistry,,47,46,,,,,,,,,,,,,,,,,,,,,,11940,11952,2008, citations,entry_citation,15954,39077,1,,entry citation,,,19636939,,,"Backbone and sidechain 1H, 15N, and 13C assignments of the human eIF5A",published,journal,Biomol. NMR Assignments,,3,1,,,,,,,,,,,,,,,,,,,,,,25,28,2009, citations,entry_citation,15955,39095,1,,entry citation,,,19799854,,,Solid-state NMR study of proteorhodopsin in the lipid environment: secondary structure and dynamics.,published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1788,12,,,,,,,,,,,,,,,,,,,,,,2563,2574,2009, citations,reference_citation,15955,39096,2,,reference citation,,,19244620,,,Three-Dimensional Solid-State NMR Study of a Seven-Helical Integral Membrane Proton Pump - Structural Insights,published,journal,J. Mol. Biol.,,386,4,,,,,,,,,,,,,,,,,,,,,,1078,1093,2009, citations,entry_citation,15956,39115,1,,entry citation,,,18937504,,,The solution structure of BMPR-IA reveals a local disorder-to-order transition upon BMP-2 binding,published,journal,Biochemistry,Biochemistry,47,46,,,,,,,,,,,,,,,,,,,,,,11930,11939,2008, citations,entry_citation,15957,39139,1,,entry citation,,,19254034,,,"Structural Studies of HIV-1 Gag p6ct and Its Interaction with Vpr Determined by Solution Nuclear Magnetic Resonance",published,journal,Biochemistry,,48,11,,,,,,,,,,,,,,,,,,,,,,2355,2367,2009, citations,entry_citation,15958,39153,1,,entry citation,,,19426738,,,The Box H/ACA snoRNP Assembly Factor Shq1p is a Chaperone Protein Homologous to Hsp90 Cochaperones that Binds to the Cbf5p Enzyme.,published,journal,J. Mol. Biol.,Journal of molecular biology,390,2,,,,,,,,,,,,,,,,,,,,,,231,244,2009, citations,entry_citation,15959,39179,1,,entry citation,,,19053277,,,Remote Changes in Dynamics of the Phosphotyrosine-Binding Domain of Insulin Receptor Substrate-1 Induced by Phosphopeptide Binding,published,journal,Biochemistry,,47,50,,,,,,,,,,,,,,,,,,,,,,13371,13382,2008, citations,reference_1,15960,39193,1,,entry citation,,,21077672,,,"Molecular level interaction of the human acidic fibroblast growth factor with the antiangiogenic agent, inositol hexaphosphate .",published,journal,Biochemistry,Biochemistry,49,50,,,,,,,,,,,,,,,,,,,,,,10756,10764,2010, citations,entry_citation,15961,39210,1,,entry citation,,,19636952,,,Complete resonance assignments for the MIC2 associated protein from Toxoplasma gondii,published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,3,1,,,,,,,,,,,,,,,,,,,,,,81,83,2009, citations,HasAp_Truncated,15962,39225,1,,entry citation,,,19072037,,,"Structural characterization of the hemophore HasAp from Pseudomonas aeruginosa: NMR spectroscopy reveals protein-protein interactions between Holo-HasAp and hemoglobin.",published,journal,Biochemistry,,48,1,,,,,,,,,,,,,,,,,,,,,,96,109,2009, citations,HasAp_Full_Length,15963,39250,1,,entry citation,,,19072037,,,"Structural characterization of the hemophore HasAp from Pseudomonas aeruginosa: NMR spectroscopy reveals protein-protein interactions between Holo-HasAp and hemoglobin.",published,journal,Biochemistry,,48,1,,,,,,,,,,,,,,,,,,,,,,96,109,2009, citations,entry_citation,15964,39275,1,,entry citation,,,19361226,,,Solution Structure and Dynamics of ERp18: a Small ER Resident Oxidoreductase,published,journal,Biochemistry,,48,21,,,,,,,,,,,,,,,,,,,,,,4596,4606,2009, citations,citations,17025,59734,1,,entry citation,,,,,,Solution NMR Structure of protein BVU3908 from Bacteroides vulgatus,in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,reference_citation,15964,39276,2,,reference citation,,,12761212,,,"Functional Characterization of ERp18, a New Endoplasmic Reticulum-located Thioredoxin Superfamily Member",published,journal,J. Biol. Chem.,,278,31,,,,,,,,,,,,,,,,,,,,,,28912,28920,2003, citations,entry_citation,15965,39298,1,,entry citation,,,19170537,,,Structure of the N Terminus of a Nonmuscle alpha-Tropomyosin in Complex with the C Terminus: Implications for Actin Binding,published,journal,Biochemistry,,48,6,,,,,,,,,,,,,,,,,,,,,,1272,1283,2009, citations,entry_citation,15966,39320,1,,entry citation,,,18922471,,,NMR solution structure of the integral membrane enzyme DsbB: functional insights into DsbB-catalyzed disulfide bond formation.,published,journal,Mol. Cell,,31,6,,,,,,,,,,,,,,,,,,,,,,896,908,2008, citations,entry_citation,15967,39340,1,,entry citation,,,19492851,,,Structure and Dynamics of the Iron-Sulfur Cluster Assembly Scaffold Protein IscU and Its Interaction with the Cochaperone HscB.,published,journal,Biochemistry,Biochemistry,48,26,,,,,,,,,,,,,,,,,,,,,,6062,6071,2009, citations,entry_citation,15968,39357,1,,entry citation,,,18948116,,,Atypical binding of the Swa2p UBA domain to ubiquitin,published,journal,J. Mol. Biol.,,386,2,,,,,,,,,,,,,,,,,,,,,,569,577,2009, citations,entry_citation,15969,39373,1,,entry citation,,,18952101,,,Moving towards high resolution descriptions of the molecular interactions and structural rearrangements of the human hepatitis B core protein,published,journal,J. Mol. Biol.,Journal of molecular biology,384,5,,,,,,,,,,,,,,,,,,,,,,1301,1303,2008, citations,citations,15970,39388,1,,entry citation,,,18765641,,,Similar Modes of Interaction Enable Trailer Hitch and Edc3 to Associate with Dcp1 and Me31B in Distinct Protein Complexes,published,journal,Mol. Cell. Biol,,28,21,,,,,,,,,,,,,,,,,,,,,,6695,6708,2008, citations,citations,15971,39404,1,,entry citation,,,18765641,,,Similar Modes of Interaction Enables Trailer Hitch and Edc3 to Associate with Dcp1 and Me31B in Distinct Protein Complexes,published,journal,Mol. Cell. Biol.,Molecular and Cellular Biology,28,21,,,,,,,,,,,,,,,,,,,,,,6695,6708,2008, citations,entry_citation,15972,39419,1,,entry citation,,,19636944,,,"1H, 13C and 15N resonance assignments of the PDZ of microtubule-associated serine/threonine kinase 205 (MAST205) in complex with the C-terminal motif from the rabies virus glycoprotein",published,journal,Biomol. NMR Assignments,,3,1,,,,,,,,,,,,,,,,,,,,,,45,48,2009, citations,entry_citation,15973,39433,1,,entry citation,,,18973760,,,Noncompetitive inhibition of Hepatocyte Growth Factor Dependent Met signaling by a phage-derived peptide,published,journal,J. Mol. Biol.,,385,1,,,,,,,,,,,,,,,,,,,,,,79,90,2009, citations,entry_citation,15974,39450,1,,entry citation,,,19604149,,,Mapping of the ligand-binding site on the b' domain of human PDI: interaction with peptide ligands and the x-linker region.,published,journal,Biochem. J.,The Biochemical journal,423,2,,,,,,,,,,,,,,,,,,,,,,209,217,2009, citations,entry_citation,15975,39466,1,,entry citation,,,19847776,,,Backbone dynamics of TFE-induced native-like fold of region 4 of Escherichia coli RNA polymerase sigma70 subunit.,published,journal,Proteins,Proteins,78,3,,,,,,,,,,,,,,,,,,,,,,754,768,2010, citations,entry_citation,15977,39484,1,,entry citation,,,19636935,,,"1H, 13C and 15N backbone and side chain resonance assignments of the C-terminal domain of CdnL from Myxococcus xanthus",published,journal,Biomol. NMR Assignments,,3,1,,,,,,,,,,,,,,,,,,,,,,9,12,2009, citations,entry_citation,15978,39505,1,,entry citation,,,18844294,,,"Lipopolysaccharide Bound Structures of the Active Fragments of Fowlicidin-1, a Cathelicidin Family of Antimicrobial and Antiendotoxic Peptide from Chicken, Determined by Transferred Nuclear Overhauser Effect Spectroscopy",published,journal,Biopolymers,Biopolymers,92,1,,,,,,,,,,,,,,,,,,,,,,9,22,2009, citations,entry_citation,15979,39519,1,,entry citation,,,18844294,,,"Lipopolysaccharide Bound Structures of the Active Fragments of Fowlicidin-1, a Cathelicidin Family of Antimicrobial and Antiendotoxic Peptide from Chicken, Determined by Transferred Nuclear Overhauser Effect Spectroscopy",published,journal,Biopolymers,Biopolymers,92,1,,,,,,,,,,,,,,,,,,,,,,9,22,2009, citations,entry_citation,15980,39533,1,,entry citation,,,18844294,,,"Lipopolysaccharide Bound Structures of the Active Fragments of Fowlicidin-1, a Cathelicidin Family of Antimicrobial and Antiendotoxic Peptide from Chicken, Determined by Transferred Nuclear Overhauser Effect Spectroscopy",published,journal,Biopolymers,Biopolymers,92,1,,,,,,,,,,,,,,,,,,,,,,9,22,2009, citations,entry_citation,15981,39547,1,,entry citation,,,18951093,,,Atomic structure of the KEOPS complex: an ancient protein kinase-containing molecular machine,published,journal,Mol. Cell,Molecular cell,32,2,,,,,,,,,,,,,,,,,,,,,,259,275,2008, citations,entry_citation,15983,39563,1,,entry citation,,,19122005,,,Engineering a stable and selective peptide blocker of the Kv1.3 channel in T lymphocytes,published,journal,Mol. Pharmacol.,,75,4,,,,,,,,,,,,,,,,,,,,,,762,773,2009, citations,entry_citation,15986,39582,1,,entry citation,,,19251642,,,Identification and structural analysis of type-I collagen sites in complex with fibronectin fragments,published,journal,"Proc. Natl. Acad. Sci., U.S.A.",,106,11,,,,,,,,,,,,,,,,,,,,,,4195,4200,2009, citations,entry_citation,15987,39607,1,,entry citation,,,19788170,,,Structure-based stability analysis of an extremely stable dimeric DNA binding protein from Sulfolobus islandicus.,published,journal,Biochemistry,Biochemistry,48,42,,,,,,,,,,,,,,,,,,,,,,10030,10037,2009, citations,entry_citation,15988,39622,1,,entry citation,,,18973471,,,MOLECULAR CHARACTERIZATION OF THE TonB2 PROTEIN FROM Vibrio anguillarum,published,journal,Biochem. J.,The Biochemical Journal,418,1,,,,,,,,,,,,,,,,,,,,,,49,59,2009, citations,entry_citation,15989,39637,1,,entry citation,,,19246540,,,NMR structural analysis of DNA recognition by a novel Myb1 DNA-binding domain in the protozoan parasite Trichomonas vaginalis,published,journal,Nucleic Acids Res.,,37,7,,,,,,,,,,,,,,,,,,,,,,2381,2394,2009, citations,entry_citation,15990,39659,1,,entry citation,,,19426742,,,Structure of the RNA Polymerase Core-Binding Domain of sigma(54) Reveals a Likely Conformational Fracture Point.,published,journal,J. Mol. Biol.,Journal of molecular biology,390,1,,,,,,,,,,,,,,,,,,,,,,70,82,2009, citations,entry_citation,15991,39676,1,,entry citation,,,19426742,,,Structure of the RNA Polymerase Core-Binding Domain of sigma(54) Reveals a Likely Conformational Fracture Point.,published,journal,J. Mol. Biol.,Journal of molecular biology,390,1,,,,,,,,,,,,,,,,,,,,,,70,82,2009, citations,citations,15992,39694,1,,entry citation,,,,,,Solution structure of Vm24 synthetic scorpion toxin.,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,15993,39712,1,,entry citation,,,19275899,,,Interaction between the C-terminal Domains Of N and P Proteins of measles virus investigated by NMR,published,journal,FEBS Lett.,FEBS Lettets,583,7,,,,,,,,,,,,,,,,,,,,,,1084,1089,2009, citations,entry_citation,15994,39729,1,,entry citation,,,19275899,,,Interaction between the C-terminal Domains Of N and P Proteins of measles virus investigated by NMR,published,journal,FEBS Lett.,FEBS letters,583,7,,,,,,,,,,,,,,,,,,,,,,1084,1089,2009, citations,citations,15995,39746,1,,entry citation,,,19383463,,,STRUCTURE OF A DOUBLE TRANSMEMBRANE FRAGMENT OF A G PROTEIN-COUPLED RECEPTOR IN MICELLES,published,journal,Biophys J.,Biophysical Journal,96,8,,,,,,,,,,,,,,,,,,,,,,3187,3196,2009, citations,entry_citation,15996,39767,1,,entry citation,,,19636945,10.1007/s12104-008-9139-z,,"1H, 15N and 13C resonance assignment of the pair of Factor-I like modules of the complement protein C7",published,journal,Biomol. NMR Assign.,,3,1,,,,,,,,,,,,,,,,,,,,,,49,52,2009, citations,citations,15997,39785,1,,entry citation,,,20385603,,,Solution structure of the dimerization domain of ribosomal protein P2 provides insights for the structural organization of eukaryotic stalk.,published,journal,Nucleic Acids Res.,Nucleic acids research,38,15,,,,,,,,,,,,,,,,,,,,,,5206,5216,2010, citations,entry_citation,15998,39801,1,,entry citation,,,19604149,,,Mapping of the ligand-binding site on the b' domain of human PDI: interaction with peptide ligands and the x-linker region.,published,journal,Biochem. J.,The Biochemical journal,423,2,,,,,,,,,,,,,,,,,,,,,,209,217,2009, citations,entry_citation,15999,39817,1,,entry citation,,,,,,"Solution NMR structure of HTH_XRE family transcriptional regulator BT_p548217 from Bacteroides thetaiotaomicron. Northeast Structural Genomics Consortium Target BtR244.",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16000,39870,1,,entry citation,,,20058326,,,Solution structure of the C-terminal X domain of the measles virus phosphoprotein and interaction with the intrinsically disordered C-terminal domain of the nucleoprotein.,published,journal,J. Mol. Recognit.,Journal of molecular recognition : JMR,23,5,,,,,,,,,,,,,,,,,,,,,,435,447,2010, citations,citations,16001,39885,1,,entry citation,,,19422057,,,Solution Structure of the DNA binding domain of AraC protein,published,journal,Proteins,Proteins,77,1,,,,,,,,,,,,,,,,,,,,,,202,208,2009, citations,cytoskeletal_complex,16002,39908,1,,entry citation,,,19074766,,,"Migfilin, a molecular switch in regulation of integrin activation",published,journal,J. Biol. Chem.,Journal of Biological Chemistry,284,7,,,,,,,,,,,,,,,,,,,,,,4713,4722,2009, citations,entry_citation,16003,39923,1,,entry citation,,,,,,1H 13C and 15N Assigned Chemical Backbone Shifts for BASP1,in preparation,journal,Proc. Natl. Acad. Sci. U. S. A.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,16005,39938,1,,entry citation,,,20197042,,,Left-handed dimer of EphA2 transmembrane domain: Helix packing diversity among receptor tyrosine kinases.,published,journal,Biophys. J.,Biophysical journal,98,5,,,,,,,,,,,,,,,,,,,,,,881,889,2010, citations,NMR_structure_of_the_protein_TM1112,16006,39958,1,,entry citation,,,20944235,,,Comparison of NMR and crystal structures for the proteins TM1112 and TM1367.,published,journal,Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.,"Acta crystallographica. Section F, Structural biology and crystallization communications",66,Pt 10,,,,,,,,,,,,,,,,,,,,,,1381,1392,2010, citations,entry_citation,16007,39980,1,,entry citation,,,20944235,,,Comparison of NMR and crystal structures for the proteins TM1112 and TM1367.,published,journal,Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.,"Acta crystallographica. Section F, Structural biology and crystallization communications",66,Pt 10,,,,,,,,,,,,,,,,,,,,,,1381,1392,2010, citations,entry_citation,16008,40003,1,,entry citation,,,19828617,,,Nuclear magnetic resonance structure of the nucleic acid-binding domain of severe acute respiratory syndrome coronavirus nonstructural protein 3.,published,journal,J. Virol.,Journal of virology,83,24,,,,,,,,,,,,,,,,,,,,,,12998,13008,2009, citations,entry_citation,16009,40022,1,,entry citation,,,19636943,,,NMR resonance assignment of DnaE intein from Nostoc punctiforme,published,journal,Biomol. NMR Assignments,,3,1,,,,,,,,,,,,,,,,,,,,,,41,43,2009, citations,citation_2,16009,40023,2,,reference citation,,,16516207,,,Highly efficient protein trans-splicing by a naturally split DnaE intein from Nostoc punctiforme.,published,journal,FEBS Lett.,,580,,,,,,,,,,,,,,,,,,,,,,,1853,1858,2006, citations,citation_1,16010,40041,1,,entry citation,,,20085318,,,NMR spectroscopy reveals that RNase A is chiefly denatured in 40% acetic acid: implications for oligomer formation by 3D domain swapping.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,132,5,,,,,,,,,,,,,,,,,,,,,,1621,1630,2010, citations,entry_citation,16011,40056,1,,entry citation,,,20085318,,,NMR spectroscopy reveals that RNase A is chiefly denatured in 40% acetic acid: implications for oligomer formation by 3D domain swapping.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,132,5,,,,,,,,,,,,,,,,,,,,,,1621,1630,2010, citations,citations,16012,40071,1,,entry citation,,,19415897,,,The structural basis for dimerization of the BNIP3 transmembrane domain,published,journal,Biochemistry,Biochemistry,48,23,,,,,,,,,,,,,,,,,,,,,,5106,5120,2009, citations,entry_citation,16014,40089,1,,entry citation,,,19214187,,,Structural basis for recruitment of CBP/p300 coactivators by STAT1 and STAT2 transactivation domains,published,journal,EMBO J.,The EMBO journal,28,7,,,,,,,,,,,,,,,,,,,,,,948,958,2009, citations,entry_citation,16015,40107,1,,entry citation,,,19214187,,,Structural basis for recruitment of CBP/p300 coactivators by STAT1 and STAT2 transactivation,published,journal,EMBO J.,The EMBO journal,28,7,,,,,,,,,,,,,,,,,,,,,,948,958,2009, citations,Citation_1,16016,40125,1,,entry citation,,,,,,Chemical shift assignment of TM0212,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,16018,40145,1,,entry citation,,,19348010,,,"Solution structure of hirsutellin A--new insights into the active site and interacting interfaces of ribotoxins",published,journal,FEBS J.,,276,8,,,,,,,,,,,,,,,,,,,,,,2381,2390,2009, citations,entry_citation,16019,40164,1,,entry citation,,,20944236,,,Comparison of NMR and crystal structures highlights conformational isomerism in protein active sites,published,journal,Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.,,66,10,,,,,,,,,,,,,,,,,,,,,,1393,1405,2010, citations,citations_1,16020,40183,1,,entry citation,,,19061899,,,Structure of Amantadine-Bound M2 Transmembrane Peptide of Influenza A in Lipid Bilayers from Magic-Angle-Spinning Solid-State NMR: the Role of Ser31 in Amantadine Binding,published,journal,J. Mol. Biol.,,385,4,,,,,,,,,,,,,,,,,,,,,,1127,1141,2009, citations,citations_2,16020,40184,2,,reference citation,,,18230730,,,Amantadine-induced conformational and dynamical changes of the influenza M2 transmembrane proton channel,published,journal,Proc. Natl. Acad. Sci. U. S. A.,,105,5,,,,,,,,,,,,,,,,,,,,,,1483,1488,2008, citations,citations_3,16020,40185,3,,reference citation,,,17705425,,,Side-Chain Conformation of the M2 Transmembrane Peptide Proton Channel of INfluenza A Virus from 19F Solid-State NMR,published,journal,J. Phys. Chem. B,,111,36,JPCBFK,1089-5647,,,,,,,,,,,,,,,,,,,,10825,10832,2007, citations,citations_4,16020,40186,4,,reference citation,,,16734478,,,Determination of the Oligomeric Number and Intermolecular Distances of Membrane Protein Assemblies by Anisotropic 1H-Drive Spin Diffusion NMR Spectroscopy,published,journal,J. Am. Chem. Soc.,,128,22,JACSAT,0002-7863,,,,,,,,,,,,,,,,,,,,7242,7251,2006, citations,entry_citation,16021,40204,1,,entry citation,,,19636950,,,NMR assignments of juvenile hormone binding protein in complex with JH III,published,journal,Biomol. NMR Assignments,,3,1,,,,,,,,,,,,,,,,,,,,,,73,76,2009, citations,entry_citation,16022,40222,1,,entry citation,,,,,,Terminal amino acid in KIA7 determines its stability,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16023,40243,1,,entry citation,,,,,,Terminal amino acid in KIA7 determines its stability,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16024,40265,1,,entry citation,,,20690702,,,"Structural and functional characterization of the ga-substituted ferredoxin from Synechocystis sp. PCC6803, a mimic of the native protein.",published,journal,Biochemistry,Biochemistry,49,36,,,,,,,,,,,,,,,,,,,,,,7790,7797,2010, citations,citations,16025,40285,1,,entry citation,,,19361445,,,"The beta-E-Domain of Wheat Ec-1 Metallothionein: A Metal-Binding Domain with a Distinctive Structure",published,journal,J. Mol. Biol.,,387,1,,,,,,,,,,,,,,,,,,,,,,207,218,2009, citations,citations,16026,40304,1,,entry citation,,,19321436,,,Enhancing the activity of a protein by stereospecific unfolding. The conformational life cycle of insulin and its evolutionary origins.,published,journal,J. Biol. Chem.,,284,21,,,,,,,,,,,,,,,,,,,,,,14586,14596,2009, citations,citations,16027,40321,1,,entry citation,,,19321436,,,Enhancing the activity of a protein by stereospecific unfolding. The conformational life cycle of insulin and its evolutionary origins,published,journal,J. Biol. Chem.,,284,21,,,,,,,,,,,,,,,,,,,,,,14586,14596,2009, citations,entry_citation,16028,40337,1,,entry citation,,,,,,Protein conformational plasticity and aggregation : transthyretin and delta-toxin as two case studies,published,journal,,,,,,,,,,,,,,,,,,,,,,,,,http://hdl.handle.net/10316/14579,,,,http://hdl.handle.net/10316/14579 citations,entry_citation,16029,40356,1,,entry citation,,,,,,Solution NMR structure of ubiquitin-like domain of Arabidopsis thaliana protein At2g32350.,in preparation,journal,Proteins: Struct. Funct. Genet.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16030,40380,1,,entry citation,,,,,,Solution structure of protein BPP2914 from Bordetella parapertussis. Northeast Structural Genomics Consortium target BpR206,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16031,40402,1,,entry citation,,,19129176,,,Solution structure of the NaV1.2 C-terminal EF-hand domain.,published,journal,J. Biol. Chem.,,284,10,,,,,,,,,,,,,,,,,,,,,,6446,6454,2009, citations,entry_citation,16032,40419,1,,entry citation,,,19129176,,,Solution structure of the NaV1.2 C-terminal EF-hand domain.,published,journal,J. Biol. Chem.,,284,10,,,,,,,,,,,,,,,,,,,,,,6446,6454,2009, citations,entry_citation,16033,40442,1,,entry citation,,,19536568,,,Solution structure and dynamics of S100A5 in the apo and Ca2+-bound states.,published,journal,J. Biol. Inorg. Chem.,Journal of biological inorganic chemistry,14,7,,,,,,,,,,,,,,,,,,,,,,1097,1107,2009, citations,entry_citation,16034,40465,1,,entry citation,,,19536568,,,Solution structure and dynamics of S100A5 in the apo and Ca2+-bound states.,published,journal,J. Biol. Inorg. Chem.,Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry,14,7,,,,,,,,,,,,,,,,,,,,,,1097,1107,2009, citations,entry_citation,16035,40490,1,,entry citation,,,19888691,10.1007/s12104-009-9175-3,,"Secondary structure and (1)H, (13)C and (15)N backbone resonance assignments of BamC, a component of the outer membrane protein assembly machinery in Escherichia coli.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,3,2,,,,,,,,,,,,,,,,,,,,,,203,206,2009, citations,entry_citation,16037,40504,1,,entry citation,,,19191473,,,Structure and Insight into Blue Light-Induced Changes in the BlrP1 BLUF Domain,published,journal,Biochemistry,,48,12,,,,,,,,,,,,,,,,,,,,,,2620,2629,2009, citations,entry_citation,16038,40526,1,,entry citation,,,19368890,,,Dynamic and Structural Characterization of a Bacterial FHA Protein Reveals a New Autoinhibition Mechanism,published,journal,Structure,,17,4,,,,,,,,,,,,,,,,,,,,,,568,578,2009, citations,entry_citation,16039,40543,1,,entry citation,,,19368890,,,Dynamic and Structural Characterization of a Bacterial FHA Protein Reveals a New Autoinhibition Mechanism,published,journal,Structure,,17,4,,,,,,,,,,,,,,,,,,,,,,568,578,2009, citations,entry_citation,16040,40558,1,,entry citation,,,19655705,,,The folding pathway of onconase is directed by a conserved intermediate,published,journal,Biochemistry,,48,35,,,,,,,,,,,,,,,,,,,,,,8449,8457,2009, citations,entry_citation,16041,40573,1,,entry citation,,,19281235,,,Hairpin Structure of a Biarsenical-Tetracysteine Motif Determined by NMR,published,journal,J. Am. Chem. Soc.,,131,13,,,,,,,,,,,,,,,,,,,,,,4613,4615,2009, citations,entry_citation,16042,40592,1,,entry citation,,,19636954,,,"Backbone and sidechain 1H, 13C and 15N resonance assignments of the human brain-type fatty acid binding protein (FABP7) in its apo form and the holo forms binding to DHA, oleic acid, linoleic acid and elaidic acid",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,3,1,,1874-2718,,,,,,,,,,,,,,,,,,,,89,93,2009, citations,entry_citation,16043,40606,1,,entry citation,,,19888688,10.1007/s12104-009-9172-6,,"(1)H, (13)C, and (15)N NMR assignments for the Bacillus subtilis yndB START domain.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,3,2,,,,,,,,,,,,,,,,,,,,,,191,194,2009, citations,entry_citation,16044,40625,1,,entry citation,,,19636961,,,Backbone assignment of the N-terminal polyomavirus large T antigen,published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,3,1,,,,,,,,,,,,,,,,,,,,,,119,123,2009, citations,entry_citation,16045,40643,1,,entry citation,,,19074138,,,"Solution NMR structure of the C-terminal EF-Hand domain of human cardiac sodium channel NaV1.5",published,journal,J. Biol. Chem.,The Journal of biological chemistry,284,10,,,,,,,,,,,,,,,,,,,,,,6436,6445,2009, citations,entry_citation,16046,40660,1,,entry citation,,,19636954,,,"Backbone and sidechain 1H, 13C and 15N resonance assignments of the human brain-type fatty acid binding protein (FABP7) in its apo form and the holo forms binding to DHA, oleic acid, linoleic acid and elaidic acid",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,3,1,,,,,,,,,,,,,,,,,,,,,,89,93,2009, citations,entry_citation,16047,40676,1,,entry citation,,,19636954,,,"Backbone and sidechain 1H, 13C and 15N resonance assignments of the human brain-type fatty acid binding protein (FABP7) in its apo form and the holo forms binding to DHA, oleic acid, linoleic acid and elaidic acid",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,3,1,,,,,,,,,,,,,,,,,,,,,,89,93,2009, citations,entry_citation,16048,40692,1,,entry citation,,,19636954,,,"Backbone and sidechain 1H, 13C and 15N resonance assignments of the human brain-type fatty acid binding protein (FABP7) in its apo form and the holo forms binding to DHA, oleic acid, linoleic acid and elaidic acid",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,3,1,,,,,,,,,,,,,,,,,,,,,,89,93,2009, citations,entry_citation,16049,40708,1,,entry citation,,,19636954,,,"Backbone and sidechain 1H, 13C and 15N resonance assignments of the human brain-type fatty acid binding protein (FABP7) in its apo form and the holo forms binding to DHA, oleic acid, linoleic acid and elaidic acid",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,3,1,,,,,,,,,,,,,,,,,,,,,,89,93,2009, citations,entry_citation,16050,40724,1,,entry citation,,,19452629,,,Solution structure of S100A1 bound to the CapZ peptide (TRTK12),published,journal,J. Mol. Biol.,Journal of Molecular Biology,386,5,,,,,,,,,,,,,,,,,,,,,,1265,1277,2009, citations,citation_1,16051,40742,1,,entry citation,,,,,,NMR structure of the OB domain of mm0293 from the archea methanosarcina mazei,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,17026,59767,1,,entry citation,,,,,,Solution NMR Structure of protein BT2368 from Bacteroides thetaiotaomicron,in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16052,40768,1,,entry citation,,,19636956,,,"NMR assignment and secondary structure of the STAS domain of Rv1739c, a putative sulfate transporter of Mycobacterium tuberculosis",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,3,1,,,,,,,,,,,,,,,,,,,,,,99,102,2009, citations,entry_citation,16053,40784,1,,entry citation,,,19140010,,,"Attachment of an NMR-invisible solubility enhancement tag (INSET) using a sortase-mediated protein ligation method",published,journal,J. Biomol. NMR,,43,3,,,,,,,,,,,,,,,,,,,,,,145,150,2009, citations,citation_1,16054,40803,1,,entry citation,,,19321501,,,Self-association of short DNA loops through minor groove C:G:G:C tetrads,published,journal,Nucleic Acids Res.,Nucleic Acids Research,37,10,,,,,,,,,,,,,,,,,,,,,,3264,3275,2009, citations,citation_1,16055,40820,1,,entry citation,,,19321501,,,Self-association of short DNA loops through minor groove C:G:G:C tetrads,published,journal,Nucleic Acids Res.,,37,10,,,,,,,,,,,,,,,,,,,,,,3264,3275,2009, citations,entry_citation,16056,40837,1,,entry citation,,,19176522,,,Structural and Functional Analysis of TM XI of the NHE1 Isoform of the Na+/H+ Exchanger,published,journal,J. Biol. Chem.,,284,17,,,,,,,,,,,,,,,,,,,,,,11546,11556,2009, citations,entry_citation,16057,40858,1,,entry citation,,,19433794,,,Structure of bacteriophage SPP1 head-to-tail connection reveals mechanism for viral DNA gating,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,106,21,,,,,,,,,,,,,,,,,,,,,,8507,8512,2009, citations,entry_citation,16058,40874,1,,entry citation,,,19196709,,,"Solution Structure of the Factor H-binding Protein, a Survival Factor and Protective Antigen of Neisseria meningitidis",published,journal,J. Biol. Chem.,The Journal of biological chemistry,284,14,,,,,,,,,,,,,,,,,,,,,,9022,9026,2009, citations,entry_citation,16059,40896,1,,entry citation,,,19636951,,,"Sequence-specific 1H N, 13C, and 15N backbone resonance assignments of the 34 kDa Paramecium bursaria Chlorella virus 1 (PBCV1) DNA ligase",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,3,1,,,,,,,,,,,,,,,,,,,,,,77,80,2009, citations,entry_citation,16060,40913,1,,entry citation,,,19447114,,,Loop 3 of Short Neurotoxin II is an Additional Interaction Site with Membrane-Bound Nicotinic Acetylcholine Receptor as Detected by Solid-State NMR Spectroscopy,published,journal,J. Mol. Biol.,Journal of Molecular Biology,390,4,,,,,,,,,,,,,,,,,,,,,,662,671,2009, citations,primary,16061,40938,1,,entry citation,,,19636963,,,"1H, 13C and 15N resonance assignments of the chaperone HybE of hydrogenase-2 from Escherichia coli",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,3,1,,,,,,,,,,,,,,,,,,,,,,129,131,2009, citations,entry_citation,16062,40959,1,,entry citation,,,19621350,,,"Molecular cold-adaptation: Comparative analysis of two homologous families of psychrophilic and mesophilic signal proteins of the protozoan ciliate, Euplotes",published,journal,IUBMB Life,,61,8,,,,,,,,,,,,,,,,,,,,,,838,845,2009, citations,entry_citation,16063,40979,1,,entry citation,,,19117955,,,Structural Basis of Focal Adhesion Localization of LIM-only Adaptor PINCH by Integrin-linked Kinase,published,journal,J. Biol. Chem.,,284,9,,,,,,,,,,,,,,,,,,,,,,5836,5844,2009, citations,entry_citation,16064,40996,1,,entry citation,,,,,,Solution NMR structure of Bacteroides fragilis protein BF1650. Northeast Structural Genomics Consortium target BfR218,in preparation,journal,Proteins: Struct. Funct. Genet.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16065,41027,1,,entry citation,,,19297318,,,"Inhibitory mechanism of E. coli RelE/RelB toxin/antitoxin module involves a helix displacement near a mRNA interferase active site",published,journal,J. Biol. Chem.,,284,21,,,,,,,,,,,,,,,,,,,,,,14628,14636,2009, citations,entry_citation,16066,41054,1,,entry citation,,,19297318,,,"Inhibitory mechanism of E. coli RelE/RelB toxin/antitoxin module involves a helix displacement near a mRNA interferase active site",published,journal,J. Biol. Chem.,,284,21,,,,,,,,,,,,,,,,,,,,,,14628,14636,2009, citations,entry_citation,16067,41077,1,,entry citation,,,19297318,,,"Inhibitory mechanism of E. coli RelE/RelB toxin/antitoxin module involves a helix displacement near a mRNA interferase active site",published,journal,J. Biol. Chem.,,284,21,,,,,,,,,,,,,,,,,,,,,,14628,14636,2009, citations,entry_citation,16068,41093,1,,entry citation,,,19433794,,,Structure of bacteriophage SPP1 head-to-tail connection reveals mechanism for viral DNA gating,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,106,21,,,,,,,,,,,,,,,,,,,,,,8507,8512,2009, citations,citation_1,16069,41113,1,,entry citation,,,19646999,,,PILZ protein structure and interactions with PILB and the FIMX EAL domain: implications for control of type IV pilus biogenesis.,published,journal,J. Mol. Biol.,Journal of molecular biology,393,4,,,,,,,,,,,,,,,,,,,,,,848,866,2009, citations,entry_citation,16070,41131,1,,entry citation,,,11786999,,,NMR solution structure of the isolated Apo Pin1 WW domain: comparison to the x-ray crystal structures of Pin1,published,journal,Biopolymers,,63,2,,,,,,,,,,,,,,,,,,,,,,111,121,2002, citations,entry_citation,16071,41152,1,,entry citation,,,19546219,,,Prion protein-detergent micelle interactions studied by NMR in solution.,published,journal,J. Biol. Chem.,,284,34,,,,,,,,,,,,,,,,,,,,,,22713,22721,2009, citations,entry_citation,16072,41166,1,,entry citation,,,,,,Solution NMR structure of SSP0047 from Staphylococcus saprophyticus. Northeast Structural Genomics Consortium Target SyR6.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,16073,41196,1,,entry citation,,,19720036,,,"Despite a conserved cystine knot motif, different cyclotides have different membrane binding modes",published,journal,Biophys. J.,,97,5,,,,,,,,,,,,,,,,,,,,,,1471,1481,2009, citations,citations,16074,41210,1,,entry citation,,,19720036,,,"Despite a conserved cystine knot motif, different cyclotides have different membrane binding modes",published,journal,Biophys. J.,,97,5,,,,,,,,,,,,,,,,,,,,,,1471,1481,2009, citations,entry_citation,16075,41224,1,,entry citation,,,19546219,,,Prion protein-detergent micelle interactions studied by NMR in solution.,published,journal,J. Biol. Chem.,,284,34,,,,,,,,,,,,,,,,,,,,,,22713,22721,2009, citations,entry_citation,16076,41238,1,,entry citation,,,19546219,,,Prion protein-detergent micelle interactions studied by NMR in solution.,published,journal,J. Biol. Chem.,,284,34,,,,,,,,,,,,,,,,,,,,,,22713,22721,2009, citations,entry_citation,16077,41252,1,,entry citation,,,19546219,,,Prion protein-detergent micelle interactions studied by NMR in solution.,published,journal,J. Biol. Chem.,,284,34,,,,,,,,,,,,,,,,,,,,,,22713,22721,2009, citations,entry_citation,16078,41266,1,,entry citation,,,19546219,,,Prion protein-detergent micelle interactions studied by NMR in solution.,published,journal,J. Biol. Chem.,,284,34,,,,,,,,,,,,,,,,,,,,,,22713,22721,2009, citations,entry_citation,16079,41280,1,,entry citation,,,19546219,,,Prion protein-detergent micelle interactions studied by NMR in solution.,published,journal,J. Biol. Chem.,,284,34,,,,,,,,,,,,,,,,,,,,,,22713,22721,2009, citations,entry_citation,16080,41294,1,,entry citation,,,19546219,,,Prion protein-detergent micelle interactions studied by NMR in solution.,published,journal,J. Biol. Chem.,,284,34,,,,,,,,,,,,,,,,,,,,,,22713,22721,2009, citations,citation_1,16147,42467,1,,entry citation,,,19888680,,,NMR assignments of oxidised thioredoxin from Plasmodium falciparum.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,3,2,,,,,,,,,,,,,,,,,,,,,,159,161,2009, citations,entry_citation,16082,41308,1,,entry citation,,,21454700,,,Molecular basis of phosphatidylinositol 4-phosphate and ARF1 GTPase recognition by the FAPP1 pleckstrin homology (PH) domain.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,286,21,,,,,,,,,,,,,,,,,,,,,,18650,18657,2011, citations,entry_citation,16083,41323,1,,entry citation,,,,,,Northeast Structural Genomics Target MrR121A,in preparation,internet,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16084,41346,1,,entry citation,,,,,,"SOLUTION STRUCTURE OF TETRATRICOPEPTIDE REPEAT DOMAIN PROTEIN SRU_0103 FROM SALINIBACTER RUBER, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET SrR115C",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,16085,41370,1,,entry citation,,,19636964,,,"1H, 15N, 13C resonance assignment of the acyl carrier protein subunit of the Saccharomyces cerevisiae fatty acid synthase",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,3,1,,,,,,,,,,,,,,,,,,,,,,133,136,2009, citations,entry_citation,16087,41384,1,,entry citation,,,19459942,,,Functional aspects of the solution structure and dynamics of PAF--a highly-stable antifungal protein from Penicillium chrysogenum,published,journal,FEBS J.,,276,10,,,,,,,,,,,,,,,,,,,,,,2875,2890,2009, citations,entry_citation,16088,41399,1,,entry citation,,,11786999,,,NMR solution structure of the isolated Apo Pin1 WW domain: comparison to the x-ray crystal structures of Pin1,published,journal,Biopolymers,,63,2,,,,,,,,,,,,,,,,,,,,,,111,121,2002, citations,entry_citation,16089,41420,1,,entry citation,,,,,,Solution NMR Structure of ribosomal protein sso0164 from Sulfolobus solfataricus,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16090,41443,1,,entry citation,,,19361528,,,NMR Structure of a Monomeric Intermediate on the Evolutionarily Optimized Assembly Pathway of a Small Trimerization Domain,published,journal,J. Mol. Biol.,,389,1,,,,,,,,,,,,,,,,,,,,,,103,114,2009, citations,entry_citation,16091,41462,1,,entry citation,,,,,,"SOLUTION STRUCTURE OF 30S RIBOSOMAL PROTEIN S8E FROM Methanothermobacter thermautotrophicus, NORTHEASTSTRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16093,41488,1,,entry citation,,,,,,"Solution structure of protein SRU_2040 from Salinibacter ruber (strain DSM 13855) . Northeast Structural Genomics Consortium target SrR106",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,16094,41511,1,,entry citation,,,19535333,,,The first gene-encoded amphibian neurotoxin.,published,journal,J. Biol. Chem.,Journal of biological chemistry,284,33,,,,,,,,,,,,,,,,,,,,,,22079,22086,2009, citations,entry_citation,16096,41528,1,,entry citation,,,,,,"SOLUTION NMR STRUCTURE OF THE OB-FOLD DOMAIN OF HEME CHAPERONE CCME FROM DESULFOVIBRIO VULGARIS. NORTHEAST STRUCTURAL GENOMICS TARGET DVR115G.",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16097,41560,1,,entry citation,,,,,,Solution NMR structure of an uncharacterized protein from Chlorobium tepidum. Northeast Structural Genomics target CtR107,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16098,41587,1,,entry citation,,,19343803,,,Solution structure of Apo-YjaB form Escherichia coli,published,journal,Proteins,,76,1,,,,,,,,,,,,,,,,,,,,,,261,265,2009, citations,entry_citation,16099,41605,1,,entry citation,,,,,,"Solution NMR Structure of Kazal-1 Domain of Human Follistatin-related protein 3 (FSTL-3). Northeast Structural Genomics Target HR6186A.",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,161,41634,1,,entry citation,,,,,"Narula, Surinder S., Dalvit, Claudio, Appleby, Cyril A., Wright, Peter E., ""NMR studies of the conformations of leghemoglobins from soybean and lupin,"" Eur. J. Biochem. 178, 419-435 (1988).",NMR studies of the conformations of leghemoglobins from soybean and lupin,published,journal,Eur. J. 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Biol.,Journal of molecular biology,386,4,,,,,,,,,,,,,,,,,,,,,,1024,1037,2009, citations,entry_citation,16104,41750,1,,entry citation,,,19244249,,,THE DYNAMIC ALPHA-HELIX STRUCTURE OF MICELLE-BOUND HUMAN AMYLIN.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,284,18,,,,,,,,,,,,,,,,,,,,,,11982,11991,2009, citations,entry_citation,16105,41766,1,,entry citation,,,19244249,,,THE DYNAMIC ALPHA-HELIX STRUCTURE OF MICELLE-BOUND HUMAN AMYLIN.,published,journal,J. Biol. Chem.,,284,18,,,,,,,,,,,,,,,,,,,,,,11982,11991,2009, citations,entry_citation,16107,41782,1,,entry citation,,,,,,Solution NMR structure of F5/8 type C-terminal domain of a putative chitobiase from Bacteroides thetaiotaomicron.,in preparation,journal,Proteins: Struct. Funct. Genet.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16108,41814,1,,entry citation,,,19636959,,,Backbone and side-chain assignment of the lipidated and non-lipidated forms of the meningococcal outer membrane protein LP2086,published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,3,1,,,,,,,,,,,,,,,,,,,,,,111,113,2009, citations,entry_citation,16109,41829,1,,entry citation,,,,,,"Structure of human homocysteine-inducible, endoplasmic reticulum stress-inducible, ubiquitin-like domain member 2 (Herpud2 or Herp)",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16110,41854,1,,entry citation,,,19530738,,,Phosphorylation of a Borealin dimerization domain is required for proper chromosome segregation,published,journal,Biochemistry,,48,29,,,,,,,,,,,,,,,,,,,,,,6783,6793,2009, citations,Citation_1,16111,41878,1,,entry citation,,,19636957,10.1007/s12104-009-9151-y,,"Sequence-specific 1H, 15N and 13C resonance assignments of Art v 1: a proline-rich allergen of Artemisia vulgaris pollen",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,3,1,,,,,,,,,,,,,,,,,,,,,,103,106,2009, citations,entry_citation,16112,41895,1,,entry citation,,,19456106,,,Solution Structure of the HsapBK K(+) Channel Voltage-Sensor Paddle Sequence,published,journal,Biochemistry,,48,50,,,,,,,,,,,,,,,,,,,,,,5813,5821,2009, citations,entry_citation,16113,41909,1,,entry citation,,,,,,Solution NMR Structure of Protein yppE from Bacillus subtilis. Northeast Structural Genomics Consortium Target SR213,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16114,41928,1,,entry citation,,,20053359,,,Conformational dynamics and structural plasticity play critical roles in the ubiquitin recognition of a UIM domain.,published,journal,J. Mol. 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Mol. Biol.,Journal of molecular biology,396,4,,,,,,,,,,,,,,,,,,,,,,1053,1069,2010, citations,entry_citation,16120,42045,1,,entry citation,,,19636965,,,"Sequence-specific 1H, 13C, and 15N resonance assignment of the autophagy-related protein Atg8",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,3,1,,,,,,,,,,,,,,,,,,,,,,137,139,2009, citations,entry_citation,16121,42063,1,,entry citation,,,19432457,,,"Structure, Stability, and Flexibility of Ribosomal Protein L14e from Sulfolobus solfataricus",published,journal,Biochemistry,,48,24,,,,,,,,,,,,,,,,,,,,,,5553,5562,2009, citations,NS4B(227-254),16122,42085,1,,entry citation,,,19357161,,,Identification of a Novel Determinant for Membrane Association in Hepatitis C Virus Nonstructural Protein 4B,published,journal,J. Virol,Journal of virology,83,12,,,,,,,,,,,,,,,,,,,,,,6257,6268,2009, citations,entry_citation,16123,42099,1,,entry citation,,,,,,Increased fluctuations and local structural reorganization triggered by the ionization of an internal lysine,in preparation,journal,Protein Sci.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16124,42113,1,,entry citation,,,19636968,,,"1H, 13C and 15N resonance assignments of RNA pyrophosphohydrolase RppH from Escherichia coli",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,3,1,,,,,,,,,,,,,,,,,,,,,,149,151,2009, citations,entry_citation,16126,42131,1,,entry citation,,,19621959,,,"Structure of a nickel chaperone, HypA, from Helicobacter pylori reveals two distinct metal binding sites",published,journal,J. Am. Chem. Soc.,,131,29,,,,,,,,,,,,,,,,,,,,,,10031,10040,2009, citations,entry_citation,16127,42148,1,,entry citation,,,19223330,,,Solution Structure of a Novel Zinc Finger Motif in the SAP30 Polypeptide of the Sin3 Corepressor Complex and its Potential Role in Nucleic Acid Recognition,published,journal,Nucleic Acids Res.,Nucleic acids research,37,7,,,,,,,,,,,,,,,,,,,,,,2145,2152,2009, citations,entry_citation,16129,42171,1,,entry citation,,,19387844,,,The NMR structure of the TC10 and Cdc42 interacting domain of CIP4,published,journal,J. Biomol. NMR,,44,2,,,,,,,,,,,,,,,,,,,,,,113,118,2009, citations,entry_citation,16130,42191,1,,entry citation,,,19306883,,,A common interaction for the entry of colicin N and filamentous phage into Escherichia Coli,published,journal,J. Mol. Biol.,Journal of molecular biology,388,4,,,,,,,,,,,,,,,,,,,,,,880,893,2009, citations,entry_citation,16131,42207,1,,entry citation,,,19306883,,,A common interaction for the entry of colicin N and filamentous phage into Escherichia coli,published,journal,J. Mol. Biol.,Journal of molecular biology,388,4,,,,,,,,,,,,,,,,,,,,,,880,893,2009, citations,entry_citation,16133,42222,1,,entry citation,,,19306883,,,A common interaction for the entry of colicin N and filamentous phage into Escherichia coli,published,journal,J. Mol. Biol.,Journal of molecular biology,388,4,,,,,,,,,,,,,,,,,,,,,,880,893,2009, citations,entry_citation,16134,42237,1,,entry citation,,,19306883,,,A common interation for the entry of colicin N and filamentous phage into Escherichia Coli,published,journal,J. Mol. Biol.,Journal of Molecular Biology,388,4,,,,,,,,,,,,,,,,,,,,,,880,893,2009, citations,entry_citation,16135,42253,1,,entry citation,,,19636967,,,"Sequence-specific 1H, 15N and 13C resonance assignments of the 23.7-kDa homodimeric toxin CcdB from Vibrio fischeri",published,journal,Biomol. NMR Assignments,Biomolcular NMR Assignments,3,1,,,,,,,,,,,,,,,,,,,,,,145,147,2009, citations,citation_1,16136,42270,1,,entry citation,,,21656569,,,"NMR structure and dynamics of recombinant wild type and mutated jerdostatin, a selective inhibitor of integrin alpha(1)beta(1).",published,journal,Proteins,Proteins,79,8,,,,,,,,,,,,,,,,,,,,,,2530,2542,2011, citations,entry_citation,16137,42287,1,,entry citation,,,,,,NMR structure of the first SAM domain from AIDA1,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16138,42303,1,,entry citation,,,21124482,,,Solution structure of a DNA double helix with consecutive metal-mediated base pairs,published,journal,Nat. 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NMR Assignments,Biomolecular NMR assignments,3,2,,,,,,,,,,,,,,,,,,,,,,163,166,2009, citations,citations,16145,42432,1,,entry citation,,,19551879,,,Monomeric structure of the cardioprotective chemokine SDF-1/CXCL12,published,journal,Protein Sci.,,18,7,,,,,,,,,,,,,,,,,,,,,,1359,1369,2009, citations,entry_citation,16146,42450,1,,entry citation,,,19888679,,,Backbone resonance assignment of Staphylococcal Enterotoxin H.,published,journal,Biomol. 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Biol.,Journal of molecular biology,394,5,,,,,,,,,,,,,,,,,,,,,,944,956,2009, citations,citation_1,16164,42827,1,,entry citation,,,19747550,,,"Structure of the Pseudomonas aeruginosa XcpT pseudopilin, a major component of the type II secretion system.",published,journal,J. Struct. Biol.,Journal of structural biology,169,1,,,,,,,,,,,,,,,,,,,,,,75,80,2010, citations,entry_citation,16165,42855,1,,entry citation,,,19297321,,,Hepatitis C Virus NS5A protein is a substrate for the Peptidyl-Prolyl cis/trans Isomerase activity of Cyclophilins A and B.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,,,,,,,,,,,,,,,,,,,,,,,,,,2009, citations,entry_citation,16166,42870,1,,entry citation,,,19249289,,,Domain 3 of non structural protein 5A from hepatitis C virus is natively unfolded,published,journal,Biochem. Biophys. Res. Commun.,Biochemical and biophysical research communications,,,,,,,,,,,,,,,,,,,,,,,,634,638,2009, citations,entry_citation,16167,42885,1,,entry citation,,,17567018,,,Structural similarity of a membrane protein in micelles and membranes.,published,journal,J. Am. Chem. Soc.,,129,26,,,,,,,,,,,,,,,,,,,,,,8078,8079,2007, citations,citations,16168,42901,1,,entry citation,,,17511473,,,"Structure of the Na,K-ATPase regulatory protein FXYD1 in micelles.",published,journal,Biochemistry,,46,23,BICHAW,0006-2960,,,,,,,,,,,,,,,,,,,,6774,6783,2007, citations,entry_citation,16169,42919,1,,entry citation,,,19720037,,,Pressure-dependent structure changes in barnase on ligand binding reveal intermediate rate fluctuations,published,journal,Biophys. J.,,97,5,,,,,,,,,,,,,,,,,,,,,,1482,1490,2009, citations,entry_citation,16170,42933,1,,entry citation,,,19720037,,,Pressure-dependent structure changes in barnase on ligand binding reveal intermediate rate fluctuations,published,journal,Biophys. J.,,97,5,,,,,,,,,,,,,,,,,,,,,,1482,1490,2009, citations,entry_citation,16171,42947,1,,entry citation,,,19720037,,,Pressure-dependent structure changes in barnase on ligand binding reveal intermediate rate fluctuations,published,journal,Biophys. J.,,97,5,,,,,,,,,,,,,,,,,,,,,,1482,1490,2009, citations,entry_citation,16172,42961,1,,entry citation,,,19720037,,,Pressure-dependent structure changes in barnase on ligand binding reveal intermediate rate fluctuations,published,journal,Biophys. J.,,97,5,,,,,,,,,,,,,,,,,,,,,,1482,1490,2009, citations,entry_citation,16173,42975,1,,entry citation,,,19216553,,,The structure of the cataract causing P23T mutant of HgD crystallin exhibits local distinctive conformational and dynamic changes.,published,journal,Biochemistry,Biochemistry,48,12,,,,,,,,,,,,,,,,,,,,,,2597,2609,2009, citations,Citation,16174,42995,1,,entry citation,,,19888683,10.1007/s12104-009-9167-3,,"(15)N, (13)C and (1)H resonance assignments and secondary structure determination of the Mycobacterium tuberculosis Rv0287-Rv0288 protein complex.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,3,2,,,,,,,,,,,,,,,,,,,,,,171,174,2009, citations,entry_citation,16175,43019,1,,entry citation,,,19888689,,,"(1)H, (15)N, and (13)C chemical shift assignments of the mosquito odorant binding protein-1 (CquiOBP1) bound to the mosquito oviposition pheromone.",published,journal,Biomol NMR Assign,Biomolecular NMR assignments,3,2,,,,,,,,,,,,,,,,,,,,,,195,197,2009, citations,Prp40_FF4_domain,16176,43033,1,,entry citation,,,19722265,,,Solution structure of the fourth FF domain of yeast Prp40 splicing factor.,published,journal,Proteins,Proteins,77,4,,,,,,,,,,,,,,,,,,,,,,1000,1003,2009, citations,entry_citation,16200,43542,1,,entry citation,,,19361520,,,Probing the interactions of early polyketide intermediates with the actinorhodin ACP from S. coelicolor A3(2),published,journal,J. Mol. Biol.,Journal of Molecular Biology,389,3,,,,,,,,,,,,,,,,,,,,,,511,528,2009, citations,E73_citations,16177,43053,1,,entry citation,,,19888695,,,"(1)H, (13)C, (15)N backbone and side chain NMR resonance assignments for E73 from Sulfolobus spindle-shaped virus ragged hills, a hyperthermophilic crenarchaeal virus from Yellowstone National Park.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,3,2,,,,,,,,,,,,,,,,,,,,,,219,222,2009, citations,entry_citation,16178,43070,1,,entry citation,,,20097251,,,Characterization of two linear cationic antimalarial peptides in the scorpion Mesobuthus eupeus,published,journal,Biochimie,,92,4,,,,,,,,,,,,,,,,,,,,,,350,359,2010, citations,entry_citation,16179,43087,1,,entry citation,,,19798736,,,"Structural insight into the interaction of proteins containing NPF, DPF, and GPF motifs with the C-terminal EH-domain of EHD1",published,journal,Protein Sci.,Protein science : a publication of the Protein Society,18,12,,,,,,,,,,,,,,,,,,,,,,2471,2479,2009, citations,entry_citation,16180,43108,1,,entry citation,,,19798736,,,"Structural insight into the interaction of proteins containing NPF, DPF, and GPF motifs with the C-terminal EH-domain of EHD1.",published,journal,Protein Sci.,Protein science : a publication of the Protein Society,18,12,,,,,,,,,,,,,,,,,,,,,,2471,2479,2009, citations,entry_citation,16181,43129,1,,entry citation,,,19798736,,,"Structural insight into the interaction of proteins containing NPF, DPF, and GPF motifs with the C-terminal EH-domain of EHD1.",published,journal,Protein Sci.,Protein science : a publication of the Protein Society,18,12,,,,,,,,,,,,,,,,,,,,,,2471,2479,2009, citations,citation_primary,16182,43150,1,,entry citation,,,20715266,,,"Solution structure of the leader sequence of the patellamide precursor peptide, PatE1-34.",published,journal,Chembiochem,Chembiochem : a European journal of chemical biology,11,13,,,,,,,,,,,,,,,,,,,,,,1867,1873,2010, citations,citations,16183,43165,1,,entry citation,,,19393664,,,Prion protein NMR structure from tammar wallaby (Macropus eugenii) shows that the beta2-alpha2 loop is modulated by long-range sequence effects.,published,journal,J. Mol. Biol.,Journal of molecular biology,389,5,,,,,,,,,,,,,,,,,,,,,,833,845,2009, citations,citations,16184,43187,1,,entry citation,,,19393664,,,Prion Protein NMR Structure from Tammar Wallaby (Macropus eugenii) Shows that the beta2-alpha2 Loop Is Modulated by Long-Range Sequence Effects,published,journal,J. Mol. Biol.,,,,,,,,,,,,,,,,,,,,,,,,,,,2009, citations,citations,16185,43209,1,,entry citation,,,19393664,,,Prion Protein NMR Structure from Tammar Wallaby (Macropus eugenii) Shows that the beta2-alpha2 Loop Is Modulated by Long-Range Sequence Effects,published,journal,J. Mol. Biol.,,,,,,,,,,,,,,,,,,,,,,,,,,,2009, citations,entry_citation,16186,43230,1,,entry citation,,,,,,Solution NMR structure of PSPTO_3016 from Pseudomonas syringae. Northeast Structural Genomics Consortium target PsR293.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation1,16187,43280,1,,entry citation,,,19292861,,,"Solubility-dependent structural formation of a 25-residue natively unfolded protein, induced by addition of a seven-residue peptide fragment",published,journal,FEBS J.,The FEBS Journal,276,8,,,,,,,,,,,,,,,,,,,,,,2336,2347,2009, citations,entry_citation,16188,43296,1,,entry citation,,,19457863,,,The Mycobacterium tuberculosis Ser/Thr kinase substrate Rv2175c is a DNA-binding protein regulated by phosphorylation,published,journal,J. Biol. Chem.,,284,29,,,,,,,,,,,,,,,,,,,,,,19290,19300,2009, citations,entry_citation,16189,43316,1,,entry citation,,,,,,Structure of the N-terminal domain of FK506-binding protein 3.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation,16190,43334,1,,entry citation,,,19419198,,,Structure of the inhibitor w7 bound to the regulatory domain of cardiac troponin C,published,journal,Biochemistry,,48,24,,,,,,,,,,,,,,,,,,,,,,5541,5552,2009, citations,1MXL,16190,43335,2,,reference citation,,,10387074,,,Binding of cardiac troponin-I147-163 induces a structural opening in human cardiac troponin-C,published,journal,Biochemistry,,38,26,,,,,,,,,,,,,,,,,,,,,,8289,8298,1999, citations,1LXF,16190,43336,3,,reference citation,,,12060657,,,Structure of the regulatory N-domain of human cardiac troponin C in complex with human cardiac troponin I147-163 and bepridil.,published,journal,Biochemistry,,277,34,,,,,,,,,,,,,,,,,,,,,,31124,31133,2002, citations,entry_citation,16191,43357,1,,entry citation,,,19636966,,,NMR-assignments of a cytosolic domain of the C-terminus of polycystin-2,published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,3,1,,,,,,,,,,,,,,,,,,,,,,141,144,2009, citations,entry_citation,16192,43374,1,,entry citation,,,20526337,,,Structural basis of G-tract recognition and encaging by hnRNP F quasi-RRMs.,published,journal,Nat. Struct. Mol. Biol.,Nature structural & molecular biology,17,7,,,,,,,,,,,,,,,,,,,,,,853,861,2010, citations,entry_citation,16193,43392,1,,entry citation,,,20526337,,,Structural basis of G-tract recognition and encaging by hnRNP F quasi-RRMs.,published,journal,Nat. Struct. Mol. Biol.,Nature structural and molecular biology,17,7,,,,,,,,,,,,,,,,,,,,,,853,861,2010, citations,entry_citation,16194,43412,1,,entry citation,,,20526337,,,Structural basis of G-tract recognition and encaging by hnRNP F quasi-RRMs.,published,journal,Nat. Struct. Mol. Biol.,Nature structural and molecular biology,17,7,,,,,,,,,,,,,,,,,,,,,,853,861,2010, citations,entry_citation,16195,43432,1,,entry citation,,,19888694,,,Resonance assignments of the human AKAP13-PH domain and stabilizing DH helix,published,journal,Biomol. NMR Assignments,,3,2,,,,,,,,,,,,,,,,,,,,,,215,218,2009, citations,Citation_1,16196,43448,1,,entry citation,,,19361520,,,Probing the interactions of early polyketide intermediates with the actinorhodin ACP from S. coelicolor A3(2),published,journal,J. Mol. Biol.,Journal of Molecular Biology,389,3,,,,,,,,,,,,,,,,,,,,,,511,528,2009, citations,entry_citation,16197,43466,1,,entry citation,,,19361520,,,Probing the interactions of early polyketide intermediates with the actinorhodin ACP from S. coelicolor A3(2),published,journal,J. Mol. 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Biol.,Journal of Molecular Biology,389,3,,,,,,,,,,,,,,,,,,,,,,511,528,2009, citations,entry_citation,16204,43613,1,,entry citation,,,19921465,,,"Backbone resonance assignments for the ligand binding subunit of the histidine permease complex (HisJ) from Escherichia coli, under histidine-bound and unbound states.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,1,,,,,,,,,,,,,,,,,,,,,,17,20,2010, citations,entry_citation,16205,43629,1,,entry citation,,,19921465,,,"Backbone resonance assignments for the ligand binding subunit of the histidine permease complex (HisJ) from Escherichia coli, under histidine-bound and unbound states.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,1,,,,,,,,,,,,,,,,,,,,,,17,20,2010, citations,citations,16206,43643,1,,entry citation,,,19295135,,,The RRM Domain in GW182 Proteins Contributes to miRNA-mediated gene silencing,published,journal,Nucleic Acids Res.,Nucleic Acids Research,37,9,,,,,,,,,,,,,,,,,,,,,,2974,2983,2009, citations,entry_citation,16207,43659,1,,entry citation,,,20828160,,,NmerA of Tn501 Mercuric Ion Reductase: Structural Modulation of the pK(a) Values of the Metal Binding Cysteine Thiols .,published,journal,Biochemistry,Biochemistry,49,41,,,,,,,,,,,,,,,,,,,,,,8988,8998,2010, citations,entry_citation,16208,43673,1,,entry citation,,,20828160,,,NmerA of Tn501 Mercuric Ion Reductase: Structural Modulation of the pK(a) Values of the Metal Binding Cysteine Thiols,published,journal,Biochemistry,Biochemistry,49,41,,,,,,,,,,,,,,,,,,,,,,8988,8998,2010, citations,citations,16209,43689,1,,entry citation,,,19430464,,,Haematopoietic malignancies caused by dysregulation of a chromatin-binding PHD finger,published,journal,Nature,,459,,,,,,,,,,,,,,,,,,,,,,,847,851,2009, citations,citations,16210,43707,1,,entry citation,,,19430464,,,Haematopoietic malignancies caused by dysregulation of a chromatin-binding PHD finger,published,journal,Nature,,459,,,,,,,,,,,,,,,,,,,,,,,847,851,2009, citations,entry_citation,16211,43728,1,,entry citation,,,19866485,,,The prolyl isomerase domain of PpiD from Escherichia coli shows a parvulin fold but is devoid of catalytic activity.,published,journal,Protein Sci.,Protein science: a publication of the Protein Society,19,1,,,,,,,,,,,,,,,,,,,,,,6,18,2010, citations,citation_1,16212,43742,1,,entry citation,,,19321501,,,Self-association of short DNA loops through minor groove C:G:G:C tetrads,published,journal,Nucleic Acids Res.,Nucleic acids research,37,10,,,,,,,,,,,,,,,,,,,,,,3264,3275,2009, citations,citation_1,16213,43759,1,,entry citation,,,20506034,,,NMR structure note: solution structure of the core domain of MESD that is essential for proper folding of LRP5/6.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,47,4,,,,,,,,,,,,,,,,,,,,,,283,288,2010, citations,entry_citation,16214,43773,1,,entry citation,,,,,,Zn-finger protein YBIL from E. Coli,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,new_citation,16215,43799,1,,entry citation,,,23349025,,,Temperature-dependent conformational change affecting Tyr11 and sweetness loops of brazzein.,published,journal,Proteins,Proteins,81,6,,,,,,,,,,,,,,,,,,,,,,919,925,2013, citations,entry_citation,16216,43821,1,,entry citation,,,,,,Solution structure of protein ITSN1 from Homo sapiens. Northeast Structural Genomics Consortium target HR5524A,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16217,43845,1,,entry citation,,,,,,Backbone Dynamics of a Large Chaperone-Free and Chaperone-Bound Hsp70 Substrate,submitted,journal,Arch. Biochem. Biophys.,Archives of Biochemistry and Biophysics,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16218,43861,1,,entry citation,,,,,,Backbone Dynamics of a Large Chaperone-Free and Chaperone-Bound Hsp70 Substrate,submitted,journal,Arch. Biochem. Biophys.,Archives of Biochemistry and Biophysics,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,16219,43878,1,,entry citation,,,19401189,,,Structural basis of the auto-inhibition mechanism of nonreceptor tyrosine kinase PTK6.,published,journal,Biochem. Biophys. Res. Commun.,Biochemical and biophysical research communications,384,2,,,,,,,,,,,,,,,,,,,,,,236,242,2009, citations,citation1,16221,43900,1,,entry citation,,,19459623,,,Nuclear magnetic resonance mapping and functional confirmation of the collagen binding sites of matrix metalloproteinase-2,published,journal,Biochemistry,Biochemistry,,48,25,1520-4995,,,,,,,,,,,,,,,,,,,,5822,5831,2009, citations,citations,16222,43918,1,,entry citation,,,19831353,,,Structural perturbations induced by the alpha-anomer of the aflatoxin B(1) formamidopyrimidine adduct in duplex and single-strand DNA.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,131,44,,,,,,,,,,,,,,,,,,,,,,16096,16107,2009, citations,entry_citation,16223,43941,1,,entry citation,,,19831353,,,Structural perturbations induced by the alpha-anomer of the aflatoxin B(1) formamidopyrimidine adduct in duplex and single-strand DNA.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,131,44,,,,,,,,,,,,,,,,,,,,,,16096,16107,2009, citations,entry_citation,16225,43962,1,,entry citation,,,19892827,,,"Binding of the human nucleotide excision repair proteins XPA and XPC/HR23B to the 5R-thymine glycol lesion and structure of the cis-(5R,6S) thymine glycol epimer in the 5'-GTgG-3' sequence: destabilization of two base pairs at the lesion site",published,journal,Nucleic Acids Res.,,38,2,,,,,,,,,,,,,,,,,,,,,,428,440,2010, citations,entry_citation,16226,43987,1,,entry citation,,,19772348,,,"The cis-(5R,6S)-thymine glycol lesion occupies the wobble position when mismatched with deoxyguanosine in DNA.",published,journal,Biochemistry,Biochemistry,48,41,,,,,,,,,,,,,,,,,,,,,,9722,9733,2009, citations,entry_citation,16228,44012,1,,entry citation,,,19597942,,,Automated NMR structure determination of stereo-array isotope labeled ubiquitin from minimal sets of spectra using the SAIL-FLYA system,published,journal,J. Biomol. NMR.,,44,4,,,,,,,,,,,,,,,,,,,,,,261,272,2009, citations,entry_citation,16229,44027,1,,entry citation,,,20696397,,,Polycomb group targeting through different binding partners of RING1B C-terminal domain.,published,journal,Structure,"Structure (London, England : 1993)",18,8,,,,,,,,,,,,,,,,,,,,,,966,975,2010, citations,Peak_Assignment,16230,44047,1,,entry citation,,,19693704,,,"(1)H, (13)C and (15)N resonance assignments of a ribonucleoprotein complex consisting of Prp24-RRM2 bound to a fragment of U6 RNA.",published,journal,Biomol NMR Assign,Biomolecular NMR assignments,3,2,,,,,,,,,,,,,,,,,,,,,,227,230,2009, citations,entry_citation,16231,44077,1,,entry citation,,,,,,"Solution Structure of a Pathogen Recognition Domain from a Lepidopteran Insect, Plodia interpunctella",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref3,4452,200844,4,,reference citation,,,,,"Delagio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J. and Bax, A. (1995) J. Biomol. NMR, 6, 277-293",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16233,44091,1,,entry citation,,,19888684,,,"Complete NMR assignments for the second microneme adhesive repeat (MAR) domain from Eimeria tenella microneme protein EtMIC3",published,journal,Biomol. NMR Assign.,,3,2,,,,,,,,,,,,,,,,,,,,,,175,177,2009, citations,reference_citation,16233,44092,2,,reference citation,,,15694485,,,"Eimeria tenella microneme protein EtMIC3: identification, localisation and role in host cell infection.",published,journal,Mol. Biochem. Parasitol.,,140,1,,,,,,,,,,,,,,,,,,,,,,43,53,2005, citations,entry_citation,16234,44109,1,,entry citation,,,19527730,,,NMR structure of the N-terminal domain of capsid protein from the Mason-Pfizer monkey virus,published,journal,J. Mol. Biol.,,392,1,,,,,,,,,,,,,,,,,,,,,,100,114,2009, citations,entry_citation,16235,44124,1,,entry citation,,,19491108,,,The biological activity of the prototypic cyclotide kalata b1 is modulated by the formation of multimeric pores.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,284,31,,,,,,,,,,,,,,,,,,,,,,20699,20707,2009, citations,entry_citation,16236,44138,1,,entry citation,,,19919093,,,Bruno protein contains an expanded RNA recognition motif,published,journal,Biochemistry,Biochemistry,48,51,,,,,,,,,,,,,,,,,,,,,,12202,12212,2009, citations,entry_citation,16237,44152,1,,entry citation,,,21117233,,,Structure of the Mycobacterium tuberculosis OmpATb protein: a model of an oligomeric channel in the mycobacterial cell wall.,published,journal,Proteins,Proteins,79,2,,,,,,,,,,,,,,,,,,,,,,645,661,2011, citations,entry_citation,16238,44174,1,,entry citation,,,,,,Solution NMR structure of VC_A0919 from Vibrio cholerae. Northeast Structural Genomics Consortium Target VcR52.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16239,44201,1,,entry citation,,,19538999,,,Three-dimensional structure of the two-peptide bacteriocin plantaricin JK,published,journal,Peptides,,30,9,,,,,,,,,,,,,,,,,,,,,,1613,1621,2009, citations,entry_citation,1624,44222,1,,entry citation,,,,,"Pelton, J.G., Torchia, Dennis A., Meadow, Norman D., Wong, Cing-Yuen, Roseman, Saul, ""Secondary structure of the phosphocarrier protein III(Glc), a signal-transducing protein from Escherichia coli, determined by heteronuclear three-dimensional NMR spectroscopy,"" Proc. Natl. Acad. Sci. U.S.A. 88, 3479-3483 (1991).","Secondary structure of the phosphocarrier protein III(Glc), a signal-transducing protein from Escherichia coli, determined by heteronuclear three-dimensional NMR spectroscopy",published,journal,Proc. Natl. Acad. Sci. U.S.A.,,88,,,,,,,,,,,,,,,,,,,,,,,3479,3483,1991, citations,entry_citation,16240,44235,1,,entry citation,,,19760519,,,Resonance assignment of SlyD from E. coli,published,journal,Biomol. NMR Assignments,,3,2,,,,,,,,,,,,,,,,,,,,,,235,237,2009, citations,entry_citation,16241,44256,1,,entry citation,,,19538999,,,Three-dimensional structure of the two-peptide bacteriocin plantaricin JK,published,journal,Peptides,,30,9,,,,,,,,,,,,,,,,,,,,,,1613,1621,2009, citations,entry_citation,16243,44276,1,,entry citation,,,19693704,,,"(1)H, (13)C and (15)N resonance assignments of a ribonucleoprotein complex consisting of Prp24-RRM2 bound to a fragment of U6 RNA.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,3,2,,,,,,,,,,,,,,,,,,,,,,227,230,2009, citations,entry_citation,16244,44293,1,,entry citation,,,19693704,,,"(1)H, (13)C and (15)N resonance assignments of a ribonucleoprotein complex consisting of Prp24-RRM2 bound to a fragment of U6 RNA.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,3,2,,,,,,,,,,,,,,,,,,,,,,227,230,2009, citations,entry_citation,16245,44311,1,,entry citation,,,15153099,,,Bacterial IscU is a well folded and functional single domain protein.,published,journal,Eur. J. Biochem.,,271,11,,,,,,,,,,,,,,,,,,,,,,2093,2100,2004, citations,entry_citation,16246,44329,1,,entry citation,,,19693704,,,"(1)H, (13)C and (15)N resonance assignments of a ribonucleoprotein complex consisting of Prp24-RRM2 bound to a fragment of U6 RNA.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,3,2,,,,,,,,,,,,,,,,,,,,,,227,230,2009, citations,citations,16247,44346,1,,entry citation,,,19820091,,,"Solution structure, determined by nuclear magnetic resonance, of the b30-82 domain of subunit b of Escherichia coli F1Fo ATP synthase.",published,journal,J. Bacteriol.,Journal of bacteriology,191,24,,,,,,,,,,,,,,,,,,,,,,7538,7544,2009, citations,entry_citation,16248,44363,1,,entry citation,,,19318624,,,An intramolecular switch regulates phosphoindependent FHA domain interactions in Mycobacterium tuberculosis,published,journal,Sci. Signal,,2,63,,,,,,,,,,,,,,,,,,,,,,,,2009, citations,entry_citation,16249,44380,1,,entry citation,,,20463741,,,A conserved spider silk domain acts as a molecular switch that controls fibre assembly.,published,journal,Nature,Nature,465,7295,,,,,,,,,,,,,,,,,,,,,,239,242,2010, citations,entry_citation,16250,44404,1,,entry citation,,,,,,NMR solution structure of the EH 1 domain from human intersectin-1 protein. Northeast Structural Genomics Consortium target HR3646e.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16251,44431,1,,entry citation,,,,,,Solution NMR structure of a phage integrase SSP1947 fragment 59-159 from Staphylococcus saprophyticus,in preparation,journal,Proteins: Struct. Funct. Genet.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16252,44459,1,,entry citation,,,19888690,,,"(1)H, (15)N, and (13)C chemical shift assignments of mouse HOXA13 DNA binding domain.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,3,2,,,,,,,,,,,,,,,,,,,,,,199,201,2009, citations,entry_citation,16253,44473,1,,entry citation,,,20434955,,,Solution structure of Rv2377c-founding member of the MbtH-like protein family.,published,journal,Tuberculosis (Edinb),"Tuberculosis (Edinburgh, Scotland)",90,4,,,,,,,,,,,,,,,,,,,,,,245,251,2010, citations,entry_citation,16254,44494,1,,entry citation,,,19963419,,,3D (13)C-(13)C-(13)C correlation NMR for de novo distance determination of solid proteins and application to a human alpha-defensin.,published,journal,J. Magn. Reson.,"Journal of magnetic resonance (San Diego, Calif. : 1997)",202,2,,,,,,,,,,,,,,,,,,,,,,203,210,2010, citations,entry_citation,16255,44513,1,,entry citation,,,,,,Solution Structure Of Protein Nmul_A0922 From Nitrosospira multiformis. Northeast Structural Genomics Consortium Target Hr5524a.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16256,44538,1,,entry citation,,,20226070,,,Solution structure of the Drosha double-stranded RNA-binding domain,published,journal,Silence,,1,2,,,,,,,,,,,,,,,,,,,,,,2,,2010, citations,entry_citation,16257,44555,1,,entry citation,,,20351248,,,"Protein folding at the membrane interface, the structure of Nogo-66 requires interactions with a phosphocholine surface.",published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,107,15,,,,,,,,,,,,,,,,,,,,,,6847,6851,2010, citations,citations,16258,44569,1,,entry citation,,,19720067,,,"Solution structure of RCL, a novel 2'-deoxyribonucleoside 5'-monophosphate N-glycosidase.",published,journal,J. Mol. Biol.,Journal of molecular biology,394,3,,,,,,,,,,,,,,,,,,,,,,423,434,2009, citations,entry_citation,16259,44593,1,,entry citation,,,19843520,,,Beta integrin tyrosine phosphorylation is a conserved mechanism for regulating talin-induced integrin activation.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,284,52,,,,,,,,,,,,,,,,,,,,,,36700,36710,2009, citations,citations,16260,44614,1,,entry citation,,,19774494,,,NMR assignments of the FK506-binding domain of FK506-binding protein 35 from Plasmodium vivax,published,journal,Biomol. NMR Assignments,,3,2,,,,,,,,,,,,,,,,,,,,,,243,245,2009, citations,citation_1,16261,44629,1,,entry citation,,,19888687,10.1007/s12104-009-9171-7,,"(1)H, (15)N and (13)C assignments of the Rhipicephalus (Boophilus) microplus anti-microbial peptide microplusin.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,3,2,,,,,,,,,,,,,,,,,,,,,,187,189,2009, citations,entry_citation,16262,44649,1,,entry citation,,,,,,The N-terminal domain of the p68 subunit tethers DNA polymerase alpha-primase to a replicative helicase for primosome function,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,Citation_NLRP7_Pyd,16263,44664,1,,entry citation,,,19888692,10.1007/s12104-009-9176-2,,"Backbone and sidechain (1)H, (15)N and (13)C assignments of the NLRP7 pyrin domain.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,3,2,,,,,,,,,,,,,,,,,,,,,,207,209,2009, citations,citations,16264,44681,1,,entry citation,,,,,,,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16265,44702,1,,entry citation,,,19459661,,,Redox Dependent Dynamics of a Dual Thioredoxin-Fold Protein: Evolution of Specialized Folds,published,journal,Biochemistry,Biochemistry,48,25,,,,,,,,,,,,,,,,,,,,,,5984,5993,2009, citations,entry_citation,16266,44717,1,,entry citation,,,19733182,,,Solution structure of an archaeal RNase P binary protein complex: formation of the 30-kDa complex between Pyrococcus furiosus RPP21 and RPP29 is accompanied by coupled protein folding and highlights critical features for protein-protein and protein-RNA interactions.,published,journal,J. Mol. Biol.,Journal of molecular biology,393,5,,,,,,,,,,,,,,,,,,,,,,1043,1055,2009, citations,entry_citation,16267,44745,1,,entry citation,,,,,,Solution NMR structure of tungsten formylmethanofuran dehydrogenase subunit D from Archaeoglobus fulgidus,in preparation,journal,Proteins: Struct. Funct. Genet.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16268,44780,1,,entry citation,,,19397896,,,"Structural biology of human cannabinoid receptor-2 helix 6 in membranemimetic environments",published,journal,Biochem. Biophys. Res. Commun.,Biochemical and Biophysical Research Communications,384,2,,,,,,,,,,,,,,,,,,,,,,243,248,2009, citations,entry_citation,16269,44796,1,,entry citation,,,,,,Biological activity and solution structure of the apo-dinitrogenase binding domain of NafY,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,16270,44811,1,,entry citation,,,19592495,,,The structure of the Staphylococcus aureus sortase-substrate complex reveals how the universally conserved LPXTG sorting signal is recognized,published,journal,J. Biol. Chem.,,284,36,,,,,,,,,,,,,,,,,,,,,,24465,24477,2009, citations,entry_citation,16271,44841,1,,entry citation,,,19536138,,,A PH domain within OCRL bridges clathrin-mediated membrane trafficking to phosphoinositide metabolism,published,journal,EMBO J.,,28,13,,,,,,,,,,,,,,,,,,,,,,1831,1842,2009, citations,entry_citation,16272,44858,1,,entry citation,,,,,,Solution NMR structure of an O6-methylguanine DNA methyltransferase family protein from Vibrio parahaemolyticus. Northeast Structural Genomics Consortium target VpR247.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16273,44887,1,,entry citation,,,19536138,,,A PH domain within OCRL bridges clathrin-mediated membrane trafficking to phosphoinositide metabolism,published,journal,EMBO J.,,28,13,,,,,,,,,,,,,,,,,,,,,,1831,1842,2009, citations,entry_citation,16274,44903,1,,entry citation,,,22907757,,,The prolyl isomerase Pin1 targets stem-loop binding protein (SLBP) to dissociate the SLBP-histone mRNA complex linking histone mRNA decay with SLBP ubiquitination.,published,journal,Mol. Cell. Biol.,Molecular and cellular biology,32,21,,,,,,,,,,,,,,,,,,,,,,4306,4322,2012, citations,entry_citation,16275,44918,1,,entry citation,,,19708686,,,Headgroup-Dependent Membrane Catalysis of Apelin-Receptor Interactions Is Likely,published,journal,J. Phys. Chem. B.,,113,30,,,,,,,,,,,,,,,,,,,,,,10465,10471,2009, citations,citations,16276,44940,1,,entry citation,,,19918063,,,A structural basis for H-NOX signaling in Shewanella oneidensis by trapping a histidine kinase inhibitory conformation.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,106,47,,,,,,,,,,,,,,,,,,,,,,19753,19760,2009, citations,citation1,16277,44963,1,,entry citation,,,19645496,,,"SOLUTION STRUCTURES OF THE ACTUATOR DOMAIN OF ATP7A AND ATP7B, THE MENKES AND WILSON DISEASE PROTEINS",published,journal,J. Biol. Chem.,,48,33,,,,,,,,,,,,,,,,,,,,,,7849,7855,2009, citations,citations,16278,44985,1,,entry citation,,,19918063,,,A structural basis for H-NOX signaling in Shewanella oneidensis by trapping a histidine kinase inhibitory conformation.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,106,47,,,,,,,,,,,,,,,,,,,,,,19753,19760,2009, citations,entry_citation,16279,45010,1,,entry citation,,,21892170,,,Structural analysis of the interaction between Hsp90 and the tumor suppressor protein p53.,published,journal,Nat. Struct. Mol. Biol.,Nature structural & molecular biology,18,10,,,,,,,,,,,,,,,,,,,,,,1086,1093,2011, citations,entry_citation,16280,45026,1,,entry citation,,,20090983,,,Structural analysis of the binding of the diquaternary pyridophenazine derivative dqdppn to B-DNA oligonucleotides.,published,journal,Org. Biomol. Chem.,Organic & biomolecular chemistry,8,3,,,,,,,,,,,,,,,,,,,,,,648,654,2010, citations,entry_citation,16281,45041,1,,entry citation,,,20090983,,,Structural analysis of the binding of the diquaternary pyridophenazine derivative dqdppn to B-DNA oligonucleotides.,published,journal,Org. Biomol. Chem.,Organic & biomolecular chemistry,8,3,,,,,,,,,,,,,,,,,,,,,,648,654,2010, citations,entry_citation,16282,45058,1,,entry citation,,,20090983,,,Structural analysis of the binding of the diquaternary pyridophenazine derivative dqdppn to B-DNA oligonucleotides.,published,journal,Org. Biomol. Chem.,Organic & biomolecular chemistry,8,3,,,,,,,,,,,,,,,,,,,,,,648,654,2010, citations,entry_citation,16283,45073,1,,entry citation,,,,,,Solution NMR structure of an O6-methylguanine DNA methyltransferase family protein from Vibrio parahaemolyticus. Northeast Structural Genomics Consortium target VpR247.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16284,45100,1,,entry citation,,,20042596,,,Structural basis for the association of the redox-sensitive target of rapamycin FATC domain with membrane-mimetic micelles.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,285,10,,,,,,,,,,,,,,,,,,,,,,7766,7775,2010, citations,entry_citation,16285,45123,1,,entry citation,,,,,,Solution structure of a PDZ domain protein,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16286,45138,1,,entry citation,,,20090983,,,Structural analysis of the binding of the diquaternary pyridophenazine derivative dqdppn to B-DNA oligonucleotides.,published,journal,Org. Biomol. Chem.,Organic & biomolecular chemistry,8,3,,,,,,,,,,,,,,,,,,,,,,648,654,2010, citations,entry_citation,16287,45153,1,,entry citation,,,20090983,,,Structural analysis of the binding of the diquaternary pyridophenazine derivative dqdppn to B-DNA oligonucleotides.,published,journal,Org. Biomol. Chem.,Organic & biomolecular chemistry,8,3,,,,,,,,,,,,,,,,,,,,,,648,654,2010, citations,entry_citation,16288,45170,1,,entry citation,,,20090983,,,Structural analysis of the binding of the diquaternary pyridophenazine derivative dqdppn to B-DNA oligonucleotides.,published,journal,Org. Biomol. Chem.,Organic & biomolecular chemistry,8,3,,,,,,,,,,,,,,,,,,,,,,648,654,2010, citations,entry_citation,16289,45187,1,,entry citation,,,20090983,,,Structural analysis of the binding of the diquaternary pyridophenazine derivative dqdppn to B-DNA oligonucleotides.,published,journal,Org. Biomol. Chem.,Organic & biomolecular chemistry,8,3,,,,,,,,,,,,,,,,,,,,,,648,654,2010, citations,entry_citation,16290,45202,1,,entry citation,,,20090983,,,Structural analysis of the binding of the diquaternary pyridophenazine derivative dqdppn to B-DNA oligonucleotides.,published,journal,Org. Biomol. Chem.,Organic & biomolecular chemistry,8,3,,,,,,,,,,,,,,,,,,,,,,648,654,2010, citations,entry_citation,16291,45219,1,,entry citation,,,20108276,,,Structure of the Complex of [Ru(tpm)(dppz)py](2+) with a B-DNA Oligonucleotide-A Single-Substituent Binding Switch for a Metallo-Intercalator.,published,journal,Chemistry,"Chemistry (Weinheim an der Bergstrasse, Germany)",16,8,,,,,,,,,,,,,,,,,,,,,,2407,2417,2010, citations,entry_citation,16292,45236,1,,entry citation,,,20108276,,,Structure of the Complex of [Ru(tpm)(dppz)py](2+) with a B-DNA Oligonucleotide-A Single-Substituent Binding Switch for a Metallo-Intercalator.,published,journal,Chemistry,"Chemistry (Weinheim an der Bergstrasse, Germany)",16,8,,,,,,,,,,,,,,,,,,,,,,2407,2417,2010, citations,reference_1,16293,45253,1,,entry citation,,,19715701,,,Structural studies of FF domains of the transcription factor CA150 provide insights into the organization of FF domain tandem arrays.,published,journal,J. Mol. Biol.,Journal of molecular biology,393,2,,,,,,,,,,,,,,,,,,,,,,409,424,2009, citations,cited_reference_1_within_the_entry,16294,45269,1,,reference citation,,,16388823,,,"Crystal Structure of Peach Pru p 3, the Prototypic Member of the Family of Plant Non-specific Lipid Transfer Protein Pan-allergens",published,journal,J. Mol. Biol.,,356,3,,,,,,,,,,,,,,,,,,,,,,684,694,2006, citations,Entry_citation_1,16294,45270,2,,entry citation,,,20121231,,,The structural characteristics of nonspecific lipid transfer proteins explain their resistance to gastroduodenal proteolysis.,published,journal,Biochemistry,Biochemistry,49,10,,,,,,,,,,,,,,,,,,,,,,2130,2139,2010, citations,entry_citation,16295,45288,1,,entry citation,,,20042596,,,Structural basis for the association of the redox-sensitive target of rapamycin FATC domain with membrane-mimetic micelles,published,journal,J. Biol. Chem.,,285,10,,,,,,,,,,,,,,,,,,,,,,7766,7775,2010, citations,entry_citation,16296,45310,1,,entry citation,,,19888685,,,NMR assignment of the intrinsically disordered C-terminal region of Homo sapiens FCP1 in the unbound state.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,3,2,,,,,,,,,,,,,,,,,,,,,,179,181,2009, citations,entry_citation,16297,45325,1,,entry citation,,,19666031,,,A Nuclear Localization Signal at the SAM-SAM Domain Interface of AIDA-1 Suggests a Requirement for Domain Uncoupling Prior to Nuclear Import,published,journal,J. Mol. Biol.,,392,5,,,,,,,,,,,,,,,,,,,,,,1168,1177,2009, citations,entry_citation,16298,45340,1,,entry citation,,,,,,"Solution NMR structure of the domain N-terminal to the integrase domain of SH1003 from Staphylococcus haemolyticus. Northeast Structural Genomics Consortium Target ShR105F (64-166).",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16299,45370,1,,entry citation,,,19888682,10.1007/s12104-009-9166-4,,NMR assignments of a 48 kDa tetramer of the T1 domain of the mammalian voltage gated potassium channel Kv1.4.,published,journal,Biomol NMR Assign,Biomolecular NMR assignments,3,2,,,,,,,,,,,,,,,,,,,,,,167,170,2009, citations,entry_citation,16300,45385,1,,entry citation,,,19481090,,,"Effect of Pseudorepeat Rearrangement on alpha-Synuclein Misfolding, Vesicle Binding, and Micelle Binding",published,journal,J. Mol. Biol.,,390,3,,,,,,,,,,,,,,,,,,,,,,516,529,2009, citations,entry_citation,16301,45399,1,,entry citation,,,19481090,,,"Effect of Pseudorepeat Rearrangement on alpha-Synuclein Misfolding, Vesicle Binding, and Micelle Binding",published,journal,J. Mol. Biol.,,390,3,,,,,,,,,,,,,,,,,,,,,,516,529,2009, citations,entry_citation,16302,45413,1,,entry citation,,,19481090,,,"Effect of Pseudorepeat Rearrangement on alpha-Synuclein Misfolding, Vesicle Binding, and Micelle Binding",published,journal,J. Mol. Biol.,,390,3,,,,,,,,,,,,,,,,,,,,,,516,529,2009, citations,entry_citation,16303,45427,1,,entry citation,,,19481090,,,"Effect of Pseudorepeat Rearrangement on alpha-Synuclein Misfolding, Vesicle Binding, and Micelle Binding",published,journal,J. Mol. Biol.,,390,3,,,,,,,,,,,,,,,,,,,,,,516,529,2009, citations,entry_citation,16304,45441,1,,entry citation,,,19481090,,,"Effect of Pseudorepeat Rearrangement on alpha-Synuclein Misfolding, Vesicle Binding, and Micelle Binding",published,journal,J. Mol. Biol.,,390,3,,,,,,,,,,,,,,,,,,,,,,516,529,2009, citations,entry_citation,16305,45455,1,,entry citation,,,19763886,,,"1H, 13C and 15N assignments of a camelid nanobody directed against human alpha-synuclein",published,journal,Biomol. NMR Assignments,Biomolecular NMR Assignments,3,2,,,,,,,,,,,,,,,,,,,,,,231,233,2009, citations,citation_1,16306,45472,1,,reference citation,,,12033922,,,Truncated hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002: evidence for hexacoordination and covalent adduct formation in the ferric recombinant protein,published,journal,Biochemistry,,41,22,,,,,,,,,,,,,,,,,,,,,,6902,6910,2002, citations,entry_citation,16306,45473,2,,entry citation,,,19888693,10.1007/s12104-009-9177-1,,"(1)H, (15)N, and (13)C resonance assignments of the 2/2 hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 in the ferric bis-histidine state",published,journal,Biomol. NMR Assignments,,3,2,,,,,,,,,,,,,,,,,,,,,,211,214,2009, citations,citation_2,16306,45474,3,,reference citation,,,17115702,,,Structural and dynamic repercussions of heme binding and heme-protein cross-linking in Synechococcus sp. PCC 7002 hemoglobin,published,journal,Biochemistry,,45,47,,,,,,,,,,,,,,,,,,,,,,14075,14084,2006, citations,citation_3,16306,45475,4,,reference citation,,,14727166,,,Characterization of the heme-histidine cross-link in cyanobacterial hemoglobins from Synechocystis sp. PCC 6803 and Synechococcus sp. PCC 7002,published,journal,J. Biol. Inorg. Chem.,,9,2,,,,,,,,,,,,,,,,,,,,,,183,194,2004, citations,citation_5,16306,45476,5,,reference citation,,,20669934,,,Functional and structural characterization of the 2/2 hemoglobin from Synechococcus sp. PCC 7002,published,journal,Biochemistry,,49,33,,,,,,,,,,,,,,,,,,,,,,7000,7011,2010, citations,entry_citation_6,16306,45477,6,,reference citation,,,,,,TBD,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16307,45503,1,,entry citation,,,19888693,10.1007/s12104-009-9177-1,,"(1)H, (15)N, and (13)C resonance assignments of the 2/2 hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 in the ferric bis-histidine state",published,journal,Biomol. NMR Assignments,,3,2,,,,,,,,,,,,,,,,,,,,,,211,214,2009, citations,citation_1,16307,45504,2,,reference citation,,,12033922,,,Truncated hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002: evidence for hexacoordination and covalent adduct formation in the ferric recombinant protein,published,journal,Biochemistry,,41,22,,,,,,,,,,,,,,,,,,,,,,6902,6910,2002, citations,citation_2,16307,45505,3,,reference citation,,,17115702,,,Structural and dynamic repercussions of heme binding and heme-protein cross-linking in Synechococcus sp. PCC 7002 hemoglobin,published,journal,Biochemistry,,45,47,,,,,,,,,,,,,,,,,,,,,,14075,14084,2006, citations,citation_3,16307,45506,4,,reference citation,,,14727166,,,Characterization of the heme-histidine cross-link in cyanobacterial hemoglobins from Synechocystis sp. PCC 6803 and Synechococcus sp. PCC 7002,published,journal,J. Biol. Inorg. Chem.,,9,2,,,,,,,,,,,,,,,,,,,,,,183,194,2004, citations,citation_5,16307,45507,5,,reference citation,,,20669934,,,Functional and structural characterization of the 2/2 hemoglobin from Synechococcus sp. PCC 7002,published,journal,Biochemistry,,49,33,,,,,,,,,,,,,,,,,,,,,,7000,7011,2010, citations,entry_citation_6,16307,45508,6,,reference citation,,,,,,TBD,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16309,45538,1,,entry citation,,,19754879,,,Disulfide bridge regulates ligand-binding site selectivity in liver bile acid-binding proteins.,published,journal,FEBS J.,The FEBS journal,276,20,,,,,,,,,,,,,,,,,,,,,,6011,6023,2009, citations,citation_1,16310,45555,1,,entry citation,,,19754879,,,Disulfide bridge regulates ligand-binding site selectivity in liver bile acid-binding proteins,published,journal,FEBS J.,The FEBS journal,276,20,,,,,,,,,,,,,,,,,,,,,,6011,6023,2009, citations,citations,16311,45570,1,,entry citation,,,19800007,,,Solution structure of the complex of VEK-30 and plasminogen kringle 2.,published,journal,J. Struct. Biol.,Journal of structural biology,169,3,,,,,,,,,,,,,,,,,,,,,,349,359,2010, citations,entry_citation,16312,45588,1,,entry citation,,,,,,"Solution NMR structure of a domain from a putative phage integrase protein Nmul_A0064 from Nitrosospira multiformis, Northeast Structural Genomics Consortium Target NmR46C.",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16313,45618,1,,entry citation,,,,,,NMR Solution Structure of Tbulin folding Cofactor B obtained from Arabidopsis thaliana: Northeast Structural Genomics Consortium,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16314,45640,1,,entry citation,,,19456151,,,Three-Dimensional Structure and Orientation of Rat Islet Amyloid Polypeptide Protein in a Membrane Environment by Solution NMR Spectroscopy.,published,journal,J. Am. Chem. Soc.,,131,23,,,,,,,,,,,,,,,,,,,,,,8252,8261,2009, citations,entry_citation,16315,45658,1,,entry citation,,,,,,NMR structure of fragment 87-196 from the putative phage integrase IntS of E. coli,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16316,45679,1,,entry citation,,,,,,NMR structure of IntB phage-integrase-like protein fragment 90-199 from Erwinia carotova subsp. atroseptica,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16317,45700,1,,entry citation,,,19888696,10.1007/s12104-009-9180-6,,NMR assignments of the human cytokine interleukin-33,published,journal,Biomol. NMR Assignments,,3,2,,,,,,,,,,,,,,,,,,,,,,223,225,2009, citations,E1A-TAZ2,16318,45724,1,,entry citation,,,19651603,,,Structural Basis for Subversion of Cellular Control Mechanisms by the Adenoviral E1A Oncoprotein,published,journal,Proc. Natl. Acad. Sci. 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Chem.,The Journal of biological chemistry,284,42,,,,,,,,,,,,,,,,,,,,,,28674,28681,2009, citations,entry_citation,1632,45760,1,,entry citation,,,,,"Hua, Qingxin and Weiss, Michael A., ""Comparative 2D NMR Studies of Human Insulin and Des-pentapeptide Insulin: Sequential Resonance Assignment and Implications for Proteins Dynamics and Receptor Recognition,"" Biochemistry 30, 5505-5515 (1991).","Comparative 2D NMR Studies of Human Insulin and Des-pentapeptide Insulin: Sequential Resonance Assignment and Implications for Proteins Dynamics and Receptor Recognition",published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,5505,5515,1991, citations,entry_citation,16320,45773,1,,entry citation,,,19768683,,,Solution structure and calcium binding of protein SSO6904 from the hyperthermophilic archaeon Sulfolobus solfataricus.,published,journal,Proteins,Proteins,78,2,,,,,,,,,,,,,,,,,,,,,,474,479,2010, citations,Citation,16321,45790,1,,entry citation,,,19928833,10.1021/bi901686j,,The structure of the UbcH8-ubiquitin complex shows a unique ubiquitin interaction site,published,journal,Biochemistry,,48,51,,,,,,,,,,,,,,,,,,,,,,12169,12179,2009, citations,Citation_2,16321,45791,2,,reference citation,,,19636915,,,"1H, 13C and 15N resonance assignments for the human E2 conjugating enzyme, UbcH7",published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,2,1,,,,,,,,,,,,,,,,,,,,,,21,23,2008, citations,entry_citation,16322,45807,1,,entry citation,,,19500591,,,Solution characterization of the extracellular region of CD147 and its interaction with its enzyme ligand cyclophilin A.,published,journal,J. Mol. Biol.,Journal of molecular biology,391,3,,,,,,,,,,,,,,,,,,,,,,518,535,2009, citations,entry_citation,16323,45828,1,,entry citation,,,22907757,,,The prolyl isomerase Pin1 targets stem-loop binding protein (SLBP) to dissociate the SLBP-histone mRNA complex linking histone mRNA decay with SLBP ubiquitination.,published,journal,Mol. Cell. Biol.,Molecular and cellular biology,32,21,,,,,,,,,,,,,,,,,,,,,,4306,4322,2012, citations,entry_citation,16325,45843,1,,entry citation,,,,,,Solution Structure of Lkr136b,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16327,45862,1,,entry citation,,,20394752,,,Assignment Strategies for Large Proteins by Magic-Angle Spinning NMR: The 21-kDa Disulfide-Bond-Forming Enzyme DsbA,published,journal,J. Mol. Biol.,,399,2,,,,,,,,,,,,,,,,,,,,,,268,282,2010, citations,reference_citation,16327,45863,2,,reference citation,,,19953303,,,High resolution NMR spectroscopy of nanocrystalline proteins at ultra-high magnetic field.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,46,2,,,,,,,,,,,,,,,,,,,,,,149,155,2010, citations,citation_information,16328,45881,1,,entry citation,,,20639199,,,Unique structural characteristics of the rabbit prion protein.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,285,41,,,,,,,,,,,,,,,,,,,,,,31682,31693,2010, citations,entry_citation,16329,45895,1,,entry citation,,,19936968,,,"Backbone and side chain 1H, 15N and 13C assignments for the oxidised and reduced forms of the oxidoreductase protein DsbA from Staphylococcus aureus.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,1,,,,,,,,,,,,,,,,,,,,,,25,28,2010, citations,entry_citation,1633,45911,1,,entry citation,,,,,"Hua, Qingxin and Weiss, Michael, A., ""Comparative 2D NMR Studies of Human Insulin and Des-pentapeptide Insulin: Sequential Resonance Assignment and Implications for Proteins Dynamics and Receptor Recognition,"" Biochemistry 30, 5505-5515 (1991).","Comparative 2D NMR Studies of Human Insulin and Des-pentapeptide Insulin: Sequential Resonance Assignment and Implications for Proteins Dynamics and Receptor Recognition",published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,5505,5515,1991, citations,entry_citation,16330,45924,1,,entry citation,,,19936968,,,"Backbone and side chain 1H, 15N and 13C assignments for the oxidised and reduced forms of the oxidoreductase protein DsbA from Staphylococcus aureus.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,1,,,,,,,,,,,,,,,,,,,,,,25,28,2010, citations,lah4_low,16332,45939,1,,entry citation,,,,,,"Structure-function relationships of the polyhistidine-rich peptide LAH4 in micellar environments; pH dependent mode of antibiotic action & DNA transfection",in preparation,journal,Biophys. J.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,lah4_neutral,16333,45953,1,,entry citation,,,,,,"Structure-function relationships of the polyhistidine-rich peptide LAH4 in micellar environments; pH dependent mode of antibiotic action & DNA transfection",in preparation,journal,Biophys. J.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,16334,45967,1,,entry citation,,,20490953,,,Resonance assignments of myristoylated and non-myristoylated neuronal calcium sensor-1(NCS-1) embedded in a membrane,published,journal,Biomol. NMR Assignments,,4,2,,,,,,,,,,,,,,,,,,,,,,155,158,2010, citations,citations_1,16335,45981,1,,entry citation,,,,,,"Resonance assignment protein YLBL(BSU15050), Northeast Structural Genomics Consortium Target sr713a",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16336,45998,1,,entry citation,,,,,,Solution Structure Of Protein NMB1076 From Neisseria meningitidis. Northeast Structural Genomics Consortium Target MR101B.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16337,46022,1,,entry citation,,,19898995,,,Backbone resonance assignments of a promiscuous aminoglycoside antibiotic resistance enzyme; the aminoglycoside phosphotransferase(3')-IIIa.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,1,,,,,,,,,,,,,,,,,,,,,,9,12,2010, citations,entry_citation,16338,46039,1,,entry citation,,,,,,"Solution NMR structure of the N-terminal Ubiquitin-like Domain from Tubulin-binding Cofactor B, CG11242, from Drosophila melanogaster. Northeast Structural Genomics Consortium Target FR629A (residues 8-92).",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,16339,46066,1,,entry citation,,,19639634,,,A designed chimeric cyanovirin-N homolog lectin: structure and molecular basis of sucrose binding.,published,journal,Proteins,Proteins,77,4,,,,,,,,,,,,,,,,,,,,,,904,915,2009, citations,entry_citation,1634,46086,1,,entry citation,,,,,"Ikura, Mitsuhiko, Kay, Lewis E., Krinks, Marie, Bax, Ad, ""Triple-Resonance Multidimensional NMR Study of Calmodulin Complexed with the Binding Domain of Skeletal Muscle Myosin Light-Chain Kinase: Indication of a Conformational Change in the Central Helix,"" Biochemistry 30, 5498-5504 (1991).","Triple-Resonance Multidimensional NMR Study of Calmodulin Complexed with the Binding Domain of Skeletal Muscle Myosin Light-Chain Kinase: Indication of a Conformational Change in the Central Helix",published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,5498,5504,1991, citations,entry_citation,16340,46099,1,,entry citation,,,21069485,,,"100% complete assignment of non-labile (1)H, (13)C, and (15)N signals for calcium-loaded calbindin D (9k) P43G.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,1,,,,,,,,,,,,,,,,,,,,,,79,84,2011, citations,entry_citation,16341,46117,1,,entry citation,,,19856131,,,"Backbone (1)H, (13)C, and (15)N NMR assignment for the inactive form of the retroviral protease of the murine intracisternal A-type particle, inMIA-14 PR.",published,journal,Biomol NMR Assign,Biomolecular NMR assignments,3,2,,,,,,,,,,,,,,,,,,,,,,261,264,2009, citations,Protein_Science,16342,46133,1,,entry citation,,,19554627,,,Structural characterization of alpha-synuclein in an aggregation prone state,published,journal,Protein Sci.,,18,9,,,,,,,,,,,,,,,,,,,,,,1840,1846,2009, citations,citations,16343,46153,1,,entry citation,,,20106984,,,An Achilles' heel in an amyloidogenic protein and its repair: insulin fibrillation and therapeutic design.,published,journal,J. Biol. Chem.,Journal of Biological Chemistry,285,14,,,,,,,,,,,,,,,,,,,,,,10806,10821,2010, citations,Citation_1,16344,46172,1,,entry citation,,,19966220,,,The HD-exchange motions of ribosomal protein S6 are insensitive to reversal of the protein-folding pathway.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,106,51,,,,,,,,,,,,,,,,,,,,,,21619,21624,2009, citations,Citation_1,16345,46195,1,,entry citation,,,19966220,,,The HD-exchange motions of ribosomal protein S6 are insensitive to reversal of the protein-folding pathway.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,106,51,,,,,,,,,,,,,,,,,,,,,,21619,21624,2009, citations,entry_citation,16347,46219,1,,entry citation,,,,,,Solution structure of protein ATC0852 from Agrobacterium tumefaciens,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16348,46242,1,,entry citation,,,,,,"SOLUTION STRUCTURE OF DEAD RINGER-LIKE PROTEIN 1 (AT-RICH INTERACTIVE DOMAIN-CONTAINING PROTEIN 3A) FROM HOMO SAPIENS, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET HR4394C",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16349,46267,1,,entry citation,,,20077570,,,NMR structure of F-actin-binding domain of Arg/Abl2 from Homo sapiens.,published,journal,Proteins,Proteins,78,5,,,,,,,,,,,,,,,,,,,,,,1326,1330,2010, citations,entry_citation,1635,46291,1,,entry citation,,,,,"van der Graaf, Marinette, van Mierlo, Carlo P.M., Hemminga, Marcus A., ""Solution Conformation of a Peptide Fragment Representing a Proposed RNA-Binding Site of a Viral Coat Protein Studied by Two-Dimensional NMR,"" Biochemistry 30, 5722-5727 (1991).","Solution Conformation of a Peptide Fragment Representing a Proposed RNA-Binding Site of a Viral Coat Protein Studied by Two-Dimensional NMR",published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,5722,5727,1991, citations,entry_citation,16350,46304,1,,entry citation,,,21300903,,,Antarctic and Arctic populations of the ciliate Euplotes nobilii show common pheromone-mediated cell-cell signaling and cross-mating.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,108,8,,,,,,,,,,,,,,,,,,,,,,3181,3186,2011, citations,entry_citation,16352,46323,1,,entry citation,,,,,,Solution NMR structure of proterin AF2094 from Archaeoglobus fulgidus.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16353,46347,1,,entry citation,,,,,,"SOLUTION STRUCTURE OF SH2 DOMAIN OF PROTO-ONCOGENE TYROSINE-PROTEIN KINASE FER FROM HOMO SAPIENS, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET HR3461D",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16354,46374,1,,entry citation,,,19760172,,,NMR solution structure of the N-terminal domain of subunit E (E1-52) of A1AO ATP synthase from Methanocaldococcus jannaschii.,published,journal,J. Bioenerg. Biomembr.,Journal of bioenergetics and biomembranes,41,4,,,,,,,,,,,,,,,,,,,,,,343,348,2009, citations,entry_citation,16355,46391,1,,entry citation,,,,,,NMR Solution Structure of a Putative Uncharacterized Protein obtained from Arabidopsis thaliana: Northeast Structural Genomics Consortium Target AR3449A,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16356,46426,1,,entry citation,,,19946019,,,Structure of a two-G-tetrad intramolecular G-quadruplex formed by a variant human telomeric sequence in K+ solution: insights into the interconversion of human telomeric G-quadruplex structures.,published,journal,Nucleic Acids Res.,Nucleic acids research,38,3,,,,,,,,,,,,,,,,,,,,,,1009,1021,2010, citations,entry_citation,16484,49040,1,,entry citation,,,20127391,,,NMR structure note: UBA domain of CIP75.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,46,3,,,,,,,,,,,,,,,,,,,,,,245,250,2010, citations,citations,16357,46441,1,,entry citation,,,,,,"Solution NMR Structure of a dimeric protein of unknown function from Methanobacterium thermoautotrophicum, Northeast Structural Genomics Consortium Target TR5",in preparation,journal,To be Published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16359,46473,1,,entry citation,,,19997625,,,NMR analysis of the dynamic exchange of the NS2B cofactor between open and closed conformations of the West Nile virus NS2B-NS3 protease.,published,journal,PLoS Negl. Trop. Dis.,PLoS neglected tropical diseases,3,12,,,,,,,,,,,,,,,,,,,,,,,,2009, citations,entry_citation,16360,46487,1,,entry citation,,,,,,"1H, 13C and 15N NMR sequence-specific resonance assignments and relaxation parameters for human apo-S100A1(aa) in the reduced form",published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16361,46520,1,,entry citation,,,19728111,,,"The NMR structure of the p62 PB1 domain, a key protein in autophagy and NF-kappaB signaling pathway.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,45,3,,,,,,,,,,,,,,,,,,,,,,335,341,2009, citations,entry_citation,16362,46535,1,,entry citation,,,19768581,,,"(1)H, (13)C, and (15)N NMR assignments of StnII-R29Q, a defective lipid binding mutant of the sea anemone actinoporin Sticholysin II.",published,journal,Biomol NMR Assign,Biomolecular NMR assignments,3,2,,,,,,,,,,,,,,,,,,,,,,239,241,2009, citations,entry_citation,16363,46551,1,,entry citation,,,20616042,,,Conformational selection in the molten globule state of the nuclear coactivator binding domain of CBP,published,journal,Proc. Natl. Acad. Sci. U S A.,,107,28,,,,,,,,,,,,,,,,,,,,,,12535,12540,2010, citations,citations,16364,46566,1,,entry citation,,,,,,Solution NMR structure of FHA domain of Mb1858 from Mycobacterium bovis. Northeast Structural Genomics Consortium Target MbR243C (24-155).,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16365,46596,1,,entry citation,,,,,,Solution NMR structure of yeast protein YOR252W,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16366,46617,1,,entry citation,,,,,,solution NMR structure of Themotoga maritima protein TM1076,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16367,46638,1,,entry citation,,,19927121,,,NMR evidence for differential phosphorylation-dependent interactions in WT and DeltaF508 CFTR.,published,journal,EMBO J.,The EMBO journal,29,1,,,,,,,,,,,,,,,,,,,,,,263,277,2010, citations,entry_citation,16368,46656,1,,entry citation,,,,,,"Solution NMR structure of the homodimeric winged helix-turn-helix DNA-binding domain (fragment 1-100) Mb0332 from Mycobacterium bovis, a possible ArsR-family transcriptional regulator. Northeast Structural Genomics Consortium Target MbR242E.",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16370,46688,1,,entry citation,,,,,,Solution NMR Structure of the Ig-like C2-type 2 Domain of Human Myotilin. Northeast Structural Genomics Target HR3158.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16371,46716,1,,entry citation,,,,,,Solution Structure Of Protein DSY2949 From Desulfitobacterium hafniense. Northeast Structural Genomics Consortium Target DhR27,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16372,46741,1,,entry citation,,,,,,Solution structure of protein af2351 from Archaeoglobus fulgidus. Northeast Structural Genomics Consortium target AtT9/Ontario Center for Structural Proteomics Target af2351,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16373,46767,1,,entry citation,,,,,,"Solution NMR structure of an integrase domain from protein SPA4288 from Salmonella enterica, Northeast Structural Genomics Consortium Target SlR105H",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,16374,46796,1,,entry citation,,,,,,"Pathogenic E. coli O157:H7 NleG family of Type 3 secretion effectors features a common C-terminal U-box domain and E3 ubiquitin ligase activity",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,16375,46823,1,,entry citation,,,,,,Pathogenic E. coli O157:H7 NleG family of Type 3 secretion effectors features a common C-terminal U-box domain and E3 ubiquitin ligase activity,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16376,46850,1,,entry citation,,,,,,Solution NMR structure of the monomeric W187R mutant of A/Udorn NS1 effector domain. Northeast Structural Genomics target OR8C[W187R].,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,16377,46879,1,,entry citation,,,,,,RpR325/RPA3574 from Rhodopseudomonas palustris,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,Citation_1,16378,46909,1,,entry citation,,,,,,Solution Structure of GtR34C,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,reference_1,16379,46932,1,,entry citation,,,20108067,,,"1H, 13C and 15N backbone and side chain resonance assignments of human interleukin 1alpha.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,1,,,,,,,,,,,,,,,,,,,,,,59,60,2010, citations,entry_citation,1638,46949,1,,entry citation,,,,,"Gadhavi, Paresh L., Davis, Adrian L., Povey, Jane F., Keeler, James, Laue, Ernest D., ""Polypeptide-metal cluster connectivities in Cd(II) GAL4,"" FEBS Lett. 281 (1-2), 223-226 (1991).",Polypeptide-metal cluster connectivities in Cd(II) GAL4,published,journal,FEBS Lett.,,281,1-2,,,,,,,,,,,,,,,,,,,,,,223,226,1991, citations,entry_citation,16380,46962,1,,entry citation,,,20944236,,,Comparison of NMR and crystal structures highlights conformational isomerism in protein active sites,published,journal,Acta Crystallogr. Sect F Struct. Biol. Cryst. Commun.,,66,Pt 10,,,,,,,,,,,,,,,,,,,,,,1393,1405,2010, citations,citations,16381,46984,1,,entry citation,,,19916553,,,Structural and functional characterization of the integral membrane protein VDAC-1 in lipid bilayer nanodiscs.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,131,49,,,,,,,,,,,,,,,,,,,,,,17777,17779,2009, citations,entry_citation,16382,46998,1,,entry citation,,,,,,Solution NMR structure of the Rhodanese-like domain from Anabaena sp Alr3790 protein. Northeast Structural Genomics Consortium Target NsR437A,in preparation,journal,Proteins: Struct. Funct. Genet.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,16384,47031,1,,entry citation,,,,,,"Solution NMR Structure of protein yutD from B.subtilis, Northeast Structural Genomics Consortium Target Target SR232",in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16385,47055,1,,entry citation,,,,,,Solution NMR structure of the CARDB domain of PF1109 from Pyrococcus furiosus.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16386,47096,1,,entry citation,,,,,,Solution NMR Structure of the EGF-like 1 Domain of Human Fibulin-4. Northeast Structural Genomics Target HR6275.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,16387,47123,1,,entry citation,,,23135467,,,Principles for designing ideal protein structures,published,journal,Nature,,491,7422,,,,,,,,,,,,,,,,,,,,,,222,227,2012, citations,entry_citation,16388,47155,1,,entry citation,,,,,,"NMR Solution structure of a diflavin flavoprotein A3 from Nostoc sp. PCC 7120, Northeast Structural Genomics Consortium Target NsR431C",in preparation,journal,To be Published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref4,4452,200845,5,,reference citation,,,,,"Garrett, D.S., Powers, R., Gronenborn, A.M. and Clore G.M. (1991) J. Magn. Reson., 95, 214-220.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,16389,47175,1,,entry citation,,,20944234,,,NMR structure of the protein NP_247299.1: comparison with the crystal structure.,published,journal,Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.,"Acta crystallographica. Section F, Structural biology and crystallization communications",66,Pt 10,,,,,,,,,,,,,,,,,,,,,,1367,1380,2010, citations,entry_citation,1639,47195,1,,entry citation,,,,,"Lian, Lu-Yun, Yang, J. C., Derrick, J. P., Sutcliffe, Michael J., Roberts, G.C.K., Murphy, J. P., Goward, C. R., Atkinson, T., ""Sequential 1H NMR Assignments and Secondary Structure of an IgG-Binding Domain from Protein G,"" Biochemistry 30, 5335-5340 (1991).","Sequential 1H NMR Assignments and Secondary Structure of an IgG-Binding Domain from Protein G",published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,5335,5340,1991, citations,entry_citation,16390,47208,1,,entry citation,,,,,,Solution structure of ubiquitin-like domain of ubiquilin 1.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,Citation_1,16391,47234,1,,entry citation,,,19609683,,,"Assigning large proteins in the solid state: a MAS NMR resonance assignment strategy using selectively and extensively 13C-labelled proteins",published,journal,J. Biomol. NMR,,44,4,,,,,,,,,,,,,,,,,,,,,,245,260,2009, citations,Citation_2,16391,47235,2,,reference citation,,,19041879,10.1016/j.jmb.2008.10.097,,"alphaB-Crystallin: A Hybrid Solid-State/Solution-State NMR Investigation Reveals Structural Aspects of the Heterogeneous Oligomer",published,journal,J. Mol. Biol.,,385,5,,,,,,,,,,,,,,,,,,,,,,1481,1497,2009, citations,citation_1,16392,47256,1,,entry citation,,,16981701,,,Backbone dynamics of TEM-1 determined by NMR: evidence for a highly ordered protein,published,journal,Biochemistry,,45,38,,,,,,,,,,,,,,,,,,,,,,11414,11424,2006, citations,entry_citation,16393,47284,1,,entry citation,,,19927121,,,NMR evidence for differential phosphorylation-dependent interactions in WT and DeltaF508 CFTR.,published,journal,EMBO J.,The EMBO journal,29,1,,,,,,,,,,,,,,,,,,,,,,263,277,2010, citations,entry_citation,16394,47301,1,,entry citation,,,19927121,,,NMR evidence for differential phosphorylation-dependent interactions in WT and DeltaF508 CFTR.,published,journal,EMBO J.,The EMBO journal,29,1,,,,,,,,,,,,,,,,,,,,,,263,277,2010, citations,entry_citation,16395,47317,1,,entry citation,,,19580326,,,The recognition Pathway for the DNA Cytosine Methyltransferase M.HhaI,published,journal,Biochemistry,,48,33,,,,,,,,,,,,,,,,,,,,,,7807,7816,2009, citations,entry_citation,16396,47332,1,,entry citation,,,20202939,,,Characterization and structure determination of the Cdt1 binding domain of human minichromosome maintenance (Mcm) 6.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,285,17,,,,,,,,,,,,,,,,,,,,,,12469,12473,2010, citations,entry_citation,16397,47351,1,,entry citation,,,20634802,,,The structural plasticity of SCA7 domains defines their differential nucleosome-binding properties.,published,journal,EMBO Rep.,EMBO reports,11,8,,,,,,,,,,,,,,,,,,,,,,612,618,2010, citations,entry_citation,16398,47369,1,,entry citation,,,19789994,,,"Sequence-specific (1)H, (13)C, and (15)N backbone assignment of Psb27 from Synechocystis PCC 6803.",published,journal,Biomol NMR Assign,Biomolecular NMR assignments,3,2,,,,,,,,,,,,,,,,,,,,,,247,249,2009, citations,entry_citation,16399,47385,1,,entry citation,,,19788311,,,"Role of tryptophan-tryptophan interactions in Trpzip beta-hairpin formation, structure, and stability.",published,journal,Biochemistry,Biochemistry,48,43,,,,,,,,,,,,,,,,,,,,,,10362,10371,2009, citations,entry_citation,1640,47401,1,,entry citation,,,,,"Summers, Michael F., South, Terri L., Kim, Bo, Hare, Dennis R., ""High-Resolution Structure of an HIV Zinc Fingerlike Domain via a New NMR-Based Distance Geometry Approach,"" Biochemistry 29, 329-340 (1990).","High-Resolution Structure of an HIV Zinc Fingerlike Domain via a New NMR-Based Distance Geometry Approach",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,329,340,1990, citations,entry_citation,16400,47414,1,,entry citation,,,19625247,,,Solution structure of an ABC collagen heterotrimer reveals a single-register helix stabilized by electrostatic interactions.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,284,39,,,,,,,,,,,,,,,,,,,,,,26851,26859,2009, citations,entry_citation,16401,47441,1,,entry citation,,,20067301,,,Determination of separate inhibitor and substrate binding sites in the dehaloperoxidase-hemoglobin from Amphitrite ornata.,published,journal,Biochemistry,,49,6,,,,,,,,,,,,,,,,,,,,,,1199,1206,2010, citations,entry_citation,16402,47458,1,,entry citation,,,20634802,,,The structural plasticity of SCA7 domains defines their differential nucleosome-binding properties.,published,journal,EMBO Rep.,EMBO reports,11,8,,,,,,,,,,,,,,,,,,,,,,612,618,2010, citations,citations,16403,47476,1,,entry citation,,,,,,SOLUTION STRUCTURE OF GLUTAREDOXIN FROM Bartonella henselae str. Houston. Seattle Structure Genomics Center for Infectious Disease (SSGCID),in preparation,journal,To be Published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,16404,47496,1,,entry citation,,,20014027,,,Solution structure and dynamics of human ubiquitin conjugating enzyme Ube2g2.,published,journal,Proteins,Proteins,78,5,,,,,,,,,,,,,,,,,,,,,,1291,1301,2010, citations,entry_citation,16405,47514,1,,entry citation,,,20949063,,,Structural Transformation of the Tandem Ubiquitin-Interacting Motifs in Ataxin-3 and Their Cooperative Interactions with Ubiquitin Chains,published,journal,PLoS ONE,,5,10,,,,,,,,,,,,,,,,,,,,,,e13202,e13202,2010, citations,citations,16406,47532,1,,entry citation,,,,,,Null,in preparation,journal,To be Published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16407,47551,1,,entry citation,,,19788311,,,"Role of tryptophan-tryptophan interactions in Trpzip beta-hairpin formation, structure, and stability.",published,journal,Biochemistry,Biochemistry,48,43,,,,,,,,,,,,,,,,,,,,,,10362,10371,2009, citations,entry_citation,16408,47565,1,,entry citation,,,20192263,,,CopK from Cupriavidus metallidurans CH34 binds Cu(I) in a tetrathioether site: characterization by X-ray absorption and NMR spectroscopy.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,132,11,,,,,,,,,,,,,,,,,,,,,,3770,3777,2010, citations,citation_2,16408,47566,2,,reference citation,,,,10.1016/j.jmb.2008.05.017,,Molecular structure and metal-binding properties of the periplasmic CopK protein expressed in Cupriavidus metallidurans CH34 during copper challenge,published,journal,J. Mol. Biol.,,380,,,,,,,,,,,,,,,,,,,,,,,386,403,2008, citations,citation_1,16409,47588,1,,entry citation,,,19852484,,,MgF(3)(-) and alpha-Galactose 1-Phosphate in the Active Site of beta-Phosphoglucomutase Form a Transition State Analogue of Phosphoryl Transfer.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,131,45,,,,,,,,,,,,,,,,,,,,,,16334,16335,2009, citations,citation_1,16411,47612,1,,entry citation,,,20818393,,,Cooperative interaction of transcription termination factors with the RNA polymerase II C-terminal domain.,published,journal,Nat. Struct. Mol. Biol.,Nature structural & molecular biology,17,10,,,,,,,,,,,,,,,,,,,,,,1195,1201,2010, citations,entry_citation,16412,47630,1,,entry citation,,,20818393,,,Cooperative interaction of transcription termination factors with the RNA polymerase II C-terminal domain.,published,journal,Nat. Struct. Mol. Biol.,Nature structural & molecular biology,17,10,,,,,,,,,,,,,,,,,,,,,,1195,1201,2010, citations,entry_citation,16413,47647,1,,entry citation,,,20556552,,,"Resonance assignments of human C35 (C17orf37) protein, a novel tumor biomarker.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,2,,,,,,,,,,,,,,,,,,,,,,191,193,2010, citations,entry_citation,16414,47663,1,,entry citation,,,9353310,,,Interaction of the Second Binding Region of Troponin I with the Regulatory Domain of Skeletal Muscle Troponin C as Determined by NMR Spectroscopy,published,journal,J. Biol. Chem.,,272,45,,,,,,,,,,,,,,,,,,,,,,28494,28500,1997, citations,entry_citation,16415,47679,1,,entry citation,,,9369197,,,1H NMR and fluorescence studies of the complexation of DMPG by wheat non-specific lipid transfer protein. Global fold of the complex,published,journal,FEBS Lett.,,1,416,,,,,,,,,,,,,,,,,,,,,,130,134,1997, citations,entry_citation,16416,47700,1,,entry citation,,,12824484,,,A solution NMR study of the binding kinetics and the internal dynamics of an HIV-1 protease-substrate complex.,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,12,7,,,,,,,,,,,,,,,,,,,,,,1376,1385,2003, citations,entry_citation,16417,47720,1,,entry citation,,,15327779,,,"An Atomic Resolution Model for Assembly, Architecture, and Function of the Dr Adhsins",published,journal,Mol. Cell,Molecular Cell,15,,,,,,,,,,,,,,,,,,,,,,,647,657,2004, citations,entry_citation,16418,47739,1,,entry citation,,,12689827,,,Interaction between calcium-free calmodulin and IQ motif of neurogranin studied by nuclear magnetic resonance spectroscopy,published,journal,Anal. Biochem.,,315,2,,,,,,,,,,,,,,,,,,,,,,175,182,2003, citations,entry_citation,16419,47759,1,,entry citation,,,7623386,,,"Local perturbations by ligand binding of hydrogen deuterium exchange kinetics in a four-helix bundle protein, acyl coenzyme A binding protein (ACBP).",published,journal,J. Mol. Biol.,Journal of molecular biology,250,5,,,,,,,,,,,,,,,,,,,,,,695,706,1995, citations,entry_citation,1642,47775,1,,entry citation,,,,,"Kessler, Horst, Schmieder, Peter, Bermel, W., ""Complete Assignment of the Noncarbonylic Carbon-13 Resonances of Tendamistat,"" Biopolymers 30, 465-475 (1990).",Complete Assignment of the Noncarbonylic Carbon-13 Resonances of Tendamistat,published,journal,Biopolymers,,30,,,,,,,,,,,,,,,,,,,,,,,465,475,1990, citations,entry_citation,16420,47788,1,,entry citation,,,16373478,,,Protein stabilization by specific binding of guanidinium to a functional arginine-binding surface on an SH3 domain,published,journal,Protein Sci.,,1,15,,,,,,,,,,,,,,,,,,,,,,162,170,2006, citations,entry_citation,16421,47805,1,,entry citation,,,16490204,,,Solution Structure and Backbone Dynamics of the Trypanosoma cruzi Cysteine Protease Inhibitor Chagasin,published,journal,J. Mol. Biol.,,1,357,,,,,,,,,,,,,,,,,,,,,,1511,1521,2006, citations,entry_citation,16422,47823,1,,entry citation,,,17059825,,,Solution Structure and Dynamics of the N-terminal Cystosolic Domain of Rhomboid Intramembrane Protease from Pseudomonas aeruginosa: Insights into a Functional Role in Intramembrane Proteolysis,published,journal,J. Mol. Biol.,,1,365,,,,,,,,,,,,,,,,,,,,,,109,122,2007, citations,entry_citation,16423,47850,1,,entry citation,,,10951192,,,Solution structure of a neurotrophic ligand bound to FKBP12 and its effects on protein dynamics,published,journal,Eur. J. Biochem.,,267,1,,,,,,,,,,,,,,,,,,,,,,5342,5354,2000, citations,Citation_1,16424,47870,1,,entry citation,,,20526702,,,"Secondary structure and 1H, 13C and 15N resonance assignments of BamE, a component of the outer membrane protein assembly machinery in Escherichia coli.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,2,,,,,,,,,,,,,,,,,,,,,,179,181,2010, citations,entry_citation,16425,47885,1,,entry citation,,,20600122,,,Novel Protein-Protein Contacts Facilitate mRNA 3'-Processing Signal Recognition by Rna15 and Hrp1.,published,journal,J. Mol. Biol.,Journal of molecular biology,401,3,,,,,,,,,,,,,,,,,,,,,,334,349,2010, citations,entry_citation,16426,47912,1,,entry citation,,,19002654,,,Detection and assignment of phosphoserine and phosphothreonine residues by (13)C- (31)P spin-echo difference NMR spectroscopy.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,43,1,,,,,,,,,,,,,,,,,,,,,,31,37,2009, citations,entry_citation,16428,47938,1,,entry citation,,,20007596,,,The structure of the KlcA and ArdB proteins reveals a novel fold and antirestriction activity against Type I DNA restriction systems in vivo but not in vitro.,published,journal,Nucleic Acids Res.,Nucleic acids research,38,5,,,,,,,,,,,,,,,,,,,,,,1723,1737,2010, citations,reference_citation,16428,47939,2,,reference citation,,,20007596,,,The structure of the KlcA and ArdB proteins reveals a novel fold and antirestriction activity against Type I DNA restriction systems in vivo but not in vitro.,published,journal,Nucleic acids research,Nucleic acids research,,,,,,,,,,,,,,,,,,,,,,,,,,2009, citations,entry_citation,1643,47964,1,,entry citation,,,,,"Meyer, Jean-Philippe, Pelton, John T., Hoflack, Jan, Saudek, Vladimir, ""Solution Structure of Salmon Calcitonin,"" Biopolymers 31, 233-241 (1991).",Solution Structure of Salmon Calcitonin,published,journal,Biopolymers,,31,,,,,,,,,,,,,,,,,,,,,,,233,241,1991, citations,entry_citation,16430,47978,1,,entry citation,,,19779849,,,Backbone resonance assignments of the 48 kDa dimeric putative rRNA-methyltransferase Nep1 from Methanocaldococcus jannaschii,published,journal,Biomol. NMR Assignments,,3,2,,,,,,,,,,,,,,,,,,,,,,251,254,2009, citations,entry_citation,16431,47998,1,,entry citation,,,19444830,,,Structures of HIV TAR RNA-ligand complexes reveal higher binding stoichiometries,published,journal,ChemBioChem,,10,9,,,,,,,,,,,,,,,,,,,,,,1490,1494,2009, citations,entry_citation,16435,48029,1,,entry citation,,,19820233,,,Deciphering the structural basis that guides the oxidative folding of leech-derived tryptase inhibitor.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,284,51,,,,,,,,,,,,,,,,,,,,,,35612,35620,2009, citations,entry_citation,16436,48048,1,,entry citation,,,19820233,,,Deciphering the structural basis that guides the oxidative folding of leech-derived tryptase inhibitor.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,284,51,,,,,,,,,,,,,,,,,,,,,,35612,35620,2009, citations,entry_citation,16437,48067,1,,entry citation,,,19820233,,,Deciphering the structural basis that guides the oxidative folding of leech-derived tryptase inhibitor.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,284,51,,,,,,,,,,,,,,,,,,,,,,35612,35620,2009, citations,entry_citation,16438,48086,1,,entry citation,,,19820233,,,Deciphering the structural basis that guides the oxidative folding of leech-derived tryptase inhibitor.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,284,51,,,,,,,,,,,,,,,,,,,,,,35612,35620,2009, citations,entry_citation,16439,48105,1,,entry citation,,,19835885,,,The central portion of factor H (modules 10-15) is compact and contains a structurally deviant CCP module.,published,journal,J. Mol. Biol.,Journal of molecular biology,395,1,,,,,,,,,,,,,,,,,,,,,,105,122,2010, citations,entry_citation,16440,48126,1,,entry citation,,,19917612,,,The Binding Mode of ATP Revealed by the Solution Structure of the N-domain of Human ATP7A.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,285,4,,,,,,,,,,,,,,,,,,,,,,2537,2544,2010, citations,entry_citation,16441,48149,1,,entry citation,,,19917612,,,The Binding Mode of ATP Revealed by the Solution Structure of the N-domain of Human ATP7A.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,285,4,,,,,,,,,,,,,,,,,,,,,,2537,2544,2010, citations,citation1,16443,48191,1,,entry citation,,,20886839,,,Redox linked conformational changes in cytochrome c3 from Desulfovibrio desulfuricans ATCC 27774.,published,journal,Biochemistry,Biochemistry,49,44,,,,,,,,,,,,,,,,,,,,,,9620,9629,2010, citations,entry_citation,16444,48213,1,,entry citation,,,20703835,,,"The (1)H, (13)C and (15)N backbone and side-chain assignment of the RRM domain of SC35, a regulator of pre-mRNA splicing.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,1,,,,,,,,,,,,,,,,,,,,,,7,10,2011, citations,entry_citation,16445,48233,1,,entry citation,,,19842064,,,NMR assignments of the intrinsically disordered K(2) and YSK (2) dehydrins,published,journal,Biomol. NMR Assignments,,3,2,,,,,,,,,,,,,,,,,,,,,,273,275,2009, citations,citation_1,16446,48248,1,,entry citation,,,19851889,,,"(1)H, (15)N, and (13)C chemical shift assignments of neuronal calcium sensor-1 homolog from fission yeast.",published,journal,Biomol NMR Assign,Biomolecular NMR assignments,3,2,,,,,,,,,,,,,,,,,,,,,,269,271,2009, citations,citation_1,16447,48262,1,,entry citation,,,19944703,,,Structural Tightening and Interdomain Communication in the Catalytic Cycle of Phosphoglycerate Kinase.,published,journal,J. Mol. Biol.,Journal of molecular biology,396,2,,,,,,,,,,,,,,,,,,,,,,345,360,2010, citations,entry_citation,16448,48276,1,,entry citation,,,19562810,,,Long-range correlations between aliphatic 13C nuclei in protein MAS NMR spectroscopy.,published,journal,Angew. Chem. Int. Ed. Engl.,Angewandte Chemie (International ed. in English),48,31,,,,,,,,,,,,,,,,,,,,,,5708,5710,2009, citations,citations,16449,48293,1,,entry citation,,,22483113,,,The structure of the XPF-ssDNA complex underscores the distinct roles of the XPF and ERCC1 helix- hairpin-helix domains in ss/ds DNA recognition.,published,journal,Structure,"Structure (London, England : 1993)",20,4,,,,,,,,,,,,,,,,,,,,,,667,675,2012, citations,entry_citation,16450,48311,1,,entry citation,,,19842064,,,NMR assignments of the intrinsically disordered K(2) and YSK (2) dehydrins,published,journal,Biomol. NMR Assignments,,3,2,,,,,,,,,,,,,,,,,,,,,,273,275,2009, citations,citation_1,16451,48326,1,,entry citation,,,19944703,,,Structural Tightening and Interdomain Communication in the Catalytic Cycle of Phosphoglycerate Kinase.,published,journal,J. Mol. Biol.,Journal of molecular biology,396,2,,,,,,,,,,,,,,,,,,,,,,345,360,2010, citations,citation_1,16452,48344,1,,entry citation,,,16846228,,,Identification of the Interaction Domain of the Small Terminase Subunit pUL89 with the Large Subunit pUL56 of Human Cytomegalovirus,published,journal,Biochemistry,,45,29,,,,,,,,,,,,,,,,,,,,,,8855,8863,2006, citations,entry_citation,16453,48359,1,,entry citation,,,12215420,,,Intramolecular Dynamics of Low Molecular Weight Protein Tyrosine Phosphatase in Monomer-Dimer Equilibrium Studied by NMR: A Model for Changes in Dynamics upon Target Binding,published,journal,J. Mol. Biol.,Journal of Molecular Biology,322,1,,,,,,,,,,,,,,,,,,,,,,137,152,2002, citations,entry_citation,16454,48381,1,,entry citation,,,10652313,,,NMR Solution Structure of Complement-like Repeat CR3 from the Low Density Lipoprotein Receptor-related Protein,published,journal,J. Biol. Chem.,Journal of Biological Chemistry,275,5,,,,,,,,,,,,,,,,,,,,,,3264,3269,2000, citations,entry_citation,16455,48399,1,,entry citation,,,8112344,,,Study of the interaction between salivary proline-rich proteins and a polyphenol by 1H-NMR spectroscopy,published,journal,Eur. J. Biochem.,European journal of biochemistry,219,1,,,,,,,,,,,,,,,,,,,,,,923,935,1994, citations,entry_citation,16456,48433,1,,entry citation,,,16815922,,,The layered fold of the TSR domain of P. falciparum TRAP contains a heparin binding site,published,journal,Protein Sci.,Protein science,15,1,,,,,,,,,,,,,,,,,,,,,,1760,1768,2006, citations,entry_citation,16457,48459,1,,entry citation,,,10973978,,,The Structurl Basis for the Ligand Specificity of Family 2 Carbohydrate-binding Modules,published,journal,J. Biol. Chem.,Journal of Biological Chemistry,275,52,,,,,,,,,,,,,,,,,,,,,,41137,41142,2000, citations,entry_citation,16458,48481,1,,entry citation,,,17607743,,,NMR-based modeling and binding studies of a ternary complex between chicken liver bile acid binding protein and bile acids,published,journal,Proteins,,69,1,,,,,,,,,,,,,,,,,,,,,,177,191,2007, citations,entry_citation,16459,48504,1,,entry citation,,,15826666,,,Solution Structure of the Ran-binding Domain 2 of RanBP2 and its Interaction with the C Terminus of Ran,published,journal,J. Mol. Biol.,Journal of Molecular Biology,348,1,,,,,,,,,,,,,,,,,,,,,,711,725,2005, citations,entry_citation,1646,48523,1,,entry citation,,,,,"Gooley, Paul R., Caffrey, Michael S., Cusanovich, Michael A., MacKenzie, Neil E., ""A spectroscopic analysis of the Pro35-->Ala mutant of Rhodobacter capsulatus cytochrome c2. The strictly conserved Pro35 is not structurally essential.,"" Eur. J. Biochem. 196, 653-661 (1991).","A spectroscopic analysis of the Pro35-->Ala mutant of Rhodobacter capsulatus cytochrome c2. The strictly conserved Pro35 is not structurally essential.",published,journal,Eur. J. Biochem.,,196,,,,,,,,,,,,,,,,,,,,,,,653,661,1991, citations,entry_citation,16460,48537,1,,entry citation,,,11397096,,,The B(12)-binding subunit of glutamate mutase from Clostridium tetanomorphum traps the nucleotide moiety of coenzyme B(12).Moiety of Coenzyme B12,published,journal,J. Mol. Biol.,Journal of Molecular Biology,309,1,,,,,,,,,,,,,,,,,,,,,,777,791,2001, citations,entry_citation,16461,48553,1,,entry citation,,,15571493,,,The C-terminal domain of the HIV-1 regulatory protein Vpr adopts an antiparallel dimeric structure in solution via its leucine-zipper-like domain,published,journal,Biochem. J.,The Biochemical Journal,387,1,,,,,,,,,,,,,,,,,,,,,,333,341,2005, citations,entry_citation,16462,48571,1,,entry citation,,,12717021,,,Ligand-induced changes in dynamics in the RT loop of the C-terminal SH3 domain of Sem-5 indicate cooperative conformational coupling,published,journal,Protein Sci.,,12,5,,,,,,,,,,,,,,,,,,,,,,982,996,2003, citations,entry_citation,16463,48590,1,,entry citation,,,19768664,,,"Backbone and side-chain (1)H, (13)C and (15)N resonance assignments of LEN, a human immunoglobulin kappaIV light-chain variable domain.",published,journal,Biomol NMR Assign,Biomolecular NMR assignments,3,2,,,,,,,,,,,,,,,,,,,,,,255,259,2009, citations,citation_1,16464,48608,1,,entry citation,,,19944703,,,Structural Tightening and Interdomain Communication in the Catalytic Cycle of Phosphoglycerate Kinase.,published,journal,J. Mol. Biol.,Journal of molecular biology,396,2,,,,,,,,,,,,,,,,,,,,,,345,360,2010, citations,entry_citation,16465,48630,1,,entry citation,,,19996092,,,Calmodulin Wraps around Its Binding Domain in the Plasma Membrane Ca2+ Pump Anchored by a Novel 18-1 Motif.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,285,6,,,,,,,,,,,,,,,,,,,,,,4015,4024,2010, citations,entry_citation,16466,48652,1,,entry citation,,,19821587,,,Solution structure and functional characterization of human plasminogen kringle 5.,published,journal,Biochemistry,Biochemistry,48,43,,,,,,,,,,,,,,,,,,,,,,10208,10219,2009, citations,entry_citation,16467,48666,1,,entry citation,,,19204326,,,Structure of the AML1-ETO eTAFH domain-HEB peptide complex and its contribution to AML1-ETO activity.,published,journal,Blood,Blood,113,15,,,,,,,,,,,,,,,,,,,,,,3558,3567,2009, citations,entry_citation,16468,48683,1,,entry citation,,,,,,High-resolution solution structure of the ASIC1a blocker PcTx1,in preparation,journal,To be Published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,Reference_citation,16468,48684,2,,reference citation,,,12824480,10.1110/ps.0307003,,"Recombinant production and solution structure of PcTx1, the specific peptide inhibitor of ASIC1a proton-gated cation channels",published,journal,Protein Sci.,,12,7,,,,,,,,,,,,,,,,,,,,,,1332,1343,2003, citations,entry_citation,16469,48701,1,,entry citation,,,,,,Refinement of Protein Tertiary Structure by Using Spin-Spin Coupling Constants from Nuclear Magnetic Resonance Measurements,published,book chapter,,,,,,,,Protein Structure,,,,,,978-953-51-0555-8,,,,,,,,,,,http://www.intechopen.com/books/protein-structure/refinement-of-protein-tertiary-structure-by-using-spin-spin-coupling-constants-from-nuclear-magnetic,95,120,2012,"Protein Structure, Dr. Eshel Faraggi (Ed.), ISBN: 978-953-51-0555-8, InTech, Rijeka, Croatia Available from: http://www.intechopen.com/books/protein-structure/refinement-of-protein-tertiary-structure-by-using-spin-spin-coupling-constants-from-nuclear-magnetic (Chapter 4, Pages 95-120, book published online as of April 20th, 2012)" citations,Lohr_&_Ruterjans_1995,16469,48702,2,,reference citation,,,7881271,,,(H)NCAHA and (H)CANNH experiments for the determination of vicinal coupling constants related to the f-torsion angle,published,journal,J. 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Biochem.,,196,,,,,,,,,,,,,,,,,,,,,,,653,661,1991, citations,entry_citation,16470,48746,1,,entry citation,,,20075861,,,The PTB domain of ShcA couples receptor activation to the cytoskeletal regulator IQGAP1.,published,journal,EMBO J.,The EMBO journal,29,5,,,,,,,,,,,,,,,,,,,,,,884,896,2010, citations,entry_citation,16471,48762,1,,entry citation,,,20075861,,,The PTB domain of ShcA couples receptor activation to the cytoskeletal regulator IQGAP1.,published,journal,EMBO J.,The EMBO journal,29,5,,,,,,,,,,,,,,,,,,,,,,884,896,2010, citations,entry_citation,16472,48777,1,,entry citation,,,21461930,,,"1H, 15N and 13C chemical shift assignments of the SH2 domain of human tensin2 (TENC1).",published,journal,Biomol. 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Acta,Biochimica et biophysica acta,1798,3,,,,,,,,,,,,,,,,,,,,,,344,353,2010, citations,citation_1,16478,48889,1,,entry citation,,,19916060,,,"Backbone and side-chain 1H, 13C and 15N assignments of the ubiquitin-associated domain of human X-linked inhibitor of apoptosis protein.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,1,,,,,,,,,,,,,,,,,,,,,,13,15,2010, citations,entry_citation,16479,48905,1,,entry citation,,,20204714,,,(1)H and (13)C resonance assignments of a guanine sensing riboswitch's terminator hairpin.,published,journal,Biomol. 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Chem.,The Journal of biological chemistry,285,25,,,,,,,,,,,,,,,,,,,,,,19409,19421,2010, citations,entry_citation,1649,49143,1,,entry citation,,,,,"Gadhavi, Paresh L., Davis, Adrian L., Povey, Jane F., Keeler, James, Laue, Ernest D., ""Polypeptide-metal cluster connectivities in Cd(II) GAL4,"" FEBS Lett. 281 (1-2), 223-226 (1991).",Polypeptide-metal cluster connectivities in Cd(II) GAL4,published,journal,FEBS Lett.,,281,1-2,,,,,,,,,,,,,,,,,,,,,,223,226,1991, citations,entry_citation,16490,49156,1,,entry citation,,,,,,Solution Structure of protein sf3929 from Shigella flexneri 2a. Northeast Structural Genomics Consortium target SfR81/Ontario Center for Structural Proteomics Target sf3929,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,16491,49180,1,,entry citation,,,,,,Solution structure of peptidyl-prolyl cis-trans isomerase from Burkholderia pseudomallei complexed with Cycloheximide-N-ethylethanoate,in preparation,journal,To be Published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16492,49205,1,,entry citation,,,20713740,,,Mechanism for pH-dependent gene regulation by amino-terminus-mediated homooligomerization of Bacillus subtilis anti-trp RNA-binding attenuation protein.,published,journal,Proc. Natl. Acad. Sci. 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J.,Biophysical journal,99,5,,,,,,,,,,,,,,,,,,,,,,L37,L39,2010, citations,entry_citation,16501,49404,1,,entry citation,,,20816043,,,Contribution of long-range interactions to the secondary structure of an unfolded globin.,published,journal,Biophys. J.,Biophysical journal,99,5,,,,,,,,,,,,,,,,,,,,,,L37,L39,2010, citations,entry_citation_1,16502,49418,1,,entry citation,,,9719643,10.1006/jmbi.1998.1977,,"Solution structure of acidic fibroblast growth factor bound to 1,3, 6-naphthalenetrisulfonate: a minimal model for the anti-tumoral action of suramins and suradistas.",published,journal,J. Mol. Biol.,,281,,,,,,,,,,,,,,,,,,,,,,,899,915,1998, citations,entry_citacion_2,16502,49419,2,,reference citation,,,7521397,10.1006/jmbi.1994.1558,,1H-NMR assignment and solution structure of human acidic fibroblast growth factor activated by inositol hexasulfate,published,journal,J. Mol. Biol.,,242,,,,,,,,,,,,,,,,,,,,,,,81,98,1994, citations,entry_citation,16503,49436,1,,entry citation,,,20085318,,,NMR spectroscopy reveals that RNase A is chiefly denatured in 40% acetic acid: implications for oligomer formation by 3D domain swapping.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,132,5,,,,,,,,,,,,,,,,,,,,,,1621,1630,2010, citations,entry_citation,16504,49454,1,,entry citation,,,19766594,,,NMR solution structure of human cannabinoid receptor-1 helix 7/8 peptide: candidate electrostatic interactions and microdomain formation.,published,journal,Biochem. Biophys. Res. Commun.,Biochemical and biophysical research communications,390,3,,,,,,,,,,,,,,,,,,,,,,441,446,2009, citations,citation_1,16505,49470,1,,entry citation,,,19913031,,,Structure of the flexible amino-terminal domain of prion protein bound to a sulfated glycan.,published,journal,J. Mol. Biol.,Journal of molecular biology,395,3,,,,,,,,,,,,,,,,,,,,,,475,490,2010, citations,entry_citation,16506,49489,1,,entry citation,,,20182923,,,Backbone chemical shift assignments of the acyl-acyl carrier protein intermediates of the fatty acid biosynthesis pathway of Plasmodium falciparum.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,1,,,,,,,,,,,,,,,,,,,,,,83,85,2010, citations,entry_citation,16508,49527,1,,entry citation,,,19918058,,,Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,106,48,,,,,,,,,,,,,,,,,,,,,,20306,20311,2009, citations,entry_citation,16509,49543,1,,entry citation,,,20030366,,,Decoding of lipoprotein-receptor interactions: properties of ligand binding modules governing interactions with apolipoprotein E.,published,journal,Biochemistry,Biochemistry,49,6,,,,,,,,,,,,,,,,,,,,,,1207,1216,2010, citations,entry_citation,1651,49562,1,,entry citation,,,,,"Evans, Philip A., Topping, Karen D., Woolfson, Derek N., Dobson, Christopher M., ""Hydrophobic Clustering in Nonnative States of a Protein: Interpretation of Chemical Shifts in NMR Spectra of Denatured States of Lysozyme,"" Proteins: Struct. Funct. Genet. 9, 248-266 (1991).","Hydrophobic Clustering in Nonnative States of a Protein: Interpretation of Chemical Shifts in NMR Spectra of Denatured States of Lysozyme",published,journal,Proteins: Struct. Funct. Genet.,,9,,,,,,,,,,,,,,,,,,,,,,,248,266,1991, citations,citation1,16510,49575,1,,entry citation,,,19293276,,,The solution structure of the first PHD finger of autoimmune regulator in complex with non-modified histone H3 tail reveals the antagonistic role of H3R2 methylation,published,journal,Nucleic Acids Res.,,37,9,,,,,,,,,,,,,,,,,,,,,,2951,2961,2009, citations,entry_citation,16511,49593,1,,entry citation,,,20411530,,,A doppel alpha-helix peptide fragment mimics the copper(II) interactions with the whole protein.,published,journal,Chemistry,"Chemistry (Weinheim an der Bergstrasse, Germany)",16,21,,,,,,,,,,,,,,,,,,,,,,6212,6223,2010, citations,entry_citation,16512,49609,1,,entry citation,,,19918058,,,Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,106,48,,,,,,,,,,,,,,,,,,,,,,20306,20311,2009, citations,entry_citation,16514,49623,1,,entry citation,,,19918058,,,Dynamic structure of lipid-bound synaptobrevin suggests a nucleation-propagation mechanism for trans-SNARE complex formation.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,106,48,,,,,,,,,,,,,,,,,,,,,,20306,20311,2009, citations,citations,16515,49641,1,,entry citation,,,,,,Macromolecular Structure Determination by NMR Sepectroscopy,published,book,Structural Bioinformatics 2nd edition,,,,,,,"Structural Bioinformatcis, 2nd edition",Macromolecular Structure Determination by NMR Sepectroscopy,,,John Wiley,New York,,,,,,,,,,,,,93,142,2009, citations,entry_citation,16516,49661,1,,entry citation,,,19888678,,,Chemical shift assignments for human apurinic/apyrimidinic endonuclease 1.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,1,,,,,,,,,,,,,,,,,,,,,,5,8,2010, citations,entry_citation,16517,49676,1,,entry citation,,,21904062,,,"Solution structure of an arsenate reductase-related protein, YffB, from Brucella melitensis, the etiological agent responsible for brucellosis.",published,journal,Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.,"Acta crystallographica. Section F, Structural biology and crystallization communications",67,9,,,,,,,,,,,,,,,,,,,,,,1129,1136,2011, citations,entry_citation,16518,49696,1,,entry citation,,,19886864,,,Structural insights into the catalytic mechanism of Trypanosoma cruzi GPXI (glutathione peroxidase-like enzyme I).,published,journal,Biochem. J.,The Biochemical journal,425,3,,,,,,,,,,,,,,,,,,,,,,513,522,2010, citations,citations,16519,49711,1,,entry citation,,,,,,TBD,in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1652,49731,1,,entry citation,,,,,"Theriault, Y., Boulanger, Y., St. Pierre, Serge A., ""Structural Determination of the Vasoactive Intestinal Peptide by Two-Dimensional 1H-NMR Spectroscopy,"" Biopolymers 31, 459-464 (1991).","Structural Determination of the Vasoactive Intestinal Peptide by Two-Dimensional 1H-NMR Spectroscopy",published,journal,Biopolymers,,31,,,,,,,,,,,,,,,,,,,,,,,459,464,1991, citations,citations,16520,49744,1,,entry citation,,,20073081,,,"Rapid, robotic, small-scale protein production for NMR screening and structure determination.",published,journal,Protein Sci.,Protein science : a publication of the Protein Society,19,3,,,,,,,,,,,,,,,,,,,,,,570,578,2010, citations,entry_citation,16521,49763,1,,entry citation,,,,,,NMR solution structure of CV_2116 from Chromobacterium violaceum. Northeast Structural Genomics Consortium Target CvT4(1-82),in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16522,49794,1,,entry citation,,,20411530,,,A Doppel alpha-Helix Peptide Fragment Mimics the Copper(II) Interactions with the Whole Protein.,published,journal,Chemistry,"Chemistry (Weinheim an der Bergstrasse, Germany)",16,21,,,,,,,,,,,,,,,,,,,,,,6212,6223,2010, citations,entry_citation,16523,49814,1,,entry citation,,,19941091,,,NMR assignment and backbone dynamics of the pore-forming domain of colicin A.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,1,,,,,,,,,,,,,,,,,,,,,,33,36,2010, citations,entry_citation,16524,49832,1,,entry citation,,,20659690,,,Recognition of intermediate functionality by acyl carrier protein over a complete cycle of fatty acid biosynthesis,published,journal,Chem. Biol.,,17,7,,,,,,,,,,,,,,,,,,,,,,776,785,2010, citations,reference_citation,16524,49833,2,,reference citation,,,20136099,,,Solution structure of an acyl carrier protein domain from a fungal type I polyketide synthase.,published,journal,Biochemistry,Biochemistry,49,10,,,,,,,,,,,,,,,,,,,,,,2186,2193,2010, citations,entry_citation,16525,49852,1,,entry citation,,,20659690,,,Recognition of intermediate functionality by acyl carrier protein over a complete cycle of fatty acid biosynthesis,published,journal,Chem. Biol.,,17,7,,,,,,,,,,,,,,,,,,,,,,776,785,2010, citations,entry_citation,16526,49871,1,,entry citation,,,20659690,,,Recognition of intermediate functionality by acyl carrier protein over a complete cycle of fatty acid biosynthesis,published,journal,Chem. Biol.,,17,7,,,,,,,,,,,,,,,,,,,,,,776,785,2010, citations,entry_citation,16527,49892,1,,entry citation,,,20659690,,,Recognition of intermediate functionality by acyl carrier protein over a complete cycle of fatty acid biosynthesis,published,journal,Chem. Biol.,,17,7,,,,,,,,,,,,,,,,,,,,,,776,785,2010, citations,entry_citation,16528,49911,1,,entry citation,,,20659690,,,Recognition of intermediate functionality by acyl carrier protein over a complete cycle of fatty acid biosynthesis,published,journal,Chem. Biol.,,17,7,,,,,,,,,,,,,,,,,,,,,,776,785,2010, citations,entry_citation,16529,49930,1,,entry citation,,,20182923,,,Backbone chemical shift assignments of the acyl-acyl carrier protein intermediates of the fatty acid biosynthesis pathway of Plasmodium falciparum.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,1,,,,,,,,,,,,,,,,,,,,,,83,85,2010, citations,entry_citation,16557,50408,1,,entry citation,,,,,,"Solution Structure Of Protein SOS-response transcriptional repressor, LexA From Eubacterium rectale. Northeast Structural Genomics Consortium Target ErR9A",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,16558,50434,1,,reference citation,,,16636753,,,"3C, 15N and 1H resonance assignment of the PDZ1 domain of MAGI-1 using QUASI.",published,journal,J. Biomol. NMR,,36,1,,,,,,,,,,,,,,,,,,,,,,33,33,2006, citations,entry_citation,1653,49947,1,,entry citation,,,,,"Evans, Philip A., Topping, Karen D., Woolfson, Derek N., Dobson, Christopher M., ""Hydrophobic Clustering in Nonnative States of a Protein: Interpretation of Chemical Shifts in NMR Spectra of Denatured States of Lysozyme,"" Proteins: Struct. Funct. Genet. 9, 248-266 (1991).","Hydrophobic Clustering in Nonnative States of a Protein: Interpretation of Chemical Shifts in NMR Spectra of Denatured States of Lysozyme",published,journal,Proteins: Struct. Funct. Genet.,,9,,,,,,,,,,,,,,,,,,,,,,,248,266,1991, citations,entry_citation,16530,49960,1,,entry citation,,,20182923,,,Backbone chemical shift assignments of the acyl-acyl carrier protein intermediates of the fatty acid biosynthesis pathway of Plasmodium falciparum.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,1,,,,,,,,,,,,,,,,,,,,,,83,85,2010, citations,entry_citation,16531,49977,1,,entry citation,,,20182923,,,Backbone chemical shift assignments of the acyl-acyl carrier protein intermediates of the fatty acid biosynthesis pathway of Plasmodium falciparum.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,1,,,,,,,,,,,,,,,,,,,,,,83,85,2010, citations,entry_citation,16532,49994,1,,entry citation,,,20182923,,,Backbone chemical shift assignments of the acyl-acyl carrier protein intermediates of the fatty acid biosynthesis pathway of Plasmodium falciparum.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,1,,,,,,,,,,,,,,,,,,,,,,83,85,2010, citations,entry_citation,16533,50011,1,,entry citation,,,20182923,,,Backbone chemical shift assignments of the acyl-acyl carrier protein intermediates of the fatty acid biosynthesis pathway of Plasmodium falciparum.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,1,,,,,,,,,,,,,,,,,,,,,,83,85,2010, citations,1,16534,50028,1,,entry citation,,,20106953,,,Structure of the Arabidopsis thaliana DCL4 DUF283 domain reveals a noncanonical double-stranded RNA-binding fold for protein-protein interaction.,published,journal,RNA,"RNA (New York, N.Y.)",16,3,,,,,,,,,,,,,,,,,,,,,,474,481,2010, citations,entry_citation,16536,50042,1,,entry citation,,,,,,The structure of the E1064A mutant reveals ATP-dependent conformational changes in the ATP7B N-domain.,in preparation,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16537,50058,1,,entry citation,,,20012716,,,Backbone assignments of the 26 kDa neuron-specific ubiquitin carboxyl-terminal hydrolase L1 (UCH-L1).,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,1,,,,,,,,,,,,,,,,,,,,,,41,43,2010, citations,MA3M_Assignments,16538,50076,1,,entry citation,,,20020227,,,Resonance Assignment and Secondary Structure of the Middle MA-3 Domain and Complete Tandem MA-3 Region of the Tumour Suppressor Protein Pdcd4.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,1,,,,,,,,,,,,,,,,,,,,,,49,53,2009, citations,entry_1,16539,50097,1,,entry citation,,,,,,Not known,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1654,50115,1,,entry citation,,,,,"Aumelas, Andre, Chiche, Laurent, Mahe, Eve, Le-Nguyen, Dung, Sizun, Philippe, Berthault, Patrick, Perly, Bruno, ""Determination of the structure of [Nle7]-endothelin by 1H NMR,"" Int. J. Pept. Protein Res. 37, 315-324 (1991).",Determination of the structure of [Nle7]-endothelin by 1H NMR,published,journal,Int. J. Pept. Protein Res.,,37,,,,,,,,,,,,,,,,,,,,,,,315,324,1991, citations,entry_1,16540,50129,1,,entry citation,,,,,,Not known,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16541,50147,1,,entry citation,,,20300892,,,Assignment of the orphan nuclear receptor Nurr1 by NMR.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,1,,,,,,,,,,,,,,,,,,,,,,101,105,2010, citations,MA-3_M-C_citations,16542,50162,1,,entry citation,,,20020227,10.1007/s12104-009-9205-1,,Resonance Assignment and Secondary Structure of the Middle MA-3 Domain and Complete Tandem MA-3 Region of the Tumour Suppressor Protein Pdcd4.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,1,,,,,,,,,,,,,,,,,,,,,,49,53,2009, citations,entry_citation,16543,50178,1,,entry citation,,,20041693,,,Differential phospholipid binding of alpha-synuclein variants implicated in Parkinson's disease revealed by solution NMR spectroscopy.,published,journal,Biochemistry,Biochemistry,49,5,,,,,,,,,,,,,,,,,,,,,,862,871,2010, citations,entry_citation,16544,50192,1,,entry citation,,,22730300,,,The N-terminus of the human RecQL4 helicase is a homeodomain-like DNA interaction motif.,published,journal,Nucleic Acids Res.,Nucleic acids research,40,17,,,,,,,,,,,,,,,,,,,,,,8309,8324,2012, citations,entry_citation,16545,50210,1,,entry citation,,,,,,Solution structure of protein CV0237 from Chromobacterium violaceum,in preparation,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16546,50235,1,,entry citation,,,20041693,,,Differential phospholipid binding of alpha-synuclein variants implicated in Parkinson's disease revealed by solution NMR spectroscopy.,published,journal,Biochemistry,Biochemistry,49,5,,,,,,,,,,,,,,,,,,,,,,862,871,2010, citations,entry_citation,16547,50249,1,,entry citation,,,20041693,,,Differential phospholipid binding of alpha-synuclein variants implicated in Parkinson's disease revealed by solution NMR spectroscopy.,published,journal,Biochemistry,Biochemistry,49,5,,,,,,,,,,,,,,,,,,,,,,862,871,2010, citations,entry_citation,16548,50263,1,,entry citation,,,20041693,,,Differential phospholipid binding of alpha-synuclein variants implicated in Parkinson's disease revealed by solution NMR spectroscopy.,published,journal,Biochemistry,Biochemistry,49,5,,,,,,,,,,,,,,,,,,,,,,862,871,2010, citations,entry_citation,16549,50277,1,,entry citation,,,,,,Solution NMR structure and DNA binding mode of the Mus81 n-terminal helix-hairpin-helix domain.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1655,50302,1,,entry citation,,,,,"Aumelas, Andre, Chiche, Laurent, Mahe, Eve, Le-Nguyen, Dung, Sizun, Philippe, Berthault, Patrick, Perly, Bruno, ""Determination of the structure of [Nle7]-endothelin by 1H NMR,"" Int. J. Pept. Protein Res. 37, 315-324 (1991).",Determination of the structure of [Nle7]-endothelin by 1H NMR,published,journal,Int. J. Pept. Protein Res.,,37,,,,,,,,,,,,,,,,,,,,,,,315,324,1991, citations,entry_citation,16550,50316,1,,entry citation,,,20153292,,,Specific motifs of the V-ATPase a2-subunit isoform interact with catalytic and regulatory domains of ARNO.,published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1797,8,,,,,,,,,,,,,,,,,,,,,,1398,1409,2010, citations,entry_citation,16551,50330,1,,entry citation,,,20153292,,,Specific motifs of the V-ATPase a2-subunit isoform interact with catalytic and regulatory domains of ARNO.,published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1797,8,,,,,,,,,,,,,,,,,,,,,,1398,1409,2010, citations,entry_citation,16555,50345,1,,entry citation,,,19921549,,,"1H, 15N and 13C assignments of the dimeric C-terminal domain of HIV-1 capsid protein.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,1,,,,,,,,,,,,,,,,,,,,,,21,23,2010, citations,entry_citation,16556,50364,1,,entry citation,,,,,,"Solution NMR structure of Streptomyces coelicolor SCO3027 modelled with Zn+2 bound. Northeast Structural Genomics Consortium Target RR58.",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_2,16587,51189,2,,reference citation,,,,,,Folding and fibrillogenesis: clues from beta2-microglobulin in aqueous trifluoroethanol,submitted,journal,na,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_2,16558,50435,2,,entry citation,,,21238461,,,The Structural and Dynamic Response of MAGI-1 PDZ1 with Noncanonical Domain Boundaries to the Binding of Human Papillomavirus E6,published,journal,J. Mol. Biol.,,406,5,,,,,,,,,,,,,,,,,,,,,,745,763,2011, citations,citation_1,16559,50457,1,,entry citation,,,21238461,,,The Structural and Dynamic Response of MAGI-1 PDZ1 with Noncanonical Domain Boundaries to the Binding of Human Papillomavirus E6,published,journal,J. Mol. Biol.,,406,5,,,,,,,,,,,,,,,,,,,,,,745,763,2011, citations,entry_citation,1656,50479,1,,entry citation,,,,,"South, Terri L., Blake, Paul R., Hare, Dennis R., Summers, Michael F., ""C-Terminal Retroviral-Type Zinc Finger Domain from the HIV-1 Nucleocapsid Protein Is Structurally Similar to the N-Terminal Zinc Finger Domain,"" Biochemistry 30, 6342-6349 (1991).","C-Terminal Retroviral-Type Zinc Finger Domain from the HIV-1 Nucleocapsid Protein Is Structurally Similar to the N-Terminal Zinc Finger Domain",published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,6342,6349,1991, citations,entry_citation,16560,50492,1,,entry citation,,,,,,Solution NMR Structure of uncharacterized protein from gene locus NE0665 of Nitrosomonas europaea. Northeast Structural Genomics Target NeR103A,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16561,50519,1,,entry citation,,,,,,Solution NMR structure of a Bacterial Ig-like (Big_3) domain from Bacillus cereus. Northeast Structural Genomics Consortium target BcR147A.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16562,50560,1,,entry citation,,,,,,"SOLUTION NMR STRUCTURE OF DENOVO DESIGNED ROSSMANN 2x2 FOLD PROTEIN, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET OR16",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,16563,50593,1,,entry citation,,,,,,Solution NMR structure of Lin0431 protein from Listeria innocua. Northeast Structural Genomics Consortium Target LkR112,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16564,50616,1,,entry citation,,,,,,NMR Structure of Agrobacterium tumefaciens protein Atu1219,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16565,50640,1,,entry citation,,,19854202,,,Triosephosphate Isomerase: (15)N and (13)C Chemical Shift Assignments and Conformational Change upon Ligand Binding by Magic-Angle Spinning Solid-State NMR Spectroscopy.,published,journal,J. Mol. Biol.,Journal of molecular biology,397,1,,,,,,,,,,,,,,,,,,,,,,233,248,2010, citations,entry_citation,16566,50657,1,,entry citation,,,19854202,,,Triosephosphate Isomerase: (15)N and (13)C Chemical Shift Assignments and Conformational Change upon Ligand Binding by Magic-Angle Spinning Solid-State NMR Spectroscopy.,published,journal,J. Mol. Biol.,Journal of molecular biology,397,1,,,,,,,,,,,,,,,,,,,,,,233,248,2010, citations,citation_1,16567,50676,1,,entry citation,,,20309651,,,"1H, 13C, and 15N chemical shift assignments for the RNA recognition motif of Nab3.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,1,,,,,,,,,,,,,,,,,,,,,,119,121,2010, citations,entry_citation,16568,50691,1,,entry citation,,,21154411,,,Structures of domains I and IV from YbbR are representative of a widely distributed protein family.,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,20,2,,,,,,,,,,,,,,,,,,,,,,396,405,2011, citations,entry_citation,16569,50711,1,,entry citation,,,,,,Solution NMR structure of the N-terminal domain of cg2496 protein from Corynebacterium glutamicum,in preparation,journal,Proteins: Struct. Funct. Genet.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1657,50742,1,,entry citation,,,,,"Yamazaki, Toshio, Yoshida, Mayumi, Kanaya, Shigenori, Nakamura, Haruki, Nagayama, Kuniaki, ""Assignments of Backbone 1H, 13C, 15N Resonances and Secondary Structure of Ribonuclease H from Escherichia coli by Heteronuclear Three-Dimensional NMR Spectroscopy,"" Biochemistry 30, 6036-6047 (1991).","Assignments of Backbone 1H, 13C, 15N Resonances and Secondary Structure of Ribonuclease H from Escherichia coli by Heteronuclear Three-Dimensional NMR Spectroscopy",published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,6036,6047,1991, citations,entry_citation,16570,50755,1,,entry citation,,,21154411,,,Structures of domains I and IV from YbbR are representative of a widely distributed protein family,published,journal,Protein Sci.,,20,2,,,,,,,,,,,,,,,,,,,,,,396,405,2011, citations,entry_citation,16571,50779,1,,entry citation,,,20020226,,,NMR assignments of the DNA binding domain of Ml4 protein from Mesorhizobium loti.,published,journal,Biomol. 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NMR,,25,,,,,,,,,,,,,,,,,,,,,,,133,145,2003, citations,entry_citation,16585,51157,1,,entry citation,,,20415411,,,Importance of the C-terminal loop l137-s141 for the folding and folding stability of staphylococcal nuclease,published,journal,Biochemistry,Biochemistry,49,20,,,,,,,,,,,,,,,,,,,,,,4318,4326,2010, citations,entry_citation,16586,51173,1,,entry citation,,,20226184,,,Structural basis for a PABPN1 aggregation-preventing antibody fragment in OPMD.,published,journal,FEBS Lett.,FEBS letters,584,8,,,,,,,,,,,,,,,,,,,,,,1558,1564,2010, citations,citation_1,16587,51188,1,,entry citation,,,20028983,,,Native-unlike long-lived intermediates along the folding pathway of the amyloidogenic protein beta2-microglobulin revealed by real-time two-dimensional NMR.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,285,8,,,,,,,,,,,,,,,,,,,,,,5827,5835,2010, citations,citation_4,16587,51191,4,,reference citation,,,15811375,,,Nuclear magnetic resonance characterization of the refolding intermediate of beta2-microglobulin trapped by non-native prolyl peptide bond.,published,journal,J. Mol. Biol.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16588,51210,1,,entry citation,,,20159554,,,Asymmetric Activation of the Hsp90 Dimer by Its Cochaperone Aha1.,published,journal,Mol. Cell,Molecular cell,37,3,,,,,,,,,,,,,,,,,,,,,,344,354,2010, citations,citation_1,16589,51226,1,,entry citation,,,20848643,,,The repeat domain of the type III effector protein PthA shows a TPR-like structure and undergoes conformational changes upon DNA interaction.,published,journal,Proteins,Proteins,78,16,,,,,,,,,,,,,,,,,,,,,,3386,3395,2010, citations,entry_citation,16590,51241,1,,entry citation,,,20439752,,,Structure of the EF-hand domain of polycystin-2 suggests a mechanism for Ca2+-dependent regulation of polycystin-2 channel activity.,published,journal,Proc. Natl. Acad. Sci. 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Biol.,Journal of molecular biology,400,4,,,,,,,,,,,,,,,,,,,,,,922,934,2010, citations,entry_citation,16594,51323,1,,entry citation,,,,,,Solution Structure of DnaK protein from Agrobacterium tumefaciens C58. Northeast Structural Genomics Consortium target AtT12/Ontario Center for Structural Proteomics Target atc0888,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16595,51351,1,,entry citation,,,18370385,10.1021/ja077302m,,Solid-state NMR Spectroscopy of human immunodeficiency virus fusion peptides associated with host-cell-like membranes: 2D correlation spectra and distance measurements support a fully extended conformation and models for specific antiparallel strand registries,published,journal,J. Am. Chem. Soc.,,130,16,,,,,,,,,,,,,,,,,,,,,,5459,5471,2008, citations,entry_citation,16596,51365,1,,entry citation,,,20098424,,,Solution structures of the two PBZ domains from human APLF and their interaction with poly(ADP-ribose).,published,journal,Nat. Struct. Mol. Biol.,Nature structural and molecular biology,17,2,,,,,,,,,,,,,,,,,,,,,,241,243,2010, citations,Sun_JACS,16597,51386,1,,entry citation,,,19711890,10.1021/ja905198q,,C13-C13 Correlation Spectroscopy of Membrane-Associated Influenza Virus Fusion Peptide Strongly Supports a Helix-Turn-Helix Motif and Two Turn Conformations,published,journal,J. Am. Chem. Soc.,,131,37,,,,,,,,,,,,,,,,,,,,,,13228,13229,2009, citations,Bodner_JCP,16597,51387,2,,reference citation,,,18266436,10.1063/1.2829984,,C13-C13 and N15-C13 correlation spectroscopy of membrane-associated and uniformly labeled human immunodeficiency virus and influenza fusion peptides: Amino acid-type assignments and evidence for multiple conformations,published,journal,J. Chem. Phys.,,128,5,,,,,,,,,,,,,,,,,,,,,,052319,,2008, citations,entry_citation,16598,51401,1,,entry citation,,,20383614,,,Backbone resonance assignments of an artificially engineered TEM-1/PSE-4 Class A -lactamase chimera.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,2,,,,,,,,,,,,,,,,,,,,,,127,130,2010, citations,entry_citation,16599,51426,1,,entry citation,,,20926380,,,NMR-derived topology of a GFP-photoprotein energy transfer complex.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,285,52,,,,,,,,,,,,,,,,,,,,,,40891,40900,2010, citations,entry_citation,1660,51443,1,,entry citation,,,,,"Miura, Shigetoshi, Ichikawa, Yoshiyuki, ""Proton nuclear magnetic resonance investigation of adrenodoxin (Assignment of aromatic resonances and evidence for a conformational similarity with ferredoxin from Spirulina platensis,"" Eur. J. Biochem. 197, 747-757 (1991).","Proton nuclear magnetic resonance investigation of adrenodoxin (Assignment of aromatic resonances and evidence for a conformational similarity with ferredoxin from Spirulina platensis",published,journal,Eur. J. Biochem.,,197,,,,,,,,,,,,,,,,,,,,,,,747,757,1991, citations,entry_citation,16600,51456,1,,entry citation,,,20926380,,,NMR-derived topology of a GFP-photoprotein energy transfer complex.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,285,52,,,,,,,,,,,,,,,,,,,,,,40891,40900,2010, citations,citation,16601,51472,1,,entry citation,,,22593157,,,Structural analysis of hepatitis C virus core-e1 signal Peptide and requirements for cleavage of the genotype 3a signal sequence by signal Peptide peptidase.,published,journal,J. Virol.,Journal of virology,86,15,,,,,,,,,,,,,,,,,,,,,,7818,7828,2012, citations,entry_citation,16602,51490,1,,entry citation,,,20044833,,,Functional delivery of a membrane protein into oocyte membranes using bicelles.,published,journal,Biochemistry,Biochemistry,49,4,,,,,,,,,,,,,,,,,,,,,,653,655,2010, citations,citations,16603,51505,1,,entry citation,,,22734684,,,Three-dimensional structure and determinants of stability of the iron-sulfur cluster scaffold protein IscU from Escherichia coli.,published,journal,Biochemistry,Biochemistry,51,28,,,,,,,,,,,,,,,,,,,,,,5557,5563,2012, citations,entry_citation,16604,51529,1,,entry citation,,,20306311,,,NMR resonance assignments of an engineered neomycin-sensing riboswitch RNA bound to ribostamycin and tobramycin,published,journal,Biomol. 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Biol.,Journal of molecular biology,400,4,,,,,,,,,,,,,,,,,,,,,,724,742,2010, citations,entry_citation,16614,51759,1,,entry citation,,,20174897,,,"1H, 13C and 15N resonance assignments of a highly-soluble murine interleukin-3 analogue with wild-type bioactivity.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,1,,,,,,,,,,,,,,,,,,,,,,73,77,2010, citations,1,16615,51776,1,,entry citation,,,,,,Backbone NMR assignment of E. coli HU proteins.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16616,51794,1,,entry citation,,,20949107,,,Solution Structure and Dynamics of the I214V Mutant of the Rabbit Prion Protein.,published,journal,PLoS ONE,PloS one,5,10,,,,,,,,,,,,,,,,,,,,,,e13273,,2010, citations,citation_1,16617,51808,1,,entry citation,,,20156445,,,"Structure of avian thymic hormone, a high-affinity avian beta-parvalbumin, in the Ca2+-free and Ca2+-bound states.",published,journal,J. Mol. Biol.,Journal of molecular biology,397,4,,,,,,,,,,,,,,,,,,,,,,991,1002,2010, citations,entry_citation,16618,51827,1,,entry citation,,,20226195,,,Structural basis of the regulation of the CbpA co-chaperone by its specific modulator CbpM.,published,journal,J. Mol. Biol.,Journal of molecular biology,398,1,,,,,,,,,,,,,,,,,,,,,,111,121,2010, citations,entry_citation,16619,51841,1,,entry citation,,,20127209,,,"Sequence-specific 1H, 13C, and 15N resonance assignments of Diva (Boo), an apoptosis regulator of the Bcl-2 family.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,1,,,,,,,,,,,,,,,,,,,,,,65,68,2010, citations,entry_citation,1662,51860,1,,entry citation,,,,,"Miura, Shigetoshi, Ichikawa, Yoshiyuki, ""Proton nuclear magnetic resonance investigation of adrenodoxin (Assignment of aromatic resonances and evidence for a conformational similarity with ferredoxin from Spirulina platensis,"" Eur. J. 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Biol.,Journal of molecular biology,311,2,,,,,,,,,,,,,,,,,,,,,,357,371,2001, citations,entry_citation,16623,51927,1,,entry citation,,,20017557,,,Structural and functional characterization of the monomeric U-box domain from E4B.,published,journal,Biochemistry,Biochemistry,49,2,,,,,,,,,,,,,,,,,,,,,,347,355,2010, citations,entry_citation,16624,51947,1,,entry citation,,,20136099,,,Solution structure of an acyl carrier protein domain from a fungal type I polyketide synthase.,published,journal,Biochemistry,Biochemistry,49,10,,,,,,,,,,,,,,,,,,,,,,2186,2193,2010, citations,entry_citation,16626,51964,1,,entry citation,,,20155903,,,Side-chain chi(1) conformations in urea-denatured ubiquitin and protein G from (3)J coupling constants and residual dipolar couplings.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,132,9,,,,,,,,,,,,,,,,,,,,,,3196,3203,2010, citations,entry_citation,16627,51981,1,,entry citation,,,20155903,,,Side-chain chi(1) conformations in urea-denatured ubiquitin and protein G from (3)J coupling constants and residual dipolar couplings.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,132,9,,,,,,,,,,,,,,,,,,,,,,3196,3203,2010, citations,citation_1,16628,51998,1,,entry citation,,,20449776,,,Resonance assignments of the nucleotide-free wildtype MloK1 cyclic nucleotide-binding domain.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,2,,,,,,,,,,,,,,,,,,,,,,147,150,2010, citations,entry_citation,16629,52016,1,,entry citation,,,,,,Structural and functional study of SlyD from helicobacter pylori,in preparation,journal,J. Am. Chem. Soc.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1663,52032,1,,entry citation,,,,,"Fairbrother, Wayne J., Cavanagh, John, Dyson, H. Jane, Palmer, Arthur G., III, Sutrina, Sarah L., Reizer, Jonathan, Saier, MIlton H. Jr., Wright, Peter E., ""Polypeptide Backbone Resonance Assignments and Secondary Structure of Bacillus subtilis Enzyme III(glc) Determined by Two-Dimensional and Three-Dimensional Heteronuclear NMR Spectroscopy,"" Biochemistry 30, 6896-6907 (1991).",Polypeptide Backbone Resonance Assignments and Secondary Structure of Bacillus subtilis Enzyme III(glc) Determined by Two-Dimensional and Three-Dimensional Heteronuclear NMR Spectroscopy,published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,6896,6907,1991, citations,entry_citation,16630,52045,1,,entry citation,,,20165934,,,"1H, 13C, and 15N NMR assignments of StnII-Y111N, a highly impaired mutant of the sea anemone actinoporin Sticholysin II",published,journal,Biomol. NMR Assignments,,4,1,,,,,,,,,,,,,,,,,,,,,,69,72,2010, citations,entry_citation,16632,52062,1,,entry citation,,,22314704,,,"N-terminal Dbl domain of the RhoGEF, Kalirin",published,journal,J. Biomol. NMR,,52,3,,,,,,,,,,,,,,,,,,,,,,269,276,2012, citations,reference_citation,16632,52063,2,,reference citation,,,,,,"NMR studies of the structure, dynamics and substrate interaction of Kalirin GEF1 domain",published,abstract,,,,,,,,,,,,,,,The 16th Triennial Conference for the International Society of Magnetic Resonance,Hengchun,Pingtung,Taiwan,2009-10-14,2009-10-19,P1-50,,,,,166,,2007, citations,entry_citation,16633,52103,1,,entry citation,,,20677202,,,Chemical synthesis and structure of the prokineticin bv8.,published,journal,Chembiochem,Chembiochem : a European journal of chemical biology,11,13,,,,,,,,,,,,,,,,,,,,,,1882,1888,2010, citations,entry_citation,16634,52120,1,,entry citation,,,20562025,,,Backbone dynamics and global effects of an activating mutation in minimized Mtu RecA inteins.,published,journal,J. Mol. Biol.,Journal of molecular biology,400,4,,,,,,,,,,,,,,,,,,,,,,755,767,2010, citations,entry_citation,16635,52137,1,,entry citation,,,20310067,,,Solution structure of the N-terminal domain of Bacillus subtilis delta subunit of RNA polymerase and its classification based on structural homologs.,published,journal,Proteins,Proteins,78,7,,,,,,,,,,,,,,,,,,,,,,1807,1810,2010, citations,entry_citation,16636,52161,1,,entry citation,,,20302877,,,NMR solution structure and DNA-binding model of the DNA-binding domain of competence protein A.,published,journal,J. Mol. Biol.,Journal of molecular biology,398,2,,,,,,,,,,,,,,,,,,,,,,248,263,2010, citations,citation_1,16637,52181,1,,entry citation,,,20042604,,,A conformational switch in the scaffolding protein NHERF1 controls autoinhibition and complex formation.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,285,13,,,,,,,,,,,,,,,,,,,,,,9981,9994,2010, citations,entry_citation,16638,52200,1,,entry citation,,,20042604,,,A conformational switch in the scaffolding protein NHERF1 controls autoinhibition and complex formation.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,285,13,,,,,,,,,,,,,,,,,,,,,,9981,9994,2010, citations,citation_1,16639,52220,1,,entry citation,,,20223219,,,Mode of interaction between beta2GPI and lipoprotein receptors suggests mutually exclusive binding of beta2GPI to the receptors and anionic phospholipids.,published,journal,"Structure (Cambridge, MA, U. S.)","Structure (Cambridge, MA, United States)",18,3,,,,,,,,,,,,,,,,,,,,,,366,376,2010, citations,entry_citation,1664,52244,1,,entry citation,,,,,"Lancelin, Jean-Marc, Kohda, Daisuke, Tate, Shin-ichi, Yanagawa, Yuchio, Abe, Teruo, Satake, Mei, Inagaki, Fuyuhiko, ""Tertiary Structure of Conotoxin GIIIA in Aqueous Solution,"" Biochemistry 30, 6908-6916 (1991).",Tertiary Structure of Conotoxin GIIIA in Aqueous Solution,published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,6908,6916,1991, citations,citations,16640,52257,1,,entry citation,,,,,,"Solution NMR Structure of 26S protease regulatory subunit 8 from H.sapiens, Northeast Structural Genomics Consortium Target HR3102A",in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16641,52282,1,,entry citation,,,21519904,,,"Solution structure, dynamics and thermodynamics of the three SH3 domains of CD2AP.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,50,2,,,,,,,,,,,,,,,,,,,,,,103,117,2011, citations,entry_citation,16642,52298,1,,entry citation,,,21519904,,,"Solution structure, dynamics and thermodynamics of the three SH3 domains of CD2AP.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,50,2,,,,,,,,,,,,,,,,,,,,,,103,117,2011, citations,entry_citation,16643,52313,1,,entry citation,,,21519904,,,"Solution structure, dynamics and thermodynamics of the three SH3 domains of CD2AP.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,50,2,,,,,,,,,,,,,,,,,,,,,,103,117,2011, citations,citations,16646,52329,1,,entry citation,,,20376532,,,"Solution structure of the RBD1,2 domains from human nucleolin.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,47,1,,,,,,,,,,,,,,,,,,,,,,79,83,2010, citations,entry_citation,16647,52348,1,,entry citation,,,,,,Solution NMR structure of SH3 domain from CPF_0587 (fragment 415-479) from Clostridium perfringens. Northeast Structural Genomics Consortium (NESG) Target CpR74A.,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16648,52401,1,,entry citation,,,21153711,,,Solution NMR and X-ray crystal structures of membrane-associated Lipoprotein-17 domain reveal a novel fold.,published,journal,J. Struct. Funct. Genomics,Journal of structural and functional genomics,12,1,,,,,,,,,,,,,,,,,,,,,,27,32,2011, citations,entry_citation,16649,52442,1,,entry citation,,,,,,Solution NMR structure of the PCP_red domain of light-independent protochlorophyllide reductase subunit B from Chlorobium tepidum. Northeast Structural Genomics Consortium Target CtR69A,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1665,52470,1,,entry citation,,,,,"Lancelin, Jean-Marc, Kohda, Daisuke, Tate, Shin-ichi, Yanagawa, Yuchio, Abe, Teruo, Satake, Mei, Inagaki, Fuyuhiko, ""Tertiary Structure of Conotoxin GIIIA in Aqueous Solution,"" Biochemistry 30, 6908-6916 (1991).",Tertiary Structure of Conotoxin GIIIA in Aqueous Solution,published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,6908,6916,1991, citations,entry_citation,16652,52483,1,,entry citation,,,,,,Solution NMR structure of asl3597 from Nostoc sp. PCC7120. Northeast Structural Genomics Consortium target NsR244.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16653,52511,1,,entry citation,,,20437142,,,"1H, 13C and 15N resonance assignment of the PDZ domain of HtrA from Streptococcus pneumoniae.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,1,,,,,,,,,,,,,,,,,,,,,,79,82,2010, citations,solution_structure_of_the_Human_mtRNAMet_f5C34,16654,52525,1,,entry citation,,,21168417,,,The human mitochondrial tRNAMet: structure/function relationship of a unique modification in the decoding of unconventional codons.,published,journal,J. Mol. Biol.,Journal of molecular biology,406,2,,,,,,,,,,,,,,,,,,,,,,257,274,2011, citations,Solution_structure_of_the_Human_Mitochondria_tRNAMet,16655,52549,1,,entry citation,,,21168417,,,The human mitochondrial tRNAMet: structure/function relationship of a unique modification in the decoding of unconventional codons.,published,journal,J. Mol. Biol.,Journal of molecular biology,406,2,,,,,,,,,,,,,,,,,,,,,,257,274,2011, citations,YabP_family,16656,52573,1,,entry citation,,,,,,Solution NMR structure of the Q251Q8_DESHY(21-82) protein from Desulfitobacterium Hafniense. Northeast Structural Genomics Consortium Target DhR8C.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16657,52604,1,,entry citation,,,20399186,,,Structure/function implications in a dynamic complex of the intrinsically disordered Sic1 with the Cdc4 subunit of an SCF ubiquitin ligase.,published,journal,"Structure (Cambridge, MA, U. S.)","Structure (Cambridge, MA, United States)",18,4,,,,,,,,,,,,,,,,,,,,,,494,506,2010, citations,citation_2,16657,52605,2,,reference citation,,,19008353,10.1073/pnas.0809222105,,Structure/function implications in a dynamic complex of the intrinsically disordered Sic1 with the Cdc4 subunit of an SCF ubiquitin ligase,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,105,46,,,,,,,,,,,,,,,,,,,,,,17772,17777,2008, citations,entry_citation,16658,52647,1,,entry citation,,,20471394,,,Spatial structure of the transmembrane domain heterodimer of ErbB1 and ErbB2 receptor tyrosine kinases.,published,journal,J. Mol. Biol.,Journal of molecular biology,400,2,,,,,,,,,,,,,,,,,,,,,,231,243,2010, citations,entry_citation,16659,52668,1,,entry citation,,,20399186,,,Structure/function implications in a dynamic complex of the intrinsically disordered Sic1 with the Cdc4 subunit of an SCF ubiquitin ligase.,published,journal,"Structure (Cambridge, MA, U. S.)","Structure (Cambridge, MA, United States)",18,4,,,,,,,,,,,,,,,,,,,,,,494,506,2010, citations,citation_2,16659,52669,2,,reference citation,,,19008353,10.1073/pnas.0809222105,,Structure/function implications in a dynamic complex of the intrinsically disordered Sic1 with the Cdc4 subunit of an SCF ubiquitin ligase,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,105,46,,,,,,,,,,,,,,,,,,,,,,17772,17777,2008, citations,entry_citation,1666,52712,1,,entry citation,,,,,"Klaus, Werner, Dieckmann, Thorsten, Wray, Victor, Schomburg, Dietmar, Wingender, Edgar, Mayer, Hubert, ""Investigation of the Solution Structure of the Human Parathyroid Hormone Fragment (1-34) by 1H NMR Spectroscopy, Distance Geometry, and Molecular Dynamics Calculations,"" Biochemistry 30, 6936-6942 (1991).","Investigation of the Solution Structure of the Human Parathyroid Hormone Fragment (1-34) by 1H NMR Spectroscopy, Distance Geometry, and Molecular Dynamics Calculations",published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,6936,6942,1991, citations,entry_citation,16660,52725,1,,entry citation,,,20937248,,,NMR evidence of GM1-induced conformational change of Substance P using isotropic bicelles.,published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1808,1,,,,,,,,,,,,,,,,,,,,,,127,139,2011, citations,citation_1,16661,52742,1,,entry citation,,,19768685,,,Plasmodium falciparum acyl carrier protein crystal structures in disulfide-linked and reduced states and their prevalence during blood stage growth.,published,journal,Proteins,Proteins,78,3,,,,,,,,,,,,,,,,,,,,,,575,588,2010, citations,citations,16662,52759,1,,entry citation,,,20356842,,,Differences in the Structure and Dynamics of the Apo- and Palmitate-ligated Forms of Aedes aegypti Sterol Carrier Protein 2 (AeSCP-2).,published,journal,J. Biol. Chem.,The Journal of biological chemistry,285,22,,,,,,,,,,,,,,,,,,,,,,17046,17053,2010, citations,citations,16663,52785,1,,entry citation,,,21204007,,,Insulin: a small protein with a long journey.,published,journal,Protein Cell,Protein & cell,1,6,,,,,,,,,,,,,,,,,,,,,,537,551,2010, citations,entry_citation,16664,52801,1,,entry citation,,,20300891,,,"Backbone 1H, 13C, and 15N resonance assignments for lysozyme from bacteriophage lambda.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,1,,,,,,,,,,,,,,,,,,,,,,111,114,2010, citations,AeSCP-2-PA_citations,16665,52817,1,,entry citation,,,20356842,,,Differences in the Structure and Dynamics of the Apo- and Palmitate-ligated Forms of Aedes aegypti Sterol Carrier Protein 2 (AeSCP-2).,published,journal,J. Biol. Chem.,The Journal of biological chemistry,285,22,,,,,,,,,,,,,,,,,,,,,,17046,17053,2010, citations,entry_citation,16666,52845,1,,entry citation,,,21220113,,,Portrayal of complex dynamic properties of sugarcane defensin 5 by NMR: multiple motions associated with membrane interaction,published,journal,Structure,Structure,19,1,,,,,,,,,,,,,,,,,,,,,,26,36,2011, citations,entry_citation,16667,52860,1,,entry citation,,,,,,"Weaponization of a hormone: recruitment of hyperglycemic hormone into the venom of spiders",in preparation,journal,To be Published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,RhoA-GDP,16668,52875,1,,entry citation,,,20018869,,,Real-time NMR study of guanine nucleotide exchange and activation of RhoA by PDZ-RhoGEF.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,285,8,,,,,,,,,,,,,,,,,,,,,,5137,5145,2010, citations,RhoA-GTPgS,16669,52895,1,,entry citation,,,20018869,,,Real-time NMR study of guanine nucleotide exchange and activation of RhoA by PDZ-RhoGEF.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,285,8,,,,,,,,,,,,,,,,,,,,,,5137,5145,2010, citations,entry_citation,16670,52915,1,,entry citation,,,14527388,,,NMR structure of the apoptosis- and inflammation-related NALP1 pyrin domain,published,journal,Structure,,11,10,,,,,,,,,,,,,,,,,,,,,,1190,1205,2003, citations,entry_citation,16671,52929,1,,entry citation,,,20106972,,,Mechanism for the Selective Interaction of C-terminal Eps15 Homology Domain Proteins with Specific Asn-Pro-Phe-containing Partners.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,285,12,,,,,,,,,,,,,,,,,,,,,,8687,8694,2010, citations,entry_citation,16672,52949,1,,entry citation,,,20441771,,,NMR structure of the transmembrane domain of the n-acetylcholine receptor beta2 subunit.,published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1798,8,,,,,,,,,,,,,,,,,,,,,,1608,1614,2010, citations,BS3_assignment,16673,52967,1,,entry citation,,,20556551,,,"1H, 13C and 15N backbone resonance assignments for the BS3 class A -lactamase from Bacillus licheniformis.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,2,,,,,,,,,,,,,,,,,,,,,,195,197,2010, citations,entry_citation,16674,52982,1,,entry citation,,,20886839,,,Redox linked conformational changes in cytochrome c3 from Desulfovibrio desulfuricans ATCC 27774.,published,journal,Biochemistry,Biochemistry,49,44,,,,,,,,,,,,,,,,,,,,,,9620,9629,2010, citations,entry_citation,16675,53006,1,,entry citation,,,20195702,,,The NMR structure of protein-glutaminase from Chryseobacterium proteolyticum.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,46,3,,,,,,,,,,,,,,,,,,,,,,251,255,2010, citations,citation_1,16676,53025,1,,entry citation,,,20630859,,,"Isolation, cDNA cloning, and structure-based functional characterization of oryctin, a hemolymph protein from the coconut rhinoceros beetle, Oryctes rhinoceros, as a novel serine protease inhibitor.",published,journal,J. Biol. Chem.,The Journal of biological chemistry,285,39,,,,,,,,,,,,,,,,,,,,,,30150,30158,2010, citations,entry_citation,16677,53039,1,,entry citation,,,20496919,,,Intermolecular interactions in a 44 kDa interferon-receptor complex detected by asymmetric reverse-protonation and two-dimensional NOESY.,published,journal,Biochemistry,Biochemistry,49,25,,,,,,,,,,,,,,,,,,,,,,5117,5133,2010, citations,entry_citation,16678,53058,1,,entry citation,,,20512150,,,Structure determination of the seven-helix transmembrane receptor sensory rhodopsin II by solution NMR spectroscopy.,published,journal,Nat. Struct. Mol. Biol.,Nature structural & molecular biology,17,6,,,,,,,,,,,,,,,,,,,,,,768,774,2010, citations,entry_citation,16679,53080,1,,entry citation,,,20300890,,,"1H, 13C and 15N assignment of the C-terminal domain of GNA2132 from Neisseria meningitidis.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,1,,,,,,,,,,,,,,,,,,,,,,107,109,2010, citations,citations,16680,53094,1,,entry citation,,,,,,Solution structure of human stem cell transcription factor Nanog,in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,16681,53108,1,,entry citation,,,,,,Solution NMR Structure of the SH3 Domain from the p85beta subunit of Phosphatidylinositol 3-kinase from H.sapiens. Northeast Structural Genomics Consortium Target HR5531E.,in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16682,53136,1,,entry citation,,,20826777,,,The v-myc-induced Q83 lipocalin is a siderocalin.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,285,53,,,,,,,,,,,,,,,,,,,,,,41646,41652,2010, citations,citations,16683,53156,1,,entry citation,,,21253573,,,Structural Basis for the Recognition of Cellular mRNA Export Factor REF by Herpes Viral Proteins HSV-1 ICP27 and HVS ORF57.,published,journal,PLoS Pathog.,PLoS pathogens,7,1,,,,,,,,,,,,,,,,,,,,,,e1001244,,2011, citations,entry_citation,16684,53175,1,,entry citation,,,20118254,,,Structural Homology between the C-Terminal Domain of the PapC Usher and Its Plug.,published,journal,J. Bacteriol.,Journal of bacteriology,192,7,,,,,,,,,,,,,,,,,,,,,,1824,1831,2010, citations,entry_citation,16685,53209,1,,entry citation,,,20623345,,,"1H, 13C and 15N resonance assignments of the major extracytoplasmic domain of the cell shape-determining protein MreC from Bacillus subtilis.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,2,,,,,,,,,,,,,,,,,,,,,,235,238,2010, citations,entry_citation,16686,53227,1,,entry citation,,,,,,Solution NMR structure of mucin-binding domain of protein lmo0835 from Listeria monocytogenes.,in preparation,journal,Proteins: Struct. Funct. Genet.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16687,53255,1,,entry citation,,,20383786,,,"1H, 13C, 15N assignments of the dimeric regulatory subunit (ilvN) of the E. coli AHAS I.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,2,,,,,,,,,,,,,,,,,,,,,,131,133,2010, citations,entry_citation,17748,73818,1,,entry citation,,,21449613,,,Solution NMR Insights into Docking Interactions Involving Inactive ERK2.,published,journal,Biochemistry,,50,18,,,,,,,,,,,,,,,,,,,,,,3660,3672,2011, citations,SH3_family,16688,53273,1,,entry citation,,,,,,Solution NMR structure of the CPE1231(468-535) protein from Clostridium perfringens. Northeast Structural Genomics Consortium Target CpR82B.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16689,53330,1,,entry citation,,,20455034,,,"Backbone and side chain 1H, 15N and 13C assignments for a thiol-disulphide oxidoreductase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,2,,,,,,,,,,,,,,,,,,,,,,151,154,2010, citations,entry_citation,1669,53349,1,,entry citation,,,,,"Tsuge, Hideaki, Koseki, Koushi, Miyano, Masashi, Shimazaki, Kazuko, Chuman, Tatsuji, Matsumoto, Takashi, Noma, Masana, Nitta, Katsutoshi, Sugai, Shintaro, ""A structural study of calcium-binding equine lysozome by two-dimensional 1H-NMR,"" Biochim. Biophys. Acta 1078, 77-84 (1991).",A structural study of calcium-binding equine lysozome by two-dimensional 1H-NMR,published,journal,Biochim. Biophys. Acta,,1078,,,,,,,,,,,,,,,,,,,,,,,77,84,1991, citations,citation_1,16690,53362,1,,entry citation,,,20304107,,,Restricted domain mobility in the Candida albicans Ess1 prolyl isomerase.,published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1804,7,,,,,,,,,,,,,,,,,,,,,,1537,1541,2010, citations,citations,16691,53376,1,,entry citation,,,,,,"Solution NMR Structure of Probable 30S ribosomal protein PSRP-3 (Ycf65-like protein) from Synechocystis sp. (PCC 6803), Northeast Structural Genomics Consortium Target Target SgR46",in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16692,53425,1,,entry citation,,,,,,"Solution NMR structure of a domain of protein A6KY75 from Bacteroides vulgatus, Northeast Structural Genomics target BvR106A.",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16693,53450,1,,entry citation,,,21256986,,,"Solution structure of BTK-2, a novel hK(v)1.1 inhibiting scorpion toxin, from the eastern Indian scorpion Mesobuthus tamulus.",published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1814,4,,,,,,,,,,,,,,,,,,,,,,459,469,2011, citations,entry_citation,16694,53466,1,,entry citation,,,20368734,,,Structural insights into selective histone H3 recognition by the human Polybromo bromodomain 2.,published,journal,Cell Res.,Cell research,20,5,,,,,,,,,,,,,,,,,,,,,,529,538,2010, citations,entry_citation,16695,53497,1,,entry citation,,,20363759,,,Solution conformation and dynamics of the HIV-1 integrase core domain.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,285,23,,,,,,,,,,,,,,,,,,,,,,18072,18084,2010, citations,citations,16696,53516,1,,entry citation,,,21253573,,,Structural Basis for the Recognition of Cellular mRNA Export Factor REF by Herpes Viral Proteins HSV-1 ICP27 and HVS ORF57.,published,journal,PLoS Pathog.,PLoS pathogens,7,1,,,,,,,,,,,,,,,,,,,,,,e1001244,,2011, citations,citations,16697,53530,1,,entry citation,,,21253573,,,Structural Basis for the Recognition of Cellular mRNA Export Factor REF by Herpes Viral Proteins HSV-1 ICP27 and HVS ORF57.,published,journal,PLoS Pathog.,PLoS pathogens,7,1,,,,,,,,,,,,,,,,,,,,,,e1001244,,2011, citations,citations,16698,53544,1,,entry citation,,,21253573,,,Structural Basis for the Recognition of Cellular mRNA Export Factor REF by Herpes Viral Proteins HSV-1 ICP27 and HVS ORF57.,published,journal,PLoS Pathog.,PLoS pathogens,7,1,,,,,,,,,,,,,,,,,,,,,,e1001244,,2011, citations,citation_1,16699,53561,1,,entry citation,,,20348105,,,The Presence of a Single N-terminal Histidine Residue Enhances the Fusogenic Properties of a Membranotropic Peptide Derived from Herpes Simplex Virus Type 1 Glycoprotein H.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,285,22,,,,,,,,,,,,,,,,,,,,,,17123,17136,2010, citations,entry_citation,1670,53577,1,,entry citation,,,,,"Tsuge, Hideaki, Koseki, Koushi, Miyano, Masashi, Shimazaki, Kazuko, Chuman, Tatsuji, Matsumoto, Takashi, Noma, Masana, Nitta, Katsutoshi, Sugai, Shintaro, ""A structural study of calcium-binding equine lysozome by two-dimensional 1H-NMR,"" Biochim. Biophys. Acta 1078, 77-84 (1991).",A structural study of calcium-binding equine lysozome by two-dimensional 1H-NMR,published,journal,Biochim. Biophys. Acta,,1078,,,,,,,,,,,,,,,,,,,,,,,77,84,1991, citations,citation_1,16700,53590,1,,entry citation,,,20348105,,,The Presence of a Single N-terminal Histidine Residue Enhances the Fusogenic Properties of a Membranotropic Peptide Derived from Herpes Simplex Virus Type 1 Glycoprotein H.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,285,22,,,,,,,,,,,,,,,,,,,,,,17123,17136,2010, citations,entry_citation,16701,53607,1,,entry citation,,,20178386,,,Challenging the Limit: NMR Assignment of a 31 kDa Helical Membrane Protein,published,journal,J. Am. Chem. Soc.,,132,11,,,,,,,,,,,,,,,,,,,,,,3662,3663,2010, citations,entry_citation,16703,53622,1,,entry citation,,,,,,High-resolution structure of atypical serine proteinase inhibitors by means of NMR spectroscopy,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16704,53640,1,,entry citation,,,,,,High-resolution structure of atypical serine proteinase inhibitors by means of NMR spectroscopy,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16705,53658,1,,entry citation,,,,,,High-resolution structure of atypical serine proteinase inhibitors by means of NMR spectroscopy,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16706,53676,1,,entry citation,,,20375014,,,Prion fibrillization is mediated by a native structural element that comprises helices H2 and H3.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,285,27,,,,,,,,,,,,,,,,,,,,,,21004,21012,2010, citations,entry_citation,16707,53691,1,,entry citation,,,20578714,,,"Isolation, structure elucidation, and synergistic antibacterial activity of a novel two-component lantibiotic lichenicidin from Bacillus licheniformis VK21.",published,journal,Biochemistry,Biochemistry,49,30,,,,,,,,,,,,,,,,,,,,,,6462,6472,2010, citations,entry_citation,16708,53712,1,,entry citation,,,20443086,,,"1H, 13C and 15N NMR assignments of RNA recognizing motifs 1 and 2 of BRUNOL-3 protein from human involved in myotonic dystrophy.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,2,,,,,,,,,,,,,,,,,,,,,,143,145,2010, citations,entry_citation,16709,53728,1,,entry citation,,,20578714,,,"Isolation, structure elucidation, and synergistic antibacterial activity of a novel two-component lantibiotic lichenicidin from Bacillus licheniformis VK21.",published,journal,Biochemistry,Biochemistry,49,30,,,,,,,,,,,,,,,,,,,,,,6462,6472,2010, citations,entry_citation,16710,53749,1,,entry citation,,,20460129,,,Computational design of a PAK1 binding protein.,published,journal,J. Mol. Biol.,Journal of molecular biology,400,2,,,,,,,,,,,,,,,,,,,,,,257,270,2010, citations,entry_citation,16711,53764,1,,entry citation,,,,,,NMR structure of the protein NP_415897.1,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16712,53783,1,,entry citation,,,20390383,,,"1H, 13C and 15N backbone and side-chain chemical shift assignments for oxidized and reduced desulfothioredoxin.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,2,,,,,,,,,,,,,,,,,,,,,,135,137,2010, citations,entry_citation,16713,53797,1,,entry citation,,,20390383,,,"1H, 13C and 15N backbone and side-chain chemical shift assignments for oxidized and reduced desulfothioredoxin.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,2,,,,,,,,,,,,,,,,,,,,,,135,137,2010, citations,citation_1,16714,53811,1,,entry citation,,,21779925,,,"H, 13C, 15N and P chemical shift assignments of a human Xist RNA A-repeat tetraloop hairpin essential for X-chromosome inactivation.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,6,1,,,,,,,,,,,,,,,,,,,,,,75,77,2012, citations,citation_2,16714,53812,2,,reference citation,,,,,,The Xist RNA A-repeat comprises a novel AUCG tetraloop fold and a platform for multimerization,in preparation,journal,PLoS Biol,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,16715,53842,1,,entry citation,,,21543316,,,NMR Solution Structure of Human Vaccinia-related Kinase 1 (VRK1) Reveals the C-terminal Tail Essential for Its Structural Stability and Autocatalytic Activity.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,286,25,,,,,,,,,,,,,,,,,,,,,,22131,22138,2011, citations,entry_citation,16716,53861,1,,entry citation,,,20654623,,,Residue-Resolved Stability of Full-Consensus Ankyrin Repeat Proteins Probed by NMR.,published,journal,J. Mol. Biol.,Journal of molecular biology,402,1,,,,,,,,,,,,,,,,,,,,,,241,258,2010, citations,entry_citation,16717,53878,1,,entry citation,,,20654623,,,Residue-Resolved Stability of Full-Consensus Ankyrin Repeat Proteins Probed by NMR.,published,journal,J. Mol. Biol.,Journal of molecular biology,402,1,,,,,,,,,,,,,,,,,,,,,,241,258,2010, citations,entry_citation,16718,53895,1,,entry citation,,,20654623,,,Residue-Resolved Stability of Full-Consensus Ankyrin Repeat Proteins Probed by NMR.,published,journal,J. Mol. Biol.,Journal of molecular biology,402,1,,,,,,,,,,,,,,,,,,,,,,241,258,2010, citations,entry_citation,16719,53912,1,,entry citation,,,22150223,,,A molten globule-to-ordered structure transition of Drosophila melanogaster crammer is required for its ability to inhibit cathepsin.,published,journal,Biochem. J.,The Biochemical journal,442,3,,,,,,,,,,,,,,,,,,,,,,563,572,2012, citations,entry_citation,1672,53931,1,,entry citation,,,,,"Feng, Yiqing, Wand, A. 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Biol.,Journal of molecular biology,400,2,,,,,,,,,,,,,,,,,,,,,,121,128,2010, citations,entry_citation,16721,53960,1,,entry citation,,,,,,Solution structure of BRD1 PHD1 finger,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16722,53982,1,,entry citation,,,20460128,,,Horse prion protein NMR structure and comparisons with related variants of the mouse prion protein.,published,journal,J. Mol. Biol.,Journal of molecular biology,400,2,,,,,,,,,,,,,,,,,,,,,,121,128,2010, citations,entry_citation,16723,53998,1,,entry citation,,,20460128,,,Horse prion protein NMR structure and comparisons with related variants of the mouse prion protein.,published,journal,J. Mol. Biol.,Journal of molecular biology,400,2,,,,,,,,,,,,,,,,,,,,,,121,128,2010, citations,entry_citation,16726,54014,1,,entry citation,,,20490953,,,Resonance assignments of myristoylated and non-myristoylated neuronal calcium sensor-1(NCS-1) embedded in a membrane,published,journal,Biomol. NMR Assignments,,4,2,,,,,,,,,,,,,,,,,,,,,,155,158,2010, citations,entry_citation,16727,54028,1,,entry citation,,,,,,The solution structure of the antimicrobial peptid culberticidin,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16729,54045,1,,entry citation,,,20397637,,,NMR characterization of the interaction of the Salmonella type III secretion system protein SipD and bile salts.,published,journal,Biochemistry,Biochemistry,49,19,,,,,,,,,,,,,,,,,,,,,,4220,4226,2010, citations,entry_citation,1673,54060,1,,entry citation,,,,,"Clubb, Robert T., Thanabal, V., Osborne, C., Wagner, Gerhard, ""1H and 15N Resonance Assignments of Oxidized Flavodoxin from Anacystis nidulans with 3D NMR,"" Biochemistry 30 (31), 7718-7730 (1991).","1H and 15N Resonance Assignments of Oxidized Flavodoxin from Anacystis nidulans with 3D NMR",published,journal,Biochemistry,,30,31,,,,,,,,,,,,,,,,,,,,,,7718,7730,1991, citations,citations,16731,54073,1,,entry citation,,,,,,Solution Structure of a putative disulphide-isomerase from Bacteroides thetaiotaomicron,in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16732,54089,1,,entry citation,,,20462494,,,The structure of PknB extracellular PASTA domain from mycobacterium tuberculosis suggests a ligand-dependent kinase activation.,published,journal,"Structure (Cambridge, MA, U. 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Commun.,Biochemical and biophysical research communications,396,3,,,,,,,,,,,,,,,,,,,,,,643,647,2010, citations,entry_citation,16736,54151,1,,entry citation,,,20300805,,,PCS-based structure determination of protein-protein complexes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,46,4,,,,,,,,,,,,,,,,,,,,,,271,280,2010, citations,entry_citation,16737,54171,1,,entry citation,,,21367854,,,"Structural and Biochemical Characterization of NarE, an Iron-containing ADP-ribosyltransferase from Neisseria meningitidis.",published,journal,J. Biol. Chem.,The Journal of biological chemistry,286,17,,,,,,,,,,,,,,,,,,,,,,14842,14851,2011, citations,citations,16738,54196,1,,entry citation,,,21543316,,,NMR Solution Structure of Human Vaccinia-related Kinase 1 (VRK1) Reveals the C-terminal Tail Essential for Its Structural Stability and Autocatalytic Activity.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,286,25,,,,,,,,,,,,,,,,,,,,,,22131,22138,2011, citations,entry_citation,16739,54216,1,,entry citation,,,20508130,,,"Plectasin, a Fungal Defensin, Targets the Bacterial Cell Wall Precursor Lipid II.",published,journal,Science,"Science (New York, N.Y.)",328,5982,,,,,,,,,,,,,,,,,,,,,,1168,1172,2010, citations,entry_citation,1674,54230,1,,entry citation,,,,,"Montelione, G.T., Wuthrich, Kurt, Scheraga, H.A., ""Sequence-specific 1H-NMR Assignments and Identification of Slowly Exchanging Amide Protons in Murine Epidermal Growth Factor,"" Biochemistry 27, 2235-2243 (1988).","Sequence-specific 1H-NMR Assignments and Identification of Slowly Exchanging Amide Protons in Murine Epidermal Growth Factor",published,journal,Biochemistry,,27,,,,,,,,,,,,,,,,,,,,,,,2235,2243,1988, citations,entry_citation,17749,73836,1,,entry citation,,,,,,Solution NMR structure of Diiron protein in presence of 2 eq Zn2+,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16740,54243,1,,entry citation,,,20873742,,,"Amicyanin Transfers Electrons from Methylamine Dehydrogenase to Cytochrome c-551i via a Ping-Pong Mechanism, not a Ternary Complex.",published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,132,41,,,,,,,,,,,,,,,,,,,,,,14537,14545,2010, citations,entry_citation,16741,54260,1,,entry citation,,,20873742,,,"Amicyanin Transfers Electrons from Methylamine Dehydrogenase to Cytochrome c-551i via a Ping-Pong Mechanism, not a Ternary Complex.",published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,132,41,,,,,,,,,,,,,,,,,,,,,,14537,14545,2010, citations,entry_citation,16742,54277,1,,entry citation,,,20600112,,,Structure of the catalytic a(0)a fragment of the protein disulfide isomerase ERp72.,published,journal,J. Mol. Biol.,Journal of molecular biology,401,4,,,,,,,,,,,,,,,,,,,,,,618,625,2010, citations,entry_citation,16743,54291,1,,entry citation,,,20661422,,,NMR structure of the human prion protein with the pathological Q212P mutation reveals unique structural features,published,journal,PLoS One,,5,7,,,,,,,,,,,,,,,,,,,,,,e11715,e11715,2010, citations,entry_citation,16744,54312,1,,entry citation,,,20439749,,,Structure and identification of ADP-ribose recognition motifs of APLF and role in the DNA damage response.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,107,20,,,,,,,,,,,,,,,,,,,,,,9129,9134,2010, citations,entry_citation,16745,54341,1,,entry citation,,,,,,"Common chickweed (Stellaria media) antifungal peptides with chitin-binding domain provide unique plant defense strategy",in preparation,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16746,54359,1,,entry citation,,,,,,Solution Structure of GmR58A,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16747,54384,1,,entry citation,,,,,,Structure of Glycocin A,in preparation,journal,Proteins,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16748,54400,1,,entry citation,,,20814767,,,"Complete 1H, 13C and 15N NMR assignments for donor-strand complemented AafA, the major pilin of aggregative adherence fimbriae (AAF/II) from enteroaggregative E. coli",published,journal,Biomol. NMR Assignments,,5,1,,,,,,,,,,,,,,,,,,,,,,1,5,2011, citations,entry_citation,16749,54414,1,,entry citation,,,21188560,,,"Backbone 1H, 15N, and 13C resonance assignments for the NOXO1 PX domain.",published,journal,Biomol. 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NMR Assignments,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16780,54963,1,,entry citation,,,,,,Biophysical characterisation of CobR,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,16781,54981,1,,entry citation,,,20351100,,,A low affinity ground state conformation for the Dynein microtubule binding domain.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,285,21,,,,,,,,,,,,,,,,,,,,,,15994,16002,2010, citations,entry_citation,16782,54995,1,,entry citation,,,21058299,,,Solution NMR structure of photosystem II reaction center protein Psb28 from Synechocystis sp. Strain PCC 6803.,published,journal,Proteins,Proteins,79,1,,,,,,,,,,,,,,,,,,,,,,340,344,2011, citations,entry_citation,16783,55047,1,,entry citation,,,20407887,,,"1H, 13C, 15N backbone NMR assignments of the Staphylococcus aureus small multidrug-resistance pump (Smr) in a functionally active conformation.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,2,,,,,,,,,,,,,,,,,,,,,,139,142,2010, citations,entry_citation,16784,55063,1,,entry citation,,,20428585,,,Stereochemistry of 4-hydroxyproline affects the conformation of conopeptides.,published,journal,Chem. Commun. (Camb.),"Chemical communications (Cambridge, England)",46,30,,,,,,,,,,,,,,,,,,,,,,5467,5469,2010, citations,entry_citation,16785,55082,1,,entry citation,,,20428585,,,Stereochemistry of 4-hydroxyproline affects the conformation of conopeptides.,published,journal,Chem. Commun. (Camb.),"Chemical communications (Cambridge, England)",46,30,,,,,,,,,,,,,,,,,,,,,,5467,5469,2010, citations,entry_citation,16786,55101,1,,entry citation,,,20428585,,,Stereochemistry of 4-hydroxyproline affects the conformation of conopeptides.,published,journal,Chem. Commun. 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Soc.,Journal of the American Chemical Society,132,23,,,,,,,,,,,,,,,,,,,,,,7908,7918,2010, citations,entry_citation,16788,55137,1,,entry citation,,,20413501,,,A NusE:NusG Complex Links Transcription and Translation,published,journal,Science,,328,5977,,,,,,,,,,,,,,,,,,,,,,501,504,2010, citations,to_be_published,16789,55157,1,,entry citation,,,,,,solution structure of the ubiquitin specific protease Usp7 ubiquitin-like domain,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation_1,16790,55175,1,,entry citation,,,,,,Solution NMR structure of uncharacterized protein CV0863 from Chromobacterium Violaceum,in preparation,journal,To Be Published,To Be Published,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16791,55204,1,,entry citation,,,,,,solution NMR structure of yaiA from Escherichia coli. Northeast Structural Genomics Target ER244,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,16792,55228,1,,entry citation,,,,,,Northeast Structural Genomics Consortium Target HR4547E,in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16794,55253,1,,entry citation,,,,,,"NMR solution structure of Q7A1E8 protein from Staphylococcus aureus, Northeast Structural Genomics Consortium target: ZR215",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,16795,55294,1,,entry citation,,,,,,Northeast Structural Genomics Consortium Target KpR49,in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16796,55319,1,,entry citation,,,20202939,,,Characterization and structure determination of the Cdt1 binding domain of human minichromosome maintenance (Mcm) 6.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,285,17,,,,,,,,,,,,,,,,,,,,,,12469,12473,2010, citations,entry_citation,16797,55345,1,,entry citation,,,20544958,,,Structure and DNA binding characteristics of the three-Cys2His2 domain of mouse testis zinc finger protein.,published,journal,Proteins,Proteins,78,10,,,,,,,,,,,,,,,,,,,,,,2202,2212,2010, citations,entry_citation,16798,55365,1,,entry citation,,,21489988,,,Domain 3 of NS5A Protein from the Hepatitis C Virus Has Intrinsic {alpha}-Helical Propensity and Is a Substrate of Cyclophilin A.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,286,23,,,,,,,,,,,,,,,,,,,,,,20441,20454,2011, citations,entry_citation,16799,55380,1,,entry citation,,,21489988,,,Domain 3 of NS5A Protein from the Hepatitis C Virus Has Intrinsic {alpha}-Helical Propensity and Is a Substrate of Cyclophilin A.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,286,23,,,,,,,,,,,,,,,,,,,,,,20441,20454,2011, citations,entry_citation,16800,55395,1,,entry citation,,,21489988,,,Domain 3 of NS5A Protein from the Hepatitis C Virus Has Intrinsic {alpha}-Helical Propensity and Is a Substrate of Cyclophilin A.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,286,23,,,,,,,,,,,,,,,,,,,,,,20441,20454,2011, citations,entry_citation,16801,55410,1,,entry citation,,,,,,Chemical shift assignments for fragment 160-235 of putative peptidoglycan bound protein lmo0835 from Listeria monocytogenes: target LmR64B of the Northeast Structural Genomics Consortium,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16802,55430,1,,entry citation,,,22789558,,,Biochemical properties and catalytic domain structure of the CcmH protein from Escherichia coli.,published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1824,12,,,,,,,,,,,,,,,,,,,,,,1394,1400,2012, citations,entry_citation,16803,55445,1,,entry citation,,,,,,"1H, 13C and 15N backbone and side chain resonance assignment of the human RANTES-E66S mutant in a dimeric form",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,1,16804,55461,1,,entry citation,,,20496909,,,NMR investigations of the Rieske protein from Thermus thermophilus support a coupled proton and electron transfer mechanism.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,132,23,,,,,,,,,,,,,,,,,,,,,,7908,7918,2010, citations,citations,16805,55477,1,,entry citation,,,,,,"Solution NMR of the specialized acyl carrier protein (RPA2022) from Rhodopseudomonas palustris, Northeast Structural Genomics Consortium Target RpR324",in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,16806,55504,1,,entry citation,,,,,,Solution NMR Structure of the Slr1183 protein from Synechocystis sp. PCC 6803. Northeast Structural Genomics Consortium Target Target SgR145.,in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,16807,55545,1,,entry citation,,,,,,Northeast Structural Genomics Consortium Target DhR1A,in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,16808,55571,1,,entry citation,,,,,,"Solution NMR Structure of Cyclin-dependent kinase 2-associated protein 1 (CDK2-associated protein 1; oral cancer suppressor Deleted in oral cancer 1, DOC-1) from H.sapiens, Northeast Structural Genomics Consortium Target Target HR3057H",in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16809,55604,1,,entry citation,,,,,,Solution Structure of the binary complex between the SH3 and SH2 domain of interleukin-2 tyrosine kinase,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,16810,55625,1,,entry citation,,,,,,"Solution NMR Structure of the N-terminal domain of protein PG_0361 from P.gingivalis, Northeast Structural Genomics Consortium Target Target PgR37A",in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16811,55652,1,,entry citation,,,20489200,,,The Sortase A enzyme that attaches proteins to the cell wall of Bacillus anthracis contains an unusual active site architecture.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,285,30,,,,,,,,,,,,,,,,,,,,,,23433,23443,2010, citations,entry_citation,16812,55678,1,,entry citation,,,19095651,,,Structural analysis of MED-1 reveals unexpected diversity in the mechanism of DNA recognition by GATA-type zinc finger domains.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,284,9,,,,,,,,,,,,,,,,,,,,,,5827,5835,2009, citations,entry_citation,16813,55697,1,,entry citation,,,20064468,,,SH3 domains from a subset of BAR proteins define a Ubl-binding domain and implicate parkin in synaptic ubiquitination.,published,journal,Mol. Cell,Molecular cell,36,6,,,,,,,,,,,,,,,,,,,,,,1034,1047,2009, citations,entry_citation,16814,55721,1,,entry citation,,,20544958,,,Structure and DNA binding characteristics of the three-Cys2His2 domain of mouse testis zinc finger protein.,published,journal,Proteins,Proteins,78,10,,,,,,,,,,,,,,,,,,,,,,2202,2212,2010, citations,entry_citation,16815,55741,1,,entry citation,,,20544958,,,Structure and DNA binding characteristics of the three-Cys2His2 domain of mouse testis zinc finger protein.,published,journal,Proteins,Proteins,78,10,,,,,,,,,,,,,,,,,,,,,,2202,2212,2010, citations,citations,16816,55760,1,,entry citation,,,,,,Northeast Structural Genomics Consortium Target HR4547E,in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,16817,55788,1,,entry citation,,,20510021,,,Analysis of the solution structure of the human antibiotic peptide dermcidin and its interaction with phospholipid vesicles.,published,journal,BMB Rep.,BMB reports,43,5,,,,,,,,,,,,,,,,,,,,,,362,368,2010, citations,citations,16818,55803,1,,entry citation,,,19423704,,,Structural basis for ubiquitin recognition by a novel domain from human phospholipase A2-activating protein,published,journal,J. Biol. Chem.,,284,28,,,,,,,,,,,,,,,,,,,,,,19043,19052,2009, citations,entry_citation,16819,55818,1,,entry citation,,,,,,Solution structure of the culberticidin dimer,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16820,55835,1,,entry citation,,,,,,"SOLUTION STRUCTURE OF RIBOSOMAL PROTEIN S8E FROM Methanothermobacter thermautotrophicus, NORTHEASTSTRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET TR71D",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16821,55861,1,,entry citation,,,,,,"SOLUTION NMR STRUCTURE OF TETRATRICOPEPTIDE REPEAT DOMAIN PROTEIN SRU_0103 FROM SALINIBACTER RUBER, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) TARGET SRR115C",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16822,55887,1,,entry citation,,,19323450,,,The solution structure of Bacillus anthracis dihydrofolate reductase yields insight into the analysis of structure-activity relationships for novel inhibitors.,published,journal,Biochemistry,Biochemistry,48,19,,,,,,,,,,,,,,,,,,,,,,4100,4108,2009, citations,entry_citation,16824,55907,1,,entry citation,,,18650809,,,Structural Mechanism of WASP Activation by the Enterohaemorrhagic E. coli Effector EspFU,published,journal,Nature,,454,7207,,,,,,,,,,,,,,,,,,,,,,1009,1013,2008, citations,entry_citation,16831,55928,1,,entry citation,,,20133735,,,Lsr2 is a nucleoid-associated protein that targets AT-rich sequences and virulence genes in Mycobacterium tuberculosis.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,107,11,,,,,,,,,,,,,,,,,,,,,,5154,5159,2010, citations,entry_citation,16832,55942,1,,entry citation,,,,,,Structure of the C-terminal domain of the mtTyrRS from A. nidulans,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16865,56608,1,,entry citation,,,20613843,,,Mechanism and regulation of acetylated histone binding by the tandem PHD finger of DPF3b,published,journal,Nature,,466,7303,,,,,,,,,,,,,,,,,,,,,,258,262,2010, citations,citations,16833,55957,1,,entry citation,,,,,,"Minimal Constraint Solution NMR Structure of Translationally-controlled tumor protein (TCTP) from C.elegans, Northeast Structural Genomics Consortium Target Target WR73",in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,16834,56001,1,,entry citation,,,19108701,,,"Structural and dynamics study of DNA dodecamer duplexes that contain un-, hemi-, or fully methylated GATC sites.",published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,130,52,,,,,,,,,,,,,,,,,,,,,,17688,17696,2008, citations,entry_citation,16835,56026,1,,entry citation,,,20428927,,,The NMR structure of the autophagy-related protein Atg8.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,47,3,,,,,,,,,,,,,,,,,,,,,,237,241,2010, citations,entry_citation,16837,56045,1,,entry citation,,,22156376,,,Functional binding of hexanucleotides to 3C protease of hepatitis A virus.,published,journal,Nucleic Acids Res.,Nucleic acids research,40,7,,,,,,,,,,,,,,,,,,,,,,3042,3055,2012, citations,entry_citation,16838,56060,1,,entry citation,,,20526825,,,"Backbone 1H, 13C and 15N resonance assignments of the extracellular domain of tissue factor.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,2,,,,,,,,,,,,,,,,,,,,,,183,185,2010, citations,citation_1,16839,56076,1,,entry citation,,,20200157,,,"NMR analysis of the structure, dynamics and unique oligomerization properties of the chemokine CCL27",published,journal,J. Biol. Chem.,The Journal of biological chemistry,285,19,,,,,,,,,,,,,,,,,,,,,,14424,14437,2010, citations,entry_citation_1,16840,56098,1,,entry citation,,,20703836,,,"1H, 15N and 13C resonance assignment of darcin, a mouse major urinary protein.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,2,,,,,,,,,,,,,,,,,,,,,,239,241,2010, citations,entry_citation,16841,56117,1,,entry citation,,,20739283,,,Implications for Collagen Binding from the Crystallographic Structure of Fibronectin 6FnI1-2FnII7FnI.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,285,44,,,,,,,,,,,,,,,,,,,,,,33764,33770,2010, citations,entry_citation,16842,56139,1,,entry citation,,,21069484,,,1H and 15N resonance assignments for fully reduced triheme cytochrome PpcA from Geobacter sulfurreducens,published,journal,Biomol. NMR Assignments,,5,1,,,,,,,,,,,,,,,,,,,,,,113,116,2011, citations,entry_citation,16843,56161,1,,entry citation,,,24805164,,,Probing the Free Energy Landscape of the Fast-Folding gpW Protein by Relaxation Dispersion NMR.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,16845,56181,1,,entry citation,,,20932308,,,Structural and antimicrobial properties of human pre-elafin/trappin-2 and derived peptides against Pseudomonas aeruginosa.,published,journal,BMC Microbiol.,BMC microbiology,10,1,,,,,,,,,,,,,,,,,,,,,,253,253,2010, citations,citation_1,16846,56200,1,,entry citation,,,20199110,,,Mycobacterium tuberculosis Rv0899 adopts a mixed alpha/beta-structure and does not form a transmembrane beta-barrel,published,journal,Biochemistry,,49,13,,,,,,,,,,,,,,,,,,,,,,2768,2777,2010, citations,entry_citation,16847,56224,1,,entry citation,,,,,,Assignments for LC8 bound to a peptide corresponding to residues 233-249 of neuronal Nitric Oxide Synthase,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16848,56239,1,,entry citation,,,19423704,,,Structural basis for ubiquitin recognition by a novel domain from human phospholipase A2-activating protein.,published,journal,J. Biol. Chem.,,284,28,,,,,,,,,,,,,,,,,,,,,,19043,19052,2009, citations,entry_citation,16849,56253,1,,entry citation,,,19997764,,,An NMR structural study of nickel-substituted rubredoxin.,published,journal,J. Biol. Inorg. Chem.,Journal of biological inorganic chemistry,15,3,,,,,,,,,,,,,,,,,,,,,,409,420,2010, citations,Msrb_Trx,16850,56272,1,,entry citation,,,22505815,,,Structural insights into interaction between mammalian methionine sulfoxide reductase B1 and thioredoxin,published,journal,J. Biomed. Biotechnol.,,2012,,,,,,,,,,,,,,,,,,,,,,,586539,586539,2012, citations,KIX_ETAD1,16851,56295,1,,entry citation,,,24682819,,,Functional redundancy between the transcriptional activation domains of E2A is mediated by binding to the KIX domain of CBP/p300.,published,journal,Nucleic Acids Res.,Nucleic acids research,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,nar10,16852,56315,1,,entry citation,,,20624819,,,Solution-state structure of a fully alternately 2'-F/2'-OMe modified 42-nt dimeric siRNA construct.,published,journal,Nucleic Acids Res.,Nucleic acids research,38,20,,,,,,,,,,,,,,,,,,,,,,7298,7307,2010, citations,entry_citation,16853,56343,1,,entry citation,,,18035040,,,Structural characterization of the transmembrane and cytoplasmic domains of human CD4.,published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1768,12,,,,,,,,,,,,,,,,,,,,,,2949,2960,2007, citations,entry_citation,16854,56360,1,,entry citation,,,,,,NMR resonance assignment of an eye lens fragment from huma aloha crystallin,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,16856,56377,1,,entry citation,,,,,,NMR Structure of acyl carrier protein from Borrelia burgdorferi.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16857,56393,1,,entry citation,,,19586525,,,Exon 6 of human JAG1 encodes a conserved structural unit.,published,journal,BMC Struct. Biol.,BMC structural biology,9,,,,,,,,,,,,,,,,,,,,,,,43,43,2009, citations,citation_1,16857,56394,2,,reference citation,,,,,,Exon 6 of human Jagged-1 encodes an autonomously folding unit,published,journal,FEBS Lett.,,574,,,,,,,,,,,,,,,,,,,,,,,156,160,2004, citations,entry_citation,16858,56410,1,,entry citation,,,20613843,,,Mechanism and regulation of acetylated histone binding by the tandem PHD finger of DPF3b,published,journal,Nature,,466,7303,,,,,,,,,,,,,,,,,,,,,,258,262,2010, citations,entry_citation,16859,56440,1,,entry citation,,,20613843,,,Mechanism and regulation of acetylated histone binding by the tandem PHD finger of DPF3b,published,journal,Nature,,466,7303,,,,,,,,,,,,,,,,,,,,,,258,262,2010, citations,entry_citation,16860,56470,1,,entry citation,,,,,,"Solution NMR structure of holo acyl carrier protein from Geobacter metallireducens refined with NH RDCs. Northeast Structural Genomics Consortium Target GmR141.",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16861,56524,1,,entry citation,,,20613843,,,Mechanism and regulation of acetylated histone binding by the tandem PHD finger of DPF3b,published,journal,Nature,,466,7303,,,,,,,,,,,,,,,,,,,,,,258,262,2010, citations,citation_1,16862,56554,1,,entry citation,,,20503119,,,"1H, 15N, and 13C chemical shift assignments of calcium-binding protein 1 with Ca2+ bound at EF1, EF3 and EF4.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,2,,,,,,,,,,,,,,,,,,,,,,159,161,2010, citations,entry_citation,16863,56570,1,,entry citation,,,20524093,,,"1H, 13C and 15N backbone and side chain resonance assignments of the N-terminal domain of the histidine kinase inhibitor KipI from Bacillus subtilis.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,2,,,,,,,,,,,,,,,,,,,,,,167,169,2010, citations,entry_citation,16864,56591,1,,entry citation,,,20526700,,,"Sequence specific 1H, 13C and 15N backbone resonance assignments of UVI31+ from Chlamydomonas reinhardtii.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,2,,,,,,,,,,,,,,,,,,,,,,171,174,2010, citations,entry_citation,16866,56640,1,,entry citation,,,20378544,,,The longin SNARE VAMP7/TI-VAMP adopts a closed conformation.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,285,23,,,,,,,,,,,,,,,,,,,,,,17965,17973,2010, citations,entry_citation,16867,56654,1,,entry citation,,,20378544,,,The longin SNARE VAMP7/TI-VAMP adopts a closed conformation.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,285,23,,,,,,,,,,,,,,,,,,,,,,17965,17973,2010, citations,entry_citation,16868,56668,1,,entry citation,,,,,,Solution structure of the aminoterminal domain of E. coli NusA,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16869,56685,1,,entry citation,,,20582735,,,Backbone assignment of the catalytic core of a Y-family DNA polymerase.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,2,,,,,,,,,,,,,,,,,,,,,,207,209,2010, citations,entry_citation,16870,56702,1,,entry citation,,,20617401,,,"1H, 13C, and 15N resonance assignments of the N-terminal domain of human Tubulin Binding Cofactor C",published,journal,Biomol. NMR Assignments,,4,2,,,,,,,,,,,,,,,,,,,,,,219,221,2010, citations,reference_citation,16870,56703,2,,reference citation,,,,,,"1H, 13C, 15N resonance assignments of the N-terminal domain of human Tubulin Cofactor C",in press,journal,Plos One,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16871,56719,1,,entry citation,,,21387411,,,Solution structure of the second PDZ domain of Zonula Occludens 1.,published,journal,Proteins,Proteins,79,4,,,,,,,,,,,,,,,,,,,,,,1342,1346,2011, citations,entry_citation,16872,56742,1,,entry citation,,,20489205,,,Solution NMR structure of the C-terminal DNA binding domain of Mcm10 reveals a conserved MCM motif.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,285,30,,,,,,,,,,,,,,,,,,,,,,22942,22949,2010, citations,entry_citation,16873,56767,1,,entry citation,,,20563223,,,NMR Determination of Protein pK(a) Values in the Solid State.,published,journal,J. Phys. Chem. Lett.,The journal of physical chemistry letters,1,10,,,,,,,,,,,,,,,,,,,,,,1623,1628,2010, citations,entry_citation,16874,56791,1,,entry citation,,,18590794,,,The solution structure and dynamics of rat Lipocalin-Type Prostaglandin D Synthase,published,journal,Biochimie,,90,11-12,,,,,,,,,,,,,,,,,,,,,,1637,1646,2008, citations,entry_citation,16876,56805,1,,entry citation,,,21336827,,,Full backbone assignment and dynamics of the intrinsically disordered dehydrin ERD14.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,2,,,,,,,,,,,,,,,,,,,,,,189,193,2011, citations,citations,16877,56828,1,,entry citation,,,19584251,,,Simultaneous recognition of HIV-1 TAR RNA bulge and loop sequences by cyclic peptide mimics of Tat protein.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,106,29,,,,,,,,,,,,,,,,,,,,,,11931,11936,2009, citations,entry_citation,16878,56855,1,,entry citation,,,19446523,,,Structure and site-specific recognition of histone H3 by the PHD finger of human autoimmune regulator.,published,journal,Structure,"Structure (London, England : 1993)",17,5,,,,,,,,,,,,,,,,,,,,,,670,679,2009, citations,entry_citation,16879,56875,1,,entry citation,,,20563762,,,"Sequence-specific 1H, 13C, and 15N assignment of the extended PDZ3 domain of the protein tyrosine phosphatase basophil-like PTP-BL.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,2,,,,,,,,,,,,,,,,,,,,,,199,202,2010, citations,UBM_Paper,16880,56892,1,,entry citation,,,20929865,,,Structural Analysis of the Conserved Ubiquitin-binding Motifs (UBMs) of the Translesion Polymerase iota in Complex with Ubiquitin.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,286,2,,,,,,,,,,,,,,,,,,,,,,1364,1373,2011, citations,entry_citation,16881,56918,1,,entry citation,,,,,,Solution NMR Structure of Streptomyces coelicolor polyketide cyclase SCO5315,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16882,56940,1,,entry citation,,,20159559,,,Unconventional ubiquitin recognition by the ubiquitin-binding motif within the Y family DNA polymerases iota and Rev1.,published,journal,Mol. Cell,Molecular cell,37,3,,,,,,,,,,,,,,,,,,,,,,408,417,2010, citations,entry_citation,16883,56955,1,,entry citation,,,20526701,,,"1H, 13C and 15N resonance assignments of human H-REV107 N-terminal domain.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,2,,,,,,,,,,,,,,,,,,,,,,175,178,2010, citations,entry_citation,16884,56973,1,,entry citation,,,20443086,,,"1H, 13C and 15N NMR assignments of RNA recognizing motifs 1 and 2 of BRUNOL-3 protein from human involved in myotonic dystrophy",published,journal,Biomol. NMR Assignments,,4,2,,,,,,,,,,,,,,,,,,,,,,143,145,2010, citations,UBM_Paper,16885,56989,1,,entry citation,,,20929865,,,Structural Analysis of the Conserved Ubiquitin-binding Motifs (UBMs) of the Translesion Polymerase iota in Complex with Ubiquitin.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,286,2,,,,,,,,,,,,,,,,,,,,,,1364,1373,2011, citations,entry_citation,16886,57015,1,,entry citation,,,21187906,,,Structural and functional studies of nonstructural protein 2 of the hepatitis C virus reveal its key role as organizer of virion assembly.,published,journal,PLoS Pathog.,PLoS pathogens,6,12,,,,,,,,,,,,,,,,,,,,,,,,2010, citations,citation_1,16887,57031,1,,entry citation,,,18657545,,,"Structure of the myristylated human immunodeficiency virus type 2 matrix protein and the role of phosphatidylinositol-(4,5)-bisphosphate in membrane targeting.",published,journal,J. Mol. Biol.,Journal of molecular biology,382,2,,,,,,,,,,,,,,,,,,,,,,434,447,2008, citations,citation_1,16888,57048,1,,entry citation,,,18657545,,,"Structure of the myristylated human immunodeficiency virus type 2 matrix protein and the role of phosphatidylinositol-(4,5)-bisphosphate in membrane targeting.",published,journal,J. Mol. Biol.,Journal of molecular biology,382,2,,,,,,,,,,,,,,,,,,,,,,434,447,2008, citations,citation_1,16889,57066,1,,entry citation,,,18657545,,,"Structure of the myristylated human immunodeficiency virus type 2 matrix protein and the role of phosphatidylinositol-(4,5)-bisphosphate in membrane targeting.",published,journal,J. Mol. Biol.,Journal of molecular biology,382,2,,,,,,,,,,,,,,,,,,,,,,434,447,2008, citations,entry_citation,16890,57086,1,,entry citation,,,20599533,,,The NMR solution structure of subunit G (G(61)(-)(101)) of the eukaryotic V1VO ATPase from Saccharomyces cerevisiae.,published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1798,10,,,,,,,,,,,,,,,,,,,,,,1961,1968,2010, citations,citation_1,16891,57104,1,,entry citation,,,,,,Assigned chemical shifts for the free alpha chain of haemoglobin,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,16892,57120,1,,entry citation,,,21187906,,,Structural and functional studies of nonstructural protein 2 of the hepatitis C virus reveal its key role as organizer of virion assembly.,published,journal,PLoS Pathog.,PLoS pathogens,6,12,,,,,,,,,,,,,,,,,,,,,,,,2010, citations,entry_citation,16893,57136,1,,entry citation,,,20515689,,,MDM4 binds ligands via a mechanism in which disordered regions become structured.,published,journal,FEBS Lett.,FEBS letters,584,14,,,,,,,,,,,,,,,,,,,,,,3035,3041,2010, citations,entry_citation,16894,57151,1,,entry citation,,,20515689,,,MDM4 binds ligands via a mechanism in which disordered regions become structured.,published,journal,FEBS Lett.,FEBS letters,584,14,,,,,,,,,,,,,,,,,,,,,,3035,3041,2010, citations,citations,16895,57168,1,,entry citation,,,,,,Null,in preparation,journal,To be Published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,16897,57192,1,,entry citation,,,21387412,,,"Solution structure of MTH1821, a putative structure homologue to RNA polymerase subunit from Methanobacterium thermoautotrophicum.",published,journal,Proteins,Proteins,79,4,,,,,,,,,,,,,,,,,,,,,,1347,1351,2011, citations,entry_citation,16898,57215,1,,entry citation,,,23696640,,,-Hemoglobin-stabilizing protein (AHSP) perturbs the proximal heme pocket of oxy--hemoglobin and weakens the iron-oxygen bond.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,27,,,,,,,,,,,,,,,,,,,,,,19986,20001,2013, citations,citations,16899,57230,1,,entry citation,,,,,,"The solution structure of the mutant of UBL domain of UBLCP1, I5M.",in preparation,journal,To be Published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,169,57253,1,,entry citation,,,,,"King, Garry C., Wright, Peter E., ""Proton NMR Studies of Plastocyanin: Assignment of Aromatic and Methyl Group Resonances from Two-Dimensional Spectra,"" Biochemistry 25, 2364-2374 (1986).","Proton NMR Studies of Plastocyanin: Assignment of Aromatic and Methyl Group Resonances from Two-Dimensional Spectra",published,journal,Biochemistry,,25,,,,,,,,,,,,,,,,,,,,,,,2364,2374,1986, citations,entry_citation,16900,57266,1,,entry citation,,,20515689,,,MDM4 binds ligands via a mechanism in which disordered regions become structured.,published,journal,FEBS Lett.,FEBS letters,584,14,,,,,,,,,,,,,,,,,,,,,,3035,3041,2010, citations,entry_citation,16901,57283,1,,entry citation,,,19053253,,,Solution Structure of a Conformationally Restricted Fully Active Derivative of the Human Relaxin-like Factor (dagger) (double dagger).,published,journal,Biochemistry,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,2008, citations,entry_citation,16902,57316,1,,entry citation,,,20556550,,,"Backbone 1H, 15N, 13C and Ile, Leu, Val methyl chemical shift assignments for the 33.5 kDa N-terminal domain of Candida albicans ALS1.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,2,,,,,,,,,,,,,,,,,,,,,,187,190,2010, citations,entry_citation,16904,57333,1,,entry citation,,,20872101,,,Backbone assignment and dynamics of human -synuclein in viscous 2M glucose solution.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,1,,,,,,,,,,,,,,,,,,,,,,43,46,2011, citations,Sma0114_peaklist,16905,57352,1,,entry citation,,,20936511,,,NMR assignments for the Sinorhizobium meliloti response regulator Sma0114.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,1,,,,,,,,,,,,,,,,,,,,,,55,58,2011, citations,entry_citation,16907,57368,1,,entry citation,,,20534508,,,The complete influenza hemagglutinin fusion domain adopts a tight helical hairpin arrangement at the lipid:water interface.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,107,25,,,,,,,,,,,,,,,,,,,,,,11341,11346,2010, citations,citations,16908,57404,1,,entry citation,,,,,,Null,in preparation,journal,To be Published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,16909,57427,1,,entry citation,,,,,,Recognition of tandem PxxP motifs as a unique Src homology 3-binding mode triggers pathogen-driven actin assembly,published,journal,Proc. Natl. Acad. Sci. U. S. A.,,107,50,,,,,,,,,,,,,,,,,,,,,,21743,21748,2010, citations,entry_citation,16910,57446,1,,entry citation,,,20471983,,,Structure of the cytosolic portion of motor protein prestin and functional role of the STAS domain in SLC26/SulP anion transporters.,published,journal,J. Mol. Biol.,Journal of molecular biology,400,3,,,,,,,,,,,,,,,,,,,,,,448,462,2010, citations,entry_citation,16911,57466,1,,entry citation,,,22249178,,,Structural Analysis of the Plasmodium falciparum Erythrocyte Membrane Protein 1 (PfEMP1) Intracellular Domain Reveals a Conserved Interaction Epitope.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,10,,,,,,,,,,,,,,,,,,,,,,7182,7189,2012, citations,entry_citation,16912,57487,1,,entry citation,,,20890634,,,Strategy for complete NMR assignment of disordered proteins with highly repetitive sequences based on resolution-enhanced 5D experiments.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,48,3,,,,,,,,,,,,,,,,,,,,,,169,177,2010, citations,entry_citation,16913,57504,1,,entry citation,,,20538608,,,Solution structure of the squash aspartic acid proteinase inhibitor (SQAPI) and mutational analysis of pepsin inhibition.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,285,35,,,,,,,,,,,,,,,,,,,,,,27019,27025,2010, citations,entry_citation,16914,57519,1,,entry citation,,,,,,Solution strcture of UBX domain of human UBXD2 protein,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16915,57533,1,,entry citation,,,21704065,,,Novel recombinant insulin analogue with flexible C-terminus in B chain. NMR structure of biosynthetic engineered A22G-B31K-B32R human insulin monomer in water/acetonitrile solution.,published,journal,Int. J. Biol. Macromol.,International journal of biological macromolecules,49,4,,,,,,,,,,,,,,,,,,,,,,548,554,2011, citations,entry_citation,16916,57552,1,,entry citation,,,20737255,,,"Backbone (1)H, (13)C, (15)N NMR assignments of the unliganded and substrate ternary complex forms of mevalonate diphosphate decarboxylase from Streptococcus pneumoniae.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,1,,,,,,,,,,,,,,,,,,,,,,11,14,2011, citations,entry_citation,16917,57573,1,,entry citation,,,21569135,,,Structure and binding specificity of the receiver domain of sensor histidine kinase CKI1 from Arabidopsis thaliana.,published,journal,Plant J.,The Plant journal : for cell and molecular biology,67,5,,,,,,,,,,,,,,,,,,,,,,827,839,2011, citations,entry_citation,16918,57596,1,,entry citation,,,21569135,,,Structure and binding specificity of the receiver domain of sensor histidine kinase CKI1 from Arabidopsis thaliana.,published,journal,Plant J.,The Plant journal : for cell and molecular biology,67,5,,,,,,,,,,,,,,,,,,,,,,827,839,2011, citations,entry_citation,16919,57621,1,,entry citation,,,20737255,,,"Backbone (1)H, (13)C, (15)N NMR assignments of the unliganded and substrate ternary complex forms of mevalonate diphosphate decarboxylase from Streptococcus pneumoniae.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,1,,,,,,,,,,,,,,,,,,,,,,11,14,2011, citations,entry_citation,1692,57636,1,,entry citation,,,,,"Bruch, Martha D., Gierasch, Lila M., ""Comparison of Helix Stability in Wild-type and Mutant LamB Signal Sequences,"" J. Biol. Chem. 265 (7), 3851-3858 (1990).",Comparison of Helix Stability in Wild-type and Mutant LamB Signal Sequences,published,journal,J. Biol. Chem.,,265,7,,,,,,,,,,,,,,,,,,,,,,3851,3858,1990, citations,entry_citation,16920,57649,1,,entry citation,,,21399644,,,Molecular basis of purine-rich RNA recognition by the human SR-like protein Tra2-1.,published,journal,Nat. Struct. Mol. Biol.,Nature structural & molecular biology,18,4,,,,,,,,,,,,,,,,,,,,,,443,450,2011, citations,entry_citation,16921,57669,1,,entry citation,,,20623208,,,"1H, 13C, 15N chemical shift assignments for the Neisseria gonorrhoeae MinE regulator of cell division septum placement.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,2,,,,,,,,,,,,,,,,,,,,,,227,229,2010, citations,entry_citation,16922,57688,1,,entry citation,,,20498088,,,Membrane domain structures of three classes of histidine kinase receptors by cell-free expression and rapid NMR analysis.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,107,24,,,,,,,,,,,,,,,,,,,,,,10902,10907,2010, citations,entry_citation,16923,57704,1,,entry citation,,,20937913,,,Coupling of tandem Smad ubiquitination regulatory factor (Smurf) WW domains modulates target specificity.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,107,43,,,,,,,,,,,,,,,,,,,,,,18404,18409,2010, citations,citation_1,16925,57720,1,,entry citation,,,21073880,,,Multi-Timescale Dynamics Study of FKBP12 Along the Rapamycin-mTOR Binding Coordinate.,published,journal,J. Mol. Biol.,Journal of molecular biology,405,2,,,,,,,,,,,,,,,,,,,,,,378,394,2011, citations,entry_citation,16926,57744,1,,entry citation,,,21207987,,,"Structural Characterization of Escherichia coli BamE, a Lipoprotein Component of the -Barrel Assembly Machinery Complex.",published,journal,Biochemistry,Biochemistry,50,6,,,,,,,,,,,,,,,,,,,,,,1081,1090,2011, citations,entry_citation,16927,57761,1,,entry citation,,,,,,"Chemical shift assignment for SuR18C from Streptococcus thermophilus, Northeast Structural Genomics Consortium Target SuR18C",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16928,57778,1,,entry citation,,,20607461,,,"1H, 13C and 15N chemical shift assignments for the N-terminal domain of the voltage-gated potassium channel-hERG.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,4,2,,,,,,,,,,,,,,,,,,,,,,211,213,2010, citations,entry_citation,16929,57796,1,,entry citation,,,21112337,,,NMR Structure and Calcium-Binding Properties of the Tellurite Resistance Protein TerD from Klebsiella pneumoniae.,published,journal,J. Mol. Biol.,Journal of molecular biology,405,5,,,,,,,,,,,,,,,,,,,,,,1188,1201,2011, citations,entry_citation,1693,57816,1,,entry citation,,,,,"Bruch, Martha D., Gierasch, Lila M., ""Comparison of Helix Stability in Wild-type and Mutant LamB Signal Sequences,"" J. Biol. Chem. 265 (7), 3851-3858 (1990).",Comparison of Helix Stability in Wild-type and Mutant LamB Signal Sequences,published,journal,J. Biol. Chem.,,265,7,,,,,,,,,,,,,,,,,,,,,,3851,3858,1990, citations,entry_citation,16930,57829,1,,entry citation,,,20947017,,,The structure of the talin/integrin complex at a lipid bilayer: an NMR and MD simulation study.,published,journal,Structure,"Structure (London, England : 1993)",18,10,,,,,,,,,,,,,,,,,,,,,,1280,1288,2010, citations,citation_1,16931,57844,1,,entry citation,,,21073880,,,Multi-Timescale Dynamics Study of FKBP12 Along the Rapamycin-mTOR Binding Coordinate.,published,journal,J. Mol. Biol.,Journal of molecular biology,405,2,,,,,,,,,,,,,,,,,,,,,,378,394,2011, citations,entry_citation,16932,57876,1,,entry citation,,,20947017,,,The structure of the talin/integrin complex at a lipid bilayer: an NMR and MD simulation study.,published,journal,Structure,"Structure (London, England : 1993)",18,10,,,,,,,,,,,,,,,,,,,,,,1280,1288,2010, citations,citation_1,16933,57891,1,,entry citation,,,21073880,,,Multi-Timescale Dynamics Study of FKBP12 Along the Rapamycin-mTOR Binding Coordinate.,published,journal,J. Mol. Biol.,Journal of molecular biology,405,2,,,,,,,,,,,,,,,,,,,,,,378,394,2011, citations,entry_citation,16934,57915,1,,entry citation,,,,,,Solution NMR structure of the PBS linker domain of phycobilisome linker polypeptide from Anabaena sp. Northeast Structural Genomics Consortium Target NsR123E,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,16935,57950,1,,entry citation,,,21464369,,,"Residues within a lipid-associated segment of the PECAM-1 cytoplasmic domain are susceptible to inducible, sequential phosphorylation.",published,journal,Blood,Blood,117,22,,,,,,,,,,,,,,,,,,,,,,6012,6023,2011, citations,entry_citation,16936,57969,1,,entry citation,,,21531701,,,Solution structure and dynamic analysis of chicken MBD2 methyl binding domain bound to a target-methylated DNA sequence.,published,journal,Nucleic Acids Res.,Nucleic acids research,39,15,,,,,,,,,,,,,,,,,,,,,,6741,6752,2011, citations,entry_citation,16937,57997,1,,entry citation,,,20799727,,,NMR characterization of copper-binding domains 4-6 of ATP7B .,published,journal,Biochemistry,Biochemistry,49,39,,,,,,,,,,,,,,,,,,,,,,8468,8477,2010, citations,citation_1,16939,58012,1,,entry citation,,,21718702,,,Structured Regions of alpha-Synuclein Fibrils Include the Early-Onset Parkinson's Disease Mutation Sites.,published,journal,J. Mol. Biol.,Journal of molecular biology,411,4,,,,,,,,,,,,,,,,,,,,,,881,895,2011, citations,entry_citation,16940,58032,1,,entry citation,,,20660315,,,NMR resonance assignments of thrombin reveal the conformational and dynamic effects of ligation.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,107,32,,,,,,,,,,,,,,,,,,,,,,14087,14092,2010, citations,entry_citation,16941,58054,1,,entry citation,,,20724442,,,Essential structural requirements for specific recognition of HIV TAR RNA by peptide mimetics of Tat protein.,published,journal,Nucleic Acids Res.,Nucleic acids research,39,1,,,,,,,,,,,,,,,,,,,,,,248,256,2011, citations,citations,16942,58078,1,,entry citation,,,,,,"Solution NMR Structure of ydhK C-terminal Domain from B.subtilis, Northeast Structural Genomics Consortium Target Target SR518",in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,publication,16943,58117,1,,entry citation,,,20715266,,,"Solution structure of the leader sequence of the patellamide precursor peptide, PatE1-34.",published,journal,Chembiochem,Chembiochem : a European journal of chemical biology,11,13,,,,,,,,,,,,,,,,,,,,,,1867,1873,2010, citations,entry_citation,16944,58135,1,,entry citation,,,,,,Solution Structure of CpR82G,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,16945,58160,1,,entry citation,,,21287610,,,Solution structures of chicken parvalbumin 3 in the Ca(2+)-free and Ca(2+)-bound states.,published,journal,Proteins,Proteins,79,3,,,,,,,,,,,,,,,,,,,,,,752,764,2011, citations,entry_citation,16946,58174,1,,entry citation,,,20711762,,,Resonance assignment and secondary structure prediction of the N-terminal domain of hERG (Kv11.1).,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,1,,,,,,,,,,,,,,,,,,,,,,15,17,2011, citations,entry_citation,16947,58192,1,,entry citation,,,20498088,,,Membrane domain structures of three classes of histidine kinase receptors by cell-free expression and rapid NMR analysis.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,107,24,,,,,,,,,,,,,,,,,,,,,,10902,10907,2010, citations,entry_citation,16948,58212,1,,entry citation,,,20936383,,,Resonance assignments of GTPase effector domain of dynamin in the aprotic solvent deuterated dimethyl sulfoxide.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,1,,,,,,,,,,,,,,,,,,,,,,59,61,2011, citations,entry_citation,16949,58226,1,,entry citation,,,,,,Protein Backbone Resonance Assignment Assisted with Predicted Local Structures,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16950,58242,1,,entry citation,,,20481618,,,"RNA internal loops with tandem AG pairs: the structure of the 5'GAGU/3'UGAG loop can be dramatically different from others, including 5'AAGU/3'UGAA.",published,journal,Biochemistry,Biochemistry,49,27,,,,,,,,,,,,,,,,,,,,,,5817,5827,2010, citations,entry_citation,16951,58263,1,,entry citation,,,20481618,,,"RNA internal loops with tandem AG pairs: the structure of the 5'GAGU/3'UGAG loop can be dramatically different from others, including 5'AAGU/3'UGAA.",published,journal,Biochemistry,Biochemistry,49,27,,,,,,,,,,,,,,,,,,,,,,5817,5827,2010, citations,entry_citation,16952,58283,1,,entry citation,,,20481618,,,"RNA internal loops with tandem AG pairs: the structure of the 5'GAGU/3'UGAG loop can be dramatically different from others, including 5'AAGU/3'UGAA.",published,journal,Biochemistry,Biochemistry,49,27,,,,,,,,,,,,,,,,,,,,,,5817,5827,2010, citations,entry_citation,16953,58303,1,,entry citation,,,20481618,,,"RNA internal loops with tandem AG pairs: the structure of the 5'GAGU/3'UGAG loop can be dramatically different from others, including 5'AAGU/3'UGAA.",published,journal,Biochemistry,Biochemistry,49,27,,,,,,,,,,,,,,,,,,,,,,5817,5827,2010, citations,Nervy_entry_citation1,16954,58322,1,,entry citation,,,20708017,,,Structure of the AML1-ETO NHR3-PKA(RII) Complex and Its Contribution to AML1-ETO Activity.,published,journal,J. Mol. Biol.,Journal of molecular biology,402,3,,,,,,,,,,,,,,,,,,,,,,560,577,2010, citations,citations,16955,58344,1,,entry citation,,,21287610,,,Solution structures of chicken parvalbumin 3 in the Ca(2+)-free and Ca(2+)-bound states.,published,journal,Proteins,Proteins,79,3,,,,,,,,,,,,,,,,,,,,,,752,764,2011, citations,entry_citation,16956,58360,1,,entry citation,,,20711760,,,"NMR assignments of (1)H, (13)C and (15)N resonances of the C-terminal subunit from Azotobacter vinelandii mannuronan C5-epimerase 6 (AlgE6R3).",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,1,,,,,,,,,,,,,,,,,,,,,,27,29,2011, citations,entry_citation,16957,58381,1,,entry citation,,,20851706,,,Solution structure and phospholipid interactions of the isolated voltage-sensor domain from KvAP.,published,journal,J. Mol. Biol.,Journal of molecular biology,403,4,,,,,,,,,,,,,,,,,,,,,,591,606,2010, citations,Citation_1,16958,58410,1,,entry citation,,,20711761,,,"(1)H, (13)C, and (15)N chemical shift assignments of ZCCHC9.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,1,,,,,,,,,,,,,,,,,,,,,,19,21,2011, citations,entry_citation,16959,58426,1,,entry citation,,,20947018,,,The Structure of the talin head reveals a novel extended conformation of the FERM domain.,published,journal,Structure,,18,10,,,,,,,,,,,,,,,,,,,,,,1288,1299,2010, citations,entry_citation,1696,58442,1,,entry citation,,,,,"Baldisseri, Donna M., Pelton, J.G., Sparks, Steven W., Torchia, Dennis A., ""Complete 1H and 13C assignment of Lys and Leu sidechains of staphylococcal nuclease using HCCH-COSY and HCCH-TOCSY 3D NMR spectroscopy,"" FEBS Lett. 281 (1-2), 33-38 (1991).","Complete 1H and 13C assignment of Lys and Leu sidechains of staphylococcal nuclease using HCCH-COSY and HCCH-TOCSY 3D NMR spectroscopy",published,journal,FEBS Lett.,,281,1-2,,,,,,,,,,,,,,,,,,,,,,33,38,1991, citations,entry_citation_1,16960,58455,1,,entry citation,,,20509680,,,"Solution structure of GxTX-1E, a high-affinity tarantula toxin interacting with voltage sensors in Kv2.1 potassium channels .",published,journal,Biochemistry,Biochemistry,49,25,,,,,,,,,,,,,,,,,,,,,,5134,5142,2010, citations,YabP_family,16961,58472,1,,entry citation,,,21904870,,,Solution NMR structure of Dsy0195 homodimer from Desulfitobacterium hafniense: first structure representative of the YabP domain family of proteins involved in spore coat assembly,published,journal,J. Struct. Funct. Genomics,,12,3,,,,,,,,,,,,,,,,,,,,,,175,179,2011, citations,entry_citation,16962,58503,1,,entry citation,,,21117079,,,One-bond and two-bond j couplings help annotate protein secondary-structure motifs: J-coupling indexing applied to human endoplasmic reticulum protein ERp18.,published,journal,Proteins,"Proteins: Structure, Function, and Bioinformatics",79,2,,,,,,,,,,,,,,,,,,,,,,428,443,2011, citations,Ottiger_et_al_1998,16962,58504,2,,reference citation,,,9571116,,,Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra,published,journal,J. Magn. Reson.,,131,,,,,,,,,,,,,,,,,,,,,,,373,378,1998, citations,Permi_et_al_1999,16962,58505,3,,reference citation,,,10479547,,,Measurement of 1JNCO and 2JHNCO couplings from spin-state-selective two-dimensional correlation spectrum,published,journal,J. Magn. Reson.,,140,,,,,,,,,,,,,,,,,,,,,,,32,40,1999, citations,Yang_et_al_1999,16962,58506,4,,reference citation,,,,,,"TROSY-based HNCO pulse sequence for the measurement of 1HN-15N, 15N-13CO, 1HN-13CO, 13CO-13Ca and 1HN-13Ca dipolar couplings in 15N, 13C, 2H-labeled proteins",published,journal,J. Biomol. NMR,,14,,,,,,,,,,,,,,,,,,,,,,,333,343,1999, citations,Cornilescu_et_al_2000,16962,58507,5,,reference citation,,,,,,Large variations in one-bond 13Ca-13Cb J couplings in polypeptides correlate with backbone conformation,published,journal,J. Am. Chem. Soc.,,122,,,,,,,,,,,,,,,,,,,,,,,2168,2171,2000, citations,Permi_&_Annila_2000,16962,58508,6,,reference citation,,,10805128,,,Transverse relaxation optimised spin-state selective NMR experiments for measurement of residual dipolar couplings,published,journal,J. Biomol. NMR,,16,,,,,,,,,,,,,,,,,,,,,,,221,227,2000, citations,Hu_et_al_2003,16962,58509,7,,reference citation,,,,,,A high sensitivity 3D experiment for measuring Calpha-Halpha residual dipolar coupling constants,published,journal,J. Magn. Reson.,,165,,,,,,,,,,,,,,,,,,,,,,,248,252,2003, citations,Ball_et_al_2006,16962,58510,8,,reference citation,,,16495100,,,Measurement of one-bond 13Ca-1Ha residual dipolar coupling constants in proteins by selective manipulation of CaHa spins,published,journal,J. Magn. Reson.,,180,,,,,,,,,,,,,,,,,,,,,,,127,136,2006, citations,Nolis_et_al_2006,16962,58511,9,,reference citation,,,16448830,,,Optimum spin-state selection for all multiplicities in the acquisition dimension of the HSQC experiment,in preparation,journal,J. Magn. Reson.,,180,,,,,,,,,,,,,,,,,,,,,,,39,50,2006, citations,entry_citation,16963,58550,1,,entry citation,,,21670253,,,Unique scorpion toxin with a putative ancestral fold provides insight into evolution of the inhibitor cystine knot motif,in preparation,journal,Proc. Natl. Acad. Sci. U. S. A.,,108,26,,,,,,,,,,,,,,,,,,,,,,10478,10483,2011, citations,entry_citation,16964,58566,1,,entry citation,,,20572250,,,Protocols for the sequential solid-state NMR spectroscopic assignment of a uniformly labeled 25 kDa protein: HET-s(1-227).,published,journal,Chembiochem,Chembiochem : a European journal of chemical biology,11,11,,,,,,,,,,,,,,,,,,,,,,1543,1551,2010, citations,entry_citation,16965,58581,1,,entry citation,,,20572250,,,Protocols for the sequential solid-state NMR spectroscopic assignment of a uniformly labeled 25 kDa protein: HET-s(1-227).,published,journal,Chembiochem,Chembiochem : a European journal of chemical biology,11,11,,,,,,,,,,,,,,,,,,,,,,1543,1551,2010, citations,entry_citation,16966,58595,1,,entry citation,,,20659683,,,Insights into protein-protein and enzyme-substrate interactions in modular polyketide synthases.,published,journal,Chem. Biol.,Chemistry and Biology,17,7,,,,,,,,,,,,,,,,,,,,,,705,716,2010, citations,entry_citation,16967,58610,1,,entry citation,,,22894835,,,Interference with the PTEN-MAST2 Interaction by a Viral Protein Leads to Cellular Relocalization of PTEN.,published,journal,Sci. Signal.,Science signaling,5,237,,,,,,,,,,,,,,,,,,,,,,ra58,ra58,2012, citations,entry_citation,16968,58632,1,,entry citation,,,19086273,,,The Solution Structure of a Conformationally Restricted Fully Active Derivative of the Human Relaxin-like Factor (RLF),published,journal,Biochemistry,,47,50,,,,,,,,,,,,,,,,,,,,,,13308,13317,2008, citations,entry_citation_1,16969,58655,1,,entry citation,,,20610388,,,"Structural basis for homodimerization of the Src-associated during mitosis, 68-kDa protein (Sam68) Qua1 domain.",published,journal,J. Biol. Chem.,The Journal of biological chemistry,285,37,,,,,,,,,,,,,,,,,,,,,,28893,28901,2010, citations,entry_citation,1697,58677,1,,entry citation,,,,,"Xu, Guang-Yi, Deber, Charles M., ""Conformations of neurotensin in solution and in membrane environments studied by 2D-NMR spectroscopy,"" Int. J. Pept. Protein Res. 37, 528-535 (1991).","Conformations of neurotensin in solution and in membrane environments studied by 2D-NMR spectroscopy",published,journal,Int. J. Pept. Protein Res.,,37,,,,,,,,,,,,,,,,,,,,,,,528,535,1991, citations,entry_citation,16970,58691,1,,entry citation,,,21489982,,,A Conserved residue in the yeast Bem1p SH3 domain maintains the high level of binding specificity required for function.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,286,22,,,,,,,,,,,,,,,,,,,,,,19470,19477,2011, citations,entry_citation,16971,58712,1,,entry citation,,,20936510,,,Chemical shift assignments for F-plasmid TraI (381-569).,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,1,,,,,,,,,,,,,,,,,,,,,,67,70,2011, citations,entry_citation,16977,58727,1,,entry citation,,,20703834,,,Resonance assignment of nsp7 from arterivirus.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,1,,,,,,,,,,,,,,,,,,,,,,23,25,2011, citations,entry_citation,16978,58748,1,,entry citation,,,21765060,,,Structural role of the terminal disulfide bond in the sweetness of brazzein.,published,journal,Chem. Senses,Chemical senses,36,9,,,,,,,,,,,,,,,,,,,,,,821,830,2011, citations,reference_citation,16978,58749,2,,reference citation,,,,,,Insights into the sweetness of brazzein from beta-hairpin peptides derived from the N- and C- termini of brazzein,published,thesis,,,,,,,,,,,,,,,,,,,,,,University of Wisconsin-Madison,"Madison, WI",USA,,,,, citations,entry_citation,16979,58776,1,,entry citation,,,,,,Solution structure of Enzyme IIB subunit of PTS system from Escherichia coli K12. Northeast Structural Genomics Consortium target ER315/Ontario Center for Structural Proteomics target ec0544,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1698,58802,1,,entry citation,,,,,"Xu, Guang-Yi, Deber, Charles M., ""Conformations of neurotensin in solution and in membrane environments studied by 2D-NMR spectroscopy,"" Int. J. Pept. Protein Res. 37, 528-535 (1991).","Conformations of neurotensin in solution and in membrane environments studied by 2D-NMR spectroscopy",published,journal,Int. J. Pept. Protein Res.,,37,,,,,,,,,,,,,,,,,,,,,,,528,535,1991, citations,entry_citation,16980,58816,1,,entry citation,,,20549304,,,Major groove width variations in RNA structures determined by NMR and impact of 13C residual chemical shift anisotropy and 1H-13C residual dipolar coupling on refinement.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,47,3,,,,,,,,,,,,,,,,,,,,,,205,219,2010, citations,citations,16981,58832,1,,entry citation,,,20709084,,,NMR Structure of the SARS-CoV Nonstructural Protein 7 in Solution at pH6.5.,published,journal,J. Mol. Biol.,Journal of molecular biology,402,4,,,,,,,,,,,,,,,,,,,,,,619,628,2010, citations,entry_citation,16982,58853,1,,entry citation,,,20711759,,,Backbone chemical shifts assignments of D: -allose binding protein in the free form and in complex with D: -allose.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,1,,,,,,,,,,,,,,,,,,,,,,31,34,2011, citations,entry_citation,16983,58867,1,,entry citation,,,20677832,,,The PHD3 Domain of MLL Acts as a CYP33-Regulated Switch between MLL-Mediated Activation and Repression .,published,journal,Biochemistry,Biochemistry,49,31,,,,,,,,,,,,,,,,,,,,,,6576,6586,2010, citations,entry_citation,16984,58883,1,,entry citation,,,20711759,,,Backbone chemical shifts assignments of D: -allose binding protein in the free form and in complex with D: -allose.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,1,,,,,,,,,,,,,,,,,,,,,,31,34,2011, citations,entry_citation,16986,58899,1,,entry citation,,,20598295,,,Solution structure of the N-terminal domain of the archaeal D-family DNA polymerase small subunit reveals evolutionary relationship to eukaryotic B-family polymerases.,published,journal,FEBS Lett.,FEBS letters,584,15,,,,,,,,,,,,,,,,,,,,,,3370,3375,2010, citations,citations,16988,58916,1,,entry citation,,,,,,"Solution NMR Structure of a domain of adhesion exoprotein from Pediococcus pentosaceus, Northeast Structural Genomics Consortium Target PtR41O",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16989,58952,1,,entry citation,,,20677832,,,The PHD3 Domain of MLL Acts as a CYP33-Regulated Switch between MLL-Mediated Activation and Repression .,published,journal,Biochemistry,Biochemistry,49,31,,,,,,,,,,,,,,,,,,,,,,6576,6586,2010, citations,entry_citation,1699,58966,1,,entry citation,,,,,"Xu, Guang-Yi, Deber, Charles M., ""Conformations of neurotensin in solution and in membrane environments studied by 2D-NMR spectroscopy,"" Int. 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U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,108,17,,,,,,,,,,,,,,,,,,,,,,6823,6827,2011, citations,entry_citation,16995,59052,1,,entry citation,,,,,,"Structural characterization of a BolA protein (ECH_0303) from Ehrlichia chaffeensis, the agent responsible for human monocytotropic ehrlichiosis.",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,16996,59071,1,,entry citation,,,21111057,,,Structural and functional characterization of the N-terminal domain of human Rad51D.,published,journal,Int. J. Biochem. Cell Biol.,The international journal of biochemistry & cell biology,43,3,,,,,,,,,,,,,,,,,,,,,,416,422,2011, citations,entry_citation,16997,59088,1,,entry citation,,,,,,Solution structure of protein SF1141 from Shigella flexneri 2a.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,16998,59111,1,,entry citation,,,,,,"Solution NMR Structure of Transcription factor NF-E2 subunit's DNA binding domain from Homo sapiens, Northeast Structural Genomics Consortium",in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,16999,59157,1,,entry citation,,,,,,Solution structure of protein CV0426 from Chromobacterium violaceum.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1700,59180,1,,entry citation,,,,,"Aumelas, Andre, Chiche, Laurent, Mahe, Eve, Le-Nguyen, Dung, Sizun, Philippe, Berthault, Patrick, Perly, Bruno, ""1H NMR Study of the Solution Structure of Sarafotoxin-S6b,"" Neurochem. 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Biol.,Journal of molecular biology,404,1,,,,,,,,,,,,,,,,,,,,,,45,55,2010, citations,entry_citation,17002,59229,1,,entry citation,,,NA,,,Solution NMR structure of the protein YP_510488.1,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,Citation1,17003,59248,1,,entry citation,,,20920334,,,The intriguing Cyclophilin A-HIV-1 Vpr interaction: prolyl cis/trans isomerisation catalysis and specific binding.,published,journal,BMC Struct. Biol.,BMC structural biology,10,1,,,,,,,,,,,,,,,,,,,,,,31,31,2010, citations,Reference_1,17005,59262,1,,reference citation,,,16008567,10.1111/j.1742-4658.2005.04794.x,,In vitro selection and characterization of a stable subdomain of phosphoribosylanthranilate isomerase.,published,journal,FEBS J.,The FEBS journal,272,14,,,,,,,,,,,,,,,,,,,,,,3684,3697,2005, citations,Entry_1,17005,59263,2,,entry citation,,,21354426,,,The structure of a truncated phosphoribosylanthranilate isomerase suggests a unified model for evolution of the ()8 barrel fold.,published,journal,J. Mol. Biol.,Journal of molecular biology,408,2,,,,,,,,,,,,,,,,,,,,,,291,303,2011, citations,entry_citation,17006,59287,1,,entry citation,,,20659891,,,Selective Transport of {alpha}-Mannosidase by Autophagic Pathways: STRUCTURAL BASIS FOR CARGO RECOGNITION BY Atg19 AND Atg34.,published,journal,J. Biol. 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Biol. Chem.,The Journal of biological chemistry,286,12,,,,,,,,,,,,,,,,,,,,,,10618,10627,2011, citations,entry_citation,17028,59817,1,,entry citation,,,20826161,,,The Solution Structure of the C-Terminal Ig-like Domain of the Bacteriophage Tail Tube Protein.,published,journal,J. Mol. Biol.,Journal of molecular biology,403,3,,,,,,,,,,,,,,,,,,,,,,468,479,2010, citations,entry_citation,17029,59832,1,,entry citation,,,21846933,,,"Structure, Dynamics, Lipid Binding, and Physiological Relevance of the Putative GTPase-binding Domain of Dictyostelium Formin C.",published,journal,J. Biol. Chem.,The Journal of biological chemistry,286,42,,,,,,,,,,,,,,,,,,,,,,36907,36920,2011, citations,citations,17030,59852,1,,entry citation,,,,,,"Solution NMR Structure of the Ras-binding domain of Serine/threonine-protein kinase B-raf from Homo sapiens, Northeast Structural Genomics Consortium Target HR4694F",in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17031,59893,1,,entry citation,,,,,,Solution NMR structure of the PBS linker polypeptide domain of phycobilisome linker protein apcE from Synechocystis sp. Northeast Structural Genomics Consortium Target SgR209C,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17032,59925,1,,entry citation,,,21765060,,,Structural role of the terminal disulfide bond in the sweetness of brazzein.,published,journal,Chem. Senses,Chemical senses,36,9,,,,,,,,,,,,,,,,,,,,,,821,830,2011, citations,reference_citation,17032,59926,2,,reference citation,,,,,,Insights into the sweetness of brazzein from beta-hairpin peptides derived from the N- and C- termini of brazzein,published,thesis,,,,,,,,,,,,,,,,,,,,,,University of Wisconsin-Madison,"Madison, WI",USA,,,,, citations,entry_citation,17033,59952,1,,entry citation,,,,,,"olution NMR Structure of Nonsense mRNA reducing factor 3A from H. Sapiens, Northeast Structural Genomics Consortium Target HR4714B",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17034,59971,1,,entry citation,,,21189021,,,Detailed Biophysical Characterization of the Acid-Induced PrP(c) to PrP() Conversion Process.,published,journal,Biochemistry,Biochemistry,50,7,,,,,,,,,,,,,,,,,,,,,,1162,1173,2011, citations,entry_citation,17035,59996,1,,entry citation,,,,,,NMR Solution Structure of asr4154 from Nostoc sp. 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NMR Assignments,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17043,60193,1,,entry citation,,,,,,TMS2 domain of Dengue virus NS4A protein,in preparation,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17044,60209,1,,entry citation,,,20818393,,,Cooperative interaction of transcription termination factors with the RNA polymerase II C-terminal domain.,published,journal,Nat. Struct. Mol. Biol.,Nature structural and molecular biology,17,10,,,,,,,,,,,,,,,,,,,,,,1195,1201,2010, citations,entry_citation,17045,60224,1,,entry citation,,,20737253,,,"Backbone and side chain (1)H, (15)N and (13)C assignments of the KSR1 CA1 domain.",published,journal,Biomol. 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Mol. Biol.,,362,4,,,,,,,,,,,,,,,,,,,,,,700,716,2006, citations,entry_citation,17056,60408,1,,entry citation,,,18310239,,,Four-alpha-Helix Bundle with Designed Anesthetic Binding Pockets. Part II: Halothane Effects on Structure and Dynamics,published,journal,Biophys. J.,,94,11,,,,,,,,,,,,,,,,,,,,,,4464,4472,2008, citations,entry_citation,17057,60423,1,,entry citation,,,18840435,,,Interaction of fatty acid with myoglobin,published,journal,FEBS Lett.,,582,25-26,,,,,,,,,,,,,,,,,,,,,,3643,3649,2008, citations,entry_citation,17058,60440,1,,entry citation,,,12763668,,,The structure of Ce(III)-Angiotensin II complex as obtained from NMR and molecular dynamics calculations,published,journal,J. Inorg. Biochem.,,95,2-3,,,,,,,,,,,,,,,,,,,,,,225,229,2003, citations,entry_citation,17059,60455,1,,entry citation,,,,,,Identification of a novel ubiquitin binding site of STAM1 VHS domain by NMR spectroscopy,published,journal,FEBS Lett.,,583,,,,,,,,,,,,,,,,,,,,,,,287,292,2009, citations,entry_citation,1706,60473,1,,entry citation,,,,,"Gould, Alison R., Mabbutt, Bridget C., Norton, Raymond S., ""Structure-function relationships in the polypeptide cardiac stimulant, anthopleurin-A (Effects of limited proteolysis by trypsin),"" Eur. J. Biochem. 189, 145-153 (1990).","Structure-function relationships in the polypeptide cardiac stimulant, anthopleurin-A (Effects of limited proteolysis by trypsin)",published,journal,Eur. J. Biochem.,,189,,,,,,,,,,,,,,,,,,,,,,,145,153,1990, citations,entry_citation,17060,60486,1,,entry citation,,,,,,"Replication protein A 32 interacts through a similar binding interface with TIPIN, XPA, and UNG2",published,journal,INT. J. BIOCHEM. 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NMR Assignments,Biomolecular NMR assignments,5,1,,,,,,,,,,,,,,,,,,,,,,101,103,2011, citations,entry_citation,17138,62030,1,,entry citation,,,,,,Solution structure and functional analyses of a coiled-coil interaction between MBD2 and p66alpha integral to the formation of the MeCP1 nucleosome remodeling complex,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,17139,62049,1,,entry citation,,,21378963,,,Structure of the VP16 transactivator target in the Mediator,published,journal,Nat. Struct. Mol. Biol.,,18,4,,,,,,,,,,,,,,,,,,,,,,410,415,2011, citations,entry_citation,17141,62073,1,,entry citation,,,20735118,,,Structure and RNA Interactions of the Plant MicroRNA Processing-Associated Protein HYL1.,published,journal,Biochemistry,Biochemistry,49,38,,,,,,,,,,,,,,,,,,,,,,8237,8239,2010, citations,entry_citation,17143,62090,1,,entry citation,,,20735118,,,Structure and RNA Interactions of the Plant MicroRNA Processing-Associated Protein HYL1.,published,journal,Biochemistry,Biochemistry,49,38,,,,,,,,,,,,,,,,,,,,,,8237,8239,2010, citations,entry_citation,17144,62107,1,,entry citation,,,21197590,,,"(1)H, (13)C, and (15)N backbone, side-chain, and heme chemical shift assignments for oxidized and reduced forms of the monoheme c-type cytochrome ApcA isolated from the acidophilic metal-reducing bacterium Acidiphilium cryptum.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,1,,,,,,,,,,,,,,,,,,,,,,89,92,2011, citations,entry_citation,17145,62129,1,,entry citation,,,21052876,,,"(1)H, (13)C and (15)N chemical shift assignments for the human Pitx2 homeodomain and a R24H homeodomain mutant.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,1,,,,,,,,,,,,,,,,,,,,,,105,107,2011, citations,entry_citation,17146,62145,1,,entry citation,,,21197590,,,"(1)H, (13)C, and (15)N backbone, side-chain, and heme chemical shift assignments for oxidized and reduced forms of the monoheme c-type cytochrome ApcA isolated from the acidophilic metal-reducing bacterium Acidiphilium cryptum.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,1,,,,,,,,,,,,,,,,,,,,,,89,92,2011, citations,entry_citation,17147,62167,1,,entry citation,,,21052876,,,"(1)H, (13)C and (15)N chemical shift assignments for the human Pitx2 homeodomain and a R24H homeodomain mutant.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,1,,,,,,,,,,,,,,,,,,,,,,105,107,2011, citations,Nephila_clavipes_MaSp-1,17148,62183,1,,entry citation,,,21152998,,,NMR assignments of the N-terminal domain of Nephila clavipes spidroin 1.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,2,,,,,,,,,,,,,,,,,,,,,,131,133,2011, citations,entry_citation,17149,62214,1,,entry citation,,,,,,"High-Resolution Structure of an Amyloidogenic Low-Populated Folding Intermediate from NMR Relaxation Dispersion Experiments",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17150,62247,1,,entry citation,,,,,,Solution Structure of cellobiose-specific phosphotransferase IIB component protein from Borrelia burgdorferi,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,17151,62269,1,,entry citation,,,,,,Null,in preparation,journal,To be Published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17152,62289,1,,entry citation,,,21561864,,,Disulfide-stabilized helical hairpin structure and activity of a novel antifungal peptide EcAMP1 from seeds of barnyard grass (Echinochloa crus-galli).,published,journal,J. Biol. Chem.,The Journal of biological chemistry,286,28,,,,,,,,,,,,,,,,,,,,,,25145,25153,2011, citations,entry_citation,17153,62303,1,,entry citation,,,21365717,10.1002/anie.201003582,,NMR Structures of Thiostrepton Derivatives for Characterization of the Ribosomal Binding Site,published,journal,Angew. Chem. Int. Ed.,,50,14,,,,,,,,,,,,,,,,,,,,,,3308,3312,2011, citations,entry_citation,17154,62328,1,,entry citation,,,21365717,10.1002/anie.201003582,,NMR Structures of Thiostrepton Derivatives for Characterization of the Ribosomal Binding Site,published,journal,Angew. Chem. Int. Ed.,,50,14,,,,,,,,,,,,,,,,,,,,,,3308,3312,2011, citations,entry_citation,17155,62353,1,,entry citation,,,21365717,10.1002/anie.201003582,,NMR Structures of Thiostrepton Derivatives for Characterization of the Ribosomal Binding Site,published,journal,Angew. Chem. Int. Ed.,,50,14,,,,,,,,,,,,,,,,,,,,,,3308,3312,2011, citations,entry_citation,17156,62378,1,,entry citation,,,21365717,10.1002/anie.201003582,,NMR Structures of Thiostrepton Derivatives for Characterization of the Ribosomal Binding Site,published,journal,Angew. Chem. Int. Ed.,,50,14,,,,,,,,,,,,,,,,,,,,,,3308,3312,2011, citations,entry_citation,17157,62403,1,,entry citation,,,21262234,,,The DNA-Binding Domain of Human PARP-1 Interacts with DNA Single-Strand Breaks as a Monomer through Its Second Zinc Finger.,published,journal,J. Mol. Biol.,Journal of molecular biology,407,1,,,,,,,,,,,,,,,,,,,,,,149,170,2011, citations,entry_citation,17158,62422,1,,entry citation,,,21262234,,,The DNA-Binding Domain of Human PARP-1 Interacts with DNA Single-Strand Breaks as a Monomer through Its Second Zinc Finger.,published,journal,J. Mol. Biol.,Journal of molecular biology,407,1,,,,,,,,,,,,,,,,,,,,,,149,170,2011, citations,entry_citation,17159,62441,1,,entry citation,,,20886513,,,N-terminal engineering of amyloid--binding Affibody molecules yields improved chemical synthesis and higher binding affinity.,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,19,12,,,,,,,,,,,,,,,,,,,,,,2319,2329,2010, citations,entry_citation,17160,62456,1,,entry citation,,,21052875,,,"(1)H, (13)C, (15)N resonance assignment of the chitin-binding protein CBP21 from Serratia marcescens.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,1,,,,,,,,,,,,,,,,,,,,,,117,119,2011, citations,entry_citation,17161,62474,1,,entry citation,,,20967574,,,Chemical shift assignments of a minimal Rna14p/Rna15p heterodimer from the yeast cleavage factor IA complex.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,1,,,,,,,,,,,,,,,,,,,,,,93,95,2011, citations,citation_1,17162,62501,1,,entry citation,,,21052778,,,Molecular basis of photochromism of a fluorescent protein revealed by direct (13)C detection under laser illumination.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,48,4,,,,,,,,,,,,,,,,,,,,,,237,246,2010, citations,citation_1,17163,62517,1,,entry citation,,,21052778,,,Molecular basis of photochromism of a fluorescent protein revealed by direct (13)C detection under laser illumination.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,48,4,,,,,,,,,,,,,,,,,,,,,,237,246,2010, citations,entry_citation_1,17165,62533,1,,entry citation,,,21255727,,,Conformational Conversion during Amyloid Formation at Atomic Resolution,published,journal,Mol. Cell.,,41,2,,,,,,,,,,,,,,,,,,,,,,161,172,2011, citations,reference_citation_1,17165,62534,2,,reference citation,,,19452600,,,A generic mechanism of beta-2-microglobulin assembly at neutral pH involving a specific proline switch.,published,journal,J. Mol. Biol.,Journal of Molecular Biology,5,386,,,,,,,,,,,,,,,,,,,,,,1312,1326,2009, citations,reference_citation_1_2,17165,62535,3,,reference citation,,,19452600,,,A generic mechanism of beta2-microglobulin amyloid assembly at neutral pH involving a specific proline switch.,published,journal,J. Mol. Biol.,Journal of molecular biology,386,5,,,,,,,,,,,,,,,,,,,,,,1312,1326,2009, citations,entry_citation_1,17166,62561,1,,entry citation,,,21255727,,,Conformational Conversion during Amyloid Formation at Atomic Resolution,published,journal,Mol. Cell.,,41,2,,,,,,,,,,,,,,,,,,,,,,161,172,2011, citations,reference_citation_1,17166,62562,2,,reference citation,,,19452600,,,A generic mechanism of beta-2-microglobulin assembly at neutral pH involving a specific proline switch.,published,journal,J. Mol. Biol.,,5,386,,,,,,,,,,,,,,,,,,,,,,1312,1326,2009, citations,reference_citation_1_2,17166,62563,3,,reference citation,,,19452600,,,A generic mechanism of beta2-microglobulin amyloid assembly at neutral pH involving a specific proline switch.,published,journal,J. Mol. Biol.,Journal of molecular biology,386,5,,,,,,,,,,,,,,,,,,,,,,1312,1326,2009, citations,citations,17169,62590,1,,entry citation,,,,,,Northeast Structural Genomics Consortium Target HR4527E,in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,17170,62626,1,,entry citation,,,,,,Resonance assignments of the Myb2 DNA binding domain in complex with its promoter MRE-1 from Trichomonas vaginalis,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,The_chemical_shift_assignment_of_the_SWIRM_domain_of_LSD1,17171,62642,1,,entry citation,,,,,,The chemical shift assignment of the SWIRM domain of LSD1,in preparation,BMRB only,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17172,62661,1,,entry citation,,,16415350,,,"Formation, structure and dissociation of the RNase S 3D domain-swapped dimer.",published,journal,J. Biol. 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Biol.,Nature structural & molecular biology,18,2,,,,,,,,,,,,,,,,,,,,,,213,221,2011, citations,entry_citation,1720,63241,1,,entry citation,,,,,"Gao, Yuan, Boyd, Jonathan, Pielak, Gary J., Williams, Robert J. P., ""Proton Nuclear Magnetic Resonance as a Probe of Differences in Structure between the C102T and F82S,C102T Variants of Iso-1-cytochrome c from the Yeast Saccharomyces cerevisiae,"" Biochemistry 30, 7033-7040 (1991).","Proton Nuclear Magnetic Resonance as a Probe of Differences in Structure between the C102T and F82S,C102T Variants of Iso-1-cytochrome c from the Yeast Saccharomyces cerevisiae",published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,7033,7040,1991, citations,entry_citation,17200,63257,1,,entry citation,,,21489993,,,Recognition of multivalent histone states associated with heterochromatin by UHRF1 protein.,published,journal,J. Biol. 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U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,104,47,,,,,,,,,,,,,,,,,,,,,,18473,18477,2007, citations,entry_citation,17249,64214,1,,entry citation,,,21188559,,,"1H, 13C and 15N resonances of the AlgE62 subunit from Azotobacter vinelandii mannuronan C5-epimerase.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,2,,,,,,,,,,,,,,,,,,,,,,147,149,2011, citations,entry_citation,17224,63722,1,,entry citation,,,11842220,,,TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,99,4,,,,,,,,,,,,,,,,,,,,,,1954,1959,2002, citations,entry_citation,17225,63744,1,,entry citation,,,11851341,,,The Solution Structure and DNA-binding Properties of the Cold-shock Domain of the Human Y-box Protein YB-1,published,journal,J. Mol. Biol.,Journal of Molecular Biology,316,,,,,,,,,,,,,,,,,,,,,,,317,326,2002, citations,entry_citation,17226,63760,1,,entry citation,,,21999759,,,Structure and dynamics of Mycobacterium tuberculosis truncated hemoglobin N: insights from NMR spectroscopy and molecular dynamics simulations.,published,journal,Biochemistry,Biochemistry,50,51,,,,,,,,,,,,,,,,,,,,,,11121,11130,2011, citations,citations_1,17227,63795,1,,entry citation,,,24821061,,,Cytotoxicity of recombinant tamapin and related toxin-like peptides on model cell lines,published,journal,Chem. Res. 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NMR Assignments,Biomolecular NMR assignments,5,1,,,,,,,,,,,,,,,,,,,,,,109,112,2011, citations,citations,17232,63880,1,,entry citation,,,,,,TBD,in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,17233,63901,1,,entry citation,,,,,,TBD,in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17234,63920,1,,entry citation,,,21338611,,,The Design Involved in PapI and Lrp Regulation of the pap Operon.,published,journal,J. Mol. Biol.,Journal of molecular biology,409,3,,,,,,,,,,,,,,,,,,,,,,311,332,2011, citations,entry_citation,17235,63939,1,,entry citation,,,,,,"Solution structure of a putative acyl carrier protein from Anaplasma phagocytophilum, the bacterium responsible for human granulocytic ehrlichiosis.",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,17236,63958,1,,entry citation,,,21181421,,,Sco proteins are involved in electron transfer processes.,published,journal,J. Biol. Inorg. 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Chem.,The Journal of biological chemistry,284,34,,,,,,,,,,,,,,,,,,,,,,23012,23023,2009, citations,entry_citation,17244,64129,1,,entry citation,,,22820306,,,Solution structure of an atypical PHD finger in BRPF2 and its interaction with DNA.,published,journal,J. Struct. Biol.,Journal of structural biology,180,1,,,,,,,,,,,,,,,,,,,,,,165,173,2012, citations,citations,17245,64151,1,,entry citation,,,22221265,,,Solution Structure of CCL21 and Identification of a Putative CCR7 Binding Site.,published,journal,Biochemistry,Biochemistry,51,3,,,,,,,,,,,,,,,,,,,,,,733,735,2012, citations,entry_citation,17246,64169,1,,entry citation,,,21367860,,,Structural and Functional Characterization of the Streptococcus pneumoniae RrgB Pilus Backbone D1 Domain.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,286,16,,,,,,,,,,,,,,,,,,,,,,14588,14597,2011, citations,citations,17247,64199,1,,entry citation,,,23438059,,,Structure of the extracellular domains of human and Xenopus Fn14: implications in the evolution of TWEAK and Fn14 interactions.,published,journal,FEBS J.,The FEBS journal,280,8,,,,,,,,,,,,,,,,,,,,,,1818,1829,2013, citations,entry_citation,1725,64233,1,,entry citation,,,,,"Mayo, Kevin H., Parra-Diaz, Dennisse, McCarthy, James B., Chelberg, Mary, ""Cell Adhesion Promoting Peptide GVKGDKGNPGWPGAP from the CollagenType IV Triple Helix: Cis/Trans Proline-Induced Multiple 1H NMR Conformations and Evidence for a KG/PG Multiple Turn Repeat Motif in the All-Trans Proline State,"" Biochemistry 30 (33), 8251-8267 (1991).","Cell Adhesion Promoting Peptide GVKGDKGNPGWPGAP from the CollagenType IV Triple Helix: Cis/Trans Proline-Induced Multiple 1H NMR Conformations and Evidence for a KG/PG Multiple Turn Repeat Motif in the All-Trans Proline State",published,journal,Biochemistry,,30,33,,,,,,,,,,,,,,,,,,,,,,8251,8267,1991, citations,entry_citation,17250,64246,1,,entry citation,,,21188561,,,"1H, 13C and 15N assignment of the GNA1946 outer membrane lipoprotein from Neisseria meningitidis",published,journal,Biomol. NMR Assignments,,5,2,,,,,,,,,,,,,,,,,,,,,,135,138,2011, citations,entry_citation,17251,64260,1,,entry citation,,,21181312,,,"1H, 13C and 15N resonance assignments of SARS-CoV main protease N-terminal domain.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,2,,,,,,,,,,,,,,,,,,,,,,143,145,2011, citations,citations,17252,64278,1,,entry citation,,,23438059,,,Structure of the extracellular domains of human and Xenopus Fn14: implications in the evolution of TWEAK and Fn14 interactions.,published,journal,FEBS J.,The FEBS journal,280,8,,,,,,,,,,,,,,,,,,,,,,1818,1829,2013, citations,entry_citation,17253,64294,1,,entry citation,,,21213258,,,"Peptide inhibitors of the malaria surface protein, apical membrane antigen 1: Identification of key binding residues.",published,journal,Biopolymers,Biopolymers,95,5,,,,,,,,,,,,,,,,,,,,,,354,364,2011, citations,citation_1,17254,64311,1,,entry citation,,,21417405,,,Promiscuous binding at the crossroads of numerous cancer pathways: insight from the binding of glutaminase interacting protein with glutaminase L.,published,journal,Biochemistry,Biochemistry,50,17,,,,,,,,,,,,,,,,,,,,,,3528,3539,2011, citations,citation_1,17255,64328,1,,entry citation,,,21417405,,,Promiscuous binding at the crossroads of numerous cancer pathways: insight from the binding of glutaminase interacting protein with glutaminase L.,published,journal,Biochemistry,Biochemistry,50,17,,,,,,,,,,,,,,,,,,,,,,3528,3539,2011, citations,citations,17256,64346,1,,entry citation,,,20933496,,,Oligomeric structure of a cathelicidin antimicrobial peptide in dodecylphosphocholine micelle determined by NMR spectroscopy.,published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1808,1,,,,,,,,,,,,,,,,,,,,,,369,381,2011, citations,Citation_1,17257,64360,1,,entry citation,,,21589901,,,A Component of the Xanthomonadaceae Type IV Secretion System Combines a VirB7 Motif with a N0 Domain Found in Outer Membrane Transport Proteins.,published,journal,PLoS Pathog.,PLoS pathogens,7,5,,,,,,,,,,,,,,,,,,,,,,,,2011, citations,entry_citation,17258,64386,1,,entry citation,,,21814766,,,Resonance assignments and secondary structure of a phytocystatin from Ananas comosus.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,6,1,,,,,,,,,,,,,,,,,,,,,,99,101,2012, citations,entry_citation,1726,64405,1,,entry citation,,,,,"Mayo, Kevin H., Parra-Diaz, Dennisse, McCarthy, James B., Chelberg, Mary, ""Cell Adhesion Promoting Peptide GVKGDKGNPGWPGAP from the CollagenType IV Triple Helix: Cis/Trans Proline-Induced Multiple 1H NMR Conformations and Evidence for a KG/PG Multiple Turn Repeat Motif in the All-Trans Proline State,"" Biochemistry 30 (33), 8251-8267 (1991).","Cell Adhesion Promoting Peptide GVKGDKGNPGWPGAP from the CollagenType IV Triple Helix: Cis/Trans Proline-Induced Multiple 1H NMR Conformations and Evidence for a KG/PG Multiple Turn Repeat Motif in the All-Trans Proline State",published,journal,Biochemistry,,30,33,,,,,,,,,,,,,,,,,,,,,,8251,8267,1991, citations,entry_citation,17260,64418,1,,entry citation,,,21298373,,,"Backbone and side-chain 1H, 15N and 13C resonance assignments of S18Y mutant of ubiquitin carboxy-terminal hydrolase L1.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,2,,,,,,,,,,,,,,,,,,,,,,165,168,2011, citations,entry_citation,17261,64433,1,,entry citation,,,21046186,,,"Structural characterization of human S100A16, a low-affinity calcium binder.",published,journal,J. Biol. Inorg. Chem.,Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry,16,2,,,,,,,,,,,,,,,,,,,,,,243,256,2011, citations,entry_citation,17262,64458,1,,entry citation,,,21046186,,,"Structural characterization of human S100A16, a low-affinity calcium binder.",published,journal,J. Biol. Inorg. Chem.,Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry,16,2,,,,,,,,,,,,,,,,,,,,,,243,256,2011, citations,entry_citation,17263,64485,1,,entry citation,,,21112336,,,Solution structure and activation mechanism of ubiquitin-like small archaeal modifier proteins.,published,journal,J. Mol. Biol.,Journal of molecular biology,405,4,,,,,,,,,,,,,,,,,,,,,,1040,1055,2011, citations,entry_citation,17264,64513,1,,entry citation,,,21167176,,,Solution NMR Structure of Apo-Calmodulin in Complex with the IQ Motif of Human Cardiac Sodium Channel NaV1.5.,published,journal,J. Mol. Biol.,Journal of molecular biology,406,1,,,,,,,,,,,,,,,,,,,,,,106,119,2011, citations,CtIP-LMO4-LIM1,17265,64534,1,,entry citation,,,21643835,,,"(1)H, (15)N and (13)C assignments of an intramolecular LMO4-LIM1/CtIP complex.",published,journal,Biomol. 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Chem.,The Journal of biological chemistry,287,28,,,,,,,,,,,,,,,,,,,,,,23819,23829,2012, citations,citations,17275,64752,1,,entry citation,,,,,,Solution Structure of Thioredoxin from Bacteroides Vulgatus,in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17276,64769,1,,entry citation,,,21821041,,,The TR-I pre-helix extension is structurally ordered in the unbound form and its flanking prolines are essential for binding.,published,journal,J. Mol. Biol.,Journal of molecular biology,412,4,,,,,,,,,,,,,,,,,,,,,,601,618,2011, citations,citations,17277,64783,1,,entry citation,,,,,,Solution Structure of a Putative Thioredoxin from Neisseria meningitidis,in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17278,64801,1,,entry citation,,,,,,NMR assignment of actin depolymerizing and dynamics regulatory protein from Toxoplasma gondii,in preparation,journal,Biomol. 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Chem.,The Journal of biological chemistry,287,16,,,,,,,,,,,,,,,,,,,,,,13194,13205,2012, citations,citations,17294,65144,1,,entry citation,,,21437709,,,Protein and metal cluster structure of the wheat metallothionein domain -E(c)-1: the second part of the puzzle.,published,journal,J. Biol. Inorg. Chem.,Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry,16,5,,,,,,,,,,,,,,,,,,,,,,683,694,2011, citations,citations,17295,65164,1,,entry citation,,,21437709,,,Protein and metal cluster structure of the wheat metallothionein domain -E(c)-1: the second part of the puzzle.,published,journal,J. Biol. Inorg. Chem.,Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry,16,5,,,,,,,,,,,,,,,,,,,,,,683,694,2011, citations,entry_citation,17296,65184,1,,entry citation,,,21167157,,,Conformational and molecular interaction studies of glucagon-like peptide-2 with its N-terminal extracellular receptor domain.,published,journal,FEBS Lett.,FEBS letters,585,2,,,,,,,,,,,,,,,,,,,,,,346,352,2011, citations,citations,17856,75888,1,,entry citation,,,22152477,,,Structural instability tuning as a regulatory mechanism in protein-protein interactions,published,journal,Mol. Cell,,44,5,,,,,,,,,,,,,,,,,,,,,,734,744,2011, citations,entry_citation,17297,65198,1,,entry citation,,,21167157,,,Conformational and molecular interaction studies of glucagon-like peptide-2 with its N-terminal extracellular receptor domain.,published,journal,FEBS Lett.,FEBS letters,585,2,,,,,,,,,,,,,,,,,,,,,,346,352,2011, citations,entry_citation,17298,65212,1,,entry citation,,,21229398,,,Resonance assignments of a putative PilT N-terminus domain protein SSO1118 from hyperthermophilic archaeon Sulfolobus solfataricus P2.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,2,,,,,,,,,,,,,,,,,,,,,,161,164,2011, citations,entry_citation,17299,65227,1,,entry citation,,,21287302,,,"1H, 13C and 15N chemical shift assignments of the thioredoxin from the obligate anaerobe Desulfovibrio vulgaris Hildenborough.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,2,,,,,,,,,,,,,,,,,,,,,,177,179,2011, citations,entry_citation,17300,65241,1,,entry citation,,,21287302,,,"1H, 13C and 15N chemical shift assignments of the thioredoxin from the obligate anaerobe Desulfovibrio vulgaris Hildenborough.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,2,,,,,,,,,,,,,,,,,,,,,,177,179,2011, citations,entry_citation,17301,65255,1,,entry citation,,,21546550,,,The DNA-recognition fold of Sso7c4 suggests a new member of SpoVT-AbrB superfamily from archaea.,published,journal,Nucleic Acids Res.,Nucleic acids research,39,15,,,,,,,,,,,,,,,,,,,,,,6764,6774,2011, citations,entry_citation,17302,65272,1,,entry citation,,,,,,Solution Structure and Backbone Dynamics of Human Liver Fatty Acid Binding Protein: Fatty Acid Binding Revisited,published,journal,Biophys. J.,Biophysical Journal,102,,,,,,,,,,,,,,,,,,,,,,,2585,2594,2012, citations,entry_citation,17303,65292,1,,entry citation,,,,,,Solution Structure and Backbone Dynamics of Human Liver Fatty Acid Binding Protein: Fatty Acid Binding Revisited,published,journal,Biophys. J.,Biophysical Journal,102,,,,,,,,,,,,,,,,,,,,,,,2585,2594,2012, citations,citations,17304,65312,1,,entry citation,,,,,,"Solution NMR structure of de novo designed rossmann 2x3 fold protein, Northeast Structural Genomics Consortium Target OR28",in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17305,65339,1,,entry citation,,,21978668,,,Three-dimensional structure of the effector PYRIN domain of NLRP12,published,journal,J. Mol. Biol.,,413,4,,,,,,,,,,,,,,,,,,,,,,790,803,2011, citations,NR1C_citation,17306,65359,1,,entry citation,,,21397186,,,"The contribution of entropy, enthalpy, and hydrophobic desolvation to cooperativity in repeat-protein folding.",published,journal,Structure,"Structure (London, England : 1993)",19,3,,,,,,,,,,,,,,,,,,,,,,349,360,2011, citations,entry_citation,17307,65384,1,,entry citation,,,18417468,,,Solution structure of a hydrocarbon stapled peptide inhibitor in complex with monomeric C-terminal domain of HIV-1 capsid.,published,journal,J. Biol. Chem.,,283,24,,,,,,,,,,,,,,,,,,,,,,16247,16278,2008, citations,entry_citation,17308,65405,1,,entry citation,,,21233223,,,Hexameric architecture of CstF supported by CstF-50 homodimerization domain structure.,published,journal,RNA,"RNA (New York, N.Y.)",17,3,,,,,,,,,,,,,,,,,,,,,,412,418,2011, citations,Citation_1,17309,65426,1,,entry citation,,,21382373,,,The solution structure of coronaviral stem-loop 2 (SL2) reveals a canonical CUYG tetraloop fold.,published,journal,FEBS Lett.,FEBS letters,585,7,,,,,,,,,,,,,,,,,,,,,,1049,1053,2011, citations,entry_citation,17310,65447,1,,entry citation,,,21410224,,,"NMR structures of apo L. casei dihydrofolate reductase and its complexes with trimethoprim and NADPH: contributions to positive cooperative binding from ligand-induced refolding, conformational changes, and interligand hydrophobic interactions.",published,journal,Biochemistry,Biochemistry,50,18,,,,,,,,,,,,,,,,,,,,,,3609,3620,2011, citations,entry_citation_1,17310,65448,2,,reference citation,,,,,,Structural Factors Determine the Selectivity of Antibacterial Drug Trimethoprim Binding to Dihydrofolate Reductase,published,journal,Pharm. Chem. J.,,41,7,,,,,,,,,,,,,,,,,,,,,,350,353,2007, citations,entry_citation,17311,65472,1,,entry citation,,,21410224,,,"NMR Structures of Apo L. casei Dihydrofolate Reductase and Its Complexes with Trimethoprim and NADPH: Contributions to Positive Cooperative Binding from Ligand-Induced Refolding, Conformational Changes, and Interligand Hydrophobic Interactions.",published,journal,Biochemistry,Biochemistry,50,18,,,,,,,,,,,,,,,,,,,,,,3609,3620,2011, citations,citation_1,17312,65497,1,,entry citation,,,22179618,,,Structure of minimal tetratricopeptide repeat domain protein Tah1 reveals mechanism of its interaction with Pih1 and Hsp90.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,8,,,,,,,,,,,,,,,,,,,,,,5698,5709,2012, citations,citation_2,17312,65498,2,,reference citation,,,,,,NMR Assignment of Tah1 protein bound to C-terminus of Hsp90,in preparation,journal,Biomol. NMR Assignments,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17313,65522,1,,entry citation,,,21233223,,,Hexameric architecture of CstF supported by CstF-50 homodimerization domain structure.,published,journal,RNA,"RNA (New York, N.Y.)",17,3,,,,,,,,,,,,,,,,,,,,,,412,418,2011, citations,entry_citation,17314,65539,1,,entry citation,,,,,,Solution Structure of a Nonphosphorylated Peptide Recognizing Domain,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17315,65553,1,,entry citation,,,21847092,,,An extended dsRBD with a novel zinc-binding motif mediates nuclear retention of fission yeast Dicer,published,journal,EMBO J.,,30,20,,,,,,,,,,,,,,,,,,,,,,4223,4235,2011, citations,entry_citation,17316,65576,1,,entry citation,,,21333656,,,Solution Structure of the K-Turn and Specifier Loop Domains from the Bacillus subtilis tyrS T-Box Leader RNA.,published,journal,J. Mol. Biol.,Journal of molecular biology,408,1,,,,,,,,,,,,,,,,,,,,,,99,117,2011, citations,entry_citation,17318,65592,1,,entry citation,,,,,,NMR solution structure of the protein YP_001092504.1,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17319,65611,1,,entry citation,,,,,,NMR solution structure of the protein NP_253742.1,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17320,65630,1,,entry citation,,,,,,NMR structure of the protein YP_926445.1 from Shewanella Amazonensis,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,17321,65649,1,,entry citation,,,22087227,,,Revisiting the NMR structure of the ultrafast downhill folding protein gpW from bacteriophage .,published,journal,PLoS ONE,PloS one,6,11,,,,,,,,,,,,,,,,,,,,,,e26409,e26409,2011, citations,citation_1,17322,65666,1,,entry citation,,,22087227,,,Revisiting the NMR structure of the ultrafast downhill folding protein gpW from bacteriophage .,published,journal,PLoS ONE,PloS one,6,11,,,,,,,,,,,,,,,,,,,,,,e26409,e26409,2011, citations,citations,17323,65683,1,,entry citation,,,21785987,,,Solution NMR structure of MED25(391-543) comprising the activator-interacting domain (ACID) of human mediator subunit 25.,published,journal,J. Struct. Funct. Genomics,Journal of structural and functional genomics,12,3,,,,,,,,,,,,,,,,,,,,,,159,166,2011, citations,citations,17324,65712,1,,entry citation,,,,,,A winged helix domain in human Mus81 is required for DNA binding,submitted,journal,to be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,Primary_reference,17325,65730,1,,entry citation,,,21516336,,,"1H, 13C and 15N resonance assignment of a 114-residue fragment of Engrailed 2 homeoprotein, a partially disordered protein.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,2,,,,,,,,,,,,,,,,,,,,,,229,231,2011, citations,Reference_paper,17326,65750,1,,entry citation,,,22252483,,,A procedure to validate and correct the (13)C chemical shift calibration of RNA datasets.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,52,2,,,,,,,,,,,,,,,,,,,,,,179,190,2012, citations,entry_citation,17327,65765,1,,entry citation,,,22034093,,,Solution NMR structure of proteorhodopsin.,published,journal,Angew. Chem. Int. Ed. Engl.,Angewandte Chemie (International ed. in English),50,50,,,,,,,,,,,,,,,,,,,,,,11942,11946,2011, citations,entry_citation,17328,65787,1,,entry citation,,,21388953,,,Solution Structures of Ca2+-CIB1 and Mg2+-CIB1 and Their Interactions with the Platelet Integrin {alpha}IIb Cytoplasmic Domain.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,286,19,,,,,,,,,,,,,,,,,,,,,,17181,17192,2011, citations,entry_citation,17329,65807,1,,entry citation,,,21388953,,,Solution Structures of Ca2+-CIB1 and Mg2+-CIB1 and Their Interactions with the Platelet Integrin {alpha}IIb Cytoplasmic Domain.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,286,19,,,,,,,,,,,,,,,,,,,,,,17181,17192,2011, citations,entry_citation,17330,65826,1,,entry citation,,,21539943,,,"Conformational, receptor interaction and alanine scan studies of glucose-dependent insulinotropic polypeptide.",published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1814,7,,,,,,,,,,,,,,,,,,,,,,882,888,2011, citations,entry_citation,17331,65842,1,,entry citation,,,21539943,,,"Conformational, receptor interaction and alanine scan studies of glucose-dependent insulinotropic polypeptide.",published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1814,7,,,,,,,,,,,,,,,,,,,,,,882,888,2011, citations,entry_citation,17332,65858,1,,entry citation,,,,,,High resolution NMR structure of gpW (W protein of bacteriophage lambda) at acidic pH,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17333,65876,1,,entry citation,,,16118278,,,Deubiquitinating function of ataxin-3: insights from the solution structure of the Josephin domain.,published,journal,Proc. Natl. Acad. Sci. 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Acta,Biochimica et biophysica acta,1808,4,,,,,,,,,,,,,,,,,,,,,,1161,1169,2011, citations,entry_citation,17347,66081,1,,entry citation,,,21262195,,,"The amyloidogenic SEVI precursor, PAP248-286, is highly unfolded in solution despite an underlying helical tendency.",published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1808,4,,,,,,,,,,,,,,,,,,,,,,1161,1169,2011, citations,entry_citation,17350,66100,1,,entry citation,,,,,,RIAM and vinculin binding to talin are mutually exclusive and regulate adhesion assembly and turnover,accepted,journal,J. Biol. 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NMR Assignments,Biomolecular NMR assignments,7,2,,,,,,,,,,,,,,,,,,,,,,171,174,2013, citations,high_calcium_androcam,17354,66171,1,,entry citation,,,22706934,,,"H, 15N and 13C chemical shifts of the D. melanogaster myosin VI light chain androcam in high calcium.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,2,,,,,,,,,,,,,,,,,,,,,,171,174,2013, citations,entry_citation,17355,66189,1,,entry citation,,,21674045,,,Solution structures of the acyl carrier protein domain from the highly reducing type I iterative polyketide synthase CalE8,published,journal,PLoS One,,6,6,,,,,,,,,,,,,,,,,,,,,,e20549,e20549,2011, citations,citation_1,17356,66207,1,,entry citation,,,21506606,,,Lipid Interacting Regions in Phosphate Stress Glycosyltransferase atDGD2 from Arabidopsis thaliana.,published,journal,Biochemistry,Biochemistry,50,21,,,,,,,,,,,,,,,,,,,,,,4451,4466,2011, citations,entry_citation,17357,66223,1,,entry citation,,,21259076,,,Backbone assignment and secondary structure of the PsbQ protein from photosystem II.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,2,,,,,,,,,,,,,,,,,,,,,,169,175,2011, citations,entry_citation,17358,66241,1,,entry citation,,,,,,Solution structure of the third Immunoglobulin-like domain of nectin-1,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,17359,66261,1,,entry citation,,,,,,"Solution NMR Structure of protein CD1104.2 from Clostridium difficile, Northeast Structural Genomics Consortium Target CfR130",in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1736,66293,1,,entry citation,,,,,"Timkovich, Russell, ""Heteronuclear Multiple-Quantum Coherence NMR Spectroscopy of Paramagnetic Heme and Cytochrome c-551,"" Inorg. Chem. 30, 37-42 (1991).","Heteronuclear Multiple-Quantum Coherence NMR Spectroscopy of Paramagnetic Heme and Cytochrome c-551",published,journal,Inorg. Chem.,,30,,,,,,,,,,,,,,,,,,,,,,,37,42,1991, citations,entry_citation,17360,66308,1,,entry citation,,,21360154,,,Fast methionine-based solution structure determination of calcium-calmodulin complexes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,50,1,,,,,,,,,,,,,,,,,,,,,,71,81,2011, citations,entry_citation,17361,66337,1,,entry citation,,,21770003,,,The conformation of bacteriorhodopsin loops in purple membranes resolved by solid-state MAS NMR spectroscopy.,published,journal,Angew. Chem. Int. Ed. Engl.,Angewandte Chemie (International ed. in English),50,36,,,,,,,,,,,,,,,,,,,,,,8432,8435,2011, citations,entry_citation,17362,66355,1,,entry citation,,,21281599,,,The E2-25K ubiquitin-associated (UBA) domain aids in polyubiquitin chain synthesis and linkage specificity.,published,journal,Biochem. Biophys. Res. Commun.,Biochemical and biophysical research communications,405,4,,,,,,,,,,,,,,,,,,,,,,662,666,2011, citations,entry_citation,17363,66372,1,,entry citation,,,,,,The Complete Domain Structure of Talin,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17364,66392,1,,entry citation,,,22645138,,,Solution structure of the phosphotyrosine binding (PTB) domain of human tensin2 protein in complex with deleted in liver cancer 1 (DLC1) peptide reveals a novel peptide binding mode.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,31,,,,,,,,,,,,,,,,,,,,,,26104,26114,2012, citations,entry_citation,17365,66415,1,,entry citation,,,21522130,,,"The CW domain, a new histone recognition module in chromatin proteins",published,journal,EMBO J.,,30,10,,,,,,,,,,,,,,,,,,,,,,1939,1952,2011, citations,ref,17367,66435,1,,entry citation,,,22150223,,,A Molten Globule-to-Ordered Structure Transition of Drosophila melanogaster Crammer Is Required for its Ability to Inhibit Cathepsin,published,journal,Biochem. J.,,442,3,,,,,,,,,,,,,,,,,,,,,,563,572,2012, citations,entry_citation,17368,66449,1,,entry citation,,,21298565,,,"1H, 13C and 15N backbone and side-chain chemical shift assignment of the Fyn SH2 domain and its complex with a phosphotyrosine peptide.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,2,,,,,,,,,,,,,,,,,,,,,,181,184,2011, citations,entry_citation,17369,66466,1,,entry citation,,,21298565,,,"1H, 13C and 15N backbone and side-chain chemical shift assignment of the Fyn SH2 domain and its complex with a phosphotyrosine peptide.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,2,,,,,,,,,,,,,,,,,,,,,,181,184,2011, citations,citations,17370,66487,1,,entry citation,,,,,,"Solution NMR structure of conjugate transposon protein BVU_1572(27-141) from Bacteroides Vulgatus, Northeast Structural Genomics Consortium Target BvR155.",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17371,66543,1,,entry citation,,,,,,Solution NMR structure of human Ubiquitin-like protein hs00113.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17373,66566,1,,entry citation,,,21113079,,,Biophysical Characterization of the Complex between Human Papillomavirus E6 Protein and Synapse-associated Protein 97.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,286,5,,,,,,,,,,,,,,,,,,,,,,3597,3606,2011, citations,entry_citation,17374,66582,1,,entry citation,,,21523437,,,"(1)H, (13)C and (15)N resonance assignments for a putative ADF/Cofilin from Trypanosoma brucei.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,2,,,,,,,,,,,,,,,,,,,,,,249,251,2011, citations,entry_citation,17375,66596,1,,entry citation,,,23139781,,,Proliferating Cell Nuclear Antigen (PCNA) Interactions in Solution Studied by NMR,published,journal,PLoS One,,7,11,,,,,,,,,,,,,,,,,,,,,,e48390,e48390,2012, citations,entry_citation,17376,66614,1,,entry citation,,,23139781,,,Proliferating Cell Nuclear Antigen (PCNA) Interactions in Solution Studied by NMR,published,journal,PLoS One,,7,11,,,,,,,,,,,,,,,,,,,,,,e48390,e48390,2012, citations,entry_citation,17377,66632,1,,entry citation,,,21311020,,,Structure of MyTH4-FERM Domains in Myosin VIIa Tail Bound to Cargo.,published,journal,Science,"Science (New York, N.Y.)",331,6018,,,,,,,,,,,,,,,,,,,,,,757,760,2011, citations,entry_citation,17378,66648,1,,entry citation,,,21565706,,,Advanced Glycation End Product Recognition by the Receptor for AGEs.,published,journal,Structure,"Structure (London, England : 1993)",19,5,,,,,,,,,,,,,,,,,,,,,,722,732,2011, citations,entry_citation,17379,66669,1,,entry citation,,,21967482,,,Solution structure of a 2:1 quindoline-c-MYC G-quadruplex: insights into G-quadruplex-interactive small molecule drug design.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,133,44,,,,,,,,,,,,,,,,,,,,,,17673,17680,2011, citations,entry_citation,17380,66688,1,,entry citation,,,21256132,,,Characterization of a Family of RanBP2-Type Zinc Fingers that Can Recognize Single-Stranded RNA.,published,journal,J. Mol. Biol.,Journal of molecular biology,407,2,,,,,,,,,,,,,,,,,,,,,,273,283,2011, citations,entry_citation,17381,66706,1,,entry citation,,,,,,1H and 15N Assigned Chemical Shifts for a putative surface protein,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,17382,66721,1,,entry citation,,,20924725,,,"1H, 13C, 15N backbone and side-chain resonance assignments of the human Raf-1 kinase inhibitor protein.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,1,,,,,,,,,,,,,,,,,,,,,,63,66,2011, citations,entry_citation,17383,66738,1,,entry citation,,,21507948,,,Structural characterization of the crimean-congo hemorrhagic Fever virus gn tail provides insight into virus assembly.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,286,24,,,,,,,,,,,,,,,,,,,,,,21678,21686,2011, citations,entry_citation,17384,66759,1,,entry citation,,,21523440,,,Backbone assignment of the tyrosine kinase Src catalytic domain in complex with imatinib.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,2,,,,,,,,,,,,,,,,,,,,,,221,224,2011, citations,entry_citation,17385,66789,1,,entry citation,,,21256132,,,Characterization of a Family of RanBP2-Type Zinc Fingers that Can Recognize Single-Stranded RNA.,published,journal,J. Mol. Biol.,Journal of molecular biology,407,2,,,,,,,,,,,,,,,,,,,,,,273,283,2011, citations,entry_citation,17386,66807,1,,entry citation,,,21256132,,,Characterization of a Family of RanBP2-Type Zinc Fingers that Can Recognize Single-Stranded RNA.,published,journal,J. Mol. Biol.,Journal of molecular biology,407,2,,,,,,,,,,,,,,,,,,,,,,273,283,2011, citations,entry_citation,17387,66825,1,,entry citation,,,21256132,,,Characterization of a Family of RanBP2-Type Zinc Fingers that Can Recognize Single-Stranded RNA.,published,journal,J. Mol. Biol.,Journal of molecular biology,407,2,,,,,,,,,,,,,,,,,,,,,,273,283,2011, citations,entry_citation,17388,66843,1,,entry citation,,,,,,Biochemical Characterization of the Ubiquitin Receptors in USP13 Reveals Different Catalytic Activation of Deubiquitination from Its Analogue USP5,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,17389,66863,1,,entry citation,,,,,,Northeast Structural Genomics Consortium Target HR5554A,in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1739,66905,1,,entry citation,,,,,"Park, Jang-su, Enoki, Minoru, Ohbu, Ayako, Fan, Kejun, Niki, Katsumi, Akutsu, Hideo, Kyogoku, Yoshimasa, ""Properties of aromatic residues in ferricytochrome c3 of Desulfovibrio vulgaris miyazaki f studied by 1H NMR,"" J. Mol. Struct. 242, 343-353 (1991).","Properties of aromatic residues in ferricytochrome c3 of Desulfovibrio vulgaris miyazaki f studied by 1H NMR",published,journal,J. Mol. 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Biol.,Chemistry & biology,18,4,,,,,,,,,,,,,,,,,,,,,,531,541,2011, citations,entry_citation,17393,67000,1,,entry citation,,,21513889,,,A Small Molecule Binding to the Coactivator CREB-Binding Protein Blocks Apoptosis in Cardiomyocytes.,published,journal,Chem. Biol.,Chemistry & biology,18,4,,,,,,,,,,,,,,,,,,,,,,531,541,2011, citations,entry_citation,17394,67028,1,,entry citation,,,21723249,,,Structure and membrane orientation of IAPP in its natively amidated form at physiological pH in a membrane environment.,published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1808,10,,,,,,,,,,,,,,,,,,,,,,2337,2342,2011, citations,entry_citation,17395,67047,1,,entry citation,,,21763489,,,The conformation and orientation of a 27-residue CCR5 peptide in a ternary complex with HIV-1 gp120 and a CD4-mimic peptide.,published,journal,J. Mol. Biol.,Journal of molecular biology,410,5,,,,,,,,,,,,,,,,,,,,,,778,797,2011, citations,entry_citation,17396,67064,1,,entry citation,,,21351738,,,Identification of Nucleic Acid Binding Residues in the FCS Domain of the Polycomb Group Protein Polyhomeotic.,published,journal,Biochemistry,Biochemistry,50,22,,,,,,,,,,,,,,,,,,,,,,4998,5007,2011, citations,entry_citation,17397,67085,1,,entry citation,,,21540209,,,Solution structure of all parallel G-quadruplex formed by the oncogene RET promoter sequence.,published,journal,Nucleic Acids Res.,Nucleic acids research,39,15,,,,,,,,,,,,,,,,,,,,,,6753,6763,2011, citations,entry_citation,17398,67103,1,,entry citation,,,22150589,,,Solution structure of the Pdp1 PWWP domain reveals its unique binding sites for methylated H4K20 and DNA.,published,journal,Biochem. J.,The Biochemical journal,442,3,,,,,,,,,,,,,,,,,,,,,,527,538,2012, citations,citations,17399,67119,1,,entry citation,,,21880019,,,Dissecting structure-function-stability relationships of a thermostable GH5-CBM3 cellulase from Bacillus subtilis 168,published,journal,Biochem. J.,,441,1,,,,,,,,,,,,,,,,,,,,,,95,104,, citations,entry_citation,17400,67139,1,,entry citation,,,22115774,,,Mechanisms of allosteric gene regulation by NMR quantification of microsecond-millisecond protein dynamics,published,journal,J. Mol. Biol.,,415,2,,,,,,,,,,,,,,,,,,,,,,372,381,2012, citations,1,17401,67154,1,,entry citation,,,21204525,,,NMR Spectroscopy and Molecular Dynamics Simulation of r(CCGCUGCGG)(2) Reveal a Dynamic UU Internal Loop Found in Myotonic Dystrophy Type 1.,published,journal,Biochemistry,Biochemistry,50,5,,,,,,,,,,,,,,,,,,,,,,599,601,2011, citations,citations,17402,67170,1,,entry citation,,,22052904,,,Solution structure and molecular interactions of lamin B receptor Tudor domain.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,2,,,,,,,,,,,,,,,,,,,,,,1032,1042,2012, citations,entry_citation,17403,67192,1,,entry citation,,,21347827,,,"1H, 15N and 13C resonance assignment of the N-terminal C39 peptidase-like domain of the ABC transporter Haemolysin B (HlyB).",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,2,,,,,,,,,,,,,,,,,,,,,,199,201,2011, citations,entry_citation,17404,67216,1,,entry citation,,,21718701,,,NMR-based substrate analog docking to Escherichia coli peptidyl-tRNA hydrolase.,published,journal,J. Mol. Biol.,Journal of molecular biology,412,4,,,,,,,,,,,,,,,,,,,,,,619,633,2011, citations,entry_citation,17405,67232,1,,entry citation,,,21516468,,,"1H, 13C and 15N chemical shift assignments of IPSENLS.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,2,,,,,,,,,,,,,,,,,,,,,,225,227,2011, citations,entry_citation,17406,67247,1,,entry citation,,,21778280,,,NMR structure of a 4 x 4 nucleotide RNA internal loop from an R2 retrotransposon: identification of a three purine-purine sheared pair motif and comparison to MC-SYM predictions.,published,journal,RNA,"RNA (New York, N.Y.)",17,9,,,,,,,,,,,,,,,,,,,,,,1664,1677,2011, citations,entry_citation,17407,67270,1,,entry citation,,,22615398,,,Structural basis for homeodomain recognition by the cell-cycle regulator Geminin.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,109,23,,,,,,,,,,,,,,,,,,,,,,8931,8936,2012, citations,citations,17408,67294,1,,entry citation,,,21763501,,,A small-molecule probe induces a conformation in HIV TAR RNA capable of binding drug-like fragments,published,journal,J. Mol. Biol.,,410,5,,,,,,,,,,,,,,,,,,,,,,984,996,2011, citations,entry_citation,17409,67316,1,,entry citation,,,22131102,,,Structure and Dynamics of Triazole-Linked DNA: Biocompatibility Explained,published,journal,Chemistry,,17,52,,,,,,,,,,,,,,,,,,,,,,14714,14717,2011, citations,entry_citation,17410,67336,1,,entry citation,,,21779926,,,"(1)H, (15)N and (13)C backbone chemical shift assignment of the titin A67-A68 domain tandem.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,6,1,,,,,,,,,,,,,,,,,,,,,,39,41,2012, citations,entry_citation,17411,67355,1,,entry citation,,,21518764,,,E2 Conjugating Enzyme Selectivity and Requirements for Function of the E3 Ubiquitin Ligase CHIP.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,286,24,,,,,,,,,,,,,,,,,,,,,,21277,21286,2011, citations,citations,17412,67371,1,,entry citation,,,21620860,,,Characterization of the Interaction of GABARAPL-1 with the LIR Motif of NBR1.,published,journal,J. Mol. Biol.,Journal of molecular biology,410,3,,,,,,,,,,,,,,,,,,,,,,477,487,2011, citations,entry_citation,17413,67397,1,,entry citation,,,22115774,,,Mechanisms of allosteric gene regulation by NMR quantification of microsecond-millisecond protein dynamics,published,journal,J. Mol. Biol.,,415,2,,,,,,,,,,,,,,,,,,,,,,372,381,2012, citations,entry_citation,17414,67413,1,,entry citation,,,21604815,,,pK(a) coupling at the intein active site: implications for the coordination mechanism of protein splicing with a conserved aspartate,published,journal,J. Am. Chem. Soc.,,133,26,,,,,,,,,,,,,,,,,,,,,,10275,10282,2011, citations,entry_citation,17415,67429,1,,entry citation,,,21265500,,,Experimentally Restrained Molecular Dynamics Simulations for Characterizing the Open States of Cytochrome P450(cam).,published,journal,Biochemistry,Biochemistry,50,10,,,,,,,,,,,,,,,,,,,,,,1664,1671,2011, citations,entry_citation,17416,67451,1,,entry citation,,,18025458,,,Structure of the deacetylase LpxC bound to the antibiotic CHIR-090: Time-dependent inhibition and specificity in ligand binding,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,104,47,,,,,,,,,,,,,,,,,,,,,,18433,18438,2007, citations,citation_1,17417,67468,1,,entry citation,,,21669869,,,An undecided coiled coil: the leucine zipper of Nek2 kinase exhibits atypical conformational exchange dynamics.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,286,31,,,,,,,,,,,,,,,,,,,,,,27537,27547,2011, citations,entry_citation,17418,67486,1,,entry citation,,,21519863,,,"(1)H, (13)C, and (15)N NMR assignments of the Pyrococcus abyssi DNA polymerase II intein.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,2,,,,,,,,,,,,,,,,,,,,,,233,235,2011, citations,citations,17419,67506,1,,entry citation,,,21688840,10.1021/bi200205v,,Multiple conformations of the cytidine repressor DNA-binding domain coalesce to one upon recognition of a specific DNA surface.,published,journal,Biochemistry,Biochemistry,50,31,,1520-4995,,,,,,,,,,,,,,,,,,,,6622,6632,2011, citations,entry_citation,17420,67526,1,,entry citation,,,,,,Solution structure of Chr148 from Cytophaga hutchinsonii. Northeast Structural Genomics Consortium Target Chr148,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,17421,67542,1,,entry citation,,,,,,"Solution structure of human C6orf130, a putative macro domain.",in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,Citation_1,17422,67563,1,,entry citation,,,21280608,,,Solution structure of a DNA duplex containing the potent anti-poxvirus agent cidofovir.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,133,7,,,,,,,,,,,,,,,,,,,,,,2264,2274,2011, citations,Citation_1,17423,67585,1,,entry citation,,,21280608,,,Solution structure of a DNA duplex containing the potent anti-poxvirus agent cidofovir.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,133,7,,,,,,,,,,,,,,,,,,,,,,2264,2274,2011, citations,entry_citation,17424,67606,1,,entry citation,,,23646163,,,"Integrin 1 has a long helix, extending from the transmembrane region to the cytoplasmic tail in detergent micelles.",published,journal,PLoS ONE,PloS one,8,4,,,,,,,,,,,,,,,,,,,,,,e62954,e62954,2013, citations,entry_citation,17425,67623,1,,entry citation,,,21821042,,,The Staphylococcus aureus pathogenicity island 1 protein gp6 functions as an internal scaffold during capsid size determination.,published,journal,J. Mol. Biol.,Journal of molecular biology,412,4,,,,,,,,,,,,,,,,,,,,,,710,722,2011, citations,entry_citation,17426,67642,1,,entry citation,,,22039263,,,"Engineering pro-angiogenic peptides using stable, disulfide-rich cyclic scaffolds.",published,journal,Blood,Blood,118,25,,,,,,,,,,,,,,,,,,,,,,6709,6717,2011, citations,entry_citation,17427,67659,1,,entry citation,,,21358637,,,Intrinsic disorder mediates the diverse regulatory functions of the Cdk inhibitor p21.,published,journal,Nat. Chem. Biol.,Nature chemical biology,7,4,,,,,,,,,,,,,,,,,,,,,,214,221,2011, citations,entry_citation,17428,67673,1,,entry citation,,,,,,Improving protein solubility by aromatic ablation,submitted,journal,J. Biomol. 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Chem.,The Journal of biological chemistry,287,30,,,,,,,,,,,,,,,,,,,,,,25589,25595,2012, citations,entry_citation,17433,67788,1,,entry citation,,,22178926,,,Basic amino-acid side chains regulate transmembrane integrin signalling.,published,journal,Nature,Nature,481,7380,,,,,,,,,,,,,,,,,,,,,,209,213,2012, citations,1,17434,67802,1,,entry citation,,,21673140,,,Structural basis for recognition of AT-rich DNA by unrelated xenogeneic silencing proteins,published,journal,Proc. Natl. Acad. Sci. U. S. A.,,108,26,,,,,,,,,,,,,,,,,,,,,,10690,10695,2011, citations,entry_citation,17435,67816,1,,entry citation,,,21673140,,,Structural basis for recognition of AT-rich DNA by unrelated xenogeneic silencing proteins,published,journal,Proc. Natl. Acad. Sci. U. S. 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Chem.,,287,41,,,,,,,,,,,,,,,,,,,,,,34120,34133,2012, citations,entry_citation,17526,69543,1,,entry citation,,,21652641,,,Structural basis for RNA recognition by NusB and NusE in the initiation of transcription antitermination.,published,journal,Nucleic Acids Res.,Nucleic acids research,39,17,,,,,,,,,,,,,,,,,,,,,,7803,7815,2011, citations,entry_citation,17442,67973,1,,entry citation,,,22869378,,,"Conformational flexibility determines selectivity and antibacterial, antiplasmodial, and anticancer potency of cationic alpha-helical peptides",published,journal,J. Biol. Chem.,,287,41,,,,,,,,,,,,,,,,,,,,,,34120,34133,2012, citations,entry_citation,17443,67993,1,,entry citation,,,21549715,,,Symmetry and Asymmetry of the RING-RING Dimer of Rad18.,published,journal,J. Mol. Biol.,Journal of molecular biology,410,3,,,,,,,,,,,,,,,,,,,,,,424,435,2011, citations,entry_citation,17444,68010,1,,entry citation,,,21320603,,,"Bacterial expression, purification, and model membrane reconstitution of the transmembrane and cytoplasmic domains of the human APP binding protein LR11/SorLA for NMR studies.",published,journal,Protein Expr. 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Biol.,Journal of molecular biology,411,1,,,,,,,,,,,,,,,,,,,,,,68,82,2011, citations,entry_citation,17475,68560,1,,entry citation,,,21615690,,,Structural basis of p63 SAM domain mutants involved in AEC syndrome.,published,journal,FEBS J.,The FEBS journal,278,15,,,,,,,,,,,,,,,,,,,,,,2680,2688,2011, citations,entry_citation,17476,68578,1,,entry citation,,,17766394,,,The solution structure of the ZnF UBP domain of USP33/VDU1.,published,journal,Protein Sci.,,16,9,,,,,,,,,,,,,,,,,,,,,,2072,2075,2007, citations,citation_1,17477,68592,1,,entry citation,,,23262193,,,NMR solution structure of C2 domain of MFG-E8 and insights into its molecular recognition with phosphatidylserine,published,journal,Biochim. Biophys. Acta,Biochimica et Biophysica Acta (BBA) - Biomembranes,1828,3,,,,,,,,,,,,,,,,,,,,,,1083,1093,2013, citations,entry_citation,17478,68610,1,,entry citation,,,21549626,,,CARD-Mediated Autoinhibition of cIAP1's E3 Ligase Activity Suppresses Cell Proliferation and Migration.,published,journal,Mol. Cell,Molecular cell,42,5,,,,,,,,,,,,,,,,,,,,,,569,583,2011, citations,entry_citation,17479,68633,1,,entry citation,,,21536732,,,Uncoupling of GTP hydrolysis from eIF6 release on the ribosome causes Shwachman-Diamond syndrome.,published,journal,Genes Dev.,Genes & development,25,9,,,,,,,,,,,,,,,,,,,,,,917,929,2011, citations,citations,17481,68660,1,,entry citation,,,,,,Northeast Structural Genomics Consortium Target SeR147,in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,17482,68687,1,,entry citation,,,21998307,,,"Structural characterization of Hsp12, the heat shock protein from Saccharomyces cerevisiae, in aqueous solution where it is intrinsically disordered and in detergent micelles where it is locally -helical.",published,journal,J. Biol. Chem.,The Journal of biological chemistry,286,50,,,,,,,,,,,,,,,,,,,,,,43447,43453,2011, citations,entry_citation,17483,68707,1,,entry citation,,,21998307,,,"Structural characterization of Hsp12, the heat shock protein from Saccharomyces cerevisiae, in aqueous solution where it is intrinsically disordered and in detergent micelles where it is locally -helical.",published,journal,J. Biol. Chem.,The Journal of biological chemistry,286,50,,,,,,,,,,,,,,,,,,,,,,43447,43453,2011, citations,citations,17484,68726,1,,entry citation,,,,,,"Solution NMR Structure of Homeobox domain of Homeobox protein Nkx-3.1 from homo sapiens, Northeast Structural Genomics Consortium Target HR6470A",in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17485,68759,1,,entry citation,,,21440557,,,Solution Structure of the mSin3A PAH2-Pf1 SID1 Complex: A Mad1/Mxd1-Like Interaction Disrupted by MRG15 in the Rpd3S/Sin3S Complex.,published,journal,J. Mol. Biol.,Journal of molecular biology,408,5,,,,,,,,,,,,,,,,,,,,,,987,1000,2011, citations,citation_1,17487,68774,1,,entry citation,,,21640070,,,NMR structural study of the intracellular loop 3 of the serotonin 5-HT(1A) receptor and its interaction with calmodulin.,published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1808,9,,,,,,,,,,,,,,,,,,,,,,2224,2232,2011, citations,entry_citation,17488,68789,1,,entry citation,,,,,,Spatial structure and dimer-monomer equilibrium of the ERBB3 transmembrane domain in DPC micelles,in preparation,journal,Biochim. Biophys. Acta,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17489,68807,1,,entry citation,,,21639149,,,Nonnative interactions in the FF domain folding pathway from an atomic resolution structure of a sparsely populated intermediate: an NMR relaxation dispersion study.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,133,28,,,,,,,,,,,,,,,,,,,,,,10974,10982,2011, citations,entry_citation,17490,68828,1,,entry citation,,,21653550,,,A novel occluded RNA recognition motif in Prp24 unwinds the U6 RNA internal stem loop.,published,journal,Nucleic Acids Res.,Nucleic acids research,39,17,,,,,,,,,,,,,,,,,,,,,,7837,7847,2011, citations,entry_citation,17491,68856,1,,entry citation,,,21653550,,,A novel occluded RNA recognition motif in Prp24 unwinds the U6 RNA internal stem loop.,published,journal,Nucleic Acids Res.,Nucleic acids research,39,17,,,,,,,,,,,,,,,,,,,,,,7837,7847,2011, citations,entry_citation,17492,68874,1,,entry citation,,,21526839,,,"The 3D Structure of Thuricin CD, a Two-Component Bacteriocin with Cysteine Sulfur to -Carbon Cross-links.",published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,133,20,,,,,,,,,,,,,,,,,,,,,,7680,7683,2011, citations,entry_citation,17493,68892,1,,entry citation,,,21565701,,,Structure-Function Analysis of a CVNH-LysM Lectin Expressed during Plant Infection by the Rice Blast Fungus Magnaporthe oryzae.,published,journal,Structure,"Structure (London, England : 1993)",19,5,,,,,,,,,,,,,,,,,,,,,,662,674,2011, citations,entry_citation,17494,68914,1,,entry citation,,,21604305,,,The PR/SET domain in PRDM4 is preceded by a zinc knuckle.,published,journal,Proteins,Proteins,79,7,,,,,,,,,,,,,,,,,,,,,,2341,2345,2011, citations,entry_citation,17495,68934,1,,entry citation,,,21526839,,,"The 3D Structure of Thuricin CD, a Two-Component Bacteriocin with Cysteine Sulfur to -Carbon Cross-links.",published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,133,20,,,,,,,,,,,,,,,,,,,,,,7680,7683,2011, citations,entry_citation,17496,68951,1,,entry citation,,,21310957,,,Solution Structure of the PilZ Domain Protein PA4608 Complex with Cyclic di-GMP Identifies Charge Clustering as Molecular Readout.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,286,16,,,,,,,,,,,,,,,,,,,,,,14304,14314,2011, citations,entry_citation,17579,70563,1,,entry citation,,,21708174,,,Structure of H/ACA RNP protein Nhp2p reveals cis/trans isomerization of a conserved proline at the RNA and Nop10 binding interface.,published,journal,J. Mol. Biol.,Journal of molecular biology,411,5,,,,,,,,,,,,,,,,,,,,,,927,942,2011, citations,entry_citation,17497,68980,1,,entry citation,,,21512128,,,Phox homology band 4.1/ezrin/radixin/moesin-like proteins function as molecular scaffolds that interact with cargo receptors and Ras GTPases.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,108,19,,,,,,,,,,,,,,,,,,,,,,7763,7768,2011, citations,entry_citation,17498,68995,1,,entry citation,,,21744165,,,Solid-state NMR sequential assignments of -synuclein.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,6,1,,,,,,,,,,,,,,,,,,,,,,51,55,2012, citations,entry_citation,17499,69011,1,,entry citation,,,21805376,,,Extensive de novo solid-state NMR assignments of the 33 kDa C-terminal domain of the Ure2 prion.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,51,3,,,,,,,,,,,,,,,,,,,,,,235,243,2011, citations,citation_1,17500,69026,1,,entry citation,,,21965682,,,"Structure and function of papiliocin with antimicrobial and anti-inflammatory activities isolated from the swallowtail butterfly, Papilio xuthus.",published,journal,J. Biol. Chem.,The Journal of biological chemistry,286,48,,,,,,,,,,,,,,,,,,,,,,41296,41311,2011, citations,entry_citation,17501,69041,1,,entry citation,,,,,,Solution NMR structure of the protein NP_344798.1,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,17502,69060,1,,entry citation,,,21931728,,,Pub1p C-terminal RRM domain interacts with Tif4631p through a conserved region neighbouring the Pab1p binding site,published,journal,PLoS One,,6,9,,,,,,,,,,,,,,,,,,,,,,e24481,,2011, citations,entry_citation,17503,69082,1,,entry citation,,,22308410,,,Ribosome clearance by FusB-type proteins mediates resistance to the antibiotic fusidic acid,published,journal,Proc. Natl. Acad. Sci. U. S. A.,,109,6,,,,,,,,,,,,,,,,,,,,,,2102,2107,2102, citations,entry_citation,17504,69106,1,,entry citation,,,21642970,,,Structure-function studies of FMRP RGG peptide recognition of an RNA duplex-quadruplex junction.,published,journal,Nat. Struct. Mol. Biol.,Nature structural & molecular biology,18,7,,,,,,,,,,,,,,,,,,,,,,796,804,2011, citations,citation_1,17505,69137,1,,entry citation,,,21643968,,,"(1)H, (13)C and (15)N resonance assignments of human muscle acylphosphatase.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,6,1,,,,,,,,,,,,,,,,,,,,,,27,29,2012, citations,entry_citation,17506,69152,1,,entry citation,,,21915914,,,Analysis of electrostatic interactions in the denatured state ensemble of the N-terminal domain of L9 under native conditions.,published,journal,Proteins,Proteins,79,12,,,,,,,,,,,,,,,,,,,,,,3500,3510,2011, citations,citation_1,17507,69168,1,,entry citation,,,18436956,,,Structural effects of Parkinson s disease linked DJ-1 mutations,published,journal,Protein Sci.,,17,5,,,,,,,,,,,,,,,,,,,,,,855,868,2008, citations,citations,17508,69187,1,,entry citation,,,,,,Northeast Structural Genomics Consortium Target HR6430A,in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,17509,69214,1,,entry citation,,,,,,Null,in preparation,journal,To be Published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1751,69233,1,,entry citation,,,,,"Yamamoto, Yasuhiko, Iwafune, Koji, Nanai, Norishige, Osawa, Akemi, Chujo, Riichiro, Suzuki, Tomohiko, ""NMR study of Galeorhinus japonicus myoglobin (1H-NMR study of molecular structure of the heme cavity),"" Eur. 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Soc.,Journal of the American Chemical Society,129,20,,,,,,,,,,,,,,,,,,,,,,6461,6469,2007, citations,entry_citation,17512,69286,1,,entry citation,,,21644056,,,"(1)H, (13)C, and (15)N NMR assignments for the helicase interaction domain of Staphylococcus aureus DnaG primase.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,6,1,,,,,,,,,,,,,,,,,,,,,,35,38,2012, citations,entry_citation,17513,69301,1,,entry citation,,,22226836,,,Conformational properties of the unfolded state of Im7 in nondenaturing conditions.,published,journal,J. Mol. Biol.,Journal of molecular biology,416,2,,,,,,,,,,,,,,,,,,,,,,300,318,2012, citations,jbc,17514,69325,1,,entry citation,,,22374868,,,Structural basis of RNA binding by leucine zipper GCN4,published,journal,Protein Sci.,,21,5,,,,,,,,,,,,,,,,,,,,,,667,676,2012, citations,entry_citation,17515,69342,1,,entry citation,,,21703451,,,"The INAD scaffold is a dynamic, redox-regulated modulator of signaling in the Drosophila eye.",published,journal,Cell,Cell,145,7,,,,,,,,,,,,,,,,,,,,,,1088,1101,2011, citations,entry_citation,17517,69364,1,,entry citation,,,21782828,,,Conformation effects of base modification on the anticodon stem-loop of Bacillus subtilis tRNA(Tyr).,published,journal,J. Mol. Biol.,Journal of molecular biology,412,2,,,,,,,,,,,,,,,,,,,,,,285,303,2011, citations,entry_citation_1,17518,69382,1,,entry citation,,,,,,A functional and structural analysis of tundem family 25 carbohydrate-binding modules from Paenibacillus polymyxa beta/alpha-amylase,in preparation,journal,Protein Sci.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation_2,17519,69399,1,,entry citation,,,,,,A functional and structural analysis of tundem family 25 carbohydrate-binding modules from Paenibacillus polymyxa beta/alpha-amylase,in preparation,journal,Protein Sci.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1752,69417,1,,entry citation,,,,,"Yamamoto, Yasuhiko, Iwafune, Koji, Nanai, Norishige, Osawa, Akemi, Chujo, Riichiro, Suzuki, Tomohiko, ""NMR study of Galeorhinus japonicus myoglobin (1H-NMR study of molecular structure of the heme cavity),"" Eur. J. 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NMR Assignments,Biomolecular NMR assignments,6,1,,,,,,,,,,,,,,,,,,,,,,19,21,2012, citations,citations,17524,69494,1,,entry citation,,,,,,Northeast Structural Genomics Consortium Target HR5460A,in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17525,69521,1,,entry citation,,,22194684,,,Structural Elucidation and Functional Characterization of the Hyaloperonospora arabidopsidis Effector Protein ATR13,published,journal,Plos Pathog.,,7,12,,,,,,,,,,,,,,,,,,,,,,e1002428,e1002428,2011, citations,entry_citation,17527,69560,1,,entry citation,,,20883017,,,"Chemical synthesis, folding, and structural insights into O-fucosylated epidermal growth factor-like repeat 12 of mouse Notch-1 receptor.",published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,132,42,,,,,,,,,,,,,,,,,,,,,,14857,14865,2010, citations,entry_citation,17528,69578,1,,entry citation,,,20883017,,,"Chemical synthesis, folding, and structural insights into O-fucosylated epidermal growth factor-like repeat 12 of mouse Notch-1 receptor.",published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,132,42,,,,,,,,,,,,,,,,,,,,,,14857,14865,2010, citations,entry_citation,17529,69594,1,,entry citation,,,21685363,,,A Smad action turnover switch operated by WW domain readers of a phosphoserine code.,published,journal,Genes Dev.,Genes & development,25,12,,,,,,,,,,,,,,,,,,,,,,1275,1288,2011, citations,citation_1,17530,69615,1,,entry citation,,,,,,"Solution NMR structure of the AHSA1-like protein RHE_CH02687 (1-152) from Rhizobium etli, Northeast Structural Genomics Consortium Target ReR242",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17531,69643,1,,entry citation,,,21593408,,,From the Cover: Discovery of an unusual biosynthetic origin for circular proteins in legumes.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,108,25,,,,,,,,,,,,,,,,,,,,,,10127,10132,2011, citations,citation_1,17532,69661,1,,entry citation,,,21608059,,,Nuclear magnetic resonance structure of calcium-binding protein 1 in a Ca(2+) -bound closed state: implications for target recognition.,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,20,8,,,,,,,,,,,,,,,,,,,,,,1356,1366,2011, citations,entry_citation,17533,69680,1,,entry citation,,,21439282,,,NMR studies of the solution conformation of the sex peptide from Drosophila melanogaster.,published,journal,FEBS Lett.,FEBS letters,585,8,,,,,,,,,,,,,,,,,,,,,,1197,1202,2011, citations,entry_citation,17534,69700,1,,entry citation,,,21643970,,,NMR resonance assignment of the autoimmunity protein SpaI from Bacillus subtilis ATCC 6633.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,6,1,,,,,,,,,,,,,,,,,,,,,,9,13,2012, citations,entry_citation,17535,69723,1,,entry citation,,,21443203,,,Structural Basis of the RNase H1 Activity on Stereo Regular Borano Phosphonate DNA/RNA Hybrids.,published,journal,Biochemistry,Biochemistry,50,19,,,,,,,,,,,,,,,,,,,,,,3903,3912,2011, citations,entry_citation,17536,69746,1,,entry citation,,,22147707,,,Insights into High Affinity Small Ubiquitin-like Modifier (SUMO) Recognition by SUMO-interacting Motifs (SIMs) Revealed by a Combination of NMR and Peptide Array Analysis.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,5,,,,,,,,,,,,,,,,,,,,,,3231,3240,2012, citations,citations,17537,69766,1,,entry citation,,,21609714,,,"Solution structure of a human minimembrane protein Ost4, a subunit of the oligosaccharyltransferase complex.",published,journal,Biochem. Biophys. Res. 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Biol. Chem.,The Journal of biological chemistry,286,45,,,,,,,,,,,,,,,,,,,,,,39307,39317,2011, citations,entry_citation,17552,70036,1,,entry citation,,,22275371,,,The growth-suppressive function of the polycomb group protein polyhomeotic is mediated by polymerization of its sterile alpha motif (SAM) domain.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,12,,,,,,,,,,,,,,,,,,,,,,8702,8713,2012, citations,entry_citation,17553,70055,1,,entry citation,,,,,,Solution structure of acyl CoA binding protein from Babesia bovis T2Bo,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17554,70077,1,,entry citation,,,22216260,,,Domain Analysis Reveals That a Deubiquitinating Enzyme USP13 Performs Non-Activating Catalysis for Lys63-Linked Polyubiquitin,published,journal,Plos One,,6,12,,,,,,,,,,,,,,,,,,,,,,e29362,e29362,2011, citations,entry_citation,17555,70096,1,,entry citation,,,22351767,,,Subcellular Localization of Talin Is Regulated by Inter-domain Interactions.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,17,,,,,,,,,,,,,,,,,,,,,,13799,13812,2012, citations,entry_citation,17556,70111,1,,entry citation,,,24234454,,,Characterization of the interaction between protein Snu13p/15.5K and the Rsa1p/NUFIP factor and demonstration of its functional importance for snoRNP assembly.,published,journal,Nucleic Acids Res.,Nucleic acids research,42,3,,,,,,,,,,,,,,,,,,,,,,2015,2036,2014, citations,entry_citation,17557,70127,1,,entry citation,,,22135285,,,Solution structure of the dimerization domain of the eukaryotic stalk P1/P2 complex reveals the structural organization of eukaryotic stalk complex.,published,journal,Nucleic Acids Res.,Nucleic acids research,40,7,,,,,,,,,,,,,,,,,,,,,,3172,3182,2012, citations,entry_citation,17558,70142,1,,entry citation,,,22128151,,,Interactions between the Conserved Hydrophobic Region of the Prion Protein and Dodecylphosphocholine Micelles.,published,journal,J. Biol. 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Soc.,,133,40,,,,,,,,,,,,,,,,,,,,,,16101,16110,2011, citations,entry_citation,17563,70252,1,,entry citation,,,,,,Structure solution of three glycyl-tRNA anticodon stem-loops,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17564,70269,1,,entry citation,,,,,,Structure solution of three glycyl-tRNA anticodon stem-loop,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17565,70286,1,,entry citation,,,,,,Structure solution of three glycyl-tRNA anticodon stem-loops,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17566,70303,1,,entry citation,,,22252483,,,A procedure to validate and correct the (13)C chemical shift calibration of RNA datasets.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,52,2,,,,,,,,,,,,,,,,,,,,,,179,190,2012, citations,entry_citation,17567,70319,1,,entry citation,,,22252483,,,A procedure to validate and correct the (13)C chemical shift calibration of RNA datasets.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,52,2,,,,,,,,,,,,,,,,,,,,,,179,190,2012, citations,entry_citation,17568,70336,1,,entry citation,,,22252483,,,A procedure to validate and correct the (13)C chemical shift calibration of RNA datasets.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,52,2,,,,,,,,,,,,,,,,,,,,,,179,190,2012, citations,entry_citation,17569,70351,1,,entry citation,,,21666677,,,Combinatorial readout of histone H3 modifications specifies localization of ATRX to heterochromatin.,published,journal,Nat. Struct. Mol. Biol.,Nature structural & molecular biology,18,7,,,,,,,,,,,,,,,,,,,,,,777,782,2011, citations,entry_citation,1757,70374,1,,entry citation,,,,,"Atkinson, R. 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NMR,Journal of biomolecular NMR,51,3,,,,,,,,,,,,,,,,,,,,,,235,243,2011, citations,entry_citation,17571,70402,1,,entry citation,,,,,,Structural Basis of the Dimerization-Induced Increase in Neurophysin-Hormone Affinity: Interplay of Inter-Domain and Inter-Subunit Interactions,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17572,70423,1,,entry citation,,,21782828,,,Conformation effects of base modification on the anticodon stem-loop of Bacillus subtilis tRNA(Tyr).,published,journal,J. Mol. Biol.,Journal of molecular biology,412,2,,,,,,,,,,,,,,,,,,,,,,285,303,2011, citations,entry_citation,17573,70442,1,,entry citation,,,21782828,,,Conformation effects of base modification on the anticodon stem-loop of Bacillus subtilis tRNA(Tyr).,published,journal,J. Mol. Biol.,Journal of molecular biology,412,2,,,,,,,,,,,,,,,,,,,,,,285,303,2011, citations,citation_1,17574,70462,1,,entry citation,,,,,,Structure of a yeast RNase III dsRBD complex with a non-canonical RNA substrate provides new insights into substrate recognition,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_2,17574,70463,2,,reference citation,,,15150409,,,Structural basis for recognition of the AGNN tetraloop RNA fold by the double-stranded RNA-binding domain of Rnt1p RNase III,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,101,22,,,,,,,,,,,,,,,,,,,,,,8307,8312,2004, citations,citations,17575,70488,1,,entry citation,,,22206986,,,Molecular Structure and Peptidoglycan Recognition of Mycobacterium tuberculosis ArfA (Rv0899).,published,journal,J. Mol. Biol.,Journal of molecular biology,416,2,,,,,,,,,,,,,,,,,,,,,,208,220,2012, citations,entry_citation,17576,70502,1,,entry citation,,,21244846,,,Separating instability from aggregation propensity in S-crystallin variants.,published,journal,Biophys. J.,Biophysical journal,100,2,,,,,,,,,,,,,,,,,,,,,,498,506,2011, citations,biophysical_characterization,17576,70503,2,,reference citation,,,21244846,,,Separating instability from aggregation propensity in (gamma)S-crystallin variants.,published,journal,Biophys. J.,,100,2,,,,,,,,,,,,,,,,,,,,,,498,506,2011, citations,Siderocalin_Q83_reveals_a_dual_ligand_binding_site,17577,70520,1,,entry citation,,,21951132,,,Lipocalin Q83 reveals a dual ligand binding mode with potential implications for the functions of siderocalins.,published,journal,Biochemistry,Biochemistry,50,43,,,,,,,,,,,,,,,,,,,,,,9192,9199,2011, citations,entry_citation,17578,70540,1,,entry citation,,,21708174,,,Structure of H/ACA RNP protein Nhp2p reveals cis/trans isomerization of a conserved proline at the RNA and Nop10 binding interface.,published,journal,J. Mol. Biol.,Journal of molecular biology,411,5,,,,,,,,,,,,,,,,,,,,,,927,942,2011, citations,1,17578,70541,2,,reference citation,,,16943774,,,Crystal structure of an H/ACA box ribonucleoprotein particle,published,journal,Nature,,443,21,,,,,,,,,,,,,,,,,,,,,,302,307,2006, citations,entry_citation,17580,70586,1,,entry citation,,,21795379,,,c-MYC promoter G-quadruplex formed at the 5'-end of NHE III1 element: insights into biological relevance and parallel-stranded G-quadruplex stability.,published,journal,Nucleic Acids Res.,Nucleic acids research,39,20,,,,,,,,,,,,,,,,,,,,,,9023,9033,2011, citations,entry_citation,17581,70600,1,,entry citation,,,22229737,,,"A novel -conopeptide, CnIIIC, exerts potent and preferential inhibition of NaV1.2/1.4 channels and blocks neuronal nicotinic acetylcholine receptors.",published,journal,Br. J. Pharmacol.,British journal of pharmacology,166,5,,,,,,,,,,,,,,,,,,,,,,1654,1668,2012, citations,entry_citation,17582,70620,1,,entry citation,,,21244846,,,Separating instability from aggregation propensity in S-crystallin variants.,published,journal,Biophys. J.,Biophysical journal,100,2,,,,,,,,,,,,,,,,,,,,,,498,506,2011, citations,biophysical_characterization,17582,70621,2,,reference citation,,,21244846,,,Separating instability from aggregation propensity in (gamma)S-crystallin variants.,published,journal,Biophys. J.,,100,2,,,,,,,,,,,,,,,,,,,,,,498,506,2011, citations,entry_citation,17583,70639,1,,entry citation,,,21786372,,,"The 3D solution structure of thurincin H, a bacteriocin with four sulfur to -carbon crosslinks.",published,journal,Angew. Chem. Int. Ed. Engl.,Angewandte Chemie (International ed. in English),50,37,,,,,,,,,,,,,,,,,,,,,,8718,8721,2011, citations,entry_citation,17584,70659,1,,entry citation,,,22130674,,,CD4+ T Cell-derived Novel Peptide Thp5 Induces Interleukin-4 Production in CD4+ T Cells to Direct T Helper 2 Cell Differentiation.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,4,,,,,,,,,,,,,,,,,,,,,,2830,2835,2012, citations,entry_citation,17585,70676,1,,entry citation,,,22000520,,,Structural Insight into the Mycobacterium tuberculosis Rv0020c Protein and Its Interaction with the PknB Kinase.,published,journal,Structure,"Structure (London, England : 1993)",19,10,,,,,,,,,,,,,,,,,,,,,,1525,1534,2011, citations,entry_citation,17586,70695,1,,entry citation,,,22000520,,,Structural Insight into the Mycobacterium tuberculosis Rv0020c Protein and Its Interaction with the PknB Kinase.,published,journal,Structure,"Structure (London, England : 1993)",19,10,,,,,,,,,,,,,,,,,,,,,,1525,1534,2011, citations,entry_citation,17588,70714,1,,entry citation,,,21821794,,,Phosphatidylinositol monophosphate-binding interface in the oomycete RXLR effector AVR3a is required for its stability in host cells to modulate plant immunity.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,108,35,,,,,,,,,,,,,,,,,,,,,,14682,14687,2011, citations,entry_citation,17589,70732,1,,entry citation,,,21653550,,,A novel occluded RNA recognition motif in Prp24 unwinds the U6 RNA internal stem loop.,published,journal,Nucleic Acids Res.,Nucleic acids research,39,17,,,,,,,,,,,,,,,,,,,,,,7837,7847,2011, citations,entry_citation,17590,70750,1,,entry citation,,,21683709,,,A eukaryotic-like interaction of soluble cyanobacterial sensory rhodopsin transducer with DNA.,published,journal,J. Mol. Biol.,Journal of molecular biology,411,2,,,,,,,,,,,,,,,,,,,,,,449,462,2011, citations,entry_citation,17591,70767,1,,entry citation,,,21683709,,,A eukaryotic-like interaction of soluble cyanobacterial sensory rhodopsin transducer with DNA.,published,journal,J. Mol. Biol.,Journal of molecular biology,411,2,,,,,,,,,,,,,,,,,,,,,,449,462,2011, citations,entry_citation,17592,70784,1,,entry citation,,,21683709,,,A eukaryotic-like interaction of soluble cyanobacterial sensory rhodopsin transducer with DNA.,published,journal,J. Mol. Biol.,Journal of molecular biology,411,2,,,,,,,,,,,,,,,,,,,,,,449,462,2011, citations,entry_citation,17593,70802,1,,entry citation,,,21791199,,,Comparative NMR analysis of an 80-residue G protein-coupled receptor fragment in two membrane mimetic environments,published,journal,Biochim. Biophys. Acta,,1808,11,,,,,,,,,,,,,,,,,,,,,,2674,2684,2011, citations,entry_citation,17594,70827,1,,entry citation,,,,,,NMR solution structure of a helical bundle from the E3 ligase HECTD1,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17595,70851,1,,entry citation,,,22156373,,,Structural and functional analysis of the archaeal endonuclease Nob1.,published,journal,Nucleic Acids Res.,Nucleic acids research,40,7,,,,,,,,,,,,,,,,,,,,,,3259,3274,2012, citations,citation_1,17596,70877,1,,entry citation,,,21845363,,,"Backbone and sidechain (1)H, (13)C and (15)N chemical shift assignments of the hydrophobin DewA from Aspergillus nidulans.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,6,1,,,,,,,,,,,,,,,,,,,,,,83,86,2012, citations,entry_citation,17597,70899,1,,entry citation,,,21761124,,,"Chemical shift assignments for Rv0577, a putative glyoxylase associated with virulence from Mycobacterium tuberculosis.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,6,1,,,,,,,,,,,,,,,,,,,,,,43,46,2012, citations,entry_citation,17598,70915,1,,entry citation,,,22053789,,,"Characterization of the PilN, PilO and PilP type IVa pilus subcomplex",published,journal,Mol. Micro.,,82,6,,,,,,,,,,,,,,,,,,,,,,1496,1514,2011, citations,citations,17599,70934,1,,entry citation,,,22078569,,,A Conformational Switch in the CRIB-PDZ Module of Par-6,published,journal,Structure,,19,11,,,,,,,,,,,,,,,,,,,,,,1711,1722,2011, citations,entry_citation,1760,70954,1,,entry citation,,,,,"Weiss, Michael A., Hua, Qing-Xin, Lynch, Claire S., Frank, Bruce H., Shoelson, Steven E., ""Heteronuclear 2D NMR Studies of an Engineered Insulin Monomer: Assignment and Characterization of the Receptor-Binding Surface by Selective 2H and 13C Labeling with Application to Protein Design,"" Biochemistry 30 (30), 7373-7389 (1991).","Heteronuclear 2D NMR Studies of an Engineered Insulin Monomer: Assignment and Characterization of the Receptor-Binding Surface by Selective 2H and 13C Labeling with Application to Protein Design",published,journal,Biochemistry,,30,30,,,,,,,,,,,,,,,,,,,,,,7373,7389,1991, citations,citations,17600,70967,1,,entry citation,,,22078569,,,A Conformational Switch in the CRIB-PDZ Module of Par-6,published,journal,Structure,,19,11,,,,,,,,,,,,,,,,,,,,,,1711,1722,2011, citations,entry_citation,17601,70987,1,,entry citation,,,22121021,,,An equilibrium-dependent retroviral mRNA switch regulates translational recoding.,published,journal,Nature,Nature,480,7378,,,,,,,,,,,,,,,,,,,,,,561,564,2011, citations,entry_citation,17602,71004,1,,entry citation,,,22242625,,,"Solution NMR of a 463-residue phosphohexomutase: domain 4 mobility, substates, and phosphoryl transfer defect.",published,journal,Biochemistry,Biochemistry,51,3,,,,,,,,,,,,,,,,,,,,,,807,819,2012, citations,entry_citation,17603,71024,1,,entry citation,,,21857680,,,Solution structure of a minor and transiently formed state of a T4 lysozyme mutant.,published,journal,Nature,Nature,477,7362,,,,,,,,,,,,,,,,,,,,,,111,114,2011, citations,entry_citation,17604,71043,1,,entry citation,,,21857680,,,Solution structure of a minor and transiently formed state of a T4 lysozyme mutant.,published,journal,Nature,Nature,477,7362,,,,,,,,,,,,,,,,,,,,,,111,114,2011, citations,entry_citation,17606,71067,1,,entry citation,,,22247551,,,Structural Insight into Recognition of Methylated Histone Tails by Retinoblastoma-binding Protein 1.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,11,,,,,,,,,,,,,,,,,,,,,,8531,8540,2012, citations,entry_citation,17692,72664,1,,entry citation,,,22079190,,,Residual structure and dynamics in DMSO-d6 denatured Dynein Light Chain protein.,published,journal,Biochimie,Biochimie,94,1,,,,,,,,,,,,,,,,,,,,,,231,241,2012, citations,entry_citation,17607,71082,1,,entry citation,,,22247551,,,Structural insight into recognition of methylated histone tails by retinoblastoma-binding protein 1.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,11,,,,,,,,,,,,,,,,,,,,,,8531,8540,2012, citations,entry_citation,17608,71101,1,,entry citation,,,21915608,,,"1H, 13C and 15N resonance assignments of the GTPase-activating (GAP) and Ral binding domains (GBD) of RLIP76 (RalBP1).",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,6,2,,,,,,,,,,,,,,,,,,,,,,119,122,2012, citations,entry_citation,17609,71120,1,,entry citation,,,,,,Solution Structure of Hr4436B.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1761,71142,1,,entry citation,,,,,"Weiss, Michael A., Hua, Qing-Xin, Lynch, Claire S., Frank, Bruce H., Shoelson, Steven E., ""Heteronuclear 2D NMR Studies of an Engineered Insulin Monomer: Assignment and Characterization of the Receptor-Binding Surface by Selective 2H and 13C Labeling with Application to Protein Design,"" Biochemistry 30 (30), 7373-7389 (1991).","Heteronuclear 2D NMR Studies of an Engineered Insulin Monomer: Assignment and Characterization of the Receptor-Binding Surface by Selective 2H and 13C Labeling with Application to Protein Design",published,journal,Biochemistry,,30,30,,,,,,,,,,,,,,,,,,,,,,7373,7389,1991, citations,entry_citation,17610,71155,1,,entry citation,,,21930707,,,Solution structure of the state 1 conformer of GTP-bound H-Ras protein and distinct dynamic properties between the state 1 and state 2 conformers.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,286,45,,,,,,,,,,,,,,,,,,,,,,39644,39653,2011, citations,AHSA1-like_protein_Rmet_5065_from_Ralstonia_metallidurans,17611,71180,1,,entry citation,,,,,,"Title: Solution NMR structure of protein Rmet_5065 from Ralstonia metallidurans. Northeast Structural Genomics Consortium Target CrR115.",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,17612,71213,1,,entry citation,,,,,,"Solution NMR Structure of a Protein With a Redesigned Hydrophobic Core, Northeast Structural Genomics Consortium Target OR38",in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,17613,71235,1,,entry citation,,,,,,Northeast Structural Genomics Consortium Target OR36,in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,17614,71264,1,,entry citation,,,21785437,,,Mitochondrial uncoupling protein 2 structure determined by NMR molecular fragment searching.,published,journal,Nature,Nature,476,7358,,,,,,,,,,,,,,,,,,,,,,109,113,2011, citations,entry_citation,17615,71290,1,,entry citation,,,22817892,,,An alpha-helix to beta-barrel domain switch transforms the transcription factor RfaH into a translation factor,published,journal,Cell,Cell Press,150,2,,,,,,,,,,,,,,,,,,,,,,291,303,2012, citations,citation_1,17616,71306,1,,entry citation,,,22567147,,,NMR Insights into Folding and Self-Association of Plasmodium falciparum P2.,published,journal,PLoS ONE,PloS one,7,5,,,,,,,,,,,,,,,,,,,,,,,,2012, citations,pepS4-3,17617,71323,1,,entry citation,,,,,,structure of S4-3 voltage sensor peptide,in preparation,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17618,71337,1,,entry citation,,,,,,Comparison of Proline Substitutions at Positions 8 and 10 in WALP19,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17619,71362,1,,entry citation,,,,,,Comparison of Proline Substitutions at Positions 8 and 10 in WALP19,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1762,71383,1,,entry citation,,,,,"Weiss, Michael A., Hua, Qing-Xin, Lynch, Claire S., Frank, Bruce H., Shoelson, Steven E., ""Heteronuclear 2D NMR Studies of an Engineered Insulin Monomer: Assignment and Characterization of the Receptor-Binding Surface by Selective 2H and 13C Labeling with Application to Protein Design,"" Biochemistry 30 (30), 7373-7389 (1991).","Heteronuclear 2D NMR Studies of an Engineered Insulin Monomer: Assignment and Characterization of the Receptor-Binding Surface by Selective 2H and 13C Labeling with Application to Protein Design",published,journal,Biochemistry,,30,30,,,,,,,,,,,,,,,,,,,,,,7373,7389,1991, citations,entry_citation,17620,71396,1,,entry citation,,,22752790,,,"1H, 13C and 15N assignment of D2 domain of human fibroblast growth factor receptor 4.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,2,,,,,,,,,,,,,,,,,,,,,,179,182,2013, citations,entry_citation,17621,71412,1,,entry citation,,,,,,Solution structure of the EF-hand domain of Human Polycystin 2,in preparation,journal,To Be Published,To Be Published,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17622,71431,1,,entry citation,,,,,,Multi-domain conformational selection underlies pre-mRNA splicing regulation by U2AF,in preparation,journal,Nature,Nature,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17623,71448,1,,entry citation,,,,,,Multi-domain conformational selection underlies pre-mRNA splicing regulation by U2AF,in preparation,journal,Nature,Nature,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17625,71466,1,,entry citation,,,21471192,,,Solution Structure of the Monovalent Lectin Microvirin in Complex with Man{alpha}(1-2)Man Provides a Basis for Anti-HIV Activity with Low Toxicity.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,286,23,,,,,,,,,,,,,,,,,,,,,,20788,20796,2011, citations,entry_citation,17626,71485,1,,entry citation,,,21925511,,,Structural characterization of the interactions between palladin and -actinin.,published,journal,J. Mol. Biol.,Journal of molecular biology,413,3,,,,,,,,,,,,,,,,,,,,,,712,725,2011, citations,entry_citation,17627,71504,1,,entry citation,,,,,,The Interaction of alpha-Actinin-2 with ZASP and Titin,published,journal,Not known,,,,,,,,,,,,,,,,,,,,,University College London,London,UK,,,,2004, citations,Citation_1,17628,71523,1,,entry citation,,,22799562,,,Structure of the Alk1 extracellular domain and characterization of its bone morphogenetic protein (BMP) binding properties.,published,journal,Biochemistry,Biochemistry,51,32,,,,,,,,,,,,,,,,,,,,,,6328,6341,2012, citations,entry_citation,17629,71549,1,,entry citation,,,,,,Not known,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17630,71571,1,,entry citation,,,24521053,,,Structural Characterization of Interactions between the Double-Stranded RNA-Binding Zinc Finger Protein JAZ and Nucleic Acids.,published,journal,Biochemistry,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,17631,71587,1,,entry citation,,,,,,Backbone assignment of human JAZ ZF2,in preparation,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17632,71604,1,,entry citation,,,21606197,,,Two closely-spaced tyrosines regulate NFAT signaling in B cells via Syk association with Vav.,published,journal,Mol. Cell. Biol.,Molecular and cellular biology,31,14,,,,,,,,,,,,,,,,,,,,,,2984,2996,2011, citations,entry_citation,17633,71622,1,,entry citation,,,22294693,,,"Structural and Functional Characterization of Bc28.1, Major Erythrocyte-binding Protein from Babesia canis Merozoite Surface.",published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,12,,,,,,,,,,,,,,,,,,,,,,9495,9508,2012, citations,citations,17634,71642,1,,entry citation,,,21688840,,,Multiple conformations of the cytidine repressor DNA-binding domain coalesce to one upon recognition of a specific DNA surface.,published,journal,Biochemistry,Biochemistry,50,31,,,,,,,,,,,,,,,,,,,,,,6622,6632,2011, citations,entry_citation,17636,71676,1,,entry citation,,,21901408,,,"(1)H, (13)C, and (15)N NMR resonance assignments of reduced full length and shortened forms of the Grx domain of Mus musculus TGR.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,6,1,,,,,,,,,,,,,,,,,,,,,,103,107,2012, citations,entry_citation,17637,71690,1,,entry citation,,,21901408,,,"(1)H, (13)C, and (15)N NMR resonance assignments of reduced full length and shortened forms of the Grx domain of Mus musculus TGR.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,6,1,,,,,,,,,,,,,,,,,,,,,,103,107,2012, citations,citations,17638,71704,1,,entry citation,,,21690393,,,Structure and function of the complete internal fusion loop from Ebolavirus glycoprotein 2.,published,journal,Proc. Natl. Acad. Sci. U. S. A.,Proceedings of the National Academy of Sciences of the United States of America,,,,,,,,,,,,,,,,,,,,,,,,,,2011, citations,citations,17639,71721,1,,entry citation,,,21690393,,,Structure and function of the complete internal fusion loop from Ebolavirus glycoprotein 2.,published,journal,Proc. Natl. Acad. Sci. U. S. A.,Proceedings of the National Academy of Sciences of the United States of America,,,,,,,,,,,,,,,,,,,,,,,,,,2011, citations,entry_citation,17640,71738,1,,entry citation,,,21606338,,,Structural basis of photosensitivity in a bacterial light-oxygen-voltage/helix-turn-helix (LOV-HTH) DNA-binding protein.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,108,23,,,,,,,,,,,,,,,,,,,,,,9449,9454,2011, citations,entry_citation,17641,71757,1,,entry citation,,,22342930,,,The role of hydration in protein stability: comparison of the cold and heat unfolded states of Yfh1.,published,journal,J. Mol. Biol.,Journal of molecular biology,417,5,,,,,,,,,,,,,,,,,,,,,,413,424,2012, citations,entry_citation,17642,71772,1,,entry citation,,,23931318,,,Structure and Topology of the Huntingtin 1-17 Membrane Anchor by a Combined Solution and Solid-State NMR Approach,published,journal,Biophys. J.,,105,3,,,,,,,,,,,,,,,,,,,,,,699,710,2013, citations,citation_1,17643,71786,1,,entry citation,,,21851109,,,"Blue flickers of hope: secondary structure, dynamics, and putative dimerization interface of the blue-light receptor YtvA from Bacillus subtilis.",published,journal,Biochemistry,Biochemistry,50,38,,,,,,,,,,,,,,,,,,,,,,8163,8171,2011, citations,entry_citation,17644,71804,1,,entry citation,,,23931318,,,Structure and Topology of the Huntingtin 1-17 Membrane Anchor by a Combined Solution and Solid-State NMR Approach,published,journal,Biophys. J.,,105,3,,,,,,,,,,,,,,,,,,,,,,699,710,2013, citations,entry_citation,17645,71818,1,,entry citation,,,22936804,,,Membrane-induced lever arm expansion allows myosin VI to walk with large and variable step sizes.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,42,,,,,,,,,,,,,,,,,,,,,,35021,35035,2012, citations,citation_1,17646,71839,1,,entry citation,,,21700214,,,Anamorsin Is a [2Fe-2S] Cluster-Containing Substrate of the Mia40-Dependent Mitochondrial Protein Trapping Machinery.,published,journal,Chem. Biol.,Chemistry & biology,18,6,,,,,,,,,,,,,,,,,,,,,,794,804,2011, citations,citation,17647,71864,1,,entry citation,,,21925508,,,In vitro evolved non-aggregating and thermostable lipase: structural and thermodynamic investigation.,published,journal,J. Mol. Biol.,Journal of molecular biology,413,3,,,,,,,,,,,,,,,,,,,,,,726,741,2011, citations,entry_citation,17648,71878,1,,entry citation,,,21718702,,,Structured Regions of -Synuclein Fibrils Include the Early-Onset Parkinson's Disease Mutation Sites.,published,journal,J. Mol. Biol.,Journal of molecular biology,411,4,,,,,,,,,,,,,,,,,,,,,,881,895,2011, citations,entry_citation,17649,71893,1,,entry citation,,,21718702,,,Structured Regions of -Synuclein Fibrils Include the Early-Onset Parkinson's Disease Mutation Sites.,published,journal,J. Mol. Biol.,Journal of molecular biology,411,4,,,,,,,,,,,,,,,,,,,,,,881,895,2011, citations,entry_citation,17650,71908,1,,entry citation,,,21845362,,,"(1)H, (13)C, and (15)N resonance assignments and secondary structure prediction of the full-length transition state regulator AbrB from Bacillus anthracis.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,6,1,,,,,,,,,,,,,,,,,,,,,,95,98,2012, citations,entry_citation,17651,71925,1,,entry citation,,,21947914,,,The structure and dynamic properties of the complete histidine phosphotransfer domain of the chemotaxis specific histidine autokinase CheA from Thermotoga maritima.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,51,1-2,,,,,,,,,,,,,,,,,,,,,,49,55,2011, citations,S108C_entry_citation,17652,71941,1,,entry citation,,,22242625,,,"Solution NMR of a 463-residue phosphohexomutase: domain 4 mobility, substates, and phosphoryl transfer defect",published,journal,Biochemistry,,51,3,,,,,,,,,,,,,,,,,,,,,,807,819,2012, citations,entry_citation,17653,71960,1,,entry citation,,,21676866,,,Structure of the 30-kDa Sin3-associated protein (SAP30) in complex with the mammalian Sin3A corepressor and its role in nucleic acid binding.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,286,31,,,,,,,,,,,,,,,,,,,,,,27814,27824,2011, citations,entry_citation,17654,71982,1,,entry citation,,,21718702,,,Structured Regions of -Synuclein Fibrils Include the Early-Onset Parkinson's Disease Mutation Sites.,published,journal,J. Mol. Biol.,Journal of molecular biology,411,4,,,,,,,,,,,,,,,,,,,,,,881,895,2011, citations,entry_citation,17655,71997,1,,entry citation,,,,,,Structure of Human Telomeric DNA in Crowded Solution,in press,journal,J. Am. Chem. Soc.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17656,72013,1,,entry citation,,,21822941,,,"(1)H, (13)C and (15)N NMR assignments of inactive form of P1 endolysin Lyz.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,6,1,,,,,,,,,,,,,,,,,,,,,,87,89,2012, citations,entry_citation,17657,72029,1,,entry citation,,,21612236,,,Design and structure of stapled peptides binding to estrogen receptors.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,133,25,,,,,,,,,,,,,,,,,,,,,,9696,9699,2011, citations,entry_citation,17658,72050,1,,entry citation,,,21612236,,,Design and structure of stapled peptides binding to estrogen receptors.,published,journal,J. Am. Chem. 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NMR Assignments,Biomolecular NMR assignments,6,1,,,,,,,,,,,,,,,,,,,,,,69,73,2012, citations,entry_citation,17661,72124,1,,entry citation,,,21889567,,,"Pharmacological and structural characterization of long-sarafotoxins, a new family of endothelin-like peptides: Role of the C-terminus extension.",published,journal,Biochimie,Biochimie,94,2,,,,,,,,,,,,,,,,,,,,,,461,470,2012, citations,entry_citation,17662,72143,1,,entry citation,,,21889567,,,"Pharmacological and structural characterization of long-sarafotoxins, a new family of endothelin-like peptides: Role of the C-terminus extension.",published,journal,Biochimie,Biochimie,94,2,,,,,,,,,,,,,,,,,,,,,,461,470,2012, citations,entry_citation,17663,72163,1,,entry citation,,,21253573,,,Structural basis for the recognition of cellular mRNA export factor REF by herpes viral proteins HSV-1 ICP27 and HVS ORF57.,published,journal,PLoS Pathog.,PLoS pathogens,7,1,,,,,,,,,,,,,,,,,,,,,,,,2011, citations,entry_citation,17664,72178,1,,entry citation,,,21253573,,,Structural basis for the recognition of cellular mRNA export factor REF by herpes viral proteins HSV-1 ICP27 and HVS ORF57.,published,journal,PLoS Pathog.,PLoS pathogens,7,1,,,,,,,,,,,,,,,,,,,,,,,,2011, citations,citation_1,17665,72192,1,,entry citation,,,22006323,,,A soluble -synuclein construct forms a dynamic tetramer.,published,journal,Proc. 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Biol.,Journal of molecular biology,415,4,,,,,,,,,,,,,,,,,,,,,,680,698,2012, citations,entry_citation,17672,72319,1,,entry citation,,,24521053,,,Structural Characterization of Interactions between the Double-Stranded RNA-Binding Zinc Finger Protein JAZ and Nucleic Acids.,published,journal,Biochemistry,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,citation_1,17673,72336,1,,entry citation,,,22864287,,,PHF20 is an effector protein of p53 double lysine methylation that stabilizes and activates p53,published,journal,Nat. Struct. Mol. Biol.,,19,9,,,,,,,,,,,,,,,,,,,,,,916,924,2012, citations,entry_citation,17674,72356,1,,entry citation,,,22683470,,,Interaction of FGF1 with a novel anti-angiogenic drug SSR128129E.,published,journal,Arch. Biochem. Biophys.,Archives of biochemistry and biophysics,,,,,,,,,,,,,,,,,,,,,,,,,,2012, citations,citation1,17675,72375,1,,entry citation,,,21915914,,,Analysis of electrostatic interactions in the denatured state ensemble of the N-terminal domain of L9 under native conditions.,published,journal,Proteins,Proteins,79,12,,,,,,,,,,,,,,,,,,,,,,3500,3510,2011, citations,citation2,17675,72376,2,,reference citation,,,,,,Structural analysis of the denatured state ensemble of the N-terminal Domain of L9 under native conditions,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,1,17678,72395,1,,entry citation,,,21814767,,,"Assignments of backbone (1)H, (13)C and (15)N resonances in H-Ras (1-166) complexed with GppNHp at physiological pH.",published,journal,Biomol. 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Biochem.,,197,,,,,,,,,,,,,,,,,,,,,,,631,641,1991, citations,entry_citation,17750,73876,1,,entry citation,,,,,,NMR solution structure of N-terminal domain of E3 ligase HECW2,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17751,73900,1,,entry citation,,,,,,Solution structure of Diiron protein in presence of 8 eq Zn2+,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17752,73925,1,,entry citation,,,,,,The WSXWS Motif in Cytokine Receptors Is a Molecular Switch Involved in Receptor Activation: Insight from Structures of the Prolactin Receptor,published,journal,Structure,,20,2,,,,,,,,,,,,,,,,,,,,,,270,282,2012, citations,citations,17753,73948,1,,entry citation,,,,,,"Solution NMR Structure of the Helix-loop-Helix Domain of Human ID3 Protein, Northeast Structural Genomics Consortium Target HR3111A",in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,Citation,17754,73975,1,,entry citation,,,,,,"Solution NMR structure of a MucBP domain (fragment 187-294) of the protein LBA1460 from Lactobacillus acidophilus, Northeast structural genomics consortium target LaR80A",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17755,74006,1,,entry citation,,,21918816,,,"1H, 13C, and 15N resonance assignments for human regenerating family I protein.",published,journal,Biomol. 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Biol.,,401,1,,,,,,,,,,,,,,,,,,,,,,7,12,2010, citations,citation_1,17760,74091,1,,entry citation,,,19755502,10.1093/nar/gkp750,,Biophysical characterizations of human mitochondrial travscription factor A and its binding to tumor suppressor p53,published,journal,Nucleic Acids Res.,,37,20,,,,,,,,,,,,,,,,,,,,,,6765,6783,2009, citations,entry_citation,17761,74105,1,,entry citation,,,21915914,,,Analysis of electrostatic interactions in the denatured state ensemble of the N-terminal domain of L9 under native conditions.,published,journal,Proteins,Proteins,79,12,,,,,,,,,,,,,,,,,,,,,,3500,3510,2011, citations,mbs_refined_structure,17762,74120,1,,entry citation,,,22253705,,,NMR Studies on Structure and Dynamics of the Monomeric Derivative of BS-RNase: New Insights for 3D Domain Swapping.,published,journal,PLoS ONE,PloS one,7,1,,,,,,,,,,,,,,,,,,,,,,,,2012, citations,entry_citation,17763,74139,1,,entry citation,,,22033478,,,Oxidative folding and structural analyses of a Kunitz-related inhibitor and its disulfide intermediates: functional implications.,published,journal,J. 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NMR Assignments,Biomolecular NMR assignments,8,1,,,,,,,,,,,,,,,,,,,,,,97,102,2014, citations,entry_citation,17772,74320,1,,entry citation,,,22130672,,,Solution Structure of RING Finger-like Domain of Retinoblastoma-binding Protein-6 (RBBP6) Suggests It Functions as a U-box.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,10,,,,,,,,,,,,,,,,,,,,,,7146,7158,2012, citations,entry_citation,17773,74341,1,,entry citation,,,22752847,,,"Backbone HN, 13C, and 15N resonance assignments of the tandem RNA-binding domains of human DGCR8.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,2,,,,,,,,,,,,,,,,,,,,,,183,186,2013, citations,citation_1,17774,74366,1,,entry citation,,,22403062,,,Antiparallel -sheet architecture in Iowa-mutant -amyloid fibrils.,published,journal,Proc. Natl. Acad. Sci. 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NMR Assignments,Biomolecular NMR assignments,6,2,,,,,,,,,,,,,,,,,,,,,,153,156,2012, citations,citations,17805,74848,1,,entry citation,,,,,,The High Resolution Structure of Ubiquitin Like Dom Ublcp1,in preparation,journal,To be Published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17806,74872,1,,entry citation,,,,,,NMR structure of the calcium-bound form of the protein YP_001302112.1 from Parabacteroides distasonis,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17807,74892,1,,entry citation,,,22711531,,,Structural Insights into Calmodulin-regulated L-selectin Ectodomain Shedding.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,32,,,,,,,,,,,,,,,,,,,,,,26513,26527,2012, citations,entry_citation,17808,74921,1,,entry citation,,,21808299,,,Structural basis for site-specific reading of unmodified R2 of histone H3 tail by UHRF1 PHD finger.,published,journal,Cell Res.,Cell research,21,9,,,,,,,,,,,,,,,,,,,,,,1379,1382,2011, citations,AHSA1-like_protein_AHA_2358_from_Aeromonas_hydrophila,17809,74938,1,,entry citation,,,,,,"Solution NMR structure of the AHSA1-like protein AHA_2358 from Aeromonas hydrophila refined with NH RDCs. Northeast Structural Genomics Consortium Target AhR99.",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1781,74990,1,,entry citation,,,,,"Moench, Susan J., Shi, Ting-Mei, Satterlee, James D., ""Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c,"" Eur. J. 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Am. Chem. Soc.,Journal of the American Chemical Society,133,43,,,,,,,,,,,,,,,,,,,,,,17434,17443,2011, citations,entry_citation,17818,75155,1,,entry citation,,,24293257,,,Solution structure of a putative FKBP-type peptidyl-propyl cis-trans isomerase from Giardia lamblia.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,57,4,,,,,,,,,,,,,,,,,,,,,,369,374,2013, citations,entry_citation,17819,75175,1,,entry citation,,,21365684,,,"Structure, dynamics, and Hck interaction of full-length HIV-1 Nef.",published,journal,Proteins,Proteins,79,5,,,,,,,,,,,,,,,,,,,,,,1609,1622,2011, citations,entry_citation,17820,75192,1,,entry citation,,,22101872,,,"Backbone 1H, 13C and 15N resonance assignments of the 39 kDa staphylococcal hemoglobin receptor IsdH.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,6,2,,,,,,,,,,,,,,,,,,,,,,169,172,2012, citations,Article,17821,75209,1,,entry citation,,,21816817,,,Functional role of two interhelical disulfide bonds in human Cox17 protein from a structural perspective.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,286,39,,,,,,,,,,,,,,,,,,,,,,34382,34390,2011, citations,entry_citation,17822,75230,1,,entry citation,,,22383581,,,Selectivity of stop codon recognition in translation termination is modulated by multiple conformations of GTS loop in eRF1,published,journal,Nucleic Acids Res.,,40,12,,,,,,,,,,,,,,,,,,,,,,5751,5765,2012, citations,entry_citation,17823,75244,1,,entry citation,,,24443564,,,Three-dimensional NMR Structure of Hen Egg Gallin (Chicken Ovodefensin) Reveals a New Variation of the -Defensin Fold.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,289,10,,,,,,,,,,,,,,,,,,,,,,7211,7220,2014, citations,entry_citation,17824,75262,1,,entry citation,,,22433864,,,Selective recruitment of an E2~ubiquitin complex by an E3 ubiquitin ligase.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,21,,,,,,,,,,,,,,,,,,,,,,17374,17385,2012, citations,entry_citation,17825,75287,1,,entry citation,,,22219199,,,The C-terminal helices of heat shock protein 70 are essential for J-domain binding and ATPase activation.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,8,,,,,,,,,,,,,,,,,,,,,,6044,6052,2012, citations,entry_citation,17826,75305,1,,entry citation,,,21898049,,,"1H, 13C, and 15N backbone and side-chain chemical shift assignments for the 31 kDa human galectin-7 (p53-induced gene 1) homodimer, a pro-apoptotic lectin.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,6,2,,,,,,,,,,,,,,,,,,,,,,127,129,2012, citations,entry_citation,17827,75323,1,,entry citation,,,22078565,,,Membrane Binding of the N-Terminal Ubiquitin-Like Domain of kindlin-2 Is Crucial for Its Regulation of Integrin Activation,published,journal,Structure,,19,11,,,,,,,,,,,,,,,,,,,,,,1664,1671,2011, citations,entry_citation,17828,75347,1,,entry citation,,,22517668,,,Solution structure of the E3 ligase HOIL-1 Ubl domain.,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,21,7,,,,,,,,,,,,,,,,,,,,,,1085,1092,2012, citations,C2_Domain_citation,17829,75370,1,,entry citation,,,22392338,,,Backbone resonance assignments of the C2 domain of coagulation factor VIII.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,1,,,,,,,,,,,,,,,,,,,,,,31,34,2013, citations,citations,17857,75902,1,,entry citation,,,,,,Chemical Shift Assignments and solution structure of human apo-S100A1 E32Q mutant,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1783,75384,1,,entry citation,,,,,"Moench, Susan J., Shi, Ting-Mei, Satterlee, James D., ""Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c,"" Eur. J. Biochem. 197, 631-641 (1991).","Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c",published,journal,Eur. J. Biochem.,,197,,,,,,,,,,,,,,,,,,,,,,,631,641,1991, citations,JBC_paper,17830,75399,1,,entry citation,,,21543317,,,Oxidation state-dependent protein-protein interactions in disulfide cascades.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,286,28,,,,,,,,,,,,,,,,,,,,,,24943,24956,2011, citations,entry_citation,17831,75416,1,,entry citation,,,21543317,,,Oxidation state-dependent protein-protein interactions in disulfide cascades.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,286,28,,,,,,,,,,,,,,,,,,,,,,24943,24956,2011, citations,citations,17832,75433,1,,entry citation,,,22307274,,,Structural basis for recognition of H3K56-acetylated histone H3-H4 by the chaperone Rtt106,published,journal,Nature,,483,7387,,,,,,,,,,,,,,,,,,,,,,104,107,2012, citations,Citation_1,17833,75449,1,,entry citation,,,,,,"Characterisation of a putative receptor binding surface on Skint-1, a critical determinant of dendritic epidermal T cell selection",in preparation,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,2016, citations,entry_citation,17834,75463,1,,entry citation,,,21848803,,,The Prion Protein Binds Thiamine,published,journal,FEBS J.,The FEBS journal,278,21,,,,,,,,,,,,,,,,,,,,,,4002,4014,2011, citations,entry_citation,17835,75485,1,,entry citation,,,22481467,,,"(1)H, (15)N and (13)C resonance assignments for the three LOTUS RNA binding domains of Tudor domain-containing protein TDRD7.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,1,,,,,,,,,,,,,,,,,,,,,,79,83,2013, citations,entry_citation,17836,75503,1,,entry citation,,,22203963,,,Disordered form of the scaffold protein IscU is the substrate for iron-sulfur cluster assembly on cysteine desulfurase,published,journal,Proc. Natl. Acad. Sci. U. S. A.,,109,2,,,,,,,,,,,,,,,,,,,,,,454,459,2012, citations,entry_citation,17837,75520,1,,entry citation,,,22203963,,,Disordered form of the scaffold protein IscU is the substrate for iron-sulfur cluster assembly on cysteine desulfurase,published,journal,Proc. Natl. Acad. Sci. U. S. A.,,109,2,,,,,,,,,,,,,,,,,,,,,,454,459,2012, citations,entry_citation,17838,75537,1,,entry citation,,,22475172,,,Molecular level interaction of inositol hexaphosphate with the C2B domain of human synaptotagmin I.,published,journal,Biochemistry,Biochemistry,51,17,,,,,,,,,,,,,,,,,,,,,,3675,3683,2012, citations,entry_citation,17839,75555,1,,entry citation,,,22325777,,,Mutational tipping points for switching protein folds and functions,published,journal,Structure,,20,2,,,,,,,,,,,,,,,,,,,,,,283,291,2012, citations,entry_citation,17840,75577,1,,entry citation,,,22325777,,,Mutational tipping points for switching protein folds and functions,published,journal,Structure,,20,2,,,,,,,,,,,,,,,,,,,,,,283,291,2012, citations,entry_citation,17841,75600,1,,entry citation,,,22325777,,,Mutational tipping points for switching protein folds and functions,published,journal,Structure,,20,2,,,,,,,,,,,,,,,,,,,,,,283,291,2012, citations,entry_citation,17842,75622,1,,entry citation,,,21865172,,,Structural basis for the interaction of lipopolysaccharide with outer membrane protein H (OprH) from Pseudomonas aeruginosa.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,286,45,,,,,,,,,,,,,,,,,,,,,,39211,39223,2011, citations,entry_citation,17843,75637,1,,entry citation,,,22325777,,,Mutational tipping points for switching protein folds and functions,published,journal,Structure,,20,2,,,,,,,,,,,,,,,,,,,,,,283,291,2012, citations,entry_citation,17844,75651,1,,entry citation,,,22203963,,,Disordered form of the scaffold protein IscU is the substrate for iron-sulfur cluster assembly on cysteine desulfurase,published,journal,Proc. Natl. Acad. Sci. U. S. A.,,109,2,,,,,,,,,,,,,,,,,,,,,,454,459,2012, citations,entry_citation,17845,75668,1,,entry citation,,,22318343,,,Redox-dependent conformational changes in eukaryotic cytochromes revealed by paramagnetic NMR spectroscopy,published,journal,J. Biomol. NMR,,52,3,,,,,,,,,,,,,,,,,,,,,,245,256,2012, citations,entry_citation,17846,75689,1,,entry citation,,,22318343,,,Redox-dependent conformational changes in eukaryotic cytochromes revealed by paramagnetic NMR spectroscopy,published,journal,J. Biomol. NMR,,52,3,,,,,,,,,,,,,,,,,,,,,,245,256,2012, citations,entry_citation,17847,75710,1,,entry citation,,,22318343,,,Redox-dependent conformational changes in eukaryotic cytochromes revealed by paramagnetic NMR spectroscopy,published,journal,J. Biomol. NMR,,52,3,,,,,,,,,,,,,,,,,,,,,,245,256,2012, citations,entry_citation,17848,75731,1,,entry citation,,,22318343,,,Redox-dependent conformational changes in eukaryotic cytochromes revealed by paramagnetic NMR spectroscopy,published,journal,J. Biomol. NMR,,52,3,,,,,,,,,,,,,,,,,,,,,,245,256,2012, citations,entry_citation,17849,75752,1,,entry citation,,,22280008,,,Solution structures of yeast Saccharomyces cerevisiae calmodulin in calcium- and target peptide-bound states reveal similarities and differences to vertebrate calmodulin.,published,journal,Genes Cells,Genes to cells : devoted to molecular & cellular mechanisms,17,3,,,,,,,,,,,,,,,,,,,,,,159,172,2012, citations,entry_citation,1785,75773,1,,entry citation,,,,,"Moench, Susan J., Shi, Ting-Mei, Satterlee, James D., ""Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c,"" Eur. J. Biochem. 197, 631-641 (1991).","Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c",published,journal,Eur. J. Biochem.,,197,,,,,,,,,,,,,,,,,,,,,,,631,641,1991, citations,entry_citation,17850,75788,1,,entry citation,,,22280008,,,Solution structures of yeast Saccharomyces cerevisiae calmodulin in calcium- and target peptide-bound states reveal similarities and differences to vertebrate calmodulin.,published,journal,Genes Cells,Genes to cells : devoted to molecular & cellular mechanisms,17,3,,,,,,,,,,,,,,,,,,,,,,159,172,2012, citations,entry_citation,17851,75811,1,,entry citation,,,22505741,,,Near attack conformers dominate beta-phosphoglucomutase complexes where geometry and charge distribution reflect those of substrate.,published,journal,Proc. Natl. Acad. Sci. U. S. A.,Proceedings of the National Academy of Sciences of the United States of America,109,18,,,,,,,,,,,,,,,,,,,,,,6910,6915,2012, citations,entry_citation,17852,75832,1,,entry citation,,,22505741,,,Near attack conformers dominate beta-phosphoglucomutase complexes where geometry and charge distribution reflect those of substrate,published,journal,Proc. Natl. Acad. Sci. U. S. A.,Proceedings of the National Academy of Sciences of the United States of America,109,18,,,,,,,,,,,,,,,,,,,,,,6910,6915,2012, citations,entry_citation,17853,75855,1,,entry citation,,,22205447,,,"Backbone and side chain 1H, 13C and 15N resonance assignments of the catalytic domain of diphtheria toxin.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,6,2,,,,,,,,,,,,,,,,,,,,,,189,192,2012, citations,entry_citation,17858,75932,1,,entry citation,,,22560733,,,Structural Basis for Polyadenosine-RNA Binding by Nab2 Zn Fingers and Its Function in mRNA Nuclear Export.,published,journal,Structure,"Structure (London, England : 1993)",20,6,,,,,,,,,,,,,,,,,,,,,,1007,1018,2012, citations,citation_1,17859,75952,1,,entry citation,,,20859962,10.1002/chem.201000959,,"Solution Structure, Mechanism of Replication, and Optimization of an Unnatural Base Pair",published,journal,Chem. Eur. J.,,16,42,,,,,,,,,,,,,,,,,,,,,,12650,12659,2010, citations,entry_citation,17860,75970,1,,entry citation,,,22961937,,,NMR Studies of HAR1 RNA Secondary Structures Reveal Conformational Dynamics in the Human RNA,published,journal,Chembiochem,,13,14,,,,,,,,,,,,,,,,,,,,,,2100,2112,2012, citations,entry_citation,17861,75996,1,,entry citation,,,22961937,,,NMR studies of HAR1 RNA secondary structures reveal conformational dynamics in the human RNA.,published,journal,Chembiochem,Chembiochem : a European journal of chemical biology,13,14,,,,,,,,,,,,,,,,,,,,,,2100,2112,2012, citations,entry_citation,17862,76018,1,,entry citation,,,21917915,,,"Structural basis for hemoglobin capture by Staphylococcus aureus cell-surface protein, IsdH.",published,journal,J. Biol. Chem.,The Journal of biological chemistry,286,44,,,,,,,,,,,,,,,,,,,,,,38439,38447,2011, citations,entry_citation,17863,76044,1,,entry citation,,,22108166,,,Structural Studies of Mycobacterium tuberculosis Rv0899 Reveal a Monomeric Membrane-Anchoring Protein with Two Separate Domains.,published,journal,J. Mol. Biol.,Journal of molecular biology,415,2,,,,,,,,,,,,,,,,,,,,,,382,392,2012, citations,FAIM-CTD_polypeptide,17864,76061,1,,entry citation,,,,,,"1H, 13C and 15N Assigned Chemical Shifts for human FAIM CTD",submitted,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17865,76075,1,,entry citation,,,22771296,,,"Structure, dynamics and domain organization of the repeat protein Cin1 from the apple scab fungus.",published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1824,10,,,,,,,,,,,,,,,,,,,,,,1118,1128,2012, citations,entry_citation,17866,76099,1,,entry citation,,,22311340,,,"1H, 13C and 15N backbone and side chain resonance assignments of human halo S100A1.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,6,2,,,,,,,,,,,,,,,,,,,,,,213,215,2012, citations,entry_citation,17867,76114,1,,entry citation,,,22235120,,,Structural Insight into Unique Cardiac Myosin-binding Protein-C Motif: A PARTIALLY FOLDED DOMAIN.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,11,,,,,,,,,,,,,,,,,,,,,,8254,8262,2012, citations,entry_citation,17868,76131,1,,entry citation,,,22444368,,,Deciphering structural elements of mucin glycoprotein recognition.,published,journal,ACS Chem. Biol.,ACS chemical biology,7,6,,,,,,,,,,,,,,,,,,,,,,1031,1039,2012, citations,entry_citation,17869,76150,1,,entry citation,,,22444368,,,Deciphering structural elements of mucin glycoprotein recognition.,published,journal,ACS Chem. Biol.,ACS chemical biology,7,6,,,,,,,,,,,,,,,,,,,,,,1031,1039,2012, citations,entry_citation,1787,76171,1,,entry citation,,,,,"Moench, Susan J., Shi, Ting-Mei, Satterlee, James D., ""Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c,"" Eur. J. Biochem. 197, 631-641 (1991).","Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c",published,journal,Eur. J. Biochem.,,197,,,,,,,,,,,,,,,,,,,,,,,631,641,1991, citations,entry_citation,17870,76186,1,,entry citation,,,22444368,,,Deciphering structural elements of mucin glycoprotein recognition.,published,journal,ACS Chem. Biol.,ACS chemical biology,7,6,,,,,,,,,,,,,,,,,,,,,,1031,1039,2012, citations,entry_citation,17871,76207,1,,entry citation,,,22444368,,,Deciphering structural elements of mucin glycoprotein recognition.,published,journal,ACS Chem. Biol.,ACS chemical biology,7,6,,,,,,,,,,,,,,,,,,,,,,1031,1039,2012, citations,entry_citation,17872,76228,1,,entry citation,,,22444368,,,Deciphering structural elements of mucin glycoprotein recognition.,published,journal,ACS Chem. Biol.,ACS chemical biology,7,6,,,,,,,,,,,,,,,,,,,,,,1031,1039,2012, citations,entry_citation,17873,76249,1,,entry citation,,,22444368,,,Deciphering structural elements of mucin glycoprotein recognition.,published,journal,ACS Chem. Biol.,ACS chemical biology,7,6,,,,,,,,,,,,,,,,,,,,,,1031,1039,2012, citations,entry_citation,17874,76270,1,,entry citation,,,22444368,,,Deciphering structural elements of mucin glycoprotein recognition.,published,journal,ACS Chem. Biol.,ACS chemical biology,7,6,,,,,,,,,,,,,,,,,,,,,,1031,1039,2012, citations,entry_citation,17875,76291,1,,entry citation,,,22444368,,,Deciphering structural elements of mucin glycoprotein recognition.,published,journal,ACS Chem. Biol.,ACS chemical biology,7,6,,,,,,,,,,,,,,,,,,,,,,1031,1039,2012, citations,citations,17876,76312,1,,entry citation,,,22238341,,,New tricks of an old pattern: structural versatility of scorpion toxins with common cysteine spacing.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,,,,,,,,,,,,,,,,,,,,,,,,,,2012, citations,entry_citation,17877,76332,1,,entry citation,,,22976989,,,Unusually high-affinity Mg(2+) binding at the AU-rich sequence within the antiterminator hairpin of a Mg(2+) riboswitch.,published,journal,Chem. Biodivers.,Chemistry & biodiversity,9,9,,,,,,,,,,,,,,,,,,,,,,2035,2049,2012, citations,entry_citation,17878,76354,1,,entry citation,,,22009680,,,Analysis of the interaction with the hepatitis C virus mRNA reveals an alternative mode of RNA recognition by the human La protein.,published,journal,Nucleic Acids Res.,Nucleic acids research,40,3,,,,,,,,,,,,,,,,,,,,,,1381,1394,2012, citations,entry_citation,17879,76370,1,,entry citation,,,22055191,,,"Structural basis of Atg8 activation and transfer to Atg3 by a homodimeric E1, Atg7",published,journal,Mol. Cell,,44,3,,,,,,,,,,,,,,,,,,,,,,462,475,2011, citations,entry_citation,17880,76393,1,,entry citation,,,22488857,,,Solution structure of SWI1 AT-rich interaction domain from Saccharomyces cerevisiae and its nonspecific binding to DNA.,published,journal,Proteins,Proteins,80,7,,,,,,,,,,,,,,,,,,,,,,1911,1917,2012, citations,citation,17881,76407,1,,entry citation,,,20973509,,,Intrinsic disorder of PEP-19 confers unique dynamic properties to apo and calcium calmodulin,published,journal,Biochemistry,,49,48,,,,,,,,,,,,,,,,,,,,,,10287,10297,2010, citations,citations,17882,76424,1,,entry citation,,,22251893,,,"Solution structure of native and recombinant expressed toxin CssII from the venom of the scorpion Centruroides suffusus suffusus, and their effects on Nav1.5 Sodium channels",published,journal,Biochim. Biophys. Acta.,,1824,3,,,,,,,,,,,,,,,,,,,,,,478,487,2012, citations,citations,17883,76440,1,,entry citation,,,22157959,,,Structural basis of pre-let-7 miRNA recognition by the zinc knuckles of pluripotency factor Lin28.,published,journal,Nat. Struct. Mol. Biol.,Nature structural & molecular biology,19,1,,,,,,,,,,,,,,,,,,,,,,84,89,2012, citations,entry_citation_1,17884,76467,1,,entry citation,,,22225807,,,NMR solution structure of rat a(1-16): toward understanding the mechanism of rats' resistance to Alzheimer's disease.,published,journal,Biophys. J.,Biophysical journal,102,1,,,,,,,,,,,,,,,,,,,,,,136,143,2012, citations,entry_citation_2,17884,76468,2,,reference citation,,,21290829,,,"Optimization of the Methods for Small Peptide Solution Structure Determination by NMR Spectroscopy",published,journal,Mol. Biol. 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Biol.,Journal of molecular biology,416,3,,,,,,,,,,,,,,,,,,,,,,425,437,2012, citations,entry_citation,17888,76550,1,,entry citation,,,22573762,,,A vitellogenin polyserine cleavage site: highly disordered conformation protected from proteolysis by phosphorylation,published,journal,J. Exp. Biol.,,215,11,,,,,,,,,,,,,,,,,,,,,,1837,1846,2012, citations,entry_citation,17889,76566,1,,entry citation,,,22573762,,,A vitellogenin polyserine cleavage site: highly disordered conformation protected from proteolysis by phosphorylation.,published,journal,J. Exp. Biol.,The Journal of experimental biology,215,11,,,,,,,,,,,,,,,,,,,,,,1837,1846,2012, citations,entry_citation,1789,76580,1,,entry citation,,,,,"Moench, Susan J., Shi, Ting-Mei, Satterlee, James D., ""Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c,"" Eur. J. Biochem. 197, 631-641 (1991).","Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c",published,journal,Eur. J. Biochem.,,197,,,,,,,,,,,,,,,,,,,,,,,631,641,1991, citations,entry_citation,17890,76595,1,,entry citation,,,22615566,,,Plasticity of the beta-Trefoil Protein Fold in the Recognition and Control of Invertebrate Predators and Parasites by a Fungal Defence System,published,journal,PLoS Pathog.,,8,5,,,,,,,,,,,,,,,,,,,,,,e1002706,e1002706,2012, citations,entry_citation,17891,76617,1,,entry citation,,,22593157,,,Structural analysis of hepatitis C virus core-e1 signal Peptide and requirements for cleavage of the genotype 3a signal sequence by signal Peptide peptidase.,published,journal,J. Virol.,Journal of virology,86,15,,,,,,,,,,,,,,,,,,,,,,7818,7828,2012, citations,entry_citation,17892,76635,1,,entry citation,,,23396077,,,Cold denaturation of a protein dimer monitored at atomic resolution.,published,journal,Nat. Chem. Biol.,Nature chemical biology,9,4,,,,,,,,,,,,,,,,,,,,,,264,270,2013, citations,entry_citation,17893,76652,1,,entry citation,,,23396077,,,Cold denaturation of a protein dimer monitored at atomic resolution.,published,journal,Nat. Chem. Biol.,Nature chemical biology,9,4,,,,,,,,,,,,,,,,,,,,,,264,270,2013, citations,entry_citation,17894,76669,1,,entry citation,,,23396077,,,Cold denaturation of a protein dimer monitored at atomic resolution.,published,journal,Nat. Chem. Biol.,Nature chemical biology,9,4,,,,,,,,,,,,,,,,,,,,,,264,270,2013, citations,entry_citation,17895,76686,1,,entry citation,,,23396077,,,Cold denaturation of a protein dimer monitored at atomic resolution.,published,journal,Nat. Chem. Biol.,Nature chemical biology,9,4,,,,,,,,,,,,,,,,,,,,,,264,270,2013, citations,entry_citation,17896,76703,1,,entry citation,,,23396077,,,Cold denaturation of a protein dimer monitored at atomic resolution.,published,journal,Nat. Chem. Biol.,Nature chemical biology,9,4,,,,,,,,,,,,,,,,,,,,,,264,270,2013, citations,entry_citation,17897,76720,1,,entry citation,,,23396077,,,Cold denaturation of a protein dimer monitored at atomic resolution.,published,journal,Nat. Chem. Biol.,Nature chemical biology,9,4,,,,,,,,,,,,,,,,,,,,,,264,270,2013, citations,entry_citation,17898,76737,1,,entry citation,,,23396077,,,Cold denaturation of a protein dimer monitored at atomic resolution.,published,journal,Nat. Chem. Biol.,Nature chemical biology,9,4,,,,,,,,,,,,,,,,,,,,,,264,270,2013, citations,entry_citation,17899,76754,1,,entry citation,,,21989955,,,"1H, 13C and 15N NMR assignments of the aciniform spidroin (AcSp1) repetitive domain of Argiope trifasciata wrapping silk.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,6,2,,,,,,,,,,,,,,,,,,,,,,147,151,2012, citations,citations,17900,76782,1,,entry citation,,,,,,Northeast Structural Genomics Consortium Target BfR322,in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,17901,76807,1,,entry citation,,,,,,"Partial 1H, 13C, 15N Chemical Shift Assignments for the U6 Spliceosomal snRNA 5' Stem-Loop 30-mer Construct.",in preparation,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17902,76823,1,,entry citation,,,22615566,,,Plasticity of the beta-Trefoil Protein Fold in the Recognition and Control of Invertebrate Predators and Parasites by a Fungal Defence System,published,journal,PLoS Pathog.,,8,5,,,,,,,,,,,,,,,,,,,,,,e1002706,e1002706,2012, citations,entry_citation,17903,76852,1,,entry citation,,,22087268,,,Conformational toggling of Yeast Iso-1-cytochrome c in the oxidized and reduced states,published,journal,PLoS One,,6,11,,,,,,,,,,,,,,,,,,,,,,e27219,,2011, citations,entry_citation,17904,76871,1,,entry citation,,,22087268,,,Conformational toggling of Yeast Iso-1-cytochrome c in the oxidized and reduced states,published,journal,PLoS One,,6,11,,,,,,,,,,,,,,,,,,,,,,e27219,,2011, citations,citation_1,17905,76890,1,,entry citation,,,22105307,,,"1H, 13C and 15N resonance assignment of the anticodon binding domain of human lysyl aminoacyl tRNA synthetase.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,6,2,,,,,,,,,,,,,,,,,,,,,,173,176,2012, citations,citations,17906,76907,1,,entry citation,,,22103656,,,Characterization of molecular interactions between ACP and halogenase domains in the Curacin A polyketide synthase.,published,journal,ACS Chem. Biol.,ACS chemical biology,7,2,,,,,,,,,,,,,,,,,,,,,,378,386,2012, citations,citations,17907,76926,1,,entry citation,,,22103656,,,Characterization of molecular interactions between ACP and halogenase domains in the Curacin A polyketide synthase.,published,journal,ACS Chem. Biol.,ACS chemical biology,7,2,,,,,,,,,,,,,,,,,,,,,,378,386,2012, citations,citations,17908,76952,1,,entry citation,,,22511981,,,Structural and functional diversity of acidic scorpion potassium channel toxins,published,journal,PLoS One,,7,4,,,,,,,,,,,,,,,,,,,,,,e35154,e35154,2012, citations,entry_citation,17909,76967,1,,entry citation,,,22392336,,,"(1)H, (13)C, and (15)N backbone chemical shift assignments of StAR-related lipid transfer domain protein 5 (STARD5).",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,1,,,,,,,,,,,,,,,,,,,,,,21,24,2013, citations,entry_citation,1791,76982,1,,entry citation,,,,,"Moench, Susan J., Shi, Ting-Mei, Satterlee, James D., ""Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c,"" Eur. J. Biochem. 197, 631-641 (1991).","Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c",published,journal,Eur. J. Biochem.,,197,,,,,,,,,,,,,,,,,,,,,,,631,641,1991, citations,entry_citation,17939,77503,1,,entry citation,,,,,,structure of a protein from Haloferax volcanii,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17910,76997,1,,entry citation,,,22352310,,,Structural intermediates during -synuclein fibrillogenesis on phospholipid vesicles.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,134,11,,,,,,,,,,,,,,,,,,,,,,5090,5099,2012, citations,entry_citation,17911,77013,1,,entry citation,,,,,,NMR solution structure of C-terminal domain of SARS-CoV main protease in 2.5M urea,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17912,77033,1,,entry citation,,,23892081,,,Structural basis for recognition of the third SH3 domain of full-length R85 (R85FL)/ponsin by ataxin-7.,published,journal,FEBS Lett.,FEBS letters,587,18,,,,,,,,,,,,,,,,,,,,,,2905,2911,2013, citations,entry_citation,17913,77047,1,,entry citation,,,23892081,,,Structural basis for recognition of the third SH3 domain of full-length R85 (R85FL)/ponsin by ataxin-7.,published,journal,FEBS Lett.,FEBS letters,587,18,,,,,,,,,,,,,,,,,,,,,,2905,2911,2013, citations,entry_citation,17914,77061,1,,entry citation,,,22217388,,,Structure determination of a membrane protein in proteoliposomes.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,134,4,,,,,,,,,,,,,,,,,,,,,,2047,2056,2012, citations,entry_citation,17915,77079,1,,entry citation,,,22508472,,,"Facile backbone (1H, 15N, 13Ca, and 13C') assignment of 13C/15N-labeled proteins using orthogonal projection planes of HNN and HN(C)N experiments and its automation.",published,journal,Magn. Reson. Chem.,Magnetic resonance in chemistry : MRC,50,5,,,,,,,,,,,,,,,,,,,,,,357,363,2012, citations,entry_citation,17916,77095,1,,entry citation,,,22095626,,,Structural and binding studies of the C-terminal domains of yeast TFIIF subunits Tfg1 and Tfg2.,published,journal,Proteins,Proteins,,,,,,,,,,,,,,,,,,,,,,,,,,2011, citations,entry_citation,17917,77111,1,,entry citation,,,22095626,,,Structural and binding studies of the C-terminal domains of yeast TFIIF subunits Tfg1 and Tfg2.,published,journal,Proteins,Proteins,,,,,,,,,,,,,,,,,,,,,,,,,,2011, citations,citations,17918,77127,1,,entry citation,,,22900083,,,Solution Structural Analysis of the Single-Domain Parvulin TbPin1,published,journal,PLoS One,,7,8,,,,,,,,,,,,,,,,,,,,,,e43017,e43017,2012, citations,entry_citation,17919,77141,1,,entry citation,,,22729708,,,Determination of structural fluctuations of proteins from structure-based calculations of residual dipolar couplings.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,53,4,,,,,,,,,,,,,,,,,,,,,,281,292,2012, citations,PHF-tau,17920,77155,1,,entry citation,,,21990182,,,The dynamic structure of filamentous tau.,published,journal,Angew. Chem. Int. Ed. Engl.,Angewandte Chemie (International ed. in English),50,48,,,,,,,,,,,,,,,,,,,,,,11520,11524,2011, citations,entry_citation,17921,77169,1,,entry citation,,,,,,"Partial 1H, 15N Chemical Shift Assignments of a GAAA Tetraloop Receptor Variant.",in preparation,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17922,77187,1,,entry citation,,,21365684,,,"Structure, dynamics, and Hck interaction of full-length HIV-1 Nef.",published,journal,Proteins,Proteins,79,5,,,,,,,,,,,,,,,,,,,,,,1609,1622,2011, citations,Citation_1,17923,77205,1,,entry citation,,,,,,Solution structure of defensin Lc-def from germinated lentil (Lens Culinaris) seeds,in preparation,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,SEVI_no_Zn,17924,77222,1,,entry citation,,,22907203,,,Inhibition of semen-derived enhancer of virus infection (SEVI) fibrillogenesis by zinc and copper.,published,journal,Eur. Biophys. J.,European biophysics journal : EBJ,41,9,,,,,,,,,,,,,,,,,,,,,,695,704,2012, citations,entry_citation,17925,77238,1,,entry citation,,,22907203,,,Inhibition of semen-derived enhancer of virus infection (SEVI) fibrillogenesis by zinc and copper.,published,journal,Eur. Biophys. J.,European biophysics journal : EBJ,41,9,,,,,,,,,,,,,,,,,,,,,,695,704,2012, citations,citations,17926,77256,1,,entry citation,,,22514274,,,Conformational selection and folding-upon-binding of the intrinsically disordered protein CP12 regulate photosynthetic enzymes assembly,published,journal,J. Biol. Chem.,,287,25,,,,,,,,,,,,,,,,,,,,,,21372,21383,2012, citations,citations,17927,77280,1,,entry citation,,,,,,Solution Structure of a putative thiol-disulfide oxidoreductase from Bacteroides vulgatus,in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17928,77300,1,,entry citation,,,22078564,,,Structural investigation of rimantadine inhibition of the AM2-BM2 chimera channel of influenza viruses,published,journal,Structure,,19,11,,,,,,,,,,,,,,,,,,,,,,1655,1663,2011, citations,entry_citation,17929,77323,1,,entry citation,,,22078564,,,Structural investigation of rimantadine inhibition of the AM2-BM2 chimera channel of influenza viruses,published,journal,Structure,,19,11,,,,,,,,,,,,,,,,,,,,,,1655,1663,2011, citations,entry_citation,1793,77347,1,,entry citation,,,,,"Moench, Susan J., Shi, Ting-Mei, Satterlee, James D., ""Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c,"" Eur. J. Biochem. 197, 631-641 (1991).","Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c",published,journal,Eur. J. Biochem.,,197,,,,,,,,,,,,,,,,,,,,,,,631,641,1991, citations,entry_citation,17930,77362,1,,entry citation,,,21956114,,,Tyrosine phosphorylation as a conformational switch: a case study of integrin 3 cytoplasmic tail.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,286,47,,,,,,,,,,,,,,,,,,,,,,40943,40953,2011, citations,entry_citation,17931,77380,1,,entry citation,,,21956114,,,Tyrosine phosphorylation as a conformational switch: a case study of integrin 3 cytoplasmic tail.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,286,47,,,,,,,,,,,,,,,,,,,,,,40943,40953,2011, citations,entry_citation,17932,77399,1,,entry citation,,,21956114,,,Tyrosine phosphorylation as a conformational switch: a case study of integrin 3 cytoplasmic tail.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,286,47,,,,,,,,,,,,,,,,,,,,,,40943,40953,2011, citations,entry_citation,17934,77417,1,,entry citation,,,23799029,,,Solution structure and peptide binding of the PTB domain from the AIDA1 postsynaptic signaling scaffolding protein.,published,journal,PLoS ONE,PloS one,8,6,,,,,,,,,,,,,,,,,,,,,,e65605,e65605,2013, citations,entry_citation,17935,77432,1,,entry citation,,,22203461,,,"1H, 13C, 15N assignment and secondary structure determination of glutamine amido transferase subunit of gaunosine monophosphate synthetase from Methanocaldococcus jannaschii.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,6,2,,,,,,,,,,,,,,,,,,,,,,193,196,2012, citations,entry_citation,17936,77448,1,,entry citation,,,22210494,,,Solution structure of the N-terminal dsRBD of Drosophila ADAR and interaction studies with RNA.,published,journal,Biochimie,Biochimie,94,7,,,,,,,,,,,,,,,,,,,,,,1499,1509,2012, citations,entry_citation,17937,77469,1,,entry citation,,,19580321,10.1021/ja902003u,,Solid-State and Solution NMR Studies of the CAP-Gly Domain of Mammalian Dynactin and Its Interaction with Microtubules,published,journal,J. Am. Chem. Soc.,,131,,,,,,,,,,,,,,,,,,,,,,,10113,10126,2009, citations,entry_citation,17938,77487,1,,entry citation,,,19580321,,,"Solid-State and Solution NMR Studies of the CAP-Gly Domain of Mammalian Dynactin and Its Interaction with Microtubules",published,journal,J. Am. Chem. Soc.,,131,,,,,,,,,,,,,,,,,,,,,,,10113,10126,2009, citations,entry_citation,17940,77520,1,,entry citation,,,22012687,,,NMR spectroscopic investigations of the activated p38 mitogen-activated protein kinase.,published,journal,Chembiochem,Chembiochem : a European journal of chemical biology,12,17,,,,,,,,,,,,,,,,,,,,,,2599,2607,2011, citations,entry_citation,17941,77535,1,,entry citation,,,,,,The Structure of Subdomain IV-B from the CVB-3 IRES,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17942,77557,1,,entry citation,,,22392342,,,NMR assignment of a PDZ domain in complex with a HPV51 E6 derived N-terminally pyroglutamic acid modified peptide.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,1,,,,,,,,,,,,,,,,,,,,,,47,49,2013, citations,CGC-19_citation,17943,77578,1,,entry citation,,,22419055,,,"(1)H, (13)C and (15)N NMR assignment of CGC-19, a single domain proteic constituent of a non ribosomal peptide synthetase.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,1,,,,,,,,,,,,,,,,,,,,,,1,4,2013, citations,entry_citation,17944,77595,1,,entry citation,,,15600367,,,Magic angle spinning solid-state NMR spectroscopy for structural studies of protein interfaces. resonance assignments of differentially enriched Escherichia coli thioredoxin reassembled by fragment complementation.,published,journal,J. Am. Chem. Soc.,,126,50,,,,,,,,,,,,,,,,,,,,,,16608,16620,2004, citations,entry_citation,17945,77610,1,,entry citation,,,22072628,,,Structural characterization by nuclear magnetic resonance of the impact of phosphorylation in the proline-rich region of the disordered Tau protein.,published,journal,Proteins,Proteins,80,2,,,,,,,,,,,,,,,,,,,,,,454,462,2012, citations,Reference,17945,77611,2,,reference citation,,,21757739,,,Systematic identification of tubulin interacting fragments of the microtubule-associated protein TAU leads to a highly efficient promoter of microtubule assembly.,published,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,2011, citations,Reference_2,17945,77612,3,,reference citation,,,18762868,,,Graphical interpretation of Boolean operators for protein NMR assignments.,in preparation,journal,J. Biomol. NMR,,42,1,,,,,,,,,,,,,,,,,,,,,,11,21,2008, citations,entry_citation,17946,77629,1,,entry citation,,,22415546,,,"Aliphatic (1)H, (13)C and (15)N chemical shift assignments of dihydrofolate reductase from the psychropiezophile Moritella profunda in complex with NADP(+) and folate.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,1,,,,,,,,,,,,,,,,,,,,,,61,64,2013, citations,entry_citation,17947,77649,1,,entry citation,,,22349976,,,"Electron self-exchange and self-amplified posttranslational modification in the hemoglobins from Synechocystis sp. PCC 6803 and Synechococcus sp. PCC 7002",published,journal,J. Biol. Inorg. Chem.,,17,4,,,,,,,,,,,,,,,,,,,,,,599,609,2012, citations,entry_citation_2,17947,77650,2,,reference citation,,,,,,TBD,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,17948,77676,1,,entry citation,,,21998307,,,"Structural characterization of Hsp12, the heat shock protein from Saccharomyces cerevisiae, in aqueous solution where it is intrinsically disordered and in detergent micelles where it is locally -helical.",published,journal,J. Biol. Chem.,The Journal of biological chemistry,286,50,,,,,,,,,,,,,,,,,,,,,,43447,43453,2011, citations,citations,17949,77694,1,,entry citation,,,22251893,,,"Solution structure of native and recombinant expressed toxin CssII from the venom of the scorpion Centruroides suffusus suffusus, and their effects on Nav1.5 Sodium channels.",published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1824,3,,,,,,,,,,,,,,,,,,,,,,478,487,2012, citations,entry_citation,1795,77708,1,,entry citation,,,,,"Moench, Susan J., Shi, Ting-Mei, Satterlee, James D., ""Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c,"" Eur. J. Biochem. 197, 631-641 (1991).","Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c",published,journal,Eur. J. Biochem.,,197,,,,,,,,,,,,,,,,,,,,,,,631,641,1991, citations,citations,17950,77723,1,,entry citation,,,22859734,,,DNA-binding domain of AtTRB2 reveals unique features of a single Myb histone protein family that binds to both Arabidopsis- and human-type telomeric DNA sequences.,published,journal,Mol. Plant,Molecular plant,5,6,,,,,,,,,,,,,,,,,,,,,,1406,1408,2012, citations,entry_citation,17952,77737,1,,entry citation,,,22423363,,,Structural analysis of Escherichia coli C5 protein.,published,journal,Proteins,Proteins,80,3,,,,,,,,,,,,,,,,,,,,,,963,967,2012, citations,entry_citation,17953,77757,1,,entry citation,,,,,,The NMR Structure of protoporphyrin-IX bound murine p22HBP,in preparation,journal,to be published,to be published,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17955,77773,1,,entry citation,,,22121114,,,"Substitution of a Conserved Disulfide in the Type IIa Bacteriocin, Leucocin A, with L-Leucine and L-Serine Residues: Effects on Activity and Three-Dimensional Structure",published,journal,Chembiochem,,13,1,,,,,,,,,,,,,,,,,,,,,,35,38,2012, citations,entry_citation,17956,77789,1,,entry citation,,,22822203,,,Cyclic Peptides Arising by Evolutionary Parallelism via Asparaginyl-Endopeptidase-Mediated Biosynthesis.,published,journal,Plant Cell,The Plant cell,24,7,,,,,,,,,,,,,,,,,,,,,,2765,2778,2012, citations,citation_1,17957,77807,1,,entry citation,,,22201035,,,"1H, 15N and 13C chemical shift assignments of the BA42 protein of the psychrophilic bacteria Bizionia argentinensis sp. nov.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,6,2,,,,,,,,,,,,,,,,,,,,,,181,183,2012, citations,entry_citation,17958,77822,1,,entry citation,,,22121114,,,"Substitution of a Conserved Disulfide in the Type IIa Bacteriocin, Leucocin A, with L-Leucine and L-Serine Residues: Effects on Activity and Three-Dimensional Structure",published,journal,Chembiochem,,13,1,,,,,,,,,,,,,,,,,,,,,,35,38,2012, citations,entry_citation,17959,77836,1,,entry citation,,,22127525,,,"Backbone and side chain 1H, 13C, and 15N assignments of the ubiquitin-like domain of human HOIL-1L, an essential component of linear ubiquitin chain assembly complex.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,6,2,,,,,,,,,,,,,,,,,,,,,,177,180,2012, citations,entry_citation,17960,77850,1,,entry citation,,,22000412,,,Structure of a Blinkin-BUBR1 complex reveals an interaction crucial for kinetochore-mitotic checkpoint regulation via an unanticipated binding Site.,published,journal,Structure,"Structure (London, England : 1993)",19,11,,,,,,,,,,,,,,,,,,,,,,1691,1700,2011, citations,entry_citation,17961,77870,1,,entry citation,,,22328579,,,Structure of the yeast U2/U6 snRNA complex.,published,journal,RNA,"RNA (New York, N.Y.)",18,4,,,,,,,,,,,,,,,,,,,,,,673,683,2012, citations,entry_citation,17962,77895,1,,entry citation,,,,,,Solution structure of putative oxidoreductase from Ehrlichia chaffeensis,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17963,77916,1,,entry citation,,,,,,Design of Integrin AlphaVbeta3-Specific Disintegrin for Cancer Therapy,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17964,77933,1,,entry citation,,,,,,"Backbone 1H, 13C, and 15N Chemical Shift Assignment for HIV-1 protease Variants",in preparation,journal,Biomol. NMR Assignments,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,17965,77950,1,,entry citation,,,,,,"Solution NMR structure of Alr2454 protein from Nostoc sp. strain PCC 7120, Northeast Structural Genomics Consortium Target NsR264",in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17966,77981,1,,entry citation,,,22619173,,,Hydrophobic Matching Controls the Tilt and Stability of the Dimeric Platelet-derived Growth Factor Receptor (PDGFR) Transmembrane Segment.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,31,,,,,,,,,,,,,,,,,,,,,,26178,26186,2012, citations,entry_citation,17967,78002,1,,entry citation,,,22483108,,,Solution structure analysis of the HPV16 E6 oncoprotein reveals a self-association mechanism required for E6-mediated degradation of p53.,published,journal,Structure,"Structure (London, England : 1993)",20,4,,,,,,,,,,,,,,,,,,,,,,604,617,2012, citations,entry_citation,17968,78025,1,,entry citation,,,22483108,,,Solution structure analysis of the HPV16 E6 oncoprotein reveals a self-association mechanism required for E6-mediated degradation of p53.,published,journal,Structure,"Structure (London, England : 1993)",20,4,,,,,,,,,,,,,,,,,,,,,,604,617,2012, citations,entry_citation,17969,78047,1,,entry citation,,,22162216,,,Targeting Zinc Finger Domains with Small Molecules: Solution Structure and Binding Studies of the RanBP2-Type Zinc Finger of RBM5,published,journal,ChemBioChem,,12,18,,,,,,,,,,,,,,,,,,,,,,2837,2845,2011, citations,entry_citation,1797,78068,1,,entry citation,,,,,"Moench, Susan J., Shi, Ting-Mei, Satterlee, James D., ""Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c,"" Eur. J. Biochem. 197, 631-641 (1991).","Proton-NMR studies of the effects of ionic strength and pH on the hyperfine-shifted resonances and phenylalanine-82 environment of three species of mitochondrial ferricytochrome c",published,journal,Eur. J. Biochem.,,197,,,,,,,,,,,,,,,,,,,,,,,631,641,1991, citations,entry_citation,17970,78083,1,,entry citation,,,22162216,,,Targeting Zinc Finger Domains with Small Molecules: Solution Structure and Binding Studies of the RanBP2-Type Zinc Finger of RBM5,published,journal,ChemBioChem,,12,18,,,,,,,,,,,,,,,,,,,,,,2837,2845,2011, citations,citations_1,17971,78106,1,,entry citation,,,,,,"Solution NMR structure of homeobox domain (171-248) of human homeobox protein TGIF1, Northeast Structural Genomics Consortium Target HR4411B.",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17972,78159,1,,entry citation,,,22328579,,,Structure of the yeast U2/U6 snRNA complex.,published,journal,RNA,"RNA (New York, N.Y.)",18,4,,,,,,,,,,,,,,,,,,,,,,673,683,2012, citations,citation_1,17973,78187,1,,entry citation,,,22392335,,,"(1)H, (13)C and (15)N resonance assignments of the Onconase FL-G zymogen.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,1,,,,,,,,,,,,,,,,,,,,,,13,15,2013, citations,entry_citation,17974,78208,1,,entry citation,,,,,,Structural and mechanistic insights into the interaction between PAT Pyk2 and Paxillin LD motif,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,17975,78223,1,,entry citation,,,22244763,,,Ligand and Receptor Dynamics Contribute to the Mechanism of Graded PPAR Agonism.,published,journal,Structure,"Structure (London, England : 1993)",20,1,,,,,,,,,,,,,,,,,,,,,,139,150,2012, citations,entry_citation,17976,78242,1,,entry citation,,,22244763,,,Ligand and Receptor Dynamics Contribute to the Mechanism of Graded PPAR Agonism.,published,journal,Structure,"Structure (London, England : 1993)",20,1,,,,,,,,,,,,,,,,,,,,,,139,150,2012, citations,entry_citation,17977,78261,1,,entry citation,,,22244763,,,Ligand and Receptor Dynamics Contribute to the Mechanism of Graded PPAR Agonism.,published,journal,Structure,"Structure (London, England : 1993)",20,1,,,,,,,,,,,,,,,,,,,,,,139,150,2012, citations,entry_citation,17978,78280,1,,entry citation,,,22610311,,,"Backbone and sidechain (1)H, (13)C and (15)N chemical shift assignments of the hydrophobin MPG1 from the rice blast fungus Magnaporthe oryzae.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,1,,,,,,,,,,,,,,,,,,,,,,109,112,2013, citations,entry_citation,17979,78299,1,,entry citation,,,,10.1007/s007750050062,,"The solution structure of desulforedoxin, a simple iron-sulfur protein - An NMR study of the zinc derivative",published,journal,J. Biol. Inorg. Chem.,,1,4,,,,,,,,,,,,,,,,,,,,,,341,354,1996, citations,entry_citation,1798,78317,1,,entry citation,,,,,"Bernard, Monique, Canioni, P., Cozzone, P., Berthou, J., Jolles, P., ""Effect of inhibitors on conformational changes in hen lysozyme around thermal transition point in solution and solid state,"" Int. J. Pept. Protein Res. 36, 46-55 (1990).","Effect of inhibitors on conformational changes in hen lysozyme around thermal transition point in solution and solid state",published,journal,Int. J. Pept. Protein Res.,,36,,,,,,,,,,,,,,,,,,,,,,,46,55,1990, citations,citation_1,17980,78330,1,,entry citation,,,23019076,,,Monomer-dimer equilibrium for the 5'-5' stacking of propeller-type parallel-stranded G-quadruplexes: NMR structural study.,published,journal,Chemistry,"Chemistry (Weinheim an der Bergstrasse, Germany)",18,46,,,,,,,,,,,,,,,,,,,,,,14752,14759,2012, citations,citation,17981,78344,1,,entry citation,,,20973509,,,Intrinsic disorder of PEP-19 confers unique dynamic properties to apo and calcium calmodulin,published,journal,Biochemistry,,49,48,,,,,,,,,,,,,,,,,,,,,,10287,10297,2010, citations,citation,17982,78362,1,,entry citation,,,20973509,,,Intrinsic disorder of PEP-19 confers unique dynamic properties to apo and calcium calmodulin,published,journal,Biochemistry,,49,48,,,,,,,,,,,,,,,,,,,,,,10287,10297,2010, citations,citation,17983,78381,1,,entry citation,,,20973509,,,Intrinsic disorder of PEP-19 confers unique dynamic properties to apo and calcium calmodulin,published,journal,Biochemistry,,49,48,,,,,,,,,,,,,,,,,,,,,,10287,10297,2010, citations,entry_citation,17985,78401,1,,entry citation,,,22072710,,,HIV-1 Vpu protein antagonizes innate restriction factor BST-2 via lipid-embedded helix-helix interactions.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,1,,,,,,,,,,,,,,,,,,,,,,58,67,2012, citations,entry_citation,17986,78417,1,,entry citation,,,23426877,,,Cyclization of the antimicrobial Peptide gomesin with native chemical ligation: influences on stability and bioactivity,published,journal,Chembiochem,,14,5,,,,,,,,,,,,,,,,,,,,,,617,624,2013, citations,citations,17987,78436,1,,entry citation,,,22238341,,,New tricks of an old pattern: structural versatility of scorpion toxins with common cysteine spacing.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,15,,,,,,,,,,,,,,,,,,,,,,12321,12330,2012, citations,MCP,17988,78451,1,,entry citation,,,21969612,,,Evolutionary Diversification of Mesobuthus -Scorpion Toxins Affecting Sodium Channels.,published,journal,Mol. Cell Proteomics,Molecular & cellular proteomics : MCP,11,1,,,,,,,,,,,,,,,,,,,,,,,,2012, citations,entry_citation,17989,78465,1,,entry citation,,,22287065,,,Secondary structure and NMR resonance assignments of the C-terminal DNA-binding domain of Uup protein.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,6,2,,,,,,,,,,,,,,,,,,,,,,197,200,2012, citations,entry_citation,18037,79434,1,,entry citation,,,22579252,,,"Dynamics Induced by beta-Lactam Antibiotics in the Active Site of Bacillus subtilisl,d-Transpeptidase.",published,journal,Structure,"Structure (London, England : 1993)",20,5,,,,,,,,,,,,,,,,,,,,,,850,861,2012, citations,entry_citation,1799,78484,1,,entry citation,,,,,"Bernard, Monique, Canioni, P., Cozzone, P., Berthou, J., Jolles, P., ""Effect of inhibitors on conformational changes in hen lysozyme around thermal transition point in solution and solid state,"" Int. J. Pept. Protein Res. 36, 46-55 (1990).","Effect of inhibitors on conformational changes in hen lysozyme around thermal transition point in solution and solid state",published,journal,Int. J. Pept. Protein Res.,,36,,,,,,,,,,,,,,,,,,,,,,,46,55,1990, citations,MAC-1_ALPHA_CYTOPLASMIC_TAIL,17990,78497,1,,entry citation,,,22052909,,,Structures and interaction analyses of integrin M2 cytoplasmic tails.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,286,51,,,,,,,,,,,,,,,,,,,,,,43842,43854,2011, citations,entry_citation,17991,78514,1,,entry citation,,,22155685,,,NMR structure and dynamics of a designed water-soluble transmembrane domain of nicotinic acetylcholine receptor.,published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1818,3,,,,,,,,,,,,,,,,,,,,,,617,626,2012, citations,entry_citation,17992,78531,1,,entry citation,,,22155685,,,NMR structure and dynamics of a designed water-soluble transmembrane domain of nicotinic acetylcholine receptor.,published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1818,3,,,,,,,,,,,,,,,,,,,,,,617,626,2012, citations,entry_citation,17993,78548,1,,entry citation,,,23434648,,,Structural Characterization of an LPA1 Second Extracellular Loop Mimetic with a Self-Assembling Coiled-Coil Folding Constraint.,published,journal,Int. J. Mol. Sci.,International journal of molecular sciences,14,2,,,,,,,,,,,,,,,,,,,,,,2788,2807,2013, citations,Backbone_1H_13C_and_15N_Chemical_Shift_Assignment_for_HIV-1_protease_Variants,17994,78563,1,,entry citation,,,,,,"Backbone 1H, 13C, and 15N Chemical Shift Assignment for HIV-1 protease Variants",in preparation,journal,Biomol. 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Protein Res.,,36,,,,,,,,,,,,,,,,,,,,,,,46,55,1990, citations,entry_citation,18000,78714,1,,entry citation,,,22244764,,,Structural Basis for Molecular Interactions Involving MRG Domains: Implications in Chromatin Biology.,published,journal,Structure,"Structure (London, England : 1993)",20,1,,,,,,,,,,,,,,,,,,,,,,151,160,2012, citations,entry_citation,18001,78734,1,,entry citation,,,22287093,,,NMR assignments of the FKBP-type PPIase domain of the human aryl-hydrocarbon receptor-interacting protein (AIP),published,journal,Biomol. NMR Assignments,,6,2,,,,,,,,,,,,,,,,,,,,,,209,212,2012, citations,entry_citation,18002,78752,1,,entry citation,,,22030399,,,Structural basis of phosphoinositide binding to kindlin-2 protein pleckstrin homology domain in regulating integrin activation.,published,journal,J. Biol. 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NMR Assignments,Biomolecular NMR assignments,6,2,,,,,,,,,,,,,,,,,,,,,,201,203,2012, citations,entry_citation,18013,78988,1,,entry citation,,,22619184,,,Mannosylglycerate stabilizes staphylococcal nuclease with restriction of slow -sheet motions.,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,21,8,,,,,,,,,,,,,,,,,,,,,,1126,1137,2012, citations,entry_citation,18014,79010,1,,entry citation,,,,,,A Myristoylated Polyproline Type II Helix Functions as a Novel Fusion Peptide During Cell-Cell Membrane Fusion Induced by the Baboon Reovirus p15 FAST Protein,submitted,journal,J. Biol. 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J. Pept. Protein Res. 36, 46-55 (1990).","Effect of inhibitors on conformational changes in hen lysozyme around thermal transition point in solution and solid state",published,journal,Int. J. Pept. Protein Res.,,36,,,,,,,,,,,,,,,,,,,,,,,46,55,1990, citations,Citation1,18020,79135,1,,entry citation,,,23339031,,,Assignments of human integrin 1I domain in the apo and Mg+ bound states.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,8,1,,,,,,,,,,,,,,,,,,,,,,117,121,2014, citations,Citation1,18021,79151,1,,entry citation,,,23339031,,,Assignments of human integrin a1I domain in the apo and Mg2+ bound states.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,8,1,,,,,,,,,,,,,,,,,,,,,,117,121,2014, citations,entry_citation,18022,79168,1,,entry citation,,,22558917,,,Phosphorylation controls the interaction of the connexin43 C-terminal domain with tubulin and microtubules.,published,journal,Biochemistry,Biochemistry,51,21,,,,,,,,,,,,,,,,,,,,,,4331,4342,2012, citations,entry_citation,18023,79183,1,,entry citation,,,22802678,,,Crystal and NMR structures of a Trp-cage mini-protein benchmark for computational fold prediction.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,109,31,,,,,,,,,,,,,,,,,,,,,,12521,12525,2012, citations,citation_1,18024,79198,1,,entry citation,,,22302441,,,"Solid-state NMR [13C,15N] resonance assignments of the nucleotide-binding domain of a bacterial cyclic nucleotide-gated channel.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,6,2,,,,,,,,,,,,,,,,,,,,,,225,229,2012, citations,citation_1,18025,79214,1,,entry citation,,,,,,1H and 15N Assigned Chemical Shifts for hUBR2 ubr-box,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18026,79229,1,,entry citation,,,22392341,,,"Backbone (1)H, (13)C, and (15)N resonance assignments of guanylyl cyclase activating protein-1, GCAP1.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,1,,,,,,,,,,,,,,,,,,,,,,39,42,2013, citations,entry_citation,18027,79249,1,,entry citation,,,22486744,,,Structure and Dynamics of Calmodulin (CaM) Bound to Nitric Oxide Synthase Peptides: Effects of a Phosphomimetic CaM Mutation,published,journal,Biochemistry,,51,17,,,,,,,,,,,,,,,,,,,,,,3651,3661,2012, citations,entry_citation,18028,79266,1,,entry citation,,,22486744,,,Structure and Dynamics of Calmodulin (CaM) Bound to Nitric Oxide Synthase Peptides: Effects of a Phosphomimetic CaM Mutation,published,journal,Biochemistry,,51,17,,,,,,,,,,,,,,,,,,,,,,3651,3661,2012, citations,entry_citation,18029,79281,1,,entry citation,,,21383138,,,Molecular recognition and substrate mimicry drive the electron-transfer process between MIA40 and ALR.,published,journal,Proc. Natl. Acad. Sci. 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NMR Assignments,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,holo-RPA2022,18032,79333,1,,entry citation,,,,,,Solution NMR structure of the specialized holo-acyl carrier protein RPA2022 from Rhodopseudomonas palustris refined with NH RDCs. Northeast Structural Genomics Consortium Target RpR324.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18034,79386,1,,entry citation,,,22605553,,,UNAC tetraloops: to what extent do they mimic GNRA tetraloops?,published,journal,Biopolymers,Biopolymers,97,8,,,,,,,,,,,,,,,,,,,,,,617,628,2012, citations,entry_citation,18035,79402,1,,entry citation,,,22605553,,,UNAC tetraloops: to what extent do they mimic GNRA tetraloops?,published,journal,Biopolymers,Biopolymers,97,8,,,,,,,,,,,,,,,,,,,,,,617,628,2012, citations,entry_citation,18036,79418,1,,entry citation,,,22605553,,,UNAC tetraloops: to what extent do they mimic GNRA tetraloops?,published,journal,Biopolymers,Biopolymers,97,8,,,,,,,,,,,,,,,,,,,,,,617,628,2012, citations,entry_citation,18039,79476,1,,entry citation,,,22399295,,,Galactose recognition by the apicomplexan parasite Toxoplasma gondii.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,20,,,,,,,,,,,,,,,,,,,,,,16720,16733,2012, citations,entry_citation,18040,79496,1,,entry citation,,,22362757,,,Double threading through DNA: NMR structural study of a bis-naphthalene macrocycle bound to a thymine-thymine mismatch.,published,journal,Nucleic Acids Res.,Nucleic acids research,40,11,,,,,,,,,,,,,,,,,,,,,,5115,5128,2012, citations,entry_citation,18041,79512,1,,entry citation,,,22085934,,,The structural basis of Edc3- and Scd6-mediated activation of the Dcp1:Dcp2 mRNA decapping complex.,published,journal,EMBO J.,The EMBO journal,31,2,,,,,,,,,,,,,,,,,,,,,,279,290,2011, citations,entry_citation,18042,79527,1,,entry citation,,,22085934,,,The structural basis of Edc3- and Scd6-mediated activation of the Dcp1:Dcp2 mRNA decapping complex.,published,journal,EMBO J.,The EMBO journal,31,2,,,,,,,,,,,,,,,,,,,,,,279,290,2011, citations,entry_citation,18043,79543,1,,entry citation,,,22322867,,,The insect defensin lucifensin from Lucilia sericata,published,journal,J. Biomol. NMR,,52,3,,,,,,,,,,,,,,,,,,,,,,277,282,2012, citations,entry_citation,18044,79563,1,,entry citation,,,22329686,,,Potential of fragment recombination for rational design of proteins,published,journal,J. Am. Chem. Soc.,,134,9,,,,,,,,,,,,,,,,,,,,,,4019,4022,2012, citations,entry_citation,18045,79581,1,,entry citation,,,22392337,,,"(1)H, (13)C, and (15)N chemical shifts assignments for human endothelial monocyte-activating polypeptide EMAP II.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,1,,,,,,,,,,,,,,,,,,,,,,25,29,2013, citations,entry_citation,18046,79598,1,,entry citation,,,24070253,,,Gelsolin-like activation of villin: calcium sensitivity of the long helix in domain 6.,published,journal,Biochemistry,Biochemistry,52,45,,,,,,,,,,,,,,,,,,,,,,7890,7900,2013, citations,entry_citation,18047,79621,1,,entry citation,,,,,,NMR structure of the protein NP_814968.1 from Enterococcus faecalis,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18048,79636,1,,entry citation,,,22707729,,,Structure of nucleophosmin DNA-binding domain and analysis of its complex with a G-quadruplex sequence from the c-MYC promoter.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,32,,,,,,,,,,,,,,,,,,,,,,26539,26548,2012, citations,citation_1,18049,79658,1,,entry citation,,,22402490,,,Air2p is critical for the assembly and RNA-binding of the TRAMP complex and the KOW domain of Mtr4p is crucial for exosome activation.,published,journal,Nucleic Acids Res.,Nucleic acids research,40,12,,,,,,,,,,,,,,,,,,,,,,5679,5693,2012, citations,entry_citation,18050,79675,1,,entry citation,,,22362757,,,Double threading through DNA: NMR structural study of a bis-naphthalene macrocycle bound to a thymine-thymine mismatch.,published,journal,Nucleic Acids Res.,Nucleic acids research,40,11,,,,,,,,,,,,,,,,,,,,,,5115,5128,2012, citations,entry_citation,18051,79693,1,,entry citation,,,,,,Solution NMR structure of the N-terminal myb-like 1 domain of the human cyclin-D-binding transcription factor 1 (hDMP1).,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18052,79718,1,,entry citation,,,23001756,,,Structural analysis of the pyroglutamate modified isoform of the Alzheimer's disease related beta-amyloid using NMR spectroscopy,published,journal,J. 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Sci.,,18,11,,,,,,,,,,,,,,,,,,,,,,691,695,2012, citations,entry_citation,18053,79736,1,,entry citation,,,,,,NMR solution structure of c-terminal globular domain of human Lamin-B2.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,Cite_1,18054,79760,1,,entry citation,,,23251481,,,Differential Dynamic Engagement within 24 SH3 Domain: Peptide Complexes Revealed by Co-Linear Chemical Shift Perturbation Analysis.,published,journal,PLoS ONE,PloS one,7,12,,,,,,,,,,,,,,,,,,,,,,e51282,e51282,2012, citations,Cite_1,18055,79774,1,,entry citation,,,23251481,,,Differential Dynamic Engagement within 24 SH3 Domain: Peptide Complexes Revealed by Co-Linear Chemical Shift Perturbation Analysis.,published,journal,PLoS ONE,PloS one,7,12,,,,,,,,,,,,,,,,,,,,,,e51282,e51282,2012, citations,Cite_1,18056,79789,1,,entry citation,,,23251481,,,Differential Dynamic Engagement within 24 SH3 Domain: Peptide Complexes Revealed by Co-Linear Chemical Shift Perturbation 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one,7,12,,,,,,,,,,,,,,,,,,,,,,e51282,e51282,2012, citations,Cite_1,18064,79909,1,,entry citation,,,23251481,,,Differential Dynamic Engagement within 24 SH3 Domain: Peptide Complexes Revealed by Co-Linear Chemical Shift Perturbation Analysis.,published,journal,PLoS ONE,PloS one,7,12,,,,,,,,,,,,,,,,,,,,,,e51282,e51282,2012, citations,Cite_1,18065,79924,1,,entry citation,,,23251481,,,Differential Dynamic Engagement within 24 SH3 Domain: Peptide Complexes Revealed by Co-Linear Chemical Shift Perturbation Analysis.,published,journal,PLoS ONE,PloS one,7,12,,,,,,,,,,,,,,,,,,,,,,e51282,e51282,2012, citations,Cite_1,18066,79939,1,,entry citation,,,23251481,,,Differential Dynamic Engagement within 24 SH3 Domain: Peptide Complexes Revealed by Co-Linear Chemical Shift Perturbation Analysis.,published,journal,PLoS ONE,PloS one,7,12,,,,,,,,,,,,,,,,,,,,,,e51282,e51282,2012, citations,Cite_1,18067,79954,1,,entry citation,,,23251481,,,Differential Dynamic Engagement within 24 SH3 Domain: Peptide 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citations,Cite_1,18071,80014,1,,entry citation,,,23251481,,,Differential Dynamic Engagement within 24 SH3 Domain: Peptide Complexes Revealed by Co-Linear Chemical Shift Perturbation Analysis.,published,journal,PLoS ONE,PloS one,7,12,,,,,,,,,,,,,,,,,,,,,,e51282,e51282,2012, citations,Cite_1,18072,80029,1,,entry citation,,,23251481,,,Differential Dynamic Engagement within 24 SH3 Domain: Peptide Complexes Revealed by Co-Linear Chemical Shift Perturbation Analysis.,published,journal,PLoS ONE,PloS one,7,12,,,,,,,,,,,,,,,,,,,,,,e51282,e51282,2012, citations,Cite_1,18073,80044,1,,entry citation,,,23251481,,,Differential Dynamic Engagement within 24 SH3 Domain: Peptide Complexes Revealed by Co-Linear Chemical Shift Perturbation Analysis.,published,journal,PLoS ONE,PloS one,7,12,,,,,,,,,,,,,,,,,,,,,,e51282,e51282,2012, citations,Cite_1,18074,80059,1,,entry citation,,,23251481,,,Differential Dynamic Engagement within 24 SH3 Domain: Peptide Complexes Revealed by Co-Linear Chemical Shift Perturbation Analysis.,published,journal,PLoS ONE,PloS one,7,12,,,,,,,,,,,,,,,,,,,,,,e51282,e51282,2012, citations,Cite_1,18075,80074,1,,entry citation,,,23251481,,,Differential Dynamic Engagement within 24 SH3 Domain: Peptide Complexes Revealed by Co-Linear Chemical Shift Perturbation Analysis.,published,journal,PLoS ONE,PloS one,7,12,,,,,,,,,,,,,,,,,,,,,,e51282,e51282,2012, citations,Cite_1,18076,80089,1,,entry citation,,,23251481,,,Differential Dynamic Engagement within 24 SH3 Domain: Peptide Complexes Revealed by Co-Linear Chemical Shift Perturbation Analysis.,published,journal,PLoS ONE,PloS one,7,12,,,,,,,,,,,,,,,,,,,,,,e51282,e51282,2012, citations,Cite_1,18077,80104,1,,entry citation,,,23251481,,,Differential Dynamic Engagement within 24 SH3 Domain: Peptide Complexes Revealed by Co-Linear Chemical Shift Perturbation Analysis.,published,journal,PLoS ONE,PloS one,7,12,,,,,,,,,,,,,,,,,,,,,,e51282,e51282,2012, citations,Cite_1,18078,80119,1,,entry citation,,,23251481,,,Differential 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Chem.,The Journal of biological chemistry,287,12,,,,,,,,,,,,,,,,,,,,,,9336,9344,2012, citations,citations,18083,80227,1,,entry citation,,,22239621,,,Structural basis for matrix metalloproteinase 1-catalyzed collagenolysis,published,journal,J. Am. Chem. Soc.,,134,4,,,,,,,,,,,,,,,,,,,,,,2100,2110,2012, citations,entry_citation,18084,80243,1,,entry citation,,,22275375,,,Structural basis for Ca2+-induced activation and dimerization of estrogen receptor by calmodulin.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,12,,,,,,,,,,,,,,,,,,,,,,9336,9344,2012, citations,entry_citation,18085,80261,1,,entry citation,,,,,,Structure of Alvinellacin,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18086,80277,1,,entry citation,,,22941047,,,A new type V toxin-antitoxin system where mRNA for toxin GhoT is cleaved by antitoxin GhoS,published,journal,Nat. Chem. Biol.,,,,,,,,,,,,,,,,,,,,,,,,,,,2012, citations,entry_citation,18087,80295,1,,entry citation,,,,,,Chemical Shift Assignments and solution structure of human apo-S100A1 C85M mutant,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18088,80330,1,,entry citation,,,22989881,,,Post-translational S-nitrosylation is an endogenous factor fine tuning the properties of human S100A1 protein.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,48,,,,,,,,,,,,,,,,,,,,,,40457,40470,2012, citations,entry_citation,18089,80348,1,,entry citation,,,22989881,,,Post-translational S-nitrosylation is an endogenous factor fine tuning the properties of human S100A1 protein.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,48,,,,,,,,,,,,,,,,,,,,,,40457,40470,2012, citations,citation_1,18090,80365,1,,entry citation,,,22227520,,,The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop.,published,journal,EMBO J.,The EMBO journal,31,6,,,,,,,,,,,,,,,,,,,,,,1506,1517,2012, citations,citation_1,18091,80387,1,,entry citation,,,22227520,,,The architecture of functional modules in the Hsp90 co-chaperone Sti1/Hop.,published,journal,EMBO J.,The EMBO journal,31,6,,,,,,,,,,,,,,,,,,,,,,1506,1517,2012, citations,entry_citation,18092,80409,1,,entry citation,,,22517631,,,Structure and dynamics in solution of the stop codon decoding N-terminal domain of the human polypeptide chain release factor eRF1.,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,21,6,,,,,,,,,,,,,,,,,,,,,,896,903,2012, citations,entry_citation,18093,80443,1,,entry citation,,,22361591,,,NMR structures of the transmembrane domains of the 42 nAChR.,published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1818,5,,,,,,,,,,,,,,,,,,,,,,1261,1268,2012, citations,entry_citation,18094,80460,1,,entry citation,,,23260655,,,Leukemia Fusion Target AF9 Is an Intrinsically Disordered Transcriptional Regulator that Recruits Multiple Partners via Coupled Folding and Binding.,published,journal,Structure,"Structure (London, England : 1993)",21,1,,,,,,,,,,,,,,,,,,,,,,176,183,2013, citations,citations,18095,80483,1,,entry citation,,,,,,Northeast Structural Genomics Consortium Target FR824D,in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18096,80506,1,,entry citation,,,22361591,,,NMR structures of the transmembrane domains of the 42 nAChR.,published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1818,5,,,,,,,,,,,,,,,,,,,,,,1261,1268,2012, citations,entry_citation,18097,80523,1,,entry citation,,,22847415,,,"Structure of the rhesus monkey TRIM5 PRYSPRY domain, the HIV capsid recognition module.",published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,109,33,,,,,,,,,,,,,,,,,,,,,,13278,13283,2012, citations,citations,18098,80543,1,,entry citation,,,,,,Solution NMR Structure of mitochondrial succinate dehydrogenase assembly factor 2 from Saccharomyces cerevisiae,in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18099,80576,1,,entry citation,,,22283712,,,Structural basis for the activation of platelet integrin IIb3 by calcium- and integrin-binding protein 1.,published,journal,J. Am. Chem. 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NMR Assignments,Biomolecular NMR assignments,6,2,,,,,,,,,,,,,,,,,,,,,,213,215,2012, citations,entry_citation,18102,80633,1,,entry citation,,,22464970,,,"Structure, activity and interactions of the cysteine deleted analog of tachyplesin-1 with lipopolysaccharide micelle: Mechanistic insights into outer-membrane permeabilization and endotoxin neutralization.",published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1818,7,,,,,,,,,,,,,,,,,,,,,,1613,1624,2012, citations,citation_1,18103,80649,1,,entry citation,,,22274999,,,Backbone resonance assignments for G protein (i3) subunit in the GTP-bound state.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,6,2,,,,,,,,,,,,,,,,,,,,,,217,220,2012, citations,citation_1,18104,80673,1,,entry citation,,,24590112,,,Structural characterization of a neuroblast-specific phosphorylated region of MARCKS,published,journal,Biochim. Biophys. 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NMR Assignments,Biomolecular NMR assignments,7,1,,,,,,,,,,,,,,,,,,,,,,35,38,2013, citations,citations,18124,81052,1,,entry citation,,,23831579,,,NMR structure of the N-terminal-most HRDC1 domain of RecQ helicase from Deinococcus radiodurans.,published,journal,FEBS Lett.,FEBS letters,587,16,,,,,,,,,,,,,,,,,,,,,,2635,2642,2013, citations,entry_citation,18125,81066,1,,entry citation,,,22392339,,,Resonance assignments of the 56kDa chimeric avidin in the biotin-bound and free forms.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,1,,,,,,,,,,,,,,,,,,,,,,35,38,2013, citations,entry_citation,18126,81085,1,,entry citation,,,22851279,,,"Lanthanide binding and IgG affinity construct: potential applications in solution NMR, MRI, and luminescence microscopy.",published,journal,Protein Sci.,Protein science : a publication of the Protein Society,21,10,,,,,,,,,,,,,,,,,,,,,,1456,1466,2012, citations,citation_1,18127,81100,1,,entry citation,,,16401079,,,Experimental Constraints on Quaternary Structure in Alzheimer's Beta-Amyloid Fibrils,published,journal,Biochemistry,,45,498,,,,,,,,,,,,,,,,,,,,,,498,512,2006, citations,citation_1,18128,81115,1,,entry citation,,,16401079,,,Experimental Constraints on Quaternary Structure in Alzheimer's Beta-Amyloid Fibrils,published,journal,Biochemistry,,45,498,,,,,,,,,,,,,,,,,,,,,,498,512,2006, citations,citation_1,18129,81130,1,,entry citation,,,16401079,,,Molecular structural basis for polymorphism in Alzheimer's beta-amyloid fibrils,published,journal,Proc. 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NMR Assignments,Biomolecular NMR assignments,7,2,,,,,,,,,,,,,,,,,,,,,,155,158,2013, citations,entry_citation,18134,81220,1,,entry citation,,,22332920,,,Solution structure of the first Sam domain of Odin and binding studies with the EphA2 receptor.,published,journal,Biochemistry,Biochemistry,51,10,,,,,,,,,,,,,,,,,,,,,,2136,2145,2012, citations,citations,18135,81237,1,,entry citation,,,23184955,,,A single N-acetylgalactosamine residue at threonine 106 modifies the dynamics and structure of interferon 2a around the glycosylation site.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,1,,,,,,,,,,,,,,,,,,,,,,247,254,2013, citations,entry_citation,18137,81256,1,,entry citation,,,22618863,,,Backbone resonance assignments of the monomeric DUF59 domain of human Fam96a.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,2,,,,,,,,,,,,,,,,,,,,,,117,120,2013, citations,citation_1,18138,81274,1,,entry citation,,,22752791,,,"Backbone 1H, 13C, and 15N chemical shift assignment for HIV-1 protease subtypes and multi-drug resistant variant MDR 769.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,2,,,,,,,,,,,,,,,,,,,,,,199,202,2013, citations,entry_citation,1814,81291,1,,entry citation,,,,,"You, Jun-ling, Scarsdale, J. Neel, Harris, Robert B., ""Calorimetric and Spectroscopic Examination of the Solution Phase Structures of Prekallikrein Binding Domain Peptides of High Molecular Weight Kininogen,"" J. Protein Chem. 10 (3), 301-311 (1991).","Calorimetric and Spectroscopic Examination of the Solution Phase Structures of Prekallikrein Binding Domain Peptides of High Molecular Weight Kininogen",published,journal,J. Protein Chem.,,10,3,,,,,,,,,,,,,,,,,,,,,,301,311,1991, citations,entry_citation,18141,81304,1,,entry citation,,,22399292,,,A Helical Conotoxin from Conus imperialis Has a Novel Cysteine Framework and Defines a New Superfamily.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,18,,,,,,,,,,,,,,,,,,,,,,14973,14983,2012, citations,entry_citation,18142,81323,1,,entry citation,,,22713874,,,Combinatorial readout of unmodified H3R2 and acetylated H3K14 by the tandem PHD finger of MOZ reveals a regulatory mechanism for HOXA9 transcription,published,journal,Genes Dev.,,26,12,,,,,,,,,,,,,,,,,,,,,,1376,1391,2012, citations,citations,18145,81342,1,,entry citation,,,23135467,,,Principles for designing ideal protein structures,published,journal,Nature,,491,7423,,,,,,,,,,,,,,,,,,,,,,222,227,2012, citations,entry_citation,18146,81382,1,,entry citation,,,23137439,,,"Insight into the antimicrobial activities of coprisin isolated from the dung beetle, Copris tripartitus, revealed by structure-activity relationships.",published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1828,2,,,,,,,,,,,,,,,,,,,,,,271,283,2013, citations,citations,18147,81397,1,,entry citation,,,22389115,,,Segmental isotope labeling of proteins for NMR structural study using a protein S tag for higher expression and solubility.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,52,4,,,,,,,,,,,,,,,,,,,,,,303,313,2012, citations,entry_citation,18148,81412,1,,entry citation,,,22363548,,,Integrin (3) Crosstalk with VEGFR Accommodating Tyrosine Phosphorylation as a Regulatory Switch.,published,journal,PLoS ONE,PloS one,7,2,,,,,,,,,,,,,,,,,,,,,,,,2012, citations,entry_citation,1815,81426,1,,entry citation,,,,,"You, Jun-ling, Scarsdale, J. Neel, Harris, Robert B., ""Calorimetric and Spectroscopic Examination of the Solution Phase Structures of Prekallikrein Binding Domain Peptides of High Molecular Weight Kininogen,"" J. 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NMR Assignments,Biomolecular NMR assignments,7,1,,,,,,,,,,,,,,,,,,,,,,65,67,2013, citations,citations,18156,81528,1,,entry citation,,,,,,Northeast Structural Genomics Consortium Target HR6741A,in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18157,81572,1,,entry citation,,,23075041,,,Structural basis for interactions of the Phytophthora sojae RxLR effector Avh5 with phosphatidylinositol 3-phosphate and for host cell entry.,published,journal,Mol. 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Chem.,,168,,,,,,,,,,,,,,,,,,,,,,,48,59,2012, citations,citations,18165,81756,1,,entry citation,,,22921828,,,Enterohaemorrhagic Escherichia coli exploits a tryptophan switch to hijack host f-actin assembly.,published,journal,Structure,"Structure (London, England : 1993)",20,10,,,,,,,,,,,,,,,,,,,,,,1692,1703,2012, citations,citations,18166,81777,1,,entry citation,,,,,,Northeast Structural Genomics Consortium Target HR4403E,in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18167,81806,1,,entry citation,,,22414666,,,Solution structure of CyanoP from Synechocystis sp. PCC 6803: new insights on the structural basis for functional specialization amongst PsbP family proteins.,published,journal,Biochim. Biophys. 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Chem.,The Journal of biological chemistry,287,31,,,,,,,,,,,,,,,,,,,,,,26388,26399,2012, citations,entry_citation,18178,81943,1,,entry citation,,,23274113,,,Metastasis-promoting anterior gradient 2 protein has a dimeric thioredoxin fold structure and a role in cell adhesion.,published,journal,J. Mol. Biol.,Journal of molecular biology,425,5,,,,,,,,,,,,,,,,,,,,,,929,943,2013, citations,entry_citation,18179,81963,1,,entry citation,,,23274113,,,Metastasis-promoting anterior gradient 2 protein has a dimeric thioredoxin fold structure and a role in cell adhesion.,published,journal,J. Mol. Biol.,Journal of molecular biology,425,5,,,,,,,,,,,,,,,,,,,,,,929,943,2013, citations,citations,18180,81982,1,,entry citation,,,,,,Solution NMR Structure of the uncharacterized protein from gene locus rrnAC0354 of Haloarcula marismortui. Northeast Structural Genomics Consortium Target HmR11.,in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18181,82019,1,,entry citation,,,22253442,,,Solution structure of homology region (HR) domain of type II secretion system.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,12,,,,,,,,,,,,,,,,,,,,,,9072,9080,2012, citations,entry_citation,18182,82040,1,,entry citation,,,22750419,,,Identification and structural basis for a novel interaction between Vav2 and Arap3,published,journal,J. Struct. Biol.,,180,1,,,,,,,,,,,,,,,,,,,,,,84,95,2012, citations,entry_citation,18183,82060,1,,entry citation,,,22750419,,,Identification and structural basis for a novel interaction between Vav2 and Arap3,published,journal,J. Struct. Biol.,,180,1,,,,,,,,,,,,,,,,,,,,,,84,95,2012, citations,entry_citation,18184,82077,1,,entry citation,,,22828329,,,Supramolecular structure of membrane-associated polypeptides by combining solid-state NMR and molecular dynamics simulations.,published,journal,Biophys. J.,Biophysical journal,103,1,,,,,,,,,,,,,,,,,,,,,,29,37,2012, citations,entry_citation,18185,82092,1,,entry citation,,,22493438,,,Evidence for cooperative and domain-specific binding of the signal transducing adaptor molecule 2 (STAM2) to Lys63-linked diubiquitin.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,22,,,,,,,,,,,,,,,,,,,,,,18687,18699,2012, citations,entry_citation,18186,82109,1,,entry citation,,,22262836,,,Get5 carboxyl-terminal domain is a novel dimerization motif that tethers an extended Get4/Get5 complex.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,11,,,,,,,,,,,,,,,,,,,,,,8310,8317,2012, citations,entry_citation,18187,82133,1,,entry citation,,,22262836,,,The Get5 carboxyl terminal domain is a novel dimerization motif that tethers an extended Get4/Get5 complex.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,11,,,,,,,,,,,,,,,,,,,,,,8310,8317,2012, citations,entry_citation,18188,82158,1,,entry citation,,,22446850,,,Resonance assignments of cohesin and dockerin domains from Clostridium acetobutylicum ATCC824.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,1,,,,,,,,,,,,,,,,,,,,,,73,76,2013, citations,entry_citation,18189,82174,1,,entry citation,,,22446850,,,Resonance assignments of cohesin and dockerin domains from Clostridium acetobutylicum ATCC824.,published,journal,Biomol. 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Biochem.,,40,,,,,,,,,,,,,,,,,,,,,,,245,253,1990, citations,entry_citation,18190,82203,1,,entry citation,,,,,,"NMR structure of the protein BC008182, DNAJ homolog from Homo sapiens",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18191,82220,1,,entry citation,,,,,,Insights into the role of SGF11 and SGF73 for the interaction between SAGA and nucleosomes,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18192,82246,1,,entry citation,,,,,,Insights into the role of SGF11 and SGF73 for the interaction between SAGA and nucleosomes,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18193,82276,1,,entry citation,,,22782235,,,NMR structure note: N-terminal domain of Thermus thermophilus CdnL,published,journal,J. Biomol. NMR,,53,4,,,,,,,,,,,,,,,,,,,,,,355,363,2012, citations,entry_citation,18194,82299,1,,entry citation,,,,,,Solution NMR structure of the 72-residue N-terminal domain of Myxococcus xanthus CarD,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18195,82318,1,,entry citation,,,,,,NMR Solution Structure of Optineurin Zinc-finger Domain,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,18196,82339,1,,entry citation,,,22585087,,,"1H, 13C and 15N chemical shift assignments for an intracellular proteinase inhibitor of Bacillus subtilis.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,2,,,,,,,,,,,,,,,,,,,,,,129,132,2013, citations,entry_citation,18197,82356,1,,entry citation,,,22477091,,,"(1)H, (13)C, (15)N backbone and side-chain resonance assignments of rat angiogenin.",published,journal,Biomol. 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NMR Assignments,Biomolecular NMR assignments,7,1,,,,,,,,,,,,,,,,,,,,,,43,46,2013, citations,entry_citation,18202,82462,1,,entry citation,,,22311970,,,Human protein N-terminal acetyltransferase hNaa50p (hNAT5/hSAN) follows ordered sequential catalytic mechanism: combined kinetic and NMR study.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,13,,,,,,,,,,,,,,,,,,,,,,10081,10088,2012, citations,entry_citation,18203,82480,1,,entry citation,,,23557677,,,Mammalian neuronal sodium channel blocker Mu-conotoxin BuIIIB has a structured N-terminus that influences potency.,published,journal,ACS Chem. 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Biol.,ACS chemical biology,8,6,,,,,,,,,,,,,,,,,,,,,,1344,1351,2013, citations,entry_citation,18207,82546,1,,entry citation,,,23505409,,,Site-Specific Perturbations of Alpha-Synuclein Fibril Structure by the Parkinson's Disease Associated Mutations A53T and E46K.,published,journal,PLoS ONE,PloS one,8,3,,,,,,,,,,,,,,,,,,,,,,e49750,e49750,2013, citations,entry_citation,18208,82561,1,,entry citation,,,23505409,,,Site-Specific Perturbations of Alpha-Synuclein Fibril Structure by the Parkinson's Disease Associated Mutations A53T and E46K.,published,journal,PLoS ONE,PloS one,8,3,,,,,,,,,,,,,,,,,,,,,,e49750,e49750,2013, citations,entry_citation,18209,82576,1,,entry citation,,,22532609,,,"Solution-state structure of an intramolecular G-quadruplex with propeller, diagonal and edgewise loops.",published,journal,Nucleic Acids Res.,Nucleic acids research,40,14,,,,,,,,,,,,,,,,,,,,,,6946,6956,2012, citations,entry_citation,1821,82594,1,,entry citation,,,,,"Moratal, Jose M., Donaire, Antonio, Salgado, Jesus, Martinez-Ferrer, Maria-Jose, ""Interaction of Sulphate and Chloride with Cobalt(II)-Carbonic Anhydrase,"" J. 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NMR Assignments,Biomolecular NMR assignments,6,1,,,,,,,,,,,,,,,,,,,,,,87,89,2012, citations,citation_1,18254,83502,1,,entry citation,,,22645370,,,Flexibility of the metal-binding region in apo-cupredoxins.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,109,24,,,,,,,,,,,,,,,,,,,,,,9254,9259,2012, citations,entry_citation,18255,83518,1,,entry citation,,,,,,"Solution structure of a MbtH-like protein from Burkholderia pseudomallei, the etiological agent responsible for melioidosis",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18256,83539,1,,entry citation,,,23968132,,,Structures of the excited states of phospholamban and shifts in their populations upon phosphorylation.,published,journal,Biochemistry,Biochemistry,52,38,,,,,,,,,,,,,,,,,,,,,,6684,6694,2013, citations,entry_citation,18257,83557,1,,entry citation,,,22766963,,,"1H, 13C and 15N resonance assignments and peptide binding site chemical shift perturbation mapping for the Escherichia coli redox enzyme chaperone DmsD.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,2,,,,,,,,,,,,,,,,,,,,,,193,197,2013, citations,entry_citation,1826,83583,1,,entry citation,,,,,"Wyss, Daniel F., Lahm, H.-W., Manneberg, M., Labhardt, Alexander M., ""Anantin-A peptide antagonist of the atrial natriuretic factor(ANF) II. Determination of the primary sequence by NMR on the basis of proton assignments,"" J. Antibiot. 44 (2), 172-180 (1991).","Anantin-A peptide antagonist of the atrial natriuretic factor(ANF) II. Determination of the primary sequence by NMR on the basis of proton assignments",published,journal,J. Antibiot.,,44,2,,,,,,,,,,,,,,,,,,,,,,172,180,1991, citations,entry_citation,18260,83596,1,,entry citation,,,22569754,,,Thermal stability of chicken brain -spectrin repeat 17: a spectroscopic study.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,53,2,,,,,,,,,,,,,,,,,,,,,,71,83,2012, citations,citations,18261,83614,1,,entry citation,,,22706024,,,pH-dependent dimerization of spider silk N-terminal domain requires relocation of a wedged tryptophan side chain.,published,journal,J. Mol. Biol.,Journal of molecular biology,422,4,,,,,,,,,,,,,,,,,,,,,,477,487,2012, citations,citations,18262,83633,1,,entry citation,,,22706024,,,pH-dependent dimerization of spider silk N-terminal domain requires relocation of a wedged tryptophan side chain.,published,journal,J. Mol. Biol.,Journal of molecular biology,422,4,,,,,,,,,,,,,,,,,,,,,,477,487,2012, citations,apo-RPA2022,18263,83652,1,,entry citation,,,,,,Solution NMR structure of the specialized apo-acyl carrier protein RPA2022 from Rhodopseudomonas palustris refined with NH RDCs. Northeast Structural Genomics Consortium Target RpR324.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18265,83692,1,,entry citation,,,23870269,,,NMR determines transient structure and dynamics in the disordered C-terminal domain of WASp interacting protein.,published,journal,Biophys. J.,Biophysical journal,105,2,,1542-0086,,,,,,,,,,,,,,,,,,,,481,493,2013, citations,entry_citation,18266,83707,1,,entry citation,,,22623057,,,"Backbone 1H, 13C and 15N resonance assignments of dengue virus NS2B-NS3p in complex with aprotinin.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,2,,,,,,,,,,,,,,,,,,,,,,137,139,2013, citations,entry_citation,18267,83725,1,,entry citation,,,22446382,,,Substrate-Dependent Millisecond Domain Motions in DNA Polymerase .,published,journal,J. Mol. Biol.,Journal of molecular biology,419,3-4,,,,,,,,,,,,,,,,,,,,,,171,182,2012, citations,entry_citation,18268,83741,1,,entry citation,,,22474326,,,Calcium-induced Conformational Changes in C-terminal Tail of Polycystin-2 Are Necessary for Channel Gating.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,21,,,,,,,,,,,,,,,,,,,,,,17232,17240,2012, citations,entry_citation,18269,83757,1,,entry citation,,,22528768,,,"(1)H-, (13)C- and (15)N-NMR assignment of the N-terminal domain of human cerebral dopamine neurotrophic factor (CDNF)",published,journal,Biomol. NMR Assign.,,,,,,,,,,,,,,,,,,,,,,,,,,,2012, citations,citation_1,18269,83758,2,,reference citation,,,,,,"1H-, 13C- and 15N-NMR assignment of the N-terminal domain of human cerebral dopamine neurotrophic factor (CDNF).",in preparation,journal,Biomol. 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Soc.,Journal of the American Chemical Society,134,13,,,,,,,,,,,,,,,,,,,,,,5807,5816,2012, citations,entry_citation,18280,83847,1,,entry citation,,,22740401,,,Structural basis of ligand interactions of the large extracellular domain of tetraspanin CD81.,published,journal,J. Virol.,Journal of virology,86,18,,,,,,,,,,,,,,,,,,,,,,9606,9616,2012, citations,entry_citation,18281,83863,1,,entry citation,,,22913709,,,Solution structure of the strawberry allergen Fra a 1.,published,journal,Biosci. Rep.,Bioscience reports,32,6,,,,,,,,,,,,,,,,,,,,,,567,575,2012, citations,entry_citation,18282,83879,1,,entry citation,,,22863803,,,"The structure of myristoylated Mason-Pfizer monkey virus matrix protein and the role of phosphatidylinositol-(4,5)-bisphosphate in its membrane binding.",published,journal,J. Mol. Biol.,Journal of molecular biology,423,3,,,,,,,,,,,,,,,,,,,,,,427,438,2012, citations,entry_citation,18283,83899,1,,entry citation,,,,,,Solution structure of homodimeric periplasmic protein YmgD in E. coli,in preparation,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18284,83914,1,,entry citation,,,,,,Solution structure of de novo designed antifreeze peptide,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18285,83929,1,,entry citation,,,22820093,,,Peptide linkage to the alpha-subunit of MHCII creates a stably inverted antigen presentation complex,published,journal,J. Mol. Biol.,Journal of molecular biology,423,3,,1089-8638,,,,,,,,,,,,,,,,,,,,294,302,2012, citations,entry_citation,18286,83948,1,,entry citation,,,,,,Solution structure of de no designed anti freeze peptide 3,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18287,83963,1,,entry citation,,,22360607,,,Site specific interaction of the polyphenol EGCG with the SEVI amyloid precursor peptide PAP(248-286).,published,journal,J. Phys. Chem. B,The journal of physical chemistry. B,116,11,,,,,,,,,,,,,,,,,,,,,,3650,3658,2012, citations,citation_1,18288,83978,1,,entry citation,,,22696136,,,"1H, 13C and 15N chemical shift assignments of Ninjurin1 Extracellular N-terminal Domain.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,2,,,,,,,,,,,,,,,,,,,,,,159,162,2013, citations,entry_citation,18289,83996,1,,entry citation,,,,,,Solution structure of de novo designed antifreeze peptide 4m,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,18290,84011,1,,entry citation,,,,,,"Solution NMR Structure of syc0711_d from Synechococcus sp., Northeast Structural Genomics Consortium (NESG) Target SnR212",in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,metGCSF_WT,18291,84038,1,,entry citation,,,,,,Comparability Study of the Structure of Filgrastim and Mutants using the NMR Fingerprint Assay,in preparation,journal,J. Pharm. 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Biol.,Journal of structural biology,180,1,,,,,,,,,,,,,,,,,,,,,,165,173,2012, citations,entry_citation,18297,84141,1,,entry citation,,,22821745,,,E2-binding surface on Uba3 -grasp domain undergoes a conformational transition.,published,journal,Proteins,Proteins,80,10,,,,,,,,,,,,,,,,,,,,,,2482,2487,2012, citations,entry_citation,18298,84158,1,,entry citation,,,23415559,,,An autoinhibited state in the structure of Thermotoga maritima NusG.,published,journal,Structure,"Structure (London, England : 1993)",21,3,,,,,,,,,,,,,,,,,,,,,,365,375,2013, citations,entry_citation,18299,84175,1,,entry citation,,,,,,Solution structure of the K60A mutant of Atox1,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,183,84195,1,,entry citation,,,,,"Brown, Stephen C., Mueller, Luciano, Jeffs, Peter W., ""1H NMR Assignment and Secondary Structural Elements of Human Transforming Growth Factor alpha,"" Biochemistry 28, 593-599 (1989).","1H NMR Assignment and Secondary Structural Elements of Human Transforming Growth Factor alpha",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,593,599,1989, citations,citation_1,18300,84208,1,,entry citation,,,23201194,,,A New Knottin from a Marine Sponge Which Enhances Neuronal Ca2+ Influx,in preparation,journal,Biochim. Biophys. Acta,,1830,3,,,,,,,,,,,,,,,,,,,,,,2591,2599,2012, citations,entry_citation,18301,84225,1,,entry citation,,,23751120,,,Copper chaperone Atox1 interacts with the metal-binding domain of Wilson's disease protein in cisplatin detoxification.,published,journal,Biochem. J.,The Biochemical journal,454,1,,,,,,,,,,,,,,,,,,,,,,147,156,2013, citations,entry_citation,18302,84242,1,,entry citation,,,22518098,,,Structural basis for the regulation of L-type voltage-gated calcium channels: interactions between the N-terminal cytoplasmic domain and Ca(2+)-calmodulin.,published,journal,Front. Mol. Neurosci.,Frontiers in molecular neuroscience,5,,,,,,,,,,,,,,,,,,,,,,,38,38,2012, citations,entry_citation,18303,84267,1,,entry citation,,,22392340,,,"(1)H, (13)C, and (15)N chemical shift assignments for PfPMT, a phosphoethanolamine methyltransferase from Plasmodium falciparum.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,1,,,,,,,,,,,,,,,,,,,,,,17,20,2013, citations,entry_citation,18304,84283,1,,entry citation,,,22593013,,,The dynamical response of hen egg white lysozyme to the binding of a carbohydrate ligand.,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,21,7,,,,,,,,,,,,,,,,,,,,,,1066,1073,2012, citations,entry_citation,18305,84300,1,,entry citation,,,22593013,,,The dynamical response of hen egg white lysozyme to the binding of a carbohydrate ligand.,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,21,7,,,,,,,,,,,,,,,,,,,,,,1066,1073,2012, citations,entry_citation,18306,84319,1,,entry citation,,,22339232,,,APOBEC2 is a Monomer in Solution: Implications for APOBEC3G Models,published,journal,Biochemistry,,51,9,,,,,,,,,,,,,,,,,,,,,,2008,2017,2012, citations,entry_citation,18307,84339,1,,entry citation,,,22339232,,,APOBEC2 is a Monomer in Solution: Implications for APOBEC3G Models,published,journal,Biochemistry,,51,9,,,,,,,,,,,,,,,,,,,,,,2008,2017,2012, citations,entry_citation,18308,84354,1,,entry citation,,,22820093,,,Peptide linkage to the alpha-subunit of MHCII creates a stably inverted antigen presentation complex,published,journal,J. Mol. Biol.,Journal of molecular biology,423,3,,1089-8638,,,,,,,,,,,,,,,,,,,,294,302,2012, citations,FliF-FliG,18309,84373,1,,entry citation,,,22670715,,,Structural insights into the interaction between the bacterial flagellar motor proteins FliF and FliG.,published,journal,Biochemistry,Biochemistry,51,25,,,,,,,,,,,,,,,,,,,,,,5052,5060,2012, citations,FliF-FliG,18310,84388,1,,entry citation,,,22670715,,,Structural insights into the interaction between the bacterial flagellar motor proteins FliF and FliG.,published,journal,Biochemistry,Biochemistry,51,25,,,,,,,,,,,,,,,,,,,,,,5052,5060,2012, citations,entry_citation,18312,84404,1,,entry citation,,,24141523,,,Structure of RNA-interacting cyclophilin A-like protein from Piriformospora indica that provides salinity-stress tolerance in plants.,published,journal,Sci. Rep.,Scientific reports,3,,,,,,,,,,,,,,,,,,,,,,,3001,3001,2013, citations,entry_citation,18313,84420,1,,entry citation,,,,,,RIAM and vinculin binding to talin are mutually exclusive and regulate adhesion assembly and turnover,in preparation,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18314,84439,1,,entry citation,,,22474372,,,Structures of KIX domain of CBP in complex with two FOXO3a transactivation domains reveal promiscuity and plasticity in coactivator recruitment.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,109,16,,,,,,,,,,,,,,,,,,,,,,6078,6083,2012, citations,entry_citation,18315,84459,1,,entry citation,,,22474372,,,Structures of KIX domain of CBP in complex with two FOXO3a transactivation domains reveal promiscuity and plasticity in coactivator recruitment.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,109,16,,,,,,,,,,,,,,,,,,,,,,6078,6083,2012, citations,citation_1,18316,84479,1,,entry citation,,,22984256,,,The C-terminal domain of the virulence factor MgtC is a divergent ACT domain.,published,journal,J. Bacteriol.,Journal of bacteriology,194,22,,,,,,,,,,,,,,,,,,,,,,6255,6263,2012, citations,citation_1,18317,84494,1,,entry citation,,,22696137,,,Chemical shift assignments of the canecystatin-1 from Saccharum officinarum.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,2,,,,,,,,,,,,,,,,,,,,,,163,165,2013, citations,entry_citation,18318,84513,1,,entry citation,,,22842048,,,Structural characterization of CHCHD5 and CHCHD7: two atypical human twin CX9C proteins.,published,journal,J. Struct. Biol.,Journal of structural biology,180,1,,,,,,,,,,,,,,,,,,,,,,190,200,2012, citations,entry_citation,18319,84541,1,,entry citation,,,22947943,,,Comparison of fragments comprising the first two helices of the human y4 and the yeast ste2p g-protein-coupled receptors.,published,journal,Biophys. J.,Biophysical journal,103,4,,,,,,,,,,,,,,,,,,,,,,817,826,2012, citations,citations,18320,84557,1,,entry citation,,,22560994,,,NMR and crystal structures of the Pyrococcus horikoshii RadA intein guide a strategy for engineering a highly efficient and promiscuous intein.,published,journal,J. Mol. Biol.,Journal of molecular biology,421,1,,,,,,,,,,,,,,,,,,,,,,85,99,2012, citations,entry_citation,18321,84579,1,,entry citation,,,22581121,,,Domain organization differences explain Bcr-Abl's preference for CrkL over CrkII,published,journal,Nat. Chem. Biol.,,8,6,,,,,,,,,,,,,,,,,,,,,,590,596,2012, citations,Mrxred,18322,84596,1,,entry citation,,,22970802,,,Mycoredoxin-1 is one of the missing links in the oxidative stress defence mechanism of Mycobacteria.,published,journal,Mol. Microbiol.,Molecular microbiology,86,4,,,,,,,,,,,,,,,,,,,,,,787,804,2012, citations,entry_citation,18323,84615,1,,entry citation,,,22518098,,,Structural basis for the regulation of L-type voltage-gated calcium channels: interactions between the N-terminal cytoplasmic domain and Ca(2+)-calmodulin.,published,journal,Front. Mol. Neurosci.,Frontiers in molecular neuroscience,5,,,,,,,,,,,,,,,,,,,,,,,38,38,2012, citations,entry_citation,18324,84634,1,,entry citation,,,22875687,,,Backbone resonance assignments of the micro-RNA precursor binding region of human TRBP.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,2,,,,,,,,,,,,,,,,,,,,,,229,233,2013, citations,MrxOx,18325,84651,1,,entry citation,,,22970802,,,Mycoredoxin-1 is one of the missing links in the oxidative stress defence mechanism of Mycobacteria.,published,journal,Mol. Microbiol.,Molecular microbiology,86,4,,,,,,,,,,,,,,,,,,,,,,787,804,2012, citations,entry_citation,18326,84670,1,,entry citation,,,22618866,,,"1H, 13C, and 15N resonance assignments of NmtR, a Ni(II)/Co(II) metalloregulatory protein of Mycobacterium tuberculosis.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,2,,,,,,,,,,,,,,,,,,,,,,145,148,2013, citations,citation,18327,84692,1,,entry citation,,,23239367,,,Solution structure of the SH3 domain of DOCK180.,published,journal,Proteins,Proteins,81,5,,,,,,,,,,,,,,,,,,,,,,906,910,2013, citations,entry_citation,18328,84712,1,,entry citation,,,22842048,,,Structural characterization of CHCHD5 and CHCHD7: two atypical human twin CX9C proteins.,published,journal,J. Struct. Biol.,Journal of structural biology,180,1,,,,,,,,,,,,,,,,,,,,,,190,200,2012, citations,entry_citation,18329,84741,1,,entry citation,,,22985470,,,Solution structure of decorin-binding protein A from Borrelia burgdorferi,published,journal,Biochemistry,,51,42,,,,,,,,,,,,,,,,,,,,,,8353,8362,2012, citations,entry_citation,18331,84760,1,,entry citation,,,22843382,,,"1H, 13C and 15N assignments of the holo-acyl carrier protein of Pseudomonas aeruginosa.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,2,,,,,,,,,,,,,,,,,,,,,,225,228,2013, citations,entry_citation,18332,84780,1,,entry citation,,,22658749,,,A protein export pathway involving Escherichia coli porins.,published,journal,Structure,"Structure (London, England : 1993)",20,7,,,,,,,,,,,,,,,,,,,,,,1154,1166,2012, citations,entry_citation,18333,84800,1,,entry citation,,,22581121,,,Domain organization differences explain Bcr-Abl's preference for CrkL over CrkII,published,journal,Nat. Chem. Biol.,,8,6,,,,,,,,,,,,,,,,,,,,,,590,596,2012, citations,citations,18334,84818,1,,entry citation,,,22612157,,,Buckwheat trypsin inhibitor with helical hairpin structure belongs to a new family of plant defence peptides.,published,journal,Biochem. J.,The Biochemical journal,446,1,,,,,,,,,,,,,,,,,,,,,,69,77,2012, citations,entry_citation,18335,84836,1,,entry citation,,,22397737,,,Structure and orientation of the gH625-644 membrane interacting region of herpes simplex virus type 1 in a membrane mimetic system.,published,journal,Biochemistry,Biochemistry,51,14,,,,,,,,,,,,,,,,,,,,,,3121,3128,2012, citations,entry_citation,18336,84854,1,,entry citation,,,22879380,,,Structure of the RNA claw of the DNA packaging motor of bacteriophage 29.,published,journal,Nucleic Acids Res.,Nucleic acids research,40,19,,,,,,,,,,,,,,,,,,,,,,9953,9963,2012, citations,citations,18337,84870,1,,entry citation,,,,,,"SOLUTION NMR STRUCTURE OF DE NOVO DESIGNED PROTEIN, P-LOOP NTPASE FOLD, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET OR136",in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18338,84912,1,,entry citation,,,23228665,,,Solution structure and dynamics of C-terminal regulatory domain of Vibrio vulnificus extracellular metalloprotease.,published,journal,Biochem. Biophys. Res. Commun.,Biochemical and biophysical research communications,430,2,,,,,,,,,,,,,,,,,,,,,,541,546,2013, citations,entry_citation,18339,84928,1,,entry citation,,,22473211,,,FtsA forms actin-like protofilaments.,published,journal,EMBO J.,The EMBO journal,31,10,,,,,,,,,,,,,,,,,,,,,,2249,2260,2012, citations,entry_citation,18340,84942,1,,entry citation,,,23213219,,,Structural mechanism of Bax inhibition by cytomegalovirus protein vMIA.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,109,51,,,,,,,,,,,,,,,,,,,,,,20901,20906,2012, citations,entry_citation,18341,84958,1,,entry citation,,,23001946,,,"1H, 13C and 15N assignments of Sgt2N-terminal dimerisation domain and its binding partner, Get5 Ubiquitin-like domain.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,2,,,,,,,,,,,,,,,,,,,,,,271,274,2013, citations,entry_citation,18342,84978,1,,entry citation,,,23001946,,,"1H, 13C and 15N assignments of Sgt2N-terminal dimerisation domain and its binding partner, Get5 Ubiquitin-like domain.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,2,,,,,,,,,,,,,,,,,,,,,,271,274,2013, citations,entry_citation,18344,84994,1,,entry citation,,,23184955,,,A single N-acetylgalactosamine residue at threonine 106 modifies the dynamics and structure of interferon 2a around the glycosylation site.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,1,,,,,,,,,,,,,,,,,,,,,,247,254,2013, citations,entry_citation,18345,85010,1,,entry citation,,,,,,Structure-function analysis of the plant defensin DEF4 from Medicago truncatula (barrel clover),in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18346,85031,1,,entry citation,,,,,,NMR structure of the protein NP_390037.1 from Bacillus subtilis,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18347,85050,1,,entry citation,,,22586077,,,Dermatophytic defensin with antiinfective potential.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,109,22,,,,,,,,,,,,,,,,,,,,,,8495,8500,2012, citations,entry_citation,18348,85068,1,,entry citation,,,23128140,,,Microtubule-binding sites of the CH domain of EB1 and its autoinhibition revealed by NMR.,published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1834,2,,,,,,,,,,,,,,,,,,,,,,499,507,2013, citations,entry_citation,18349,85082,1,,entry citation,,,,,,NMR structure of a LINE-1 type transposase domain-containing protein 1 (L1TD1) from HOMO SAPINES,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18350,85101,1,,entry citation,,,23594231,,,Structure and function of a potent lipopolysaccharide-binding antimicrobial and anti-inflammatory peptide,published,journal,J. Med. Chem.,Journal of medicinal chemistry,56,9,,1520-4804,,,,,,,,,,,,,,,,,,,,3546,3556,2013, citations,entry_citation,18351,85115,1,,entry citation,,,24218020,,,"Solution structure and interface-driven self-assembly of NC2, a new member of the Class II hydrophobin proteins.",published,journal,Proteins,Proteins,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,citations,18352,85183,1,,entry citation,,,,,,"Solution NMR Structure of CASP8-associated protein 2 from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR8150A",in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18353,85209,1,,entry citation,,,22688683,,,"1H, 15N and 13C backbone resonance assignments of the Kelch domain of mouse Keap1.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,2,,,,,,,,,,,,,,,,,,,,,,149,153,2013, citations,entry_citation,18354,85226,1,,entry citation,,,23184947,,,Conopeptide -TIA defines a new allosteric site on the extracellular surface of the 1B-adrenoceptor.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,3,,,,,,,,,,,,,,,,,,,,,,1814,1827,2013, citations,entry_citation,18355,85243,1,,entry citation,,,,,,NMR Structure of Signal Sequence Deleted (SSD) Rv0603 Protein from Mycobacterium tuberculosis without N-terminal His-tag,in preparation,journal,J. Mol. Biol.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18356,85260,1,,entry citation,,,,,,NMR Structure and Backbone dynamics of ADF like UNC-60A protein from Caenorhabditis elegans: its divergence from conventional ADF/cofilin,in preparation,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18357,85281,1,,entry citation,,,,,,The solution structure of the monomeric Acanthaporin,submitted,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18358,85299,1,,entry citation,,,,,,The solution structure of the dimeric Acanthaporin,submitted,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18359,85318,1,,entry citation,,,22734684,,,Three-Dimensional Structure and Determinants of Stability of the Iron-Sulfur Cluster Scaffold Protein IscU from Escherichia coli.,published,journal,Biochemistry,Biochemistry,51,28,,,,,,,,,,,,,,,,,,,,,,5557,5563,2012, citations,entry_citation,18360,85337,1,,entry citation,,,22734684,,,Three-Dimensional Structure and Determinants of Stability of the Iron-Sulfur Cluster Scaffold Protein IscU from Escherichia coli.,published,journal,Biochemistry,Biochemistry,51,28,,,,,,,,,,,,,,,,,,,,,,5557,5563,2012, citations,entry_citation,18361,85356,1,,entry citation,,,22734684,,,Three-Dimensional Structure and Determinants of Stability of the Iron-Sulfur Cluster Scaffold Protein IscU from Escherichia coli.,published,journal,Biochemistry,Biochemistry,51,28,,,,,,,,,,,,,,,,,,,,,,5557,5563,2012, citations,entry_citation,18362,85375,1,,entry citation,,,22734684,,,Three-Dimensional Structure and Determinants of Stability of the Iron-Sulfur Cluster Scaffold Protein IscU from Escherichia coli.,published,journal,Biochemistry,Biochemistry,51,28,,,,,,,,,,,,,,,,,,,,,,5557,5563,2012, citations,citation_1,18363,85394,1,,entry citation,,,,,,Structure and NMR assignments of Scylla Serrata anti lipopolysaccharide Factor-24 (SsALF-24),in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18364,85412,1,,entry citation,,,,,,NMR structure of the protein YP_001300941.1 from Bacteroides vulgatus,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18365,85431,1,,entry citation,,,22468860,,,Disentangling the coil: modulation of conformational and dynamic properties by site-directed mutation in the non-native state of hen egg white lysozyme.,published,journal,Biochemistry,Biochemistry,51,16,,,,,,,,,,,,,,,,,,,,,,3361,3372,2012, citations,entry_citation,18366,85447,1,,entry citation,,,22468860,,,Disentangling the coil: modulation of conformational and dynamic properties by site-directed mutation in the non-native state of hen egg white lysozyme.,published,journal,Biochemistry,Biochemistry,51,16,,,,,,,,,,,,,,,,,,,,,,3361,3372,2012, citations,entry_citation,18367,85462,1,,entry citation,,,22468860,,,Disentangling the coil: modulation of conformational and dynamic properties by site-directed mutation in the non-native state of hen egg white lysozyme.,published,journal,Biochemistry,Biochemistry,51,16,,,,,,,,,,,,,,,,,,,,,,3361,3372,2012, citations,entry_citation,18368,85477,1,,entry citation,,,22468860,,,Disentangling the coil: modulation of conformational and dynamic properties by site-directed mutation in the non-native state of hen egg white lysozyme.,published,journal,Biochemistry,Biochemistry,51,16,,,,,,,,,,,,,,,,,,,,,,3361,3372,2012, citations,entry_citation,18369,85492,1,,entry citation,,,22468860,,,Disentangling the coil: modulation of conformational and dynamic properties by site-directed mutation in the non-native state of hen egg white lysozyme.,published,journal,Biochemistry,Biochemistry,51,16,,,,,,,,,,,,,,,,,,,,,,3361,3372,2012, citations,entry_citation,18370,85507,1,,entry citation,,,22468860,,,Disentangling the coil: modulation of conformational and dynamic properties by site-directed mutation in the non-native state of hen egg white lysozyme.,published,journal,Biochemistry,Biochemistry,51,16,,,,,,,,,,,,,,,,,,,,,,3361,3372,2012, citations,entry_citation,18371,85522,1,,entry citation,,,23128140,,,Microtubule-binding sites of the CH domain of EB1 and its autoinhibition revealed by NMR.,published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1834,2,,,,,,,,,,,,,,,,,,,,,,499,507,2013, citations,citations,18372,85536,1,,entry citation,,,,,,"SOLUTION NMR STRUCTURE OF DE NOVO DESIGNED PROTEIN, P-LOOP NTPASE FOLD, NORTHEAST STRUCTURAL GENOMICS CONSORTIUM TARGET OR137",in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18373,85577,1,,entry citation,,,,,,Exchange,in preparation,journal,J. Am. Chem. Soc.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18374,85591,1,,entry citation,,,23074189,,,AIRE-PHD fingers are structural hubs to maintain the integrity of chromatin-associated interactome.,published,journal,Nucleic Acids Res.,Nucleic acids research,40,22,,,,,,,,,,,,,,,,,,,,,,11756,11768,2012, citations,entry_citation,18375,85612,1,,entry citation,,,,,,Solution structure of a putative S. aureus enzyme involved in the biosynthesis of staphyloxanthin,in preparation,BMRB only,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18376,85628,1,,entry citation,,,22932904,,,Regulation of the Plasmodium motor complex: phosphorylation of myosin A tail-interacting protein (MTIP) loosens its grip on MyoA.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,44,,,,,,,,,,,,,,,,,,,,,,36968,36977,2012, citations,entry_citation,18377,85643,1,,entry citation,,,22932904,,,Regulation of the Plasmodium motor complex: phosphorylation of myosin A tail-interacting protein (MTIP) loosens its grip on MyoA.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,44,,,,,,,,,,,,,,,,,,,,,,36968,36977,2012, citations,entry_citation,18378,85659,1,,entry citation,,,,,,unknown at present,in preparation,journal,unknown at present,unknown at present,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18379,85679,1,,entry citation,,,22593574,,,"Solution structure of the IIAChitobiose-HPr complex of the N,N'-diacetylchitobiose branch of the Escherichia coli phosphotransferase system.",published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,28,,,,,,,,,,,,,,,,,,,,,,23819,23829,2012, citations,entry_citation,18380,85701,1,,entry citation,,,22497251,,,"Solution NMR structure, backbone dynamics, and heme-binding properties of a novel cytochrome c maturation protein CcmE from Desulfovibrio vulgaris.",published,journal,Biochemistry,Biochemistry,51,18,,,,,,,,,,,,,,,,,,,,,,3705,3707,2012, citations,entry_citation,18381,85736,1,,entry citation,,,22782893,,,"Specialized Hsp70 Chaperone (HscA) Binds Preferentially to the Disordered Form, whereas J-protein (HscB) Binds Preferentially to the Structured Form of the Iron-Sulfur Cluster Scaffold Protein (IscU).",published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,37,,,,,,,,,,,,,,,,,,,,,,31406,31413,2012, citations,entry_citation,18385,85754,1,,entry citation,,,22493481,,,Characterization of Chromoshadow Domain-mediated Binding of Heterochromatin Protein 1 (HP1) to Histone H3.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,22,,,,,,,,,,,,,,,,,,,,,,18730,18737,2012, citations,entry_citation,18386,85769,1,,entry citation,,,22493481,,,Characterization of Chromoshadow Domain-mediated Binding of Heterochromatin Protein 1 (HP1) to Histone H3.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,22,,,,,,,,,,,,,,,,,,,,,,18730,18737,2012, citations,citations,18387,85784,1,,entry citation,,,,,,Solution structure of a thiol:disulfide interchange protein from Bacteroides sp.,in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,18388,85807,1,,entry citation,,,23356867,,,"Solution structure, dynamics and binding studies of a family 11 carbohydrate-binding module from Clostridium thermocellum (CtCBM11).",published,journal,Biochem. J.,The Biochemical journal,451,2,,,,,,,,,,,,,,,,,,,,,,289,300,2013, citations,citation_1,18389,85829,1,,entry citation,,,23356867,,,"Solution structure, dynamics and binding studies of a family 11 carbohydrate-binding module from Clostridium thermocellum (CtCBM11).",published,journal,Biochem. J.,The Biochemical journal,451,2,,,,,,,,,,,,,,,,,,,,,,289,300,2013, citations,entry_citation,1839,85852,1,,entry citation,,,,,"Satterlee, James D., Erman, James E., ""Proton NMR Assignments of Heme Contacts and Catalytically Implicated Amino Acids in Cyanide-Ligated Cytochrome c Peroxidase Determined from One- and Two-Dimensional Nuclear Overhauser Effects,"" Biochemistry 30 (18), 4398-4405 (1991).","Proton NMR Assignments of Heme Contacts and Catalytically Implicated Amino Acids in Cyanide-Ligated Cytochrome c Peroxidase Determined from One- and Two-Dimensional Nuclear Overhauser Effects",published,journal,Biochemistry,,30,18,,,,,,,,,,,,,,,,,,,,,,4398,4405,1991, citations,entry_citation,18390,85865,1,,entry citation,,,,,,Solution Structure of Fr822A from Drosophila melanogaster.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,18391,85887,1,,entry citation,,,22999958,,,Structural Basis for 5'-End-Specific Recognition of Single-Stranded DNA by the R3H Domain from Human Smubp-2,published,journal,J. Mol. Biol.,,12,,,,,,,,,,,,,,,,,,,,,,,760,767,2012, citations,entry_citation,18392,85909,1,,entry citation,,,22722931,,,Conformational Selection and Substrate Binding Regulate the Monomer/Dimer Equilibrium of the C-terminal domain of Escherichia coli Enzyme I.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,32,,,,,,,,,,,,,,,,,,,,,,26989,26998,2012, citations,entry_citation,18393,85926,1,,entry citation,,,23194006,,,Second double-stranded RNA binding domain of dicer-like ribonuclease 1: structural and biochemical characterization.,published,journal,Biochemistry,Biochemistry,51,51,,,,,,,,,,,,,,,,,,,,,,10159,10166,2012, citations,citations,18394,85947,1,,entry citation,,,,,,Solution structure of the uncharacterized thioredoxin-like protein BVU_1432 from Bacteroides vulgatus,in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18395,85969,1,,entry citation,,,22986689,,,Solid-state NMR analysis of membrane proteins and protein aggregates by proton detected spectroscopy.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,54,3,,,,,,,,,,,,,,,,,,,,,,291,305,2012, citations,entry_citation,18396,85986,1,,entry citation,,,22986689,,,Solid-state NMR analysis of membrane proteins and protein aggregates by proton detected spectroscopy.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,54,3,,,,,,,,,,,,,,,,,,,,,,291,305,2012, citations,entry_citation,18397,86001,1,,entry citation,,,22986689,,,Solid-state NMR analysis of membrane proteins and protein aggregates by proton detected spectroscopy.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,54,3,,,,,,,,,,,,,,,,,,,,,,291,305,2012, citations,entry_citation,18398,86016,1,,entry citation,,,23376100,,,"Solution Structure of the WNK1 Autoinhibitory Domain, a WNK-Specific PF2 Domain.",published,journal,J. Mol. Biol.,Journal of molecular biology,425,8,,,,,,,,,,,,,,,,,,,,,,1245,1252,2013, citations,entry_citation,18399,86033,1,,entry citation,,,,,,Solution structure of a ubiqutin-like protein from Trypanosoma bucei,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18400,86047,1,,entry citation,,,,,,Chaperones modulate RNA structural dynamics through anti-folding,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18403,86066,1,,entry citation,,,22841719,,,Competitive binding of UBPY and ubiquitin to the STAM2 SH3 domain revealed by NMR.,published,journal,FEBS Lett.,FEBS letters,586,19,,,,,,,,,,,,,,,,,,,,,,3379,3384,2012, citations,entry_citation,18404,86083,1,,entry citation,,,23184858,,,Solution structure of the recombinant target recognition domain of zoocin A.,published,journal,Proteins,Proteins,81,4,,,,,,,,,,,,,,,,,,,,,,722,727,2013, citations,entry_citation,18405,86111,1,,entry citation,,,,,,"Structure and biosynthesis of Sviceucin, an type I lasso peptide from Streptomyces sviceus",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18406,86125,1,,entry citation,,,23934139,,,Solid-state NMR sequential assignments of the amyloid core of Sup35pNM,published,journal,Biomol. NMR Assign.,,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,18407,86142,1,,entry citation,,,23943018,,,Solid-state NMR sequential assignments of the amyloid core of full-length Sup35p,published,journal,Biomol. NMR Assign.,,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,18408,86159,1,,entry citation,,,22615137,,,Structural insights into the transmembrane domains of human copper transporter 1.,published,journal,J. Pept. Sci.,Journal of peptide science : an official publication of the European Peptide Society,18,7,,,,,,,,,,,,,,,,,,,,,,449,455,2012, citations,entry_citation,18409,86173,1,,entry citation,,,22615137,,,Structural insights into the transmembrane domains of human copper transporter 1.,published,journal,J. Pept. Sci.,Journal of peptide science : an official publication of the European Peptide Society,18,7,,,,,,,,,,,,,,,,,,,,,,449,455,2012, citations,entry_citation,1841,86187,1,,entry citation,,,,,"Satterlee, James D., Erman, James E., ""Proton Hyperfine Resonance Assignments in Cyanide-ligated Cytochrome c Peroxidase Using the Nuclear Overhauser Effect,"" J. Biol. Chem. 262 (24), 11578-11583 (1987).","Proton Hyperfine Resonance Assignments in Cyanide-ligated Cytochrome c Peroxidase Using the Nuclear Overhauser Effect",published,journal,J. Biol. Chem.,,262,24,,,,,,,,,,,,,,,,,,,,,,11578,11583,1987, citations,entry_citation,18410,86200,1,,entry citation,,,22615137,,,Structural insights into the transmembrane domains of human copper transporter 1.,published,journal,J. Pept. Sci.,Journal of peptide science : an official publication of the European Peptide Society,18,7,,,,,,,,,,,,,,,,,,,,,,449,455,2012, citations,citations,18411,86214,1,,entry citation,,,,,,Solution structure of a putative protein disulfide isomerase from Bacteroides thetaiotaomicron,in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,18412,86238,1,,entry citation,,,22732408,,,High-definition NMR structure of PED/PEA-15 death effector domain reveals details of key polar side chain interactions,published,journal,Biochem. Biophys. Res. Commun.,,424,1,,,,,,,,,,,,,,,,,,,,,,141,146,2012, citations,apo-AdcR,18413,86252,1,,entry citation,,,23138857,,,Backbone and sterospecific methyl side chain resonance assignments of the homodimeric zinc sensor AdcR (32kDa) in the apo- and Zn(II)-bound states.,published,journal,Biomol. NMR Assignments,,8,1,,,,,,,,,,,,,,,,,,,,,,11,14,2014, citations,Zn-AdcR,18414,86268,1,,entry citation,,,23138857,,,Backbone and sterospecific methyl side chain resonance assignments of the homodimeric zinc sensor AdcR (32 kDa) in the apo- and Zn(II)-bound states.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,8,1,,,,,,,,,,,,,,,,,,,,,,11,14,2014, citations,citations,18415,86286,1,,entry citation,,,,,,Solution structure of human C-type lectin domain family 4 member D,in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18416,86309,1,,entry citation,,,22903788,,,"Backbone and side-chain resonance assignments (1H, 15N and 13C) of the ubiquitin homology domain of mouse BAG-1.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,2,,,,,,,,,,,,,,,,,,,,,,235,239,2013, citations,entry_citation,18417,86324,1,,entry citation,,,23179057,,,"1H, 13C and 15N resonance assignments of human BASP1.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,2,,,,,,,,,,,,,,,,,,,,,,315,319,2013, citations,MD_paper_LSV,18418,86339,1,,entry citation,,,,,,All Atom Simulations of the Initial Binding of Magainin and Pleurocidin to Membranes Comprising of a Mixture of Anionic and Zwitterionic Lipids,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18419,86357,1,,entry citation,,,23028322,,,Structure and assembly of a trans-periplasmic channel for type IV pili in Neisseria meningitidis.,published,journal,PLoS Pathog.,PLoS pathogens,8,9,,,,,,,,,,,,,,,,,,,,,,,,2012, citations,entry_citation,18420,86380,1,,entry citation,,,,,,All Atom Simulations of the Initial Binding of Magainin and Pleurocidin to Membranes Comprising a Mixture of Anionic and Zwitterionic Lipids,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18447,86930,1,,entry citation,,,24012479,,,High-resolution structural analysis shows how Tah1 tethers Hsp90 to the R2TP complex.,published,journal,Structure,"Structure (London, England : 1993)",21,10,,,,,,,,,,,,,,,,,,,,,,1834,1847,2013, citations,citation_eiavCA,18421,86398,1,,entry citation,,,23184932,,,The maturational refolding of the -hairpin motif of equine infectious anemia virus capsid protein extends its helix 1 at capsid assembly locus.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,3,,,,,,,,,,,,,,,,,,,,,,1511,1520,2013, citations,entry_citation,18422,86414,1,,entry citation,,,23999883,,,The 2/2 hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 with covalently attached heme: comparison of X-ray and NMR structures.,published,journal,Proteins,Proteins,82,3,,,,,,,,,,,,,,,,,,,,,,528,534,2014, citations,entry_citation,18423,86442,1,,entry citation,,,23999883,,,The 2/2 hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 with covalently attached heme: comparison of X-ray and NMR structures.,published,journal,Proteins,Proteins,82,3,,,,,,,,,,,,,,,,,,,,,,528,534,2014, citations,entry_citation,18424,86470,1,,entry citation,,,23999883,,,The 2/2 hemoglobin from the cyanobacterium Synechococcus sp. PCC 7002 with covalently attached heme: comparison of X-ray and NMR structures.,published,journal,Proteins,Proteins,82,3,,,,,,,,,,,,,,,,,,,,,,528,534,2014, citations,entry_citation,18425,86494,1,,entry citation,,,22825890,,,Resonance assignments of Ca2+-bound human S100A11.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,2,,,,,,,,,,,,,,,,,,,,,,211,214,2013, citations,entry_citation,18426,86511,1,,entry citation,,,22676969,,,Structural basis for the protective effect of the human prion protein carrying the dominant-negative E219K polymorphism.,published,journal,Biochem. J.,The Biochemical journal,446,2,,,,,,,,,,,,,,,,,,,,,,243,251,2012, citations,citation_1,18427,86530,1,,entry citation,,,22798499,,,The solution structure of double helical arabino nucleic acids (ANA and 2'F-ANA): effect of arabinoses in duplex-hairpin interconversion.,published,journal,Nucleic Acids Res.,Nucleic acids research,40,18,,,,,,,,,,,,,,,,,,,,,,9329,9339,2012, citations,entry_citation,18428,86552,1,,entry citation,,,23028322,,,Structure and assembly of a trans-periplasmic channel for type IV pili in Neisseria meningitidis.,published,journal,PLoS Pathog.,PLoS pathogens,8,9,,,,,,,,,,,,,,,,,,,,,,,,2012, citations,citations,18429,86568,1,,entry citation,,,,,,"Solution NMR Structure of a Denovo Design Four Helix Bundle Protein, Northeast Structural Genomics Consortium Target OR188",in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1843,86595,1,,entry citation,,,,,"Fairbrother, Wayne J., Walker, Philip A., Minard, Phillipe, Littlechild, Jennifer A., Watson, Herman C., Williams, Robert J. P., ""NMR analysis of site-specific mutants of yeast phosphoglycerate kinase An investigation of the triose-binding site,"" Eur. J. Biochem. 183, 57-67 (1989).","NMR analysis of site-specific mutants of yeast phosphoglycerate kinase An investigation of the triose-binding site",published,journal,Eur. J. Biochem.,,183,,,,,,,,,,,,,,,,,,,,,,,57,67,1989, citations,entry_citation,18430,86608,1,,entry citation,,,22928555,,,"Structure and stability of duplex DNA containing (5'S)-5',8-cyclo-2'-deoxyadenosine: an oxidatively generated lesion repaired by NER.",published,journal,Chem. Res. Toxicol.,Chemical research in toxicology,25,10,,,,,,,,,,,,,,,,,,,,,,2103,2111,2012, citations,entry_citation,18431,86634,1,,entry citation,,,22700975,,,Multifaceted recognition of vertebrate Rev1 by translesion polymerases and .,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,31,,,,,,,,,,,,,,,,,,,,,,26400,26408,2012, citations,entry_citation,18432,86654,1,,entry citation,,,23220741,,,Insights into the regulation of human Rev1 for translesion synthesis polymerases revealed by the structural studies on its polymerase-interacting domain.,published,journal,J. Mol. Cell Biol.,Journal of molecular cell biology,5,3,,,,,,,,,,,,,,,,,,,,,,204,206,2013, citations,entry_citation,18433,86669,1,,entry citation,,,22700975,,,Multifaceted recognition of vertebrate Rev1 by translesion polymerases and .,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,31,,,,,,,,,,,,,,,,,,,,,,26400,26408,2012, citations,entry_citation,18434,86689,1,,entry citation,,,22691049,,,NMR structure and dynamics of the C-terminal domain from human Rev1 and its complex with Rev1 interacting region of DNA polymerase .,published,journal,Biochemistry,Biochemistry,51,27,,,,,,,,,,,,,,,,,,,,,,5506,5520,2012, citations,entry_citation,18435,86709,1,,entry citation,,,22705372,,,Structural basis for telomerase RNA recognition and RNP assembly by the holoenzyme La family protein p65.,published,journal,Mol. Cell,Molecular cell,47,1,,,,,,,,,,,,,,,,,,,,,,16,26,2012, citations,entry_citation,18437,86729,1,,entry citation,,,22801427,,,Structural and biochemical characterization of phage FI protein (gpFI) reveals a novel mechanism of DNA packaging chaperone activity.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,38,,,,,,,,,,,,,,,,,,,,,,32085,32095,2012, citations,citations,18438,86747,1,,entry citation,,,,,,"Solution NMR Structure of the Globular Domain of Human Histone H1x, Northeast Structural Genomics Consortium (NESG) Target HR7057A",in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18439,86778,1,,entry citation,,,22645123,,,Down-regulation of NF-B transcriptional activity in HIV-associated kidney disease by BRD4 inhibition.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,34,,,,,,,,,,,,,,,,,,,,,,28840,28851,2012, citations,entry_citation,1844,86807,1,,entry citation,,,,,"Fairbrother, Wayne J., Walker, Philip A., Minard, Phillipe, Littlechild, Jennifer A., Watson, Herman C., Williams, Robert J. P., ""NMR analysis of site-specific mutants of yeast phosphoglycerate kinase An investigation of the triose-binding site,"" Eur. J. Biochem. 183, 57-67 (1989).","NMR analysis of site-specific mutants of yeast phosphoglycerate kinase An investigation of the triose-binding site",published,journal,Eur. J. Biochem.,,183,,,,,,,,,,,,,,,,,,,,,,,57,67,1989, citations,citations,18440,86820,1,,entry citation,,,,,,Not applicable,in preparation,journal,To be Published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18441,86837,1,,entry citation,,,22879593,,,Large protein assemblies formed by multivalent interactions between cadherin23 and harmonin suggest a stable anchorage structure at the tip link of stereocilia.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,40,,,,,,,,,,,,,,,,,,,,,,33460,33471,2012, citations,citations,18442,86854,1,,entry citation,,,23143233,,,Solution structure of the cold-shock-like protein from Rickettsia rickettsii.,published,journal,Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.,"Acta crystallographica. Section F, Structural biology and crystallization communications",68,Pt 11,,,,,,,,,,,,,,,,,,,,,,1284,1288,2012, citations,citations,18443,86873,1,,entry citation,,,,,,Solution structure of a thioredoxin from Thermus thermophilus,in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18445,86897,1,,entry citation,,,24012479,,,High-resolution structural analysis shows how Tah1 tethers Hsp90 to the R2TP complex.,published,journal,Structure,"Structure (London, England : 1993)",21,10,,,,,,,,,,,,,,,,,,,,,,1834,1847,2013, citations,entry_citation,18446,86916,1,,entry citation,,,22836948,,,"Backbone 1H, 13C and 15N resonance assignments of an intrinsically unstructured -crystallin from Hahella chejuensis.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,2,,,,,,,,,,,,,,,,,,,,,,221,224,2013, citations,entry_citation,18448,86951,1,,entry citation,,,23241245,,,NIPP1 maintains EZH2 phosphorylation and promoter occupancy at proliferation-related target genes,published,journal,Nucleic Acids Res.,,41,2,,,,,,,,,,,,,,,,,,,,,,842,854,2013, citations,citation_1,18449,86967,1,,entry citation,,,22977233,,,"Structure, sulfatide binding properties, and inhibition of platelet aggregation by a disabled-2 protein-derived peptide.",published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,45,,,,,,,,,,,,,,,,,,,,,,37691,37702,2012, citations,entry_citation,1845,86983,1,,entry citation,,,,,"Fairbrother, Wayne J., Walker, Philip A., Minard, Phillipe, Littlechild, Jennifer A., Watson, Herman C., Williams, Robert J. P., ""NMR analysis of site-specific mutants of yeast phosphoglycerate kinase An investigation of the triose-binding site,"" Eur. J. 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Biol. Chem.,The Journal of biological chemistry,287,48,,,,,,,,,,,,,,,,,,,,,,40493,40501,2012, citations,Collagelin_NMR,18537,88618,1,,entry citation,,,,,,Collagelin 1H and 13C NMR data,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18538,88633,1,,entry citation,,,,,,1H and 13C NMR of GPVI mimetic,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18539,88648,1,,entry citation,,,22763700,,,NMR structure of Carcinoscorpius rotundicauda thioredoxin related protein 16 and its role in regulating transcription factor NF-kB activity,published,journal,J. Biol. Chem.,,287,35,,,,,,,,,,,,,,,,,,,,,,29417,29428,2012, citations,entry_citation,1854,88667,1,,entry citation,,,,,"Uchida, Kenichi, Miyake, Yoko, Kainosho, Masatsune, ""Reductive cleavage and regeneration of the disulfide bonds in Streptomyces subtilisin inhibitor (SSI) as studied by the carbonyl 13C NMR resonances of cysteinyl residues,"" J. Biomol. NMR 1 (1), 49-64 (1991).","Reductive cleavage and regeneration of the disulfide bonds in Streptomyces subtilisin inhibitor (SSI) as studied by the carbonyl 13C NMR resonances of cysteinyl residues",published,journal,J. Biomol. NMR,,1,1,,,,,,,,,,,,,,,,,,,,,,49,64,1991, citations,citations,18540,88680,1,,entry citation,,,23418741,,,Structure-function analysis of full-length midkine reveals novel residues important for heparin binding and zebrafish embryogenesis.,published,journal,Biochem. J.,The Biochemical journal,451,3,,,,,,,,,,,,,,,,,,,,,,407,415,2013, citations,entry_citation,18541,88700,1,,entry citation,,,23418741,,,Structure-function analysis of full-length midkine reveals novel residues important for heparin binding and zebrafish embryogenesis.,published,journal,Biochem. J.,The Biochemical journal,451,3,,,,,,,,,,,,,,,,,,,,,,407,415,2013, citations,entry_citation,18542,88717,1,,entry citation,,,22844534,,,Structure and binding interface of the cytosolic tails of X2 integrin.,published,journal,PLoS ONE,PloS one,7,7,,,,,,,,,,,,,,,,,,,,,,e41924,e41924,2012, citations,entry_citation,18543,88734,1,,entry citation,,,23527473,,,Solid-State NMR Study of a 41 kDa Membrane Protein Complex DsbA/DsbB.,published,journal,J. Phys. Chem. B,The journal of physical chemistry. B,117,20,,,,,,,,,,,,,,,,,,,,,,6052,6060,2013, citations,entry_citation,18544,88751,1,,entry citation,,,23527473,,,Solid-State NMR Study of a 41 kDa Membrane Protein Complex DsbA/DsbB.,published,journal,J. Phys. Chem. B,The journal of physical chemistry. B,117,20,,,,,,,,,,,,,,,,,,,,,,6052,6060,2013, citations,citation,18545,88769,1,,entry citation,,,,,,Solution structure of human holo-S100A1 C85M mutant,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18546,88802,1,,entry citation,,,23613586,,,Structural analysis of Stc1 provides insights into the coupling of RNAi and chromatin modification.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,110,21,,,,,,,,,,,,,,,,,,,,,,E1879,E1888,2013, citations,citations,18547,88824,1,,entry citation,,,,,,"Solution NMR Structure of CalU16 from Micromonospora echinospora, Northeast Structural Genomics Consortium (NESG) Target MiR12",in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18548,88854,1,,entry citation,,,23793605,,,Solution structure of monomeric human FAM96A,published,journal,J. Biomol. NMR,,56,4,,,,,,,,,,,,,,,,,,,,,,387,392,2013, citations,entry_citation,18549,88870,1,,entry citation,,,,,,Solution Structure of Helix-35 Stem-loop from E. coli 23S rRNA,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1855,88891,1,,entry citation,,,,,"Uchida, Kenichi, Miyake, Yoko, Kainosho, Masatsune, ""Reductive cleavage and regeneration of the disulfide bonds in Streptomyces subtilisin inhibitor (SSI) as studied by the carbonyl 13C NMR resonances of cysteinyl residues,"" J. Biomol. NMR 1 (1), 49-64 (1991).","Reductive cleavage and regeneration of the disulfide bonds in Streptomyces subtilisin inhibitor (SSI) as studied by the carbonyl 13C NMR resonances of cysteinyl residues",published,journal,J. Biomol. NMR,,1,1,,,,,,,,,,,,,,,,,,,,,,49,64,1991, citations,entry_citation,18550,88904,1,,entry citation,,,22947063,,,Structural Rearrangements at Physiological pH: Nuclear Magnetic Resonance Insights from the V210I Human Prion Protein Mutant.,published,journal,Biochemistry,Biochemistry,51,38,,,,,,,,,,,,,,,,,,,,,,7465,7474,2012, citations,Solution_NMR_structure_of_HR7614B,18551,88919,1,,entry citation,,,,,,"Solution NMR structure of C2H2-type Zinc-fingers 4 and 5 from human Insulinoma-associated protein 1 (fragment 424-497), Northeast Structural Genomics Consortium Target HR7614B.",in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18552,88954,1,,entry citation,,,23065337,,,"1H, 13C, and 15N backbone resonance assignments of the connexin43 carboxyl terminal domain attached to the 4th transmembrane domain in detergent micelles.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,2,,,,,,,,,,,,,,,,,,,,,,299,303,2013, citations,citations,18553,88971,1,,entry citation,,,22810234,,,The zinc regulated antivirulence pathway of Salmonella is a multiprotein immunoglobulin adhesion system.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,39,,,,,,,,,,,,,,,,,,,,,,32324,32337,2012, citations,entry_citation,18555,88991,1,,entry citation,,,,,,"NMR solution structure of PA1075, an essential protein in Pseudomonas Aeruginosa",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18556,89011,1,,entry citation,,,22908850,,,Contrast-matched small-angle X-ray scattering from a heavy-atom-labeled protein in structure determination: application to a lead-substituted calmodulin-peptide complex.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,134,36,,,,,,,,,,,,,,,,,,,,,,14686,14689,2012, citations,entry_citation,18557,89034,1,,entry citation,,,22989873,,,Solution NMR structure of the Ca2+-bound N-terminal domain of CaBP7: a regulator of golgi trafficking.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,45,,,,,,,,,,,,,,,,,,,,,,38231,38243,2012, citations,entry_citation,18559,89088,1,,entry citation,,,24130829,,,Solution NMR structure and histone binding of the PHD domain of human MLL5.,published,journal,PLoS ONE,PloS one,8,10,,,,,,,,,,,,,,,,,,,,,,e77020,e77020,2013, citations,entry_citation,1856,89111,1,,entry citation,,,,,"Uchida, Kenichi, Miyake, Yoko, Kainosho, Masatsune, ""Reductive cleavage and regeneration of the disulfide bonds in Streptomyces subtilisin inhibitor (SSI) as studied by the carbonyl 13C NMR resonances of cysteinyl residues,"" J. Biomol. NMR 1 (1), 49-64 (1991).","Reductive cleavage and regeneration of the disulfide bonds in Streptomyces subtilisin inhibitor (SSI) as studied by the carbonyl 13C NMR resonances of cysteinyl residues",published,journal,J. Biomol. NMR,,1,1,,,,,,,,,,,,,,,,,,,,,,49,64,1991, citations,entry_citation,18560,89124,1,,entry citation,,,,,,NMR solution structure of the N-terminal domain of human USP28,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,18561,89148,1,,entry citation,,,23135467,,,Principles for designing ideal protein structures,published,journal,Nature,,491,7423,,,,,,,,,,,,,,,,,,,,,,222,227,2012, citations,entry_citation_1,18562,89176,1,,entry citation,,,23765285,,,Backbone and side-chain assignments of an effector membrane localization domain from Vibrio vulnificus MARTX toxin.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,citations,18563,89191,1,,entry citation,,,,,,"Solution NMR Structure of Ig like domain (805-892) of Obscurin-like protein 1 from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR8578K",in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18565,89221,1,,entry citation,,,23765284,,,Backbone and side-chain resonance assignments of the membrane localization domain from Pasteurella multocida toxin.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,8,1,,,,,,,,,,,,,,,,,,,,,,221,224,2014, citations,entry_citation,18566,89236,1,,entry citation,,,22987227,,,NMR assignments for the telokin-like domain of bacteriophage P22 coat protein.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,2,,,,,,,,,,,,,,,,,,,,,,257,260,2013, citations,entry_citation,18567,89256,1,,entry citation,,,23266947,,,"H, 13C and 15N resonance assignments of S114A mutant of UVI31+ from Chlamydomonas reinhardtii.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,8,1,,,,,,,,,,,,,,,,,,,,,,71,74,2014, citations,entry_citation,18568,89270,1,,entry citation,,,,,,Aminoterminal Amphipathic alpha-Helix AH1 of Hepatitis C Virus Nonstructural Protein 4B Possesses a Dual Role in RNA Replication and Virus Production,accepted,journal,PLOS Pathogens,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18569,89287,1,,entry citation,,,10990454,10.1093/emboj/19.18.4903,,Dual epitope recognition by the VASP EVH1 domain modulates polyproline ligand specificity and binding affinity,published,journal,EMBO J.,,19,18,,,,,,,,,,,,,,,,,,,,,,4903,4914,2000, citations,entry_citation,1857,89312,1,,entry citation,,,,,"Uchida, Kenichi, Miyake, Yoko, Kainosho, Masatsune, ""Reductive cleavage and regeneration of the disulfide bonds in Streptomyces subtilisin inhibitor (SSI) as studied by the carbonyl 13C NMR resonances of cysteinyl residues,"" J. Biomol. NMR 1 (1), 49-64 (1991).","Reductive cleavage and regeneration of the disulfide bonds in Streptomyces subtilisin inhibitor (SSI) as studied by the carbonyl 13C NMR resonances of cysteinyl residues",published,journal,J. Biomol. NMR,,1,1,,,,,,,,,,,,,,,,,,,,,,49,64,1991, citations,entry_citation,18570,89325,1,,entry citation,,,23326363,,,Solution structure of an archaeal DNA binding protein with an eukaryotic zinc finger fold,published,journal,PLoS One,,8,1,,,,,,,,,,,,,,,,,,,,,,e52908,e52908,2013, citations,citation1,18571,89350,1,,entry citation,,,23011803,,,"Solution structures of polcalcin Phl p 7 in three ligation states: Apo-, hemi-Mg(2+) -bound, and fully Ca(2+) -bound.",published,journal,Proteins,Proteins,81,2,,,,,,,,,,,,,,,,,,,,,,300,315,2013, citations,citation_1,18572,89368,1,,entry citation,,,23011803,,,"Solution structures of polcalcin Phl p 7 in three ligation states: Apo-, hemi-Mg(2+) -bound, and fully Ca(2+) -bound.",published,journal,Proteins,Proteins,81,2,,,,,,,,,,,,,,,,,,,,,,300,315,2013, citations,citation1,18573,89388,1,,entry citation,,,23011803,,,"Solution structures of polcalcin Phl p 7 in three ligation states: Apo-, hemi-Mg(2+) -bound, and fully Ca(2+) -bound.",published,journal,Proteins,Proteins,81,2,,,,,,,,,,,,,,,,,,,,,,300,315,2013, citations,entry_citation,18574,89408,1,,entry citation,,,22267088,,,Biophysical characterization of mutants of Bacillus subtilis lipase evolved for thermostability: factors contributing to increased activity retention.,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,21,4,,,,,,,,,,,,,,,,,,,,,,487,497,2012, citations,entry_citation,18575,89425,1,,entry citation,,,22267088,,,Biophysical characterization of mutants of Bacillus subtilis lipase evolved for thermostability: factors contributing to increased activity retention.,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,21,4,,,,,,,,,,,,,,,,,,,,,,487,497,2012, citations,entry_citation,18576,89441,1,,entry citation,,,22827601,,,The role of individual carbohydrate-binding sites in the function of the potent anti-HIV lectin griffithsin.,published,journal,Mol. Pharm.,Molecular pharmaceutics,9,9,,,,,,,,,,,,,,,,,,,,,,2613,2625,2012, citations,Citation_1,18577,89455,1,,entry citation,,,23070843,,,Chemical shift assignments of the connexin45 carboxyl terminal domain: monomer and dimer conformations.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,2,,,,,,,,,,,,,,,,,,,,,,293,297,2013, citations,entry_citation,18578,89470,1,,entry citation,,,23070843,,,Chemical shift assignments of the connexin45 carboxyl terminal domain: monomer and dimer conformations.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,2,,,,,,,,,,,,,,,,,,,,,,293,297,2013, citations,entry_citation,18579,89485,1,,entry citation,,,,,,Methylated Histone Complex,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1858,89512,1,,entry citation,,,,,"Uchida, Kenichi, Miyake, Yoko, Kainosho, Masatsune, ""Reductive cleavage and regeneration of the disulfide bonds in Streptomyces subtilisin inhibitor (SSI) as studied by the carbonyl 13C NMR resonances of cysteinyl residues,"" J. Biomol. NMR 1 (1), 49-64 (1991).","Reductive cleavage and regeneration of the disulfide bonds in Streptomyces subtilisin inhibitor (SSI) as studied by the carbonyl 13C NMR resonances of cysteinyl residues",published,journal,J. Biomol. NMR,,1,1,,,,,,,,,,,,,,,,,,,,,,49,64,1991, citations,entry_citation,18580,89525,1,,entry citation,,,23179058,,,"1H, 13C, and 15N backbone and side chain resonance assignments of the C-terminal DNA binding and dimerization domain of v-Myc.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,2,,,,,,,,,,,,,,,,,,,,,,321,324,2013, citations,Solution_structure_of_gp78CUE_domain,18581,89539,1,,entry citation,,,23123110,,,Promiscuous interactions of gp78 E3 ligase CUE domain with polyubiquitin chains.,published,journal,Structure,"Structure (London, England : 1993)",20,12,,,,,,,,,,,,,,,,,,,,,,2138,2150,2012, citations,Solution_structure_of_gp78CUE-Ub_complex,18582,89558,1,,entry citation,,,23123110,,,Promiscuous interactions of gp78 E3 ligase CUE domain with polyubiquitin chains.,published,journal,Structure,"Structure (London, England : 1993)",20,12,,,,,,,,,,,,,,,,,,,,,,2138,2150,2012, citations,entry_citation,18583,89578,1,,entry citation,,,23123110,,,Promiscuous interactions of gp78 E3 ligase CUE domain with polyubiquitin chains.,published,journal,Structure,"Structure (London, England : 1993)",20,12,,,,,,,,,,,,,,,,,,,,,,2138,2150,2012, citations,entry_citation,18584,89598,1,,entry citation,,,23123110,,,Promiscuous interactions of gp78 E3 ligase CUE domain with polyubiquitin chains.,published,journal,Structure,"Structure (London, England : 1993)",20,12,,,,,,,,,,,,,,,,,,,,,,2138,2150,2012, citations,GRFT_assignment,18585,89619,1,,entry citation,,,22827601,,,The role of individual carbohydrate-binding sites in the function of the potent anti-HIV lectin griffithsin.,published,journal,Mol. Pharm.,Molecular pharmaceutics,9,9,,,,,,,,,,,,,,,,,,,,,,2613,2625,2012, citations,entry_citation,18586,89633,1,,entry citation,,,22986688,,,NMR structure note: solution structure of human Miz-1 zinc fingers 8 to 10.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,54,3,,,,,,,,,,,,,,,,,,,,,,317,323,2012, citations,entry_citation,18587,89654,1,,entry citation,,,23302895,,,Solution Structure of Mouse Hepatitis Virus (MHV) nsp3a and Determinants of the Interaction with MHV Nucleocapsid (N) Protein.,published,journal,J. Virol.,Journal of virology,87,6,,,,,,,,,,,,,,,,,,,,,,3502,3515,2013, citations,citation_1,18588,89674,1,,entry citation,,,22960997,,,3D-TROSY-based backbone and ILV-methyl resonance assignments of a 319-residue homodimer from a single protein sample.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,54,2,,,,,,,,,,,,,,,,,,,,,,135,143,2012, citations,citation_1,18589,89688,1,,entry citation,,,23325851,,,Solution properties of the archaeal CRISPR DNA repeat-binding homeodomain protein Cbp2.,published,journal,Nucleic Acids Res.,Nucleic acids research,41,5,,,,,,,,,,,,,,,,,,,,,,3424,3435,2013, citations,entry_citation,1859,89708,1,,entry citation,,,,,"Uchida, Kenichi, Miyake, Yoko, Kainosho, Masatsune, ""Reductive cleavage and regeneration of the disulfide bonds in Streptomyces subtilisin inhibitor (SSI) as studied by the carbonyl 13C NMR resonances of cysteinyl residues,"" J. Biomol. NMR 1 (1), 49-64 (1991).","Reductive cleavage and regeneration of the disulfide bonds in Streptomyces subtilisin inhibitor (SSI) as studied by the carbonyl 13C NMR resonances of cysteinyl residues",published,journal,J. Biomol. NMR,,1,1,,,,,,,,,,,,,,,,,,,,,,49,64,1991, citations,entry_citation,18590,89721,1,,entry citation,,,23129767,,,Functional and structural insights of a Staphylococcus aureus apoptotic-like membrane peptide from a toxin-antitoxin module.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,52,,,,,,,,,,,,,,,,,,,,,,43454,43463,2012, citations,entry_citation,18591,89739,1,,entry citation,,,23205845,,,The coil-to-helix transition in IlvN regulates the allosteric control of Escherichia coli acetohydroxyacid synthase I,published,journal,Biochemistry,Biochemistry,52,1,,,,,,,,,,,,,,,,,,,,,,70,83,2013, citations,citations,18592,89764,1,,entry citation,,,23609449,,,"Structure of the Lectin Mannose 6-Phosphate Receptor Homology (MRH) Domain of Glucosidase II, an Enzyme That Regulates Glycoprotein Folding Quality Control in the Endoplasmic Reticulum.",published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,23,,,,,,,,,,,,,,,,,,,,,,16460,16475,2013, citations,entry_citation,18593,89783,1,,entry citation,,,23455628,,,The biolabile 2'-O-pivaloyloxymethyl modification in an RNA helix: an NMR solution structure,published,journal,Org. Biomol. Chem.,,11,16,,,,,,,,,,,,,,,,,,,,,,2638,2647,2013, citations,entry_citation,18595,89803,1,,entry citation,,,22983928,,,Solid-state NMR 13C and 15N resonance assignments of a seven-transmembrane helical protein Anabaena Sensory Rhodopsin,published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,7,2,,1874-270X,,,,,,,,,,,,,,,,,,,,253,256,2013, citations,entry_citation,18596,89822,1,,entry citation,,,23025322,,,Insights into the glycosaminoglycan-mediated cytotoxic mechanism of eosinophil cationic protein revealed by NMR,published,journal,ACS Chem. Biol.,,8,1,,,,,,,,,,,,,,,,,,,,,,144,151,2013, citations,citation_1,18598,89842,1,,entry citation,,,23181972,,,Identification of a hydrophobic cleft in the LytTR domain of AgrA as a locus for small molecule interactions that inhibit DNA binding.,published,journal,Biochemistry,Biochemistry,51,50,,,,,,,,,,,,,,,,,,,,,,10035,10043,2012, citations,entry_citation,18599,89859,1,,entry citation,,,23017427,,,"Solution structure of CCP modules 10-12 illuminates functional architecture of the complement regulator, factor H.",published,journal,J. Mol. Biol.,Journal of molecular biology,424,5,,,,,,,,,,,,,,,,,,,,,,295,312,2012, citations,entry_citation,186,89886,1,,entry citation,,,,,"King, Garry C., Wright, Peter E., ""Proton NMR Studies of Plastocyanin: Assignment of Aromatic and Methyl Group Resonances from Two-Dimensional Spectra,"" Biochemistry 25, 2364-2374 (1986).","Proton NMR Studies of Plastocyanin: Assignment of Aromatic and Methyl Group Resonances from Two-Dimensional Spectra",published,journal,Biochemistry,,25,,,,,,,,,,,,,,,,,,,,,,,2364,2374,1986, citations,entry_citation,18600,89899,1,,entry citation,,,23342149,,,Solution Structures of Two Homologous Venom Peptides from Sicarius dolichocephalus.,published,journal,PLoS ONE,PloS one,8,1,,,,,,,,,,,,,,,,,,,,,,e54401,e54401,2013, citations,entry_citation,18601,89969,1,,entry citation,,,,,,GGBP free solution structure,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18602,89989,1,,entry citation,,,23431276,,,Discovery of a Siderophore Export System Essential for Virulence of Mycobacterium tuberculosis,published,journal,Plos Pathog.,,9,1,,,,,,,,,,,,,,,,,,,,,,e1003120,e1003120,2013, citations,entry_citation,18603,90012,1,,entry citation,,,23148479,,,Carbohydrate affinity for the glucose-galactose binding protein is regulated by allosteric domain motions,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,134,48,,1520-5126,,,,,,,,,,,,,,,,,,,,19869,19876,2012, citations,entry_citation,18604,90033,1,,entry citation,,,23017427,,,"Solution structure of CCP modules 10-12 illuminates functional architecture of the complement regulator, factor H.",published,journal,J. Mol. Biol.,Journal of molecular biology,424,5,,,,,,,,,,,,,,,,,,,,,,295,312,2012, citations,citations,18605,90058,1,,entry citation,,,,,,"Solution NMR Structure of Human Transcription Elongation Factor A protein 2, Central Domain",in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18606,90085,1,,entry citation,,,23242138,,,Bacteriophage genes that inactivate the CRISPR/Cas bacterial immune system.,published,journal,Nature,Nature,493,7432,,,,,,,,,,,,,,,,,,,,,,429,432,2013, citations,entry_citation,18607,90102,1,,entry citation,,,23334361,,,Solution structure of the Magnaporthe oryzae avirulence protein AvrPiz-t.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,55,2,,,,,,,,,,,,,,,,,,,,,,219,223,2013, citations,entry_citation,18608,90119,1,,entry citation,,,23066025,,,Multiple binding sites on the pyrin domain of ASC protein allow self-association and interaction with NLRP3 protein.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,287,50,,,,,,,,,,,,,,,,,,,,,,41732,41743,2012, citations,entry_citation,18609,90138,1,,entry citation,,,23148479,,,Carbohydrate affinity for the glucose-galactose binding protein is regulated by allosteric domain motions.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,134,48,,,,,,,,,,,,,,,,,,,,,,19869,19876,2012, citations,entry_citation,18610,90157,1,,entry citation,,,23284170,,,High-pressure NMR reveals close similarity between cold and alcohol protein denaturation in ubiquitin.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,110,5,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,18611,90175,1,,entry citation,,,23284170,,,High-pressure NMR reveals close similarity between cold and alcohol protein denaturation in ubiquitin.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,110,5,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,18612,90190,1,,entry citation,,,,,,NMR solution structure of human HisRS splice variant,in preparation,journal,Structure,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation1,18613,90204,1,,entry citation,,,22277260,,,"Protein dynamics at Eph receptor-ligand interfaces as revealed by crystallography, NMR and MD simulations.",published,journal,BMC Biophys.,BMC biophysics,5,,,,,,,,,,,,,,,,,,,,,,,2,2,2012, citations,citation_2,18613,90205,2,,reference citation,,,,,,NMR solution structure of Eph receptor,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18614,90219,1,,entry citation,,,23012428,,,Antiparallel coiled-coil-mediated dimerization of myosin X.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,109,43,,,,,,,,,,,,,,,,,,,,,,17388,17393,2012, citations,entry_citation,18615,90237,1,,entry citation,,,23179059,,,"1H, 13C and 15N resonance assignments of human parvulin 17",published,journal,Biomol. NMR Assign.,,7,2,,,,,,,,,,,,,,,,,,,,,,325,329,2013, citations,entry_citation,18616,90255,1,,entry citation,,,27003380,10.1016/j.jmr.2016.02.016,,Spectral density mapping at multiple magnetic fields suitable for (13)C NMR relaxation studies,published,journal,J. Magn. Reson.,"Journal of magnetic resonance (San Diego, Calif. : 1997)",266,,,1096-0856,,,,,,,,,,,,,,,,,,,,23,40,2016, citations,entry_citation,18617,90286,1,,entry citation,,,23169643,,,"pH-triggered, activated-state conformations of the influenza hemagglutinin fusion peptide revealed by NMR",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,109,49,,,,,,,,,,,,,,,,,,,,,,19994,19999,2012, citations,entry_citation,18618,90312,1,,entry citation,,,23853587,,,Structure and function of a fungal adhesin that binds heparin and mimics thrombospondin-1 by blocking T cell activation and effector function.,published,journal,PLoS Pathog.,PLoS pathogens,9,7,,,,,,,,,,,,,,,,,,,,,,e1003464,e1003464,2013, citations,menk-suv-dmpc,18619,90328,1,,entry citation,,,,,,Menk in DMPC SUV,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18620,90341,1,,entry citation,,,23239108,,,"H, 15N, 13C assignment and secondary structure determination of two domains of La protein from D. discoideum.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,8,1,,,,,,,,,,,,,,,,,,,,,,47,51,2014, citations,entry_citation,18621,90357,1,,entry citation,,,23239108,,,"H, 15N, 13C assignment and secondary structure determination of two domains of La protein from D. discoideum.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,8,1,,,,,,,,,,,,,,,,,,,,,,47,51,2014, citations,entry_citation,18622,90373,1,,entry citation,,,23063562,,,Structure and dynamics of the second CARD of human RIG-I provide mechanistic insights into regulation of RIG-I activation.,published,journal,Structure,"Structure (London, England : 1993)",20,12,,,,,,,,,,,,,,,,,,,,,,2048,2061,2012, citations,entry_citation,18623,90394,1,,entry citation,,,23063562,,,Structure and dynamics of the second CARD of human RIG-I provide mechanistic insights into regulation of RIG-I activation.,published,journal,Structure,"Structure (London, England : 1993)",20,12,,,,,,,,,,,,,,,,,,,,,,2048,2061,2012, citations,entry_citation,18624,90414,1,,entry citation,,,,,,Solution structure of N-terminal domain of a plant glutaredoxin,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18625,90431,1,,entry citation,,,23355266,,,Molecular basis for sequence-dependent induced DNA bending.,published,journal,Chembiochem,Chembiochem : a European journal of chemical biology,14,3,,,,,,,,,,,,,,,,,,,,,,323,331,2013, citations,entry_citation,18626,90449,1,,entry citation,,,23355266,,,Molecular basis for sequence-dependent induced DNA bending.,published,journal,Chembiochem,Chembiochem : a European journal of chemical biology,14,3,,,,,,,,,,,,,,,,,,,,,,323,331,2013, citations,entry_citation,18627,90468,1,,entry citation,,,23250791,,,"H, 13C, and 15N chemical shift assignments of neuronal calcium sensor protein, hippocalcin.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,8,1,,,,,,,,,,,,,,,,,,,,,,63,66,2014, citations,entry_citation,18628,90487,1,,entry citation,,,23138858,,,"1H, 13C, and 15N backbone and side chain resonance assignments of thermophilic Geobacillus kaustophilus cyclophilin-A.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2012, citations,entry_citation,18629,90518,1,,entry citation,,,23630290,,,In silico discovery of small-molecule Ras inhibitors that display antitumor activity by blocking the Ras-effector interaction,published,journal,Proc. Natl. Acad. Sci. U. S. A.,,110,20,,,,,,,,,,,,,,,,,,,,,,8182,8187,2013, citations,entry_citation,18630,90545,1,,entry citation,,,23207295,,,An intrinsically disordered domain has a dual function coupled to compartment-dependent redox control.,published,journal,J. Mol. Biol.,Journal of molecular biology,425,3,,,,,,,,,,,,,,,,,,,,,,594,608,2013, citations,entry_citation,18631,90561,1,,entry citation,,,23207295,,,An intrinsically disordered domain has a dual function coupled to compartment-dependent redox control.,published,journal,J. Mol. Biol.,Journal of molecular biology,425,3,,,,,,,,,,,,,,,,,,,,,,594,608,2013, citations,entry_citation,18632,90577,1,,entry citation,,,23225165,,,"Resonance assignment of As-p18, a fatty acid binding protein secreted by developing larvae of the parasitic nematode Ascaris suum.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,8,1,,,,,,,,,,,,,,,,,,,,,,33,36,2014, citations,citations,18633,90614,1,,entry citation,,,24247110,,,A novel small-molecule binds to the influenza A virus RNA promoter and inhibits viral replication.,published,journal,Chem. Commun. 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Chem.,The Journal of biological chemistry,289,33,,1083-351X,,,,,,,,,,,,,,,,,,,,22969,22979,2014, citations,entry_citation,18636,90661,1,,entry citation,,,23070845,,,"1H, 13C and 15N resonance assignment of the soluble form of the Lipid-modified Azurin from Neisseria gonorrhoeae.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,2,,,,,,,,,,,,,,,,,,,,,,311,314,2013, citations,entry_citation,18637,90684,1,,entry citation,,,23179061,,,"H, 13C and 15N chemical shift assignments of Na-FAR-1, a helix-rich fatty acid and retinol binding protein of the parasitic nematode Necator americanus.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,8,1,,,,,,,,,,,,,,,,,,,,,,19,21,2014, citations,entry_citation,18638,90716,1,,entry citation,,,22897814,,,Solution Structure of Duplex DNA Containing a b-Carba-Fapy-dG Lesion,published,journal,Chem. Res. 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Biol.,Nature structural & molecular biology,19,12,,,,,,,,,,,,,,,,,,,,,,1282,1286,2012, citations,reference_citation,18702,91909,2,,reference citation,,,,,,THE STRUCTURE OF THE C-TERMINAL KH DOMAINS OF KSRP REVEALS A NONCANONICAL MOTIF IMPORTANT FOR MRNA DEGRADATION,in preparation,journal,Structure,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18703,91932,1,,entry citation,,,23373469,,,Reversible phenol oxidation-reduction in the structurally well-defined 2-mercaptophenol-3C protein.,published,journal,Biochemistry,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,reference_citation_1,18703,91933,2,,reference citation,,,22675121,,,Reversible voltammograms and a Pourbaix diagram for a protein tyrosine radical,published,journal,Proc. Natl. Acad. Sci. 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Soc.,,124,,,,,,,,,,,,,,,,,,,,,,,10952,10953,2002, citations,reference_citation_5,18703,91937,6,,reference citation,,,10413527,,,De novo proteins as models of radical enzymes,published,journal,Biochemistry,,38,,,,,,,,,,,,,,,,,,,,,,,9495,9507,1999, citations,entry_citation,18704,91960,1,,entry citation,,,,,,NMR chemical shift mapping of refolded human sialic-acid-binding immunoglobulin-like lectin 5 binding to complex carbohydrates,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18705,91978,1,,entry citation,,,23163963,,,NMR solution structure and condition-dependent oligomerization of the antimicrobial peptide human defensin 5.,published,journal,Biochemistry,Biochemistry,51,48,,,,,,,,,,,,,,,,,,,,,,9624,9637,2012, citations,entry_citation,18706,91992,1,,entry citation,,,23302696,,,Structure and inhibition of the drug-resistant S31N mutant of the M2 ion channel of influenza A virus.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,110,4,,,,,,,,,,,,,,,,,,,,,,1315,1320,2013, citations,entry_citation,18707,92016,1,,entry citation,,,,,,The C-terminal beta-signal-like motif of TamB facilitates efficient autotransporter secretion.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18708,92034,1,,entry citation,,,22916960,,,Rapid measurement of pseudocontact shifts in metalloproteins by proton-detected solid-state NMR spectroscopy.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,134,36,,,,,,,,,,,,,,,,,,,,,,14730,14733,2012, citations,entry_citation,19055,98752,1,,entry citation,,,,,,ns5a D2 con1,in preparation,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18709,92054,1,,entry citation,,,23063560,,,"HMGB1-facilitated p53 DNA binding occurs via HMG-Box/p53 transactivation domain interaction, regulated by the acidic tail.",published,journal,Structure,"Structure (London, England : 1993)",20,12,,,,,,,,,,,,,,,,,,,,,,2014,2024,2012, citations,entry_citation,1871,92073,1,,entry citation,,,,,"Kjaer, Mogens, Ludvigsen, Svend, Sorensen, Ole W., Denys, Lydia A., Kindtler, Jens, Poulsen, Flemming M., ""Sequence specific assignment of the proton nuclear magnetic resonance spectrum of barley serine proteinase inhibitor 2,"" Carlsberg Res. Commun. 52, 327-354 (1987).","Sequence specific assignment of the proton nuclear magnetic resonance spectrum of barley serine proteinase inhibitor 2",published,journal,Carlsberg Res. Commun.,,52,,,,,,,,,,,,,,,,,,,,,,,327,354,1987, citations,citation1,18710,92086,1,,entry citation,,,23349025,,,Temperature-dependent conformational change affecting Tyr11 and sweetness loops of brazzein.,published,journal,Proteins,Proteins,81,6,,,,,,,,,,,,,,,,,,,,,,919,925,2013, citations,entry_citation,18711,92104,1,,entry citation,,,,,,TBA,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18712,92125,1,,entry citation,,,,,,NusA binding to the b-flap tip of RNA polymerase determined by NMR.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18713,92142,1,,entry citation,,,,,,The budding yeast chaperone Scm3 recognizes the partially unfolded dimer of the,in preparation,journal,J. Mol. Biol.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,18714,92165,1,,entry citation,,,,,,"Solution NMR Structure of Homeobox 2 Domain from Human ZHX1 repressor, Northeast Structural Genomics Consortium (NESG) Target HR7907F",in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18715,92191,1,,entry citation,,,,,,Model for the interaction between HIV-1 Gag and plasma membrane,in preparation,journal,Proc. Natl. Acad. Sci. U.S.A.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18716,92211,1,,entry citation,,,,,,Model for the interaction between HIV-1 Gag and plasma membrane,in preparation,journal,Proc. Natl. Acad. Sci. U.S.A.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18717,92231,1,,entry citation,,,23085020,,,The kinetochore-bound Ska1 complex tracks depolymerizing microtubules and binds to curved protofilaments.,published,journal,Dev. Cell,Developmental cell,23,5,,,,,,,,,,,,,,,,,,,,,,968,980,2012, citations,entry_citation,18718,92253,1,,entry citation,,,23763993,,,Characterization of 14-3-3- Interactions with integrin tails.,published,journal,J. Mol. Biol.,Journal of molecular biology,425,17,,,,,,,,,,,,,,,,,,,,,,3060,3072,2013, citations,entry_citation,18719,92268,1,,entry citation,,,23763993,,,Characterization of 14-3-3- Interactions with integrin tails.,published,journal,J. Mol. Biol.,Journal of molecular biology,425,17,,,,,,,,,,,,,,,,,,,,,,3060,3072,2013, citations,entry_citation,1872,92283,1,,entry citation,,,,,"Kjaer, Mogens, Ludvigsen, Svend, Sorensen, Ole W., Denys, Lydia A., Kindtler, Jens, Poulsen, Flemming M., ""Sequence specific assignment of the proton nuclear magnetic resonance spectrum of barley serine proteinase inhibitor 2,"" Carlsberg Res. Commun. 52, 327-354 (1987).","Sequence specific assignment of the proton nuclear magnetic resonance spectrum of barley serine proteinase inhibitor 2",published,journal,Carlsberg Res. Commun.,,52,,,,,,,,,,,,,,,,,,,,,,,327,354,1987, citations,entry_citation,18720,92296,1,,entry citation,,,23142987,,,A direct interaction between DCP1 and XRN1 couples mRNA decapping to 5' exonucleolytic degradation.,published,journal,Nat. Struct. Mol. Biol.,Nature structural & molecular biology,19,12,,,,,,,,,,,,,,,,,,,,,,1324,1331,2012, citations,StarD5_complex_with_cholic_acid,18721,92312,1,,entry citation,,,23872533,,,Thermodynamic and solution state NMR characterization of the binding of secondary and conjugated bile acids to STARD5.,published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1831,11,,,,,,,,,,,,,,,,,,,,,,1589,1599,2013, citations,entry_citation,18722,92336,1,,entry citation,,,23148585,,,Structural Characterization of the Cyclic Cystine Ladder Motif of -Defensins.,published,journal,Biochemistry,Biochemistry,51,48,,,,,,,,,,,,,,,,,,,,,,9718,9726,2012, citations,entry_citation,18723,92356,1,,entry citation,,,23148585,,,Structural Characterization of the Cyclic Cystine Ladder Motif of -Defensins.,published,journal,Biochemistry,Biochemistry,51,48,,,,,,,,,,,,,,,,,,,,,,9718,9726,2012, citations,entry_citation,18724,92376,1,,entry citation,,,,,,Monosaccharide interactions with G-quadruplex DNA: induced-fit effect on thrombin-binding aptamer with sugars at the 5 -end,in preparation,journal,J. Am. Chem. Soc.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,18725,92395,1,,entry citation,,,23661679,,,The Fanconi anemia associated protein FAAP24 uses two substrate specific binding surfaces for DNA recognition.,published,journal,Nucleic Acids Res.,Nucleic acids research,41,13,,,,,,,,,,,,,,,,,,,,,,6739,6749,2013, citations,entry_citation,18726,92416,1,,entry citation,,,23129012,,,NMR structure note: repetitive domain of aciniform spidroin 1 from Nephila antipodiana,in preparation,journal,J. Biomol. NMR,,54,4,,,,,,,,,,,,,,,,,,,,,,415,420,2012, citations,citation_1,18728,92433,1,,entry citation,,,23247503,,,Solution structure of the two RNA recognition motifs of hnRNP A1 using segmental isotope labeling: how the relative orientation between RRMs influences the nucleic acid binding topology.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,55,1,,,,,,,,,,,,,,,,,,,,,,119,138,2013, citations,entry_citation,18729,92460,1,,entry citation,,,23342149,,,Solution Structures of Two Homologous Venom Peptides from Sicarius dolichocephalus.,published,journal,PLoS ONE,PloS one,8,1,,,,,,,,,,,,,,,,,,,,,,e54401,e54401,2013, citations,entry_citation,18730,92506,1,,entry citation,,,23211132,,,Exploring the binding of peptidic West Nile virus NS2B-NS3 protease inhibitors by NMR.,published,journal,Antiviral Res.,Antiviral research,97,2,,,,,,,,,,,,,,,,,,,,,,137,144,2013, citations,entry_citation,18731,92522,1,,entry citation,,,23138856,,,Solid-state NMR sequential assignments of the C-terminal oligomerization domain of human C4b-binding protein.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2012, citations,entry_citation,18732,92537,1,,entry citation,,,,,,NMR structure of the protein NP_390345.1 from Bacilus subtilis,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18733,92556,1,,entry citation,,,,,,NMR structure of the protein NB7890A from Shewanella sp,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18734,92571,1,,entry citation,,,,,,NMR structure of the hypothetical protein ZP_02034617.1 from Bacteroides capillosus ATCC 29799,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,18735,92591,1,,entry citation,,,,,,"Solution NMR Structure of the DNA-Binding Domain of Human NF-E2-Related Factor 2, Northeast Structural Genomics Consortium (NESG) Target HR3520O",in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18736,92617,1,,entry citation,,,23184959,,,Characterization of a Novel alpha-Conotoxin from Conus textile That Selectively Targets alpha6/alpha3beta2beta3 Nicotinic Acetylcholine Receptors,published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,2,,,,,,,,,,,,,,,,,,,,,,894,902,2013, citations,entry_citation,18738,92657,1,,entry citation,,,23325513,,,Backbone resonance assignment of the HEAT1-domain of the human eukaryotic translation initiation factor 4GI.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,1874,92676,1,,entry citation,,,,,"Wang, Jinfeng, Hinck, Andrew P., Loh, Stewart N., LeMaster, David M., Markley, John L., ""Solution Studies of Staphylococcal Nuclease H124L. 2. 1H, 13C, and 15N Chemical Shift Assignments for the Unligated Enzyme and Analysis of Chemical Shift Changes That Accompany Formation of the Nuclease-Thymidine 3',5'-Bisphosphate-Calcium,"" Biochemistry 31 (3), 921-936 (1992).","Solution Studies of Staphylococcal Nuclease H124L. 2. 1H, 13C, and 15N Chemical Shift Assignments for the Unligated Enzyme and Analysis of Chemical Shift Changes That Accompany Formation of the Nuclease-Thymidine 3',5'-Bisphosphate-Calcium",published,journal,Biochemistry,,31,3,,,,,,,,,,,,,,,,,,,,,,921,936,1992, citations,entry_citation,18740,92689,1,,entry citation,,,23250398,,,"A CC-SAM, for coiled coil-sterile alpha motif, domain targets the scaffold KSR-1 to specific sites in the plasma membrane",published,journal,Sci. Signal,,5,255,,,,,,,,,,,,,,,,,,,,,,ra94,ra94,2012, citations,entry_citation,18741,92705,1,,entry citation,,,23325512,,,NMR backbone assignments of the tyrosine kinase domain of human fibroblast growth factor receptor 1.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,18748,92732,1,,entry citation,,,22726438,10.1016/j.cell.2012.04.033,,Inhibition of Basal FGF Receptor Signaling by Dimeric Grb2,published,journal,Cell,,149,,,,,,,,,,,,,,,,,,,,,,,1514,1524,2012, citations,entry_citation,18749,92750,1,,entry citation,,,23222886,,,Structure and dynamics of a primordial catalytic fold generated by in vitro evolution.,published,journal,Nat. Chem. Biol.,Nature chemical biology,9,2,,,,,,,,,,,,,,,,,,,,,,81,83,2013, citations,entry_citation,1875,92769,1,,entry citation,,,,,"Wang, Jinfeng, Hinck, Andrew P., Loh, Stewart N., LeMaster, David M., Markley, John L., ""Solution Studies of Staphylococcal Nuclease H124L. 2. 1H, 13C, and 15N Chemical Shift Assignments for the Unligated Enzyme and Analysis of Chemical Shift Changes That Accompany Formation of the Nuclease-Thymidine 3',5'-Bisphosphate-Calcium,"" Biochemistry 31 (3), 921-936 (1992).","Solution Studies of Staphylococcal Nuclease H124L. 2. 1H, 13C, and 15N Chemical Shift Assignments for the Unligated Enzyme and Analysis of Chemical Shift Changes That Accompany Formation of the Nuclease-Thymidine 3',5'-Bisphosphate-Calcium",published,journal,Biochemistry,,31,3,,,,,,,,,,,,,,,,,,,,,,921,936,1992, citations,entry_citation,18750,92782,1,,entry citation,,,23110687,,,Metamorphic Protein IscU Changes Conformation by cis-trans Isomerizations of Two Peptidyl-Prolyl Peptide Bonds.,published,journal,Biochemistry,Biochemistry,51,48,,,,,,,,,,,,,,,,,,,,,,9595,9602,2012, citations,entry_citation,18753,92800,1,,entry citation,,,,,,Structure of the biofilm matrix promoter AbbA from B. subtilis,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18754,92820,1,,entry citation,,,23110687,,,Metamorphic Protein IscU Changes Conformation by cis-trans Isomerizations of Two Peptidyl-Prolyl Peptide Bonds.,published,journal,Biochemistry,Biochemistry,51,48,,,,,,,,,,,,,,,,,,,,,,9595,9602,2012, citations,entry_citation,18755,92837,1,,entry citation,,,22991965,,,Ordering of the N-terminus of human MDM2 by small molecule inhibitors.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,134,41,,,,,,,,,,,,,,,,,,,,,,17059,17067,2012, citations,entry_citation,18756,92855,1,,entry citation,,,23274114,,,Long-Range Effects and Functional Consequences of Stabilizing Mutations in the Ankyrin Repeat Domain of IB.,published,journal,J. Mol. Biol.,Journal of molecular biology,425,5,,,,,,,,,,,,,,,,,,,,,,902,913,2013, citations,entry_citation,18757,92876,1,,entry citation,,,23148585,,,Structural Characterization of the Cyclic Cystine Ladder Motif of -Defensins.,published,journal,Biochemistry,Biochemistry,51,48,,,,,,,,,,,,,,,,,,,,,,9718,9726,2012, citations,entry_citation,18758,92896,1,,entry citation,,,24211821,,,NMR structural studies of the first catalytic half-domain of ubiquitin activating enzyme.,published,journal,J. Struct. Biol.,Journal of structural biology,185,1,,,,,,,,,,,,,,,,,,,,,,69,78,2014, citations,entry_citation,18759,92921,1,,entry citation,,,23274114,,,Long-Range Effects and Functional Consequences of Stabilizing Mutations in the Ankyrin Repeat Domain of IB.,published,journal,J. Mol. Biol.,Journal of molecular biology,425,5,,,,,,,,,,,,,,,,,,,,,,902,913,2013, citations,entry_citation,1876,92937,1,,entry citation,,,,,"Wang, Jinfeng, Hinck, Andrew P., Loh, Stewart N., LeMaster, David M., Markley, John L., ""Solution Studies of Staphylococcal Nuclease H124L. 2. 1H, 13C, and 15N Chemical Shift Assignments for the Unligated Enzyme and Analysis of Chemical Shift Changes That Accompany Formation of the Nuclease-Thymidine 3',5'-Bisphosphate-Calcium,"" Biochemistry 31 (3), 921-936 (1992).","Solution Studies of Staphylococcal Nuclease H124L. 2. 1H, 13C, and 15N Chemical Shift Assignments for the Unligated Enzyme and Analysis of Chemical Shift Changes That Accompany Formation of the Nuclease-Thymidine 3',5'-Bisphosphate-Calcium",published,journal,Biochemistry,,31,3,,,,,,,,,,,,,,,,,,,,,,921,936,1992, citations,entry_citation,18760,92950,1,,entry citation,,,23274114,,,Long-Range Effects and Functional Consequences of Stabilizing Mutations in the Ankyrin Repeat Domain of IB.,published,journal,J. Mol. Biol.,Journal of molecular biology,425,5,,,,,,,,,,,,,,,,,,,,,,902,913,2013, citations,citation_1,18761,92966,1,,entry citation,,,23315337,,,"(1)H, (13)C, and (15)N chemical shift assignments of the phosphotyrosine binding domain 2 (PTB2) of human FE65.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,18762,92985,1,,entry citation,,,23121427,,,"Nuclear Magnetic Resonance Solution Structure of an N(2)-Guanine DNA Adduct Derived from the Potent Tumorigen Dibenzo[a,l]pyrene: Intercalation from the Minor Groove with Ruptured Watson-Crick Base Pairing.",published,journal,Biochemistry,Biochemistry,51,48,,,,,,,,,,,,,,,,,,,,,,9751,9762,2012, citations,citations,18763,93004,1,,entry citation,,,24120763,,,Structure of FGFR3 transmembrane domain dimer: implications for signaling and human pathologies.,published,journal,Structure,"Structure (London, England : 1993)",21,11,,,,,,,,,,,,,,,,,,,,,,2087,2093,2013, citations,entry_citation,18764,93021,1,,entry citation,,,23104054,,,Phf19 links methylated Lys36 of histone H3 to regulation of Polycomb activity.,published,journal,Nat. Struct. Mol. Biol.,Nature structural & molecular biology,19,12,,,,,,,,,,,,,,,,,,,,,,1257,1265,2012, citations,entry_citation,18765,93042,1,,entry citation,,,23384725,,,Molecular mechanism of oxidation-induced TDP-43 RRM1 aggregation and loss of function.,published,journal,FEBS Lett.,FEBS letters,587,6,,,,,,,,,,,,,,,,,,,,,,575,582,2013, citations,citations,18766,93058,1,,entry citation,,,23801332,,,Sea anemone peptide with uncommon -hairpin structure inhibits acid-sensing ion channel 3 (ASIC3) and reveals analgesic activity.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,32,,,,,,,,,,,,,,,,,,,,,,23116,23127,2013, citations,citations_1,18813,93957,1,,entry citation,,,23273982,,,An H3K36 Methylation-Engaging Tudor Motif of Polycomb-like Proteins Mediates PRC2 Complex Targeting.,published,journal,Mol. Cell,Molecular cell,49,3,,,,,,,,,,,,,,,,,,,,,,571,582,2013, citations,entry_citation,18767,93074,1,,entry citation,,,25378334,,,Hug1 is an intrinsically disordered protein that inhibits ribonucleotide reductase activity by directly binding Rnr2 subunit,published,journal,Nucleic Acids Res.,Nucleic acids research,42,21,,1362-4962,,,,,,,,,,,,,,,,,,,,13174,13185,2014, citations,ns22,18768,93089,1,,entry citation,,,24741107,,,NS2 proteins of GB virus B and hepatitis C virus share common protease activities and membrane topologies.,published,journal,J. Virol.,Journal of virology,88,13,,,,,,,,,,,,,,,,,,,,,,7426,7444,2014, citations,entry_citation,18769,93106,1,,entry citation,,,24741107,,,NS2 proteins of GB virus B and hepatitis C virus share common protease activities and membrane topologies.,published,journal,J. Virol.,Journal of virology,88,13,,,,,,,,,,,,,,,,,,,,,,7426,7444,2014, citations,entry_citation,1877,93123,1,,entry citation,,,,,"Wang, Jinfeng, Hinck, Andrew P., Loh, Stewart N., LeMaster, David M., Markley, John L., ""Solution Studies of Staphylococcal Nuclease H124L. 2. 1H, 13C, and 15N Chemical Shift Assignments for the Unligated Enzyme and Analysis of Chemical Shift Changes That Accompany Formation of the Nuclease-Thymidine 3',5'-Bisphosphate-Calcium,"" Biochemistry 31 (3), 921-936 (1992).","Solution Studies of Staphylococcal Nuclease H124L. 2. 1H, 13C, and 15N Chemical Shift Assignments for the Unligated Enzyme and Analysis of Chemical Shift Changes That Accompany Formation of the Nuclease-Thymidine 3',5'-Bisphosphate-Calcium",published,journal,Biochemistry,,31,3,,,,,,,,,,,,,,,,,,,,,,921,936,1992, citations,entry_citation,18770,93136,1,,entry citation,,,23471988,,,Structural model for the protein-translocating element of the twin-arginine transport system.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,110,12,,,,,,,,,,,,,,,,,,,,,,E1092,E1101,2013, citations,entry_citation,18771,93156,1,,entry citation,,,23471988,,,Structural model for the protein-translocating element of the twin-arginine transport system.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,110,12,,,,,,,,,,,,,,,,,,,,,,E1092,E1101,2013, citations,entry_citation,18772,93180,1,,entry citation,,,23233676,,,A Structurally Dynamic N-terminal Helix Is a Key Functional Determinant in Staphylococcal Complement Inhibitor (SCIN) Proteins.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,4,,,,,,,,,,,,,,,,,,,,,,2870,2881,2013, citations,entry_citation,18773,93197,1,,entry citation,,,23233676,,,A Structurally Dynamic N-terminal Helix Is a Key Functional Determinant in Staphylococcal Complement Inhibitor (SCIN) Proteins.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,4,,,,,,,,,,,,,,,,,,,,,,2870,2881,2013, citations,entry_citation,18774,93214,1,,entry citation,,,23315339,,,"Backbone (1)H, (13)C, (15)N NMR assignments of yeast OMP synthase in unliganded form and in complex with orotidine 5'-monophosphate.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,18775,93235,1,,entry citation,,,23315339,,,"Backbone (1)H, (13)C, (15)N NMR assignments of yeast OMP synthase in unliganded form and in complex with orotidine 5'-monophosphate.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,18776,93256,1,,entry citation,,,23417794,,,"(1)H, (13)C, (15)N backbone and side chain NMR resonance assignments for the N-terminal RNA recognition motif of the HvGR-RBP1 protein involved in the regulation of barley (Hordeum vulgare L.) senescence.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,18777,93273,1,,entry citation,,,,,,"1H, 13C, and 15N backbone chemical shift assignments of StAR-related lipid transfer domain protein 6 (STARD6)",in preparation,journal,Biomol. NMR Assignments,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,18778,93295,1,,entry citation,,,,,,Solution Structure of LIMD2,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18779,93320,1,,entry citation,,,23225222,,,Backbone resonance assignments of the outer membrane lipoprotein FrpD from Neisseria meningitidis.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2012, citations,entry_citation,1878,93336,1,,entry citation,,,,,"Wang, Jinfeng, Hinck, Andrew P., Loh, Stewart N., LeMaster, David M., Markley, John L., ""Solution Studies of Staphylococcal Nuclease H124L. 2. 1H, 13C, and 15N Chemical Shift Assignments for the Unligated Enzyme and Analysis of Chemical Shift Changes That Accompany Formation of the Nuclease-Thymidine 3',5'-Bisphosphate-Calcium,"" Biochemistry 31 (3), 921-936 (1992).","Solution Studies of Staphylococcal Nuclease H124L. 2. 1H, 13C, and 15N Chemical Shift Assignments for the Unligated Enzyme and Analysis of Chemical Shift Changes That Accompany Formation of the Nuclease-Thymidine 3',5'-Bisphosphate-Calcium",published,journal,Biochemistry,,31,3,,,,,,,,,,,,,,,,,,,,,,921,936,1992, citations,entry_citation,18780,93349,1,,entry citation,,,,,,Solution structures of DNA duplexes containing mispair-aligned O4U-heptylene-O4U and O6G-heptylene-O6G interstrand cross-links,in preparation,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18781,93372,1,,entry citation,,,,,,Solution structures of DNA duplexes containing mispair-aligned O4U-heptylene-O4U and O6G-heptylene-O6G interstrand cross-links,in preparation,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18782,93395,1,,entry citation,,,23520467,,,"Solution structure of the QUA1 dimerization domain of pXqua, the Xenopus ortholog of Quaking",published,journal,PLOS ONE,PLOS ONE,8,3,,,,,,,,,,,,,,,,,,,,,,e57345,e57345,2013, citations,entry_citation,18783,93412,1,,entry citation,,,24225326,,,"Asteropsins B-D, sponge-derived knottins with potential utility as a novel scaffold for oral peptide drugs.",published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1840,3,,,,,,,,,,,,,,,,,,,,,,977,984,2014, citations,entry_citation,18784,93428,1,,entry citation,,,23225198,,,"Sequence-specific backbone (1)H, (13)C and (15)N assignments of the catalytic domain of the Escherichia coli protein tyrosine kinase, Wzc.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2012, citations,entry_citation,18785,93444,1,,entry citation,,,23159126,,,Design of a phosphorylatable PDZ domain with Peptide-specific affinity changes.,published,journal,Structure,"Structure (London, England : 1993)",21,1,,,,,,,,,,,,,,,,,,,,,,54,64,2013, citations,entry_citation,18786,93460,1,,entry citation,,,23159126,,,Design of a phosphorylatable PDZ domain with Peptide-specific affinity changes.,published,journal,Structure,"Structure (London, England : 1993)",21,1,,,,,,,,,,,,,,,,,,,,,,54,64,2013, citations,entry_citation,18787,93476,1,,entry citation,,,23313804,,,Solution structure of a mutant of the triheme cytochrome PpcA from Geobacter sulfurreducens sheds light on the role of the conserved aromatic residue F15.,published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1827,4,,,,,,,,,,,,,,,,,,,,,,484,492,2013, citations,entry_citation,18788,93498,1,,entry citation,,,23416741,,,Modeling of the [E43S]SNase-ssDNA-Cd(2+) complex: structural insight into the action of nuclease on ssDNA.,published,journal,Arch. Biochem. Biophys.,Archives of biochemistry and biophysics,532,2,,,,,,,,,,,,,,,,,,,,,,103,113,2013, citations,entry_citation,18789,93514,1,,entry citation,,,23573241,,,Genomic and structural characterization of Kunitz-type peptide LmKTT-1a highlights diversity and evolution of scorpion potassium channel toxins,published,journal,Plos One,,8,4,,,,,,,,,,,,,,,,,,,,,,e60201,e60201,2013, citations,entry_citation,18791,93537,1,,entry citation,,,23225198,,,"Sequence-specific backbone (1)H, (13)C and (15)N assignments of the catalytic domain of the Escherichia coli protein tyrosine kinase, Wzc.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2012, citations,entry_citation,18792,93554,1,,entry citation,,,23340338,,,PUMA binding induces partial unfolding within BCL-xL to disrupt p53 binding and promote apoptosis.,published,journal,Nat. Chem. Biol.,Nature chemical biology,9,3,,,,,,,,,,,,,,,,,,,,,,163,168,2013, citations,entry_citation,18793,93572,1,,entry citation,,,23340338,,,PUMA binding induces partial unfolding within BCL-xL to disrupt p53 binding and promote apoptosis.,published,journal,Nat. Chem. Biol.,Nature chemical biology,9,3,,,,,,,,,,,,,,,,,,,,,,163,168,2013, citations,entry_citation,18794,93592,1,,entry citation,,,24276282,,,Quantification of copper binding to amyloid precursor protein domain 2 and its Caenorhabditis elegans ortholog. Implications for biological function.,published,journal,Metallomics,Metallomics : integrated biometal science,6,1,,,,,,,,,,,,,,,,,,,,,,105,116,2014, citations,NMR_assignments_of_amylin_in_DMSO,18795,93610,1,,entry citation,,,23457571,,,Amide proton solvent protection in amylin fibrils probed by quenched hydrogen exchange NMR,published,journal,PLOS One,,8,2,,,,,,,,,,,,,,,,,,,,,,e56467,e56467,2013, citations,entry_citation,18796,93625,1,,entry citation,,,23294159,,,Optimized phospholipid bilayer nanodiscs facilitate high-resolution structure determination of membrane proteins.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,135,5,,,,,,,,,,,,,,,,,,,,,,1919,1925,2013, citations,entry_citation,18797,93643,1,,entry citation,,,23294159,,,Optimized phospholipid bilayer nanodiscs facilitate high-resolution structure determination of membrane proteins.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,135,5,,,,,,,,,,,,,,,,,,,,,,1919,1925,2013, citations,entry_citation,18798,93660,1,,entry citation,,,25209143,,,Backbone assignments of the apo and Zn(II) protoporphyrin IX-bound states of the soluble form of rat heme oxygenase-1,published,journal,Biomol. NMR Assign.,,9,1,,,,,,,,,,,,,,,,,,,,,,197,200,2015, citations,entry_citation_2,18798,93661,2,,reference citation,,,25496210,,,Distal regulation of heme binding of heme oxygenase-1 mediated by conformational fluctuations,published,journal,Biochemistry,,54,2,,,,,,,,,,,,,,,,,,,,,,340,348,2015, citations,entry_citation,18799,93678,1,,entry citation,,,25496210,,,Distal regulation of heme binding of heme oxygenase-1 mediated by conformational fluctuations,published,journal,Biochemistry,,54,2,,,,,,,,,,,,,,,,,,,,,,340,348,2015, citations,entry_citation,188,93695,1,,entry citation,,,,,"Torchia, Dennis A., Sparks, Steven W., Bax, Ad, ""NMR Signal Assignments of Amide Protons in the alpha-Helical Domains of Staphylococcal Nuclease,"" Biochemistry 27 (14), 5135-5141 (1988).","NMR Signal Assignments of Amide Protons in the alpha-Helical Domains of Staphylococcal Nuclease",published,journal,Biochemistry,,27,14,,,,,,,,,,,,,,,,,,,,,,5135,5141,1988, citations,entry_citation,18800,93708,1,,entry citation,,,25209143,,,Backbone assignments of the apo and Zn(II) protoporphyrin IX-bound states of the soluble form of rat heme oxygenase-1,published,journal,Biomol. NMR Assign.,,9,1,,,,,,,,,,,,,,,,,,,,,,197,200,2015, citations,entry_citation_2,18800,93709,2,,reference citation,,,25496210,,,Distal regulation of heme binding of heme oxygenase-1 mediated by conformational fluctuations,published,journal,Biochemistry,,54,2,,,,,,,,,,,,,,,,,,,,,,340,348,2015, citations,entry_citation,18801,93728,1,,entry citation,,,27349962,10.1186/s12915-016-0274-1,,NmPin from the marine thaumarchaeote Nitrosopumilus maritimus is an active membrane associated prolyl isomerase,published,journal,BMC Biol.,,14,1,,,,,,,,,,,,,,,,,,,,,,53,53,2016, citations,entry_citation,18802,93746,1,,entry citation,,,23175611,,,"Structure, phosphorylation and U2AF65 binding of the N-terminal domain of splicing factor 1 during 3'-splice site recognition",published,journal,Nucleic Acids Res.,,41,2,,,,,,,,,,,,,,,,,,,,,,1343,1354,2013, citations,entry_citation,18803,93767,1,,entry citation,,,23302895,,,Solution Structure of Mouse Hepatitis Virus (MHV) nsp3a and Determinants of the Interaction with MHV Nucleocapsid (N) Protein.,published,journal,J. Virol.,Journal of virology,87,6,,,,,,,,,,,,,,,,,,,,,,3502,3515,2013, citations,citations,18804,93783,1,,entry citation,,,,,,"Homodimeric transmembrane domain of the human receptor tyrosine kinase ErbB1 (EGFR, HER1) in micelles",in preparation,journal,To be Published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,18805,93801,1,,entry citation,,,,,,"Solution NMR Structure of Homeobox Domain of Human ALX4, Northeast Structural Genomics Consortium (NESG) Target HR4490C",in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18806,93826,1,,entry citation,,,23975355,,,Structural and dynamical characterization of the Miz-1 zinc fingers 5-8 by solution-state NMR.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,57,2,,,,,,,,,,,,,,,,,,,,,,103,116,2013, citations,entry_citation,18807,93846,1,,entry citation,,,23798409,,,Caenorhabditis elegans centriolar protein SAS-6 forms a spiral that is consistent with imparting a ninefold symmetry,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,110,28,,1091-6490,,,,,,,,,,,,,,,,,,,,11373,11378,2013, citations,reference,18807,93847,2,,reference citation,,,21277013,,,Structural basis of the 9-fold symmetry of centrioles.,published,journal,Cell,,144,3,,,,,,,,,,,,,,,,,,,,,,364,375,2011, citations,entry_citation,18808,93866,1,,entry citation,,,23175611,,,"Structure, phosphorylation and U2AF65 binding of the N-terminal domain of splicing factor 1 during 3'-splice site recognition",published,journal,Nucleic Acids Res.,,41,2,,,,,,,,,,,,,,,,,,,,,,1343,1354,2013, citations,entry_citation,18809,93888,1,,entry citation,,,,,,Solution NMR structures of the C-terminal segment of surfactant protein B (residues 59-80) in DPC detergent micelles and methanol.,in preparation,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1881,93902,1,,entry citation,,,,,"Evans, Philip A., Topping, Karen D., Woolfson, Derek N., Dobson, Christopher M., ""Hydrophobic Clustering in Nonnative States of a Protein: Interpretation of Chemical Shifts in NMR Spectra of Denatured States of Lysozyme,"" Proteins: Struct. Funct. Genet. 9, 248-266 (1991).","Hydrophobic Clustering in Nonnative States of a Protein: Interpretation of Chemical Shifts in NMR Spectra of Denatured States of Lysozyme",published,journal,Proteins: Struct. Funct. Genet.,,9,,,,,,,,,,,,,,,,,,,,,,,248,266,1991, citations,entry_citation,18811,93915,1,,entry citation,,,23418525,,,Structural characterization of minor ampullate spidroin domains and their distinct roles in fibroin solubility and fiber formation.,published,journal,PLoS ONE,PloS one,8,2,,,,,,,,,,,,,,,,,,,,,,e56142,e56142,2013, citations,entry_citation,18812,93935,1,,entry citation,,,,,,Evidence for further structural diversity in the DUF3349 family,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18887,95579,1,,entry citation,,,,,,Solution structure of hypothetical protein lmo0427,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18814,93976,1,,entry citation,,,23601147,,,Protein oligomers studied by solid-state NMR--the case of the full-length nucleoid-associated protein histone-like nucleoid structuring protein.,published,journal,FEBS J.,The FEBS journal,280,12,,,,,,,,,,,,,,,,,,,,,,2916,2928,2013, citations,Citation,18815,93993,1,,entry citation,,,,,,eiav-ca,submitted,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18816,94009,1,,entry citation,,,23275343,,,Gentamicin binds to the megalin receptor as a competitive inhibitor using the common ligand binding motif of complement type repeats: insight from the nmr structure of the 10th complement type repeat domain alone and in complex with gentamicin.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,6,,,,,,,,,,,,,,,,,,,,,,4424,4435,2013, citations,entry_citation,18817,94030,1,,entry citation,,,24827085,,,Differential modulations of KCNQ1 by auxiliary proteins KCNE1 and KCNE2.,published,journal,Sci. Rep.,Scientific reports,4,,,,,,,,,,,,,,,,,,,,,,,4973,4973,2014, citations,entry_citation,18818,94049,1,,entry citation,,,23197251,,,Solution structure and dynamics of human S100A14.,published,journal,J. Biol. Inorg. Chem.,Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry,18,2,,,,,,,,,,,,,,,,,,,,,,183,194,2013, citations,entry_citation,18819,94069,1,,entry citation,,,21152998,,,NMR assignments of the N-terminal domain of Nephila clavipes spidroin 1.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,2,,,,,,,,,,,,,,,,,,,,,,131,133,2011, citations,entry_citation,1882,94086,1,,entry citation,,,,,"Evans, Philip A., Topping, Karen D., Woolfson, Derek N., Dobson, Christopher M., ""Hydrophobic Clustering in Nonnative States of a Protein: Interpretation of Chemical Shifts in NMR Spectra of Denatured States of Lysozyme,"" Proteins: Struct. Funct. Genet. 9, 248-266 (1991).","Hydrophobic Clustering in Nonnative States of a Protein: Interpretation of Chemical Shifts in NMR Spectra of Denatured States of Lysozyme",published,journal,Proteins: Struct. Funct. Genet.,,9,,,,,,,,,,,,,,,,,,,,,,,248,266,1991, citations,entry_citation,18820,94099,1,,entry citation,,,21152998,,,NMR assignments of the N-terminal domain of Nephila clavipes spidroin 1.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,2,,,,,,,,,,,,,,,,,,,,,,131,133,2011, citations,entry_citation,18821,94116,1,,entry citation,,,21152998,,,NMR assignments of the N-terminal domain of Nephila clavipes spidroin 1.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,5,2,,,,,,,,,,,,,,,,,,,,,,131,133,2011, citations,citations,18822,94133,1,,entry citation,,,23408612,,,Membrane Topology and Function of Dengue Virus NS2A Protein.,published,journal,J. Virol.,Journal of virology,87,8,,,,,,,,,,,,,,,,,,,,,,4609,4622,2013, citations,entry_citation,18823,94150,1,,entry citation,,,23242787,,,"(1)H, (15)N and (13)C resonance assignments of PpdD, a type IV pilin from enterohemorrhagic Escherichia coli.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2012, citations,entry_citation,18824,94165,1,,entry citation,,,23583913,,,Ligand-Induced Dynamic Changes in Extended PDZ Domains from NHERF1.,published,journal,J. Mol. Biol.,Journal of molecular biology,425,14,,,,,,,,,,,,,,,,,,,,,,2509,2528,2013, citations,entry_citation,18825,94187,1,,entry citation,,,23583913,,,Ligand-Induced Dynamic Changes in Extended PDZ Domains from NHERF1.,published,journal,J. Mol. Biol.,Journal of molecular biology,425,14,,,,,,,,,,,,,,,,,,,,,,2509,2528,2013, citations,entry_citation,18826,94209,1,,entry citation,,,23583913,,,Ligand-Induced Dynamic Changes in Extended PDZ Domains from NHERF1.,published,journal,J. Mol. Biol.,Journal of molecular biology,425,14,,,,,,,,,,,,,,,,,,,,,,2509,2528,2013, citations,entry_citation,18827,94233,1,,entry citation,,,26284781,10.1021/acs.biochem.5b00366,,Conformational Polymorphism in Autophagy-Related Protein GATE-16.,published,journal,Biochemistry,Biochemistry,54,35,,1520-4995,,,,,,,,,,,,,,,,,,,,5469,5479,2015, citations,entry_citation,18828,94255,1,,entry citation,,,23438074,,,"Communication between (L)-galactono-1,4-lactone dehydrogenase and cytochrome c.",published,journal,FEBS J.,The FEBS journal,280,8,,,,,,,,,,,,,,,,,,,,,,1830,1840,2013, citations,entry_citation,18829,94273,1,,entry citation,,,23902765,,,RNA binding of T-cell intracellular antigen-1 (TIA-1) C-terminal RNA recognition motif is modified by pH conditions.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,36,,,,,,,,,,,,,,,,,,,,,,25986,25994,2013, citations,entry_citation,1883,94287,1,,entry citation,,,,,"Evans, Philip A., Topping, Karen D., Woolfson, Derek N., Dobson, Christopher M., ""Hydrophobic Clustering in Nonnative States of a Protein: Interpretation of Chemical Shifts in NMR Spectra of Denatured States of Lysozyme,"" Proteins: Struct. Funct. Genet. 9, 248-266 (1991).","Hydrophobic Clustering in Nonnative States of a Protein: Interpretation of Chemical Shifts in NMR Spectra of Denatured States of Lysozyme",published,journal,Proteins: Struct. Funct. Genet.,,9,,,,,,,,,,,,,,,,,,,,,,,248,266,1991, citations,entry_citation,18830,94300,1,,entry citation,,,,,,Structure of ALPS peptide in SDS micelles.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18831,94314,1,,entry citation,,,23801757,,,Conformational dynamics control ubiquitin-deubiquitinase interactions and influence in vivo signaling.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,110,28,,,,,,,,,,,,,,,,,,,,,,11379,11384,2013, citations,citation,18832,94329,1,,entry citation,,,23239367,,,Solution structure of the SH3 domain of DOCK180.,published,journal,Proteins,Proteins,81,5,,,,,,,,,,,,,,,,,,,,,,906,910,2013, citations,entry_citation,18833,94350,1,,entry citation,,,23818626,,,Kinetic response of a photoperturbed allosteric protein.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,110,29,,,,,,,,,,,,,,,,,,,,,,11725,11730,2013, citations,entry_citation,18834,94377,1,,entry citation,,,23818626,,,Kinetic response of a photoperturbed allosteric protein.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,110,29,,,,,,,,,,,,,,,,,,,,,,11725,11730,2013, citations,citation_1,18835,94404,1,,entry citation,,,23748954,,,Recognition of O6-benzyl-2'-deoxyguanosine by a perimidinone-derived synthetic nucleoside: a DNA interstrand stacking interaction.,published,journal,Nucleic Acids Res.,Nucleic acids research,41,15,,,,,,,,,,,,,,,,,,,,,,7566,7576,2013, citations,entry_citation,18836,94428,1,,entry citation,,,23853076,,,"Backbone 1H, 13C and 15N assignments of YibK and avariant containing a unique cysteine residue at C-terminus in 8 M urea-denatured states",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,8,2,,,,,,,,,,,,,,,,,,,,,,439,442,2014, citations,reference_citation,18836,94429,2,,reference citation,,,20393125,,,Experimental detection of knotted conformations in denatured proteins.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,107,18,,,,,,,,,,,,,,,,,,,,,,8189,8194,2010, citations,entry_citation,18837,94445,1,,entry citation,,,23359223,,,"(15)N, (13)C and (1)H resonance assignments and secondary structure determination of a variable heavy domain of a heavy chain antibody",published,journal,Biomol. NMR Assignments,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18838,94468,1,,entry citation,,,24243113,,,Role of helical constraints of the EBS1-IBS1 duplex of a group II intron on demarcation of the 5' splice site.,published,journal,RNA,"RNA (New York, N.Y.)",20,1,,,,,,,,,,,,,,,,,,,,,,24,35,2014, citations,citation_1,18839,94490,1,,entry citation,,,22696137,,,Chemical shift assignments of the canecystatin-1 from Saccharum officinarum.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,2,,,,,,,,,,,,,,,,,,,,,,163,165,2013, citations,entry_citation,1884,94509,1,,entry citation,,,,,"Evans, Philip A., Topping, Karen D., Woolfson, Derek N., Dobson, Christopher M., ""Hydrophobic Clustering in Nonnative States of a Protein: Interpretation of Chemical Shifts in NMR Spectra of Denatured States of Lysozyme,"" Proteins: Struct. Funct. Genet. 9, 248-266 (1991).","Hydrophobic Clustering in Nonnative States of a Protein: Interpretation of Chemical Shifts in NMR Spectra of Denatured States of Lysozyme",published,journal,Proteins: Struct. Funct. Genet.,,9,,,,,,,,,,,,,,,,,,,,,,,248,266,1991, citations,entry_citation,18840,94522,1,,entry citation,,,23500490,,,The C-Terminal Region of Cytoplasmic Polyadenylation Element Binding Protein Is a ZZ Domain with Potential for Protein-Protein Interactions.,published,journal,J. Mol. Biol.,Journal of molecular biology,425,11,,,,,,,,,,,,,,,,,,,,,,2015,2026,2013, citations,entry_citation,18841,94546,1,,entry citation,,,24768114,,,Small-Angle X-Ray Scattering- and Nuclear Magnetic Resonance-Derived Conformational Ensemble of the Highly Flexible Antitoxin PaaA2.,published,journal,Structure,"Structure (London, England : 1993)",,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,18842,94581,1,,entry citation,,,23295669,,,Structural and functional evidence that Rad4 competes with Rad2 for binding to the Tfb1 subunit of TFIIH in NER.,published,journal,Nucleic Acids Res.,Nucleic acids research,41,4,,,,,,,,,,,,,,,,,,,,,,2736,2745,2013, citations,entry_citation,18843,94610,1,,entry citation,,,23264024,,,"(1)H, (13)C and (15)N assignments of the four N-terminal domains of human fibrillin-1.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2012, citations,entry_citation,18844,94630,1,,entry citation,,,23667555,,,Solution Structure and Rpn1 Interaction of the UBL Domain of Human RNA Polymerase II C-Terminal Domain Phosphatase.,published,journal,PLoS ONE,PloS one,8,5,,,,,,,,,,,,,,,,,,,,,,e62981,e62981,2013, citations,entry_citation,18845,94653,1,,entry citation,,,23334698,,,Protein chemical shift assignments of the unbound and RNA-bound forms of the alternative splicing factor SUP-12 from C. elegans.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,18846,94674,1,,entry citation,,,23334698,,,Protein chemical shift assignments of the unbound and RNA-bound forms of the alternative splicing factor SUP-12 from C. elegans.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,18847,94694,1,,entry citation,,,23445442,,,Structure of Human Telomeric RNA (TERRA): Stacking of Two G-Quadruplex Blocks in K(+) Solution.,published,journal,Biochemistry,Biochemistry,52,13,,,,,,,,,,,,,,,,,,,,,,2176,2183,2013, citations,entry_citation,18848,94710,1,,entry citation,,,23494870,,,"Backbone (1)H, (13)C and (15)N resonance assignment of the C-terminal EGF-cbEGF pair of LTBP1 and flanking residues.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,18849,94728,1,,entry citation,,,23264007,,,Chemical shift assignments and secondary structure prediction of the C-terminal domain of the response regulator BfmR from Acinetobacter baumannii.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2012, citations,entry_citation,1885,94745,1,,entry citation,,,,,"Chandrasekhar, Kasibhatla, Profy, Albert T., Dyson, H. Jane, ""Solution Conformational Preferences of Immunogenic Peptides Derived from the Principal Neutralizing Determinant of the HIV-1 Envelope Glycoprotein gp120,"" Biochemistry 30, 9187-9194 (1991).","Solution Conformational Preferences of Immunogenic Peptides Derived from the Principal Neutralizing Determinant of the HIV-1 Envelope Glycoprotein gp120",published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,9187,9194,1991, citations,entry_citation,18850,94759,1,,entry citation,,,23821306,,,Crystal structure of the ubiquitin-like small archaeal modifier protein 2 from Haloferax volcanii.,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,22,9,,,,,,,,,,,,,,,,,,,,,,1206,1217,2013, citations,citations,18851,94780,1,,entry citation,,,23972852,,,The Arginine-Rich RNA-Binding Motif of HIV-1 Rev Is Intrinsically Disordered and Folds upon RRE Binding,published,journal,Biophys. J.,,105,4,,,,,,,,,,,,,,,,,,,,,,1004,1017,2013, citations,citations,18852,94799,1,,entry citation,,,23972852,,,The Arginine-Rich RNA-Binding Motif of HIV-1 Rev Is Intrinsically Disordered and Folds upon RRE Binding,published,journal,Biophys. J.,,105,4,,,,,,,,,,,,,,,,,,,,,,1004,1017,2013, citations,entry_citation,18853,94817,1,,entry citation,,,24493340,,,"Backbone and side-chain (1)H, (13)C, and (15)N NMR assignments of the N-terminal domain of Escherichia coli LpoA.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,18854,94835,1,,entry citation,,,22311340,,,"1H, 13C and 15N backbone and side chain resonance assignments of human halo S100A1.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,6,2,,,,,,,,,,,,,,,,,,,,,,213,215,2012, citations,entry_citation,18855,94850,1,,entry citation,,,23853076,,,"Backbone 1H, 13C and 15N assignments of YibK and avariant containing a unique cysteine residue at C-terminus in 8 M urea-denatured states",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,8,2,,,,,,,,,,,,,,,,,,,,,,439,442,2014, citations,reference_citation,18855,94851,2,,reference citation,,,20393125,,,Experimental detection of knotted conformations in denatured proteins.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,107,18,,,,,,,,,,,,,,,,,,,,,,8189,8194,2010, citations,citations,18856,94867,1,,entry citation,,,23504327,,,Solution structure of the PAS domain of a thermophilic YybT protein homolog reveals a potential ligand-binding site.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,17,,,,,,,,,,,,,,,,,,,,,,11949,11959,2013, citations,entry_citation,18857,94882,1,,entry citation,,,,,,"Backbone 1H, 13C,and 15N chemical shift assignments for alpha-synuclein at different pH and temperature",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18858,94960,1,,entry citation,,,23404086,,,Biosynthetic engineered B28(K)-B29 (P) human insulin monomer structure in water and in water/acetonitrile solutions.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,55,3,,,,,,,,,,,,,,,,,,,,,,303,309,2013, citations,entry_citation,18859,94980,1,,entry citation,,,23404086,,,Biosynthetic engineered B28(K)-B29 (P) human insulin monomer structure in water and in water/acetonitrile solutions.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,55,3,,,,,,,,,,,,,,,,,,,,,,303,309,2013, citations,citation_1,18888,95597,1,,entry citation,,,23374349,,,Conformational Coupling across the Plasma Membrane in Activation of the EGF Receptor,published,journal,Cell,,152,3,,,,,,,,,,,,,,,,,,,,,,543,556,2013, citations,entry_citation,1886,95000,1,,entry citation,,,,,"Chandrasekhar, Kasibhatla, Profy, Albert T., Dyson, H. Jane, ""Solution Conformational Preferences of Immunogenic Peptides Derived from the Principal Neutralizing Determinant of the HIV-1 Envelope Glycoprotein gp120,"" Biochemistry 30, 9187-9194 (1991).","Solution Conformational Preferences of Immunogenic Peptides Derived from the Principal Neutralizing Determinant of the HIV-1 Envelope Glycoprotein gp120",published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,9187,9194,1991, citations,entry_citation,18860,95014,1,,entry citation,,,21744165,,,Solid-state NMR sequential assignments of -synuclein.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,6,1,,,,,,,,,,,,,,,,,,,,,,51,55,2012, citations,entry_citation,18861,95031,1,,entry citation,,,23681729,,,"Peptaibol antiamoebin I: spatial structure, backbone dynamics, interaction with bicelles and lipid-protein nanodiscs, and pore formation in context of barrel-stave model.",published,journal,Chem. Biodivers.,Chemistry & biodiversity,10,5,,,,,,,,,,,,,,,,,,,,,,838,863,2013, citations,entry_citation,18862,95054,1,,entry citation,,,23521511,,,Dramatic effect of furanose c2' substitution on structure and stability: directing the folding of the human telomeric quadruplex with a single fluorine atom,published,journal,J. Am. Chem. Soc.,,135,14,,,,,,,,,,,,,,,,,,,,,,5344,5347,2013, citations,entry_citation,18863,95075,1,,entry citation,,,24022996,,,Structure-guided design affirms inhibitors of hepatitis C virus p7 as a viable class of antivirals targeting virion release.,published,journal,Hepatology,"Hepatology (Baltimore, Md.)",59,2,,,,,,,,,,,,,,,,,,,,,,408,422,2014, citations,reference_citation,18863,95076,2,,reference citation,,,,,,"Structural and functional characterisation of the hepititis C virus proteins p7, NS2-3 and NS5A",published,thesis,,,,,,,,,,,,,,,,,,,,,,Leeds University,Leeds,UK,,,,, citations,entry_citation,18864,95123,1,,entry citation,,,,,,High resolution structure and dynamics of CsPinA parvulin at physiological temperature,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18865,95156,1,,entry citation,,,23973967,,,NMR solution structure and SRP54M predicted interaction of the N-terminal sequence (1-30) of the ovine Doppel protein,published,journal,Peptides,,49,,,,,,,,,,,,,,,,,,,,,,,32,40,2013, citations,entry_citation,18867,95173,1,,entry citation,,,23667548,,,Highly efficient NMR assignment of intrinsically disordered proteins: application to B- and T cell receptor domains,published,journal,PLoS One,,8,5,,,,,,,,,,,,,,,,,,,,,,e62947,e62947,2013, citations,entry_citation,18868,95194,1,,entry citation,,,23537648,,,Interaction of the S100A6 mutant (C3S) with the V domain of the receptor for advanced glycation end products (RAGE),published,journal,Biochem. Biophys. Res. Commun.,,434,2,,,,,,,,,,,,,,,,,,,,,,328,333,2013, citations,citation_1,18869,95215,1,,entry citation,,,,,,"Solution NMR Structure of CDK2-associated protein 2 (CDK2AP2; Deleted in Oral Cancer 1 Related protein, DOC-1R)",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1887,95247,1,,entry citation,,,,,"Chandrasekhar, Kasibhatla, Profy, Albert T., Dyson, H. Jane, ""Solution Conformational Preferences of Immunogenic Peptides Derived from the Principal Neutralizing Determinant of the HIV-1 Envelope Glycoprotein gp120,"" Biochemistry 30, 9187-9194 (1991).","Solution Conformational Preferences of Immunogenic Peptides Derived from the Principal Neutralizing Determinant of the HIV-1 Envelope Glycoprotein gp120",published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,9187,9194,1991, citations,entry_citation,18870,95261,1,,entry citation,,,,,,Solution structure of the dimerization domain of Aux/IAA transcription factor Ps-IAA4 from pea (Pisum sativum),in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,Citation_1,18871,95278,1,,entry citation,,,23523349,,,Substrate-Activated Conformational Switch on Chaperones Encodes a Targeting Signal in Type III Secretion,published,journal,Cell. Rep.,,3,3,,,,,,,,,,,,,,,,,,,,,,709,715,2013, citations,entry_citation,18872,95293,1,,entry citation,,,,,,ID3 stem,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18873,95312,1,,entry citation,,,24001318,,,Stabilization of Branched Oligosaccharides: Lewis(x) Benefits from a Nonconventional C-H...O Hydrogen Bond,published,journal,J. Am. Chem. Soc.,,135,36,,,,,,,,,,,,,,,,,,,,,,13464,13472,2013, citations,citation_1,18874,95334,1,,entry citation,,,20705953,10.1093/carcin/bgq171,,Functional impact of cancer-associated mutations in the tumor suppressor protein ING4,published,journal,Carinogenesis,,31,11,,,,,,,,,,,,,,,,,,,,,,1932,1938,2010, citations,SSbonds_JBC,18875,95356,1,,entry citation,,,23430740,,,"The Cyclic Cystine Ladder in -Defensins Is Important for Structure and Stability, but Not Antibacterial Activity.",published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,15,,,,,,,,,,,,,,,,,,,,,,10830,10840,2013, citations,citation_1,18876,95376,1,,entry citation,,,25591003,,,Structural convergence of unstructured p53 family transactivation domains in MDM2 recognition,published,journal,Cell Cycle,,14,4,,,,,,,,,,,,,,,,,,,,,,533,543,2015, citations,chemical_shift_assignment_of_Ca2+_bound_CaBP4,18877,95392,1,,entry citation,,,23925854,,,"(1)H, (15)N, and (13)C chemical shift assignments of murine calcium-binding protein 4.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,18878,95415,1,,entry citation,,,23656834,,,Nucleosomal DNA binding drives the recognition of H3K36-methylated nucleosomes by the PSIP1-PWWP domain.,published,journal,Epigenetics Chromatin,Epigenetics & chromatin,6,1,,,,,,,,,,,,,,,,,,,,,,12,12,2013, citations,entry_citation,18879,95434,1,,entry citation,,,,,,Solution NMR structures of the C-terminal segment of surfactant protein B (residues 59-80) in DPC detergent micelles and methanol.,submitted,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18880,95453,1,,entry citation,,,24790102,,,Structure of the Small Dictyostelium discoideum Myosin Light Chain MlcB Provides Insights into MyoB IQ motif Recognition.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,18881,95475,1,,entry citation,,,,,,Determinants of DNA cleavage site recognition in group II intron retrohoming - Solution structure and metal-ion binding sites of the Sc.ai5gamma RNA:DNA contact,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18882,95506,1,,entry citation,,,24255114,,,Structures and interface mapping of the TIR domain-containing adaptor molecules involved in interferon signaling,published,journal,Proc. Natl. Acad. Sci. U. S. A.,,110,49,,,,,,,,,,,,,,,,,,,,,,19908,19913,2013, citations,entry_citation,18883,95525,1,,entry citation,,,24255114,,,Structures and interface mapping of the TIR domain-containing adaptor molecules involved in interferon signaling,published,journal,Proc. Natl. Acad. Sci. U. S. A.,,110,49,,,,,,,,,,,,,,,,,,,,,,19908,19913,2013, citations,entry_citation,18884,95544,1,,entry citation,,,23667548,,,Highly efficient NMR assignment of intrinsically disordered proteins: application to B- and T cell receptor domains,published,journal,PLoS One,,8,5,,,,,,,,,,,,,,,,,,,,,,e62947,e62947,2013, citations,Rpt6-C,18885,95565,1,,entry citation,,,23562395,,,Conformational dynamics of the rpt6 ATPase in proteasome assembly and rpn14 binding.,published,journal,Structure,"Structure (London, England : 1993)",21,5,,,,,,,,,,,,,,,,,,,,,,753,765,2013, citations,entry_citation,18889,95624,1,,entry citation,,,23667548,,,Highly efficient NMR assignment of intrinsically disordered proteins: application to B- and T cell receptor domains,published,journal,PLoS One,,8,5,,,,,,,,,,,,,,,,,,,,,,e62947,e62947,2013, citations,entry_citation,1889,95648,1,,entry citation,,,,,"Satterlee, James D., Russell, David J., Erman, James E., ""Proton Homonuclear Correlated Spectroscopy as an Assignment Tool for Hyperfine-Shifted Resonances in Medium-Sized Paramagnetic Proteins: Cyanide-Ligated Yeast Cytochrome c Peroxidase as an Example,"" Biochemistry 30, 9072-9077 (1991).","Proton Homonuclear Correlated Spectroscopy as an Assignment Tool for Hyperfine-Shifted Resonances in Medium-Sized Paramagnetic Proteins: Cyanide-Ligated Yeast Cytochrome c Peroxidase as an Example",published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,9072,9077,1991, citations,entry_citation,18890,95661,1,,entry citation,,,23667548,,,Highly efficient NMR assignment of intrinsically disordered proteins: application to B- and T cell receptor domains,published,journal,PLoS One,,8,5,,,,,,,,,,,,,,,,,,,,,,e62947,e62947,2013, citations,entry_citation,18891,95682,1,,entry citation,,,16809815,,,Solution structure of the Tetrahymena telomerase RNA stem IV terminal loop,published,journal,RNA,,12,8,,,,,,,,,,,,,,,,,,,,,,1475,1485,2006, citations,entry_citation,18892,95702,1,,entry citation,,,16452301,,,Solution structure of the helix II template boundary element from Tetrahymena telomerase RNA,published,journal,Nucleic Acids Res.,,34,3,,,,,,,,,,,,,,,,,,,,,,816,825,2006, citations,entry_citation,18893,95722,1,,entry citation,,,24448450,,,NMR structure of the 5'-splice site in the group IIB intron Sc.ai5--conformational requirements for exon-intron recognition.,published,journal,RNA,"RNA (New York, N.Y.)",,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,18894,95751,1,,entry citation,,,24448450,,,NMR structure of the 5'-splice site in the group IIB intron Sc.ai5--conformational requirements for exon-intron recognition.,published,journal,RNA,"RNA (New York, N.Y.)",,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,18895,95781,1,,entry citation,,,23339032,,,Backbone and partial side chain assignment of the microtubule binding domain of the MAP1B light chain.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,citations,18896,95798,1,,entry citation,,,,,,Bi-Functional Lysozyme-Protease Inhibitor Protein from the Defense Gland of Coptotermes Formosanus Shiraki Soldiers (Isoptera: Rhinotermitidae),in preparation,journal,To be Published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18897,95820,1,,entry citation,,,23281027,,,Structure of the O-Glycosylated Conopeptide CcTx from Conus consors Venom.,published,journal,Chemistry,"Chemistry (Weinheim an der Bergstrasse, Germany)",19,3,,,,,,,,,,,,,,,,,,,,,,870,879,2013, citations,entry_citation,18898,95845,1,,entry citation,,,23417771,,,Backbone and side-chain assignments of a tethered complex between LMO4 and DEAF-1.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,18899,95863,1,,entry citation,,,23420131,,,"(1)H, (13)C, and (15)N backbone and side-chain chemical shift assignment of the toxin Doc in the unbound state",published,journal,Biomol. NMR Assignments,,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,189,95879,1,,entry citation,,,,,"Torchia, Dennis A., Sparks, Steven W., Bax, Ad, ""NMR Signal Assignments of Amide Protons in the alpha-Helical Domains of Staphylococcal Nuclease,"" Biochemistry 27 (14), 5135-5141 (1988).","NMR Signal Assignments of Amide Protons in the alpha-Helical Domains of Staphylococcal Nuclease",published,journal,Biochemistry,,27,14,,,,,,,,,,,,,,,,,,,,,,5135,5141,1988, citations,entry_citation,18900,95892,1,,entry citation,,,23574509,,,"Structure of Enterococcus faeciuml,d-transpeptidase acylated by ertapenem provides insight into the inactivation mechanism.",published,journal,ACS Chem. Biol.,ACS chemical biology,8,6,,,,,,,,,,,,,,,,,,,,,,1140,1146,2013, citations,entry_citation,18901,95914,1,,entry citation,,,,,,NMR structure of the C-terminal domain of the protein HCFC1 from MUS MUSCULUS,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18902,95930,1,,entry citation,,,24005038,,,Solution structure of the major G-quadruplex formed in the human VEGF promoter in K+: insights into loop interactions of the parallel G-quadruplexes.,published,journal,Nucleic Acids Res.,Nucleic acids research,41,22,,,,,,,,,,,,,,,,,,,,,,10584,10592,2013, citations,entry_citation,18903,95944,1,,entry citation,,,24515886,,,Spectral density mapping protocols for analysis of molecular motions in disordered proteins.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,18904,95968,1,,entry citation,,,,,,NMR solution structure of the two domain PPIase SlpA from Escherichia coli,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18905,95985,1,,entry citation,,,,,,NMR structure of the RRM2 domain of the protein RBM10 from homo sapiens,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18906,96000,1,,entry citation,,,23417793,,,"1H, 13C and 15N resonance assignments of an N-terminal domain of CHD4",published,journal,Biomol. NMR Assignments,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,18907,96016,1,,entry citation,,,,,,Structural Insights of DNA Duplex Stabilization by Potent Antimicrobial Peptide Indolicidin.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18908,96033,1,,entry citation,,,23417675,,,Structure and interactions of the human programmed cell death 1 receptor.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,17,,,,,,,,,,,,,,,,,,,,,,11771,11785,2013, citations,entry_citation,18909,96053,1,,entry citation,,,,,,NMR solution structure of the SANT domain of human DnaJC2.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1891,96077,1,,entry citation,,,,,"Lee, Bong Jin, Aiba, Hiroji, Kyogoku, Yoshimasa, ""Nuclear Magnetic Resonance Study on the Structure and Interaction of Cyclic AMP Receptor Protein and Its Mutants: A Deuterium-Labeling and Photo-CIDNP Study,"" Biochemistry 30, 9047-9054 (1991).","Nuclear Magnetic Resonance Study on the Structure and Interaction of Cyclic AMP Receptor Protein and Its Mutants: A Deuterium-Labeling and Photo-CIDNP Study",published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,9047,9054,1991, citations,entry_citation,18910,96090,1,,entry citation,,,,,,NMR SOLUTION STRUCTURE OF THE AVR3A11 FROM PHYTOPHTHORA CAPSI,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18911,96112,1,,entry citation,,,23574509,,,"Structure of Enterococcus faeciuml,d-transpeptidase acylated by ertapenem provides insight into the inactivation mechanism.",published,journal,ACS Chem. Biol.,ACS chemical biology,8,6,,,,,,,,,,,,,,,,,,,,,,1140,1146,2013, citations,entry_citation,18912,96136,1,,entry citation,,,23521534,,,The membrane-proximal domain of ADAM17 represents the putative molecular switch of its shedding activity operated by protein-disulfide isomerase,published,journal,J. Am. Chem. Soc.,,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,citation_1,18912,96137,2,,reference citation,,,,,,The membrane-proximal domain of ADAM17 represents the putative molecular switch of its shedding activity operated by protein-disulfide isomerase,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18913,96151,1,,entry citation,,,23430740,,,"The Cyclic Cystine Ladder in -Defensins Is Important for Structure and Stability, but Not Antibacterial Activity.",published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,15,,,,,,,,,,,,,,,,,,,,,,10830,10840,2013, citations,entry_citation,18914,96171,1,,entry citation,,,23430740,,,"The Cyclic Cystine Ladder in -Defensins Is Important for Structure and Stability, but Not Antibacterial Activity.",published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,15,,,,,,,,,,,,,,,,,,,,,,10830,10840,2013, citations,entry_citation,18915,96191,1,,entry citation,,,25044683,,,"Micelle bound structure and DNA interaction of brevinin-2-related peptide, an antimicrobial peptide derived from frog skin",published,journal,J. Pept. Sci.,Journal of peptide science : an official publication of the European Peptide Society,20,10,,1099-1387,,,,,,,,,,,,,,,,,,,,811,821,2014, citations,entry_citation,18916,96207,1,,entry citation,,,23747975,,,NMR mapping of PCNA interaction with translesion synthesis DNA polymerase Rev1 mediated by Rev1-BRCT domain.,published,journal,J. Mol. Biol.,Journal of molecular biology,425,17,,,,,,,,,,,,,,,,,,,,,,3091,3105,2013, citations,entry_citation,18917,96228,1,,entry citation,,,,,,"NMR solution structure of the N-terminal STM1478, from Salmonella typhimurium LT2",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,18918,96252,1,,entry citation,,,23480024,,,The denatured state ensemble contains significant local and long-range structure under native conditions: analysis of the N-terminal domain of ribosomal protein L9.,published,journal,Biochemistry,Biochemistry,52,15,,,,,,,,,,,,,,,,,,,,,,2662,2671,2013, citations,entry_citation,18919,96268,1,,entry citation,,,24105099,,,"(1)H, (13)C and (15)N resonance assignments for the full-length mammalian cytochrome b5 in a membrane environment.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,1892,96286,1,,entry citation,,,,,"Lee, Bong Jin, Aiba, Hiroji, Kyogoku, Yoshimasa, ""Nuclear Magnetic Resonance Study on the Structure and Interaction of Cyclic AMP Receptor Protein and Its Mutants: A Deuterium-Labeling and Photo-CIDNP Study,"" Biochemistry 30, 9047-9054 (1991).","Nuclear Magnetic Resonance Study on the Structure and Interaction of Cyclic AMP Receptor Protein and Its Mutants: A Deuterium-Labeling and Photo-CIDNP Study",published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,9047,9054,1991, citations,entry_citation,18920,96299,1,,entry citation,,,,,,Characterization of putative readers of epigenetic methyl-marks from Entamoeba histolytica,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18921,96320,1,,entry citation,,,23447530,,,Structural integrity of the b24 site in human insulin is important for hormone functionality.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,15,,,,,,,,,,,,,,,,,,,,,,10230,10240,2013, citations,entry_citation,18922,96338,1,,entry citation,,,23861396,,,Structural basis of a physical blockage mechanism for the interaction of response regulator PmrA with connector protein PmrD from Klebsiella pneumoniae.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,35,,,,,,,,,,,,,,,,,,,,,,25551,25561,2013, citations,entry_citation,18923,96354,1,,entry citation,,,23447530,,,Structural integrity of the b24 site in human insulin is important for hormone functionality.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,15,,,,,,,,,,,,,,,,,,,,,,10230,10240,2013, citations,entry_citation,18924,96372,1,,entry citation,,,23447530,,,Structural integrity of the b24 site in human insulin is important for hormone functionality.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,15,,,,,,,,,,,,,,,,,,,,,,10230,10240,2013, citations,entry_citation,18925,96390,1,,entry citation,,,23447530,,,Structural integrity of the b24 site in human insulin is important for hormone functionality.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,15,,,,,,,,,,,,,,,,,,,,,,10230,10240,2013, citations,entry_citation,18926,96408,1,,entry citation,,,24116036,,,Novel Inhibitor Cystine Knot Peptides from Momordica charantia,published,journal,PLoS One,,8,10,,,,,,,,,,,,,,,,,,,,,,e75334,e75334,2013, citations,entry_citation,18927,96422,1,,entry citation,,,23762412,,,"The C-terminal V5 domain of Protein Kinase C is intrinsically disordered, with propensity to associate with a membrane mimetic.",published,journal,PLoS ONE,PloS one,8,6,,,,,,,,,,,,,,,,,,,,,,e65699,e65699,2013, citations,entry_citation,18928,96437,1,,entry citation,,,23762412,,,"The C-terminal V5 domain of Protein Kinase C is intrinsically disordered, with propensity to associate with a membrane mimetic.",published,journal,PLoS ONE,PloS one,8,6,,,,,,,,,,,,,,,,,,,,,,e65699,e65699,2013, citations,entry_citation,18929,96452,1,,entry citation,,,23762412,,,"The C-terminal V5 domain of Protein Kinase C is intrinsically disordered, with propensity to associate with a membrane mimetic.",published,journal,PLoS ONE,PloS one,8,6,,,,,,,,,,,,,,,,,,,,,,e65699,e65699,2013, citations,entry_citation,1893,96469,1,,entry citation,,,,,"Xu, Guang-Yi, Deber, Charles M., ""Conformations of neurotensin in solution and in membrane environments studied by 2D-NMR spectroscopy,"" Int. J. Pept. Protein Res. 37, 528-535 (1991).","Conformations of neurotensin in solution and in membrane environments studied by 2D-NMR spectroscopy",published,journal,Int. J. Pept. Protein Res.,,37,,,,,,,,,,,,,,,,,,,,,,,528,535,1991, citations,entry_citation,18930,96483,1,,entry citation,,,23762412,,,"The C-terminal V5 domain of Protein Kinase C is intrinsically disordered, with propensity to associate with a membrane mimetic.",published,journal,PLoS ONE,PloS one,8,6,,,,,,,,,,,,,,,,,,,,,,e65699,e65699,2013, citations,entry_citation,18931,96500,1,,entry citation,,,23430740,,,"The Cyclic Cystine Ladder in -Defensins Is Important for Structure and Stability, but Not Antibacterial Activity.",published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,15,,,,,,,,,,,,,,,,,,,,,,10830,10840,2013, citations,entry_citation,18933,96520,1,,entry citation,,,24617852,,,How a low-fidelity DNA polymerase chooses non-watson-crick from watson-crick incorporation.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,136,13,,,,,,,,,,,,,,,,,,,,,,4927,4937,2014, citations,entry_citation,18934,96537,1,,entry citation,,,24617852,,,How a low-fidelity DNA polymerase chooses non-watson-crick from watson-crick incorporation.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,136,13,,,,,,,,,,,,,,,,,,,,,,4927,4937,2014, citations,entry_citation,18935,96559,1,,entry citation,,,24617852,,,How a low-fidelity DNA polymerase chooses non-watson-crick from watson-crick incorporation.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,136,13,,,,,,,,,,,,,,,,,,,,,,4927,4937,2014, citations,entry_citation,18937,96581,1,,entry citation,,,23430740,,,"The Cyclic Cystine Ladder in -Defensins Is Important for Structure and Stability, but Not Antibacterial Activity.",published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,15,,,,,,,,,,,,,,,,,,,,,,10830,10840,2013, citations,entry_citation,18938,96602,1,,entry citation,,,23430740,,,"The Cyclic Cystine Ladder in -Defensins Is Important for Structure and Stability, but Not Antibacterial Activity.",published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,15,,,,,,,,,,,,,,,,,,,,,,10830,10840,2013, citations,citations,18940,96641,1,,entry citation,,,24200677,,,Structural analysis of the starfish SALMFamide neuropeptides S1 and S2: the N-terminal region of S2 facilitates self-association.,published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1844,2,,,,,,,,,,,,,,,,,,,,,,358,365,2014, citations,entry_citation,18941,96656,1,,entry citation,,,17868072,10.1111/j.1747-0285.2007.00566.x,,ICAM-1 peptide inhibitors of T-cell adhesion bind to the allosteric site of LFA-1. An NMR characterization,published,journal,Chem. Biol. Drug Design,,70,4,,,,,,,,,,,,,,,,,,,,,,347,353,2007, citations,entry_citation,18942,96673,1,,entry citation,,,24187131,,,The structure of integrin 1I domain in complex with a collagen-mimetic peptide.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,52,,,,,,,,,,,,,,,,,,,,,,36796,36809,2013, citations,entry_citation,18943,96694,1,,entry citation,,,24312273,,,New insights into histidine triad proteins: solution structure of a Streptococcus pneumoniae PhtD domain and zinc transfer to AdcAII.,published,journal,PLoS ONE,PloS one,8,11,,,,,,,,,,,,,,,,,,,,,,e81168,e81168,2013, citations,reference_citation_1,18943,96695,2,,reference citation,,,21425866,,,Biochemical characterization of the histidine triad protein PhtD as a cell surface zinc-binding protein of Pneumococcus,published,journal,Biochemistry,Biochemistry,50,17,,,,,,,,,,,,,,,,,,,,,,3551,3558,2011, citations,entry_citation,18944,96717,1,,entry citation,,,27396829,,,Dynamic Local Polymorphisms in the Gbx1 Homeodomain Induced by DNA Binding,published,journal,Structure,,24,8,,,,,,,,,,,,,,,,,,,,,,1372,1379,2016, citations,entry_citation,18945,96736,1,,entry citation,,,,,,NMR study of k-Ssm1a,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation_1,18946,96754,1,,reference citation,,,1440641,,,"Identification of insecticidal peptides from venom of the trap-door spider, Aptostichus schlingeri (Ctenizidae)",published,journal,Toxicon,,30,,,,,,,,,,,,,,,,,,,,,,,1043,1050,1992, citations,entry_citation_2,18946,96755,2,,entry citation,,,,,,"The insecticidal toxin Aps III is an atypical knottin peptide that potently blocks insect voltage-gated sodium channels",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18947,96775,1,,entry citation,,,23489133,,,The missing linker: a dimerization motif located within polyketide synthase modules.,published,journal,ACS Chem. 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Biochem.,,107,,,,,,,,,,,,,,,,,,,,,,,304,309,1990, citations,entry_citation,18950,96830,1,,entry citation,,,24012551,,,NMR structure of 2'-O-(2-methoxyethyl) modified and C5-methylated RNA dodecamer duplex.,published,journal,Biochimie,,95,12,,,,,,,,,,,,,,,,,,,,,,2385,2391,2013, citations,entry_citation,18951,96852,1,,entry citation,,,,,,Centromere epigenome stability is mediated by structural recognition by the Centromere Licensing Complex,in preparation,journal,Science,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18952,96870,1,,entry citation,,,24207128,,,Structural Dynamics and Topology of Phosphorylated Phospholamban Homopentamer Reveal Its Role in the Regulation of Calcium Transport,published,journal,Structure,,21,12,,,,,,,,,,,,,,,,,,,,,,2119,2130,2013,doi 10.1016/j.str.2013.09.008 citations,entry_citation,18953,96898,1,,entry citation,,,23597261,,,"Structure and Dynamics of the Fish Eye Lens Protein, M7-Crystallin.",published,journal,Biochemistry,Biochemistry,52,20,,,,,,,,,,,,,,,,,,,,,,3579,3587,2013, citations,entry_citation,18954,96919,1,,entry citation,,,,,,NMR structure of the GUCT domain from human DEAD box polypeptide 21 (DDX21),in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18955,96938,1,,entry citation,,,23994011,,,Two singular types of CCCH tandem zinc finger in Nab2p contribute to polyadenosine RNA recognition.,published,journal,Structure,"Structure (London, England : 1993)",21,10,,,,,,,,,,,,,,,,,,,,,,1800,1811,2013, citations,entry_citation,18956,96962,1,,entry citation,,,23994011,,,Two singular types of CCCH tandem zinc finger in Nab2p contribute to polyadenosine RNA recognition.,published,journal,Structure,"Structure (London, England : 1993)",21,10,,,,,,,,,,,,,,,,,,,,,,1800,1811,2013, citations,entry_citation,18958,96986,1,,entry citation,,,24069290,,,Transmembrane and Juxtamembrane Structure of L Integrin in Bicelles.,published,journal,PLoS ONE,PloS one,8,9,,,,,,,,,,,,,,,,,,,,,,e74281,e74281,2013, citations,entry_citation,18959,97009,1,,entry citation,,,24234454,,,Characterization of the interaction between protein Snu13p/15.5K and the Rsa1p/NUFIP factor and demonstration of its functional importance for snoRNP assembly.,published,journal,Nucleic Acids Res.,Nucleic acids research,42,3,,,,,,,,,,,,,,,,,,,,,,2015,2036,2014, citations,entry_citation,18961,97029,1,,entry citation,,,23824732,,,NMR assignments of a hypothetical pseudo-knotted protein HP0242 from Helicobacter pylori.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,18963,97046,1,,entry citation,,,23579637,,,NMR structure note: PHD domain from death inducer obliterator protein and its interaction with H3K4me3,published,journal,J. Biomol. NMR,,56,2,,,,,,,,,,,,,,,,,,,,,,183,190,2013, citations,entry_citation,18964,97068,1,,entry citation,,,24200193,,,Characterization of a Novel -Conotoxin TxID from Conus textile That Potently Blocks Rat 34 Nicotinic Acetylcholine Receptors.,published,journal,J. Med. Chem.,Journal of medicinal chemistry,56,23,,,,,,,,,,,,,,,,,,,,,,9655,9663,2013, citations,entry_citation,18965,97086,1,,entry citation,,,24499386,,,Solution structure of a sponge-derived cystine knot peptide and its notable stability.,published,journal,J. Nat. Prod.,Journal of natural products,77,2,,,,,,,,,,,,,,,,,,,,,,304,310,2014, citations,entry_citation,18966,97103,1,,entry citation,,,23386723,,,Specific DNA recognition mediated by a type IV pilin.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,110,8,,,,,,,,,,,,,,,,,,,,,,3065,3070,2013, citations,entry_citation,18967,97118,1,,entry citation,,,23638119,,,Structural insights into a wildtype domain of the oncoprotein E6 and its interaction with a PDZ domain,published,journal,PLOS One,,8,4,,,,,,,,,,,,,,,,,,,,,,e62584,e62584,2013, citations,citation1,18968,97139,1,,entry citation,,,,,,Diffuse binding of Zn2+ to the denatured ensemble of Cu/Zn superoxide dismutase 1,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18969,97155,1,,entry citation,,,23979961,,,"(1)H, (13)C and (15)N NMR assignments of a mutant of UV inducible transcript (S55A-UVI31+) from Chlamydomonas reinhardtii.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,18970,97170,1,,entry citation,,,23988198,,,Therapeutic potential of the peptide leucine arginine as a new nonplant bowman-birk-like serine protease inhibitor.,published,journal,J. Med. Chem.,Journal of medicinal chemistry,56,17,,,,,,,,,,,,,,,,,,,,,,6732,6744,2013, citations,entry_citation,18971,97190,1,,entry citation,,,23665454,,,Structure and dynamics of human Nedd4-1 WW3 in complex with the ENaC PY motif.,published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1834,8,,,,,,,,,,,,,,,,,,,,,,1632,1641,2013, citations,entry_citation,18972,97226,1,,entry citation,,,23567999,,,"Identification, structural and pharmacological characterization of tau-CnVA, a conopeptide that selectively interacts with somatostatin sst3 receptor",published,journal,Biochem. Pharmacol.,,85,11,,,,,,,,,,,,,,,,,,,,,,1663,1671,2013, citations,entry_citation,18973,97244,1,,entry citation,,,24384094,,,Structure and Dynamics of DNA Duplexes Containing a Cluster of Mutagenic 8-Oxoguanine and Abasic Site Lesions.,published,journal,J. Mol. Biol.,Journal of molecular biology,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,18974,97262,1,,entry citation,,,24371282,,,Structure modulation of helix 69 from Escherichia coli 23S ribosomal RNA by pseudouridylations.,published,journal,Nucleic Acids Res.,Nucleic acids research,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,18975,97282,1,,entry citation,,,24371282,,,Structure modulation of helix 69 from Escherichia coli 23S ribosomal RNA by pseudouridylations.,published,journal,Nucleic Acids Res.,Nucleic acids research,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,18976,97301,1,,entry citation,,,23630096,,,A single mutation in a regulatory protein produces evolvable allosterically regulated catalyst of nonnatural reaction,published,journal,Angew. Chem. Int. Ed. Engl.,,52,24,,,,,,,,,,,,,,,,,,,,,,6246,6249,2013, citations,entry_citation,18977,97328,1,,entry citation,,,22392344,,,"Backbone and sidechain (1)H, (15)N and (13)C assignments of Tyrosine Phosphatase related to Biofilm formation A (TpbA) of Pseudomonas aeruginosa.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,1,,,,,,,,,,,,,,,,,,,,,,57,59,2013, citations,entry_citation,18978,97347,1,,entry citation,,,20961124,,,Optimized measurement temperature gives access to the solution structure of a 49 kDa homohexameric -propeller.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,132,44,,,,,,,,,,,,,,,,,,,,,,15692,15698,2010, citations,reference_citation,18978,97348,2,,reference citation,,,20961124,10.1021/ja1064608,,Optimized measurement temperature gives access to the solution structure of a 49 kDa homohexameric -propeller,published,journal,J. Am. Chem. 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Biol.,Journal of molecular biology,426,7,,,,,,,,,,,,,,,,,,,,,,1524,1538,2014, citations,entry_citation,18982,97427,1,,entry citation,,,24155902,,,Protein-Protein Interactions as a Strategy towards Protein-Specific Drug Design: The Example of Ataxin-1,published,journal,PLoS One,,8,10,,,,,,,,,,,,,,,,,,,,,,e76456,e76456,2013, citations,Citation_2,18982,97428,2,,reference citation,,,,,,"1H,13C, and 15N resonance assignment of the ataxin-1 AXH domain in complex with CIC ligand peptide",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18984,97450,1,,entry citation,,,24384094,,,Structure and dynamics of DNA duplexes containing a cluster of mutagenic 8-oxoguanine and abasic site lesions.,published,journal,J. Mol. Biol.,Journal of molecular biology,426,7,,,,,,,,,,,,,,,,,,,,,,1524,1538,2014, citations,entry_citation,18985,97467,1,,entry citation,,,24384094,,,Structure and dynamics of DNA duplexes containing a cluster of mutagenic 8-oxoguanine and abasic site lesions.,published,journal,J. Mol. Biol.,Journal of molecular biology,426,7,,,,,,,,,,,,,,,,,,,,,,1524,1538,2014, citations,entry_citation,18986,97484,1,,entry citation,,,23934138,,,"(1)H, (15)N and (13)C chemical shift assignments for the winged helix domains of two archeal MCM C-termini.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,citation_SACOL0876,18987,97502,1,,entry citation,,,,,,"Solution NMR structure of SACOL0876 from Staphylococcus aureus COL, NESG target ZR353 and CSGID target IDP00841",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,18988,97531,1,,entry citation,,,23379514,,,Small Molecule Antivirulents Targeting the Iron-Regulated Heme Oxygenase (HemO) of P. aeruginosa.,published,journal,J. Med. Chem.,Journal of medicinal chemistry,56,5,,,,,,,,,,,,,,,,,,,,,,2097,2109,2013, citations,citations,18989,97548,1,,entry citation,,,,,,"Solution NMR structure of the Polyketide_cyc-like protein Cgl2372 from Corynebacterium glutamicum, Northeast Structural Genomics Consortium Target CgR160.",in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,18990,97575,1,,entry citation,,,,,,A molecular explanation for the recessive nature of parkin-linked Parkinson's disease,published,journal,Nat. Commun.,,4,1983,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,18991,97600,1,,entry citation,,,23682711,,,[2Fe-2S]-Ferredoxin Binds Directly to Cysteine Desulfurase and Supplies an Electron for Iron-Sulfur Cluster Assembly but Is Displaced by the Scaffold Protein or Bacterial Frataxin.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,135,22,,,,,,,,,,,,,,,,,,,,,,8117,8120,2013, citations,entry_citation,18992,97619,1,,entry citation,,,23682711,,,[2Fe-2S]-Ferredoxin Binds Directly to Cysteine Desulfurase and Supplies an Electron for Iron-Sulfur Cluster Assembly but Is Displaced by the Scaffold Protein or Bacterial Frataxin.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,135,22,,,,,,,,,,,,,,,,,,,,,,8117,8120,2013, citations,entry_citation,18993,97638,1,,entry citation,,,23715812,,,"Backbone resonance assignment of Alt a 1, a unique -barrel protein and the major allergen of Alternaria alternata.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,Entry_Citation,18994,97655,1,,entry citation,,,24414223,,,"(1)H, (13)C and (15)N chemical shift assignments for the cyclic-nucleotide binding homology domain of a KCNH channel.",published,journal,Biomol. 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Virol.,Journal of virology,87,10,,,,,,,,,,,,,,,,,,,,,,5318,5330,2013, citations,citation1,19004,97839,1,,entry citation,,,23517193,,,"Expression, Purification, Characterization, and Solution Nuclear Magnetic Resonance Study of Highly Deuterated Yeast Cytochrome c Peroxidase with Enhanced Solubility",published,journal,Biochemistry,,52,13,,,,,,,,,,,,,,,,,,,,,,2165,2175,2013, citations,citation1,19005,97859,1,,entry citation,,,23517193,,,"Expression, Purification, Characterization, and Solution Nuclear Magnetic Resonance Study of Highly Deuterated Yeast Cytochrome c Peroxidase with Enhanced Solubility",published,journal,Biochemistry,,52,13,,,,,,,,,,,,,,,,,,,,,,2165,2175,2013, citations,entry_citation,19006,97879,1,,entry citation,,,23604692,,,Chemical shift assignments and secondary structure prediction of the phosphorelay protein VanU from Vibrio anguillarum.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,8,1,,,,,,,,,,,,,,,,,,,,,,177,179,2014, citations,citations,19007,97897,1,,entry citation,,,24366721,,,Backbone and side chain NMR assignments for the N-terminal domain of the cell division regulator MinC from Bacillus subtilis.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,19008,97919,1,,entry citation,,,23475644,,,"Chemical shift assignments and secondary structure prediction of the master biofilm regulator, SinR, from Bacillus subtilis.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,8,1,,,,,,,,,,,,,,,,,,,,,,155,158,2014, citations,entry_citation,19009,97941,1,,entry citation,,,24034249,,,Molecular Structure of beta-Amyloid Fibrils in Alzheimer's Disease Brain Tissue,published,journal,Cell,,154,6,,,,,,,,,,,,,,,,,,,,,,1257,1268,2013, citations,entry_citation,19010,97957,1,,entry citation,,,24469996,,,"(1)H, (15)N and (13)C backbone chemical shift assignment of titin domains A59-A60 and A60 alone.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,19011,97977,1,,entry citation,,,24469996,,,"(1)H, (15)N and (13)C backbone chemical shift assignment of titin domains A59-A60 and A60 alone.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,19012,97997,1,,entry citation,,,,,,NMR structure of hypothetical protein BT_0846 from Bacteroides thetaiotaomicron VPI-5482 (NP_809759.1),in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,19013,98016,1,,entry citation,,,,,,Solution structure of the RRM domain of the hypothetical protein CAGL0M09691g from Candida glabrata,in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,19014,98038,1,,entry citation,,,,,,"Solution structure of the putative Ras interaction domain of AFD-1, isoform a from Caenorhabditis elegans",in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,19015,98064,1,,entry citation,,,23771857,,,Backbone resonance assignments for G protein alpha i3 subunit in the GDP-bound state,published,journal,Biomol. NMR Assignments,,8,2,,,,,,,,,,,,,,,,,,,,,,237,241,2014, citations,entry_citation,19017,98085,1,,entry citation,,,23521617,,,Bulges in g-quadruplexes: broadening the definition of g-quadruplex-forming sequences.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,135,13,,,,,,,,,,,,,,,,,,,,,,5017,5028,2013, citations,entry_citation,19018,98099,1,,entry citation,,,23416053,,,The impact of aminoglycosides on the dynamics of translation elongation.,published,journal,Cell Rep.,Cell reports,3,2,,,,,,,,,,,,,,,,,,,,,,497,508,2013, citations,entry_citation,19023,98117,1,,entry citation,,,23548911,,,Structural characterization of Mycobacterium tuberculosis RNA polymerase binding protein A (RbpA) and its interactions with sigma factors,published,journal,J. Biol. Chem.,,288,20,,,,,,,,,,,,,,,,,,,,,,14438,14450,2013, citations,entry_citation,19024,98138,1,,entry citation,,,,,,Binding of a naphtyridine analogue to the single G-bulge in a conserved regulatory region of the HEV genome,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19025,98155,1,,entry citation,,,23648839,,,Three-Dimensional Structure of CAP-Gly Domain of Mammalian Dynactin Determined by Magic Angle Spinning NMR Spectroscopy: Conformational Plasticity and Interactions with End-Binding Protein EB1.,published,journal,J. Mol. Biol.,Journal of molecular biology,425,22,,,,,,,,,,,,,,,,,,,,,,4249,4266,2013, citations,citations,19026,98171,1,,entry citation,,,23760503,,,Analysis of the Structural and Molecular Basis of Voltage-sensitive Sodium Channel Inhibition by the Spider Toxin Huwentoxin-IV (-TRTX-Hh2a).,published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,31,,,,,,,,,,,,,,,,,,,,,,22707,22720,2013, citations,citations,19027,98185,1,,entry citation,,,,,,"Backbone 1H, 13C, and 15N Chemical Shift Assignments for rubredoxin type protein from Mycobacterium ulcerans",in preparation,journal,To be Published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19029,98217,1,,entry citation,,,25726759,10.1038/srep08617,,Dynamic association of PfEMP1 and KAHRP in knobs mediates cytoadherence during Plasmodium invasion,published,journal,Sci Rep.,,5,,,,,,,,,,,,,,,,,,,,,,,8617,8617,2015, citations,citations,19030,98233,1,,entry citation,,,23760503,,,Analysis of the Structural and Molecular Basis of Voltage-sensitive Sodium Channel Inhibition by the Spider Toxin Huwentoxin-IV (-TRTX-Hh2a).,published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,31,,,,,,,,,,,,,,,,,,,,,,22707,22720,2013, citations,entry_citation,19031,98247,1,,entry citation,,,23648839,,,Three-Dimensional Structure of CAP-Gly Domain of Mammalian Dynactin Determined by Magic Angle Spinning NMR Spectroscopy: Conformational Plasticity and Interactions with End-Binding Protein EB1.,published,journal,J. Mol. Biol.,Journal of molecular biology,425,22,,,,,,,,,,,,,,,,,,,,,,4249,4266,2013, citations,citations,19032,98263,1,,entry citation,,,23760503,,,Analysis of the Structural and Molecular Basis of Voltage-sensitive Sodium Channel Inhibition by the Spider Toxin Huwentoxin-IV (-TRTX-Hh2a).,published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,31,,,,,,,,,,,,,,,,,,,,,,22707,22720,2013, citations,entry_citation,19033,98277,1,,entry citation,,,,,,NMR structure of the SH3 domain of human RAS p21 protein activator (GTPase activating protein) 1,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19034,98296,1,,entry citation,,,,,,NMR Structure of the third RNA Recognition Motif (RRM) of U2 small nuclear ribonucleoprotein auxiliary factor (U2AF) 2,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19035,98315,1,,entry citation,,,23935071,,,G-rich VEGF aptamer with locked and unlocked nucleic acid modifications exhibits a unique G-quadruplex fold.,published,journal,Nucleic Acids Res.,Nucleic acids research,41,20,,,,,,,,,,,,,,,,,,,,,,9524,9536,2013, citations,entry_citation,19036,98338,1,,entry citation,,,23607618,,,NMR Structure of Calmodulin Complexed to an N-Terminally Acetylated -Synuclein Peptide.,published,journal,Biochemistry,Biochemistry,52,20,,,,,,,,,,,,,,,,,,,,,,3436,3445,2013, citations,entry_citation,19037,98362,1,,entry citation,,,23448979,,,Neuroblastoma tumorigenesis is regulated through the Nm23-H1/h-Prune C-terminal interaction.,published,journal,Sci. Rep.,Scientific reports,3,,,,,,,,,,,,,,,,,,,,,,,1351,1351,2013, citations,entry_citation,19038,98377,1,,entry citation,,,23856620,,,The structure of the cytochrome p450cam-putidaredoxin complex determined by paramagnetic NMR spectroscopy and crystallography.,published,journal,J. Mol. Biol.,Journal of molecular biology,425,22,,,,,,,,,,,,,,,,,,,,,,4353,4365,2013, citations,entry_citation,19039,98401,1,,entry citation,,,,,,Acid-base equilibria near neutral pH in the catalytic triad and the bulge of domain 5 of a bacterial group II intron,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19040,98436,1,,entry citation,,,23472843,,,Structural principles of RNA catalysis in a 2'-5' lariat-forming ribozyme,published,journal,J. Am. Chem. Soc.,,135,11,,,,,,,,,,,,,,,,,,,,,,4403,4411,2013, citations,citations,19041,98459,1,,entry citation,,,,,,Spatial structure of dimeric VEGFR2 membrane domain in DPC micelles,in preparation,journal,To be Published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,Citation_1,19042,98476,1,,entry citation,,,23616103,,,"1H, 13C, and 15N backbone and side chain NMR resonance assignments of BPSL1050 from Burkholderia pseudomallei.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,8,1,,,,,,,,,,,,,,,,,,,,,,181,184,2014, citations,entry_citation,19043,98498,1,,entry citation,,,23924760,,,High-affinity binding to staphylococcal protein A by an engineered dimeric Affibody molecule.,published,journal,Protein Eng. Des. Sel.,"Protein engineering, design & selection : PEDS",26,10,,,,,,,,,,,,,,,,,,,,,,635,644,2013, citations,entry_citation,19044,98519,1,,entry citation,,,,,,"Backbone and Side Chain 1H, 13C and 15N Chemical Shift Assignments for Domain 4 of Phosphomannomutase/Phosphoglucomutase from Pseudomonas aeruginosa",in preparation,BMRB only,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19045,98534,1,,entry citation,,,23604079,,,BID-induced structural changes in BAK promote apoptosis.,published,journal,Nat. Struct. Mol. Biol.,Nature structural & molecular biology,20,5,,,,,,,,,,,,,,,,,,,,,,589,597,2013, citations,entry_citation,19046,98554,1,,entry citation,,,23640000,,,"Sequence-specific backbone 1H, 13C and 15N assignments of the 34 kDa catalytic domain of PTPN5 (STEP).",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,8,1,,,,,,,,,,,,,,,,,,,,,,185,188,2014, citations,Structure_citation,19047,98576,1,,entry citation,,,23838816,,,"Complete 1H, 15N and 13C resonance assignments of Bacillus cereus metallo-beta-lactamase and its complex with the inhibitor R-thiomandelic acid",published,journal,Biomol. NMR Assign.,,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,19047,98577,2,,entry citation,,,,,,"Complete 1H, 15N and 13C Resonance Assignments of the 25 kDa Bacillus cereus Metallo-Beta-Lactamase BcII and its Complex with the Broad Spectrum Inhibitor R-Thiomandelic Acid",in preparation,journal,Biomol. NMR Assignments,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation_1,19048,98607,1,,entry citation,,,23838816,,,"Complete 1H, 15N and 13C resonance assignments of Bacillus cereus metallo-beta-lactamase and its complex with the inhibitor R-thiomandelic acid",published,journal,Biomol. NMR Assign.,,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,19049,98638,1,,entry citation,,,23931315,,,Investigation of homeodomain membrane translocation properties: insights from the structure determination of engrailed-2 homeodomain in aqueous and membrane-mimetic environments,published,journal,Biophys. J.,,105,3,,,,,,,,,,,,,,,,,,,,,,667,678,2013, citations,entry_citation,19050,98658,1,,entry citation,,,28343066,10.1016/j.bpc.2017.02.006,,Calcium triggers reversal of calmodulin on nested anti-parallel sites in the IQ motif of the neuronal voltage-dependent sodium channel NaV1.2.,published,journal,Biophys. Chem.,,224,,,,,,,,,,,,,,,,,,,,,,,1,19,2017, citations,entry_citations,19050,98659,2,,reference citation,,,21439835,10.1016/j.str.2011.02.009,,"Structural and Energetic Determinants of Apo Calmodulin Binding to the IQ Motif of the NaV1.2 Voltage-Dependent Sodium Channel",published,journal,Structure,,19,,,,,,,,,,,,,,,,,,,,,,,733,747,2011, citations,entry_citation,19051,98686,1,,entry citation,,,23712306,,,"(1)H, (13)C, and (15)N backbone resonance assignments of the 37kDa voltage-gated Ca(2+) channel 4 subunit core SH3-GK domains.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,19052,98702,1,,entry citation,,,24696482,,,Ebolavirus Entry Requires a Compact Hydrophobic Fist at the Tip of the Fusion Loop.,published,journal,J. Virol.,Journal of virology,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,19053,98717,1,,entry citation,,,24184277,,,Intramolecular Donor Strand Complementation in the E. coli Type 1 Pilus Subunit FimA Explains the Existence of FimA Monomers As Off-Pathway Products of Pilus Assembly That Inhibit Host Cell Apoptosis.,published,journal,J. Mol. Biol.,Journal of molecular biology,426,3,,,,,,,,,,,,,,,,,,,,,,542,549,2014, citations,entry_citation,19054,98732,1,,entry citation,,,24158446,,,"Structural insights of tBid, the caspase-8-activated Bid, and its BH3 domain.",published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,50,,,,,,,,,,,,,,,,,,,,,,35840,35851,2013, citations,entry_citation,19056,98766,1,,entry citation,,,23686822,,,"1H, 13C, 15N backbone and side chain NMR resonance assignments of the N-terminal NEAr iron transporter domain 1 (NEAT 1) of the hemoglobin receptor IsdB of Staphylococcus aureus.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,8,1,,,,,,,,,,,,,,,,,,,,,,201,205,2014, citations,entry_citation,19057,98785,1,,entry citation,,,25044683,10.1002/psc.2673,,"Micelle bound structure and DNA interaction of brevinin-2-related peptide, an antimicrobial peptide derived from frog skin.",published,journal,J. Pept. Sci.,Journal of peptide science : an official publication of the European Peptide Society,20,10,,1099-1387,,,,,,,,,,,,,,,,,,,,811,821,2014, citations,entry_citation,19058,98800,1,,entry citation,,,23513222,,,Atomic structure and hierarchical assembly of a cross-beta amyloid fibril,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,110,14,,,,,,,,,,,,,,,,,,,,,,5468,5473,2013, citations,ns5a308,19059,98816,1,,entry citation,,,,,,ns5a308,in preparation,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19060,98834,1,,entry citation,,,23513222,,,Atomic structure and hierarchical assembly of a cross-beta amyloid fibril,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,110,14,,,,,,,,,,,,,,,,,,,,,,5468,5473,2013, citations,entry_citation,19061,98850,1,,entry citation,,,22392334,,,"(1)H, (15)N and (13)C assignments of the calcium bound S100P.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,1,,,,,,,,,,,,,,,,,,,,,,5,8,2013, citations,entry_citation,19062,98865,1,,entry citation,,,23513222,,,Atomic structure and hierarchical assembly of a cross- amyloid fibril.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,110,14,,,,,,,,,,,,,,,,,,,,,,5468,5473,2013, citations,entry_citation,19063,98881,1,,entry citation,,,23603827,,,Distinct binding properties of TIAR RRMs and linker region.,published,journal,RNA Biol,RNA biology,10,4,,,,,,,,,,,,,,,,,,,,,,579,589,2013, citations,entry_citation,19064,98897,1,,entry citation,,,23603827,,,Distinct binding properties of TIAR RRMs and linker region.,published,journal,RNA Biol,RNA biology,10,4,,,,,,,,,,,,,,,,,,,,,,579,589,2013, citations,RNaseA_citation,19065,98914,1,,entry citation,,,24619609,,,Assignments of RNase A by ADAPT-NMR and enhancer.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,19066,98930,1,,entry citation,,,24476493,,,Study of the Structural and Dynamic Effects in the FimH Adhesin upon alfa-D-Heptyl Mannose Binding,published,journal,J. Med. Chem.,Journal of medicinal chemistry,57,4,,,,,,,,,,,,,,,,,,,,,,1416,1427,2014, citations,entry_citation,19067,98958,1,,entry citation,,,,,,"The structure of latherin, a surfactant allergen protein from horse sweat and saliva",in preparation,journal,To Be Published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,reference_citation_1,19067,98959,2,,reference citation,,,19478940,,,Latherin: A Surfactant Protein of Horse Sweat and Saliva,published,journal,PLOS ONE,PLOS ONE,4,5,,,,,,,,,,,,,,,,,,,,,,e5726,e5726,2009, citations,reference_citation_1_2,19067,98960,3,,reference citation,,,,,,The Relationship between Structure and Function in Natural Surfactant Proteins,published,thesis,,,,,,,,,,,,,,,,,,,,,,,,,,,,2012, citations,citations,19068,98979,1,,entry citation,,,,,,"Solution NMR Structure CTD domain of NFU1 Iron-Sulfur Cluster Scaffold Homolog from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR2876C",in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19069,99013,1,,entry citation,,,,,,NMR signature of HBDI chromophore in folded EFGP,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,19070,99031,1,,entry citation,,,24327962,,,Peptide lipidation stabilizes structure to enhance biological function.,published,journal,Mol Metab,Molecular metabolism,2,4,,,,,,,,,,,,,,,,,,,,,,468,479,2013, citations,citations,19071,99052,1,,entry citation,,,24327962,,,Peptide lipidation stabilizes structure to enhance biological function.,published,journal,Mol Metab,Molecular metabolism,2,4,,,,,,,,,,,,,,,,,,,,,,468,479,2013, citations,Backbone_1H_13C_and_15N_Chemical_Shift_Assignment_for_HIV-1_protease_Variants,19072,99073,1,,entry citation,,,22752791,,,"Backbone H, C, and N chemical shift assignment for HIV-1 protease subtypes and multi-drug resistant variant MDR 769.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,2,,,,,,,,,,,,,,,,,,,,,,199,202,2013, citations,entry_citation,19074,99090,1,,entry citation,,,23579637,,,NMR structure note: PHD domain from death inducer obliterator protein and its interaction with H3K4me3.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,56,2,,,,,,,,,,,,,,,,,,,,,,183,190,2013, citations,citation1,19075,99107,1,,entry citation,,,23832496,,,Paramagnetic properties of the low- and high-spin states of yeast cytochrome c peroxidase.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,57,1,,,,,,,,,,,,,,,,,,,,,,21,26,2013, citations,citation1,19076,99123,1,,entry citation,,,23832496,,,Paramagnetic properties of the low- and high-spin states of yeast cytochrome c peroxidase.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,57,1,,,,,,,,,,,,,,,,,,,,,,21,26,2013, citations,entry_citation,19077,99139,1,,entry citation,,,23754699,,,"(1)H, (13)C and (15)N backbone and side-chain resonance assignments of the N-terminal ubiquitin-binding domains of the human deubiquitinase Usp28.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,19078,99155,1,,entry citation,,,23649688,,,"(1)H, (13)C and (15)N resonance assignments for the fibrillin-1 EGF2-EGF3-hybrid1-cbEGF1 four-domain fragment.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,8,1,,,,,,,,,,,,,,,,,,,,,,189,194,2014, citations,entry_citation,19079,99171,1,,entry citation,,,24937088,,,"Solution Structure of the 2A Protease from a Common Cold Agent, Human Rhinovirus C2, Strain W12.",published,journal,PLoS ONE,PloS one,9,6,,,,,,,,,,,,,,,,,,,,,,e97198,e97198,2014, citations,entry_citation,19080,99192,1,,entry citation,,,23511634,,,NMR Analysis of a Novel Enzymatically Active Unlinked Dengue NS2B-NS3 Protease Complex.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,18,,,,,,,,,,,,,,,,,,,,,,12891,12900,2013, citations,entry_citation,19081,99212,1,,entry citation,,,24652468,,,Solution structure and metal ion binding sites of the human CPEB3 ribozyme's P4 domain.,published,journal,J. Biol. Inorg. Chem.,Journal of biological inorganic chemistry,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,19082,99230,1,,entry citation,,,23653343,,,Backbone and ILV methyl resonance assignments of E. coli thymidylate synthase bound to cofactor and a nucleotide analogue.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,8,1,,,,,,,,,,,,,,,,,,,,,,195,199,2014, citations,entry_citation,19083,99252,1,,entry citation,,,23614497,,,Identification and Characterization of a New Chemotype of Noncovalent SENP Inhibitors.,published,journal,ACS Chem. Biol.,ACS chemical biology,8,7,,,,,,,,,,,,,,,,,,,,,,1435,1441,2013, citations,mengoL,19084,99266,1,,entry citation,,,,,,"Solution Structures of Mengovirus Leader Protein, its Phosphorylated Derivatives, and in Complex with Nuclear Transport Protein, RanGTPase",in press,journal,"Proc. Nat. Acad. 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NMR Assignments,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19099,99484,1,,entry citation,,,24006098,,,NMR spectroscopy reveals unexpected structural variation at the protein-protein interface in MHC class I molecules.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,57,2,,,,,,,,,,,,,,,,,,,,,,167,178,2013, citations,entry_citation,191,99499,1,,entry citation,,,,,"Fairbrother, Wayne J., Bowen, Derrick, Hall, Len, Williams, Robert J. P., ""One- and two-dimensional NMR studies of yeast phosphoglycerate kinase,"" Eur. J. Biochem. 184, 617-625 (1989).",One- and two-dimensional NMR studies of yeast phosphoglycerate kinase,published,journal,Eur. J. 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Biomol. NMR,Journal of biomolecular NMR,58,3,,,,,,,,,,,,,,,,,,,,,,227,230,2014, citations,citation_1,19107,99611,1,,entry citation,,,,,,Principles of efficient IgE cross-linking by allergens derived by the Structure of the Major Grass Pollen Allergen Phl p 5a,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19108,99628,1,,entry citation,,,23695684,,,NMR structure of human restriction factor APOBEC3A reveals substrate binding and enzyme specificity.,published,journal,Nat. Commun.,Nature communications,4,1890,,,,,,,,,,,,,,,,,,,,,,1890,1890,2013, citations,entry_citation,19109,99655,1,,entry citation,,,23754701,,,Chemical shift assignments of the C-terminal Eps15 homology domain-3 EH domain.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,1911,99672,1,,entry citation,,,,,"Kochoyan, Michel, Keutmann, Henry T., Weiss, Michael A., ""Alternating Zinc Fingers in the Human Male-Associated Protein ZFY: HX3H and HX4H Motifs Encode a Local Structural Switch,"" Biochemistry 30 (39), 9396-9402 (1991).","Alternating Zinc Fingers in the Human Male-Associated Protein ZFY: HX3H and HX4H Motifs Encode a Local Structural Switch",published,journal,Biochemistry,,30,39,,,,,,,,,,,,,,,,,,,,,,9396,9402,1991, citations,entry_citation,19110,99685,1,,entry citation,,,23832674,,,NMR assignments of PI3-SH3 domain aided by protonless NMR spectroscopy.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,19111,99698,1,,entry citation,,,23754700,,,"(1)H, (13)C and (15)N backbone and side-chain resonance assignments of the N-terminal ubiquitin-binding domains of USP25.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,19112,99715,1,,entry citation,,,23624647,,,Structural characterization by NMR of a double phosphorylated chimeric Peptide vaccine for treatment of Alzheimer's disease,published,journal,Molecules,,18,5,,,,,,,,,,,,,,,,,,,,,,4929,4941,2013, citations,entry_citation,19113,99733,1,,entry citation,,,24006098,,,NMR spectroscopy reveals unexpected structural variation at the protein-protein interface in MHC class I molecules.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,57,2,,,,,,,,,,,,,,,,,,,,,,167,178,2013, citations,entry_citation,19114,99752,1,,entry citation,,,24207126,,,Interaction of the eukaryotic initiation factor 4E with 4E-BP2 at a dynamic bipartite interface.,published,journal,Structure,"Structure (London, England : 1993)",21,12,,,,,,,,,,,,,,,,,,,,,,2186,2196,2013, citations,reference_citation,19114,99753,2,,reference citation,,,25533957,,,Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch,published,journal,Nature,,519,,,,,,,,,,,,,,,,,,,,,,,106,109,2015, citations,entry_citation,19115,99767,1,,entry citation,,,23763519,,,The Structure of the Mercury Transporter MerF in Phospholipid Bilayers: A Large Conformational Rearrangement Results from N-Terminal Truncation,published,journal,J. Am. Chem. 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NMR,Journal of biomolecular NMR,57,2,,,,,,,,,,,,,,,,,,,,,,167,178,2013, citations,entry_citation,19119,99840,1,,entry citation,,,24006098,,,NMR spectroscopy reveals unexpected structural variation at the protein-protein interface in MHC class I molecules.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,57,2,,,,,,,,,,,,,,,,,,,,,,167,178,2013, citations,entry_citation,19120,99858,1,,entry citation,,,24006098,,,NMR spectroscopy reveals unexpected structural variation at the protein-protein interface in MHC class I molecules.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,57,2,,,,,,,,,,,,,,,,,,,,,,167,178,2013, citations,entry_citation,19121,99876,1,,entry citation,,,24006098,,,NMR spectroscopy reveals unexpected structural variation at the protein-protein interface in MHC class I molecules.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,57,2,,,,,,,,,,,,,,,,,,,,,,167,178,2013, citations,entry_citation,19122,99894,1,,entry citation,,,24006098,,,NMR spectroscopy reveals unexpected structural variation at the protein-protein interface in MHC class I molecules.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,57,2,,,,,,,,,,,,,,,,,,,,,,167,178,2013, citations,entry_citation,19123,99912,1,,entry citation,,,24006098,,,NMR spectroscopy reveals unexpected structural variation at the protein-protein interface in MHC class I molecules.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,57,2,,,,,,,,,,,,,,,,,,,,,,167,178,2013, citations,citations,19124,99930,1,,entry citation,,,,,,NMR spatial structure of the antimicrobial peptide Tk-Amp-X2,in preparation,journal,To be Published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19125,99945,1,,entry citation,,,24333487,,,Molecular Insights into the Recognition of N-Terminal Histone Modifications by the BRPF1 Bromodomain.,published,journal,J. Mol. Biol.,Journal of molecular biology,426,8,,,,,,,,,,,,,,,,,,,,,,1661,1676,2014, citations,entry_citation,19126,99959,1,,entry citation,,,23994010,,,Open-Channel Structures of the Human Glycine Receptor 1 Full-Length Transmembrane Domain.,published,journal,Structure,"Structure (London, England : 1993)",21,10,,,,,,,,,,,,,,,,,,,,,,1897,1904,2013, citations,entry_citation,19127,99982,1,,entry citation,,,23801644,,,The dynamics of lysozyme from bacteriophage lambda in solution probed by NMR and MD simulations.,published,journal,Chembiochem,Chembiochem : a European journal of chemical biology,14,14,,,,,,,,,,,,,,,,,,,,,,1780,1788,2013, citations,entry_citation,19128,100003,1,,entry citation,,,24115170,,,Conformational Diversity in Contryphans from Conus Venom: cis-trans Isomerisation and Aromatic/Proline Interactions in the 23-Membered Ring of a 7-Residue Peptide Disulfide Loop,published,journal,Chemistry,,19,45,,,,,,,,,,,,,,,,,,,,,,15175,15189,2013, citations,entry_citation,19129,100017,1,,entry citation,,,24115170,,,Conformational Diversity in Contryphans from Conus Venom: cis-trans Isomerisation and Aromatic/Proline Interactions in the 23-Membered Ring of a 7-Residue Peptide Disulfide Loop,published,journal,Chemistry,,19,45,,,,,,,,,,,,,,,,,,,,,,15175,15189,2013, citations,entry_citation,19130,100031,1,,entry citation,,,24115170,,,Conformational Diversity in Contryphans from Conus Venom: cis-trans Isomerisation and Aromatic/Proline Interactions in the 23-Membered Ring of a 7-Residue Peptide Disulfide Loop,published,journal,Chemistry,,19,45,,,,,,,,,,,,,,,,,,,,,,15175,15189,2013, citations,entry_citation,19131,100045,1,,entry citation,,,24115170,,,Conformational Diversity in Contryphans from Conus Venom: cis-trans Isomerisation and Aromatic/Proline Interactions in the 23-Membered Ring of a 7-Residue Peptide Disulfide Loop,published,journal,Chemistry,,19,45,,,,,,,,,,,,,,,,,,,,,,15175,15189,2013, citations,entry_citation,19132,100059,1,,entry citation,,,24115170,,,Conformational Diversity in Contryphans from Conus Venom: cis-trans Isomerisation and Aromatic/Proline Interactions in the 23-Membered Ring of a 7-Residue Peptide Disulfide Loop,published,journal,Chemistry,,19,45,,,,,,,,,,,,,,,,,,,,,,15175,15189,2013, citations,entry_citation,19133,100073,1,,entry citation,,,24115170,,,Conformational Diversity in Contryphans from Conus Venom: cis-trans Isomerisation and Aromatic/Proline Interactions in the 23-Membered Ring of a 7-Residue Peptide Disulfide Loop,published,journal,Chemistry,,19,45,,,,,,,,,,,,,,,,,,,,,,15175,15189,2013, citations,entry_citation,19134,100087,1,,entry citation,,,23821130,10.1007/s12104-013-9501-7,,Backbone NMR assignments of a topologically knotted protein in urea-denatured state.,published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,8,2,,1874-270X,,,,,,,,,,,,,,,,,,,,283,285,2014, citations,entry_citation_2,19134,100088,2,,reference citation,,,,,,Experimental detection of knotted conformations in denatured proteins.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,107,18,,,,,,,,,,,,,,,,,,,,,,8189,8194,2010, citations,entry_citation,19135,100102,1,,entry citation,,,23877929,,,"Efficient protocol for backbone and side-chain assignments of large, intrinsically disordered proteins: transient secondary structure analysis of 49.2 kDa microtubule associated protein 2c.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,56,4,,,,,,,,,,,,,,,,,,,,,,291,301,2013, citations,citation_1,19136,100116,1,,entry citation,,,23898196,,,Structural and dynamic studies of the transcription factor ERG reveal DNA binding is allosterically autoinhibited.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,110,33,,,,,,,,,,,,,,,,,,,,,,13374,13379,2013, citations,entry_citation,19137,100131,1,,entry citation,,,23898196,,,Structural and dynamic studies of the transcription factor ERG reveal DNA binding is allosterically autoinhibited.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,110,33,,,,,,,,,,,,,,,,,,,,,,13374,13379,2013, citations,entry_citation,19138,100146,1,,entry citation,,,23898196,,,Structural and dynamic studies of the transcription factor ERG reveal DNA binding is allosterically autoinhibited.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,110,33,,,,,,,,,,,,,,,,,,,,,,13374,13379,2013, citations,entry_citation,19139,100163,1,,entry citation,,,27410476,10.7554/eLife.18124,,Talin-KANK1 interaction controls the recruitment of cortical microtubule stabilizing complexes to focal adhesions,published,journal,Elife,eLife,5,,,2050-084X,,,,,,,,,,,,,,,,,,,,e18124,e18124,2016, citations,entry_citation,19140,100177,1,,entry citation,,,23705820,,,Membrane interaction of disease-related dynorphin a variants.,published,journal,Biochemistry,Biochemistry,52,24,,,,,,,,,,,,,,,,,,,,,,4157,4167,2013, citations,entry_citation,19141,100194,1,,entry citation,,,23705820,,,Membrane interaction of disease-related dynorphin a variants.,published,journal,Biochemistry,Biochemistry,52,24,,,,,,,,,,,,,,,,,,,,,,4157,4167,2013, citations,entry_citation,19142,100211,1,,entry citation,,,,,,Structure of a novel vertebrate toxin from the badge huntsman spider,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19143,100228,1,,entry citation,,,,,,"The structure, binding properties, and dynamics of the 34 kDa bacterial siderophore binding protein FepB in solution.",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19144,100244,1,,entry citation,,,23644478,,,Allosteric inhibition through suppression of transient conformational states.,published,journal,Nat. Chem. Biol.,Nature chemical biology,9,7,,,,,,,,,,,,,,,,,,,,,,462,465,2013, citations,entry_citation,19145,100263,1,,entry citation,,,23644478,,,Allosteric inhibition through suppression of transient conformational states.,published,journal,Nat. Chem. Biol.,Nature chemical biology,9,7,,,,,,,,,,,,,,,,,,,,,,462,465,2013, citations,citation1,19146,100285,1,,entry citation,,,,,,Solution structure of RING domain of E3 ubiquitin ligase Doa10,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19147,100303,1,,entry citation,,,,,,EM Structure of APC/C_CDH1-EMI1: multimodal mechanism of E3 ligase shutdown,submitted,journal,Nat. Struct. Biol.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19148,100320,1,,entry citation,,,23605043,,,The actinobacterial transcription factor RbpA binds to the principal sigma subunit of RNA polymerase,published,journal,Nucleic Acids Res.,,41,11,,,,,,,,,,,,,,,,,,,,,,5679,5691,2013, citations,entry_citation,19149,100336,1,,entry citation,,,23605043,,,The actinobacterial transcription factor RbpA binds to the principal sigma subunit of RNA polymerase,published,journal,Nucleic Acids Res.,,41,11,,,,,,,,,,,,,,,,,,,,,,5679,5691,2013, citations,entry_citation,19150,100352,1,,entry citation,,,23749453,,,"(1)H, (15)N, and (13)C chemical shift assignments of cyanobacteriochrome NpF2164g3 in the photoproduct state.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,apo_YqcA,19151,100370,1,,entry citation,,,23749454,,,"(1)H, (13)C and (15)N resonance assignments of the apo and holo states of flavodoxin YqcA from Escherichia coli.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,citations_1,19152,100387,1,,entry citation,,,23749454,,,"(1)H, (13)C and (15)N resonance assignments of the apo and holo states of flavodoxin YqcA from Escherichia coli.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,19153,100406,1,,entry citation,,,,,,Directed evolution of structurally selected IGF2R domain 11 binding loop residues generates an IGF2 super-antagonist,in preparation,journal,EMBO J.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19154,100437,1,,entry citation,,,23662937,,,"Sungsanpin, a lasso Peptide from a deep-sea streptomycete.",published,journal,J. Nat. Prod.,Journal of natural products,76,5,,,,,,,,,,,,,,,,,,,,,,873,879,2013, citations,entry_citation,19155,100452,1,,entry citation,,,,,,Host Specification of Factor H Binding by Streptococcus pneumoniae,submitted,journal,Nature,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,19156,100467,1,,entry citation,,,23765287,,,"(1)H, (13)C, and (15)N NMR assignments of a Drosophila Hedgehog autoprocessing domain.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,19157,100490,1,,entry citation,,,23513222,,,ATOMIC STRUCTURE AND HIERARCHICAL ASSEMBLY OF A CROSS-BETA AMYLOID FIBRIL.,published,journal,Proc. Natl. Acad. Sci. U. S. A.,,110,14,,,,,,,,,,,,,,,,,,,,,,5468,5473,2013, citations,entry_citation,19158,100506,1,,entry citation,,,23791747,,,DNA quadruplex folding formalism--a tutorial on quadruplex topologies.,published,journal,Methods,"Methods (San Diego, Calif.)",64,1,,,,,,,,,,,,,,,,,,,,,,28,35,2013, citations,entry_citation,19159,100529,1,,entry citation,,,23791747,,,DNA quadruplex folding formalism--a tutorial on quadruplex topologies.,published,journal,Methods,"Methods (San Diego, Calif.)",64,1,,,,,,,,,,,,,,,,,,,,,,28,35,2013, citations,entry_citation,19160,100552,1,,entry citation,,,,,,Ligand binding promiscuity of human liver fatty acid binding protein: structural and dynamic insights from an interaction study with glycocholate and oleate,submitted,journal,ChemBioChem,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19161,100572,1,,entry citation,,,24114119,,,Structural adaptation of tooth enamel protein amelogenin in the presence of SDS micelles.,published,journal,Biopolymers,Biopolymers,101,5,,,,,,,,,,,,,,,,,,,,,,525,535,2014, citations,entry_citation,19162,100587,1,,entry citation,,,23739335,,,Unusual architecture of the p7 channel from hepatitis C virus.,published,journal,Nature,Nature,498,7455,,,,,,,,,,,,,,,,,,,,,,521,525,2013, citations,entry_citation,19163,100609,1,,entry citation,,,24512202,,,Structure and function of human DnaJ homologue subfamily a member 1 (DNAJA1) and its relationship to pancreatic cancer.,published,journal,Biochemistry,Biochemistry,53,8,,,,,,,,,,,,,,,,,,,,,,1360,1372,2014, citations,entry_citation,19164,100628,1,,entry citation,,,22528768,,,"(1)H-, (13)C- and (15)N-NMR assignment of the N-terminal domain of human cerebral dopamine neurotrophic factor (CDNF).",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,7,1,,,,,,,,,,,,,,,,,,,,,,101,103,2013, citations,entry_citation,19165,100651,1,,entry citation,,,24375557,,,NMR-monitored titration of acid-stress bacterial chaperone HdeA reveals that Asp and Glu charge neutralization produces a loosened dimer structure in preparation for protein unfolding and chaperone activation.,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,23,2,,,,,,,,,,,,,,,,,,,,,,167,178,2014, citations,citations,19167,100668,1,,entry citation,,,,,,Structural determination of the Citrus sinensis Poly(A)-Binding Protein CsPABP1,in preparation,journal,To be Published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,19168,100688,1,,entry citation,,,,,,"Solution structure of the a C-terminal domain of translation initiation factor IF-3 from Campylobacter jejuni",in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,19169,100714,1,,entry citation,,,,,,Solution structure of uncharacterized thioredoxin-like protein PG_2175 from Porphyromonas gingivalis,in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19192,101162,1,,entry citation,,,23932450,,,Structural studies of -hairpin peptidomimetic antibiotics that target LptD in Pseudomonas sp.,published,journal,Bioorg. Med. Chem.,Bioorganic & medicinal chemistry,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,19193,101181,1,,entry citation,,,23782698,,,Functional manipulation of a calcium binding protein from E. histolytica guided by paramagnetic NMR,published,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1917,100741,1,,entry citation,,,,,"Clore, G. Marius, Gronenborn, Angela M., Nilges, Michael, Ryan, Clarence A., ""Three-Dimensional Structure of Potato Carboxypeptidase Inhibitor in Solution. A Study Using Nuclear Magnetic Resonance, Distance Geometry, and Restrained Molecular Dynamics,"" Biochemistry 26 (24), 8012-8023 (1987).","Three-Dimensional Structure of Potato Carboxypeptidase Inhibitor in Solution. A Study Using Nuclear Magnetic Resonance, Distance Geometry, and Restrained Molecular Dynamics",published,journal,Biochemistry,,26,24,,,,,,,,,,,,,,,,,,,,,,8012,8023,1987, citations,entry_citation,19170,100755,1,,entry citation,,,,,,Structural characterization of the interaction between a plant calmodulin and three distinct calcium-ATPase pumps,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19171,100769,1,,entry citation,,,24810720,10.1038/srep04896,,Transcriptional repressor domain of MBD1 is intrinsically disordered and interacts with its binding partners in a selective manner.,published,journal,Sci. Rep.,Scientific reports,4,,,2045-2322,,,,,,,,,,,,,,,,,,,,4896,4896,2014, citations,entry_citation,19172,100785,1,,entry citation,,,23838815,,,"(1)H, (13)C, and (15)N backbone and side-chain chemical shift assignments of the free and bound forms of the human PTPN11 second SH2 domain.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,19173,100801,1,,entry citation,,,23838815,,,"(1)H, (13)C, and (15)N backbone and side-chain chemical shift assignments of the free and bound forms of the human PTPN11 second SH2 domain.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,19174,100818,1,,entry citation,,,24037959,,,Structural characterization of the regulatory domain of brain carnitine palmitoyltransferase 1.,published,journal,Biopolymers,Biopolymers,101,4,,,,,,,,,,,,,,,,,,,,,,398,405,2014, citations,RGD_peptides,19175,100832,1,,entry citation,,,24382674,,,"The Cyclic Cystine Ladder of Theta-Defensins as a Stable, Bifunctional Scaffold: A Proof-of-Concept Study Using the Integrin-Binding RGD Motif",published,journal,ChemBioChem,,15,3,,,,,,,,,,,,,,,,,,,,,,451,459,2014, citations,RGD_peptides,19176,100851,1,,entry citation,,,24382674,,,"The Cyclic Cystine Ladder of Theta-Defensins as a Stable, Bifunctional Scaffold: A Proof-of-Concept Study Using the Integrin-Binding RGD Motif",published,journal,ChemBioChem,,15,3,,,,,,,,,,,,,,,,,,,,,,451,459,2014, citations,RGD_peptides,19177,100870,1,,entry citation,,,24382674,,,"The Cyclic Cystine Ladder of Theta-Defensins as a Stable, Bifunctional Scaffold: A Proof-of-Concept Study Using the Integrin-Binding RGD Motif",published,journal,ChemBioChem,,15,3,,,,,,,,,,,,,,,,,,,,,,451,459,2014, citations,entry_citation,19178,100889,1,,entry citation,,,23672713,,,The Solution Structures of Two Prophage Homologues of the Bacteriophage Ea8.5 Protein Reveal a Newly Discovered Hybrid Homeodomain/Zinc-Finger Fold.,published,journal,Biochemistry,Biochemistry,52,21,,,,,,,,,,,,,,,,,,,,,,3612,3614,2013, citations,entry_citation,19179,100908,1,,entry citation,,,23672713,,,The Solution Structures of Two Prophage Homologues of the Bacteriophage Ea8.5 Protein Reveal a Newly Discovered Hybrid Homeodomain/Zinc-Finger Fold.,published,journal,Biochemistry,Biochemistry,52,21,,,,,,,,,,,,,,,,,,,,,,3612,3614,2013, citations,entry_citation,1918,100927,1,,entry citation,,,,,"Clore, G. Marius, Gronenborn, Angela M., Nilges, Michael, Ryan, Clarence A., ""Three-Dimensional Structure of Potato Carboxypeptidase Inhibitor in Solution. A Study Using Nuclear Magnetic Resonance, Distance Geometry, and Restrained Molecular Dynamics,"" Biochemistry 26 (24), 8012-8023 (1987).","Three-Dimensional Structure of Potato Carboxypeptidase Inhibitor in Solution. A Study Using Nuclear Magnetic Resonance, Distance Geometry, and Restrained Molecular Dynamics",published,journal,Biochemistry,,26,24,,,,,,,,,,,,,,,,,,,,,,8012,8023,1987, citations,entry_citation,19180,100940,1,,entry citation,,,24376912,,,Circular Permutation of the Trp-cage: Fold Rescue upon Addition of a Hydrophobic Staple.,published,journal,RSC Adv.,RSC advances,2013,43,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,19181,100956,1,,entry citation,,,24100136,,,"NMR localization of the O-mycoloylation on PorH, a channel forming peptide from Corynebacterium glutamicum.",published,journal,FEBS Lett.,FEBS letters,587,22,,,,,,,,,,,,,,,,,,,,,,3687,3691,2013, citations,citation_1,19182,100970,1,,entry citation,,,23943084,,,Resonance assignment for a particularly challenging protein based on systematic unlabeling of amino acids to complement incomplete NMR data sets,published,journal,J. Biomol. NMR,,57,1,,,,,,,,,,,,,,,,,,,,,,65,72,2013, citations,entry_citation,19183,100988,1,,entry citation,,,24376912,,,Circular Permutation of the Trp-cage: Fold Rescue upon Addition of a Hydrophobic Staple.,published,journal,RSC Adv.,RSC advances,2013,43,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,19184,101005,1,,entry citation,,,,,,Structural characterization of the interactions between calmodulin and three distinct plant calcium-ATPase pumps,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19185,101019,1,,entry citation,,,,,,Structure of the Type IVa Major Pilin from the Electrically Conductive Bacterial Nanowires of Geobacter sulfurreducens,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19186,101039,1,,entry citation,,,23861868,,,The Effects of Threonine Phosphorylation on the Stability and Dynamics of the Central Molecular Switch Region of 18.5-kDa Myelin Basic Protein.,published,journal,PLoS ONE,PloS one,8,7,,,,,,,,,,,,,,,,,,,,,,e68175,e68175,2013, citations,entry_citation,19187,101056,1,,entry citation,,,23934138,,,"(1)H, (15)N and (13)C chemical shift assignments for the winged helix domains of two archeal MCM C-termini.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,19188,101074,1,,entry citation,,,,,,Ligand binding promiscuity of human liver fatty acid binding protein: structural and dynamic insights from an interaction study with glycocholate and oleate,submitted,journal,ChemBioChem,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19189,101094,1,,entry citation,,,,,,Ligand binding promiscuity of human liver fatty acid binding protein: structural and dynamic insights from an interaction study with glycocholate and oleate,submitted,journal,ChemBioChem,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,1919,101112,1,,entry citation,,,,,"Dekker, N., Peters, Anton R., Slotboom, A.J., Boelens, Rolf, Kaptein, Robert, Dijkman, Ruud, de Haas, Gerard, ""Two-dimensional 1H-NMR studies of phospholipase-A2-inhibitor complexes bound to a micellar lipid-water interface,"" Eur. J. 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Ed.,,52,33,,,,,,,,,,,,,,,,,,,,,,8746,8751,2013, citations,entry_citation,19195,101219,1,,entry citation,,,,,,alfa-actinin from parasite Entamoeba histolytica,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19196,101237,1,,entry citation,,,23782698,,,Functional manipulation of a calcium-binding protein from Entamoeba histolytica guided by paramagnetic NMR.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,32,,,,,,,,,,,,,,,,,,,,,,23473,23487,2013, citations,entry_citation,19197,101257,1,,entry citation,,,23782698,,,Functional manipulation of a calcium-binding protein from Entamoeba histolytica guided by paramagnetic NMR.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,32,,,,,,,,,,,,,,,,,,,,,,23473,23487,2013, citations,entry_citation,19198,101278,1,,entry citation,,,,,,NMR Structure of the protein NP_346341.1 from Streptococcus pneumoniae,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,192,101298,1,,entry citation,,,,,"Kraulis, Per J., Clore, G. Marius, Nilges, Michael, Jones, Alwyn, Petterson, Goran, Knowles, Jonathan, Gronenborn, Angela M., ""Determination of the Three-Dimensional Solution Structure of the C-Terminal Domain of CellobiohydrolOCe I from Trichodermi reesi. A Study using NMR and Hybrid distance Geometry-Dynamical Simulated Annealing.,"" Biochemistry 28, 7241-7257 (1989).","Determination of the Three-Dimensional Solution Structure of the C-Terminal Domain of CellobiohydrolOCe I from Trichodermi reesi. A Study using NMR and Hybrid distance Geometry-Dynamical Simulated Annealing.",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,7241,7257,1989, citations,entry_citation,1920,101311,1,,entry citation,,,,,"Dekker, N., Peters, Anton R., Slotboom, A.J., Boelens, Rolf, Kaptein, Robert, Dijkman, Ruud, de Haas, Gerard, ""Two-dimensional 1H-NMR studies of phospholipase-A2-inhibitor complexes bound to a micellar lipid-water interface,"" Eur. J. Biochem. 199 (3), 601-607 (1991).","Two-dimensional 1H-NMR studies of phospholipase-A2-inhibitor complexes bound to a micellar lipid-water interface",published,journal,Eur. J. Biochem.,,199,3,,,,,,,,,,,,,,,,,,,,,,601,607,1991, citations,entry_citation,19200,101324,1,,entry citation,,,23926099,,,The Relaxin Receptor (RXFP1) Utilizes Hydrophobic Moieties on a Signaling Surface of Its N-terminal Low Density Lipoprotein Class A Module to Mediate Receptor Activation.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,39,,,,,,,,,,,,,,,,,,,,,,28138,28151,2013, citations,entry_citation,19201,101344,1,,entry citation,,,24239949,,,The Structure of TAX1BP1 UBZ1+2 Provides Insight into Target Specificity and Adaptability.,published,journal,J. Mol. Biol.,Journal of molecular biology,426,3,,,,,,,,,,,,,,,,,,,,,,674,690,2014, citations,citations,19202,101364,1,,entry citation,,,24508768,,,From molecular phylogeny towards differentiating pharmacology for NMDA receptor subtypes.,published,journal,Toxicon,Toxicon : official journal of the International Society on Toxinology,81,,,,,,,,,,,,,,,,,,,,,,,67,79,2014, citations,entry_citation,19203,101381,1,,entry citation,,,,,,"NMR structure of RNA recognition motif 2 (RRM2) of Homo sapiens splicing factor, arginine/serine-rich 1",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,19204,101400,1,,entry citation,,,23996527,,,"(1)H, (15)N, and (13)C resonance assignments and secondary structure of the SWIRM domain of human BAF155, a chromatin remodeling complex component.",published,journal,Mol. Cells,Molecules and cells,36,4,,,,,,,,,,,,,,,,,,,,,,333,339,2013, citations,entry_citation,19205,101415,1,,entry citation,,,24318984,,,"Challenging the state of the art in protein structure prediction: Highlights of experimental target structures for the 10th Critical Assessment of Techniques for Protein Structure Prediction Experiment CASP10",published,journal,Proteins,,82,2,,,,,,,,,,,,,,,,,,,,,,26,42,2014, citations,entry_citation,19206,101431,1,,entry citation,,,23835623,,,"(1)H, (13)C and (15)N backbone and side-chain resonance assignments of a family 36 carbohydrate binding module of xylanase from Paenibacillus campinasensis.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,19207,101451,1,,entry citation,,,,,,"design, synthesis, functional and structural characterization of an inhibitor of N-acetylneuraminate-9-phosphate phosphatase: observation of extensive dynamics in an enzyme/inhibitor complex",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,Citation_1,19208,101465,1,,entry citation,,,23893440,,,Backbone resonance assignments of the 42kDa enzyme arginine kinase in the transition state analogue form.,published,journal,Biomol. 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Biochem.,,199,3,,,,,,,,,,,,,,,,,,,,,,601,607,1991, citations,entry_citation,19210,101518,1,,entry citation,,,,,,The C-terminal Region of Disintegrin Modulate its 3D Conformation and Cooperate with RGD Loop in Regulating Recognitions of Integrins,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19211,101538,1,,entry citation,,,,,,The C-terminal Region of Disintegrin Modulate its 3D Conformation and Cooperate with RGD Loop in Regulating Recognitions of Integrins,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19212,101558,1,,entry citation,,,,,,The C-terminal Region of Disintegrin Modulate its 3D Conformation and Cooperate with RGD Loop in Regulating Recognitions of Integrins,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19213,101578,1,,entry citation,,,24337572,,,Dynamic Structural Changes Underpin Photoconversion of a Blue/Green Cyanobacteriochrome between Its Dark and Photoactivated States.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,289,5,,,,,,,,,,,,,,,,,,,,,,3055,3065,2014, citations,entry_citation,19214,101599,1,,entry citation,,,24337572,,,Dynamic Structural Changes Underpin Photoconversion of a Blue/Green Cyanobacteriochrome between Its Dark and Photoactivated States.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,289,5,,,,,,,,,,,,,,,,,,,,,,3055,3065,2014, citations,entry_citation,19215,101620,1,,entry citation,,,24474763,,,"Structure of an HIV-1-neutralizing antibody target, the lipid-bound gp41 envelope membrane proximal region trimer.",published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,111,4,,,,,,,,,,,,,,,,,,,,,,1391,1396,2014, citations,entry_citation,19216,101637,1,,entry citation,,,23836910,,,Structural and Functional Analysis of Transmembrane Segment IV of the Salt Tolerance Protein Sod2.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,34,,,,,,,,,,,,,,,,,,,,,,24609,24624,2013, citations,entry_citation,19217,101654,1,,entry citation,,,24429291,,,"Solution Structure, Membrane Interactions, and Protein Binding Partners of the Tetraspanin Sm-TSP-2, a Vaccine Antigen from the Human Blood Fluke Schistosoma mansoni.",published,journal,J. Biol. Chem.,The Journal of biological chemistry,289,10,,,,,,,,,,,,,,,,,,,,,,7151,7163,2014, citations,entry_citation,19218,101668,1,,entry citation,,,24611845,,,Structure-guided activity enhancement and catalytic mechanism of yeast grx8.,published,journal,Biochemistry,Biochemistry,53,13,,,,,,,,,,,,,,,,,,,,,,2185,2196,2014, citations,entry_citation,19219,101687,1,,entry citation,,,25631053,,,Solution Structure of Yeast Rpn9: Insights for Proteasome Lid Assembly,published,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,2015, citations,entry_citation,19220,101704,1,,entry citation,,,25631053,,,Solution Structure of Yeast Rpn9: Insights for Proteasome Lid Assembly,published,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,2015, citations,entry_citation,19221,101720,1,,entry citation,,,25631053,,,Solution Structure of Yeast Rpn9: Insights for Proteasome Lid Assembly,published,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,2015, citations,entry_citation,19222,101736,1,,entry citation,,,25102280,,,NMR Studies of DNA Support the Role of Pre-Existing Minor Groove Variations in Nucleosome Indirect Readout,published,journal,Biochemistry,Biochemistry,53,35,,0006-2960,,,,,,,,,,,,,,,,,,,,5601,5612,2014, citations,entry_citation,19223,101766,1,,entry citation,,,24845231,10.1038/nchembio.1528,,Targeting the disordered C terminus of PTP1B with an allosteric inhibitor.,published,journal,Nat. Chem. Biol.,Nature chemical biology,10,7,,1552-4469,,,,,,,,,,,,,,,,,,,,558,566,2014, citations,entry_citation,19224,101787,1,,entry citation,,,24845231,10.1038/nchembio.1528,,Targeting the disordered C terminus of PTP1B with an allosteric inhibitor.,published,journal,Nat. Chem. Biol.,Nature chemical biology,10,7,,1552-4469,,,,,,,,,,,,,,,,,,,,558,566,2014, citations,entry_citation,19225,101806,1,,entry citation,,,,,,Molecular basis for Protein Phosphatase-1 regulation by the muscle glycogen-targeting subunit GM,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19226,101826,1,,entry citation,,,24115468,,,Backbone FC(e)H...O Hydrogen Bonds in 2'F-Substituted Nucleic Acids.,published,journal,Angew. Chem. Int. Ed. Engl.,Angewandte Chemie (International ed. in English),,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,19227,101854,1,,entry citation,,,23796517,,,Thermodynamic and Structural Determinants of Differential Pdx1 Binding to Elements from the Insulin and IAPP Promoters.,published,journal,J. Mol. Biol.,Journal of molecular biology,425,18,,,,,,,,,,,,,,,,,,,,,,3360,3377,2013, citations,entry_citation,19228,101871,1,,entry citation,,,23796517,,,Thermodynamic and Structural Determinants of Differential Pdx1 Binding to Elements from the Insulin and IAPP Promoters.,published,journal,J. Mol. Biol.,Journal of molecular biology,425,18,,,,,,,,,,,,,,,,,,,,,,3360,3377,2013, citations,entry_citation,19229,101888,1,,entry citation,,,23907177,,,PHD domain from human SHPRH.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,56,4,,,,,,,,,,,,,,,,,,,,,,393,399,2013, citations,citation_1,19230,101911,1,,entry citation,,,23848581,,,In Vivo Activation of the p53 Tumor Suppressor Pathway by an Engineered Cyclotide.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,135,31,,,,,,,,,,,,,,,,,,,,,,11623,11633,2013, citations,citation_1,19231,101929,1,,entry citation,,,24371275,,,Solution structure and tandem DNA recognition of the C-terminal effector domain of PmrA from Klebsiella pneumoniae.,published,journal,Nucleic Acids Res.,Nucleic acids research,42,6,,,,,,,,,,,,,,,,,,,,,,4080,4093,2014, citations,citation_1,19232,101949,1,,entry citation,,,,,,Structure and semi-sequence-specific RNA binding of Nrd1,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19233,101976,1,,entry citation,,,24403012,,,"The structure of Plasmodium yoelii merozoite surface protein 119, antibody specificity and implications for malaria vaccine design",published,journal,Open Biol.,,4,1,,,,,,,,,,,,,,,,,,,,,,130091,130091,2014, citations,entry_citation,19234,101996,1,,entry citation,,,24403012,,,"The structure of Plasmodium yoelii merozoite surface protein 119, antibody specificity and implications for malaria vaccine design",published,journal,Open Biol.,,4,1,,,,,,,,,,,,,,,,,,,,,,130091,130091,2014, citations,entry_citation,19235,102016,1,,entry citation,,,,,,Discriminating the Symmetric Dimer Interface of the 33kDa Aha1 Domain by combining NMR and SAXS data in a hybrid method,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19236,102040,1,,entry citation,,,,,,Dynamics in the complex of plastocyanin and tetralysine peptides,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,Citation_1,19237,102057,1,,entry citation,,,,,,Folding and structural studies of the protein AhPDF1,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19238,102076,1,,entry citation,,,24705785,,,Capping of the N-terminus of PSD-95 by calmodulin triggers its postsynaptic release,published,journal,Embo J.,,33,12,,,,,,,,,,,,,,,,,,,,,,1341,1353,2014, citations,entry_citation,19239,102091,1,,entry citation,,,,,,Assigned Chemical Shifts for the mini 2C TCR,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19240,102108,1,,entry citation,,,23688288,,,Analyzing the visible conformational substates of the FK506-binding protein FKBP12.,published,journal,Biochem. J.,The Biochemical journal,453,3,,,,,,,,,,,,,,,,,,,,,,371,380,2013, citations,entry_citation,19241,102126,1,,entry citation,,,23688288,,,Analyzing the visible conformational substates of the FK506-binding protein FKBP12.,published,journal,Biochem. J.,The Biochemical journal,453,3,,,,,,,,,,,,,,,,,,,,,,371,380,2013, citations,entry_citation,19242,102144,1,,entry citation,,,24036119,,,Role of the Two Structural Domains from the Periplasmic Escherichia coli Histidine-binding Protein HisJ.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,44,,,,,,,,,,,,,,,,,,,,,,31409,31422,2013, citations,entry_citation,19243,102163,1,,entry citation,,,24036119,,,Role of the Two Structural Domains from the Periplasmic Escherichia coli Histidine-binding Protein HisJ.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,44,,,,,,,,,,,,,,,,,,,,,,31409,31422,2013, citations,entry_citation,19244,102180,1,,entry citation,,,24036119,,,Role of the Two Structural Domains from the Periplasmic Escherichia coli Histidine-binding Protein HisJ.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,44,,,,,,,,,,,,,,,,,,,,,,31409,31422,2013, citations,entry_citation,19245,102197,1,,entry citation,,,24036119,,,Role of the Two Structural Domains from the Periplasmic Escherichia coli Histidine-binding Protein HisJ.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,44,,,,,,,,,,,,,,,,,,,,,,31409,31422,2013, citations,entry_citation,19246,102216,1,,entry citation,,,26748655,,,"1H, 15N, 13C resonance assignment of human GAP-43",published,journal,Biomol. NMR Assign.,,10,1,,,,,,,,,,,,,,,,,,,,,,171,174,2016, citations,entry_citation,19248,102248,1,,entry citation,,,23836656,,,Isolated pseudo-RNA-recognition motifs of SR proteins can regulate splicing using a noncanonical mode of RNA recognition.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,110,30,,,,,,,,,,,,,,,,,,,,,,E2802,E2811,2013, citations,entry_citation,19249,102265,1,,entry citation,,,24243759,,,NMR structural analysis of Sleeping Beauty transposase binding to DNA.,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,23,1,,,,,,,,,,,,,,,,,,,,,,23,33,2014, citations,entry_citation,19250,102281,1,,entry citation,,,23862624,,,Discovery and characterization of an isopeptidase that linearizes lasso peptides.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,135,32,,,,,,,,,,,,,,,,,,,,,,12038,12047,2013, citations,entry_citation,19251,102298,1,,entry citation,,,23818155,,,"Structure, function, and tethering of DNA-binding domains in (54) transcriptional activators.",published,journal,Biopolymers,Biopolymers,99,12,,,,,,,,,,,,,,,,,,,,,,1082,1096,2013, citations,entry_citation,19252,102318,1,,entry citation,,,,,,RNA binding properties of the human NEXT complex,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19253,102334,1,,entry citation,,,23740819,,,Structural transitions in tau k18 on micelle binding suggest a hierarchy in the efficacy of individual microtubule-binding repeats in filament nucleation.,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,22,8,,,,,,,,,,,,,,,,,,,,,,1037,1048,2013, citations,entry_citation,19254,102353,1,,entry citation,,,24476493,,,Study of the Structural and Dynamic Effects in the FimH Adhesin upon alfa-D-Heptyl Mannose Binding,published,journal,J. 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Chem.,Journal of medicinal chemistry,57,4,,,,,,,,,,,,,,,,,,,,,,1416,1427,2014, citations,entry_citation,19257,102418,1,,entry citation,,,23991082,,,In-cell NMR characterization of the secondary structure populations of a disordered conformation of -synuclein within E. coli cells.,published,journal,PLoS ONE,PloS one,8,8,,,,,,,,,,,,,,,,,,,,,,e72286,e72286,2013, citations,citations,19258,102435,1,,entry citation,,,23991082,,,In-cell NMR characterization of the secondary structure populations of a disordered conformation of -synuclein within E. coli cells.,published,journal,PLoS ONE,PloS one,8,8,,,,,,,,,,,,,,,,,,,,,,e72286,e72286,2013, citations,citations,19259,102454,1,,entry citation,,,23968199,,,Molecular crowding drives active Pin1 into nonspecific complexes with endogenous proteins prior to substrate recognition,published,journal,J. Am. Chem. Soc.,,135,37,,,,,,,,,,,,,,,,,,,,,,13796,13803,2013, citations,entry_citation,19260,102473,1,,entry citation,,,,,,A pyrimidine motif triple helix in the Kluyveromyces lactis telomerase RNA pseudoknot is essential for function in vivo,in preparation,journal,Proc. Natl. Acad. Sci. U.S.A.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19261,102502,1,,entry citation,,,24066695,,,Structure and Dynamics of Full-Length HIV-1 Capsid Protein in Solution.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,135,43,,,,,,,,,,,,,,,,,,,,,,16133,16147,2013, citations,entry_citation,19262,102519,1,,entry citation,,,,,,Structure and immunogenicity of a peptide vaccine based on the membrane proximal external region of HIV-1 gp41,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19263,102536,1,,entry citation,,,,,,Structure and immunogenicity of a peptide vaccine based on the membrane proximal external region of HIV-1 gp41,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19264,102553,1,,entry citation,,,24066695,,,Structure and Dynamics of Full-Length HIV-1 Capsid Protein in Solution.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,135,43,,,,,,,,,,,,,,,,,,,,,,16133,16147,2013, citations,entry_citation,19266,102570,1,,entry citation,,,24218570,,,Prefusion structure of syntaxin-1A suggests pathway for folding into neuronal trans-SNARE complex fusion intermediate.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,110,48,,,,,,,,,,,,,,,,,,,,,,19384,19389,2013, citations,entry_citation,19267,102591,1,,entry citation,,,24205117,,,High-resolution NMR reveals secondary structure and folding of amino acid transporter from outer chloroplast membrane.,published,journal,PLoS ONE,PloS one,8,10,,,,,,,,,,,,,,,,,,,,,,e78116,e78116,2013, citations,citations,19268,102608,1,,entry citation,,,23871665,,,Thermodynamic Stabilization of the Folded Domain of Prion Protein Inhibits Prion Infection in Vivo,published,journal,Cell Rep.,,4,2,,,,,,,,,,,,,,,,,,,,,,248,254,2013, citations,entry_citation,19269,102633,1,,entry citation,,,24086265,,,Conformational dissection of a viral intrinsically disordered domain involved in cellular transformation.,published,journal,PLoS ONE,PloS one,8,9,,,,,,,,,,,,,,,,,,,,,,e72760,e72760,2013, citations,entry_citation,19270,102650,1,,entry citation,,,23760505,,,Characterization of the human sigma-1 receptor chaperone domain structure and binding immunoglobulin protein (BiP) interactions.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,29,,,,,,,,,,,,,,,,,,,,,,21448,21457,2013, citations,entry_citation,19271,102666,1,,entry citation,,,23810905,,,The Role of Aromatic-Aromatic Interactions in Strand-Strand Stabilization of -Sheets.,published,journal,J. Mol. Biol.,Journal of molecular biology,425,18,,,,,,,,,,,,,,,,,,,,,,3522,3535,2013, citations,entry_citation,19272,102683,1,,entry citation,,,,,,"1H, 15N, 13C resonance assignments of Yersinia phosphatase YopH",in preparation,journal,Biomol. NMR Assignments,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19273,102703,1,,entry citation,,,24265733,,,Cluster and fold stability of E. coli ISC-type ferredoxin.,published,journal,PLoS ONE,PloS one,8,11,,,,,,,,,,,,,,,,,,,,,,e78948,e78948,2013, citations,MlcC,19274,102723,1,,entry citation,,,,,,"Solution Structure of the Dictyostelium discodieum Myosin Light Chain, MlcC",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19275,102741,1,,entry citation,,,24814218,,,"Type AII Lantibiotic Bovicin HJ50 with a Rare Disulfide Bond: Structure, Structure-Activity Relationships and Mode of Action",published,journal,Biochem. J.,,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,Citation_1,19276,102761,1,,entry citation,,,23794476,,,Structural basis of DNA quadruplex-duplex junction formation.,published,journal,Angew. Chem. Int. Ed. 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Engl.,Angewandte Chemie (International ed. in English),52,33,,,,,,,,,,,,,,,,,,,,,,8566,8569,2013, citations,entry_citation,19282,102892,1,,entry citation,,,,,,NMR structure of the lymphocyte receptor NKR-P1A reveals a different conformation of the conserved loop compared to crystal structure,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,19283,102913,1,,entry citation,,,,,,Solution NMR structure of the RXFP2 LDLa module,in preparation,journal,To be Published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19284,102933,1,,entry citation,,,23868186,,,Structural Study of the Partially Disordered Full-Length Subunit of RNA Polymerase from Bacillus subtilis.,published,journal,Chembiochem,Chembiochem : a European journal of chemical biology,14,14,,,,,,,,,,,,,,,,,,,,,,1772,1779,2013, citations,entry_citation,19285,102949,1,,entry citation,,,24390440,,,Optimized ratiometric calcium sensors for functional in vivo imaging of neurons and T lymphocytes.,published,journal,Nat. 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NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,citation_1,19342,103960,1,,entry citation,,,,,,Transmembrane-cytosolic part of Trop2 explored by NMR and Molecular Dynamics,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19308,103374,1,,entry citation,,,23979961,,,"(1)H, (13)C and (15)N NMR assignments of a mutant of UV inducible transcript (S55A-UVI31+) from Chlamydomonas reinhardtii.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,19309,103389,1,,entry citation,,,23830862,,,3D NMR structure of a complex between the amyloid beta peptide (1-40) and the polyphenol epsilon-viniferin glucoside: Implications in Alzheimer's disease,published,journal,Biochim. Biophys. Acta,,1830,11,,,,,,,,,,,,,,,,,,,,,,5068,5074,2013, citations,entry_citation,19311,103406,1,,entry citation,,,24344315,,,Structure of Est3 reveals a bimodal surface with differential roles in telomere replication.,published,journal,Proc. Natl. Acad. Sci. 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J.,The Biochemical journal,453,3,,,,,,,,,,,,,,,,,,,,,,371,380,2013, citations,entry_citation,19325,103654,1,,entry citation,,,24037519,,,"(1)H, (13)C and (15)N resonance assignments of the VWA domain of Saccharomyces cerevisiae Rpn10, a regulatory subunit of 26S proteasome.",published,journal,Biomol. 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Chem.,The Journal of biological chemistry,289,3,,,,,,,,,,,,,,,,,,,,,,1294,1302,2014, citations,entry_citation,19392,104792,1,,entry citation,,,24074955,,,Structural Architecture of the CARMA1/Bcl10/MALT1 Signalosome: Nucleation-Induced Filamentous Assembly,published,journal,Mol. Cell,,51,6,,,,,,,,,,,,,,,,,,,,,,766,779,2013, citations,entry_citation,19393,104807,1,,entry citation,,,24395155,,,Solid-state NMR sequential assignment of Osaka-mutant amyloid-beta (A1-40 E22) fibrils.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,19394,104826,1,,entry citation,,,24789524,,,"Sparsely-sampled, high-resolution 4-D omit spectra for detection and assignment of intermolecular NOEs of protein complexes",published,journal,J. Biomol. NMR,,59,2,,,,,,,,,,,,,,,,,,,,,,51,56,2014, citations,entry_citation,19395,104850,1,,entry citation,,,,,,"Structure of human PRL-3, the phosphatase associated with cancer metastasis",published,journal,FEBS Lett.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19396,104869,1,,entry citation,,,24339323,,,Structural basis for antimicrobial activity of lasiocepsin.,published,journal,Chembiochem,Chembiochem : a European journal of chemical biology,15,2,,,,,,,,,,,,,,,,,,,,,,301,308,2014, citations,citation_1,19397,104886,1,,entry citation,,,,,,Structure of FAT10 first domain,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,19398,104905,1,,entry citation,,,,,,Solution structure of the forkhead domain of Brugia malayi DAF-16a,in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19399,104925,1,,entry citation,,,24139988,,,Structural Characterization of a Noncovalent Complex between Ubiquitin and the Transactivation Domain of the Erythroid-Specific Factor EKLF.,published,journal,Structure,"Structure (London, England : 1993)",21,11,,,,,,,,,,,,,,,,,,,,,,2014,2024,2013, citations,entry_citation,194,104943,1,,entry citation,,,,,"Saudek, Vladimir, Hoflack, Jan, Pelton, John T., ""1H-NMR study of endothelin, sequence-specific assignment of the spectrum and a solution structure,"" FEBS Lett. 257 (1), 145-148 (1989).","1H-NMR study of endothelin, sequence-specific assignment of the spectrum and a solution structure",published,journal,FEBS Lett.,,257,1,,,,,,,,,,,,,,,,,,,,,,145,148,1989, citations,entry_citation,19400,104956,1,,entry citation,,,24121435,,,The structure of the box C/D enzyme reveals regulation of RNA methylation.,published,journal,Nature,Nature,502,7472,,,,,,,,,,,,,,,,,,,,,,519,523,2013, citations,entry_citation,19402,104978,1,,entry citation,,,23999095,,,Structure of the human telomere in Na+ solution: an antiparallel (2+2) G-quadruplex scaffold reveals additional diversity.,published,journal,Nucleic Acids Res.,Nucleic acids research,41,22,,,,,,,,,,,,,,,,,,,,,,10556,10562,2013, citations,entry_citation,19403,104999,1,,entry citation,,,24071977,,,The Clip-Segment of the von Willebrand Domain 1 of the BMP Modulator Protein Crossveinless 2 Is Preformed,published,journal,Molecules,,18,10,,,,,,,,,,,,,,,,,,,,,,11658,11682,2013, citations,citations,19404,105018,1,,entry citation,,,,,,"Solution NMR Structure of DE NOVO DESIGNED Top7 Fold Protein Top7m13, Northeast Structural Genomics Consortium (NESG) Target OR33",in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19406,105053,1,,entry citation,,,23823328,,,"Unique structural, dynamical, and functional properties of K11-linked polyubiquitin chains",published,journal,Structure,,21,7,,,,,,,,,,,,,,,,,,,,,,1168,1181,2013, citations,entry_citation,19407,105069,1,,entry citation,,,24077225,,,Conformation and dynamics of the periplasmic membrane-protein-chaperone complexes OmpX-Skp and tOmpA-Skp,published,journal,Nat. Struct. Mol. Biol.,Nature Structural and Molecular Biology,20,11,,,,,,,,,,,,,,,,,,,,,,1265,1272,2013, citations,entry_citation,19408,105084,1,,entry citation,,,24077225,,,Conformation and dynamics of the periplasmic membrane-protein-chaperone complexes OmpX-Skp and tOmpA-Skp,published,journal,Nat. Struct. Mol. Biol.,Nature Structural and Molecular Biology,20,11,,,,,,,,,,,,,,,,,,,,,,1265,1272,2013, citations,entry_citation,19409,105100,1,,entry citation,,,24077225,,,Conformation and dynamics of the periplasmic membrane-protein-chaperone complexes OmpX-Skp and tOmpA-Skp,published,journal,Nat. Struct. Mol. Biol.,Nature Structural and Molecular Biology,20,11,,,,,,,,,,,,,,,,,,,,,,1265,1272,2013, citations,entry_citation,19410,105116,1,,entry citation,,,24077225,,,Conformation and dynamics of the periplasmic membrane-protein-chaperone complexes OmpX-Skp and tOmpA-Skp,published,journal,Nat. Struct. Mol. Biol.,Nature Structural and Molecular Biology,20,11,,,,,,,,,,,,,,,,,,,,,,1265,1272,2013, citations,entry_citation,19411,105132,1,,entry citation,,,24077225,,,Conformation and dynamics of the periplasmic membrane-protein-chaperone complexes OmpX-Skp and tOmpA-Skp,published,journal,Nat. Struct. Mol. Biol.,Nature Structural and Molecular Biology,20,11,,,,,,,,,,,,,,,,,,,,,,1265,1272,2013, citations,entry_citation,19412,105148,1,,entry citation,,,23823328,,,"Unique structural, dynamical, and functional properties of K11-linked polyubiquitin chains",published,journal,Structure,,21,7,,,,,,,,,,,,,,,,,,,,,,1168,1181,2013, citations,entry_citation,19413,105166,1,,entry citation,,,24244651,,,"Comparative Sequence, Structure and Redox Analyses of Klebsiella pneumoniae DsbA Show That Anti-Virulence Target DsbA Enzymes Fall into Distinct Classes",published,journal,PLOS One,,8,11,,,,,,,,,,,,,,,,,,,,,,e80210,e80210,2013, citations,entry_citation,19414,105184,1,,entry citation,,,,,,The DsbA oxidoreductase from Pseudomonas aeruginosa binds ligands at a site alternate to other DsbAs,in preparation,journal,PLOS One,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19415,105204,1,,entry citation,,,23417771,,,Backbone and side-chain assignments of a tethered complex between LMO4 and DEAF-1.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,8,1,,,,,,,,,,,,,,,,,,,,,,141,144,2014, citations,entry_citation,19416,105222,1,,entry citation,,,24130456,,,An RNA-binding complex involved in ribosome biogenesis contains a protein with homology to tRNA CCA-adding enzyme.,published,journal,PLoS Biol.,PLoS biology,11,10,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,19417,105240,1,,entry citation,,,,,,The DsbA oxidoreductase from Pseudomonas aeruginosa binds ligands at a site alternate to other DsbAs,in preparation,journal,PLOS One,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,PICK1_PDZ_binding_promiscuity,19418,105258,1,,entry citation,,,25023278,,,Protein interacting with C-kinase 1 (PICK1) binding promiscuity relies on unconventional PSD-95/discs-large/ZO-1 homology (PDZ) binding modes for nonclass II PDZ ligand,published,journal,J. Biol. Chem.,The Journal of biological chemistry,289,36,,1083-351X,,,,,,,,,,,,,,,,,,,,25327,25340,2014, citations,entry_citation,19419,105275,1,,entry citation,,,24258519,10.1007/s12104-013-9529-8,,"(1)H, (15)N and (13)C chemical shift assignments of the C-Ala domain of the alanyl-tRNA synthetase of the psychrophilic bacterium Bizionia argentinensis sp. nov.",published,journal,Biomol NMR Assign,Biomolecular NMR assignments,8,2,,1874-270X,,,,,,,,,,,,,,,,,,,,415,418,2014, citations,entry_citation,19421,105294,1,,entry citation,,,,,,Structural Basis of a Thiopeptide Antibiotic Multidrug Resistance System from Streptomyces lividans,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19422,105329,1,,entry citation,,,,,,Structural Basis of a Thiopeptide Antibiotic Multidrug Resistance System from Streptomyces lividans,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19423,105366,1,,entry citation,,,23955592,,,Differential recognition of syk-binding sites by each of the two phosphotyrosine-binding pockets of the Vav SH2 domain.,published,journal,Biopolymers,Biopolymers,99,11,,,,,,,,,,,,,,,,,,,,,,897,907,2013, citations,entry_citation,19424,105385,1,,entry citation,,,23978697,,,Type 2 ryanodine receptor domain A contains a unique and dynamic -helix that transitions to a -strand in a mutant linked with a heritable cardiomyopathy.,published,journal,J. Mol. Biol.,Journal of molecular biology,425,21,,,,,,,,,,,,,,,,,,,,,,4034,4046,2013, citations,entry_citation,19425,105400,1,,entry citation,,,23978697,,,Type 2 Ryanodine Receptor Domain A Contains a Unique and Dynamic -Helix That Transitions to a -Strand in a Mutant Linked with a Heritable Cardiomyopathy.,published,journal,J. Mol. Biol.,Journal of molecular biology,425,21,,,,,,,,,,,,,,,,,,,,,,4034,4046,2013, citations,entry_citation,19426,105418,1,,entry citation,,,24082096,,,Heme impairs the ball-and-chain inactivation of potassium channels.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,110,42,,,,,,,,,,,,,,,,,,,,,,E4036,E4044,2013, citations,entry_citation,19427,105436,1,,entry citation,,,24356916,,,The C-terminal domain of the transcriptional regulator BldD from Streptomyces coelicolor A3(2) constitutes a novel fold of winged-helix domains.,published,journal,Proteins,Proteins,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,19428,105454,1,,entry citation,,,24482445,,,A bacteriophage transcription regulator inhibits bacterial transcription initiation by -factor displacement.,published,journal,Nucleic Acids Res.,Nucleic acids research,42,7,,,,,,,,,,,,,,,,,,,,,,4294,4305,2014, citations,entry_citation,19429,105469,1,,entry citation,,,24482445,,,A bacteriophage transcription regulator inhibits bacterial transcription initiation by -factor displacement.,published,journal,Nucleic Acids Res.,Nucleic acids research,42,7,,,,,,,,,,,,,,,,,,,,,,4294,4305,2014, citations,entry_citation,19430,105487,1,,entry citation,,,24140750,,,"Binding of MgtR, a Salmonella Transmembrane Regulatory Peptide, to MgtC, a Mycobacterium tuberculosis Virulence Factor: A Structural Study.",published,journal,J. Mol. Biol.,Journal of molecular biology,426,2,,,,,,,,,,,,,,,,,,,,,,436,446,2014, citations,entry_citation,19431,105503,1,,entry citation,,,,,,NMR structure of a hypothetical protein RUMGNA_01855 from Ruminococcus gnavus ATCC 29149,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19432,105522,1,,entry citation,,,,,,"Primary identification, biochemical characterization, and immunologic properties of the allergenic pollen cyclophilin Cat r 1",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19433,105542,1,,entry citation,,,,,,NMR structure of the protein YP_002937094.1 from Eubacterium rectale,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,19435,105561,1,,entry citation,,,24088028,,,Structural Studies on Dinuclear Ruthenium(II) Complexes That Bind Diastereoselectively to an Antiparallel Folded Human Telomere Sequence.,published,journal,J. Med. Chem.,Journal of medicinal chemistry,56,21,,,,,,,,,,,,,,,,,,,,,,8674,8683,2013, citations,citation_1,19436,105580,1,,entry citation,,,24273131,,,Murine norovirus protein NS1/2 aspartate to glutamate mutation sufficient for persistence reorients sidechain of surface exposed tryptophan within a novel structured domain,published,journal,Proteins,,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,19437,105603,1,,entry citation,,,15522780,10.1016/j.jsb.2004.08.008,,Membrane-induced structure of the mammalian tachykinin neuropeptide gamma,published,journal,J. Struct. Biol.,,148,3,,,,,,,,,,,,,,,,,,,,,,315,325,2004, citations,entry_citation,19438,105620,1,,entry citation,,,,,,NMR structure of Tgam,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,19439,105635,1,,entry citation,,,24273131,,,Murine norovirus protein NS1/2 aspartate to glutamate mutation sufficient for persistence reorients sidechain of surface exposed tryptophan within a novel structured domain,published,journal,Proteins,,82,7,,,,,,,,,,,,,,,,,,,,,,1200,1209,2014, citations,entry_citation,19440,105658,1,,entry citation,,,24361616,,,"Polyaminooligonucleotide: NMR structure of duplex DNA containing a nucleoside with spermine residue, N-[4,9,13-triazatridecan-1-yl]-2'-deoxycytidine.",published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1840,3,,,,,,,,,,,,,,,,,,,,,,1163,1170,2014, citations,entry_citation,19441,105678,1,,entry citation,,,24361616,,,"Polyaminooligonucleotide: NMR structure of duplex DNA containing a nucleoside with spermine residue, N-[4,9,13-triazatridecan-1-yl]-2'-deoxycytidine",published,journal,Biochim. Biophys. Acta,,1840,3,,,,,,,,,,,,,,,,,,,,,,1163,1170,2014, citations,entry_citation,19442,105700,1,,entry citation,,,23940009,,,The Heterogeneous Structural Behavior of E7 from HPV16 Revealed by NMR Spectroscopy.,published,journal,Chembiochem,Chembiochem : a European journal of chemical biology,14,14,,,,,,,,,,,,,,,,,,,,,,1876,1882,2013, citations,citation_1,19443,105721,1,,entry citation,,,24510398,,,"(1)H, (13)C and (15)N backbone assignment of the EC-1 domain of human E-cadherin.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,9,1,,,,,,,,,,,,,,,,,,,,,,31,35,2015, citations,citation_1,19444,105735,1,,entry citation,,,24273131,,,Murine norovirus protein NS1/2 aspartate to glutamate mutation sufficient for persistence reorients sidechain of surface exposed tryptophan within a novel structured domain,published,journal,Proteins,,82,7,,,,,,,,,,,,,,,,,,,,,,1200,1209,2014, citations,entry_citation,19446,105758,1,,entry citation,,,24606314,,,Bound or Free: Interaction of the C-Terminal Domain of Escherichia coli Single-Stranded DNA-Binding Protein (SSB) with the Tetrameric Core of SSB.,published,journal,Biochemistry,Biochemistry,53,12,,,,,,,,,,,,,,,,,,,,,,1925,1934,2014, citations,citations,19447,105773,1,,entry citation,,,24039852,,,Distinct ubiquitin binding modes exhibited by SH3 domains: molecular determinants and functional implications,published,journal,PLoS One,,8,9,,,,,,,,,,,,,,,,,,,,,,e73018,e73018,2013, citations,citation_1,19448,105798,1,,entry citation,,,24088028,,,Structural Studies on Dinuclear Ruthenium(II) Complexes That Bind Diastereoselectively to an Antiparallel Folded Human Telomere Sequence.,published,journal,J. Med. Chem.,Journal of medicinal chemistry,56,21,,,,,,,,,,,,,,,,,,,,,,8674,8683,2013, citations,citations,19449,105818,1,,entry citation,,,,,,"NMR structure of a BolA-like hypothetical protein RP812 from RICKETTSIA PROWAZEKII, SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)",in preparation,journal,To be Published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19450,105835,1,,entry citation,,,24891519,,,Kv1.3 channel-blocking immunomodulatory peptides from parasitic worms: implications for autoimmune diseases,published,journal,FASEB J.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19451,105854,1,,entry citation,,,24591642,,,Understanding the antagonism of retinoblastoma protein dephosphorylation by PNUTS provides insights into the PP1 regulatory code.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,111,11,,,,,,,,,,,,,,,,,,,,,,4097,4102,2014, citations,entry_citation,19452,105870,1,,entry citation,,,,,,Solution structure of the Ehrlichia chaffeensis thioredoxin ECH_0218 in the reduced state: disorder around the CXXC active site.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19453,105890,1,,entry citation,,,,,,NMR structure of the protein ZP_02042476.1 from Ruminococcus gnavus.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,19454,105908,1,,entry citation,,,24410116,,,"High-Resolution Structures and Orientations of Antimicrobial Peptides Piscidin 1 and Piscidin 3 in Fluid Bilayers Reveal Tilting, Kinking, and Bilayer Immersion",published,journal,J. Am. Chem. Soc.,,136,9,,,,,,,,,,,,,,,,,,,,,,3491,3504,2014, citations,citations,19455,105941,1,,entry citation,,,24410116,,,"High-Resolution Structures and Orientations of Antimicrobial Peptides Piscidin 1 and Piscidin 3 in Fluid Bilayers Reveal Tilting, Kinking, and Bilayer Immersion",published,journal,J. Am. Chem. Soc.,,136,9,,,,,,,,,,,,,,,,,,,,,,3491,3504,2014, citations,citations,19456,105971,1,,entry citation,,,24410116,,,"High-Resolution Structures and Orientations of Antimicrobial Peptides Piscidin 1 and Piscidin 3 in Fluid Bilayers Reveal Tilting, Kinking, and Bilayer Immersion",published,journal,J. Am. Chem. Soc.,,136,9,,,,,,,,,,,,,,,,,,,,,,3491,3504,2014, citations,citations,19457,105999,1,,entry citation,,,24410116,,,"High-Resolution Structures and Orientations of Antimicrobial Peptides Piscidin 1 and Piscidin 3 in Fluid Bilayers Reveal Tilting, Kinking, and Bilayer Immersion",published,journal,J. Am. Chem. Soc.,,136,9,,,,,,,,,,,,,,,,,,,,,,3491,3504,2014, citations,entry_citation,19458,106028,1,,entry citation,,,24214979,,,Using Mutagenesis and Structural Biology to Map the Binding Site for the Plasmodium falciparum Merozoite Protein PfRh4 on the Human Immune Adherence Receptor.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,289,1,,,,,,,,,,,,,,,,,,,,,,450,463,2014, citations,entry_citation,19459,106048,1,,entry citation,,,24214979,,,Using Mutagenesis and Structural Biology to Map the Binding Site for the Plasmodium falciparum Merozoite Protein PfRh4 on the Human Immune Adherence Receptor.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,289,1,,,,,,,,,,,,,,,,,,,,,,450,463,2014, citations,entry_citation,19460,106068,1,,entry citation,,,24891519,,,Kv1.3 channel-blocking immunomodulatory peptides from parasitic worms: implications for autoimmune diseases,published,journal,Faseb J.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19461,106088,1,,entry citation,,,24234348,,,NMR assignments for the cis and trans forms of the hemolysin II C-terminal domain.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,19462,106108,1,,entry citation,,,24234348,,,NMR assignments for the cis and trans forms of the hemolysin II C-terminal domain.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,19463,106128,1,,entry citation,,,24234348,,,NMR assignments for the cis and trans forms of the hemolysin II C-terminal domain.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,19464,106147,1,,entry citation,,,24502667,,,The HicA toxin from Burkholderia pseudomallei has a role in persister cell formation.,published,journal,Biochem. J.,The Biochemical journal,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,citation_1,19497,106699,1,,entry citation,,,24070253,,,Gelsolin-like activation of villin: calcium sensitivity of the long helix in domain 6.,published,journal,Biochemistry,Biochemistry,52,45,,,,,,,,,,,,,,,,,,,,,,7890,7900,2013, citations,PICK1_PDZ_ASIC1a_C-terminal,19466,106174,1,,entry citation,,,25023278,,,Protein interacting with C-kinase 1 (PICK1) binding promiscuity relies on unconventional PSD-95/discs-large/ZO-1 homology (PDZ) binding modes for nonclass II PDZ ligand,published,journal,J. Biol. Chem.,The Journal of biological chemistry,289,36,,1083-351X,,,,,,,,,,,,,,,,,,,,25327,25340,2014, citations,PKCalpha,19467,106193,1,,entry citation,,,25023278,,,Protein interacting with C-kinase 1 (PICK1) binding promiscuity relies on unconventional PSD-95/discs-large/ZO-1 homology (PDZ) binding modes for nonclass II PDZ ligand,published,journal,J. Biol. Chem.,The Journal of biological chemistry,289,36,,1083-351X,,,,,,,,,,,,,,,,,,,,25327,25340,2014, citations,entry_citation,19468,106209,1,,entry citation,,,,,,Fragment based approach and binding behavior of LFampinB with Lipopolysaccharide: biophysical aspects,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19469,106224,1,,entry citation,,,,,,Fragment based approach and binding behaviour of LFampinB with Lipopolysaccharide: biophysical aspects,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19470,106239,1,,entry citation,,,,,,Fragment based approach and binding behavior of LFampinB with Lipopolysaccharide: biophysical aspects,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19471,106254,1,,entry citation,,,,,,Fragment based approach and binding behaviour of LFampinB with Lipopolysaccharide: biophysical aspects,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,Sp140_PHD_finger,19472,106269,1,,entry citation,,,24267382,,,Structure of human Sp140 PHD finger: an atypical fold interacting with Pin1.,published,journal,FEBS J.,The FEBS journal,281,1,,,,,,,,,,,,,,,,,,,,,,216,231,2014, citations,Sp140_PHD_finger,19473,106292,1,,entry citation,,,24267382,,,Structure of human Sp140 PHD finger: an atypical fold interacting with Pin1.,published,journal,FEBS J.,The FEBS journal,281,1,,,,,,,,,,,,,,,,,,,,,,216,231,2014, citations,entry_citation,19474,106315,1,,entry citation,,,24333486,,,Steric Mechanism of Auto-Inhibitory Regulation of Specific and Non-Specific DNA Binding by the ETS Transcriptional Repressor ETV6.,published,journal,J. Mol. Biol.,Journal of molecular biology,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,citations,19476,106335,1,,entry citation,,,24567324,,,"Structure-Function Elucidation of a New -Conotoxin, Lo1a, from Conus longurionis.",published,journal,J. Biol. Chem.,The Journal of biological chemistry,289,14,,,,,,,,,,,,,,,,,,,,,,9573,9583,2014, citations,entry_citation,19477,106351,1,,entry citation,,,24052412,,,HN(CA)N and HN(COCA)N experiments for assignment of large disordered proteins.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,57,2,,,,,,,,,,,,,,,,,,,,,,83,89,2013, citations,Pfaff_PNAS2013,19478,106366,1,,entry citation,,,24043833,,,Structural features of Argonaute-GW182 protein interactions.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,110,40,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,Citation_1,19479,106380,1,,entry citation,,,24704508,,,Crystal Structure of a PCP/Sfp Complex Reveals the Structural Basis for Carrier Protein Posttranslational Modification.,published,journal,Chem. Biol.,Chemistry & biology,21,4,,,,,,,,,,,,,,,,,,,,,,552,562,2014, citations,entry_citation,19480,106399,1,,entry citation,,,24361276,,,The Solution Structure of the Regulatory Domain of Tyrosine Hydroxylase.,published,journal,J. Mol. Biol.,Journal of molecular biology,426,7,,,,,,,,,,,,,,,,,,,,,,1483,1497,2013, citations,entry_citation,19481,106416,1,,entry citation,,,24361276,,,The Solution Structure of the Regulatory Domain of Tyrosine Hydroxylase.,published,journal,J. Mol. Biol.,Journal of molecular biology,426,7,,,,,,,,,,,,,,,,,,,,,,1483,1497,2013, citations,entry_citation,19482,106433,1,,entry citation,,,24361276,10.1016/j.jmb.2013.12.015,,The Solution Structure of the Regulatory Domain of Tyrosine Hydroxylase,published,journal,J. Mol. Biol.,,426,7,,,,,,,,,,,,,,,,,,,,,,1483,1497,2013, citations,entry_citation,19483,106461,1,,entry citation,,,24412394,,,Autoinhibitory Structure of the WW Domain of HYPB/SETD2 Regulates Its Interaction with the Proline-Rich Region of Huntingtin.,published,journal,Structure,"Structure (London, England : 1993)",,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,19484,106481,1,,entry citation,,,24840010,,,Structural and Functional Analysis of the Transmembrane Segment Pair VI and VII of the NHE1 Isoform of the Na(+)/H(+) Exchanger,published,journal,Biochemistry,,53,22,,,,,,,,,,,,,,,,,,,,,,3658,3670,2014, citations,entry_citation,19485,106500,1,,entry citation,,,24055875,,,Structure and expression of a novel compact myelin protein - small VCP-interacting protein (SVIP).,published,journal,Biochem. Biophys. Res. Commun.,Biochemical and biophysical research communications,440,1,,,,,,,,,,,,,,,,,,,,,,173,178,2013, citations,citations,19486,106514,1,,entry citation,,,,,,"Solution NMR Structure of Zinc finger protein 423 from Homo sapiens, Northeast Structural Genomics Consortium (NESG) Target HR7298F",in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19487,106541,1,,entry citation,,,24412394,,,Autoinhibitory Structure of the WW Domain of HYPB/SETD2 Regulates Its Interaction with the Proline-Rich Region of Huntingtin.,published,journal,Structure,"Structure (London, England : 1993)",,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,19488,106560,1,,entry citation,,,24412394,,,Autoinhibitory Structure of the WW Domain of HYPB/SETD2 Regulates Its Interaction with the Proline-Rich Region of Huntingtin,published,journal,Structure,,22,3,,,,,,,,,,,,,,,,,,,,,,378,386,2014, citations,entry_citation,19489,106578,1,,entry citation,,,23333387,,,ALS-causing P56S mutation and splicing variation on the hVAPB MSP domain transform its -sandwich fold into lipid-interacting helical conformations.,published,journal,Biochem. Biophys. Res. Commun.,Biochemical and biophysical research communications,431,3,,,,,,,,,,,,,,,,,,,,,,398,403,2013, citations,entry_citation,19490,106593,1,,entry citation,,,24234349,,,Backbone resonance assignments of human cytosolic dNT-1 nucleotidase.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,19491,106610,1,,entry citation,,,24504927,,,"(1)H, (13)C, and (15)N backbone and side-chain chemical shift assignments for the 36 proline-containing, full length 29kDa human chimera-type galectin-3.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,19493,106633,1,,entry citation,,,,,,NMR structure of purotoxin-2 in water,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,19494,106652,1,,entry citation,,,25584704,,,The C-terminal RNA binding motif of HuR is a multi-functional domain leading to HuR oligomerization and binding to U-rich RNA targets,published,journal,RNA Biol.,,11,10,,,,,,,,,,,,,,,,,,,,,,1250,1261,2014, citations,entry_citation,19495,106669,1,,entry citation,,,24414222,,,"H(N), N(H), C (), C (), and methyl group assignments of filamin multidomain fragments IgFLNc4-5 and IgFLNa3-5.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,19496,106684,1,,entry citation,,,24414222,,,"H(N), N(H), C (), C (), and methyl group assignments of filamin multidomain fragments IgFLNc4-5 and IgFLNa3-5.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,19498,106717,1,,entry citation,,,,,,The bacteriophage T7 encoded inhibitor (gp1.2) of E. coli dGTP triphosphohydrolase,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,19499,106738,1,,entry citation,,,25584704,,,The C-terminal RNA binding motif of HuR is a multi-functional domain leading to HuR oligomerization and binding to U-rich RNA targets,published,journal,RNA Biol.,,11,10,,,,,,,,,,,,,,,,,,,,,,1250,1261,2014, citations,entry_citation,195,106755,1,,entry citation,,,,,"Neri, Dario, Szyperski, Thomas, Otting, Gottfried, Senn, Hans, Wuthrich, Kurt, ""Stereospecific Nuclear Magnetic Resonance Assignments of the Methyl Groups of Valine and Leucine in the DNA-Binding Domain of the 434 Repressor by Biosynthetically Directed Fractional 13C Labeling,"" Biochemistry 28, 7510-7516 (1989).","Stereospecific Nuclear Magnetic Resonance Assignments of the Methyl Groups of Valine and Leucine in the DNA-Binding Domain of the 434 Repressor by Biosynthetically Directed Fractional 13C Labeling",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,7510,7516,1989, citations,citation_1,19500,106768,1,,entry citation,,,25584704,,,The C-terminal RNA binding motif of HuR is a multi-functional domain leading to HuR oligomerization and binding to U-rich RNA targets,published,journal,RNA Biol.,,11,10,,,,,,,,,,,,,,,,,,,,,,1250,1261,2014, citations,entry_citation,19501,106785,1,,entry citation,,,24398291,,,A novel 4/7-conotoxin LvIA from Conus lividus that selectively blocks 32 vs. 6/323 nicotinic acetylcholine receptors.,published,journal,FASEB J.,FASEB journal : official publication of the Federation of American Societies for Experimental Biology,28,4,,,,,,,,,,,,,,,,,,,,,,1842,1853,2014, citations,entry_citation,19502,106805,1,,entry citation,,,24753571,,,A bimodular nuclear localization signal assembled via an extended double-stranded RNA-binding domain acts as an RNA-sensing signal for transportin 1.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,19503,106832,1,,entry citation,,,24350581,,,Circular Permutation of a WW Domain: Folding Still Occurs after Excising the Turn of the Folding-Nucleating Hairpin.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,136,2,,,,,,,,,,,,,,,,,,,,,,741,749,2014, citations,entry_citation,19504,106848,1,,entry citation,,,,,,Covalent Assembly of Homooligomeric Proteins Using Structure-templating Hubs,in preparation,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19505,106865,1,,entry citation,,,,,,Covalent Assembly of Homooligomeric Proteins Using Structure-templating Hubs,in preparation,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19506,106882,1,,entry citation,,,24452424,,,"Backbone (1)H, (13)C and (15)N resonance assignments of the human eukaryotic release factor eRF1.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,19507,106899,1,,entry citation,,,,,,Pseudo 5D HN(C)N Experiment to Facilitate the Assignment of Backbone Resonances in Proteins Exhibiting High Backbone Shift Degeneracy,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,19508,106913,1,,entry citation,,,,,,Solution structure of the human wild type FAPP1-PH domain,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19510,106930,1,,entry citation,,,,,,NMR structure of the putative ATPase regulatory protein YP_916642.1 from Paracoccus denitrificans,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19511,106947,1,,entry citation,,,27396829,,,Dynamic Local Polymorphisms in the Gbx1 Homeodomain Induced by DNA Binding,published,journal,Structure,,24,8,,,,,,,,,,,,,,,,,,,,,,1372,1379,2016, citations,entry_citation,19512,106967,1,,entry citation,,,24075869,,,Disruption of helix-capping residues 671 and 674 reveals a role in HIV-1 entry for a specialized hinge segment of the membrane proximal external region of gp41.,published,journal,J. Mol. Biol.,Journal of molecular biology,426,5,,,,,,,,,,,,,,,,,,,,,,1095,1108,2014, citations,entry_citation,19513,106991,1,,entry citation,,,24075869,,,Disruption of helix-capping residues 671 and 674 reveals a role in HIV-1 entry for a specialized hinge segment of the membrane proximal external region of gp41.,published,journal,J. Mol. Biol.,Journal of molecular biology,426,5,,,,,,,,,,,,,,,,,,,,,,1095,1108,2014, citations,entry_citation,19514,107015,1,,entry citation,,,24075869,,,Disruption of helix-capping residues 671 and 674 reveals a role in HIV-1 entry for a specialized hinge segment of the membrane proximal external region of gp41.,published,journal,J. Mol. Biol.,Journal of molecular biology,426,5,,,,,,,,,,,,,,,,,,,,,,1095,1108,2014, citations,entry_citation,19515,107039,1,,entry citation,,,24075869,,,Disruption of helix-capping residues 671 and 674 reveals a role in HIV-1 entry for a specialized hinge segment of the membrane proximal external region of gp41.,published,journal,J. Mol. Biol.,Journal of molecular biology,426,5,,,,,,,,,,,,,,,,,,,,,,1095,1108,2014, citations,citation1,19516,107063,1,,entry citation,,,,,,Solution NMR structure of Dot1L in complex with AF9 (Dot1L-AF9).,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19517,107087,1,,entry citation,,,24192053,,,Architecture of the hepatitis C virus E1 glycoprotein transmembrane domain studied by NMR.,published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1838,3,,,,,,,,,,,,,,,,,,,,,,784,792,2014, citations,entry_citation,19518,107104,1,,entry citation,,,24414277,,,Solution NMR assignment of the heavy chain complex of the human cardiac myosin regulatory light chain,published,journal,J. Biomol. NMR,,9,1,,,,,,,,,,,,,,,,,,,,,,51,53,2014, citations,entry_citation,19519,107127,1,,entry citation,,,24821061,,,Cytotoxicity of recombinant tamapin and related toxin-like peptides on model cell lines.,published,journal,Chem. Res. Toxicol.,Chemical research in toxicology,27,6,,,,,,,,,,,,,,,,,,,,,,960,967,2014, citations,entry_citation,19520,107142,1,,entry citation,,,,,,The DNA Binding Domain is a Promiscuous Interaction Hub that Mediates the Nuclear and Cytoplasmic Functions of p53,submitted,journal,Nat. Struct. Biol.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19521,107160,1,,entry citation,,,,,,The DNA Binding Domain is a Promiscuous Interaction Hub that Mediates the Nuclear and Cytoplasmic Functions of p53,submitted,journal,Nat. Struct. Biol.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19522,107178,1,,entry citation,,,,,,The DNA Binding Domain is a Promiscuous Interaction Hub that Mediates the Nuclear and Cytoplasmic Functions of p53,submitted,journal,Nat. Struct. Biol.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19523,107207,1,,entry citation,,,24362019,,,Structure of the TbBILBO1 protein N-terminal domain from Trypanosoma brucei reveals an essential requirement for a conserved surface patch.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,289,6,,,,,,,,,,,,,,,,,,,,,,3724,3735,2014, citations,entry_citation,19524,107226,1,,entry citation,,,24821061,,,Cytotoxicity of recombinant tamapin and related toxin-like peptides on model cell lines.,published,journal,Chem. Res. Toxicol.,Chemical research in toxicology,27,6,,,,,,,,,,,,,,,,,,,,,,960,967,2014, citations,entry_citation,19525,107243,1,,entry citation,,,,,,Structural basis of nucleic acid binding by Nicotiana tabacum glycine-rich RNA binding protein: implications for its RNA chaperone function,in preparation,journal,To be published,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19526,107261,1,,entry citation,,,24727478,,,Solution NMR Structure of the DNA-binding Domain from Scml2 (Sex Comb onMidleg-like 2),published,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,19527,107280,1,,entry citation,,,24821061,,,Cytotoxicity of recombinant tamapin and related toxin-like peptides on model cell lines.,published,journal,Chem. Res. Toxicol.,Chemical research in toxicology,27,6,,,,,,,,,,,,,,,,,,,,,,960,967,2014, citations,entry_citation,19528,107297,1,,entry citation,,,24821061,,,Cytotoxicity of recombinant tamapin and related toxin-like peptides on model cell lines.,published,journal,Chem. Res. Toxicol.,Chemical research in toxicology,27,6,,,,,,,,,,,,,,,,,,,,,,960,967,2014, citations,entry_citation,19530,107314,1,,entry citation,,,24435566,10.1007/s10858-014-9812-8,,Solution structure of the RecQ C-terminal domain of human Bloom syndrome protein.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,58,2,JBNME9,0925-2738,,,,,,,,,,,,,,,,,,,,141,147,2014, citations,citations,19531,107328,1,,entry citation,,,,,,NMR spatial structure of the trimeric mutant TM domain of VEGFR2 receptor,in preparation,journal,To be Published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,19532,107345,1,,entry citation,,,,,,NMR spatial structure of mutant dimeric TM domain of VEGFR2 receptor,in preparation,journal,To be Published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19533,107362,1,,entry citation,,,,,,Solution Structure of NusE from Thermotoga maritima,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19534,107378,1,,entry citation,,,24828038,,,Structural basis of the non-coding RNA RsmZ acting as a protein sponge.,published,journal,Nature,Nature,509,7502,,,,,,,,,,,,,,,,,,,,,,588,592,2014, citations,entry_citation,19535,107405,1,,entry citation,,,,,,Structure of SGTX1-SF1A,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19536,107424,1,,entry citation,,,,,,NMR assignements of ACP5a,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19538,107441,1,,entry citation,,,24653034,,,Structure of the mitochondrial translocator protein in complex with a diagnostic ligand.,published,journal,Science,"Science (New York, N.Y.)",343,6177,,,,,,,,,,,,,,,,,,,,,,1363,1366,2014, citations,entry_citation,19539,107459,1,,entry citation,,,,,,"1H, 13C, 15N chemical shifts assignments of streptomyces virginiae VirA acp5b",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19540,107478,1,,entry citation,,,24097990,,,A structural analysis of DNA binding by myelin transcription factor 1 double zinc fingers.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,49,,,,,,,,,,,,,,,,,,,,,,35180,35191,2013, citations,entry_citation,19541,107496,1,,entry citation,,,,,,Structure of the Nucleoplasmin-like N-terminal domain of FKBP39,in preparation,journal,To BE Published,To BE Published,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19542,107527,1,,entry citation,,,24323786,,,"Chemical Synthesis, 3D Structure, and ASIC Binding Site of the Toxin Mambalgin-2.",published,journal,Angew. Chem. Int. Ed. Engl.,Angewandte Chemie (International ed. in English),53,4,,,,,,,,,,,,,,,,,,,,,,1017,1020,2014, citations,entry_citation,19544,107547,1,,entry citation,,,24561806,,,Molecular basis for the wide range of affinity found in Csr/Rsm protein-RNA recognition.,published,journal,Nucleic Acids Res.,Nucleic acids research,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,19545,107576,1,,entry citation,,,,,,The Solution Structure of a cGCUUAg RNA Pentaloop from Bovine Enterovirus Vir 404/03,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19546,107597,1,,entry citation,,,24561806,,,Molecular basis for the wide range of affinity found in Csr/Rsm protein-RNA recognition.,published,journal,Nucleic Acids Res.,Nucleic acids research,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,19547,107626,1,,entry citation,,,24561806,,,Molecular basis for the wide range of affinity found in Csr/Rsm protein-RNA recognition.,published,journal,Nucleic Acids Res.,Nucleic acids research,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,19548,107655,1,,entry citation,,,24561806,,,Molecular basis for the wide range of affinity found in Csr/Rsm protein-RNA recognition.,published,journal,Nucleic Acids Res.,Nucleic acids research,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,19549,107684,1,,entry citation,,,24561806,,,Molecular basis for the wide range of affinity found in Csr/Rsm protein-RNA recognition.,published,journal,Nucleic Acids Res.,Nucleic acids research,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,19550,107711,1,,entry citation,,,24682851,,,Resonance assignment of the ribosome binding domain of E. coli ribosomal protein S1.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,19551,107735,1,,entry citation,,,24414276,,,"(1)H, (13)C and (15)N resonance assignments of human FK506 binding protein 25.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,19552,107754,1,,entry citation,,,,,,Solution structure of Blo 1 19,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19553,107779,1,,entry citation,,,,,,Solution structure of Blo 1 12 CBD domain.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19554,107800,1,,entry citation,,,24682851,,,Resonance assignment of the ribosome binding domain of E. coli ribosomal protein S1.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,19555,107824,1,,entry citation,,,24211833,,,Solution NMR studies of the plant peptide hormone CEP inform function,published,journal,FEBS Lett.,,587,24,,,,,,,,,,,,,,,,,,,,,,3979,3985,2013, citations,entry_citation,19556,107842,1,,entry citation,,,24211833,,,Solution NMR studies of the plant peptide hormone CEP inform function,published,journal,FEBS Lett.,,587,24,,,,,,,,,,,,,,,,,,,,,,3979,3985,2013, citations,entry_citation,19557,107860,1,,entry citation,,,24284492,,,Solution Structure of the Circular -Domain Analog from the Wheat Metallothionein Ec-1.,published,journal,Molecules,"Molecules (Basel, Switzerland)",18,11,,,,,,,,,,,,,,,,,,,,,,14414,14429,2013, citations,entry_citation,19558,107885,1,,entry citation,,,24496608,,,"Backbone and stereospecific (13)C methyl Ile (1), Leu and Val side-chain chemical shift assignments of Crc.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,19559,107906,1,,entry citation,,,24240096,,,Interaction of Bcl-2 with the Autophagy-related GABAA Receptor-associated Protein (GABARAP): BIOPHYSICAL CHARACTERIZATION AND FUNCTIONAL IMPLICATIONS.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,288,52,,,,,,,,,,,,,,,,,,,,,,37204,37215,2013, citations,entry_citation,19560,107927,1,,entry citation,,,21460846,10.1038/nsmb.2045,,The client protein p53 forms a molten globule-like state in the presence of Hsp90,published,journal,Nat. Struct. Biol.,,18,5,,,,,,,,,,,,,,,,,,,,,,537,542,2011, citations,entry_citation,19561,107947,1,,entry citation,,,24659459,,,Sequence-specific resonance assignments of human TAF15-RRM and TAF15-RRM-RanBP2.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,19904,113776,1,,entry citation,,,,,,Solution structure of TbPar42,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19562,107962,1,,entry citation,,,24470253,,,Structural insights into FRS2 PTB domain recognition by neurotrophin receptor TrkB.,published,journal,Proteins,Proteins,82,7,,,,,,,,,,,,,,,,,,,,,,1534,1541,2014, citations,entry_citation,19563,107993,1,,entry citation,,,24498949,,,Side Chain Conformational Averaging in Human Dihydrofolate Reductase,published,journal,Biochemistry,Biochemistry,53,7,,,,,,,,,,,,,,,,,,,,,,1134,1145,2014, citations,citation_2,19563,107994,2,,reference citation,,,,,,The Dynamics and Conformations of human Dihydrofolate Reductase Side Chains,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19564,108012,1,,entry citation,,,24498949,,,Side Chain Conformational Averaging in Human Dihydrofolate Reductase,published,journal,Biochemistry,Biochemistry,53,7,,,,,,,,,,,,,,,,,,,,,,1134,1145,2014, citations,citation_2,19564,108013,2,,reference citation,,,,,,The Dynamics and Conformations of human Dihydrofolate Reductase Side Chains,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19565,108033,1,,entry citation,,,24498949,,,Side Chain Conformational Averaging in Human Dihydrofolate Reductase,published,journal,Biochemistry,Biochemistry,53,7,,,,,,,,,,,,,,,,,,,,,,1134,1145,2014, citations,citation_2,19565,108034,2,,reference citation,,,,,,The Dynamics and Conformations of human Dihydrofolate Reductase Side Chains,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19566,108056,1,,entry citation,,,24498949,,,Side Chain Conformational Averaging in Human Dihydrofolate Reductase,published,journal,Biochemistry,Biochemistry,53,7,,,,,,,,,,,,,,,,,,,,,,1134,1145,2014, citations,citation_2,19566,108057,2,,reference citation,,,,,,The Dynamics and Conformations of human Dihydrofolate Reductase Side Chains,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19567,108077,1,,entry citation,,,24498949,,,Side Chain Conformational Averaging in Human Dihydrofolate Reductase,published,journal,Biochemistry,Biochemistry,53,7,,,,,,,,,,,,,,,,,,,,,,1134,1145,2014, citations,citation_2,19567,108078,2,,reference citation,,,,,,The Dynamics and Conformations of human Dihydrofolate Reductase Side Chains,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19568,108100,1,,entry citation,,,24440425,,,Solution structure of the transmembrane domain of the insulin receptor in detergent micelles.,published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1838,5,,,,,,,,,,,,,,,,,,,,,,1313,1321,2014, citations,entry_citation,19569,108118,1,,entry citation,,,24366722,,,Backbone and side-chain NMR assignments for the C-terminal domain of mammalian Vps28.,published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,19570,108136,1,,entry citation,,,,,,A cactus derived toxin-like cystine knot peptide with selective antimicrobial activity,submitted,journal,ChemBioChem,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19571,108155,1,,entry citation,,,30182059,,,Encoding canonical DNA quadruplex structure.,published,journal,Sci. Adv.,Science advances,4,8,,2375-2548,0353,,,,,,,,,,,,,,,,,,,eaat3007,eaat3007,2018, citations,entry_citation,19572,108176,1,,entry citation,,,,,,In preparation,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,19573,108196,1,,entry citation,,,24446383,,,Xanthomonins I-III: a new class of lasso peptides with a seven-residue macrolactam ring.,published,journal,Angew. Chem. Int. Ed. Engl.,Angewandte Chemie (International ed. in English),53,8,,,,,,,,,,,,,,,,,,,,,,2230,2234,2014, citations,entry_citation,19575,108211,1,,entry citation,,,24370930,,,Site-specific structural variations accompanying tubular assembly of the HIV-1 capsid protein.,published,journal,J. Mol. Biol.,Journal of molecular biology,426,5,,,,,,,,,,,,,,,,,,,,,,1109,1127,2014, citations,entry_citation,19576,108232,1,,entry citation,,,24462251,,,Interaction of Fapp1 with Arf1 and PI4P at a membrane surface: an example of coincidence detection.,published,journal,Structure,"Structure (London, England : 1993)",22,3,,,,,,,,,,,,,,,,,,,,,,421,430,2014, citations,entry_citation,19577,108250,1,,entry citation,,,23768016,,,Dicarba alpha-conotoxin Vc1.1 analogues with differential selectivity for nicotinic acetylcholine and GABAB receptors,published,journal,ACS Chem. Biol.,,8,8,,,,,,,,,,,,,,,,,,,,,,1815,1821,2013, citations,entry_citation,19578,108269,1,,entry citation,,,23768016,,,Dicarba alpha-conotoxin Vc1.1 analogues with differential selectivity for nicotinic acetylcholine and GABAB receptors,published,journal,ACS Chem. Biol.,,8,8,,,,,,,,,,,,,,,,,,,,,,1815,1821,2013, citations,entry_citation,19579,108288,1,,entry citation,,,25093327,,,Carbonic Anhydrase Generates CO2 and H+ That Drive Spider Silk Formation Via Opposite Effects on the Terminal Domains,published,journal,Plos Biol.,,12,8,,,,,,,,,,,,,,,,,,,,,,e1001921,e1001921,2014, citations,PAP262-270,19580,108309,1,,entry citation,,,,,,PAP262-270 in SDS micelles,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,19581,108327,1,,entry citation,,,,,,The Atomic Structure of the HIV-1 gp41 Transmembrane Domain and its Connection to the Inmmunogenic Membrane-proximal External Region,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,19582,108344,1,,entry citation,,,,,,The Atomic Structure of the HIV-1 gp41 Transmembrane Domain and its Connection to the Inmmunogenic Membrane-proximal External Region,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,19583,108362,1,,entry citation,,,,,,The Atomic Structure of the HIV-1 gp41 Transmembrane Domain and its Connection to the Inmmunogenic Membrane-proximal External Region,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19584,108380,1,,entry citation,,,24606934,,,Biophysical and Molecular-Dynamics Studies of Phosphatidic Acid Binding by the Dvl-2 DEP Domain.,published,journal,Biophys. J.,Biophysical journal,106,5,,,,,,,,,,,,,,,,,,,,,,1101,1111,2014, citations,entry_citation,19585,108396,1,,entry citation,,,,,,Computational design and experimental verification of a symmetric homodimer,in preparation,journal,Proc. Natl. Acad. Sci. U.S.A.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19586,108411,1,,entry citation,,,24495081,,,Solution structure of calmodulin bound to the target peptide of endothelial nitric oxide synthase phosphorylated at Thr495.,published,journal,Biochemistry,Biochemistry,53,8,,,,,,,,,,,,,,,,,,,,,,1241,1249,2014, citations,entry_citation,19587,108427,1,,entry citation,,,23768016,,,Dicarba alpha-conotoxin Vc1.1 analogues with differential selectivity for nicotinic acetylcholine and GABAB receptors,published,journal,ACS Chem. Biol.,,8,8,,,,,,,,,,,,,,,,,,,,,,1815,1821,2013, citations,entry_citation,19589,108446,1,,entry citation,,,29280056,10.1007/s12104-017-9794-z,,"Assignment of 1H, 13C and 15N resonances and secondary structure of the Rgd1-RhoGAP domain",published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,12,1,,1874-270X,,,,,,,,,,,,,,,,,,,,129,132,2018, citations,citation_1,19590,108464,1,,entry citation,,,24211467,,,Visualizing side chains of invisible protein conformers by solution NMR.,published,journal,J. Mol. Biol.,Journal of molecular biology,426,3,,,,,,,,,,,,,,,,,,,,,,763,774,2014, citations,citation_1,19591,108479,1,,entry citation,,,24211467,,,Visualizing side chains of invisible protein conformers by solution NMR.,published,journal,J. Mol. Biol.,Journal of molecular biology,426,3,,,,,,,,,,,,,,,,,,,,,,763,774,2014, citations,entry_citation,19592,108494,1,,entry citation,,,24711371,,,Solution structure of a 2:1 complex of anticancer drug XR5944 with TFF1 estrogen response element: insights into DNA recognition by a bis-intercalator.,published,journal,Nucleic Acids Res.,Nucleic acids research,42,9,,,,,,,,,,,,,,,,,,,,,,6012,6024,2014, citations,entry_citation,19593,108513,1,,entry citation,,,24440079,,,Design and synthesis of truncated EGF-A peptides that restore LDL-R recycling in the presence of PCSK9 in vitro.,published,journal,Chem. Biol.,Chemistry & biology,21,2,,,,,,,,,,,,,,,,,,,,,,284,294,2014, citations,entry_citation,19594,108535,1,,entry citation,,,24356977,,,Solution Structure of a G-quadruplex Bound to the Bisquinolinium Compound Phen-DC3.,published,journal,Angew. Chem. Int. Ed. Engl.,Angewandte Chemie (International ed. in English),53,4,,,,,,,,,,,,,,,,,,,,,,999,1002,2014, citations,entry_citation,19595,108558,1,,entry citation,,,24248349,,,Oxytocic plant cyclotides as templates for peptide G protein-coupled receptor ligand design.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,110,52,,,,,,,,,,,,,,,,,,,,,,21183,21188,2013, citations,entry_citation,19596,108577,1,,entry citation,,,24333248,,,Generating NMR chemical shift assignments of intrinsically disordered proteins using carbon-detected NMR methods.,published,journal,Anal. Biochem.,Analytical biochemistry,449C,,,,,,,,,,,,,,,,,,,,,,,17,25,2013, citations,entry_citation,19597,108593,1,,entry citation,,,24947608,,,"Solution structures and model membrane interactions of Ctriporin, an anti-methicillin-resistant Staphylococcus aureus Peptide from Scorpion Venom",published,journal,Biopolymers,Biopolymers,101,12,,,,,,,,,,,,,,,,,,,,,,1143,1153,2014, citations,entry_1,19598,108608,1,,entry citation,,,24378977,,,"(1)H, (13)C and (15)N resonance assignment of WHEP domains of human glutamyl-prolyl tRNA synthetase.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,19599,108622,1,,entry citation,,,24378977,,,"(1)H, (13)C and (15)N resonance assignment of WHEP domains of human glutamyl-prolyl tRNA synthetase.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,196,108636,1,,entry citation,,,,,"Kraulis, Per J., Clore, G. Marius, Nilges, Michael, Jones, Alwyn, Petterson, Goran, Knowles, Jonathan, Gronenborn, Angela M., ""Determination of the Three-Dimensional Solution Structure of the C-Terminal Domain of CellobiohydrolOCe I from Trichodermi reesi. A Study using NMR and Hybrid distance Geometry-Dynamical Simulated Annealing.,"" Biochemistry 28, 7241-7257 (1989).","Determination of the Three-Dimensional Solution Structure of the C-Terminal Domain of CellobiohydrolOCe I from Trichodermi reesi. A Study using NMR and Hybrid distance Geometry-Dynamical Simulated Annealing.",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,7241,7257,1989, citations,citations,19600,108649,1,,entry citation,,,24361878,,,Solution structure of CEH-37 homeodomain of the nematode Caenorhabditis elegans.,published,journal,Biochem. Biophys. Res. Commun.,Biochemical and biophysical research communications,443,2,,,,,,,,,,,,,,,,,,,,,,370,375,2014, citations,entry_citation,19601,108664,1,,entry citation,,,24695525,,,Solution Structure of CXCL5 - A Novel Chemokine and Adipokine Implicated in Inflammation and Obesity.,published,journal,PLoS ONE,PloS one,9,4,,,,,,,,,,,,,,,,,,,,,,e93228,e93228,2014, citations,entry_citation,19602,108682,1,,entry citation,,,21290829,,,Optimization of the methods for small peptide solution structure determination by NMR spectroscopy,published,journal,Mol. Biol. 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Chem.,The Journal of biological chemistry,289,12,,,,,,,,,,,,,,,,,,,,,,8697,8705,2014, citations,PonA2-Pasta_citation,19605,108749,1,,entry citation,,,24281824,,,"Structural and binding properties of the PASTA domain of PonA2, a key penicillin binding protein from Mycobacterium tuberculosis.",published,journal,Biopolymers,Biopolymers,101,7,,,,,,,,,,,,,,,,,,,,,,712,719,2014, citations,entry_citation,19606,108771,1,,entry citation,,,24692539,,,Solution Structure of the Ubiquitin-associated (UBA) Domain of Human Autophagy Receptor NBR1 and its Interaction with Ubiquitin and Polyubiquitin.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,19607,108791,1,,entry citation,,,24486611,,,The C-Terminal Domain of SRA1p Has a Fold More Similar to PRP18 than to an RRM and Does Not Directly Bind to the SRA1 RNA STR7 Region.,published,journal,J. Mol. Biol.,Journal of molecular biology,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,19608,108808,1,,entry citation,,,24653034,,,Structure of the mitochondrial translocator protein in complex with a diagnostic ligand,published,journal,Science,,343,6177,,,,,,,,,,,,,,,,,,,,,,1363,1366,2014, citations,entry_citation,19609,108835,1,,entry citation,,,,,,Solution Structure of Protein-RNA Ternary Complex,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19610,108854,1,,entry citation,,,,,,Solution NMR structure of the p300 Taz2:ETAD1 complex,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19611,108876,1,,entry citation,,,24425873,,,Semienzymatic cyclization of disulfide-rich peptides using Sortase A.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,289,10,,,,,,,,,,,,,,,,,,,,,,6627,6638,2014, citations,citation_1,19613,108896,1,,entry citation,,,24711446,,,Solution Structure and DNA-binding Properties of the Winged Helix Domain of the Meiotic Recombination HOP2 Protein.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,19614,108916,1,,entry citation,,,24403087,,,The basic helix-loop-helix region of the transcriptional repressor hairy and enhancer of split 1 is preorganized to bind DNA.,published,journal,Proteins,Proteins,82,4,,,,,,,,,,,,,,,,,,,,,,537,545,2014, citations,entry_citation,19615,108936,1,,entry citation,,,24484052,,,Ligand-dependent dynamics of the active-site lid in bacterial dimethylarginine dimethylaminohydrolase.,published,journal,Biochemistry,Biochemistry,53,6,,,,,,,,,,,,,,,,,,,,,,1092,1104,2014, citations,Journal,19616,108956,1,,entry citation,,,24484052,,,Ligand-dependent dynamics of the active-site lid in bacterial dimethylarginine dimethylaminohydrolase.,published,journal,Biochemistry,Biochemistry,53,6,,,,,,,,,,,,,,,,,,,,,,1092,1104,2014, citations,citation_1,19617,108971,1,,entry citation,,,,,,Solution structure of the Big domain from Leptospira interrogans,submitted,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19618,108986,1,,entry citation,,,24699374,,,Solution structure of the TatB component of the twin-arginine translocation system.,published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1838,7,,,,,,,,,,,,,,,,,,,,,,1881,1888,2014, citations,entry_citation,19619,109003,1,,entry citation,,,24627484,,,The Lantibiotic NAI-107 Binds to Bactoprenol-bound Cell Wall Precursors and Impairs Membrane Functions.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,289,17,,,,,,,,,,,,,,,,,,,,,,12063,12076,2014, citations,entry_citation,19620,109029,1,,entry citation,,,24931822,10.1002/cmdc.201402121,,"NMR Structure of an Ethylene Interstrand Cross-Linked DNA which Mimics the Lesion Formed by 1,3-Bis(2-chloroethyl)-1-nitrosourea.",published,journal,ChemMedChem,ChemMedChem,9,9,,1860-7187,,,,,,,,,,,,,,,,,,,,2099,2103,2014, citations,entry_citation,19621,109051,1,,entry citation,,,24414223,,,"(1)H, (13)C and (15)N chemical shift assignments for the cyclic-nucleotide binding homology domain of a KCNH channel.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,19622,109073,1,,entry citation,,,,,,Redirecting Elctrons from Photosystem I to Hydrogenase: Towards Increased Hydrogen Production in Algae,in preparation,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19623,109094,1,,entry citation,,,25564862,,,Subdomain interactions foster the design of two protein pairs with ~80% sequence identity but different folds,published,journal,Biophys J.,,108,2,,,,,,,,,,,,,,,,,,,,,,154,162,2015, citations,entry_citation,19624,109115,1,,entry citation,,,,,,1H and 15N chemical shift assignments for circular sortase A,submitted,journal,to be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,19625,109131,1,,entry citation,,,,,,Solution Structure and DNA Binding of the Catalytic of the Large Serine Resolvase Tnpx,in preparation,journal,To be Published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19626,109149,1,,entry citation,,,25170085,10.1093/nar/gku612,,"Protein Hit1, a novel box C/D snoRNP assembly factor, controls cellular concentration of the scaffolding protein Rsa1 by direct interaction.",published,journal,Nucleic Acids Res.,Nucleic acids research,42,16,,1362-4962,,,,,,,,,,,,,,,,,,,,10731,10747,2014, citations,entry_citation,19627,109166,1,,entry citation,,,,,,NMR strucutre of the hypothetical protein BACUNI_03114 from Bacteroides uniformis ATCC 8492,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19628,109185,1,,entry citation,,,,,,NMR structure of the protein NP_419126.1 from CAULOBACTER CRESCENTUS,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19629,109203,1,,entry citation,,,23749453,,,"(1)H, (15)N, and (13)C chemical shift assignments of cyanobacteriochrome NpF2164g3 in the photoproduct state.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,entry_citation,19632,109221,1,,entry citation,,,,,,NMR structure of protein NP_254181.1 from Pseudomonas aeruginosa PA01,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19633,109240,1,,entry citation,,,24558196,,,The number and location of EF hand motifs dictates the calcium dependence of polycystin-2 function.,published,journal,FASEB J.,FASEB journal : official publication of the Federation of American Societies for Experimental Biology,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,medaka_CR4-5_telomerase_RNA-citation,19634,109259,1,,entry citation,,,24335084,,,Structure and sequence elements of the CR4/5 domain of medaka telomerase RNA important for telomerase function.,published,journal,Nucleic Acids Res.,Nucleic acids research,42,5,,,,,,,,,,,,,,,,,,,,,,3395,3408,2014, citations,entry_citation,19635,109288,1,,entry citation,,,,,,Structure-function analysis reveals a dual role of the Pseudomonas aeruginosa Tps4 two-partner secretion system,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,19637,109306,1,,entry citation,,,25017731,10.1016/j.str.2014.05.016,,NMR polypeptide backbone conformation of the E. coli outer membrane protein W.,published,journal,Structure,"Structure (London, England : 1993)",22,8,,1878-4186,,,,,,,,,,,,,,,,,,,,1204,1209,2014, citations,citations,19638,109322,1,,entry citation,,,25210769,,,Structural Basis for Cytochrome c Y67H Mutant to Function as a Peroxidase,published,journal,Plos One,,9,9,,,,,,,,,,,,,,,,,,,,,,e107305,e107305,2014, citations,1,19641,109340,1,,entry citation,,,24816896,,,"(1)H, (15)N and (13)C resonance assignments for 3rC and 3rCWP: amyloidogenic variants of imunoglobulin lambda 3 light-chain",published,journal,Biomol NMR Assign.,,9,1,,,,,,,,,,,,,,,,,,,,,,139,142,2015, citations,entry_citation,19642,109356,1,,entry citation,,,,,,NMR structure of the first RRM domain of the protein RBM39 from homo sapiens,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19643,109373,1,,entry citation,,,,,,"Interactions of the 5-Hydroxytryptamine Receptor 2a and 2c Variants with the PSD-MAGUK proteins, PSD-95 and SAP997",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19644,109394,1,,entry citation,,,23667548,,,Highly efficient NMR assignment of intrinsically disordered proteins: application to B- and T cell receptor domains.,published,journal,PLoS ONE,PloS one,8,5,,,,,,,,,,,,,,,,,,,,,,e62947,e62947,2013, citations,entry_citation,19645,109415,1,,entry citation,,,23667548,,,Highly efficient NMR assignment of intrinsically disordered proteins: application to B- and T cell receptor domains.,published,journal,PLoS ONE,PloS one,8,5,,,,,,,,,,,,,,,,,,,,,,e62947,e62947,2013, citations,entry_citation,19646,109436,1,,entry citation,,,24700780,,,Solution structure of the major factor VIII binding region on von Willebrand factor.,published,journal,Blood,Blood,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,19648,109463,1,,entry citation,,,23667548,,,Highly efficient NMR assignment of intrinsically disordered proteins: application to B- and T cell receptor domains.,published,journal,PLoS ONE,PloS one,8,5,,,,,,,,,,,,,,,,,,,,,,e62947,e62947,2013, citations,entry_citation,19649,109482,1,,entry citation,,,23667548,,,Highly efficient NMR assignment of intrinsically disordered proteins: application to B- and T cell receptor domains.,published,journal,PLoS ONE,PloS one,8,5,,,,,,,,,,,,,,,,,,,,,,e62947,e62947,2013, citations,entry_citation,19650,109501,1,,entry citation,,,23667548,,,Highly efficient NMR assignment of intrinsically disordered proteins: application to B- and T cell receptor domains.,published,journal,PLoS ONE,PloS one,8,5,,,,,,,,,,,,,,,,,,,,,,e62947,e62947,2013, citations,entry_citation,19651,109520,1,,entry citation,,,23667548,,,Highly efficient NMR assignment of intrinsically disordered proteins: application to B- and T cell receptor domains.,published,journal,PLoS ONE,PloS one,8,5,,,,,,,,,,,,,,,,,,,,,,e62947,e62947,2013, citations,entry_citation,19653,109539,1,,entry citation,,,23334698,,,Protein chemical shift assignments of the unbound and RNA-bound forms of the alternative splicing factor SUP-12 from C. elegans.,published,journal,Biomol. 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Commun.,,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,19654,109562,1,,entry citation,,,24789074,,,High-quality NMR Structure of Human Anti-apoptotic Protein Domain Mcl-1(171-327) for Cancer Drug Design,published,journal,PLOS,,9,5,,,,,,,,,,,,,,,,,,,,,,e96521,e96521,2014, citations,entry_citation,19655,109586,1,,entry citation,,,23667548,,,Highly efficient NMR assignment of intrinsically disordered proteins: application to B- and T cell receptor domains.,published,journal,PLoS ONE,PloS one,8,5,,,,,,,,,,,,,,,,,,,,,,e62947,e62947,2013, citations,entry_citation,19656,109605,1,,entry citation,,,23667548,,,Highly efficient NMR assignment of intrinsically disordered proteins: application to B- and T cell receptor domains.,published,journal,PLoS ONE,PloS one,8,5,,,,,,,,,,,,,,,,,,,,,,e62947,e62947,2013, citations,entry_citation,19657,109624,1,,entry citation,,,,,,NMR Analysis of Constrained Cold and Heat Unfolding of the Antifungal Disulfide Protein PAF: 15N-CEST Reveals Hidden Conformers,in preparation,journal,J. 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NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19692,110236,1,,entry citation,,,24364590,,,NMR Localization of Divalent Cations at the Active Site of the Neurospora VS Ribozyme Provides Insights into RNA-Metal-Ion Interactions.,published,journal,Biochemistry,Biochemistry,53,3,,,,,,,,,,,,,,,,,,,,,,579,590,2014, citations,entry_citation,19693,110262,1,,entry citation,,,25181039,,,Discovery and Characterization of a Disulfide-Locked C2-Symmetric Defensin Peptide,published,journal,J. Am. Chem. Soc.,,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,19694,110282,1,,entry citation,,,,,,Structure of FHL2 LIM adaptor and its Interaction with Ski,submitted,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19695,110303,1,,entry citation,,,24617538,,,"Nuclear Magnetic Resonance Studies of an N(2)-Guanine Adduct Derived from the Tumorigen Dibenzo[a,l]pyrene in DNA: Impact of Adduct Stereochemistry, Size, and Local DNA Sequence on Solution Conformations",published,journal,Biochemistry,,53,11,,,,,,,,,,,,,,,,,,,,,,1827,1841,2014, citations,entry_citation,19696,110323,1,,entry citation,,,24617538,,,"Nuclear Magnetic Resonance Studies of an N(2)-Guanine Adduct Derived from the Tumorigen Dibenzo[a,l]pyrene in DNA: Impact of Adduct Stereochemistry, Size, and Local DNA Sequence on Solution Conformations",published,journal,Biochemistry,,53,11,,,,,,,,,,,,,,,,,,,,,,1827,1841,2014, citations,entry_citation,19697,110343,1,,entry citation,,,24713808,,,Sample Limited Characterization of a Novel Disulfide-Rich Venom Peptide Toxin from Terebrid Marine Snail Terebra variegata.,published,journal,PLoS ONE,PloS one,9,4,,,,,,,,,,,,,,,,,,,,,,e94122,e94122,2014, citations,entry_citation,19698,110361,1,,entry citation,,,24469808,,,Structural determinants for ligand capture by a class II preQ1 riboswitch.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,111,6,,,,,,,,,,,,,,,,,,,,,,E663,E671,2014, citations,entry_citation,19699,110392,1,,entry citation,,,,,,The murine Cytomegalovirus gp34/m04 protein contains a core domain with novel structure revealed by solution NMR,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,19700,110418,1,,entry citation,,,,,,"Interaction of Weak Toxin from Naja kaouthia with Muscarinic Acetylcholine Receptors: Mutagenesis, NMR and Modeling Study",in preparation,journal,To be Published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19701,110433,1,,entry citation,,,25284368,,,NMR structure of the water soluble Abeta17-34 peptide,published,journal,Biosci. 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Virol.,Journal of virology,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,citation_3,19702,110448,2,,entry citation,,,21920573,,,Human polyomavirus JC small regulatory agnoprotein forms highly stable dimers and oligomers: implications for their roles in agnoprotein function.,published,journal,Virology,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,19702,110449,3,,entry citation,,,,,,"Nuclear magnetic resonance structure revealed that human polyoma, JC virus agnoprotein contains an alpha-helix encompassing the Leu/Ile/Phe-rich domain",in preparation,journal,J Virol.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19703,110468,1,,entry citation,,,,,,"Backbone 1H, 13C, and 15N Chemical Shift Assignments and structure of Iron-sulfur cluster binding protein from Ehrlichia chaffeensis",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,19704,110487,1,,entry citation,,,,,,An NMR-based approach for validation of protein side-chains dynamics in silico,in preparation,journal,To be Published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19707,110530,1,,entry citation,,,25203403,10.1371/journal.pone.0107168,,"Mechanism of the pH-Induced Conformational Change in the Sensor Domain of the DraK Histidine Kinase via the E83, E105, and E107 Residues",published,journal,PLoS One,,9,9,,,,,,,,,,,,,,,,,,,,,,e107168,e107168,2014, citations,citations_1,19708,110544,1,,entry citation,,,24606221,,,Purification and Structural Study of the Voltage-Sensor Domain of the Human KCNQ1 Potassium Ion Channel.,published,journal,Biochemistry,Biochemistry,53,12,,,,,,,,,,,,,,,,,,,,,,2032,2042,2014, citations,citations,19709,110561,1,,entry citation,,,,,,"Solution NMR structure of beta-adaptin appendage domain of human adaptor protein complex 4 subunit beta, Northeast Structural Genomics Consortium (NESG) Target HR8998C",in preparation,journal,To be published,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19710,110599,1,,entry citation,,,,,,Solution structure of CDYL2 chromodomain,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19711,110619,1,,entry citation,,,24751877,,,A streamlined method for preparing split intein for NMR study.,published,journal,Protein Expr. Purif.,Protein expression and purification,99,,,,,,,,,,,,,,,,,,,,,,,106,112,2014, citations,citations,19712,110638,1,,entry citation,,,24828921,,,Rational Design of -Helix-Stabilized Exendin-4 Analogues.,published,journal,Biochemistry,Biochemistry,53,22,,,,,,,,,,,,,,,,,,,,,,3540,3552,2014, citations,citations,19713,110652,1,,entry citation,,,25162988,,,Micelle-Catalyzed Domain Swapping in the GlpG Rhomboid Protease Cytoplasmic Domain,published,journal,Biochemistry,,53,37,,,,,,,,,,,,,,,,,,,,,,5907,5915,2014, citations,entry_citation,19714,110667,1,,entry citation,,,25090434,,,Structural basis for TatA oligomerization: an NMR study of Escherichia coli TatA dimeric structure,published,journal,Plos One,,9,8,,,,,,,,,,,,,,,,,,,,,,e103157,e103157,2014, citations,citation_1,19715,110688,1,,entry citation,,,24696326,,,"(13)C, (15)N and (1)H resonance assignments of receiver domain of ethylene receptor ETR1.",published,journal,Biomol. NMR Assignments,Biomolecular NMR assignments,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,19716,110705,1,,entry citation,,,,,,"Solution NMR structure of the Zn-binding domain of eukaryotic translation initiation factor 3, subunit G",in preparation,journal,Proteins: Struct. Funct. Genet.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation_1,19717,110724,1,,entry citation,,,25358379,,,Functional reconstitution of mitochondrial Fe/S cluster synthesis on Isu1 reveals the involvement of ferredoxin,published,journal,Nat. Commun.,,5,,,,,,,,,,,,,,,,,,,,,,,5013,5013,2014, citations,entry_citation_1,19718,110746,1,,entry citation,,,25358379,,,Functional reconstitution of mitochondrial Fe/S cluster synthesis on Isu1 reveals the involvement of ferredoxin,published,journal,Nat. Commun.,,5,,,,,,,,,,,,,,,,,,,,,,,5013,5013,2014, citations,entry_citation,19719,110768,1,,entry citation,,,24983468,10.1096/fj.14-256057,,A Plasmodium falciparum PHIST protein binds the virulence factor PfEMP1 and comigrates to knobs on the host cell surface,published,journal,FASEB J.,FASEB journal,28,10,,0892-6638,,,,,,,,,,,,,,,,,,,,4420,4433,2014, citations,entry_citation,19720,110784,1,,entry citation,,,24625274,,,Replacing the Axial Ligand Tyrosine 75 or Its Hydrogen Bond Partner Histidine 83 Minimally Affects Hemin Acquisition by the Hemophore HasAp from Pseudomonas aeruginosa.,published,journal,Biochemistry,Biochemistry,53,13,,,,,,,,,,,,,,,,,,,,,,2112,2125,2014, citations,entry_citation,19721,110799,1,,entry citation,,,24625274,,,Replacing the Axial Ligand Tyrosine 75 or Its Hydrogen Bond Partner Histidine 83 Minimally Affects Hemin Acquisition by the Hemophore HasAp from Pseudomonas aeruginosa.,published,journal,Biochemistry,Biochemistry,53,13,,,,,,,,,,,,,,,,,,,,,,2112,2125,2014, citations,entry_citation,19722,110814,1,,entry citation,,,24625274,,,Replacing the Axial Ligand Tyrosine 75 or Its Hydrogen Bond Partner Histidine 83 Minimally Affects Hemin Acquisition by the Hemophore HasAp from Pseudomonas aeruginosa.,published,journal,Biochemistry,Biochemistry,53,13,,,,,,,,,,,,,,,,,,,,,,2112,2125,2014, citations,citation_2,19723,110829,1,,entry citation,,,,,,A heterodimeric construct mimicking the cytoplasmic region of the B-cell antigen receptor complex-associated protein,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,19723,110830,2,,reference citation,,,10623552,,,A heterodimeric coiled-coil peptide pair selected in vivo from a designed library-versus-library ensemble,published,journal,J. 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Biol.,,295,3,,,,,,,,,,,,,,,,,,,,,,627,639,2000, citations,citation_3,19724,110851,3,,reference citation,,,11545598,,,"Helix-stabilized Fv (hsFv) Antibody Fragments: Substituting the Constant Domains of a Fab Fragment for a Heterodimeric Coiled-coil Domain",published,journal,J. Mol. Biol.,,312,1,,,,,,,,,,,,,,,,,,,,,,221,228,2001, citations,citation_2,19725,110871,1,,entry citation,,,,,,A heterodimeric construct mimicking the cytoplasmic region of the B-cell antigen receptor complex-associated protein,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,19725,110872,2,,reference citation,,,10623552,,,A heterodimeric coiled-coil peptide pair selected in vivo from a designed library-versus-library ensemble,published,journal,J. Mol. 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Commun.,,5,,,,,,,,,,,,,,,,,,,,,,,5831,5831,2014, citations,citations,19729,110964,1,,entry citation,,,24443564,,,3D NMR structure of hen egg gallin (chicken ovo-defensin) reveals a new variation of the beta-defensin fold.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,19730,110981,1,,entry citation,,,24700611,,,Structural Mapping of a Chaperone-Substrate Interaction Surface.,published,journal,Angew. Chem. Int. Ed. Engl.,Angewandte Chemie (International ed. in English),,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,19731,110998,1,,entry citation,,,,,,Solution structure of peptidyl-tRNA hydrolase from Vibrio cholerae,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19732,111018,1,,entry citation,,,,10.1021/bi500177x,,The solution NMR structure of the NLRC5 caspase recruitment domain (CARD) reveals unusual structural features,published,journal,Biochemistry,,53,,,,,,,,,,,,,,,,,,,,,,,3106,3117,, citations,entry_citation,19733,111037,1,,entry citation,,,24700611,,,Structural Mapping of a Chaperone-Substrate Interaction Surface.,published,journal,Angew. Chem. Int. Ed. Engl.,Angewandte Chemie (International ed. in English),,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,19734,111053,1,,entry citation,,,24447194,,,Complete chemical shift assignment of the ssDNA in the filamentous bacteriophage fd reports on its conformation and on its interface with the capsid shell.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,136,6,,,,,,,,,,,,,,,,,,,,,,2292,2301,2014, citations,entry_citation,19735,111070,1,,entry citation,,,24682828,,,"Structure, dynamics and RNA binding of the multi-domain splicing factor TIA-1.",published,journal,Nucleic Acids Res.,Nucleic acids research,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,1C-Grx-1,19736,111094,1,,entry citation,,,24830542,,,"1H, 13C and 15N resonance assignment of the mature form of monothiol glutaredoxin 1 from the pathogen Trypanosoma brucei",published,journal,Biomol. 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Commun.,Biochemical and biophysical research communications,451,3,,1090-2104,,,,,,,,,,,,,,,,,,,,402,407,2014, citations,1,19917,114014,1,,entry citation,,,,,,Characterization of 5-hydroxycytosine in DNA,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,hIFABP_oleate_complex,19921,114031,1,,entry citation,,,,,,Structure of oleate bound human intestinal fatty acid binding protein,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,19922,114052,1,,entry citation,,,,,,"Backbone 1H, 13C, and 15N Chemical Shift Assignments of human TDP-43 RRM2",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19923,114067,1,,entry citation,,,24814369,,,Interactions of disulfide-deficient selenocysteine analogs of mu-conotoxin BuIIIB with the alpha-subunit of the voltage-gated sodium channel subtype 1.3,published,journal,FEBS J,The FEBS journal,281,13,,1742-4658,,,,,,,,,,,,,,,,,,,,2885,2898,2014, citations,entry_citation,19925,114082,1,,entry citation,,,,,,Characterization of 5-hydroxycytosine in DNA,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19926,114098,1,,entry citation,,,25006247,,,Identification of multifaceted binding modes for pyrin and ASC pyrin domains gives insights into pyrin inflammasome assembly,published,journal,J. 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Struct. Mol. Biol.,Nature structural & molecular biology,21,8,,1545-9985,,,,,,,,,,,,,,,,,,,,704,711,2014, citations,entry_citation,19931,114185,1,,entry citation,,,,,,Structural Characterization of the DC-SIGN-LewisX Complex,in preparation,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19932,114202,1,,entry citation,,,,,,Synthetic di-thiol containing amino acids for structurally shaping polypeptides and enhancing target-ligand binding interactions,submitted,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19933,114222,1,,entry citation,,,,,,Membrane induced structure of novel human tachykinin Hemokinin-1,in preparation,journal,Biopolymers,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19934,114237,1,,entry citation,,,25038803,10.1038/nsmb.2861,,Allosteric enhancement of MAP kinase p38a's activity and substrate selectivity by docking interactions.,published,journal,Nat. Struct. Mol. Biol.,Nature structural & molecular biology,21,8,,1545-9985,,,,,,,,,,,,,,,,,,,,704,711,2014, citations,entry_citation,19935,114257,1,,entry citation,,,25038803,10.1038/nsmb.2861,,Allosteric enhancement of MAP kinase p38a's activity and substrate selectivity by docking interactions.,published,journal,Nat. Struct. Mol. Biol.,Nature structural & molecular biology,21,8,,1545-9985,,,,,,,,,,,,,,,,,,,,704,711,2014, citations,entry_citation,19936,114279,1,,entry citation,,,25038803,10.1038/nsmb.2861,,Allosteric enhancement of MAP kinase p38a's activity and substrate selectivity by docking interactions.,published,journal,Nat. Struct. Mol. Biol.,Nature structural & molecular biology,21,8,,1545-9985,,,,,,,,,,,,,,,,,,,,704,711,2014, citations,entry_citation,19937,114300,1,,entry citation,,,25038803,10.1038/nsmb.2861,,Allosteric enhancement of MAP kinase p38a's activity and substrate selectivity by docking interactions.,published,journal,Nat. Struct. Mol. Biol.,Nature structural & molecular biology,21,8,,1545-9985,,,,,,,,,,,,,,,,,,,,704,711,2014, citations,entry_citation,19938,114323,1,,entry citation,,,,,,Solution structure of the Ehrlichia chaffeensis thioredoxin ECH_0218 in the reduced and oxidized states: disorder around the CXXC active site,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19939,114344,1,,entry citation,,,25183517,,,Solution structure and intramolecular exchange of methyl-cytosine binding domain protein 4 (MBD4) on DNA suggests a mechanism to scan for mCpG/TpG mismatches,published,journal,Nucleic Acids Res.,,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,19940,114366,1,,entry citation,,,,,,Structure of outer membrane protein A transmembrane domain by NMR spectroscopy,published,journal,Nat. Struct. 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Chem.,The Journal of biological chemistry,289,34,,1083-351X,,,,,,,,,,,,,,,,,,,,23482,23503,2014, citations,holo_FldA,19945,114433,1,,entry citation,,,,,,NMR study of YqcA from Escherichia coli,in preparation,journal,Biochem. J.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19946,114452,1,,entry citation,,,24958726,10.1074/jbc.M114.571935,,Solution NMR Structure and Functional Analysis of the Integral Membrane Protein YgaP from Escherichia coli.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,289,34,,1083-351X,,,,,,,,,,,,,,,,,,,,23482,23503,2014, citations,entry_citation,19947,114468,1,,entry citation,,,25363287,,,"NMR structure of bitistatin, a missing piece in the evolutionary pathway of snake venom disintegrins",published,journal,FEBS J.,,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,19948,114486,1,,entry citation,,,25343306,,,The proline-rich region of 18.5 kDa myelin basic protein binds to the SH3-domain of Fyn tyrosine kinase with the aid of an upstream segment to form a dynamic complex in vitro,published,journal,Biosci. Rep.,Bioscience reports,34,6,,1573-4935,,,,,,,,,,,,,,,,,,,,e00157,e00157,2014, citations,entry_citation,19949,114505,1,,entry citation,,,25343306,,,The proline-rich region of 18.5 kDa myelin basic protein binds to the SH3-domain of Fyn tyrosine kinase with the aid of an upstream segment to form a dynamic complex in vitro,published,journal,Biosci. 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Cell,,55,3,,,,,,,,,,,,,,,,,,,,,,467,481,2014, citations,entry_citation,19955,114619,1,,entry citation,,,,,,Structural Investigation of the Interaction between the Tandem SH3 Domains of c-Cbl-Associated Protein and Vinculin,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,19957,114639,1,,entry citation,,,25212183,,,Chemical shifts assignments of the archaeal MC1 protein and a strongly bent 15 base pairs DNA duplex in complex,published,journal,Biomol. NMR Assignments,,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,19958,114661,1,,entry citation,,97207064,,,,Protein Phosphorylation upon a Fleeting Encounter,published,journal,Nature,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_one,19958,114662,2,,reference citation,,,,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. 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Mark P., Edwards, Robert G., Smith, Richard A.G., Dobson, Christopher M., ""Secondary Structure and Topology of Human Interleukin 4 in Solution,"" Biochemistry 30 (46), 11029-11035 (1991).",Secondary Structure and Topology of Human Interleukin 4 in Solution,published,journal,Biochemistry,,30,46,,,,,,,,,,,,,,,,,,,,,,11029,11035,1991, citations,entry_citation,2038,117738,1,,entry citation,,,,,"de Ropp, Jeffrey S., La Mar, Gerd N., Wariishi, Hiroyuki, Gold, Michael H., ""NMR Study of the Active Site of Resting State and Cyanide-inhibited Lignin Peroxidase from Phanerochaete chrysosporium (Comparison with horseradish peroxidase),"" J. Biol. Chem. 266 (23), 15001-15008 (1991).","NMR Study of the Active Site of Resting State and Cyanide-inhibited Lignin Peroxidase from Phanerochaete chrysosporium (Comparison with horseradish peroxidase)",published,journal,J. Biol. Chem.,,266,23,,,,,,,,,,,,,,,,,,,,,,15001,15008,1991, citations,entry_citation,2039,117751,1,,entry citation,,,,,"Folkers, P.J.M., van Duynhoven, John P.M., Jonker, Aafke J., Harmsen, B.J.M., Konings, R.N.H., Hilbers, C. W., ""Sequence-specific 1H-NMR assignment and secondary structure of the Tyr41->His mutant of the single-stranded DNA binding protein, gene V protein, encoded by the filamentous bacteriophage M13,"" Eur. J. Biochem. 202, 349-360 (1991).","Sequence-specific 1H-NMR assignment and secondary structure of the Tyr41->His mutant of the single-stranded DNA binding protein, gene V protein, encoded by the filamentous bacteriophage M13",published,journal,Eur. J. Biochem.,,202,,,,,,,,,,,,,,,,,,,,,,,349,360,1991, citations,entry_citation,2040,117764,1,,entry citation,,,,,"Borden, Katherine L. B., Beckmann, Pamela, Lane, Andrew, ""Determination of the orientations of tryptophan analogues bound to the trp repressor and the relationship to activation,"" Eur. J. Biochem. 202, 459-470 (1991).","Determination of the orientations of tryptophan analogues bound to the trp repressor and the relationship to activation",published,journal,Eur. J. Biochem.,,202,,,,,,,,,,,,,,,,,,,,,,,459,470,1991, citations,entry_citation,2042,117777,1,,entry citation,,,,,"Borden, Katherine L. B., Beckmann, Pamela, Lane, Andrew, ""Determination of the orientations of tryptophan analogues bound to the trp repressor and the relationship to activation,"" Eur. J. Biochem. 202, 459-470 (1991).","Determination of the orientations of tryptophan analogues bound to the trp repressor and the relationship to activation",published,journal,Eur. J. Biochem.,,202,,,,,,,,,,,,,,,,,,,,,,,459,470,1991, citations,entry_citation,2043,117790,1,,entry citation,,,,,"Borden, Katherine L. B., Beckmann, Pamela, Lane, Andrew, ""Determination of the orientations of tryptophan analogues bound to the trp repressor and the relationship to activation,"" Eur. J. Biochem. 202, 459-470 (1991).","Determination of the orientations of tryptophan analogues bound to the trp repressor and the relationship to activation",published,journal,Eur. J. Biochem.,,202,,,,,,,,,,,,,,,,,,,,,,,459,470,1991, citations,entry_citation,2047,117803,1,,entry citation,,,,,"Motta, Andrea, Pastore, Annalisa, Goud, Nagana, Castiglione Morelli, Maria Antoinetta, ""Solution Conformation of Salmon Calcitonin in Sodium Dodecyl Sulfate Micelles As Determined by Two-Dimensional NMR and Distance Geometry Calculations,"" Biochemistry 30 (43), 10444-10450 (1991).","Solution Conformation of Salmon Calcitonin in Sodium Dodecyl Sulfate Micelles As Determined by Two-Dimensional NMR and Distance Geometry Calculations",published,journal,Biochemistry,,30,43,,,,,,,,,,,,,,,,,,,,,,10444,10450,1991, citations,entry_citation,2048,117817,1,,entry citation,,,,,"Motta, Andrea, Pastore, Annalisa, Goud, Nagana, Castiglione Morelli, Maria Antoinetta, ""Solution Conformation of Salmon Calcitonin in Sodium Dodecyl Sulfate Micelles As Determined by Two-Dimensional NMR and Distance Geometry Calculations,"" Biochemistry 30 (43), 10444-10450 (1991).","Solution Conformation of Salmon Calcitonin in Sodium Dodecyl Sulfate Micelles As Determined by Two-Dimensional NMR and Distance Geometry Calculations",published,journal,Biochemistry,,30,43,,,,,,,,,,,,,,,,,,,,,,10444,10450,1991, citations,entry_citation,2049,117831,1,,entry citation,,,,,"Andersen, Kim V., Ludvigsen, Svend, Mandrup, Susanne, Knudsen, Jens, Poulsen, Flemming M., ""The Secondary Structure in Solution of Acyl-Coenzyme A Binding Protein from Bovine Liver Using 1H Nuclear Magnetic Resonance Spectroscopy,"" Biochemistry 30 (44), 10654-10663 (1991).","The Secondary Structure in Solution of Acyl-Coenzyme A Binding Protein from Bovine Liver Using 1H Nuclear Magnetic Resonance Spectroscopy",published,journal,Biochemistry,,30,44,,,,,,,,,,,,,,,,,,,,,,10654,10663,1991, citations,entry_citation,2050,117844,1,,entry citation,,,,,"Andersen, Kim V., Ludvigsen, Svend, Mandrup, Susanne, Knudsen, Jens, Poulsen, Flemming M., ""The Secondary Structure in Solution of Acyl-Coenzyme A Binding Protein from Bovine Liver Using 1H Nuclear Magnetic Resonance Spectroscopy,"" Biochemistry 30 (44), 10654-10663 (1991).","The Secondary Structure in Solution of Acyl-Coenzyme A Binding Protein from Bovine Liver Using 1H Nuclear Magnetic Resonance Spectroscopy",published,journal,Biochemistry,,30,44,,,,,,,,,,,,,,,,,,,,,,10654,10663,1991, citations,entry_citation,2051,117857,1,,entry citation,,,,,"Gardner, Kevin H., Pan, Tao, Narula, Surinder S., Rivera, Edwin, Coleman, Joseph E., ""Structure of the Binuclear Metal-Binding Site in the GAL4 Transcription Factor,"" Biochemistry 30 (47), 11292-11302 (1991).",Structure of the Binuclear Metal-Binding Site in the GAL4 Transcription Factor,published,journal,Biochemistry,,30,47,,,,,,,,,,,,,,,,,,,,,,11292,11302,1991, citations,entry_citation,2052,117870,1,,entry citation,,,,,"Gardner, Kevin H., Pan, Tao, Narula, Surinder S., Rivera, Edwin, Coleman, Joseph E., ""Structure of the Binuclear Metal-Binding Site in the GAL4 Transcription Factor,"" Biochemistry 30 (47), 11292-11302 (1991).",Structure of the Binuclear Metal-Binding Site in the GAL4 Transcription Factor,published,journal,Biochemistry,,30,47,,,,,,,,,,,,,,,,,,,,,,11292,11302,1991, citations,entry_citation,2053,117883,1,,entry citation,,,,,"Gardner, Kevin H., Pan, Tao, Narula, Surinder S., Rivera, Edwin, Coleman, Joseph E., ""Structure of the Binuclear Metal-Binding Site in the GAL4 Transcription Factor,"" Biochemistry 30 (47), 11292-11302 (1991).",Structure of the Binuclear Metal-Binding Site in the GAL4 Transcription Factor,published,journal,Biochemistry,,30,47,,,,,,,,,,,,,,,,,,,,,,11292,11302,1991, citations,entry_citation,2059,117896,1,,entry citation,,,,,"Lommen, Arjen, Wijmenga, Sybren S., Hilbers, C. W., Canters, Gerard W., ""Assignment of the 600-MHz 1H-NMR spectrum of amicyanin from Thiobacillus versutus by two-dimensional NMR methods provides information on secondary structure,"" Eur. J. Biochem. 201, 695-702 (1991).","Assignment of the 600-MHz 1H-NMR spectrum of amicyanin from Thiobacillus versutus by two-dimensional NMR methods provides information on secondary structure",published,journal,Eur. J. Biochem.,,201,,,,,,,,,,,,,,,,,,,,,,,695,702,1991, citations,entry_citation,2060,117910,1,,entry citation,,,,,"Hammen, Philip K., Waygood, E. Bruce, Klevit, Rachel E., ""Reexamination of the Secondary and Tertiary Structure of Histidine-Containing Protein from Escherichia coli by Homonuclear and Heteronuclear NMR Spectroscopy,"" Biochemistry 30 (51), 11842-11850 (1991).","Reexamination of the Secondary and Tertiary Structure of Histidine-Containing Protein from Escherichia coli by Homonuclear and Heteronuclear NMR Spectroscopy",published,journal,Biochemistry,,30,51,,,,,,,,,,,,,,,,,,,,,,11842,11850,1991, citations,entry_citation,2061,117923,1,,entry citation,,,,,"Chen, Yuan, Pitzenberger, Steven M., Garsky, Victor M., Lumma, Patricia K., Sanyal, Gautam, Baum, Jean, ""Proton NMR Assignments and Secondary Structure of the Snake Venom Protein Echistatin,"" Biochemistry 30 (50), 11625-11636 (1991).","Proton NMR Assignments and Secondary Structure of the Snake Venom Protein Echistatin",published,journal,Biochemistry,,30,50,,,,,,,,,,,,,,,,,,,,,,11625,11636,1991, citations,entry_citation,2062,117936,1,,entry citation,,,,,"Goodman, Elizabeth M., Kim, Peter S., ""Periodicity of Amide Proton Exchange Rates in a Coiled-Coil Leucine Zipper Peptide,"" Biochemistry 30 (50), 11615-11620 (1991).","Periodicity of Amide Proton Exchange Rates in a Coiled-Coil Leucine Zipper Peptide",published,journal,Biochemistry,,30,50,,,,,,,,,,,,,,,,,,,,,,11615,11620,1991, citations,entry_citation,2063,117951,1,,entry citation,,,,,"Moore, Jonathan M., Lepre, Christopher A., Gippert, Garry P., Chazin, Walter J., Case, David A., Wright, Peter E., ""High-resolution Solution Structure of Reduced French Bean Plastocyanin and Comparison with the Crystal Structure of Poplar Plastocyanin,"" J. Mol. Biol. 221, 533-555 (1991).","High-resolution Solution Structure of Reduced French Bean Plastocyanin and Comparison with the Crystal Structure of Poplar Plastocyanin",published,journal,J. Mol. Biol.,,221,,,,,,,,,,,,,,,,,,,,,,,533,555,1991, citations,entry_citation,2065,117964,1,,entry citation,,,,,"Simorre, J. P., Caille, A., Marion, Dominique, Marion, Didier, Ptak, M., ""Two- and Three-Dimensional 1H NMR Studies of a Wheat Phospholipid Transfer Protein: Sequential Resonance Assignments and Secondary Structure,"" Biochemistry 30 (49), 11600-11608 (1991).","Two- and Three-Dimensional 1H NMR Studies of a Wheat Phospholipid Transfer Protein: Sequential Resonance Assignments and Secondary Structure",published,journal,Biochemistry,,30,49,,,,,,,,,,,,,,,,,,,,,,11600,11608,1991, citations,entry_citation,2066,117977,1,,entry citation,,,,,"Meiering, Elizabeth M., Bycroft, Mark, Fersht, Alan R., ""Characterization of Phosphate Binding in the Active Site of Barnase by Site-Directed Mutagenesis and NMR,"" Biochemistry 30 (47), 11348-11356 (1991).","Characterization of Phosphate Binding in the Active Site of Barnase by Site-Directed Mutagenesis and NMR",published,journal,Biochemistry,,30,47,,,,,,,,,,,,,,,,,,,,,,11348,11356,1991, citations,entry_citation,2067,117990,1,,entry citation,,,,,"Meiering, Elizabeth M., Bycroft, Mark, Fersht, Alan R., ""Characterization of Phosphate Binding in the Active Site of Barnase by Site-Directed Mutagenesis and NMR,"" Biochemistry 30 (47), 11348-11356 (1991).","Characterization of Phosphate Binding in the Active Site of Barnase by Site-Directed Mutagenesis and NMR",published,journal,Biochemistry,,30,47,,,,,,,,,,,,,,,,,,,,,,11348,11356,1991, citations,entry_citation,2068,118003,1,,entry citation,,,,,"Meiering, Elizabeth M., Bycroft, Mark, Fersht, Alan R., ""Characterization of Phosphate Binding in the Active Site of Barnase by Site-Directed Mutagenesis and NMR,"" Biochemistry 30 (47), 11348-11356 (1991).","Characterization of Phosphate Binding in the Active Site of Barnase by Site-Directed Mutagenesis and NMR",published,journal,Biochemistry,,30,47,,,,,,,,,,,,,,,,,,,,,,11348,11356,1991, citations,entry_citation,2069,118016,1,,entry citation,,,,,"Meiering, Elizabeth M., Bycroft, Mark, Fersht, Alan R., ""Characterization of Phosphate Binding in the Active Site of Barnase by Site-Directed Mutagenesis and NMR,"" Biochemistry 30 (47), 11348-11356 (1991).","Characterization of Phosphate Binding in the Active Site of Barnase by Site-Directed Mutagenesis and NMR",published,journal,Biochemistry,,30,47,,,,,,,,,,,,,,,,,,,,,,11348,11356,1991, citations,entry_citation,2070,118029,1,,entry citation,,,,,"Meiering, Elizabeth M., Bycroft, Mark, Fersht, Alan R., ""Characterization of Phosphate Binding in the Active Site of Barnase by Site-Directed Mutagenesis and NMR,"" Biochemistry 30 (47), 11348-11356 (1991).","Characterization of Phosphate Binding in the Active Site of Barnase by Site-Directed Mutagenesis and NMR",published,journal,Biochemistry,,30,47,,,,,,,,,,,,,,,,,,,,,,11348,11356,1991, citations,entry_citation,2071,118042,1,,entry citation,,,,,"Meiering, Elizabeth M., Bycroft, Mark, Fersht, Alan R., ""Characterization of Phosphate Binding in the Active Site of Barnase by Site-Directed Mutagenesis and NMR,"" Biochemistry 30 (47), 11348-11356 (1991).","Characterization of Phosphate Binding in the Active Site of Barnase by Site-Directed Mutagenesis and NMR",published,journal,Biochemistry,,30,47,,,,,,,,,,,,,,,,,,,,,,11348,11356,1991, citations,entry_citation,2074,118055,1,,entry citation,,,,,"Borden, Katherine L. B., Beckmann, Pamela, Lane, Andrew, ""Determination of the orientations of tryptophan analogues bound to the trp repressor and the relationship to activation,"" Eur. J. Biochem. 202, 459-470 (1991).","Determination of the orientations of tryptophan analogues bound to the trp repressor and the relationship to activation",published,journal,Eur. J. Biochem.,,202,,,,,,,,,,,,,,,,,,,,,,,459,470,1991, citations,entry_citation,2075,118068,1,,entry citation,,,,,"Hommel, Ulrich, Dudgeon, Timothy J., Fallon, Anthony, Edwards, R.M., Campbell, Iain D., ""Structure-Function Relationships in Human Epidermal Growth Factor Studied by Site-Directed Mutagenesis and 1H NMR,"" Biochemistry 30, 8891-8898 (1991).","Structure-Function Relationships in Human Epidermal Growth Factor Studied by Site-Directed Mutagenesis and 1H NMR",published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,8891,8898,1991, citations,entry_citation,2076,118081,1,,entry citation,,,,,"Hommel, Ulrich, Dudgeon, Timothy J., Fallon, Anthony, Edwards, R.M., Campbell, Iain D., ""Structure-Function Relationships in Human Epidermal Growth Factor Studied by Site-Directed Mutagenesis and 1H NMR,"" Biochemistry 30, 8891-8898 (1991).","Structure-Function Relationships in Human Epidermal Growth Factor Studied by Site-Directed Mutagenesis and 1H NMR",published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,8891,8898,1991, citations,entry_citation,2077,118094,1,,entry citation,,,,,"Hommel, Ulrich, Dudgeon, Timothy J., Fallon, Anthony, Edwards, R.M., Campbell, Iain D., ""Structure-Function Relationships in Human Epidermal Growth Factor Studied by Site-Directed Mutagenesis and 1H NMR,"" Biochemistry 30, 8891-8898 (1991).","Structure-Function Relationships in Human Epidermal Growth Factor Studied by Site-Directed Mutagenesis and 1H NMR",published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,8891,8898,1991, citations,entry_citation,2078,118107,1,,entry citation,,,,,"Hommel, Ulrich, Dudgeon, Timothy J., Fallon, Anthony, Edwards, R.M., Campbell, Iain D., ""Structure-Function Relationships in Human Epidermal Growth Factor Studied by Site-Directed Mutagenesis and 1H NMR,"" Biochemistry 30, 8891-8898 (1991).","Structure-Function Relationships in Human Epidermal Growth Factor Studied by Site-Directed Mutagenesis and 1H NMR",published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,8891,8898,1991, citations,entry_citation,21,118120,1,,entry citation,,,,,"Mayo, Kevin H., Burke, Carl, ""Structural and dynamical comparison of alpha, beta, and gamma forms of murine epidermal growth factor,"" Eur. J. Biochem. 169, 201-207 (1987).","Structural and dynamical comparison of alpha, beta, and gamma forms of murine epidermal growth factor",published,journal,Eur. J. Biochem.,,169,,,,,,,,,,,,,,,,,,,,,,,201,207,1987, citations,entry_citation,21000,118133,1,,entry citation,,,21812076,,,Introducing lasso peptides as molecular scaffolds for drug design: engineering of an integrin antagonist,published,journal,Angew Chem Int Ed Engl.,,50,37,,,,,,,,,,,,,,,,,,,,,,8714,8717,2011, citations,entry_citation,21001,118151,1,,entry citation,,,22928939,,,Elucidation by NMR solution of neurotensin in small unilamellar vesicle environment: molecular surveys for neurotensin receptor recognition,published,journal,J. Biomol. Struct. Dyn.,,,,,,,,,,,,,,,,,,,,,,,,,,,2012, citations,citation2,21002,118170,1,,entry citation,,,21989967,,,Role of different beta-turns in beta-hairpin conformation and stability studied by optical spectroscopy,published,journal,,,80,1,,,,,,,,,,,,,,,,,,,,,,44,60,2012, citations,entry_citation,21006,118186,1,,entry citation,,,21899353,,,Alpha-Conotoxin ImI Incorporating Stable Cystathionine Bridges Maintains Full Potency and Identical Three-Dimensional Structure,published,journal,J. Am. Chem. Soc.,,133,40,,,,,,,,,,,,,,,,,,,,,,15866,15869,2011, citations,entry_citation,21007,118206,1,,entry citation,,,21899353,,,Alpha-Conotoxin ImI Incorporating Stable Cystathionine Bridges Maintains Full Potency and Identical Three-Dimensional Structure,published,journal,J. Am. Chem. Soc.,,133,40,,,,,,,,,,,,,,,,,,,,,,15866,15869,2011, citations,entry_citation,21008,118226,1,,entry citation,,,21586570,,,NMR Structures and Interactions of Temporin-1Tl and Temporin-1Tb with Lipopolysaccharide Micelles: MECHANISTIC INSIGHTS INTO OUTER MEMBRANE PERMEABILIZATION AND SYNERGISTIC ACTIVITY,published,journal,J. Biol. Chem.,,286,27,,,,,,,,,,,,,,,,,,,,,,24394,24406,2011, citations,entry_citation,21009,118242,1,,entry citation,,,21802428,,,The binding mechanism of a peptidic cyclic serine protease inhibitor,published,journal,J. Mol. Biol.,,412,2,,,,,,,,,,,,,,,,,,,,,,235,250,2011, citations,entry_citation,21010,118262,1,,entry citation,,,21802428,,,The binding mechanism of a peptidic cyclic serine protease inhibitor,published,journal,J. Mol. Biol.,,412,2,,,,,,,,,,,,,,,,,,,,,,235,250,2011, citations,entry_citation,21011,118281,1,,entry citation,,,22464970,10.1016/j.bbamem.2012.03.015,,"Structure, activity and interactions of the cysteine deleted analog of tachyplesin-1 with lipopolysaccharide micelle: Mechanistic insights into outer-membrane permeabilization and endotoxin neutralization.",published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1818,7,,0006-3002,,,,,,,,,,,,,,,,,,,,1613,1624,2012, citations,entry_citation,21013,118295,1,,entry citation,,,,,,,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,21014,118309,1,,entry citation,,,21968500,10.1007/s00726-011-1093-x,,Solution structure of a novel conotoxin with a distinctive loop spacing pattern,published,journal,Amino Acids,Amino Acids,,,,0939-4451,,,,,,,,,,,,,,,,,,,,,,2011, citations,entry_citation,21015,118327,1,,entry citation,,,21968500,10.1007/s00726-011-1093-x,,Solution structure of a novel conotoxin with a distinctive loop spacing pattern,published,journal,Amino Acids,Amino Acids,,,,0939-4451,,,,,,,,,,,,,,,,,,,,,,2011, citations,entry_citation,21018,118344,1,,entry citation,,,22795972,,,New analogs of the clinical complement inhibitor Compstatin with subnanomolar affinity and enhanced pharmacokinetic properties,published,journal,Immunobiology,,218,4,,,,,,,,,,,,,,,,,,,,,,496,505,2013, citations,entry_citation,21019,118363,1,,entry citation,,,22978677,,,"NMR structure, Localization and Vesicle fusion of Chikungunya Virus Fusion Peptide",published,journal,Biochemistry,,51,,BICHAW,0006-2960,0033,,,,,,,,,,,,,,,,,,,7863,7872,2012, citations,Our_article,21022,118377,1,,entry citation,,,23458158,,,Peptide Models of Cu(I) and Zn(II) Metallochaperones: The Effect of pH on Coordination and Mechanistic Implications.,published,journal,Inorg. Chem.,Inorganic chemistry,52,6,,,,,,,,,,,,,,,,,,,,,,2993,3000,2013, citations,Our_article,21023,118391,1,,entry citation,,,23458158,,,Peptide Models of Cu(I) and Zn(II) Metallochaperones: The Effect of pH on Coordination and Mechanistic Implications.,published,journal,Inorg. Chem.,Inorganic chemistry,52,6,,,,,,,,,,,,,,,,,,,,,,2993,3000,2013, citations,Our_article,21024,118405,1,,entry citation,,,23458158,,,Peptide Models of Cu(I) and Zn(II) Metallochaperones: The Effect of pH on Coordination and Mechanistic Implications.,published,journal,Inorg. Chem.,Inorganic chemistry,52,6,,,,,,,,,,,,,,,,,,,,,,2993,3000,2013, citations,Our_article,21025,118421,1,,entry citation,,,23458158,,,Peptide Models of Cu(I) and Zn(II) Metallochaperones: The Effect of pH on Coordination and Mechanistic Implications.,published,journal,Inorg. Chem.,Inorganic chemistry,52,6,,,,,,,,,,,,,,,,,,,,,,2993,3000,2013, citations,Our_article,21026,118435,1,,entry citation,,,23458158,,,Peptide Models of Cu(I) and Zn(II) Metallochaperones: The Effect of pH on Coordination and Mechanistic Implications.,published,journal,Inorg. Chem.,Inorganic chemistry,52,6,,,,,,,,,,,,,,,,,,,,,,2993,3000,2013, citations,Our_article,21027,118449,1,,entry citation,,,23458158,,,Peptide Models of Cu(I) and Zn(II) Metallochaperones: The Effect of pH on Coordination and Mechanistic Implications.,published,journal,Inorg. Chem.,Inorganic chemistry,52,6,,,,,,,,,,,,,,,,,,,,,,2993,3000,2013, citations,Our_article,21028,118467,1,,entry citation,,,23458158,,,Peptide Models of Cu(I) and Zn(II) Metallochaperones: The Effect of pH on Coordination and Mechanistic Implications.,published,journal,Inorg. Chem.,Inorganic chemistry,52,6,,,,,,,,,,,,,,,,,,,,,,2993,3000,2013, citations,entry_citation,21031,118485,1,,entry citation,,,28654715,10.1002/chem.201701866,,A Secondary Structural Element in a Wide Range of Fucosylated Glycoepitopes.,published,journal,Chemistry,"Chemistry (Weinheim an der Bergstrasse, Germany)",23,48,,1521-3765,,,,,,,,,,,,,,,,,,,,11598,11610,2017, citations,entry_citation,21032,118507,1,,entry citation,,,28654715,10.1002/chem.201701866,,A Secondary Structural Element in a Wide Range of Fucosylated Glycoepitopes.,published,journal,Chemistry,"Chemistry (Weinheim an der Bergstrasse, Germany)",23,48,,1521-3765,,,,,,,,,,,,,,,,,,,,11598,11610,2017, citations,entry_citation,21033,118531,1,,entry citation,,,24001318,,,Stabilization of Branched Oligosaccharides: Lewis(x) Benefits from a Nonconventional C-H...O Hydrogen Bond,published,journal,J. Am. Chem. Soc.,,135,36,,,,,,,,,,,,,,,,,,,,,,13464,13472,2013, citations,entry_citation,21034,118554,1,,entry citation,,,28654715,10.1002/chem.201701866,,A Secondary Structural Element in a Wide Range of Fucosylated Glycoepitopes.,published,journal,Chemistry,"Chemistry (Weinheim an der Bergstrasse, Germany)",23,48,,1521-3765,,,,,,,,,,,,,,,,,,,,11598,11610,2017, citations,entry_citation,21035,118579,1,,entry citation,,,,,,Structural Characterization of an Autoinducing Peptide and Abiotic Analogs Reveals Key Features Essential for Activation and Inhibition of an AgrC Quorum Sensing Receptor in Staphylococcus aureus,submitted,journal,J. Am. Chem. Soc.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,21036,118594,1,,entry citation,,,,,,Structural Characterization of an Autoinducing Peptide and Abiotic Analogs Reveals Key Features Essential for Activation and Inhibition of an AgrC Quorum Sensing Receptor in Staphylococcus aureus,submitted,journal,J. Am. Chem. Soc.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,21037,118609,1,,entry citation,,,,,,Structural Characterization of an Autoinducing Peptide and Abiotic Analogs Reveals Key Features Essential for Activation and Inhibition of an AgrC Quorum Sensing Receptor in Staphylococcus aureus,submitted,journal,J. Am. Chem. Soc.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,21038,118625,1,,entry citation,,,,,,Structural Characterization of an Autoinducing Peptide and Abiotic Analogs Reveals Key Features Essential for Activation and Inhibition of an AgrC Quorum Sensing Receptor in Staphylococcus aureus,submitted,journal,J. Am. Chem. Soc.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,21039,118641,1,,entry citation,,,,,,Structural Characterization of an Autoinducing Peptide and Abiotic Analogs Reveals Key Features Essential for Activation and Inhibition of an AgrC Quorum Sensing Receptor in Staphylococcus aureus,submitted,journal,J. Am. Chem. 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P., Mollison, Karl W., Henkin, Jack, Carter, George W., ""Sequence Specific Assignments in the 1H NMR Spectrum of the Human Inflammatory Protein C5a,"" Biochemistry 27 (10), 3568-3580 (1988).","Sequence Specific Assignments in the 1H NMR Spectrum of the Human Inflammatory Protein C5a",published,journal,Biochemistry,,27,10,,,,,,,,,,,,,,,,,,,,,,3568,3580,1988, citations,entry_citation,2197,119476,1,,entry citation,,,,,"Roongta, Vikram, Powers, Robert, Jones, Claude R., Beakage, Michael J., Sheilds, James E., Gorenstein, David G., ""Solution Conformation of a Synthetic Fragment of Human Pituitary Growth Hormone. Two-Dimensional NMR of an alpha-Helical Dimer,"" Biochemistry 28 (3), 1048-1054 (1989).","Solution Conformation of a Synthetic Fragment of Human Pituitary Growth Hormone. Two-Dimensional NMR of an alpha-Helical Dimer",published,journal,Biochemistry,,28,3,,,,,,,,,,,,,,,,,,,,,,1048,1054,1989, citations,entry_citation,2198,119489,1,,entry citation,,,,,"Moore, Jonathan M., Chazin, Walter J., Powls, Roy, Wright, Peter E., ""1H NMR Studies of Plastocyanin from Scenedesmus obliquus: Complete Sequence-Specific Assignment, Secondary Structure Analysis, and Global Fold,"" Biochemistry 27 (20), 7806-7816 (1988).","1H NMR Studies of Plastocyanin from Scenedesmus obliquus: Complete Sequence-Specific Assignment, Secondary Structure Analysis, and Global Fold",published,journal,Biochemistry,,27,20,,,,,,,,,,,,,,,,,,,,,,7806,7816,1988, citations,entry_citation,2199,119502,1,,entry citation,,,,,"Fry, David C., Madison, Vincent S., Bolin, David R., Greeley, David N., Toome, Voldemar, Wegrzynski, Bogda B., ""Solution Structure of an Analogue of Vasoactive Intestinal Peptide As Determined by Two-Dimensional NMR and Circular Dichroism Spectroscopies and Constrained Molecular Dynamics,"" Biochemistry 28 (6), 2399-2409 (1989).","Solution Structure of an Analogue of Vasoactive Intestinal Peptide As Determined by Two-Dimensional NMR and Circular Dichroism Spectroscopies and Constrained Molecular Dynamics",published,journal,Biochemistry,,28,6,,,,,,,,,,,,,,,,,,,,,,2399,2409,1989, citations,entry_citation,220,119518,1,,entry citation,,,,,"Boswell, Andrew P., Eley, Crispin G.S., Moore, Geoffrey R., Robinson, Martin N., Williams, Glyn, Williams, Robert J. P., Neupert, Walter J., Hennig, Bernd, ""1H NMR Studies of Eukaryotic Cytochrome c Resonance Assignments and Iron-Hexacyanide-Mediated Electron Exchange,"" Eur. J. Biochem. 124, 289-294 (1982).","1H NMR Studies of Eukaryotic Cytochrome c Resonance Assignments and Iron-Hexacyanide-Mediated Electron Exchange",published,journal,Eur. J. Biochem.,,124,,,,,,,,,,,,,,,,,,,,,,,289,294,1982, citations,entry_citation,2200,119533,1,,entry citation,,,,,"Fry, David C., Madison, Vincent S., Bolin, David R., Greeley, David N., Toome, Voldemar, Wegrzynski, Bogda B., ""Solution Structure of an Analogue of Vasoactive Intestinal Peptide As Determined by Two-Dimensional NMR and Circular Dichroism Spectroscopies and Constrained Molecular Dynamics,"" Biochemistry 28 (6), 2399-2409 (1989).","Solution Structure of an Analogue of Vasoactive Intestinal Peptide As Determined by Two-Dimensional NMR and Circular Dichroism Spectroscopies and Constrained Molecular Dynamics",published,journal,Biochemistry,,28,6,,,,,,,,,,,,,,,,,,,,,,2399,2409,1989, citations,entry_citation,2235,119936,1,,entry citation,,,,,"Matheson, Nancy R., van Halbeek, Herman, Travis, James, ""Evidence for a Tetrahedral Intermediate Complex during Serpin-Proteinase Interactions,"" J. Biol. Chem. 266 (21), 13489-13491 (1991).","Evidence for a Tetrahedral Intermediate Complex during Serpin-Proteinase Interactions",published,journal,J. Biol. Chem.,,266,21,,,,,,,,,,,,,,,,,,,,,,13489,13491,1991, citations,entry_citation,2201,119547,1,,entry citation,,,,,"Montelione, G.T., Wuthrich, Kurt, Burgess, A.W., Nice, E.C., Wagner, Gerhard, Gibson, Kenneth D., Scheraga, H.A., ""Solution Structure of Murine Epidermal Growth Factor Determined by NMR Spectroscopy and Refined by Energy Minimization with Restraints,"" Biochemistry 31 (1), 236-249 (1992).","Solution Structure of Murine Epidermal Growth Factor Determined by NMR Spectroscopy and Refined by Energy Minimization with Restraints",published,journal,Biochemistry,,31,1,,,,,,,,,,,,,,,,,,,,,,236,249,1992, citations,entry_citation,2202,119560,1,,entry citation,,,,,"Precheur, Benedicte, Munier, Helene, Mispelter, Joel, Barzu, Octavian, Craescu, Constantin T., ""1H and 15N NMR Characterization of Free and Bound States of an Amphiphilic Peptide Interacting with Calmodulin,"" Biochemistry 31 (1), 229-236 (1992).","1H and 15N NMR Characterization of Free and Bound States of an Amphiphilic Peptide Interacting with Calmodulin",published,journal,Biochemistry,,31,1,,,,,,,,,,,,,,,,,,,,,,229,236,1992, citations,entry_citation,2203,119575,1,,entry citation,,,,,"Precheur, Benedicte, Munier, Helene, Mispelter, Joel, Barzu, Octavian, Craescu, Constantin T., ""1H and 15N NMR Characterization of Free and Bound States of an Amphiphilic Peptide Interacting with Calmodulin,"" Biochemistry 31 (1), 229-236 (1992).","1H and 15N NMR Characterization of Free and Bound States of an Amphiphilic Peptide Interacting with Calmodulin",published,journal,Biochemistry,,31,1,,,,,,,,,,,,,,,,,,,,,,229,236,1992, citations,entry_citation,2204,119590,1,,entry citation,,,,,"Saudek, Vladimir, Atkinson, R. Andrew, Lepage, Pierre, Pelton, John T., ""The secondary structure of echistatin from 1H-NMR, circular-dichroism and Raman spectroscopy,"" Eur. J. Biochem. 202, 329-338 (1991).","The secondary structure of echistatin from 1H-NMR, circular-dichroism and Raman spectroscopy",published,journal,Eur. J. Biochem.,,202,,,,,,,,,,,,,,,,,,,,,,,329,338,1991, citations,entry_citation,2205,119603,1,,entry citation,,,,,"Dalvit, Claudio, Widmer, Hans, Boverman, Gunter, Breckenridge, Robin, Metternich, Rainer, ""1H NMR studies of echistatin in solution Sequential resonance assignments and secondary structure,"" Eur. J. Biochem. 202, 315-321 (1991).","1H NMR studies of echistatin in solution Sequential resonance assignments and secondary structure",published,journal,Eur. J. Biochem.,,202,,,,,,,,,,,,,,,,,,,,,,,315,321,1991, citations,entry_citation,2206,119616,1,,entry citation,,,,,"Cooke, Robert M., Carter, Brian G., Martin, David M. A., Murray-Rust, Peter, Weir, Malcolm P., ""Nuclear magnetic resonance studies of the snake toxin echistatin 1H resonance assignments and secondary structure,"" Eur. J. Biochem. 202, 323-328 (1991).","Nuclear magnetic resonance studies of the snake toxin echistatin 1H resonance assignments and secondary structure",published,journal,Eur. J. Biochem.,,202,,,,,,,,,,,,,,,,,,,,,,,323,328,1991, citations,entry_citation,2207,119629,1,,entry citation,,,,,"Cooke, Robert M., Carter, Brian G., Martin, David M. A., Murray-Rust, Peter, Weir, Malcolm P., ""Nuclear magnetic resonance studies of the snake toxin echistatin 1H resonance assignments and secondary structure,"" Eur. J. Biochem. 202, 323-328 (1991).","Nuclear magnetic resonance studies of the snake toxin echistatin 1H resonance assignments and secondary structure",published,journal,Eur. J. Biochem.,,202,,,,,,,,,,,,,,,,,,,,,,,323,328,1991, citations,entry_citation,2208,119642,1,,entry citation,,,,,"Neri, Placido, Meadows, Robert P., Gemmecker, G., Olejniczak, E.T., Nettesheim, David G., Logan, Timothy, Simmer, R., Helfrich, R., Holzman, Thomas F., Severin, Jean, Fesik, Stephen W., ""1H, 13C and 15N backbone assignments of cyclophilin when bound to cyclosporin A (CsA) and preliminary structural characterization of the CsA binding site,"" FEBS Lett. 294 (1-2), 81-88 (1991).","1H, 13C and 15N backbone assignments of cyclophilin when bound to cyclosporin A (CsA) and preliminary structural characterization of the CsA binding site",published,journal,FEBS Lett.,,294,1-2,,,,,,,,,,,,,,,,,,,,,,81,88,1991, citations,entry_citation,2209,119655,1,,entry citation,,,,,"Borden, Katherine L. B., Beckmann, Pamela, Lane, Andrew, ""Determination of the orientations of tryptophan analogues bound to the trp repressor and the relationship to activation,"" Eur. J. Biochem. 202, 459-470 (1991).","Determination of the orientations of tryptophan analogues bound to the trp repressor and the relationship to activation",published,journal,Eur. J. Biochem.,,202,,,,,,,,,,,,,,,,,,,,,,,459,470,1991, citations,entry_citation,221,119668,1,,entry citation,,,,,"Boswell, Andrew P., Eley, Crispin G.S., Moore, Geoffrey R., Robinson, Martin N., Williams, Glyn, Williams, Robert J. P., Neupert, Walter J., Hennig, Bernd, ""1H NMR Studies of Eukaryotic Cytochrome c Resonance Assignments and Iron-Hexacyanide-Mediated Electron Exchange,"" Eur. J. Biochem. 124, 289-294 (1982).","1H NMR Studies of Eukaryotic Cytochrome c Resonance Assignments and Iron-Hexacyanide-Mediated Electron Exchange",published,journal,Eur. J. Biochem.,,124,,,,,,,,,,,,,,,,,,,,,,,289,294,1982, citations,entry_citation,2217,119683,1,,entry citation,,,,,"Omichinski, James G., Clore, G. Marius, Sakaguchi, Kazuyasu, Appella, Ettore, Gronenborn, Angela M., ""Structural characterization of a 39-residue synthetic peptide containing the two zinc binding domains from the HIV-1 p7 nucleocapsid protein by CD and NMR spectroscopy,"" FEBS Lett. 292 (1-2), 25-30 (1991).","Structural characterization of a 39-residue synthetic peptide containing the two zinc binding domains from the HIV-1 p7 nucleocapsid protein by CD and NMR spectroscopy",published,journal,FEBS Lett.,,292,1-2,,,,,,,,,,,,,,,,,,,,,,25,30,1991, citations,entry_citation,2218,119696,1,,entry citation,,,,,"Pande, Usha, La Mar, Gerd N., Lecomte, Juliette T.J., Ascoli, Franca, Brunori, Maurizio, Smith, Kevin M., Pandey, Ravindra K., Parish, Daniel W., Thanabal, V., ""NMR Study of the Molecular and Electronic Structure of the Heme Cavity of Aplysia Metmyoglobin. Resonance Assignments Based on Isotope Labeling and Proton Nuclear Overhauser Effect Measurements,"" Biochemistry 25, 5638-5646 (1986).","NMR Study of the Molecular and Electronic Structure of the Heme Cavity of Aplysia Metmyoglobin. Resonance Assignments Based on Isotope Labeling and Proton Nuclear Overhauser Effect Measurements",published,journal,Biochemistry,,25,,,,,,,,,,,,,,,,,,,,,,,5638,5646,1986, citations,entry_citation,2219,119710,1,,entry citation,,,,,"Nettesheim, David G., Harder, Scott R., Feinberg, Benjamin A., Otvos, James D., ""Sequential Resonance Assignments of Oxidized High-Potential Iron-Sulfur Protein from Chromatium vinosum,"" Biochemistry 31 (4), 1234-1244 (1992).","Sequential Resonance Assignments of Oxidized High-Potential Iron-Sulfur Protein from Chromatium vinosum",published,journal,Biochemistry,,31,4,,,,,,,,,,,,,,,,,,,,,,1234,1244,1992, citations,entry_citation,222,119723,1,,entry citation,,,,,"Boswell, Andrew P., Eley, Crispin G.S., Moore, Geoffrey R., Robinson, Martin N., Williams, Glyn, Williams, Robert J. P., Neupert, Walter J., Hennig, Bernd, ""1H NMR Studies of Eukaryotic Cytochrome c Resonance Assignments and Iron-Hexacyanide-Mediated Electron Exchange,"" Eur. J. Biochem. 124, 289-294 (1982).","1H NMR Studies of Eukaryotic Cytochrome c Resonance Assignments and Iron-Hexacyanide-Mediated Electron Exchange",published,journal,Eur. J. Biochem.,,124,,,,,,,,,,,,,,,,,,,,,,,289,294,1982, citations,entry_citation,25027,121755,1,,entry citation,,,,,,NMR structure of the hypothetical protein BVU_0925 from Bacteroides vulgatus ATCC 8482,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,2220,119738,1,,entry citation,,,,,"Nettesheim, David G., Harder, Scott R., Feinberg, Benjamin A., Otvos, James D., ""Sequential Resonance Assignments of Oxidized High-Potential Iron-Sulfur Protein from Chromatium vinosum,"" Biochemistry 31 (4), 1234-1244 (1992).","Sequential Resonance Assignments of Oxidized High-Potential Iron-Sulfur Protein from Chromatium vinosum",published,journal,Biochemistry,,31,4,,,,,,,,,,,,,,,,,,,,,,1234,1244,1992, citations,entry_citation,2221,119751,1,,entry citation,,,,,"Nettesheim, David G., Harder, Scott R., Feinberg, Benjamin A., Otvos, James D., ""Sequential Resonance Assignments of Oxidized High-Potential Iron-Sulfur Protein from Chromatium vinosum,"" Biochemistry 31 (4), 1234-1244 (1992).","Sequential Resonance Assignments of Oxidized High-Potential Iron-Sulfur Protein from Chromatium vinosum",published,journal,Biochemistry,,31,4,,,,,,,,,,,,,,,,,,,,,,1234,1244,1992, citations,entry_citation,2222,119764,1,,entry citation,,,,,"Nettesheim, David G., Harder, Scott R., Feinberg, Benjamin A., Otvos, James D., ""Sequential Resonance Assignments of Oxidized High-Potential Iron-Sulfur Protein from Chromatium vinosum,"" Biochemistry 31 (4), 1234-1244 (1992).","Sequential Resonance Assignments of Oxidized High-Potential Iron-Sulfur Protein from Chromatium vinosum",published,journal,Biochemistry,,31,4,,,,,,,,,,,,,,,,,,,,,,1234,1244,1992, citations,entry_citation,2223,119777,1,,entry citation,,,,,"Li, Xiang, Sutcliffe, Michael J., Schwartz, Thue W., Dobson, Christopher M., ""Sequence-Specific 1H NMR Assignments and Solution Structure of Bovine Pancreatic Polypeptide,"" Biochemistry 31 (4), 1245-1253 (1992).","Sequence-Specific 1H NMR Assignments and Solution Structure of Bovine Pancreatic Polypeptide",published,journal,Biochemistry,,31,4,,,,,,,,,,,,,,,,,,,,,,1245,1253,1992, citations,entry_citation,2224,119791,1,,entry citation,,,,,"van Duynhoven, John P.M., Folkers, P.J.M., Prinse, W.J.M., Harmsen, B.J.M., Konings, R.N.H., Hilbers, C. W., ""Assignment of the 1H NMR Spectrum and Secondary Structure Elucidation of the Single-Stranded DNA Binding Protein Encoded by the Filamentous Bacteriophage IKe,"" Biochemistry 31 (4), 1254-1262 (1992).","Assignment of the 1H NMR Spectrum and Secondary Structure Elucidation of the Single-Stranded DNA Binding Protein Encoded by the Filamentous Bacteriophage IKe",published,journal,Biochemistry,,31,4,,,,,,,,,,,,,,,,,,,,,,1254,1262,1992, citations,entry_citation,2225,119804,1,,entry citation,,,,,"Krishnamoorthi, Ramaswamy, Sun Lin, Chan-Lan, Gong, YuXi, VanderVelde, David, Hahn, Karl, ""Proton NMR Studies of Cucurbita maxima Trypsin Inhibitors: Evidence for pH-Dependent Conformational Change and His25-Tyr27 Interaction,"" Biochemistry 31 (3), 905-910 (1992).","Proton NMR Studies of Cucurbita maxima Trypsin Inhibitors: Evidence for pH-Dependent Conformational Change and His25-Tyr27 Interaction",published,journal,Biochemistry,,31,3,,,,,,,,,,,,,,,,,,,,,,905,910,1992, citations,entry_citation,2226,119817,1,,entry citation,,,,,"Krishnamoorthi, Ramaswamy, Sun Lin, Chan-Lan, Gong, YuXi, VanderVelde, David, Hahn, Karl, ""Proton NMR Studies of Cucurbita maxima Trypsin Inhibitors: Evidence for pH-Dependent Conformational Change and His25-Tyr27 Interaction,"" Biochemistry 31 (3), 905-910 (1992).","Proton NMR Studies of Cucurbita maxima Trypsin Inhibitors: Evidence for pH-Dependent Conformational Change and His25-Tyr27 Interaction",published,journal,Biochemistry,,31,3,,,,,,,,,,,,,,,,,,,,,,905,910,1992, citations,entry_citation,2227,119830,1,,entry citation,,,,,"Krishnamoorthi, Ramaswamy, Gong, YuXi, Sun Lin, Chan-Lan, VanderVelde, David, ""Two-Dimensional NMR Studies of Squash Family Inhibitors. Sequence-Specific Proton Assignments and Secondary Structure of Reactive-Site Hydrolyzed Cucurbita maxima Trypsin Inhibitor III,"" Biochemistry 31 (3), 898-904 (1992).","Two-Dimensional NMR Studies of Squash Family Inhibitors. Sequence-Specific Proton Assignments and Secondary Structure of Reactive-Site Hydrolyzed Cucurbita maxima Trypsin Inhibitor III",published,journal,Biochemistry,,31,3,,,,,,,,,,,,,,,,,,,,,,898,904,1992, citations,entry_citation,2228,119843,1,,entry citation,,,,,"Krishnamoorthi, Ramaswamy, Gong, YuXi, Sun Lin, Chan-Lan, VanderVelde, David, ""Two-Dimensional NMR Studies of Squash Family Inhibitors. Sequence-Specific Proton Assignments and Secondary Structure of Reactive-Site Hydrolyzed Cucurbita maxima Trypsin Inhibitor III,"" Biochemistry 31 (3), 898-904 (1992).","Two-Dimensional NMR Studies of Squash Family Inhibitors. Sequence-Specific Proton Assignments and Secondary Structure of Reactive-Site Hydrolyzed Cucurbita maxima Trypsin Inhibitor III",published,journal,Biochemistry,,31,3,,,,,,,,,,,,,,,,,,,,,,898,904,1992, citations,entry_citation,2229,119856,1,,entry citation,,,,,"Kleanthous, Colin, Wemmer, David, Schachman, H. K., ""The Role of an Active Site Histidine in the Catalytic Mechanism of Aspartate Transcarbamoylase,"" J. Biol. Chem. 263 (26), 13062-13067 (1988).","The Role of an Active Site Histidine in the Catalytic Mechanism of Aspartate Transcarbamoylase",published,journal,J. Biol. Chem.,,263,26,,,,,,,,,,,,,,,,,,,,,,13062,13067,1988, citations,entry_citation,223,119869,1,,entry citation,,,,,"Boswell, Andrew P., Eley, Crispin G.S., Moore, Geoffrey R., Robinson, Martin N., Williams, Glyn, Williams, Robert J. P., Neupert, Walter J., Hennig, Bernd, ""1H NMR Studies of Eukaryotic Cytochrome c Resonance Assignments and Iron-Hexacyanide-Mediated Electron Exchange,"" Eur. J. Biochem. 124, 289-294 (1982).","1H NMR Studies of Eukaryotic Cytochrome c Resonance Assignments and Iron-Hexacyanide-Mediated Electron Exchange",published,journal,Eur. J. Biochem.,,124,,,,,,,,,,,,,,,,,,,,,,,289,294,1982, citations,entry_citation,2231,119884,1,,entry citation,,,,,"Ueda, Tadashi, Yamada, Hidenori, Sakamoto, Noriko, Abe, Yoshito, Kawano, Keiichi, Terada, Yoshihiro, Imoto, Taiji, ""Preparation of a Lysozyme Derivative in Which Two Domains Are Cross-Linked Intramolecularly between Trp62 and Asp101,"" J. Biochem. 110, 719-725 (1991).","Preparation of a Lysozyme Derivative in Which Two Domains Are Cross-Linked Intramolecularly between Trp62 and Asp101",published,journal,J. Biochem.,,110,,,,,,,,,,,,,,,,,,,,,,,719,725,1991, citations,entry_citation,2232,119897,1,,entry citation,,,,,"Ueda, Tadashi, Yamada, Hidenori, Sakamoto, Noriko, Abe, Yoshito, Kawano, Keiichi, Terada, Yoshihiro, Imoto, Taiji, ""Preparation of a Lysozyme Derivative in Which Two Domains Are Cross-Linked Intramolecularly between Trp62 and Asp101,"" J. Biochem. 110, 719-725 (1991).","Preparation of a Lysozyme Derivative in Which Two Domains Are Cross-Linked Intramolecularly between Trp62 and Asp101",published,journal,J. Biochem.,,110,,,,,,,,,,,,,,,,,,,,,,,719,725,1991, citations,entry_citation,2233,119910,1,,entry citation,,,,,"Coddington, Jan M., Barling, Peter M., ""Proton Nuclear Magnetic Resonance Studies of Intact Native Bovine Parathyroid Hormone,"" Mol. Endocrinol. 3 (4), 749-753 (1989).","Proton Nuclear Magnetic Resonance Studies of Intact Native Bovine Parathyroid Hormone",published,journal,Mol. Endocrinol.,,3,4,,,,,,,,,,,,,,,,,,,,,,749,753,1989, citations,entry_citation,2234,119923,1,,entry citation,,,,,"Coddington, Jan M., Barling, Peter M., ""Proton Nuclear Magnetic Resonance Studies of Intact Native Bovine Parathyroid Hormone,"" Mol. Endocrinol. 3 (4), 749-753 (1989).","Proton Nuclear Magnetic Resonance Studies of Intact Native Bovine Parathyroid Hormone",published,journal,Mol. Endocrinol.,,3,4,,,,,,,,,,,,,,,,,,,,,,749,753,1989, citations,entry_citation,25028,121773,1,,entry citation,,,,,,NMR structure of the hypotheical protein Lreu_0056 from Lactobacillus reuteri,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,2236,119949,1,,entry citation,,,,,"Matheson, Nancy R., van Halbeek, Herman, Travis, James, ""Evidence for a Tetrahedral Intermediate Complex during Serpin-Proteinase Interactions,"" J. Biol. Chem. 266 (21), 13489-13491 (1991).","Evidence for a Tetrahedral Intermediate Complex during Serpin-Proteinase Interactions",published,journal,J. Biol. Chem.,,266,21,,,,,,,,,,,,,,,,,,,,,,13489,13491,1991, citations,entry_citation,224,119962,1,,entry citation,,,,,"Boswell, Andrew P., Eley, Crispin G.S., Moore, Geoffrey R., Robinson, Martin N., Williams, Glyn, Williams, Robert J. P., Neupert, Walter J., Hennig, Bernd, ""1H NMR Studies of Eukaryotic Cytochrome c Resonance Assignments and Iron-Hexacyanide-Mediated Electron Exchange,"" Eur. J. Biochem. 124, 289-294 (1982).","1H NMR Studies of Eukaryotic Cytochrome c Resonance Assignments and Iron-Hexacyanide-Mediated Electron Exchange",published,journal,Eur. J. Biochem.,,124,,,,,,,,,,,,,,,,,,,,,,,289,294,1982, citations,entry_citation,2247,119977,1,,entry citation,,,,,"Krudy, George A., Brito, Rui M.M., Putkey, John A., Rosevear, Paul R., ""Conformational Changes in the Metal-Binding Sites of Cardiac Troponin C Induced by Calcium Binding,"" Biochemistry 31 (6), 1595-1602 (1992).","Conformational Changes in the Metal-Binding Sites of Cardiac Troponin C Induced by Calcium Binding",published,journal,Biochemistry,,31,6,,,,,,,,,,,,,,,,,,,,,,1595,1602,1992, citations,entry_citation,2249,119990,1,,entry citation,,,,,"Kohda, Daisuke, Inagaki, Fuyuhiko, ""Structure of Epidermal Growth Factor Bound to Perdeuterated Dodecylphosphocholine Micelles Determined by Two-Dimensional NMR and Simulated Annealing Calculations,"" Biochemistry 31 (3), 677-685 (1992).","Structure of Epidermal Growth Factor Bound to Perdeuterated Dodecylphosphocholine Micelles Determined by Two-Dimensional NMR and Simulated Annealing Calculations",published,journal,Biochemistry,,31,3,,,,,,,,,,,,,,,,,,,,,,677,685,1992, citations,entry_citation,225,120003,1,,entry citation,,,,,"Boswell, Andrew P., Eley, Crispin G.S., Moore, Geoffrey R., Robinson, Martin N., Williams, Glyn, Williams, Robert J. P., Neupert, Walter J., Hennig, Bernd, ""1H NMR Studies of Eukaryotic Cytochrome c Resonance Assignments and Iron-Hexacyanide-Mediated Electron Exchange,"" Eur. J. Biochem. 124, 289-294 (1982).","1H NMR Studies of Eukaryotic Cytochrome c Resonance Assignments and Iron-Hexacyanide-Mediated Electron Exchange",published,journal,Eur. J. Biochem.,,124,,,,,,,,,,,,,,,,,,,,,,,289,294,1982, citations,entry_citation,226,120018,1,,entry citation,,,,,"Boswell, Andrew P., Eley, Crispin G.S., Moore, Geoffrey R., Robinson, Martin N., Williams, Glyn, Williams, Robert J. P., Neupert, Walter J., Hennig, Bernd, ""1H NMR Studies of Eukaryotic Cytochrome c Resonance Assignments and Iron-Hexacyanide-Mediated Electron Exchange,"" Eur. J. Biochem. 124, 289-294 (1982).","1H NMR Studies of Eukaryotic Cytochrome c Resonance Assignments and Iron-Hexacyanide-Mediated Electron Exchange",published,journal,Eur. J. Biochem.,,124,,,,,,,,,,,,,,,,,,,,,,,289,294,1982, citations,entry_citation,2261,120033,1,,entry citation,,,,,"Byeon, In-Ja L., Llinas, M., ""Solution Structure of the Tissue-type Plasminogen Activator Kringle 2 Domain complexed to 6-Aminohexanoic Acid an Antifibrinolytic Drug,"" J. Mol. Biol. 222, 1035-1051 (1991).","Solution Structure of the Tissue-type Plasminogen Activator Kringle 2 Domain complexed to 6-Aminohexanoic Acid an Antifibrinolytic Drug",published,journal,J. Mol. Biol.,,222,,,,,,,,,,,,,,,,,,,,,,,1035,1051,1991, citations,entry_citation,2262,120046,1,,entry citation,,,,,"Andersen, Niels H., Chen, Chinpan, Marschner, Thomas M., Krystek, Stanley R. Jr., Bassolino, Donna A., ""Conformational Isomerism of Endothelin in Acidic Aqueous Media: A Quantitative NOESY Analysis,"" Biochemistry 31 (5), 1280-1295 (1992).","Conformational Isomerism of Endothelin in Acidic Aqueous Media: A Quantitative NOESY Analysis",published,journal,Biochemistry,,31,5,,,,,,,,,,,,,,,,,,,,,,1280,1295,1992, citations,entry_citation,2263,120059,1,,entry citation,,,,,"Andersen, Niels H., Chen, Chinpan, Marschner, Thomas M., Krystek, Stanley R. Jr., Bassolino, Donna A., ""Conformational Isomerism of Endothelin in Acidic Aqueous Media: A Quantitative NOESY Analysis,"" Biochemistry 31 (5), 1280-1295 (1992).","Conformational Isomerism of Endothelin in Acidic Aqueous Media: A Quantitative NOESY Analysis",published,journal,Biochemistry,,31,5,,,,,,,,,,,,,,,,,,,,,,1280,1295,1992, citations,entry_citation,2265,120072,1,,entry citation,,,,,"Westler, William M., Kainosho, Masatsune, Nagao, Hiromasa, Tomonaga, Noriko, Markley, John L., ""Two-Dimensional NMR Strategies for Carbon-Carbon Correlations and Sequence-Specific Assignments in Carbon-13 Labeled Proteins,"" J. Am. Chem. Soc. 110, 4093-4095 (1988).","Two-Dimensional NMR Strategies for Carbon-Carbon Correlations and Sequence-Specific Assignments in Carbon-13 Labeled Proteins",published,journal,J. Am. Chem. Soc.,,110,,,,,,,,,,,,,,,,,,,,,,,4093,4095,1988, citations,entry_citation,2266,120083,1,,entry citation,,,,,"Weaver, Arthur J., Kemple, Marvin D., Brauner, Joseph W., Mendelsohn, Richard, Prendergast, Franklyn G., ""Fluorescence, CD, Attenuated Total Reflectance (ATR) FTIR, and 13C NMR Characterization of the Structure and Dynamics of Synthetic Melittin and Melittin Analogues in Lipid Environments,"" Biochemistry 31 (5), 1301-1313 (1992).","Fluorescence, CD, Attenuated Total Reflectance (ATR) FTIR, and 13C NMR Characterization of the Structure and Dynamics of Synthetic Melittin and Melittin Analogues in Lipid Environments",published,journal,Biochemistry,,31,5,,,,,,,,,,,,,,,,,,,,,,1301,1313,1992, citations,entry_citation,2267,120095,1,,entry citation,,,,,"Weaver, Arthur J., Kemple, Marvin D., Brauner, Joseph W., Mendelsohn, Richard, Prendergast, Franklyn G., ""Fluorescence, CD, Attenuated Total Reflectance (ATR) FTIR, and 13C NMR Characterization of the Structure and Dynamics of Synthetic Melittin and Melittin Analogues in Lipid Environments,"" Biochemistry 31 (5), 1301-1313 (1992).","Fluorescence, CD, Attenuated Total Reflectance (ATR) FTIR, and 13C NMR Characterization of the Structure and Dynamics of Synthetic Melittin and Melittin Analogues in Lipid Environments",published,journal,Biochemistry,,31,5,,,,,,,,,,,,,,,,,,,,,,1301,1313,1992, citations,entry_citation,2268,120109,1,,entry citation,,,,,"Weaver, Arthur J., Kemple, Marvin D., Brauner, Joseph W., Mendelsohn, Richard, Prendergast, Franklyn G., ""Fluorescence, CD, Attenuated Total Reflectance (ATR) FTIR, and 13C NMR Characterization of the Structure and Dynamics of Synthetic Melittin and Melittin Analogues in Lipid Environments,"" Biochemistry 31 (5), 1301-1313 (1992).","Fluorescence, CD, Attenuated Total Reflectance (ATR) FTIR, and 13C NMR Characterization of the Structure and Dynamics of Synthetic Melittin and Melittin Analogues in Lipid Environments",published,journal,Biochemistry,,31,5,,,,,,,,,,,,,,,,,,,,,,1301,1313,1992, citations,entry_citation,2269,120123,1,,entry citation,,,,,"Weaver, Arthur J., Kemple, Marvin D., Brauner, Joseph W., Mendelsohn, Richard, Prendergast, Franklyn G., ""Fluorescence, CD, Attenuated Total Reflectance (ATR) FTIR, and 13C NMR Characterization of the Structure and Dynamics of Synthetic Melittin and Melittin Analogues in Lipid Environments,"" Biochemistry 31 (5), 1301-1313 (1992).","Fluorescence, CD, Attenuated Total Reflectance (ATR) FTIR, and 13C NMR Characterization of the Structure and Dynamics of Synthetic Melittin and Melittin Analogues in Lipid Environments",published,journal,Biochemistry,,31,5,,,,,,,,,,,,,,,,,,,,,,1301,1313,1992, citations,entry_citation,227,120137,1,,entry citation,,,,,"Senn, Hans, Eugster, Albert, Wuthrich, Kurt, ""Determination of the Coordination Geometry at the Heme Iron in Three Cytochromes c from Saccharomyces cerevisiae and from Candida krusei Based on Individual 1H-NMR Assignments for Heme c and the Axially Coordinated Amino Acids,"" Biochim. Biophys. Acta 743, 58-68 (1983).","Determination of the Coordination Geometry at the Heme Iron in Three Cytochromes c from Saccharomyces cerevisiae and from Candida krusei Based on Individual 1H-NMR Assignments for Heme c and the Axially Coordinated Amino Acids",published,journal,Biochim. Biophys. Acta,,743,,,,,,,,,,,,,,,,,,,,,,,58,68,1983, citations,entry_citation,2270,120152,1,,entry citation,,,,,"Weaver, Arthur J., Kemple, Marvin D., Brauner, Joseph W., Mendelsohn, Richard, Prendergast, Franklyn G., ""Fluorescence, CD, Attenuated Total Reflectance (ATR) FTIR, and 13C NMR Characterization of the Structure and Dynamics of Synthetic Melittin and Melittin Analogues in Lipid Environments,"" Biochemistry 31 (5), 1301-1313 (1992).","Fluorescence, CD, Attenuated Total Reflectance (ATR) FTIR, and 13C NMR Characterization of the Structure and Dynamics of Synthetic Melittin and Melittin Analogues in Lipid Environments",published,journal,Biochemistry,,31,5,,,,,,,,,,,,,,,,,,,,,,1301,1313,1992, citations,entry_citation,2271,120166,1,,entry citation,,,,,"Weaver, Arthur J., Kemple, Marvin D., Brauner, Joseph W., Mendelsohn, Richard, Prendergast, Franklyn G., ""Fluorescence, CD, Attenuated Total Reflectance (ATR) FTIR, and 13C NMR Characterization of the Structure and Dynamics of Synthetic Melittin and Melittin Analogues in Lipid Environments,"" Biochemistry 31 (5), 1301-1313 (1992).","Fluorescence, CD, Attenuated Total Reflectance (ATR) FTIR, and 13C NMR Characterization of the Structure and Dynamics of Synthetic Melittin and Melittin Analogues in Lipid Environments",published,journal,Biochemistry,,31,5,,,,,,,,,,,,,,,,,,,,,,1301,1313,1992, citations,entry_citation,2272,120180,1,,entry citation,,,,,"Dyson, H. Jane, Norrby, Erling, Hoey, Kenway, Parks, D. Elliot, Lerner, Richard A., Wright, Peter E., ""Immunogenic Peptides Corresponding to the Dominant Antigenic Region Alanine-597 to Cysteine-619 in the Transmembrane Protein of Simian Immunodeficiency Virus Have a Propensity To Fold in Aqueous Solution,"" Biochemistry 31 (5), 1458-1463 (1992).","Immunogenic Peptides Corresponding to the Dominant Antigenic Region Alanine-597 to Cysteine-619 in the Transmembrane Protein of Simian Immunodeficiency Virus Have a Propensity To Fold in Aqueous Solution",published,journal,Biochemistry,,31,5,,,,,,,,,,,,,,,,,,,,,,1458,1463,1992, citations,entry_citation,2274,120192,1,,entry citation,,,,,"Hua, Qing-Xin, ""1H Spin System Identifications of S-Sulfonated Insulin B Chain with 2D-NMR,"" Sci. China Ser. B 32 (8), 948-959 (1989).",1H Spin System Identifications of S-Sulfonated Insulin B Chain with 2D-NMR,published,journal,Sci. China Ser. B,,32,8,,,,,,,,,,,,,,,,,,,,,,948,959,1989, citations,entry_citation,2275,120205,1,,entry citation,,,,,"Lee, Chang-Shin, Yu, Chin, ""Identification of Two Antiparallel-sheet Structure of Cobrotoxin in Aqueous Solution by 1H NMR,"" Bull. Magn. Reson. 11 (3/4), 188-192 (1989).","Identification of Two Antiparallel-sheet Structure of Cobrotoxin in Aqueous Solution by 1H NMR",published,journal,Bull. Magn. Reson.,,11,3/4,,,,,,,,,,,,,,,,,,,,,,188,192,1989, citations,entry_citation,2276,120218,1,,entry citation,,,,,"Di Bello, C., Scatturin, A., Vertuani, Gianni, D'Auria, Gabriella, Gargiulo, Mario, Paolillo, Livio, Trivellone, E., Gozzini, L., De Castiglione, Roberto, ""Conformational Studies on Bombesin Antagonists: CD and NMR Characterization of [Thr6, Leu13psi(CH2NH) Met14] Bombesin (6-14),"" Biopolymers 31, 1397-1408 (1991).","Conformational Studies on Bombesin Antagonists: CD and NMR Characterization of [Thr6, Leu13psi(CH2NH) Met14] Bombesin (6-14)",published,journal,Biopolymers,,31,,,,,,,,,,,,,,,,,,,,,,,1397,1408,1991, citations,entry_citation,2277,120234,1,,entry citation,,,,,"Ballio, A., Barra, D., Bossa, F., Collina, A., Grgurina, I., Marino, G., Moneti, G., Paci, Maurizio, Pucci, P., Segre, A., Simmaco, M., ""Syringopeptins, new phytotoxic lipodepsipeptides of Pseudomonas syringae pv. syringae,"" FEBS Lett. 291 (1), 109-112 (1991).","Syringopeptins, new phytotoxic lipodepsipeptides of Pseudomonas syringae pv. syringae",published,journal,FEBS Lett.,,291,1,,,,,,,,,,,,,,,,,,,,,,109,112,1991, citations,entry_citation,2278,120249,1,,entry citation,,,,,"Ye, Xiao Mei, Pochapsky, Thomas C., Pochapsky, Susan Sondej, ""1H NMR Sequential Assignments and Identification of Secondary Structural Elements in Oxidized Putidaredoxin, an Electron-Transfer Protein from Pseudomonas,"" Biochemistry 31 (7), 1961-1968 (1992).","1H NMR Sequential Assignments and Identification of Secondary Structural Elements in Oxidized Putidaredoxin, an Electron-Transfer Protein from Pseudomonas",published,journal,Biochemistry,,31,7,,,,,,,,,,,,,,,,,,,,,,1961,1968,1992, citations,entry_citation,2279,120262,1,,entry citation,,,,,"Slijper, M., Hilbers, C. W., Konings, R.N.H., van de Ven, F. J. M., ""NMR studies of lantibiotics Assignment of the 1H-NMR spectrum of nisin and identification of interresidual contacts,"" FEBS Lett. 252 (1,2), 22-28 (1989).","NMR studies of lantibiotics Assignment of the 1H-NMR spectrum of nisin and identification of interresidual contacts",published,journal,FEBS Lett.,,252,"1,2",,,,,,,,,,,,,,,,,,,,,,22,28,1989, citations,entry_citation,228,120280,1,,entry citation,,,,,"Senn, Hans, Eugster, Albert, Wuthrich, Kurt, ""Determination of the Coordination Geometry at the Heme Iron in Three Cytochromes c from Saccharomyces cerevisiae and from Candida krusei Based on Individual 1H-NMR Assignments for Heme c and the Axially Coordinated Amino Acids,"" Biochim. Biophys. Acta 743, 58-68 (1983).","Determination of the Coordination Geometry at the Heme Iron in Three Cytochromes c from Saccharomyces cerevisiae and from Candida krusei Based on Individual 1H-NMR Assignments for Heme c and the Axially Coordinated Amino Acids",published,journal,Biochim. Biophys. Acta,,743,,,,,,,,,,,,,,,,,,,,,,,58,68,1983, citations,entry_citation,2281,120293,1,,entry citation,,,,,"Baron, Martin, Main, Alison L., Driscoll, Paul C., Mardon, Helen J., Boyd, Jonathan, Campbell, Iain D., ""1H NMR Assignment and Secondary Structure of the Cell Adhesion Type III Module of Fibronectin,"" Biochemistry 31 (7), 2068-2073 (1992).","1H NMR Assignment and Secondary Structure of the Cell Adhesion Type III Module of Fibronectin",published,journal,Biochemistry,,31,7,,,,,,,,,,,,,,,,,,,,,,2068,2073,1992, citations,entry_citation,2282,120306,1,,entry citation,,,,,"Arseniev, Alexander S., Maslennikov, Innokenti V., Bystrov, Vladimir F., Kozhich, Alexander T., Ivanov, Vadim T., Ovchinnikov, Yuri A., ""Two-dimensional 1H-NMR study of bacterioopsin-(34-65)-polypeptide conformation,"" FEBS Lett. 231 (1), 81-88 (1988).",Two-dimensional 1H-NMR study of bacterioopsin-(34-65)-polypeptide conformation,published,journal,FEBS Lett.,,231,1,,,,,,,,,,,,,,,,,,,,,,81,88,1988, citations,entry_citation,2283,120320,1,,entry citation,,,,,"Mikou, Afaf, LaPlante, Steven R., Guittet, Eric, Lallemand, Jean-Yves, Martin-Eau Claire, Marie-France, Rochat, Herve, ""Toxin III of the scorpion Androctonus australis Hector: Proton nuclear magnetic resonance assignments and secondary structure,"" J. Biomol. NMR 2 (1), 57-70 (1992).","Toxin III of the scorpion Androctonus australis Hector: Proton nuclear magnetic resonance assignments and secondary structure",published,journal,J. Biomol. NMR,,2,1,,,,,,,,,,,,,,,,,,,,,,57,70,1992, citations,entry_citation,2284,120333,1,,entry citation,,,,,"Mikou, Afaf, LaPlante, Steven R., Guittet, Eric, Lallemand, Jean-Yves, Martin-Eau Claire, Marie-France, Rochat, Herve, ""Toxin III of the scorpion Androctonus australis Hector: Proton nuclear magnetic resonance assignments and secondary structure,"" J. Biomol. NMR 2 (1), 57-70 (1992).","Toxin III of the scorpion Androctonus australis Hector: Proton nuclear magnetic resonance assignments and secondary structure",published,journal,J. Biomol. NMR,,2,1,,,,,,,,,,,,,,,,,,,,,,57,70,1992, citations,entry_citation,2285,120346,1,,entry citation,,,,,"Bachovchin, William W., Kaiser, John H., Richards, John H., Roberts, John D., ""Catalytic mechanism of serine proteases: Reexamination of the pH dependence of the histidyl 1J13C2-H coupling constant in the catalytic triad of alpha-lytic protease,"" Proc. Natl. Acad. Sci. U.S.A. 78 (12), 7323-7326 (1981).","Catalytic mechanism of serine proteases: Reexamination of the pH dependence of the histidyl 1J13C2-H coupling constant in the catalytic triad of alpha-lytic protease",published,journal,Proc. Natl. Acad. Sci. U.S.A.,,78,12,,,,,,,,,,,,,,,,,,,,,,7323,7326,1981, citations,entry_citation,2288,120359,1,,entry citation,,,,,"Kainosho, Masatsune, Tsuji, Takashi, ""Assignment of the Three Methionyl Carbonyl Carbon Resonances in Streptomyces Subtilisin Inhibitor by a Carbon-13 and Nitrogen-15 Double -Labeling Technique. A New Strategy for Structural Studies of Proteins in Solution,"" Biochemistry 21, 6273-6278 (1982).","Assignment of the Three Methionyl Carbonyl Carbon Resonances in Streptomyces Subtilisin Inhibitor by a Carbon-13 and Nitrogen-15 Double -Labeling Technique. A New Strategy for Structural Studies of Proteins in Solution",published,journal,Biochemistry,,21,,,,,,,,,,,,,,,,,,,,,,,6273,6278,1982, citations,entry_citation,229,120372,1,,entry citation,,,,,"Senn, Hans, Eugster, Albert, Wuthrich, Kurt, ""Determination of the Coordination Geometry at the Heme Iron in Three Cytochromes c from Saccharomyces cerevisiae and from Candida krusei Based on Individual 1H-NMR Assignments for Heme c and the Axially Coordinated Amino Acids,"" Biochim. Biophys. Acta 743, 58-68 (1983).","Determination of the Coordination Geometry at the Heme Iron in Three Cytochromes c from Saccharomyces cerevisiae and from Candida krusei Based on Individual 1H-NMR Assignments for Heme c and the Axially Coordinated Amino Acids",published,journal,Biochim. Biophys. Acta,,743,,,,,,,,,,,,,,,,,,,,,,,58,68,1983, citations,entry_citation,23,120388,1,,entry citation,,,,,"Wider, Gerhard, Lee, Kong Hung, Wuthrich, Kurt, ""Sequential Resonance Assignments in Protein 1H Nuclear Magnetic Resonance Spectra (Glucagon Bound to Perdeuterated Dodecylphosphocholine Micelles),"" J. Mol. Biol. 155, 367-388 (1982).","Sequential Resonance Assignments in Protein 1H Nuclear Magnetic Resonance Spectra (Glucagon Bound to Perdeuterated Dodecylphosphocholine Micelles)",published,journal,J. Mol. Biol.,,155,,,,,,,,,,,,,,,,,,,,,,,367,388,1982, citations,entry_citation,2324,120401,1,,entry citation,,,,,"Kalbitzer, H.R., Marquetant, Rainer, Rosch, Paul, Schirmer, R. Heiner, ""The Structural Isomerisation of Human-Muscle Adenylate Kinase as Studied by 1H-Nuclear Magnetic Resonance,"" Eur. J. Biochem. 126, 531-536 (1982).","The Structural Isomerisation of Human-Muscle Adenylate Kinase as Studied by 1H-Nuclear Magnetic Resonance",published,journal,Eur. J. Biochem.,,126,,,,,,,,,,,,,,,,,,,,,,,531,536,1982, citations,entry_citation,2325,120415,1,,entry citation,,,,,"Kalbitzer, H.R., Marquetant, Rainer, Rosch, Paul, Schirmer, R. Heiner, ""The Structural Isomerisation of Human-Muscle Adenylate Kinase as Studied by 1H-Nuclear Magnetic Resonance,"" Eur. J. Biochem. 126, 531-536 (1982).","The Structural Isomerisation of Human-Muscle Adenylate Kinase as Studied by 1H-Nuclear Magnetic Resonance",published,journal,Eur. J. Biochem.,,126,,,,,,,,,,,,,,,,,,,,,,,531,536,1982, citations,entry_citation,2326,120429,1,,entry citation,,,,,"Kalbitzer, H.R., Marquetant, Rainer, Rosch, Paul, Schirmer, R. Heiner, ""The Structural Isomerisation of Human-Muscle Adenylate Kinase as Studied by 1H-Nuclear Magnetic Resonance,"" Eur. J. Biochem. 126, 531-536 (1982).","The Structural Isomerisation of Human-Muscle Adenylate Kinase as Studied by 1H-Nuclear Magnetic Resonance",published,journal,Eur. J. Biochem.,,126,,,,,,,,,,,,,,,,,,,,,,,531,536,1982, citations,entry_citation,2327,120443,1,,entry citation,,,,,"Eberle, Wolfgang, Sander, Chris, Klaus, Werner, Schmidt, Bernhard, von Figura, Kurt, Peters, Christoph, ""The Essential Tyrosine of the Internalization Signal in Lysosomal Acid Phosphatase Is Part of a beta Turn,"" Cell 67, 1203-1209 (1991).","The Essential Tyrosine of the Internalization Signal in Lysosomal Acid Phosphatase Is Part of a beta Turn",published,journal,Cell,,67,,,,,,,,,,,,,,,,,,,,,,,1203,1209,1991, citations,entry_citation,2328,120456,1,,entry citation,,,,,"Mortishire-Smith, Russell J., Lee, Min S., Bolinger, Lizann, Wright, Peter E., ""Structural determinants of Cys2His2 zinc fingers,"" FEBS Lett. 296 (1), 11-15 (1992).",Structural determinants of Cys2His2 zinc fingers,published,journal,FEBS Lett.,,296,1,,,,,,,,,,,,,,,,,,,,,,11,15,1992, citations,entry_citation,2329,120471,1,,entry citation,,,,,"Mortishire-Smith, Russell J., Lee, Min S., Bolinger, Lizann, Wright, Peter E., ""Structural determinants of Cys2His2 zinc fingers,"" FEBS Lett. 296 (1), 11-15 (1992).",Structural determinants of Cys2His2 zinc fingers,published,journal,FEBS Lett.,,296,1,,,,,,,,,,,,,,,,,,,,,,11,15,1992, citations,entry_citation,233,120484,1,,entry citation,,,,,"Senn, Hans, Eugster, Albert, Wuthrich, Kurt, ""Determination of the Coordination Geometry at the Heme Iron in Three Cytochromes c from Saccharomyces cerevisiae and from Candida krusei Based on Individual 1H-NMR Assignments for Heme c and the Axially Coordinated Amino Acids,"" Biochim. Biophys. Acta 743, 58-68 (1983).","Determination of the Coordination Geometry at the Heme Iron in Three Cytochromes c from Saccharomyces cerevisiae and from Candida krusei Based on Individual 1H-NMR Assignments for Heme c and the Axially Coordinated Amino Acids",published,journal,Biochim. Biophys. Acta,,743,,,,,,,,,,,,,,,,,,,,,,,58,68,1983, citations,entry_citation,2331,120499,1,,entry citation,,,,,"Inagaki, Fuyuhiko, Clayden, Nigel J., Tamiya, Nobuo, Williams, Robert J. P., ""Individual Assignments of the Amide Proton Resonances Involved in the Triple-Stranded Antiparallel Pleated beta-Sheet Structure of a Long Neurotoxin, Laticauda Semifasciata III from Laticauda semifasciata,"" Eur. J. Biochem. 123, 99-104 (1982).","Individual Assignments of the Amide Proton Resonances Involved in the Triple-Stranded Antiparallel Pleated beta-Sheet Structure of a Long Neurotoxin, Laticauda Semifasciata III from Laticauda semifasciata",published,journal,Eur. J. Biochem.,,123,,,,,,,,,,,,,,,,,,,,,,,99,104,1982, citations,entry_citation,2338,120512,1,,entry citation,,,,,"King, Garry C., Wright, Peter E., ""A Two-Dimensional NMR Method for Assignment of Imidazole Ring Proton Resonances of Histidine Residues in Proteins,"" Biochem. Biophys. Res. Commun. 106 (2), 559-565 (1982).","A Two-Dimensional NMR Method for Assignment of Imidazole Ring Proton Resonances of Histidine Residues in Proteins",published,journal,Biochem. Biophys. Res. Commun.,,106,2,,,,,,,,,,,,,,,,,,,,,,559,565,1982, citations,entry_citation,25029,121791,1,,entry citation,,,24969589,10.1021/ja503546j,,Specific and nonspecific interactions in ultraweak protein-protein associations revealed by solvent paramagnetic relaxation enhancements.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,136,29,,1520-5126,,,,,,,,,,,,,,,,,,,,10277,10286,2014, citations,entry_citation,234,120525,1,,entry citation,,,,,"Senn, Hans, Eugster, Albert, Wuthrich, Kurt, ""Determination of the Coordination Geometry at the Heme Iron in Three Cytochromes c from Saccharomyces cerevisiae and from Candida krusei Based on Individual 1H-NMR Assignments for Heme c and the Axially Coordinated Amino Acids,"" Biochim. Biophys. Acta 743, 58-68 (1983).","Determination of the Coordination Geometry at the Heme Iron in Three Cytochromes c from Saccharomyces cerevisiae and from Candida krusei Based on Individual 1H-NMR Assignments for Heme c and the Axially Coordinated Amino Acids",published,journal,Biochim. Biophys. Acta,,743,,,,,,,,,,,,,,,,,,,,,,,58,68,1983, citations,entry_citation,2345,120540,1,,entry citation,,,,,"Dugad, Laxmichand B., La Mar, Gerd N., Unger, Stephen W., ""Influence of Molecular Correlation Time on the Homonuclear Overhauser Effect in Paramagnetic Proteins,"" J. Am. Chem. Soc. 112, 1386-1392 (1990).","Influence of Molecular Correlation Time on the Homonuclear Overhauser Effect in Paramagnetic Proteins",published,journal,J. Am. Chem. Soc.,,112,,,,,,,,,,,,,,,,,,,,,,,1386,1392,1990, citations,entry_citation,2346,120553,1,,entry citation,,,,,"Dugad, Laxmichand B., La Mar, Gerd N., Unger, Stephen W., ""Influence of Molecular Correlation Time on the Homonuclear Overhauser Effect in Paramagnetic Proteins,"" J. Am. Chem. Soc. 112, 1386-1392 (1990).","Influence of Molecular Correlation Time on the Homonuclear Overhauser Effect in Paramagnetic Proteins",published,journal,J. Am. Chem. Soc.,,112,,,,,,,,,,,,,,,,,,,,,,,1386,1392,1990, citations,entry_citation,2347,120566,1,,entry citation,,,,,"Dugad, Laxmichand B., La Mar, Gerd N., Unger, Stephen W., ""Influence of Molecular Correlation Time on the Homonuclear Overhauser Effect in Paramagnetic Proteins,"" J. Am. Chem. Soc. 112, 1386-1392 (1990).","Influence of Molecular Correlation Time on the Homonuclear Overhauser Effect in Paramagnetic Proteins",published,journal,J. Am. Chem. Soc.,,112,,,,,,,,,,,,,,,,,,,,,,,1386,1392,1990, citations,entry_citation,2348,120579,1,,entry citation,,,,,"Dugad, Laxmichand B., La Mar, Gerd N., Unger, Stephen W., ""Influence of Molecular Correlation Time on the Homonuclear Overhauser Effect in Paramagnetic Proteins,"" J. Am. Chem. Soc. 112, 1386-1392 (1990).","Influence of Molecular Correlation Time on the Homonuclear Overhauser Effect in Paramagnetic Proteins",published,journal,J. Am. Chem. Soc.,,112,,,,,,,,,,,,,,,,,,,,,,,1386,1392,1990, citations,entry_citation,235,120592,1,,entry citation,,,,,"Senn, Hans, Eugster, Albert, Wuthrich, Kurt, ""Determination of the Coordination Geometry at the Heme Iron in Three Cytochromes c from Saccharomyces cerevisiae and from Candida krusei Based on Individual 1H-NMR Assignments for Heme c and the Axially Coordinated Amino Acids,"" Biochim. Biophys. Acta 743, 58-68 (1983).","Determination of the Coordination Geometry at the Heme Iron in Three Cytochromes c from Saccharomyces cerevisiae and from Candida krusei Based on Individual 1H-NMR Assignments for Heme c and the Axially Coordinated Amino Acids",published,journal,Biochim. Biophys. Acta,,743,,,,,,,,,,,,,,,,,,,,,,,58,68,1983, citations,entry_citation,2352,120608,1,,entry citation,,,,,"Lecomte, Juliette T.J., Smit, Jan Derk G., Winterhalter, Kaspar H., La Mar, Gerd N., ""Structural and Electronic Properties of the Liver Fluke Heme Cavity by Nuclear Magnetic Resonance and Optical Spectroscopy. Evidence for a Distal Tyrosine Residue in a Normally Functioning Hemoglobin.,"" J. Mol. Biol. 209, 235-247 (1989).","Structural and Electronic Properties of the Liver Fluke Heme Cavity by Nuclear Magnetic Resonance and Optical Spectroscopy. Evidence for a Distal Tyrosine Residue in a Normally Functioning Hemoglobin.",published,journal,J. Mol. Biol.,,209,,,,,,,,,,,,,,,,,,,,,,,235,247,1989, citations,entry_citation,2353,120621,1,,entry citation,,,,,"Torigoe, Hidetaka, Shimada, Ichio, Waelchli, Markus, Saito, Akiko, Sato, Moriyuki, Arata, Yoji, ""15N nuclear magnetic resonance studies of the B domain of Staphylococcal protein A: Sequence specific assignments of the imide 15N resonances of the proline residues and the interaction with human immunoglobin G,"" FEBS Lett. 269 (1), 174-176 (1990).","15N nuclear magnetic resonance studies of the B domain of Staphylococcal protein A: Sequence specific assignments of the imide 15N resonances of the proline residues and the interaction with human immunoglobin G",published,journal,FEBS Lett.,,269,1,,,,,,,,,,,,,,,,,,,,,,174,176,1990, citations,entry_citation,236,120634,1,,entry citation,,,,,"Dubs, Andreas, Wagner, Gerhard, Wuthrich, Kurt, ""Individual Assignments of Amide Protein Resonances in the Proton NMR Spectrum of the Basic Pancreatic Trypsin Inhibitor,"" Biochim. Biophys. Acta 577, 177-194 (1979).","Individual Assignments of Amide Protein Resonances in the Proton NMR Spectrum of the Basic Pancreatic Trypsin Inhibitor",published,journal,Biochim. Biophys. Acta,,577,,,,,,,,,,,,,,,,,,,,,,,177,194,1979, citations,entry_citation,2366,120647,1,,entry citation,,,,,"Moore, Geoffrey R., Williams, Robert J. P., Chien, James C.W., Dickinson, L.Charles, ""Nuclear Magnetic Resonance Studies of Metal Substituted Horse Cytochrome c,"" J. Inorg. Biochem. 12, 1-15 (1980).",Nuclear Magnetic Resonance Studies of Metal Substituted Horse Cytochrome c,published,journal,J. Inorg. Biochem.,,12,,,,,,,,,,,,,,,,,,,,,,,1,15,1980, citations,entry_citation,2367,120663,1,,entry citation,,,,,"Moore, Geoffrey R., Williams, Robert J. P., Chien, James C.W., Dickinson, L.Charles, ""Nuclear Magnetic Resonance Studies of Metal Substituted Horse Cytochrome c,"" J. Inorg. Biochem. 12, 1-15 (1980).",Nuclear Magnetic Resonance Studies of Metal Substituted Horse Cytochrome c,published,journal,J. Inorg. Biochem.,,12,,,,,,,,,,,,,,,,,,,,,,,1,15,1980, citations,entry_citation,2368,120679,1,,entry citation,,,,,"Moore, Geoffrey R., Williams, Robert J. P., Chien, James C.W., Dickinson, L.Charles, ""Nuclear Magnetic Resonance Studies of Metal Substituted Horse Cytochrome c,"" J. Inorg. Biochem. 12, 1-15 (1980).",Nuclear Magnetic Resonance Studies of Metal Substituted Horse Cytochrome c,published,journal,J. Inorg. Biochem.,,12,,,,,,,,,,,,,,,,,,,,,,,1,15,1980, citations,entry_citation,237,120693,1,,entry citation,,,,,"Nagayama, Kuniaki, Wuthrich, Kurt, ""Systematic Application of Two-Dimensional 1H Nuclear-Magnetic-Resonance Techniques for Studies of Proteins 1. Combined Use of Spin-Echo-Correlated Spectroscopy and J-Resolved Spectroscopy for the Identification of Complete Spin Systems of,"" Eur. J. Biochem. 114, 365-374 (1981).","Systematic Application of Two-Dimensional 1H Nuclear-Magnetic-Resonance Techniques for Studies of Proteins 1. Combined Use of Spin-Echo-Correlated Spectroscopy and J-Resolved Spectroscopy for the Identification of Complete Spin Systems of",published,journal,Eur. J. Biochem.,,114,,,,,,,,,,,,,,,,,,,,,,,365,374,1981, citations,entry_citation,2371,120706,1,,entry citation,,,,,"van Nuland, Nico A.J., van Dijk, Alard A., Dijkstra, Klaas, van Hoesel, Frans H.J., Scheek, Ruud M., Robillard, G.T., ""Three-Dimensional 15N-1H-1H and 15N-13C-1H nuclear-magnetic resonance studies of HPr a central component of the phosphoenolpyruvate-dependent phosphotransferase system from Escherichia coli,"" Eur. J. Biochem. 203, 483-491 (1992).","Three-Dimensional 15N-1H-1H and 15N-13C-1H nuclear-magnetic resonance studies of HPr a central component of the phosphoenolpyruvate-dependent phosphotransferase system from Escherichia coli",published,journal,Eur. J. Biochem.,,203,,,,,,,,,,,,,,,,,,,,,,,483,491,1992, citations,citation_1,25232,125139,2,,reference citation,,,,,,The ERCC1 mutation F231L causes dissociation of the Nucleotide Excision Repair complex ERCC1-XPF,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,238,120719,1,,entry citation,,,,,"Gooley, Paul R., Blunt, John W., Beress, Lazlo, Norton, Ted R., Norton, Raymond S., ""Assignment of Aromatic Resonances in the H1 Nuclear Magnetic Resonance Spectra of Cardioactive Polypeptides from Sea Anemones,"" J. Biol. Chem. 261 (4), 1536-1541 (1986).","Assignment of Aromatic Resonances in the H1 Nuclear Magnetic Resonance Spectra of Cardioactive Polypeptides from Sea Anemones",published,journal,J. Biol. Chem.,,261,4,,,,,,,,,,,,,,,,,,,,,,1536,1541,1986, citations,entry_citation,2384,120732,1,,entry citation,,,,,"Carr, Mark D., ""1H NMR-Based Determination of the Secondary Structure of Porcine Pancreatic Spasmolytic Polypeptide: One of a New Family of ""Trefoil"" Motif Containing Cell Growth Factors,"" Biochemistry 31 (7), 1998-2004 (1992).","1H NMR-Based Determination of the Secondary Structure of Porcine Pancreatic Spasmolytic Polypeptide: One of a New Family of ""Trefoil"" Motif Containing Cell Growth Factors",published,journal,Biochemistry,,31,7,,,,,,,,,,,,,,,,,,,,,,1998,2004,1992, citations,entry_citation,239,120745,1,,entry citation,,,,,"Gooley, Paul R., Blunt, John W., Beress, Lazlo, Norton, Ted R., Norton, Raymond S., ""Assignment of Aromatic Resonances in the H1 Nuclear Magnetic Resonance Spectra of Cardioactive Polypeptides from Sea Anemones,"" J. Biol. Chem. 261 (4), 1536-1541 (1986).","Assignment of Aromatic Resonances in the H1 Nuclear Magnetic Resonance Spectra of Cardioactive Polypeptides from Sea Anemones",published,journal,J. Biol. Chem.,,261,4,,,,,,,,,,,,,,,,,,,,,,1536,1541,1986, citations,entry_citation,2395,120758,1,,entry citation,,,,,"Gooley, Paul R., MacKenzie, Neil E., ""Location of an alpha-Helix in Fragment 96-133 from Bovine Somatotropin by 1H NMR Spectroscopy,"" Biochemistry 27 (11), 4032-4040 (1988).","Location of an alpha-Helix in Fragment 96-133 from Bovine Somatotropin by 1H NMR Spectroscopy",published,journal,Biochemistry,,27,11,,,,,,,,,,,,,,,,,,,,,,4032,4040,1988, citations,entry_citation,2396,120771,1,,entry citation,,,,,"Penington, Christopher J., Rule, Gordon S., ""Mapping the Substrate-Binding Site of a Human Class Mu Glutathione Transferase Using Nuclear Magnetic Resonance Spectroscopy,"" Biochemistry 31 (11), 2912-2920 (1992).","Mapping the Substrate-Binding Site of a Human Class Mu Glutathione Transferase Using Nuclear Magnetic Resonance Spectroscopy",published,journal,Biochemistry,,31,11,,,,,,,,,,,,,,,,,,,,,,2912,2920,1992, citations,entry_citation,24,120784,1,,entry citation,,,,,"Clore, G. Marius, Martin, Stephen R., Gronenborn, Angela M., ""Solution Structure of Human Growth Hormone Releasing Factor (Combined Use of Circular Dichroism and Nuclear Magnetic Resonance Spectroscopy),"" J. Mol. Biol. 191, 553-561 (1986).","Solution Structure of Human Growth Hormone Releasing Factor (Combined Use of Circular Dichroism and Nuclear Magnetic Resonance Spectroscopy)",published,journal,J. Mol. Biol.,,191,,,,,,,,,,,,,,,,,,,,,,,553,561,1986, citations,entry_citation,240,120799,1,,entry citation,,,,,"Gooley, Paul R., Blunt, John W., Beress, Lazlo, Norton, Ted R., Norton, Raymond S., ""Assignment of Aromatic Resonances in the H1 Nuclear Magnetic Resonance Spectra of Cardioactive Polypeptides from Sea Anemones,"" J. Biol. Chem. 261 (4), 1536-1541 (1986).","Assignment of Aromatic Resonances in the H1 Nuclear Magnetic Resonance Spectra of Cardioactive Polypeptides from Sea Anemones",published,journal,J. Biol. Chem.,,261,4,,,,,,,,,,,,,,,,,,,,,,1536,1541,1986, citations,entry_citation,241,120812,1,,entry citation,,,,,"Gooley, Paul R., Blunt, John W., Beress, Lazlo, Norton, Ted R., Norton, Raymond S., ""Assignment of Aromatic Resonances in the H1 Nuclear Magnetic Resonance Spectra of Cardioactive Polypeptides from Sea Anemones,"" J. Biol. Chem. 261 (4), 1536-1541 (1986).","Assignment of Aromatic Resonances in the H1 Nuclear Magnetic Resonance Spectra of Cardioactive Polypeptides from Sea Anemones",published,journal,J. Biol. Chem.,,261,4,,,,,,,,,,,,,,,,,,,,,,1536,1541,1986, citations,entry_citation,2410,120825,1,,entry citation,,,,,,"Letter to the Editor: Sequence-specific 1H, 15N, and 13C assignment of the N-terminal domain of the human oncoprotein MDM2 that binds to p53",published,journal,J. Biomol. NMR,,17,1,,,,,,,,,,,,,,,,,,,,,,91,92,2000, citations,entry_citation,242,120842,1,,entry citation,,,,,"Gooley, Paul R., Blunt, John W., Beress, Lazlo, Norton, Ted R., Norton, Raymond S., ""Assignment of Aromatic Resonances in the H1 Nuclear Magnetic Resonance Spectra of Cardioactive Polypeptides from Sea Anemones,"" J. Biol. Chem. 261 (4), 1536-1541 (1986).","Assignment of Aromatic Resonances in the H1 Nuclear Magnetic Resonance Spectra of Cardioactive Polypeptides from Sea Anemones",published,journal,J. Biol. Chem.,,261,4,,,,,,,,,,,,,,,,,,,,,,1536,1541,1986, citations,entry_citation,2425,120855,1,,entry citation,,,,,"Kuwajima, Kunihiro, Baldwin, Robert L., ""Nature and Locations of the Most Slowly Exchanging Peptide NH Protons in Residues 1 to 19 of Ribonuclease S,"" Mol. Biol. 169, 281-297 (1983).","Nature and Locations of the Most Slowly Exchanging Peptide NH Protons in Residues 1 to 19 of Ribonuclease S",published,journal,Mol. Biol.,,169,,,,,,,,,,,,,,,,,,,,,,,281,297,1983, citations,entry_citation,2426,120868,1,,entry citation,,,,,"Kuwajima, Kunihiro, Baldwin, Robert L., ""Nature and Locations of the Most Slowly Exchanging Peptide NH Protons in Residues 1 to 19 of Ribonuclease S,"" Mol. Biol. 169, 281-297 (1983).","Nature and Locations of the Most Slowly Exchanging Peptide NH Protons in Residues 1 to 19 of Ribonuclease S",published,journal,Mol. Biol.,,169,,,,,,,,,,,,,,,,,,,,,,,281,297,1983, citations,entry_citation,243,120881,1,,entry citation,,,,,"Wand, A. Joshua, Englander, S. Walter, ""Two-Dimensional 1H NMR Studies of Cytochrome c: Assignment of the N-Terminal Helix,"" Biochemistry 25, 1100-1106 (1986).","Two-Dimensional 1H NMR Studies of Cytochrome c: Assignment of the N-Terminal Helix",published,journal,Biochemistry,,25,,,,,,,,,,,,,,,,,,,,,,,1100,1106,1986, citations,entry_citation,2431,120894,1,,entry citation,,,,,"La Mar, Gerd N., Emerson, S. Donald, Lecomte, Juliette T.J., Pande, Usha, Smith, Kevin M., Craig, G. Wayne, Kehres, Lisa A., ""Influence of Propionate Side Chains on the Equilibrium Heme Orientation in Sperm Whale Myoglobin. Heme Resonance Assignments and Structure Determination by Nuclear Overhauser Effect Measurements,"" J. Am. Chem. Soc. 108 (18), 5568-5573 (1986).","Influence of Propionate Side Chains on the Equilibrium Heme Orientation in Sperm Whale Myoglobin. Heme Resonance Assignments and Structure Determination by Nuclear Overhauser Effect Measurements",published,journal,J. Am. Chem. Soc.,,108,18,,,,,,,,,,,,,,,,,,,,,,5568,5573,1986, citations,entry_citation,2432,120907,1,,entry citation,,,,,"La Mar, Gerd N., Emerson, S. Donald, Lecomte, Juliette T.J., Pande, Usha, Smith, Kevin M., Craig, G. Wayne, Kehres, Lisa A., ""Influence of Propionate Side Chains on the Equilibrium Heme Orientation in Sperm Whale Myoglobin. Heme Resonance Assignments and Structure Determination by Nuclear Overhauser Effect Measurements,"" J. Am. Chem. Soc. 108 (18), 5568-5573 (1986).","Influence of Propionate Side Chains on the Equilibrium Heme Orientation in Sperm Whale Myoglobin. Heme Resonance Assignments and Structure Determination by Nuclear Overhauser Effect Measurements",published,journal,J. Am. Chem. Soc.,,108,18,,,,,,,,,,,,,,,,,,,,,,5568,5573,1986, citations,entry_citation,25030,121805,1,,entry citation,,,25135663,,,The periplasmic domain of Escherichia coli outer membrane protein A can undergo a localized temperature dependent structural transition,published,journal,Biochim. Biophys. Acta,,,,,,,,,,,,,,,,,,,,,,,,,,,2014, citations,entry_citation,2433,120920,1,,entry citation,,,,,"La Mar, Gerd N., Emerson, S. Donald, Lecomte, Juliette T.J., Pande, Usha, Smith, Kevin M., Craig, G. Wayne, Kehres, Lisa A., ""Influence of Propionate Side Chains on the Equilibrium Heme Orientation in Sperm Whale Myoglobin. Heme Resonance Assignments and Structure Determination by Nuclear Overhauser Effect Measurements,"" J. Am. Chem. Soc. 108 (18), 5568-5573 (1986).","Influence of Propionate Side Chains on the Equilibrium Heme Orientation in Sperm Whale Myoglobin. Heme Resonance Assignments and Structure Determination by Nuclear Overhauser Effect Measurements",published,journal,J. Am. Chem. Soc.,,108,18,,,,,,,,,,,,,,,,,,,,,,5568,5573,1986, citations,entry_citation,2434,120933,1,,entry citation,,,,,"La Mar, Gerd N., Emerson, S. Donald, Lecomte, Juliette T.J., Pande, Usha, Smith, Kevin M., Craig, G. Wayne, Kehres, Lisa A., ""Influence of Propionate Side Chains on the Equilibrium Heme Orientation in Sperm Whale Myoglobin. Heme Resonance Assignments and Structure Determination by Nuclear Overhauser Effect Measurements,"" J. Am. Chem. Soc. 108 (18), 5568-5573 (1986).","Influence of Propionate Side Chains on the Equilibrium Heme Orientation in Sperm Whale Myoglobin. Heme Resonance Assignments and Structure Determination by Nuclear Overhauser Effect Measurements",published,journal,J. Am. Chem. Soc.,,108,18,,,,,,,,,,,,,,,,,,,,,,5568,5573,1986, citations,entry_citation,2435,120946,1,,entry citation,,,,,"Ikura, Mitsuhiko, Hiraoki, Toshifumi, Hikichi, Kunio, Mikuni, Toshiaki, Yazawa, Michio, Yagi, Koichi, ""Nuclear Magnetic Resonance Studies on Calmodulin: Calcium-Induced Conformational Change,"" Biochemistry 22 (10), 2573-2579 (1983).",Nuclear Magnetic Resonance Studies on Calmodulin: Calcium-Induced Conformational Change,published,journal,Biochemistry,,22,10,,,,,,,,,,,,,,,,,,,,,,2573,2579,1983, citations,entry_citation,2436,120958,1,,entry citation,,,,,"Ikura, Mitsuhiko, Hiraoki, Toshifumi, Hikichi, Kunio, Mikuni, Toshiaki, Yazawa, Michio, Yagi, Koichi, ""Nuclear Magnetic Resonance Studies on Calmodulin: Calcium-Induced Conformational Change,"" Biochemistry 22 (10), 2573-2579 (1983).","Nuclear Magnetic Resonance Studies on Calmodulin: Calcium-Induced Conformational Change",published,journal,Biochemistry,,22,10,,,,,,,,,,,,,,,,,,,,,,2573,2579,1983, citations,entry_citation,2437,120970,1,,entry citation,,,,,"Ikura, Mitsuhiko, Hiraoki, Toshifumi, Hikichi, Kunio, Mikuni, Toshiaki, Yazawa, Michio, Yagi, Koichi, ""Nuclear Magnetic Resonance Studies on Calmodulin: Calcium-Induced Conformational Change,"" Biochemistry 22 (10), 2573-2579 (1983).",Nuclear Magnetic Resonance Studies on Calmodulin: Calcium-Induced Conformational Change,published,journal,Biochemistry,,22,10,,,,,,,,,,,,,,,,,,,,,,2573,2579,1983, citations,entry_citation,2438,120982,1,,entry citation,,,,,"Ikura, Mitsuhiko, Hiraoki, Toshifumi, Hikichi, Kunio, Mikuni, Toshiaki, Yazawa, Michio, Yagi, Koichi, ""Nuclear Magnetic Resonance Studies on Calmodulin: Calcium-Induced Conformational Change,"" Biochemistry 22 (10), 2573-2579 (1983).","Nuclear Magnetic Resonance Studies on Calmodulin: Calcium-Induced Conformational Change",published,journal,Biochemistry,,22,10,,,,,,,,,,,,,,,,,,,,,,2573,2579,1983, citations,entry_citation,2439,120995,1,,entry citation,,,,,"Ikura, Mitsuhiko, Hiraoki, Toshifumi, Hikichi, Kunio, Mikuni, Toshiaki, Yazawa, Michio, Yagi, Koichi, ""Nuclear Magnetic Resonance Studies on Calmodulin: Calcium-Induced Conformational Change,"" Biochemistry 22 (10), 2573-2579 (1983).","Nuclear Magnetic Resonance Studies on Calmodulin: Calcium-Induced Conformational Change",published,journal,Biochemistry,,22,10,,,,,,,,,,,,,,,,,,,,,,2573,2579,1983, citations,entry_citation,244,121008,1,,entry citation,,,,,"Wand, A. Joshua, Englander, S. Walter, ""Two-Dimensional 1H NMR Studies of Cytochrome c: Assignment of the N-Terminal Helix,"" Biochemistry 25, 1100-1106 (1986).","Two-Dimensional 1H NMR Studies of Cytochrome c: Assignment of the N-Terminal Helix",published,journal,Biochemistry,,25,,,,,,,,,,,,,,,,,,,,,,,1100,1106,1986, citations,entry_citation,2440,121021,1,,entry citation,,,,,"Ikura, Mitsuhiko, Hiraoki, Toshifumi, Hikichi, Kunio, Mikuni, Toshiaki, Yazawa, Michio, Yagi, Koichi, ""Nuclear Magnetic Resonance Studies on Calmodulin: Calcium-Induced Conformational Change,"" Biochemistry 22 (10), 2573-2579 (1983).","Nuclear Magnetic Resonance Studies on Calmodulin: Calcium-Induced Conformational Change",published,journal,Biochemistry,,22,10,,,,,,,,,,,,,,,,,,,,,,2573,2579,1983, citations,entry_citation,2442,121034,1,,entry citation,,,,,"Limmer, Stefan, Reiser, Christian O.A., Schirmer, Norbert K., Grillenbeck, Norbert W., Sprinzl, Mathias, ""Nucleotide Binding and GTP Hydrolysis by Elongation Factor Tu from Thermus thermophilus As Monitored by Proton NMR,"" Biochemistry 31 (11), 2970-2977 (1992).","Nucleotide Binding and GTP Hydrolysis by Elongation Factor Tu from Thermus thermophilus As Monitored by Proton NMR",published,journal,Biochemistry,,31,11,,,,,,,,,,,,,,,,,,,,,,2970,2977,1992, citations,entry_citation,2443,121047,1,,entry citation,,,,,"Limmer, Stefan, Reiser, Christian O.A., Schirmer, Norbert K., Grillenbeck, Norbert W., Sprinzl, Mathias, ""Nucleotide Binding and GTP Hydrolysis by Elongation Factor Tu from Thermus thermophilus As Monitored by Proton NMR,"" Biochemistry 31 (11), 2970-2977 (1992).","Nucleotide Binding and GTP Hydrolysis by Elongation Factor Tu from Thermus thermophilus As Monitored by Proton NMR",published,journal,Biochemistry,,31,11,,,,,,,,,,,,,,,,,,,,,,2970,2977,1992, citations,entry_citation,2446,121060,1,,entry citation,,,,,"Delepierre, Muriel, Dobson, Christopher M., Poulsen, Flemming M., ""Studies of beta-Sheet Structure in Lysozyme by Proton Nuclear Magnetic Resonance. Assignments and Analysis of Spin-Spin Coupling Constants,"" Biochemistry 21 (19), 4756-4761 (1982).","Studies of beta-Sheet Structure in Lysozyme by Proton Nuclear Magnetic Resonance. Assignments and Analysis of Spin-Spin Coupling Constants",published,journal,Biochemistry,,21,19,,,,,,,,,,,,,,,,,,,,,,4756,4761,1982, citations,entry_citation,245,121073,1,,entry citation,,,,,"Inagaki, Fuyuhiko, Shimada, Ichio, Kawaguchi, Ken, Hirano, Masahiko, Terasawa, Isao, Ikura, Teikichi, Go, Nobuhiro, ""Structure of Melittin Bound to Perdeuterated Dodecylphosphocholine Micelles As Studied by Two-Dimensional NMR and Distance Geometry Calculations,"" Biochemistry 28, 5985-5991 (1989).","Structure of Melittin Bound to Perdeuterated Dodecylphosphocholine Micelles As Studied by Two-Dimensional NMR and Distance Geometry Calculations",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,5985,5991,1989, citations,entry_citation,2454,121087,1,,entry citation,,,,,"Mayo, Kevin H., Tyrell, P.M., Prestegard, J.H., ""Acyl Carrier Protein from Escherichia coli I. Aspects of the Solution Structure As Evidenced by Proton Nuclear Overhauser Experiments at 500 MHz,"" Biochemistry 22 (19), 4485-4493 (1983).",Acyl Carrier Protein from Escherichia coli I. Aspects of the Solution Structure As Evidenced by Proton Nuclear Overhauser Experiments at 500 MHz,published,journal,Biochemistry,,22,19,,,,,,,,,,,,,,,,,,,,,,4485,4493,1983, citations,entry_citation,2455,121099,1,,entry citation,,,,,"De Marco, A., Menegatti, Enea, Guarneri, Mario, ""pH and Temperature Effects on the Molecular Conformation of the Porcine Pancreatic Secretory Trypsin Inhibitor As Detected by Hydrogen-1 Nuclear Magnetic Resonance,"" Biochemistry 21 (2), 222-229 (1982).","pH and Temperature Effects on the Molecular Conformation of the Porcine Pancreatic Secretory Trypsin Inhibitor As Detected by Hydrogen-1 Nuclear Magnetic Resonance",published,journal,Biochemistry,,21,2,,,,,,,,,,,,,,,,,,,,,,222,229,1982, citations,entry_citation,2457,121112,1,,entry citation,,,,,"Strop, Petr, Cechova, Dana, Wuthrich, Kurt, ""Preliminary Structural Comparison of the Proteinase Isoinhibitors IIA and IIB from Bull Seminal Plasma Based on Individual Assignments of the 1H Nuclear Magnetic Resonance Spectra by Two-dimensional Nuclear Magnetic Resonance at 500 MHz,"" J. Mol. Biol. 166, 669-676 (1983).","Preliminary Structural Comparison of the Proteinase Isoinhibitors IIA and IIB from Bull Seminal Plasma Based on Individual Assignments of the 1H Nuclear Magnetic Resonance Spectra by Two-dimensional Nuclear Magnetic Resonance at 500 MHz",published,journal,J. Mol. Biol.,,166,,,,,,,,,,,,,,,,,,,,,,,669,676,1983, citations,entry_citation,246,121125,1,,entry citation,,,,,"Kohda, Daisuke, Shimada, Ichio, Miyake, Tetsuo, Fuwa, Toru, Inagaki, Fuyuhiko, ""Polypeptide Chain Fold of Human Transforming Growth Factor alpha Analogous to Those of Mouse and Human Epidermal Growth Factors as Studied by Two-Dimensional 1H NMR,"" Biochemistry 28, 953-958 (1989).","Polypeptide Chain Fold of Human Transforming Growth Factor alpha Analogous to Those of Mouse and Human Epidermal Growth Factors as Studied by Two-Dimensional 1H NMR",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,953,958,1989, citations,entry_citation,2463,121136,1,,entry citation,,,,,"Chan, Tze-Ming, Markley, John L., ""Heternuclear (1H,13C) Two-Dimensional Chemical Shift Correlation NMR Spectroscopy of a Protein. Ferredoxin from Anabaena variabilis,"" J. Am. Chem. Soc. 104, 4010-4011 (1982).","Heternuclear (1H,13C) Two-Dimensional Chemical Shift Correlation NMR Spectroscopy of a Protein. Ferredoxin from Anabaena variabilis",published,journal,J. Am. Chem. Soc.,,104,,,,,,,,,,,,,,,,,,,,,,,4010,4011,1982, citations,entry_citation,247,121149,1,,entry citation,,,,,"Kordel, Johan, Forsen, Sture, Chazin, Walter J., ""1H NMR Sequential Resonance Assignments, Secondary Structure, and Global Fold in Solution of the Major (trans-Pro43) Form of Bovine Calbindin D9k,"" Biochemistry 28, 7065-7074 (1989).","1H NMR Sequential Resonance Assignments, Secondary Structure, and Global Fold in Solution of the Major (trans-Pro43) Form of Bovine Calbindin D9k",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,7065,7074,1989, citations,entry_citation,2472,121162,1,,entry citation,,,,,"Gochin, Miriam, Degani, Hadassa, ""1H NMR Studies of a Two-Iron: Two-Sulfur Ferredoxin from Halobacterium of the Dead Sea,"" J. Inorg. Biochem. 25, 151-161 (1985).","1H NMR Studies of a Two-Iron: Two-Sulfur Ferredoxin from Halobacterium of the Dead Sea",published,journal,J. Inorg. Biochem.,,25,,,,,,,,,,,,,,,,,,,,,,,151,161,1985, citations,entry_citation,2473,121175,1,,entry citation,,,,,"De Marco, A., Petros, Andrew M., Llinas, M., Kaptein, Robert, Boelens, Rolf, ""Ligand-binding effects on the kringle 4 domain from human plasminogen: a study by laser photo-CIDNP 1H-NMR spectroscopy,"" Biochim. Biophys. Acta 994, 121-137 (1989).","Ligand-binding effects on the kringle 4 domain from human plasminogen: a study by laser photo-CIDNP 1H-NMR spectroscopy",published,journal,Biochim. Biophys. Acta,,994,,,,,,,,,,,,,,,,,,,,,,,121,137,1989, citations,entry_citation,2474,121188,1,,entry citation,,,,,"De Marco, A., Petros, Andrew M., Llinas, M., Kaptein, Robert, Boelens, Rolf, ""Ligand-binding effects on the kringle 4 domain from human plasminogen: a study by laser photo-CIDNP 1H-NMR spectroscopy,"" Biochim. Biophys. Acta 994, 121-137 (1989).","Ligand-binding effects on the kringle 4 domain from human plasminogen: a study by laser photo-CIDNP 1H-NMR spectroscopy",published,journal,Biochim. Biophys. Acta,,994,,,,,,,,,,,,,,,,,,,,,,,121,137,1989, citations,entry_citation,2475,121201,1,,entry citation,,,,,"De Marco, A., Petros, Andrew M., Llinas, M., Kaptein, Robert, Boelens, Rolf, ""Ligand-binding effects on the kringle 4 domain from human plasminogen: a study by laser photo-CIDNP 1H-NMR spectroscopy,"" Biochim. Biophys. Acta 994, 121-137 (1989).","Ligand-binding effects on the kringle 4 domain from human plasminogen: a study by laser photo-CIDNP 1H-NMR spectroscopy",published,journal,Biochim. Biophys. Acta,,994,,,,,,,,,,,,,,,,,,,,,,,121,137,1989, citations,entry_citation,2476,121214,1,,entry citation,,,,,"Reid, David G., Saunders, Martin, ""A Proton NMR and Nuclear Overhauser Effect (NOE) Study of Human Plasma Prealbumin, Including the Development and Application to Spectral Assignment of a Combined Ring Current Shift and NOE Prediction Program,"" J. Biol. Chem. 264 (4), 2003-2012 (1989).","A Proton NMR and Nuclear Overhauser Effect (NOE) Study of Human Plasma Prealbumin, Including the Development and Application to Spectral Assignment of a Combined Ring Current Shift and NOE Prediction Program",published,journal,J. Biol. Chem.,,264,4,,,,,,,,,,,,,,,,,,,,,,2003,2012,1989, citations,entry_citation,248,121227,1,,entry citation,,,,,"Malikayil, J.A., Lerch, Konrad, Armitage, Ian M., ""Proton NMR Studies of a Metallothionein from Neurospora crassa: Sequence-Specific Assignments by NOE Measurements in the Rotating Frame,"" Biochemistry 28, 2991-2995 (1989).","Proton NMR Studies of a Metallothionein from Neurospora crassa: Sequence-Specific Assignments by NOE Measurements in the Rotating Frame",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,2991,2995,1989, citations,entry_citation,2488,121240,1,,entry citation,,,,,"Satterlee, James D., Avizonis, Daina Z., Moench, Susan J., ""Assignment of hyperfine-shifted resonances in yeast ferricytochrome c isozyme 2 using the proton pre-steady-state nuclear Overhauser effect,"" Biochim. Biophys. 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Biol.,Nature structural & molecular biology,24,2,,1545-9985,,,,,,,,,,,,,,,,,,,,187,193,2017, citations,entry_citation,25711,133625,1,,entry citation,,,,,,Characterization of HLA-b27:05 and :09 complexed with TIS and pVIPR by NMR,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,25712,133645,1,,entry citation,,,26699905,,,"Biochemical and structural characterization of dehydroascorbate reductases from poplar (Populus trichocarpa), enzymes contributing to the maintenance of the ascorbate pool in plants",published,journal,Biochem. 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NMR Assign.,,10,1,,,,,,,,,,,,,,,,,,,,,,121,123,, citations,entry_citation,25731,134014,1,,entry citation,,,,,,Dynamic equilibrium between closed and partially-closed states of the Enzyme I-phosphoenolpyruvate complex from the bacterial phosphotransferase system uncovered by NMR residual dipolar couplings and solution X-ray scattering,in preparation,journal,Proc. Natl. Acad. Sci. U.S.A.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,25732,134031,1,,entry citation,,,27033306,,,The cyanobacterial cytochrome b6f subunit PetP adopts an SH3 fold in solution,published,journal,Biochim. Biophys. Acta,,1857,6,,,,,,,,,,,,,,,,,,,,,,705,714,2016, citations,entry_citation,25734,134050,1,,entry citation,,,27370208,,,Recruitment of TBK1 to cytosol-invading Salmonella induces WIPI2-dependent antibacterial autophagy,published,journal,EMBO J.,The EMBO journal,35,16,,1460-2075,,,,,,,,,,,,,,,,,,,,1779,1792,2016, citations,entry_citation,25735,134068,1,,entry citation,,,26451915,,,The Autophagy Receptor TAX1BP1 and the Molecular Motor Myosin VI Are Required for Clearance of Salmonella Typhimurium by Autophagy,published,journal,PLoS Pathog.,PLoS pathogens,11,10,,1553-7374,,,,,,,,,,,,,,,,,,,,e1005174,e1005174,2015, citations,entry_citation,25736,134086,1,,entry citation,,,27370208,,,Recruitment of TBK1 to cytosol-invading Salmonella induces WIPI2-dependent antibacterial autophagy,published,journal,EMBO J.,The EMBO journal,35,16,,1460-2075,,,,,,,,,,,,,,,,,,,,1779,1792,2016, citations,entry_citation,25737,134104,1,,entry citation,,,27688760,,,Antimicrobial lipopeptide tridecaptin A1 selectively binds to Gram-negative lipid II.,published,journal,Proc. 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U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,113,41,,1091-6490,,,,,,,,,,,,,,,,,,,,11561,11566,2016, citations,entry_citation,25742,134212,1,,entry citation,,,27370208,,,Recruitment of TBK1 to cytosol-invading Salmonella induces WIPI2-dependent antibacterial autophagy,published,journal,EMBO J.,The EMBO journal,35,16,,1460-2075,,,,,,,,,,,,,,,,,,,,1779,1792,2016, citations,entry_citation,25743,134230,1,,entry citation,,,26542424,,,Backbone and side-chain NMR assignments for the bromodomain of mouse BAZ1A (ACF1),published,journal,Biomol. NMR Assign.,,10,1,,,,,,,,,,,,,,,,,,,,,,131,134,2016, citations,entry_citation,25744,134244,1,,entry citation,,,26576056,,,NMR Structure and Dynamics of the Resuscitation Promoting Factor RpfC Catalytic Domain,published,journal,PLoS One,,10,11,,,,,,,,,,,,,,,,,,,,,,e0142807,e0142807,2015, citations,entry_citation,25745,134261,1,,entry citation,,,26434928,,,Structure of the N-terminal domain of the metalloprotease PrtV from Vibrio cholerae,published,journal,Protein Sci.,,24,12,,,,,,,,,,,,,,,,,,,,,,2076,2080,2015, citations,entry_citation,25746,134278,1,,entry citation,,,26673723,,,G-quadruplexes with (4n - 1) guanines in the G-tetrad core: formation of a G-triadwater complex and implication for small-molecule binding,published,journal,Nucleic Acids Res.,,44,2,,,,,,,,,,,,,,,,,,,,,,910,916,2016, citations,citation_1,25748,134300,1,,entry citation,,,27466710,,,A strategy for co-translational folding studies of ribosome-bound nascent chain complexes using NMR spectroscopy,published,journal,Nat. 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Chem.,,291,37,,,,,,,,,,,,,,,,,,,,,,19487,19501,2016, citations,entry_citation,25944,137820,1,,entry citation,,,28522546,,,The RxLR Motif of the Host Targeting Effector AVR3a of Phytophthora infestans Is Cleaved before Secretion.,published,journal,Plant Cell,The Plant cell,29,6,,1532-298X,,,,,,,,,,,,,,,,,,,,1184,1195,2017, citations,entry_citation,25945,137837,1,,entry citation,,,26988723,,,"(1)H, (13)C and (15)N resonance assignments of the Cdc42-binding domain of TOCA1",published,journal,Biomol NMR Assign.,,10,2,,,,,,,,,,,,,,,,,,,,,,407,411,2016, citations,entry_citation,25946,137871,1,,entry citation,,,27137928,,,Role of Aromatic Amino Acids in Lipopolysaccharide and Membrane Interactions of Antimicrobial Peptides for Use in Plant Disease Control,published,journal,J. Biol. 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Chem.,,291,25,,,,,,,,,,,,,,,,,,,,,,13301,13317,2016, citations,entry_citation,25948,137899,1,,entry citation,,,,,,GLP-1 and exendin-4 alpha-conotoxin pl14a chimeras as potent GLP1-R agonists,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,25949,137918,1,,entry citation,,,,,,GLP-1 and exendin-4 alpha-conotoxin pl14a chimeras as potent GLP-1R agonists,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,25950,137936,1,,entry citation,,,26845253,,,Anomer-Specific Recognition and Dynamics in a Fucose-Binding Lectin,published,journal,Biochemistry,,55,8,,,,,,,,,,,,,,,,,,,,,,1195,1203,2016, citations,entry_citation,25951,137954,1,,entry citation,,,26845253,,,Anomer-Specific Recognition and Dynamics in a Fucose-Binding Lectin,published,journal,Biochemistry,,55,8,,,,,,,,,,,,,,,,,,,,,,1195,1203,2016, citations,entry_citation,25952,137973,1,,entry citation,,,26845253,,,Anomer-Specific Recognition and Dynamics in a Fucose-Binding Lectin,published,journal,Biochemistry,,55,8,,,,,,,,,,,,,,,,,,,,,,1195,1203,2016, citations,entry_citation,25953,137989,1,,entry citation,,,27780845,,,The C-terminus of Pcf11 forms a novel zinc-finger structure that plays an essential role in mRNA 3'- end processing,published,journal,RNA,,23,1,,,,,,,,,,,,,,,,,,,,,,98,107,2017, citations,entry_citation,25954,138015,1,,entry citation,,,,,,Bt1.8 peptide,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,25955,138030,1,,entry citation,,,27432510,,,The anti-sigma factor RsrA responds to oxidative stress by reburying its hydrophobic core,published,journal,Nat. 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Commun.,,7,,,,,,,,,,,,,,,,,,,,,,,12194,12194,2016, citations,entry_citation,25957,138062,1,,entry citation,,,28072824,,,"D19S Mutation of the Cationic, Cysteine-Rich Protein PAF: Novel Insights into Its Structural Dynamics, Thermal Unfolding and Antifungal Function",published,journal,Plos One,,12,1,,,,,,,,,,,,,,,,,,,,,,e0169920,e0169920,2017, citations,citations,25958,138081,1,,entry citation,,,27716744,,,Mechanism of TAp73 inhibition by Delta Np63 and structural basis of p63/p73 hetero-tetramerization,published,journal,Cell Death Differ.,,23,12,,,,,,,,,,,,,,,,,,,,,,1930,1940,2016, citations,entry_citation,25959,138110,1,,entry citation,,,,,,A novel type of hairpin-like defense peptides from blackseed (Nigella sativa L.) contains three disulfide bridges,in preparation,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,25961,138132,1,,entry citation,,,26917351,,,Solution structure of Q388A3 PDZ domain from Trypanosoma brucei,published,journal,J. Struct. 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NMR Assignments,,10,2,,,,,,,,,,,,,,,,,,,,,,287,290,2016, citations,entry_citation,25969,138266,1,,entry citation,,,27161979,,,A Comparative Structure/Function Analysis of Two Type IV Pilin DNA Receptors Defines a Novel Mode of DNA Binding,published,journal,Structure,,24,6,,,,,,,,,,,,,,,,,,,,,,926,934,2016, citations,entry_citation,25970,138280,1,,entry citation,,,27081926,,,The acidic domain is a unique structural feature of the splicing factor SYNCRIP,published,journal,Protein Sci.,,25,8,,,,,,,,,,,,,,,,,,,,,,1545,1550,2016, citations,entry_citation,25971,138295,1,,entry citation,,,27474999,,,Isolation and characterization of a structurally unique beta-hairpin venom peptide from the predatory ant Anochetus emarginatus,published,journal,Biochim. Biophys. Acta,,1860,11,,,,,,,,,,,,,,,,,,,,,,2553,2562,2016, citations,entry_citation,25972,138314,1,,entry citation,,,27111887,,,Observing a late folding intermediate of Ubiquitin at atomic resolution by NMR,published,journal,Protein Sci.,,25,8,,,,,,,,,,,,,,,,,,,,,,1438,1450,2016, citations,entry_citation,25973,138328,1,,entry citation,,,27111887,,,Observing a late folding intermediate of Ubiquitin at atomic resolution by NMR,published,journal,Protein Sci.,,25,8,,,,,,,,,,,,,,,,,,,,,,1438,1450,2016, citations,entry_citation,25974,138342,1,,entry citation,,,30321182,,,"Calcium binding of the antifungal protein PAF: Structure, dynamics and function aspects by NMR and MD simulations.",published,journal,PLoS ONE,PloS one,13,10,,1932-6203,,,,,,,,,,,,,,,,,,,,e0204825,e0204825,2018, citations,entry_citation,25975,138362,1,,entry citation,,,27364543,,,A model for the interaction of the G3-subdomain of Geobacillus stearothermophilus IF2 with the 30S ribosomal subunit,published,journal,Protein Sci.,,25,9,,,,,,,,,,,,,,,,,,,,,,1722,1733,2016, citations,entry_citation,25976,138381,1,,entry citation,,,,,,Structure of a fungal hydrophobin,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,25979,138398,1,,entry citation,,,28598414,,,Structure of the Rpn13-Rpn2 complex provides insights for Rpn13 and Uch37 as anticancer targets.,published,journal,Nat. 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Struct. Mol. Biol.,Nature structural & molecular biology,24,4,,1545-9985,,,,,,,,,,,,,,,,,,,,407,413,2017, citations,entry_citation,25987,138527,1,,entry citation,,,27885756,,,Structure of Monomeric Transthyretin Carrying the Clinically Important T119M Mutation.,published,journal,Angew. Chem. Int. Ed. 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Cell,Molecular cell,62,2,MOCEFL,1097-2765,2168,,,,,,,,,,,,,,,,,,,260,271,2016, citations,entry_citation,26016,139126,1,,entry citation,,,29642029,10.1016/j.bpj.2017.12.030,,Structural Basis of Protein Kinase Calpha Regulation by the C-Terminal Tail.,published,journal,Biophys. J.,Biophysical journal,114,7,,1542-0086,,,,,,,,,,,,,,,,,,,,1590,1603,2018, citations,entry_citation,26021,139150,1,,entry citation,,,27791121,,,The CC domain structure from the wheat stem rust resistance protein Sr33 challenges paradigms for dimerization in plant NLR proteins,published,journal,Proc. Natl. Acad. Sci. 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NMR Assign.,,10,2,,,,,,,,,,,,,,,,,,,,,,401,406,2016, citations,entry_citation,26031,139339,1,,entry citation,,,27532772,,,Mitochondrial Bol1 and Bol3 function as assembly factors for specific iron-sulfur proteins,published,journal,eLife,,5,,,,,,,,,,,,,,,,,,,,,,,e16673,e16673,2016, citations,entry_citation,26032,139363,1,,entry citation,,,,,,Structural insights reveal the dynamics of the repeating r(CGG) motif found in Fragile X Syndrome and Fragile-X associated tremor/ataxia syndrome (FXTAS),in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,26033,139379,1,,entry citation,,,,,,Structural insights reveal the dynamics of the repeating r(CGG) motif found in Fragile X Syndrome and Fragile-X associated tremor/ataxia syndrome (FXTAS),in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,26034,139395,1,,entry citation,,,27905530,,,Structural basis for broad neutralization of HIV-1 through the molecular recognition of 10E8 helical epitope at the membrane interface,published,journal,Sci Rep,Scientific reports,6,,,2045-2322,,,,,,,,,,,,,,,,,,,,38177,38177,2016, citations,entry_citation,26035,139414,1,,entry citation,,,27905530,,,Structural basis for broad neutralization of HIV-1 through the molecular recognition of 10E8 helical epitope at the membrane interface,published,journal,Sci Rep,Scientific reports,6,,,2045-2322,,,,,,,,,,,,,,,,,,,,38177,38177,2016, citations,citation_1,26036,139435,1,,entry citation,,,28303012,,,Tryptophan end-tagging for promoted lipopolysaccharide interactions and anti-inflammatory effects.,published,journal,Sci. 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NMR Assign.,,10,2,,,,,,,,,,,,,,,,,,,,,,335,339,2016, citations,entry_citation,26045,139592,1,,entry citation,,,27626386,,,Accurate de novo design of hyperstable constrained peptides.,published,journal,Nature,,538,7625,NATUAS,1476-4687,,,,,,,,,,,,,,,,,,,,329,335,2016, citations,entry_citation,26046,139616,1,,entry citation,,,27626386,,,Accurate de novo design of hyperstable constrained peptides.,published,journal,Nature,,538,7625,NATUAS,1476-4687,,,,,,,,,,,,,,,,,,,,329,335,2016, citations,citation_1,26047,139640,1,,entry citation,,,,,,NMR Observation of Protein Surface Salt Bridges at Neutral pH,in preparation,journal,J. Am. Chem. Soc.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,26048,139658,1,,entry citation,,,27614467,,,"(1)H, (13)C, (15)N backbone and side-chain resonance assignment of Nostoc sp. C139A variant of the heme-nitric oxide/oxygen binding (H-NOX) domain",published,journal,Biomol. 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L., Farr-Jones, Shauna, Shenvi, Ashok B., Kettner, Charles A., ""Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes,"" Biochemistry 27 (20), 7689-7697 (1988).","Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes",published,journal,Biochemistry,,27,20,,,,,,,,,,,,,,,,,,,,,,7689,7697,1988, citations,entry_citation,2609,140065,1,,entry citation,,,,,"Bachovchin, William W., Wong, Winona Y. L., Farr-Jones, Shauna, Shenvi, Ashok B., Kettner, Charles A., ""Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes,"" Biochemistry 27 (20), 7689-7697 (1988).","Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes",published,journal,Biochemistry,,27,20,,,,,,,,,,,,,,,,,,,,,,7689,7697,1988, citations,entry_citation,261,140078,1,,entry citation,,,,,"Chazin, Walter J., Wright, Peter E., ""Complete Assignment of the 1H Nuclear Magnetic Resonance Spectrum of French Bean Plastocyanin: Sequential Resonance Assignments, Secondary Structure and Global Fold,"" J. Mol. Biol. 202, 623-636 (1988).","Complete Assignment of the 1H Nuclear Magnetic Resonance Spectrum of French Bean Plastocyanin: Sequential Resonance Assignments, Secondary Structure and Global Fold",published,journal,J. Mol. Biol.,,202,,,,,,,,,,,,,,,,,,,,,,,623,636,1988, citations,entry_citation,2610,140091,1,,entry citation,,,,,"Bachovchin, William W., Wong, Winona Y. L., Farr-Jones, Shauna, Shenvi, Ashok B., Kettner, Charles A., ""Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes,"" Biochemistry 27 (20), 7689-7697 (1988).","Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes",published,journal,Biochemistry,,27,20,,,,,,,,,,,,,,,,,,,,,,7689,7697,1988, citations,entry_citation,2611,140104,1,,entry citation,,,,,"Bachovchin, William W., Wong, Winona Y. L., Farr-Jones, Shauna, Shenvi, Ashok B., Kettner, Charles A., ""Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes,"" Biochemistry 27 (20), 7689-7697 (1988).","Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes",published,journal,Biochemistry,,27,20,,,,,,,,,,,,,,,,,,,,,,7689,7697,1988, citations,entry_citation,2612,140117,1,,entry citation,,,,,"Bachovchin, William W., Wong, Winona Y. 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L., Farr-Jones, Shauna, Shenvi, Ashok B., Kettner, Charles A., ""Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes,"" Biochemistry 27 (20), 7689-7697 (1988).","Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes",published,journal,Biochemistry,,27,20,,,,,,,,,,,,,,,,,,,,,,7689,7697,1988, citations,entry_citation,2614,140143,1,,entry citation,,,,,"Bachovchin, William W., Wong, Winona Y. L., Farr-Jones, Shauna, Shenvi, Ashok B., Kettner, Charles A., ""Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes,"" Biochemistry 27 (20), 7689-7697 (1988).","Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes",published,journal,Biochemistry,,27,20,,,,,,,,,,,,,,,,,,,,,,7689,7697,1988, citations,entry_citation,2615,140156,1,,entry citation,,,,,"Bachovchin, William W., Wong, Winona Y. L., Farr-Jones, Shauna, Shenvi, Ashok B., Kettner, Charles A., ""Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes,"" Biochemistry 27 (20), 7689-7697 (1988).","Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes",published,journal,Biochemistry,,27,20,,,,,,,,,,,,,,,,,,,,,,7689,7697,1988, citations,entry_citation,2616,140169,1,,entry citation,,,,,"Bachovchin, William W., Wong, Winona Y. L., Farr-Jones, Shauna, Shenvi, Ashok B., Kettner, Charles A., ""Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes,"" Biochemistry 27 (20), 7689-7697 (1988).","Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes",published,journal,Biochemistry,,27,20,,,,,,,,,,,,,,,,,,,,,,7689,7697,1988, citations,entry_citation,2617,140182,1,,entry citation,,,,,"Bachovchin, William W., Wong, Winona Y. 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L., Farr-Jones, Shauna, Shenvi, Ashok B., Kettner, Charles A., ""Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes,"" Biochemistry 27 (20), 7689-7697 (1988).","Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes",published,journal,Biochemistry,,27,20,,,,,,,,,,,,,,,,,,,,,,7689,7697,1988, citations,entry_citation,2621,140247,1,,entry citation,,,,,"Bachovchin, William W., Wong, Winona Y. L., Farr-Jones, Shauna, Shenvi, Ashok B., Kettner, Charles A., ""Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes,"" Biochemistry 27 (20), 7689-7697 (1988).","Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes",published,journal,Biochemistry,,27,20,,,,,,,,,,,,,,,,,,,,,,7689,7697,1988, citations,entry_citation,2622,140260,1,,entry citation,,,,,"Bachovchin, William W., Wong, Winona Y. L., Farr-Jones, Shauna, Shenvi, Ashok B., Kettner, Charles A., ""Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes,"" Biochemistry 27 (20), 7689-7697 (1988).","Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes",published,journal,Biochemistry,,27,20,,,,,,,,,,,,,,,,,,,,,,7689,7697,1988, citations,entry_citation,2623,140273,1,,entry citation,,,,,"Bachovchin, William W., Wong, Winona Y. L., Farr-Jones, Shauna, Shenvi, Ashok B., Kettner, Charles A., ""Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes,"" Biochemistry 27 (20), 7689-7697 (1988).","Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes",published,journal,Biochemistry,,27,20,,,,,,,,,,,,,,,,,,,,,,7689,7697,1988, citations,entry_citation,2624,140286,1,,entry citation,,,,,"Bachovchin, William W., Wong, Winona Y. L., Farr-Jones, Shauna, Shenvi, Ashok B., Kettner, Charles A., ""Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes,"" Biochemistry 27 (20), 7689-7697 (1988).","Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes",published,journal,Biochemistry,,27,20,,,,,,,,,,,,,,,,,,,,,,7689,7697,1988, citations,entry_citation,2625,140299,1,,entry citation,,,,,"Bachovchin, William W., Wong, Winona Y. L., Farr-Jones, Shauna, Shenvi, Ashok B., Kettner, Charles A., ""Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes,"" Biochemistry 27 (20), 7689-7697 (1988).","Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes",published,journal,Biochemistry,,27,20,,,,,,,,,,,,,,,,,,,,,,7689,7697,1988, citations,entry_citation,2627,140312,1,,entry citation,,,,,"Bachovchin, William W., Wong, Winona Y. L., Farr-Jones, Shauna, Shenvi, Ashok B., Kettner, Charles A., ""Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes,"" Biochemistry 27 (20), 7689-7697 (1988).","Nitrogen-15 NMR Spectroscopy of the Catalytic-Triad Histidine of a Serine Protease in Peptide Boronic Acid Inhibitor Complexes",published,journal,Biochemistry,,27,20,,,,,,,,,,,,,,,,,,,,,,7689,7697,1988, citations,entry_citation,2628,140325,1,,entry citation,,,,,"Bachovchin, William W., Wong, Winona Y. 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NMR 2, 149-160 (1992).","Multidimensional 1H and 15N NMR investigation of glutamine-binding protein of Escherichia coli",published,journal,J. Biomol. NMR,,2,,,,,,,,,,,,,,,,,,,,,,,149,160,1992, citations,entry_citation,26517,140843,1,,entry citation,,,,,,A novel RNA binding surface of the TAM domain of TIP5/BAZ2A mediates epigenetic regulation of rRNA genes,published,journal,Nucleic Acids Res.,,,,,,,,,,,,,,,,,,,,,,,,,,,2015, citations,entry_citation,26518,140863,1,,entry citation,,,27103580,,,VirB8-like protein TraH is crucial for DNA transfer in Enterococcus faecalis,published,journal,Sci. Rep.,,6,,,,,,,,,,,,,,,,,,,,,,,24643,24643,2016, citations,entry_citation,2638,140390,1,,entry citation,,,,,"Moratal, Jose M., Martinez-Ferrer, Maria-Jose, Jimenez, Hermas R., Donaire, Antonio, Castells, Josep, Salgado, Jesus, ""1H NMR and UV-Vis Spectroscopic Characterization of Sulfonamide Complexes of Nickel(II)-Carbonic Anhydrase. Resonance Assignments Based on NOE Effects,"" J. Inorg. 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Biol.,Journal of Molecular Biology,371,3,,,,,,,,,,,,,,,,,,,,,,703,716,2007, citations,entry_citation_2,26712,143619,2,,reference citation,,,18085410,10.1007/s10858-007-9214-2,"d'Auvergne, E. J. and Gooley, P. R. (2008). Optimisation of NMR dynamic models I. Minimisation algorithms and their performance within the model-free and Brownian rotational diffusion spaces. J. Biomol. NMR, 40(2), 107-119.",Optimisation of NMR dynamic models I. Minimisation algorithms and their performance within the model-free and Brownian rotational diffusion spaces.,published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,40,2,,,,,,,,,,,,,,,,,,,,,,107,119,2008, citations,entry_citation_3,26712,143620,3,,reference citation,,,18085411,10.1007/s10858-007-9213-3,"d'Auvergne, E. J. and Gooley, P. R. (2008). Optimisation of NMR dynamic models II. A new methodology for the dual optimisation of the model-free parameters and the Brownian rotational diffusion tensor. J. Biomol. 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NMR,Journal of Biomolecular NMR,40,2,,,,,,,,,,,,,,,,,,,,,,121,133,2008, citations,entry_citation_1,26714,143708,1,,entry citation,,,18085410,10.1007/s10858-007-9214-2,"d'Auvergne, E. J. and Gooley, P. R. (2008). Optimisation of NMR dynamic models I. Minimisation algorithms and their performance within the model-free and Brownian rotational diffusion spaces. J. Biomol. NMR, 40(2), 107-119.",Optimisation of NMR dynamic models I. Minimisation algorithms and their performance within the model-free and Brownian rotational diffusion spaces.,published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,40,2,,,,,,,,,,,,,,,,,,,,,,107,119,2008, citations,entry_citation_2,26714,143709,2,,entry citation,,,18085411,10.1007/s10858-007-9213-3,"d'Auvergne, E. J. and Gooley, P. R. (2008). Optimisation of NMR dynamic models II. A new methodology for the dual optimisation of the model-free parameters and the Brownian rotational diffusion tensor. J. Biomol. 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Rep.,Biochemistry and biophysics reports,8,,,2405-5808,,,,,,,,,,,,,,,,,,,,75,80,2016, citations,entry_citation,26717,143769,1,,entry citation,,,27147444,,,"Backbone and side-chain (1)H, (13)C, and (15)N chemical shift assignments for the apo-form of the lytic polysaccharide monooxygenase NcLPMO9C",published,journal,Biomol. NMR Assign.,,10,2,,,,,,,,,,,,,,,,,,,,,,277,280,2016, citations,entry_citation,26718,143785,1,,entry citation,,,26773054,,,Unfolding the HIV-1 reverse transcriptase RNase H domain - how to lose a molecular tug-of-war,published,journal,Nucleic Acids Res.,,44,4,,,,,,,,,,,,,,,,,,,,,,1776,1788,2016, citations,entry_citation,26719,143800,1,,entry citation,,,27807972,10.1021/jacs.6b10272,,Sequence Determinants of the Conformational Properties of an Intrinsically Disordered Protein Prior to and upon Multisite Phosphorylation,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,138,47,,1520-5126,,,,,,,,,,,,,,,,,,,,15323,15335,2016, citations,entry_citation,26720,143814,1,,entry citation,,,27807972,10.1021/jacs.6b10272,,Sequence Determinants of the Conformational Properties of an Intrinsically Disordered Protein Prior to and upon Multisite Phosphorylation,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,138,47,,1520-5126,,,,,,,,,,,,,,,,,,,,15323,15335,2016, citations,entry_citation,26721,143828,1,,entry citation,,,26612092,,,Native Chemical Ligation to Minimize Aspartimide Formation during Chemical Synthesis of Small LDLa Protein,published,journal,Chemistry,,22,3,,,,,,,,,,,,,,,,,,,,,,1146,1151,2016, citations,entry_citation,26722,143848,1,,entry citation,,,27524295,,,Basis of Mutual Domain Inhibition in a Bacterial Response Regulator,published,journal,Cell Chem. Biol.,,23,8,,,,,,,,,,,,,,,,,,,,,,945,954,2016, citations,entry_citation,26723,143866,1,,entry citation,,,27155947,10.1007/s12104-016-9684-9,,"Backbone and side-chain chemical shift assignments for the C-terminal domain of Tcb2, a cytoskeletal calcium-binding protein from Tetrahymena thermophila",published,journal,Biomol. NMR Assign.,,,,,,,,,,,,,,,,,,,,,,,,,,,2016, citations,reference_citation,26723,143867,2,,reference citation,,,27155947,10.1002/prot.25111,,Solution NMR Structures of the C-domain of Tetrahymena Cytoskeletal Protein Tcb2 Reveal Distinct Calcium-Induced Structural Rearrangements,published,journal,Proteins,,,,,,,,,,,,,,,,,,,,,,,,,,,2016, citations,entry_citation,26724,143889,1,,entry citation,,,27155947,10.1007/s12104-016-9684-9,,"Backbone and side-chain chemical shift assignments for the C-terminal domain of Tcb2, a cytoskeletal calcium-binding protein from Tetrahymena thermophila",published,journal,Biomol. NMR Assign.,,,,,,,,,,,,,,,,,,,,,,,,,,,2016, citations,reference_citation,26724,143890,2,,reference citation,,,27155947,10.1002/prot.25111,,Solution NMR Structures of the C-domain of Tetrahymena Cytoskeletal Protein Tcb2 Reveal Distinct Calcium-Induced Structural Rearrangements,published,journal,Proteins,,,,,,,,,,,,,,,,,,,,,,,,,,,2016, citations,entry_citation,26725,143914,1,,entry citation,,,27412769,,,"(1)H, (15)N, (13)C resonance assignments for pyrazinoic acid binding domain of ribosomal protein S1 from Mycobacterium tuberculosis",published,journal,Biomol. NMR Assign.,,10,2,,,,,,,,,,,,,,,,,,,,,,321,324,2016, citations,entry_citation,26726,143928,1,,entry citation,,,27372920,,,"1H, 15N, and 13C resonance assignments of Staphylococcus aureus extracellular adherence protein domain 4",published,journal,Biomol. NMR Assignments,,10,2,,,,,,,,,,,,,,,,,,,,,,301,305,2016, citations,entry_citation,26727,143946,1,,entry citation,,,27226599,,,Crystal Structures of the Human Doublecortin C- and N-terminal Domains in Complex with Specific Antibodies,published,journal,J. Biol. Chem.,,291,31,,,,,,,,,,,,,,,,,,,,,,16292,16306,2016, citations,entry_citation,26728,143962,1,,entry citation,,,27653629,,,The nearest-neighbor effect on random-coil NMR chemical shifts demonstrated using a low-complexity amino-acid sequence,published,journal,Protein Pept. Lett.,,23,11,,,,,,,,,,,,,,,,,,,,,,967,975,2016, citations,entry_citation,26730,143976,1,,entry citation,,,27067111,,,Structural and Dynamics Studies of Pax5 Reveal Asymmetry in Stability and DNA Binding by the Paired Domain,published,journal,J. Mol. Biol.,,428,11,,,,,,,,,,,,,,,,,,,,,,2372,2391,2016, citations,entry_citation,26731,143990,1,,entry citation,,,27067111,,,Structural and Dynamics Studies of Pax5 Reveal Asymmetry in Stability and DNA Binding by the Paired Domain,published,journal,J. Mol. Biol.,,428,11,,,,,,,,,,,,,,,,,,,,,,2372,2391,2016, citations,entry_citation,26732,144006,1,,entry citation,,,27353957,,,NMR Characterization of Information Flow and Allosteric Communities in the MAP Kinase p38\u03b3,published,journal,Sci. Rep.,,6,,,,,,,,,,,,,,,,,,,,,,,28655,28655,2016, citations,entry_citation,26733,144025,1,,entry citation,,,27353957,,,NMR Characterization of Information Flow and Allosteric Communities in the MAP Kinase p38\u03b3,published,journal,Sci. Rep.,,6,,,,,,,,,,,,,,,,,,,,,,,28655,28655,2016, citations,entry_citation,26734,144042,1,,entry citation,,,28072824,,,"D19S Mutation of the Cationic, Cysteine-Rich Protein PAF: Novel Insights into Its Structural Dynamics, Thermal Unfolding and Antifungal Function",published,journal,Plos One,,12,1,,,,,,,,,,,,,,,,,,,,,,e0169920,e0169920,2017, citations,entry_citation,26735,144057,1,,entry citation,,,27265850,,,Mechanism of Amyloidogenesis of a Bacterial AAA+ Chaperone,published,journal,Structure,,24,7,,,,,,,,,,,,,,,,,,,,,,1095,1109,2016, citations,entry_citation,26738,144072,1,,entry citation,,,27524699,,,Blocking the interaction between S100A9 and RAGE V domain using CHAPS molecule: A novel route to drug development against cell proliferation,published,journal,Biochim. Biophys. Acta,,1864,11,,,,,,,,,,,,,,,,,,,,,,1558,1569,2016, citations,entry_citation,26739,144088,1,,entry citation,,,27093649,,,NMR Identification of the Binding Surfaces Involved in the Salmonella and Shigella Type III Secretion Tip-Translocon Protein-Protein Interactions,published,journal,Proteins,,84,8,,,,,,,,,,,,,,,,,,,,,,1097,1107,2016, citations,entry_citation,26740,144103,1,,entry citation,,,28905237,10.1007/s12104-017-9773-4,,,published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,12,1,,1874-270X,,,,,,,,,,,,,,,,,,,,23,26,2018, citations,Manuscript_in_Preparation,26741,144118,1,,entry citation,,,29522057,10.1039/c8cc00387d,,2-Oxoglutarate regulates binding of hydroxylated hypoxia-inducible factor to prolyl hydroxylase domain 2.,published,journal,Chem. Commun. 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NMR Assign.,,10,2,,,,,,,,,,,,,,,,,,,,,,253,257,2016, citations,entry_citation,26745,144206,1,,entry citation,,,27109553,,,"The ""Lid"" in the Streptococcus pneumoniae SrtC1 Sortase Adopts a Rigid Structure that Regulates Substrate Access to the Active Site",published,journal,J. Phys. Chem. B,,120,33,,,,,,,,,,,,,,,,,,,,,,8302,8312,2016, citations,entry_citation,26746,144221,1,,entry citation,,,27298341,,,Conformational dynamics of a G-protein alpha subunit is tightly regulated by nucleotide binding,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,113,26,,,,,,,,,,,,,,,,,,,,,,E3629,E3638,2016, citations,entry_citation,26748,144237,1,,entry citation,,,27624767,,,"NMR study of Met-1 human Angiogenin: (1)H, (13)C, (15)N backbone and side-chain resonance assignment",published,journal,Biomol. NMR Assign.,,10,2,,,,,,,,,,,,,,,,,,,,,,379,383,2016, citations,entry_citation,26750,144256,1,,entry citation,,,28488849,10.1021/acs.biochem.7b00291,,Solution Conformations and Dynamics of Substrate-Bound Cytochrome P450 MycG,published,journal,Biochemistry,Biochemistry,56,21,,1520-4995,,,,,,,,,,,,,,,,,,,,2701,2714,2017, citations,entry_citation,26751,144276,1,,entry citation,,,26997265,,,Structural Model of the Extracellular Assembly of the TCR-CD3 Complex,published,journal,Cell Rep.,,14,12,,,,,,,,,,,,,,,,,,,,,,2833,2845,2016, citations,entry_citation,26752,144296,1,,entry citation,,,27193589,,,"Backbone 1H, 13C and 15N resonance assignments of the OB domain of the single stranded DNA-binding protein hSSB1 (NABP2/OBFC2B) and chemical shift mapping of the DNA-binding interface",published,journal,Biomol. NMR Assign.,,10,2,,,,,,,,,,,,,,,,,,,,,,297,300,2016, citations,entry_citation,26753,144312,1,,entry citation,,,,,,"NMR study of non-structural proteins: 1H, 13C, 15N backbone and side-chain resonance assignment of macro domain of Venezuelan equine encephalitis virus (VEEV) in complex with ADP-ribose",in preparation,journal,Biomol. 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NMR Assign.,Biomolecular NMR assignments,11,1,,1874-270X,,,,,,,,,,,,,,,,,,,,63,67,2017, citations,entry_citation,26761,144457,1,,entry citation,,,27387012,,,Ligand Binding Enhances Millisecond Conformational Exchange in Xylanase B2 from Streptomyces lividans,published,journal,Biochemistry,,55,30,,,,,,,,,,,,,,,,,,,,,,4184,4196,2016, citations,entry_citation,26762,144472,1,,entry citation,,,27738173,10.1126/science.aad1872,,Opposing effects of Elk-1 multisite phosphorylation shape its response to ERK activation,published,journal,Science,"Science (New York, N.Y.)",354,6309,,1095-9203,,,,,,,,,,,,,,,,,,,,233,237,2016, citations,entry_citation,26763,144487,1,,entry citation,,,27340016,,,"STARD6 on steroids: solution structure, multiple timescale backbone dynamics and ligand binding mechanism",published,journal,Sci. 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Biol.,,24,2,,,,,,,,,,,,,,,,,,,,,,152,161,2017, citations,entry_citation,26940,147219,1,,entry citation,,,27927196,,,"The topology, structure and PE interaction of LITAF underpin a Charcot-Marie-Tooth disease type 1C",published,journal,BMC Biol.,,14,1,,,,,,,,,,,,,,,,,,,,,,109,109,2016, citations,entry_citation,26942,147239,1,,entry citation,,,29241299,,,NMR elucidation of monomer-dimer transition and conformational heterogeneity in histone-like DNA binding protein of Helicobacter pylori,published,journal,Magn. Reson. Chem.,Magnetic resonance in chemistry : MRC,56,4,,1097-458X,,,,,,,,,,,,,,,,,,,,285,299,2018, citations,entry_citation,26943,147255,1,,entry citation,,,28228478,,,An engineered TGF-beta monomer that functions as a dominant negative to block TGF-beta signaling,published,journal,J. Biol. 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NMR Assign.,Biomolecular NMR assignments,11,1,,1874-270X,,,,,,,,,,,,,,,,,,,,95,98,2017, citations,entry_citation,26954,147406,1,,entry citation,,,28156097,,,Confinement and Stabilization of Fyn SH3 Folding Intermediate Mimetics within the Cavity of the Chaperonin GroEL Demonstrated by Relaxation-Based NMR,published,journal,Biochemistry,,56,7,,,,,,,,,,,,,,,,,,,,,,903,906,2017, citations,entry_citation,26955,147421,1,,entry citation,,,28156097,,,Confinement and Stabilization of Fyn SH3 Folding Intermediate Mimetics within the Cavity of the Chaperonin GroEL Demonstrated by Relaxation-Based NMR,published,journal,Biochemistry,,56,7,,,,,,,,,,,,,,,,,,,,,,903,906,2017, citations,entry_citation,26956,147436,1,,entry citation,,,28493957,,,Ezrin interacts with S100A4 via both its N- and C-terminal domains,published,journal,PLoS ONE,PloS one,12,5,,1932-6203,,,,,,,,,,,,,,,,,,,,e0177489,e0177489,2017, citations,entry_citation,26957,147454,1,,entry citation,,,28505309,10.1093/nar/gkx419,,The herpes viral transcription factor ICP4 forms a novel DNA recognition complex,published,journal,Nucleic Acids Res.,Nucleic acids research,45,13,,1362-4962,,,,,,,,,,,,,,,,,,,,8064,8078,2017, citations,entry_citation,26958,147468,1,,entry citation,,,28502793,10.1016/j.jmb.2017.05.006,,Salt-Mediated Oligomerization of the Mouse Prion Protein Monitored by Real-Time NMR,published,journal,J. Mol. Biol.,Journal of molecular biology,429,12,,1089-8638,,,,,,,,,,,,,,,,,,,,1852,1872,2017, citations,entry_citation,26959,147483,1,,entry citation,,,28348247,,,Entropy redistribution controls allostery in a metalloregulatory protein,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,114,17,,,,,,,,,,,,,,,,,,,,,,4424,4429,2017, citations,entry_citation,26960,147510,1,,entry citation,,,28258221,,,"Quantitative mapping of microtubule-associated protein 2c (MAP2c) phosphorylation and regulatory protein 14-3-3& Zeta binding sites reveals key differences between MAP2c and its homolog Tau",published,journal,J. Biol. Chem.,,292,16,,,,,,,,,,,,,,,,,,,,,,6715,6727,2017, citations,citation_1,26961,147527,1,,entry citation,,,28000315,,,The Mechanism of p53 Rescue by SUSP4,published,journal,Angew. Chem. Int. Ed. Engl.,,56,5,,,,,,,,,,,,,,,,,,,,,,1278,1282,2017, citations,entry_citation,26962,147542,1,,entry citation,,,28236225,,,Backbone resonance assignment of an insect arylalkylamine N-acetyltransferase from Bombyx mori reveals conformational heterogeneity,published,journal,J. Biomol. NMR,,11,1,,,,,,,,,,,,,,,,,,,,,,105,109,2017, citations,entry_citation,26963,147560,1,,entry citation,,,,,,Structure and Dynamics of Pseudomonas Aeruginosa Icp,published,thesis,,,,,,,,,,,,,,,,,,,,,,University of Glasgow,Glasgow,UK,,,,, citations,entry_citation,26964,147592,1,,entry citation,,,28085263,,,Structure and Dynamics of the Huntingtin Exon-1 N-Terminus: A Solution NMR Perspective,published,journal,J. Am. Chem. Soc.,,139,3,,,,,,,,,,,,,,,,,,,,,,1168,1176,2017, citations,entry_citation,26965,147606,1,,entry citation,,,28085263,,,Structure and Dynamics of the Huntingtin Exon-1 N-Terminus: A Solution NMR Perspective,published,journal,J. Am. Chem. Soc.,,139,3,,,,,,,,,,,,,,,,,,,,,,1168,1176,2017, citations,entry_citation,26966,147622,1,,entry citation,,,28243889,10.1007/s12104-017-9728-9,,"(1)H, (13)C, (15)N backbone assignment of the human heat-labile enterotoxin B-pentamer and chemical shift mapping of neolactotetraose binding",published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,11,1,,1874-270X,,,,,,,,,,,,,,,,,,,,99,9104,2017, citations,1,26967,147637,1,,entry citation,,,29251491,,,Glycosylation Promotes the Random Coil to Helix Transition in a Region of a Protist Skp1 Associated with F-Box Binding.',published,journal,Biochemistry,Biochemistry,57,5,,,,,,,,,,,,,,,,,,,,,,511,515,2018, citations,1,26968,147654,1,,entry citation,,,29251491,,,Glycosylation Promotes the Random Coil to Helix Transition in a Region of a Protist Skp1 Associated with F-Box Binding.',published,journal,Biochemistry,Biochemistry,57,5,,,,,,,,,,,,,,,,,,,,,,511,515,2018, citations,entry_citation,26969,147671,1,,entry citation,,,29342354,,,A Highly Dynamic Loop of the Pseudomonas aeruginosa PA14 Type IV Pilin Is Essential for Pilus Assembly.,published,journal,ACS Infect. Dis.,ACS infectious diseases,4,6,,2373-8227,,,,,,,,,,,,,,,,,,,,936,943,2018, citations,entry_citation,26970,147688,1,,entry citation,,,28266846,10.1021/acs.biochem.6b01079,,Ligand Binding Properties of the Lentil Lipid Transfer Protein: Molecular Insight into the Possible Mechanism of Lipid Uptake,published,journal,Biochemistry,Biochemistry,56,12,,1520-4995,,,,,,,,,,,,,,,,,,,,1785,1796,2017, citations,entry_citation,26971,147702,1,,entry citation,,,28266846,10.1021/acs.biochem.6b01079,,Ligand Binding Properties of the Lentil Lipid Transfer Protein: Molecular Insight into the Possible Mechanism of Lipid Uptake,published,journal,Biochemistry,Biochemistry,56,12,,1520-4995,,,,,,,,,,,,,,,,,,,,1785,1796,2017, citations,entry_citation,26972,147718,1,,entry citation,,,28808922,,,Backbone resonance assignments for the SET domain of human methyltransferase NSD3 in complex with its cofactor,published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,11,2,,1874-270X,,,,,,,,,,,,,,,,,,,,225,229,2017, citations,entry_citation,26973,147733,1,,entry citation,,,28260216,,,Near-complete backbone resonance assignments of acid-denatured human cytochrome c in dimethylsulfoxide: a prelude to studying interactions with phospholipids,published,journal,Biomol. NMR Assign.,,11,2,,,,,,,,,,,,,,,,,,,,,,165,168,2017, citations,entry_citation,26974,147753,1,,entry citation,,,28258548,,,"Backbone resonance assignments of the Escherichia coli 62 kDa protein, Hsp31",published,journal,Biomol. NMR Assign.,,11,2,,,,,,,,,,,,,,,,,,,,,,159,163,2017, citations,citations_1,26975,147767,1,,entry citation,,,28223697,10.1038/ncomms14523,,Dynamic regulation of GDP binding to G proteins revealed by magnetic field dependent NMR relaxation analyses,published,journal,Nat. Commun.,,8,14523,,,,,,,,,,,,,,,,,,,,,,,,2017, citations,citations_1,26976,147784,1,,entry citation,,,28223697,10.1038/ncomms14523,,Dynamic regulation of GDP binding to G proteins revealed by magnetic field dependent NMR relaxation analyses,published,journal,Nat. Commun.,,8,14523,,,,,,,,,,,,,,,,,,,,,,,,2017, citations,entry_citation,26977,147802,1,,entry citation,,,28508865,10.1038/ncomms15260,,An allosteric site in the T-cell receptor Cbeta domain plays a critical signalling role,published,journal,Nat. Commun.,Nature communications,8,,,2041-1723,,,,,,,,,,,,,,,,,,,,15260,15260,2017, citations,entry_citation,26978,147823,1,,entry citation,,,28450074,,,Structural Basis of MeCP2 Distribution on Non-CpG Methylated and Hydroxymethylated DNA,published,journal,J. Mol. Biol.,,429,10,,,,,,,,,,,,,,,,,,,,,,1581,1594,2017, citations,citations_1,26979,147840,1,,entry citation,,,28739907,,,A promiscuous split intein with expanded protein engineering applications,published,journal,Proc. Natl. Acad. Sci. U. S. A.,,114,32,,,,,,,,,,,,,,,,,,,,,,8538,8543,2017, citations,Iwai,26979,147841,2,,reference citation,,,19636943,,,NMR resonance assignment of DnaE intein from Nostoc punctiforme.,published,journal,Biomol NMR Assign.,,3,1,,,,,,,,,,,,,,,,,,,,,,41,43,2009, citations,citations_1,26980,147857,1,,entry citation,,,28739907,,,A promiscuous split intein with expanded protein engineering applications,published,journal,Proc. Natl. Acad. Sci. U. S. A.,,114,32,,,,,,,,,,,,,,,,,,,,,,8538,8543,2017, citations,Iwai,26980,147858,2,,reference citation,,,19636943,,,NMR resonance assignment of DnaE intein from Nostoc punctiforme.,published,journal,Biomol NMR Assign.,,3,1,,,,,,,,,,,,,,,,,,,,,,41,43,2009, citations,citations_1,26981,147874,1,,entry citation,,,28739907,,,A promiscuous split intein with expanded protein engineering applications,published,journal,Proc. Natl. Acad. Sci. U. S. A.,,114,32,,,,,,,,,,,,,,,,,,,,,,8538,8543,2017, citations,Iwai,26981,147875,2,,reference citation,,,19636943,,,NMR resonance assignment of DnaE intein from Nostoc punctiforme.,published,journal,Biomol NMR Assign.,,3,1,,,,,,,,,,,,,,,,,,,,,,41,43,2009, citations,entry_citation,26982,147890,1,,entry citation,,,29320735,,,RYBP Is a K63-Ubiquitin-Chain-Binding Protein that Inhibits Homologous Recombination Repair,published,journal,Cell Rep.,,22,2,,,,,,,,,,,,,,,,,,,,,,383,395,2018, citations,citation-1,26983,147908,1,,entry citation,,,28584100,,,Entropy in molecular recognition by proteins,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,114,25,,1091-6490,,,,,,,,,,,,,,,,,,,,6563,6568,2017, citations,citations_1,26984,147930,1,,entry citation,,,28739907,,,A promiscuous split intein with expanded protein engineering applications,published,journal,Proc. Natl. Acad. Sci. U. S. A.,,114,32,,,,,,,,,,,,,,,,,,,,,,8538,8543,2017, citations,Iwai,26984,147931,2,,reference citation,,,19636943,,,NMR resonance assignment of DnaE intein from Nostoc punctiforme.,published,journal,Biomol NMR Assign.,,3,1,,,,,,,,,,,,,,,,,,,,,,41,43,2009, citations,entry_citation,26985,147946,1,,entry citation,,,28258549,,,"Backbone and side-chain resonance assignments for the tmRNA-binding protein, SmpB, from Mycobacterium tuberculosis",published,journal,Biomol. NMR Assign.,,11,2,,,,,,,,,,,,,,,,,,,,,,175,179,2017, citations,entry_citation,26986,147962,1,,entry citation,,,28808882,,,"1H, 13C and 15N chemical shift assignments of Saccharomyces cerevisiae type 1 thioredoxin in the oxidized state by solution NMR spectroscopy",published,journal,Biomol. NMR Assign.,,11,2,,,,,,,,,,,,,,,,,,,,,,221,224,2017, citations,entry_citation,26990,147977,1,,entry citation,,,28803387,,,"1H, 15N, and 13C chemical shift assignments of the regulatory domain of human calcineurin",published,journal,Biomol. NMR Assign.,,11,2,,,,,,,,,,,,,,,,,,,,,,215,219,2017, citations,entry_citation,26991,147994,1,,entry citation,,,,,,The structure commonality between human and mouse CCL5,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,26992,148011,1,,entry citation,,,28065835,,,NMR investigation of the isolated second voltage-sensing domain of human Nav1.4 channel,published,journal,Biochim. Biophys. Acta,,1859,3,,,,,,,,,,,,,,,,,,,,,,493,506,2017, citations,entry_citation,26993,148031,1,,entry citation,,,28065835,,,NMR investigation of the isolated second voltage-sensing domain of human Nav1.4 channel,published,journal,Biochim. Biophys. Acta,,1859,3,,,,,,,,,,,,,,,,,,,,,,493,506,2017, citations,human_hsp27_CTR,26994,148050,1,,entry citation,,,28547731,,,Proline isomerization in the C-terminal region of HSP27,published,journal,Cell Stress Chaperones,Cell stress & chaperones,22,4,,1466-1268,,,,,,,,,,,,,,,,,,,,639,651,2017, citations,citation_1,26995,148064,1,,entry citation,,,,,,Assigned Chemical Shifts for a consensus homeodomain,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,26996,148080,1,,entry citation,,,28751017,10.1016/j.pep.2017.07.002,,Co-refolding of a functional complex of Dengue NS3 protease and NS2B co-factor domain and backbone resonance assignment by solution NMR,published,journal,Protein Expr. Purif.,Protein expression and purification,140,,,1096-0279,,,,,,,,,,,,,,,,,,,,16,27,2017, citations,entry_citation,26997,148100,1,,entry citation,,,28589219,10.1007/s12104-017-9744-9,,"(1)H, (13)C, and (15)N backbone chemical shift assignments of 4E-BP144-87 and 4E-BP144-87 bound to eIF4E",published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,11,2,,1874-270X,,,,,,,,,,,,,,,,,,,,187,191,2017, citations,entry_citation,26998,148115,1,,entry citation,,,28408762,,,Interplay of buried histidine protonation and protein stability in prion misfolding,published,journal,Sci. Rep.,Scientific Reports,7,1,,,,,,,,,,,,,,,,,,,,,,882,882,2017, citations,entry_citation,26999,148132,1,,entry citation,,,31339702,,,Nucleation of an Activating Conformational Change by a Cation-pi Interaction,published,journal,Biochemistry,Biochemistry,58,32,,1520-4995,,,,,,,,,,,,,,,,,,,,3408,3412,2019, citations,entry_citation,27,148148,1,,entry citation,,,,,"Sukumaran, Dinesh K., Clore, G. 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NMR Assign.,Biomolecular NMR assignments,11,2,,1874-270X,,,,,,,,,,,,,,,,,,,,187,191,2017, citations,entry_citation,27004,148225,1,,entry citation,,,31339702,,,Nucleation of an Activating Conformational Change by a Cation-pi Interaction,published,journal,Biochemistry,Biochemistry,58,32,,1520-4995,,,,,,,,,,,,,,,,,,,,3408,3412,2019, citations,entry_citation,27005,148243,1,,entry citation,,,31339702,,,Nucleation of an Activating Conformational Change by a Cation-pi Interaction,published,journal,Biochemistry,Biochemistry,58,32,,1520-4995,,,,,,,,,,,,,,,,,,,,3408,3412,2019, citations,entry_citation,27007,148261,1,,entry citation,,,31339702,,,Nucleation of an Activating Conformational Change by a Cation-pi Interaction,published,journal,Biochemistry,Biochemistry,58,32,,1520-4995,,,,,,,,,,,,,,,,,,,,3408,3412,2019, citations,entry_citation,27008,148279,1,,entry citation,,,31339702,,,Nucleation of an Activating Conformational Change by a Cation-pi Interaction,published,journal,Biochemistry,Biochemistry,58,32,,1520-4995,,,,,,,,,,,,,,,,,,,,3408,3412,2019, citations,entry_citation,27010,148297,1,,entry citation,,,31339702,,,Nucleation of an Activating Conformational Change by a Cation-pi Interaction,published,journal,Biochemistry,Biochemistry,58,32,,1520-4995,,,,,,,,,,,,,,,,,,,,3408,3412,2019, citations,citation_1,27011,148315,1,,entry citation,,,28539362,,,Solution Structure of Domain 1.1 of the sigma(A) Factor from Bacillus subtilis is Preformed for Binding to the RNA Polymerase Core,published,journal,J. Biol. Chem.,The Journal of biological chemistry,292,28,,1083-351X,,,,,,,,,,,,,,,,,,,,11610,11617,2017, citations,entry_citation,27012,148343,1,,entry citation,,,28589218,,,"H(N), N, C(alpha) and C(beta) assignments of the two periplasmic domains of Neisseria meningitidis DsbD",published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,11,2,,1874-270X,,,,,,,,,,,,,,,,,,,,181,186,2017, citations,entry_citation,27013,148359,1,,entry citation,,,28589218,,,"H(N), N, C(alpha) and C(beta) assignments of the two periplasmic domains of Neisseria meningitidis DsbD",published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,11,2,,1874-270X,,,,,,,,,,,,,,,,,,,,181,186,2017, citations,entry_citation,27014,148375,1,,entry citation,,,28589218,,,"H(N), N, C(alpha) and C(beta) assignments of the two periplasmic domains of Neisseria meningitidis DsbD",published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,11,2,,1874-270X,,,,,,,,,,,,,,,,,,,,181,186,2017, citations,entry_citation,27015,148391,1,,entry citation,,,28589218,,,"H(N), N, C(alpha) and C(beta) assignments of the two periplasmic domains of Neisseria meningitidis DsbD",published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,11,2,,1874-270X,,,,,,,,,,,,,,,,,,,,181,186,2017, citations,citation_1,27016,148407,1,,entry citation,,,29309054,10.1038/nchembio.2549,,Mechanism of intersubunit ketosynthase-dehydratase interaction in polyketide synthases,published,journal,Nat. Chem. Biol.,Nature chemical biology,14,3,,1552-4469,,,,,,,,,,,,,,,,,,,,270,275,2018, citations,entry_citation,27017,148422,1,,entry citation,,,28815458,,,Backbone and side-chain resonance assignments of (Ca2+)4-calmodulin bound to beta calcineurin A CaMBD peptide,published,journal,Biomol. NMR Assign.,,11,2,,,,,,,,,,,,,,,,,,,,,,275,280,2017, citations,ref_cite_1,27017,148423,2,,reference citation,,,21287611,,,Recognition of beta calcineurin by the domains of calmodulin: Thermodynamic and structural evidence for distinct roles,published,journal,Proteins,,79,3,,,,,,,,,,,,,,,,,,,,,,765,786,2011, citations,ref_cite_2,27017,148424,3,,reference citation,,,12450379,,,Calcium-Induced Conformational Switching of Paramecium Calmodulin Provides Evidence for Domain Coupling,published,journal,Biochemistry,,41,48,,,,,,,,,,,,,,,,,,,,,,14158,14166,2002, citations,entry_citation,27019,148447,1,,entry citation,,,,,,The involvement of the LDLa linker in the mode of activation of the GPCR RXFP2,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation,27020,148463,1,,entry citation,,,28238532,10.1016/j.str.2017.02.001,,Human betaB2-Crystallin Forms a Face-en-Face Dimer in Solution: An Integrated NMR and SAXS Study,published,journal,Structure,"Structure (London, England : 1993)",25,3,,1878-4186,,,,,,,,,,,,,,,,,,,,496,505,2017, citations,entry_citation,27022,148480,1,,entry citation,,,28866776,,,"1H, 15N, 13C backbone resonance assignments of human phosphoglycerate kinase in a transition state analogue complex with ADP, 3-phosphoglycerate and magnesium trifluoride",published,journal,Biomol. NMR Assignments,,11,2,,,,,,,,,,,,,,,,,,,,,,251,256,2017, citations,Baronti_et_al.,27023,148503,1,,entry citation,,,28402879,10.1016/j.bpj.2017.02.025,,Fragment-Based NMR Study of the Conformational Dynamics in the bHLH Transcription Factor Ascl1',published,journal,Biophys. J.,Biophysical journal,112,7,,1542-0086,,,,,,,,,,,,,,,,,,,,1366,1373,2017, citations,Baronti_et_al.,27024,148520,1,,entry citation,,,28402879,10.1016/j.bpj.2017.02.025,,Fragment-Based NMR Study of the Conformational Dynamics in the bHLH Transcription Factor Ascl1',published,journal,Biophys. J.,Biophysical journal,112,7,,1542-0086,,,,,,,,,,,,,,,,,,,,1366,1373,2017, citations,Baronti_et_al.,27025,148537,1,,entry citation,,,28402879,10.1016/j.bpj.2017.02.025,,Fragment-Based NMR Study of the Conformational Dynamics in the bHLH Transcription Factor Ascl1',published,journal,Biophys. J.,Biophysical journal,112,7,,1542-0086,,,,,,,,,,,,,,,,,,,,1366,1373,2017, citations,Baronti_et_al.,27026,148554,1,,entry citation,,,28402879,10.1016/j.bpj.2017.02.025,,Fragment-Based NMR Study of the Conformational Dynamics in the bHLH Transcription Factor Ascl1',published,journal,Biophys. J.,Biophysical journal,112,7,,1542-0086,,,,,,,,,,,,,,,,,,,,1366,1373,2017, citations,entry_citation,27027,148571,1,,entry citation,,,28820253,,,Bioinorganic Chemistry of Parkinson's Disease: Affinity and Structural Features of Cu(I) Binding to the Full-Length beta-Synuclein Protein,published,journal,Inorg. Chem.,,56,17,,,,,,,,,,,,,,,,,,,,,,10387,10395,2017, citations,entry_citation,27028,148585,1,,entry citation,,,28348247,,,Entropy redistribution controls allostery in a metalloregulatory protein,published,journal,Proc. Natl. Acad. Sci. 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Biol.,Nature chemical biology,13,12,,1552-4469,,,,,,,,,,,,,,,,,,,,1280,1285,2017, citations,entry_citation,27033,148661,1,,entry citation,,,28875299,,,"1H, 13C and 15N resonance assignments and secondary structures of cyclophilin 2 from Trichomonas vaginalis",published,journal,Biomol. NMR Assignments,,12,1,,,,,,,,,,,,,,,,,,,,,,27,30,2018, citations,entry_citation,27034,148676,1,,entry citation,,,28593560,,,"1H, 13C and 15N NMR chemical shift assignments of A. thaliana RCD1 RST",published,journal,Biomol. NMR Assignments,,11,2,,,,,,,,,,,,,,,,,,,,,,207,210,2017, citations,entry_citation,27035,148691,1,,entry citation,,,28437106,10.1021/acs.jmedchem.7b00147,,Allosteric targeting of the Fanconi anemia ubiquitin-conjugating enzyme Ube2T by fragment screening,published,journal,J. Med. Chem.,Journal of medicinal chemistry,60,9,,1520-4804,,,,,,,,,,,,,,,,,,,,4093,4098,2017, citations,citation_1,27036,148705,1,,entry citation,,,28819722,,,Carbon and amide detect backbone assignment methods of a novel repeat protein from the staphylocoagulase in S. aureus,published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,11,2,,1874-270X,,,,,,,,,,,,,,,,,,,,243,249,2017, citations,entry_citation,27037,148724,1,,entry citation,,,28653216,,,"NMR characterization of HtpG, the E. coli Hsp90, using sparse labeling with (13)C-methyl alanine",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,68,3,,1573-5001,,,,,,,,,,,,,,,,,,,,225,236,2017, citations,entry_citation,27038,148746,1,,entry citation,,,28653216,,,"NMR characterization of HtpG, the E. coli Hsp90, using sparse labeling with (13)C-methyl alanine",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,68,3,,1573-5001,,,,,,,,,,,,,,,,,,,,225,236,2017, citations,Citation_1,27039,148767,1,,entry citation,,,28474685,10.1038/NCOMMS15137,,Cataract-associated P23T gamma-D-crystallin retains a native-like fold in amorphous-looking aggregates formed at physiological pH,published,journal,Nat Commun,Nature communications,8,,,2041-1723,,,,,,,,,,,,,,,,,,,,15137,15137,2017, citations,entry_citation,27040,148781,1,,entry citation,,,28587205,10.3390/ijms18061192,,Conformational Flexibility Differentiates Naturally Occurring Bet v 1 Isoforms,published,journal,Int. J. Mol. Sci.,International journal of molecular sciences,18,6,,1422-0067,,,,,,,,,,,,,,,,,,,,E1192,E1192,2017, citations,citation_1,27041,148795,1,,entry citation,,,28581722,,,"The PipX protein, when not bound to its targets, has its signalling C-terminal helix in a flexed conformation",published,journal,Biochemistry,,56,25,,,,,,,,,,,,,,,,,,,,,,3211,3224,2017, citations,entry_citation,27043,148815,1,,entry citation,,,28808891,,,NMR resonance assignment of New Delhi Metallo-beta-lactamase,published,journal,Biomol. NMR Assignments,,11,2,,1874-270X,,,,,,,,,,,,,,,,,,,,239,242,2017, citations,entry_citation,27044,148832,1,,entry citation,,,29075633,,,Structure and Interactions of the TPR Domain of Sgt2 with Yeast Chaperones and Ybr137wp.,published,journal,Front Mol Biosci,Frontiers in molecular biosciences,4,68,,2296-889X,,,,,,,,,,,,,,,,,,,,,,2017, citations,citation_1,27045,148849,1,,entry citation,,,28537272,10.1038/NCOMMS15462,,Fibril polymorphism affects immobilized non-amyloid flanking domains of huntingtin exon1 rather than its polyglutamine core,published,journal,Nat Commun.,,8,,,,,,,,,,,,,,,,,,,,,,,15462,15462,2017, citations,citation_2,27045,148850,2,,reference citation,,,25280367,,,Polyglutamine amyloid core boundaries and flanking domain dynamics in huntingtin fragment fibrils determined by solid-state NMR,published,journal,Biochemistry,,53,42,,,,,,,,,,,,,,,,,,,,,,6653,6666,2014, citations,entry_citation,27046,148868,1,,entry citation,,,28547731,,,Proline isomerization in the C-terminal region of HSP27,published,journal,Cell Stress Chaperones,Cell stress & chaperones,22,4,,1466-1268,,,,,,,,,,,,,,,,,,,,639,651,2017, citations,entry_citation,27047,148882,1,,entry citation,,,28408762,,,Interplay of buried histidine protonation and protein stability in prion misfolding,published,journal,Sci. Rep.,Scientific Reports,7,1,,,,,,,,,,,,,,,,,,,,,,882,882,2017, citations,entry_citation,27048,148899,1,,entry citation,,,28560616,,,"1H, 13C, and 15N backbone and sidechain resonance assignments of a monomeric variant of E. coli deoxyribose-5-phosphate aldolase",published,journal,Biomol. NMR Assignments,,11,2,,,,,,,,,,,,,,,,,,,,,,197,201,2017, citations,entry_citation,27049,148917,1,,entry citation,,,28573456,,,"Backbone NMR assignments of tryparedoxin, the central protein in the hydroperoxide detoxification cascade of African trypanosomes, in the oxidized and reduced form",published,journal,Biomol NMR Assign,Biomolecular NMR assignments,11,2,,1874-270X,,,,,,,,,,,,,,,,,,,,193,196,2017, citations,entry_citation,27050,148939,1,,entry citation,,,28573456,,,"Backbone NMR assignments of tryparedoxin, the central protein in the hydroperoxide detoxification cascade of African trypanosomes, in the oxidized and reduced form",published,journal,Biomol NMR Assign,Biomolecular NMR assignments,11,2,,1874-270X,,,,,,,,,,,,,,,,,,,,193,196,2017, citations,entry_citation,27051,148961,1,,entry citation,,,28856584,,,"1H, 15N and 13C resonance assignments of Ixolaris, a tissue factor pathway inhibitor from the tick salivary gland",published,journal,Biomol. NMR Assign.,,11,2,,,,,,,,,,,,,,,,,,,,,,293,296,2017, citations,entry_citation,27052,148976,1,,entry citation,,,,,,"Backbone 1H, 13C, and 15N and ALV methyl Chemical Shift Assignments of the yeast TIM9/10 complex",in preparation,BMRB only,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,27053,148996,1,,entry citation,,,28330874,10.1074/jbc.M117.781906,,High-resolution 3D NMR structure of the KRAS proto-oncogene promoter reveals key features of a G-quadruplex involved in transcriptional regulation,published,journal,J. Biol. Chem.,The Journal of biological chemistry,292,19,,1083-351X,,,,,,,,,,,,,,,,,,,,8082,8091,2017, citations,entry_citation,27055,149011,1,,entry citation,,,29450990,,,Splicing Site Recognition by Synergy of Three Domains in Splicing Factor RBM10,published,journal,Biochemistry,Biochemistry,57,10,,1520-4995,,,,,,,,,,,,,,,,,,,,1563,1567,2018, citations,entry_citation,27056,149028,1,,entry citation,,,29367435,,,Interaction between the C. elegans centriolar protein SAS-5 and microtubules facilitates organelle assembly,published,journal,Mol. Biol. Cell,Molecular biology of the cell,29,6,,1939-4586,,,,,,,,,,,,,,,,,,,,722,735,2018, citations,entry_citation,27057,149044,1,,entry citation,,,30100357,,,KNL1 Binding to PP1 and Microtubules Is Mutually Exclusive.,published,journal,Structure,"Structure (London, England : 1993)",26,10,,1878-4186,,,,,,,,,,,,,,,,,,,,1327,11336,2018, citations,entry_citation,27058,149060,1,,entry citation,,,28336532,10.1074/jbc.M116.764886,,MOAG-4 promotes the aggregation of alpha-synuclein by competing with self-protective electrostatic interactions.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,292,20,,1083-351X,,,,,,,,,,,,,,,,,,,,8269,8278,2017, citations,entry_citation,27060,149076,1,,entry citation,,,28780126,,,"Membrane targeting peptides toward antileishmanial activity: Design, structural determination and mechanism of interaction",published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,,,,0006-3002,,,,,,,,,,,,,,,,,,,,30248,30249,2017, citations,entry_citation,27061,149095,1,,entry citation,,,,,,Backbone assignment of E. coli acyl carrier protein,in preparation,journal,J. Mol. Biol.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,27062,149111,1,,entry citation,,,28593559,,,"(1)H, (13)C and (15)N NMR assignments of a bacterial immunoglobulin-like domain (group 2) of a protein of a bacterium Paenarthrobacter aurescens TC1",published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,11,2,,1874-270X,,,,,,,,,,,,,,,,,,,,203,206,2017, citations,entry_citation,27063,149128,1,,entry citation,,,28945358,,,Lysines in RNA polymerase II C-terminal domain contribute to TAF15 fibril recruitment,published,journal,Biochemistry,,57,17,,,,,,,,,,,,,,,,,,,,,,2549,2563,2018, citations,entry_citation,27064,149147,1,,entry citation,,,28822092,10.1007/s13238-017-0443-1,,Zn(II) can mediate self-association of the extracellular C-terminal domain of CD147.,published,journal,Protein Cell,Protein & cell,9,3,,1674-8018,,,,,,,,,,,,,,,,,,,,310,315,2018, citations,citation_1,27065,149162,1,,entry citation,,,28746363,10.1371/journal.pone.0181799,,MAK33 antibody light chain amyloid fibrils are similar to oligomeric precursors.,published,journal,PLoS ONE,PloS one,12,7,,1932-6203,,,,,,,,,,,,,,,,,,,,e0181799,e0181799,2017, citations,entry_citation,27066,149176,1,,entry citation,,,30100357,,,KNL1 Binding to PP1 and Microtubules Is Mutually Exclusive.,published,journal,Structure,"Structure (London, England : 1993)",26,10,,1878-4186,,,,,,,,,,,,,,,,,,,,1327,11336,2018, citations,CcpNmr,27067,149192,1,,reference citation,,,15815974,10.1002/prot.20449,,The CCPN data model for NMR spectroscopy: Development of a software pipeline,published,journal,Proteins,,59,4,,,,,,,,,,,,,,,,,,,,,,687,696,2005, citations,Entry,27067,149193,2,,entry citation,,,29087696,,,Phosphate promotes the recovery of Mycobacterium tuberculosis \u03b2-lactamase from clavulanic acid inhibition,published,journal,Biochemistry,,56,47,,,,,,,,,,,,,,,,,,,,,,6257,6267,2017, citations,Ambler1991,27067,149194,3,,reference citation,,,6109327,10.1042/bj2760269,,A standard numbering scheme for the Class A beta-lactamases,published,journal,Biochem. J.,,276,,,,,,,,,,,,,,,,,,,,,,,269,272,1991, citations,citation1,27069,149209,1,,entry citation,,,28815423,,,"Backbone and side-chain (1)H, (15)N, and (13)C resonance assignments of a novel Staphylococcal inhibitor of myeloperoxidase",published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,11,2,,1874-270X,,,,,,,,,,,,,,,,,,,,285,288,2017, citations,entry_citation,27091,149646,1,,entry citation,,,28951478,,,Structural Basis for EarP-Mediated Arginine Glycosylation of Translation Elongation Factor EF-P,published,journal,MBio,mBio,8,5,,2150-7511,,,,,,,,,,,,,,,,,,,,e01412,e01417,2017, citations,entry_citation,2707,149226,1,,entry citation,,,,,"Nagai, Kiyoshi, La Mar, Gerd N., Jue, Thomas, Bunn, H. Franklin, ""Proton Magnetic Resonance Investigation of the Influence of Quaternary Structure on Iron-Histidine Bonding in Deoxyhemoglobins,"" Biochemistry 21, 842-847 (1982).","Proton Magnetic Resonance Investigation of the Influence of Quaternary Structure on Iron-Histidine Bonding in Deoxyhemoglobins",published,journal,Biochemistry,,21,,,,,,,,,,,,,,,,,,,,,,,842,847,1982, citations,entry_citation,27070,149239,1,,entry citation,,,29036638,,,The basic tilted helix bundle domain of the prolyl isomerase FKBP25 is a novel double-stranded RNA binding module.,published,journal,Nucleic Acids Res.,Nucleic acids research,45,20,,1362-4962,,,,,,,,,,,,,,,,,,,,11989,12004,2017, citations,entry_citation,27071,149255,1,,entry citation,,,29036638,,,The basic tilted helix bundle domain of the prolyl isomerase FKBP25 is a novel double-stranded RNA binding module.,published,journal,Nucleic Acids Res.,Nucleic acids research,45,20,,1362-4962,,,,,,,,,,,,,,,,,,,,11989,12004,2017, citations,entry_citation,27072,149271,1,,entry citation,,,28663553,10.1038/s41467-017-00062-0,,Functional and dynamic polymerization of the ALS-linked protein TDP-43 antagonizes its pathologic aggregation,published,journal,Nat. Commun.,Nature communications,8,1,,2041-1723,,,,,,,,,,,,,,,,,,,,45,45,2017, citations,entry_citation,27073,149287,1,,entry citation,,,28912275,,,NMR reveals the intrinsically disordered domain 2 of NS5A protein as an allosteric regulator of the hepatitis C virus RNA polymerase NS5B,published,journal,J. Biol. Chem.,The Journal of biological chemistry,117,,,1083-351X,,,,,,,,,,,,,,,,,,,,813766,813766,2017, citations,entry_citation,27074,149316,1,,entry citation,,,29603451,,,Exploring the role of post-translational modifications in regulating alpha-synuclein interactions by studying the effects of phosphorylation on nanobody binding,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,27,7,,1469-896X,,,,,,,,,,,,,,,,,,,,1262,1274,2018, citations,entry_citation,27075,149331,1,,entry citation,,,29603451,,,Exploring the role of post-translational modifications in regulating alpha-synuclein interactions by studying the effects of phosphorylation on nanobody binding,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,27,7,,1469-896X,,,,,,,,,,,,,,,,,,,,1262,1274,2018, citations,entry_citation,27076,149347,1,,entry citation,,,29603451,,,Exploring the role of post-translational modifications in regulating alpha-synuclein interactions by studying the effects of phosphorylation on nanobody binding,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,27,7,,1469-896X,,,,,,,,,,,,,,,,,,,,1262,1274,2018, citations,entry_citation,27077,149362,1,,entry citation,,,29603451,,,Exploring the role of post-translational modifications in regulating alpha-synuclein interactions by studying the effects of phosphorylation on nanobody binding,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,27,7,,1469-896X,,,,,,,,,,,,,,,,,,,,1262,1274,2018, citations,entry_citation,27078,149378,1,,entry citation,,,28822070,,,"Chemical shift assignments for the apo-form of the catalytic domain, the linker region, and the carbohydrate-binding domain of the cellulose-active lytic polysaccharide monooxygenase ScLPMO10C",published,journal,Biomol. NMR Assign,,11,2,,,,,,,,,,,,,,,,,,,,,,257,264,2017, citations,entry_citation,27079,149406,1,,entry citation,,,28929458,,,Backbone resonance assignment of the BCL6-BTB/POZ domain,published,journal,Biomol. NMR Assignments,,12,1,,,,,,,,,,,,,,,,,,,,,,47,50,2018, citations,entry_citation,2708,149426,1,,entry citation,,,,,"Nagai, Kiyoshi, La Mar, Gerd N., Jue, Thomas, Bunn, H. Franklin, ""Proton Magnetic Resonance Investigation of the Influence of Quaternary Structure on Iron-Histidine Bonding in Deoxyhemoglobins,"" Biochemistry 21, 842-847 (1982).","Proton Magnetic Resonance Investigation of the Influence of Quaternary Structure on Iron-Histidine Bonding in Deoxyhemoglobins",published,journal,Biochemistry,,21,,,,,,,,,,,,,,,,,,,,,,,842,847,1982, citations,entry_citation,27080,149439,1,,entry citation,,,28940147,,,Backbone resonance assignment of the Human Uracil DNA Glycosylase-2,published,journal,Biomol. NMR Assignments,,12,1,,,,,,,,,,,,,,,,,,,,,,37,42,2018, citations,citation_1,27081,149454,1,,entry citation,,,28766175,,,Backbone and side chain resonance assignments for a structured domain within Atg32,published,journal,Biomol. NMR Assignments,,11,2,,,,,,,,,,,,,,,,,,,,,,211,214,2017, citations,entry_citation,27082,149470,1,,entry citation,,,29478821,10.1016/j.str.2018.01.016,,Disease Variants of FGFR3 Reveal Molecular Basis for the Recognition and Additional Roles for Cdc37 in Hsp90 Chaperone System,published,journal,Structure,"Structure (London, England : 1993)",26,3,,1878-4186,,,,,,,,,,,,,,,,,,,,446,458,2018, citations,entry_citation,27083,149487,1,,entry citation,,,29478821,10.1016/j.str.2018.01.016,,Disease Variants of FGFR3 Reveal Molecular Basis for the Recognition and Additional Roles for Cdc37 in Hsp90 Chaperone System,published,journal,Structure,"Structure (London, England : 1993)",26,3,,1878-4186,,,,,,,,,,,,,,,,,,,,446,458,2018, citations,entry_citation,27084,149506,1,,entry citation,,,28733600,10.1038/s41598-017-06598-x,,beta-Ginkgotides: Hyperdisulfide-constrained peptides from Ginkgo biloba.,published,journal,Sci. Rep.,Scientific reports,7,1,,2045-2322,,,,,,,,,,,,,,,,,,,,6140,6140,2017, citations,entry_citation,27085,149523,1,,entry citation,,,28980143,,,NMR assignments of the N-terminal domain of Staphylococcus aureus hibernation promoting factor (SaHPF),published,journal,Biomol. NMR Assignments,,12,1,,,,,,,,,,,,,,,,,,,,,,85,89,2018, citations,entry_citation,27086,149548,1,,entry citation,,,28749688,,,"Structural and Dynamic ""Portraits"" of Recombinant and Native Cytotoxin I from Naja oxiana: How Close Are They?",published,journal,Biochemistry,Biochemistry,56,34,,1520-4995,,,,,,,,,,,,,,,,,,,,4468,4477,2017, citations,entry_citation,27087,149564,1,,entry citation,,,29372458,,,"1H, 15N, and 13C resonance assignments of the third domain from the S. aureus innate immune evasion protein Eap",published,journal,Biomol. NMR Assignments,,12,1,,,,,,,,,,,,,,,,,,,,,,175,178,2018, citations,entry_citation,27088,149582,1,,entry citation,,,29406711,10.1021/acs.biochem.7b01234,,ISCU(M108I) and ISCU(D39V) Differ from Wild-Type ISCU in Their Failure To Form Cysteine Desulfurase Complexes Containing Both Frataxin and Ferredoxin,published,journal,Biochemistry,Biochemistry,57,9,,1520-4995,,,,,,,,,,,,,,,,,,,,1491,1500,2018, citations,entry_citation,27089,149598,1,,entry citation,,,29406711,10.1021/acs.biochem.7b01234,,ISCU(M108I) and ISCU(D39V) Differ from Wild-Type ISCU in Their Failure To Form Cysteine Desulfurase Complexes Containing Both Frataxin and Ferredoxin,published,journal,Biochemistry,Biochemistry,57,9,,1520-4995,,,,,,,,,,,,,,,,,,,,1491,1500,2018, citations,entry_citation,2709,149614,1,,entry citation,,,,,"Nagai, Kiyoshi, La Mar, Gerd N., Jue, Thomas, Bunn, H. Franklin, ""Proton Magnetic Resonance Investigation of the Influence of Quaternary Structure on Iron-Histidine Bonding in Deoxyhemoglobins,"" Biochemistry 21, 842-847 (1982).","Proton Magnetic Resonance Investigation of the Influence of Quaternary Structure on Iron-Histidine Bonding in Deoxyhemoglobins",published,journal,Biochemistry,,21,,,,,,,,,,,,,,,,,,,,,,,842,847,1982, citations,EarP,27090,149627,1,,entry citation,,,28951478,,,Structural Basis for EarP-Mediated Arginine Glycosylation of Translation Elongation Factor EF-P,published,journal,MBio,mBio,8,5,,2150-7511,,,,,,,,,,,,,,,,,,,,e01412,e01417,2017, citations,entry_citation,27092,149665,1,,entry citation,,,29038548,10.1038/s41598-017-12701-z,,Transmembrane Segment XI of the Na(+)/H(+) Antiporter of S. pombe is a Critical Part of the Ion Translocation Pore.,published,journal,Sci. Rep.,Scientific reports,7,1,,2045-2322,,,,,,,,,,,,,,,,,,,,12793,12793,2017, citations,citation_1,27093,149682,1,,entry citation,,,28851027,,,"NMR secondary structure and interactions of recombinant human MOZART1 protein, a component of the gamma-tubulin complex",published,journal,Protein Sci.,Protein science : a publication of the Protein Society,26,11,,1469-896X,,,,,,,,,,,,,,,,,,,,2240,2248,2017, citations,entry_citation,27094,149699,1,,entry citation,,,28823028,,,Backbone resonance assignments of complexes of human voltage-dependent sodium channel NaV1.2 IQ motif peptide bound to apo calmodulin and to the C-domain fragment of apo calmodulin,published,journal,Biomol. NMR Assignments,,11,2,,,,,,,,,,,,,,,,,,,,,,297,303,2017, citations,entry_citation,27095,149717,1,,entry citation,,,28823028,,,Backbone resonance assignments of complexes of human voltage-dependent sodium channel NaV1.2 IQ motif peptide bound to apo calmodulin and to the C-domain fragment of apo calmodulin,published,journal,Biomol. NMR Assignments,,11,2,,,,,,,,,,,,,,,,,,,,,,297,303,2017, citations,entry_citation,27096,149737,1,,entry citation,,,28955759,,,Protocols and pitfalls in obtaining fatty acid-binding proteins for biophysical studies of ligand-protein and protein-protein interactions,published,journal,Biochem. Biophys. Rep.,,10,,,,,,,,,,,,,,,,,,,,,,,318,324,2017, citations,entry_citation,27097,149753,1,,entry citation,,,28812261,,,"Backbone and side-chain (1)H, (15)N and (13)C resonance assignments of two Sac10b family members Mvo10b and Mth10bTQQA from archaea",published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,11,2,,1874-270X,,,,,,,,,,,,,,,,,,,,269,273,2017, citations,entry_citation,27098,149772,1,,entry citation,,,28812261,,,"Backbone and side-chain (1)H, (15)N and (13)C resonance assignments of two Sac10b family members Mvo10b and Mth10bTQQA from archaea",published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,11,2,,1874-270X,,,,,,,,,,,,,,,,,,,,269,273,2017, citations,entry_citation,27099,149791,1,,entry citation,,,28644511,,,Bacteriophage Tail Tube Assembly Studied by Proton-Detected 4D Solid-State NMR,published,journal,Angew. Chem. Int. Ed. Engl.,Angewandte Chemie (International ed. in English),56,32,,1521-3773,,,,,,,,,,,,,,,,,,,,9497,9501,2017, citations,entry_citation,2710,149806,1,,entry citation,,,,,"Nagai, Kiyoshi, La Mar, Gerd N., Jue, Thomas, Bunn, H. Franklin, ""Proton Magnetic Resonance Investigation of the Influence of Quaternary Structure on Iron-Histidine Bonding in Deoxyhemoglobins,"" Biochemistry 21, 842-847 (1982).","Proton Magnetic Resonance Investigation of the Influence of Quaternary Structure on Iron-Histidine Bonding in Deoxyhemoglobins",published,journal,Biochemistry,,21,,,,,,,,,,,,,,,,,,,,,,,842,847,1982, citations,entry_citation,27104,149819,1,,entry citation,,,28890360,10.1016/j.str.2017.07.019,,Synergistic regulation of coregulator/nuclear receptor interaction by ligand and DNA,published,journal,Structure,"Structure (London, England : 1993)",,,,1878-4186,,,,,,,,,,,,,,,,,,,,30253,30258,2017, citations,entry_citation,27106,149834,1,,entry citation,,,28706277,,,DNA binding drives the association of BRG1/hBRM bromodomains with nucleosomes,published,journal,Nat Commun.,,8,,,,,,,,,,,,,,,,,,,,,,,16080,16080,2017, citations,Noxa1_SH3,27108,149849,1,,entry citation,,,28625920,10.1016/j.bbrc.2017.06.083,,C-terminal tail of NADPH oxidase organizer 1 (Noxo1) mediates interaction with NADPH oxidase activator (Noxa1) in the NOX1 complex,published,journal,Biochem. Biophys. Res. Commun.,Biochemical and biophysical research communications,490,3,,1090-2104,,,,,,,,,,,,,,,,,,,,594,600,2017, citations,entry_citation,27109,149863,1,,entry citation,,,31792453,,,The structure and oxidation of the eye lens chaperone alphaA-crystallin,published,journal,Nat. Struct. Mol. Biol.,Nature structural & molecular biology,26,12,,1545-9985,,,,,,,,,,,,,,,,,,,,1141,1150,2019, citations,entry_citation,2711,149878,1,,entry citation,,,,,"Nagai, Kiyoshi, La Mar, Gerd N., Jue, Thomas, Bunn, H. Franklin, ""Proton Magnetic Resonance Investigation of the Influence of Quaternary Structure on Iron-Histidine Bonding in Deoxyhemoglobins,"" Biochemistry 21, 842-847 (1982).","Proton Magnetic Resonance Investigation of the Influence of Quaternary Structure on Iron-Histidine Bonding in Deoxyhemoglobins",published,journal,Biochemistry,,21,,,,,,,,,,,,,,,,,,,,,,,842,847,1982, citations,entry_citation,27110,149891,1,,entry citation,,,29056482,,,Solution Structure and Membrane Interaction of the Cytoplasmic Tail of HIV-1 gp41 Protein,published,journal,Structure,"Structure (London, England : 1993)",0969-2126,17,,1878-4186,0353,,,,,,,,,,,,,,,,,,,30301,30305,2017, citations,entry_citation,27111,149908,1,,entry citation,,,,,,Human oncoprotein Musashi-2 N-terminal RNA recognition motif backbone assignment and identification of RNA-binding pocket,published,journal,Oncotarget,,8,,,,,,,,,,,,,,,,,,,,,,,106587,106597,2017, citations,entry_citation,27112,149928,1,,entry citation,,,31404652,,,The ligand-mediated affinity of brain-type fatty acid-binding protein for membranes determines the directionality of lipophilic cargo transport,published,journal,Biochim Biophys Acta Mol Cell Biol Lipids,Biochimica et biophysica acta. Molecular and cell biology of lipids,1864,12,,1879-2618,,,,,,,,,,,,,,,,,,,,158506,158506,2019, citations,citations_1,27113,149944,1,,entry citation,,,31404652,,,The ligand-mediated affinity of brain-type fatty acid-binding protein for membranes determines the directionality of lipophilic cargo transport,published,journal,Biochim Biophys Acta Mol Cell Biol Lipids,Biochimica et biophysica acta. Molecular and cell biology of lipids,1864,12,,1879-2618,,,,,,,,,,,,,,,,,,,,158506,158506,2019, citations,entry_citation,27119,149958,1,,entry citation,,,29127727,,,Diversity in Peptide Recognition by the SH2 Domain of SH2B1,published,journal,Proteins,,86,2,,,,,,,,,,,,,,,,,,,,,,164,176,2018, citations,entry_citation,2712,149973,1,,entry citation,,,,,"Nagai, Kiyoshi, La Mar, Gerd N., Jue, Thomas, Bunn, H. Franklin, ""Proton Magnetic Resonance Investigation of the Influence of Quaternary Structure on Iron-Histidine Bonding in Deoxyhemoglobins,"" Biochemistry 21, 842-847 (1982).","Proton Magnetic Resonance Investigation of the Influence of Quaternary Structure on Iron-Histidine Bonding in Deoxyhemoglobins",published,journal,Biochemistry,,21,,,,,,,,,,,,,,,,,,,,,,,842,847,1982, citations,entry_citation,27120,149986,1,,entry citation,,,28691252,10.1002/pro.3228,,Peptide backbone circularization enhances antifreeze protein thermostability.,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,26,10,,1469-896X,,,,,,,,,,,,,,,,,,,,1932,1941,2017, citations,entry_citation,27121,150001,1,,entry citation,,,28856606,,,"1H, 15N and 13C sequence specific backbone assignment of the vanadate inhibited hematopoietic tyrosine phosphatase",published,journal,Biomol. NMR Assign.,,12,1,,,,,,,,,,,,,,,,,,,,,,5,9,2018, citations,entry_citation,27122,150016,1,,entry citation,,,28856606,,,"1H, 15N and 13C sequence specific backbone assignment of the vanadate inhibited hematopoietic tyrosine phosphatase",published,journal,Biomol. NMR Assign.,,12,1,,,,,,,,,,,,,,,,,,,,,,5,9,2018, citations,entry_citation,27123,150033,1,,entry citation,,,29358076,,,"Disease mutation, protein interactions, and posttranslational modifications modulate hnRNPA2 liquid-liquid phase separation",published,journal,Mol. Cell,,69,3,,,,,,,,,,,,,,,,,,,,,,465,479,2018, citations,entry_citation,27124,150048,1,,entry citation,,,29358076,,,"Disease mutation, protein interactions, and posttranslational modifications modulate hnRNPA2 liquid-liquid phase separation",published,journal,Mol. Cell,,69,3,,,,,,,,,,,,,,,,,,,,,,465,479,2018, citations,entry_citation,27125,150063,1,,entry citation,,,28790177,,,"Phosphorylation of the FUS low-complexity domain disrupts phase separation, aggregation, and toxicity",published,journal,EMBO J.,,36,20,,1460-2075,,,,,,,,,,,,,,,,,,,,2951,2967,2017, citations,entry_citation,27126,150078,1,,entry citation,,,29127727,,,Diversity in Peptide Recognition by the SH2 Domain of SH2B1,published,journal,Proteins,,86,2,,,,,,,,,,,,,,,,,,,,,,164,176,2018, citations,entry_citation,27127,150094,1,,entry citation,,,28570045,,,Characterization of DNA Binding by the Isolated N-Terminal Domain of Vaccinia Virus DNA Topoisomerase IB,published,journal,Biochemistry,,56,26,,,,,,,,,,,,,,,,,,,,,,3307,3317,2017, citations,entry_citation,27128,150110,1,,entry citation,,,31862297,,,The Structural Basis for Low Conductance in the Membrane Protein VDAC upon beta-NADH Binding and Voltage Gating,published,journal,Structure,"Structure (London, England : 1993)",28,2,,1878-4186,0353,,,,,,,,,,,,,,,,,,,206,214,2020, citations,entry_citation,27129,150124,1,,entry citation,,,28668637,10.1016/j.bbapap.2017.06.025,,Molecular differences between human liver fatty acid binding protein and its T94A variant in their unbound and lipid-bound states,published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1865,9,,0006-3002,,,,,,,,,,,,,,,,,,,,1152,1159,2017, citations,entry_citation,27130,150141,1,,entry citation,,,,,,Structural dynamics of RbmA governs plasticity of Vibrio cholerae biofilms,published,journal,Elife,,6,,,,,,,,,,,,,,,,,,,,,,,e26163,e26163,2017, citations,entry_citation,27131,150157,1,,entry citation,,,28860187,,,Analysis of DNA binding by human factor xeroderma pigmentosum complementation group A (XPA) provides insight into its interactions with nucleotide excision repair substrates,published,journal,J. Biol. Chem.,,292,41,,,,,,,,,,,,,,,,,,,,,,16847,16857,2017, citations,entry_citation,27133,150175,1,,entry citation,,,28879561,,,"Backbone 1H, 13C and 15N chemical shift assignment of full-length human uracil DNA glycosylase UNG2",published,journal,Biomol. NMR Assign.,,12,1,,,,,,,,,,,,,,,,,,,,,,15,22,2018, citations,entry_citation,27134,150199,1,,entry citation,,,28618199,10.1111/febs.14135,,Lipid interactions modulate the structural and antigenic properties of the C-terminal domain of the malaria antigen merozoite surface protein 2,published,journal,FEBS J.,The FEBS journal,284,16,,1742-4658,,,,,,,,,,,,,,,,,,,,2649,2662,2017, citations,entry_citation,27135,150218,1,,entry citation,,,28838205,10.1093/nar/gkx535,,A new role for FBP21 as regulator of Brr2 helicase activity.,published,journal,Nucleic Acids Res.,Nucleic acids research,45,13,,1362-4962,,,,,,,,,,,,,,,,,,,,7922,7937,2017, citations,citations_1,27136,150240,1,,entry citation,,,28668637,10.1016/j.bbapap.2017.06.025,,Molecular differences between human liver fatty acid binding protein and its T94A variant in their unbound and lipid-bound states,published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1865,9,,0006-3002,,,,,,,,,,,,,,,,,,,,1152,1159,2017, citations,citation_1,27137,150256,1,,entry citation,,,29786756,,,Backbone NMR assignments of HypF-N under conditions generating toxic and non-toxic oligomers,published,journal,Biomol. NMR Assign.,,12,2,,,,,,,,,,,,,,,,,,,,,,273,277,2018, citations,entry_citation,27138,150271,1,,entry citation,,,29786756,,,Backbone NMR assignments of HypF-N under conditions generating toxic and non-toxic oligomers,published,journal,Biomol. NMR Assign.,,12,2,,,,,,,,,,,,,,,,,,,,,,273,277,2018, citations,citation_1,27139,150286,1,,entry citation,,,29786756,,,Backbone NMR assignments of HypF-N under conditions generating toxic and non-toxic oligomers,published,journal,Biomol. NMR Assign.,,12,2,,,,,,,,,,,,,,,,,,,,,,273,277,2018, citations,entry_citation,27140,150301,1,,entry citation,,,28935965,,,Aromatic side-chain conformational switch on the surface of the RNA Recognition Motif enables RNA discrimination,published,journal,Nat. Commun.,Nature communications,8,1,,2041-1723,,,,,,,,,,,,,,,,,,,,654,654,2017, citations,entry_citation,27141,150316,1,,entry citation,,,29071576,,,NMR assignments of the N-terminal signaling domain of the TonB-dependent outer membrane transducer PupB,published,journal,Biomol. NMR Assignments,,12,1,,,,,,,,,,,,,,,,,,,,,,91,94,2018, citations,citation_1,27142,150334,1,,entry citation,,,28935965,,,Aromatic side-chain conformational switch on the surface of the RNA Recognition Motif enables RNA discrimination,published,journal,Nat. Commun.,Nature communications,8,1,,2041-1723,,,,,,,,,,,,,,,,,,,,654,654,2017, citations,entry_citation,27143,150351,1,,entry citation,,,29045748,10.1093/nar/gkx928,,Conserved asymmetry underpins homodimerization of Dicer-associated double-stranded RNA-binding proteins.,published,journal,Nucleic Acids Res.,Nucleic acids research,45,21,,1362-4962,,,,,,,,,,,,,,,,,,,,12577,12584,2017, citations,entry_citation,27144,150382,1,,entry citation,,,,10.1038/s41467-018-06315-w,,DNA with compounds,published,journal,Nat. Commun.,,9,4229,,,,,,,,,,,,,,,,,,,,,,,,2018, citations,entry_citation,27145,150408,1,,entry citation,,,28942089,,,Biochemical basis for distinct roles of the heterochromatin proteins Swi6 and Chp2,published,journal,J. Mol. Biol.,Journal of molecular biology,,,,1089-8638,,,,,,,,,,,,,,,,,,,,30449,30449,2017, citations,entry_citation,27146,150423,1,,entry citation,,,28916982,,,Chemical shift assignments and the secondary structure of the Est3 telomerase subunit in the yeast Hansenula polymorpha,published,journal,Biomol. NMR Assignments,,12,1,,,,,,,,,,,,,,,,,,,,,,57,62,2018, citations,entry_citation,27147,150448,1,,entry citation,,,28791761,,,Degree of Biomimicry of Artificial Spider Silk Spinning Assessed by NMR Spectroscopy.,published,journal,Angew. Chem. Int. Ed. Engl.,Angewandte Chemie (International ed. in English),56,41,,1521-3773,,,,,,,,,,,,,,,,,,,,12571,12575,2017, citations,entry_citation,27148,150466,1,,entry citation,,,29045748,10.1093/nar/gkx928,,Conserved asymmetry underpins homodimerization of Dicer-associated double-stranded RNA-binding proteins.,published,journal,Nucleic Acids Res.,Nucleic acids research,45,21,,1362-4962,,,,,,,,,,,,,,,,,,,,12577,12584,2017, citations,entry_citation,27151,150485,1,,entry citation,,,28861857,,,"1H, 13C and 15N resonance assignment of human guanylate kinase",published,journal,Biomol. NMR Assignments,,12,1,,,,,,,,,,,,,,,,,,,,,,11,14,2018, citations,citation_1,27152,150505,1,,entry citation,,,28935965,,,Aromatic side-chain conformational switch on the surface of the RNA Recognition Motif enables RNA discrimination,published,journal,Nat. Commun.,Nature communications,8,1,,2041-1723,,,,,,,,,,,,,,,,,,,,654,654,2017, citations,citation_1,27153,150522,1,,entry citation,,,28935965,,,Aromatic side-chain conformational switch on the surface of the RNA Recognition Motif enables RNA discrimination,published,journal,Nat. Commun.,Nature communications,8,1,,2041-1723,,,,,,,,,,,,,,,,,,,,654,654,2017, citations,citation_1,27154,150539,1,,entry citation,,,28935965,,,Aromatic side-chain conformational switch on the surface of the RNA Recognition Motif enables RNA discrimination,published,journal,Nat. Commun.,Nature communications,8,1,,2041-1723,,,,,,,,,,,,,,,,,,,,654,654,2017, citations,entry_citation,27271,152326,1,,entry citation,,,,,,"Direct Recruitment of BCoR, but not CBX8, is Required for MLL-AF9 Leukemia",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,27155,150556,1,,entry citation,,,28935965,,,Aromatic side-chain conformational switch on the surface of the RNA Recognition Motif enables RNA discrimination,published,journal,Nat. Commun.,Nature communications,8,1,,2041-1723,,,,,,,,,,,,,,,,,,,,654,654,2017, citations,citation_1,27156,150572,1,,entry citation,,,28935965,,,Aromatic side-chain conformational switch on the surface of the RNA Recognition Motif enables RNA discrimination,published,journal,Nat. Commun.,Nature communications,8,1,,2041-1723,,,,,,,,,,,,,,,,,,,,654,654,2017, citations,citation_1,27157,150588,1,,entry citation,,,28935965,,,Aromatic side-chain conformational switch on the surface of the RNA Recognition Motif enables RNA discrimination,published,journal,Nat. Commun.,Nature communications,8,1,,2041-1723,,,,,,,,,,,,,,,,,,,,654,654,2017, citations,entry_citation,27158,150604,1,,entry citation,,,28875416,,,"NMR study of non-structural proteins-part III: 1H, 13C, 15N backbone and side-chain resonance assignment of macro domain from Chikungunya virus (CHIKV)",published,journal,Biomol. NMR Assignments,,12,1,,,,,,,,,,,,,,,,,,,,,,31,35,2018, citations,entry_citation,27159,150621,1,,entry citation,,,29353448,,,"1H, 13C and 15N NMR assignments of cyclophilin LRT2 (OsCYP2) from rice",published,journal,Biomol. NMR Assignments,,12,1,,,,,,,,,,,,,,,,,,,,,,171,174,2018, citations,entry_citation,27160,150637,1,,entry citation,,,29718417,,,Regional conformational flexibility couples substrate specificity and scissile phosphate diester selectivity in human flap endonuclease 1,published,journal,Nucleic Acids Res.,Nucleic acids research,46,11,,1362-4962,,,,,,,,,,,,,,,,,,,,5618,5633,2018, citations,Citation1,27161,150653,1,,entry citation,,,29627459,10.1016/j.jmb.2018.03.031,,Tadpole-like Conformations of Huntingtin Exon 1 Are Characterized by Conformational Heterogeneity that Persists regardless of Polyglutamine Length,published,journal,J. Mol. Biol.,Journal of molecular biology,430,10,,1089-8638,,,,,,,,,,,,,,,,,,,,1442,1458,2018, citations,entry_citation,27162,150670,1,,entry citation,,,28831766,,,NMR resonance assignments of the EVH1 domain of neurofibromin's recruitment factor Spred1,published,journal,Biomol. NMR Assignments,,11,2,,,,,,,,,,,,,,,,,,,,,,305,308,2017, citations,entry_citation,27165,150684,1,,entry citation,,,29224116,,,Chemical shift assignments of the partially deuterated Fyn SH2-SH3 domain,published,journal,Biomol. NMR Assign.,,12,1,,,,,,,,,,,,,,,,,,,,,,117,122,2018, citations,entry_citation,27166,150702,1,,entry citation,,,29067546,,,"1H, 13C and 15N chemical shift assignment of lissencephaly-1 homology (LisH) domain homodimer of human two-hybrid-associated protein 1 with RanBPM (Twa1)",published,journal,Biomol. NMR Assign.,,12,1,,,,,,,,,,,,,,,,,,,,,,99,102,2018, citations,citation_1,27167,150718,1,,entry citation,,,29349619,,,"1H, 15N, and 13C chemical shift assignments of the micelle immersed FAT C-terminal (FATC) domains of the human protein kinases ataxia-telangiectasia mutated (ATM) and DNA-dependent protein kinase catalytic subunit (DNA-PKcs) fused to the B1 domain of streptococcal protein G (GB1)",published,journal,Biomol. NMR Assign.,,,,,,,,,,,,,,,,,,,,,,,,,,,2018, citations,citation_2,27167,150719,2,,reference citation,,,23671275,10.1074/jbc.M113.467233,,NMR- and CD-Monitored Lipid Binding Studies Suggest a General Role for the FATC domain as Membrane Anchor of Phosphatidyl-Inositol-3 Kinase-Related Kinases (PIKKs),published,journal,J. Biol. Chem.,,288,27,,,,,,,,,,,,,,,,,,,,,,20046,20063,2013, citations,citation_1,27168,150741,1,,entry citation,,,29349619,,,"1H, 15N, and 13C chemical shift assignments of the micelle immersed FAT C-terminal (FATC) domains of the human protein kinases ataxia-telangiectasia mutated (ATM) and DNA-dependent protein kinase catalytic subunit (DNA-PKcs) fused to the B1 domain of streptococcal protein G (GB1)",published,journal,Biomol. NMR Assign.,,,,,,,,,,,,,,,,,,,,,,,,,,,2018, citations,citation_2,27168,150742,2,,reference citation,,,23671275,10.1074/jbc.M113.467233,,NMR- and CD-Monitored Lipid Binding Studies Suggest a General Role for the FATC domain as Membrane Anchor of Phosphatidyl-Inositol-3 Kinase-Related Kinases (PIKKs),published,journal,J. Biol. Chem.,,288,27,,,,,,,,,,,,,,,,,,,,,,20046,20063,2013, citations,entry_citation,27169,150760,1,,entry citation,,,28750053,10.1371/journal.pone.0182132,,"Comprehensive structural analysis of designed incomplete polypeptide chains of the replicase nonstructural protein 1 from the severe acute respiratory syndrome coronavirus",published,journal,PLoS ONE,PloS one,12,7,,1932-6203,,,,,,,,,,,,,,,,,,,,e0182132,e0182132,2017, citations,entry_citation,27170,150774,1,,entry citation,,,28936763,,,"Sequence specific 1H, 13C and 15N resonance assignments of a cataract-related variant G57W of human Gamma S-Crystallin",published,journal,Biomol. NMR Assignments,,12,1,,,,,,,,,,,,,,,,,,,,,,51,55,2018, citations,entry_citation,27171,150788,1,,entry citation,,,29576242,10.1016/j.jinorgbio.2018.03.007,,Interactions of iron-bound frataxin with ISCU and ferredoxin on the cysteine desulfurase complex leading to Fe-S cluster assembly.,published,journal,J. Inorg. Biochem.,Journal of inorganic biochemistry,183,,,1873-3344,,,,,,,,,,,,,,,,,,,,107,116,2018, citations,Future,27172,150814,1,,entry citation,,,,,,Ubiquitin mutant V26A pH 5.0,published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,27173,150830,1,,entry citation,,,29189986,,,"1H, 13C, and 15N chemical shift assignments of a G-quadruplex forming sequence within the KRAS proto-oncogene promoter region",published,journal,Biomol. NMR Assignments,,12,1,,,,,,,,,,,,,,,,,,,,,,123,127,2018, citations,entry_citation,27174,150846,1,,entry citation,,,,,,"van der Waals Contact between Nucleophile and Transferring Phosphorus Is Insufficient To Achieve Enzyme Transition-State Architecture",published,journal,ACS Catal.,,8,,,,,,,,,,,,,,,,,,,,,,,8140,8153,2018, citations,entry_citation,27175,150865,1,,entry citation,,,,,,"van der Waals Contact between Nucleophile and Transferring Phosphorus Is Insufficient To Achieve Enzyme Transition-State Architecture",published,journal,ACS Catal.,,8,,,,,,,,,,,,,,,,,,,,,,,8140,8153,2018, citations,entry_citation,27176,150882,1,,entry citation,,,28750053,10.1371/journal.pone.0182132,,"Comprehensive structural analysis of designed incomplete polypeptide chains of the replicase nonstructural protein 1 from the severe acute respiratory syndrome coronavirus",published,journal,PLoS ONE,PloS one,12,7,,1932-6203,,,,,,,,,,,,,,,,,,,,e0182132,e0182132,2017, citations,entry_citation,27177,150896,1,,entry citation,,,28750053,10.1371/journal.pone.0182132,,"Comprehensive structural analysis of designed incomplete polypeptide chains of the replicase nonstructural protein 1 from the severe acute respiratory syndrome coronavirus",published,journal,PLoS ONE,PloS one,12,7,,1932-6203,,,,,,,,,,,,,,,,,,,,e0182132,e0182132,2017, citations,Citation_1,27179,150910,1,,entry citation,,,,,,"1H, 15N, 13C assignments and 15N relaxation data of the intrinsically disordered hepatitis B virus X protein (HBx) in a detergent mixture",in preparation,BMRB only,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,2718,150933,1,,entry citation,,,,,"Gronenborn, Angela M., Clore, G. 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NMR Assignments,,12,1,,,,,,,,,,,,,,,,,,,,,,103,106,2018, citations,entry_citation,27184,150978,1,,entry citation,,,29063999,,,"Backbone 1H, 13C and 15N resonance assignments of the OB domain of the single stranded DNA-binding protein hSSB2 (NABP1/OBFC1B) and chemical shift mapping of the DNA-binding interface",published,journal,Biomol. NMR Assignments,,12,1,,,,,,,,,,,,,,,,,,,,,,107,111,2018, citations,entry_citation,27185,150993,1,,entry citation,,,28768811,10.1073/pnas.1703925114,,Conformational and chemical selection by a trans-acting editing domain.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,114,33,,1091-6490,,,,,,,,,,,,,,,,,,,,E6774,E6783,2017, citations,citation_1,27186,151009,1,,entry citation,,,29905837,,,DNA repair factor APLF acts as a H2A-H2B histone chaperone through binding its DNA interaction surface,published,journal,Nucleic Acids Res.,,46,14,,,,,,,,,,,,,,,,,,,,,,7138,7152,2018, citations,citation_1,27187,151023,1,,entry citation,,,29905837,,,DNA repair factor APLF acts as a H2A-H2B histone chaperone through binding its DNA interaction surface,published,journal,Nucleic Acids Res.,,46,14,,,,,,,,,,,,,,,,,,,,,,7138,7152,2018, citations,entry_citation,27188,151038,1,,entry citation,,,29184123,,,"Dynamic domain arrangement of CheA-CheY complex regulates bacterial thermotaxis, as revealed by NMR",published,journal,Sci. Rep.,,7,1,,,,,,,,,,,,,,,,,,,,,,16462,16462,2017, citations,entry_citation,27189,151052,1,,entry citation,,,29184123,,,"Dynamic domain arrangement of CheA-CheY complex regulates bacterial thermotaxis, as revealed by NMR",published,journal,Sci. Rep.,,7,1,,,,,,,,,,,,,,,,,,,,,,16462,16462,2017, citations,entry_citation,2719,151067,1,,entry citation,,,,,"Gronenborn, Angela M., Clore, G. Marius, Schmeissner, Ursula, Wingfield, Paul, ""A 1H-NMR study of human interleukin-1beta Sequence-specific assignment of aromatic residues using site-directed mutant proteins,"" Eur. J. Biochem. 161, 37-43 (1986).","A 1H-NMR study of human interleukin-1beta Sequence-specific assignment of aromatic residues using site-directed mutant proteins",published,journal,Eur. J. Biochem.,,161,,,,,,,,,,,,,,,,,,,,,,,37,43,1986, citations,entry_citation,27190,151080,1,,entry citation,,,29728980,,,"Backbone resonance assignments of complexes of apo human calmodulin bound to IQ motif peptides of voltage-dependent sodium channels NaV1.1, NaV1.4 and NaV1.7",published,journal,Biomol. NMR Assignments,,12,2,,,,,,,,,,,,,,,,,,,,,,283,289,2018, citations,entry_citation,27191,151098,1,,entry citation,,,28768811,10.1073/pnas.1703925114,,Conformational and chemical selection by a trans-acting editing domain.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,114,33,,1091-6490,,,,,,,,,,,,,,,,,,,,E6774,E6783,2017, citations,entry_citation,27192,151114,1,,entry citation,,,30241678,,,Structural and Biophysical Characterization of Rab5a from Leishmania Donovani,published,journal,Biophys. J.,Biophysical journal,115,7,,1542-0086,,,,,,,,,,,,,,,,,,,,1217,1230,2018, citations,entry_citation,27193,151131,1,,entry citation,,,28783324,10.1021/acs.biochem.7b00618,,A Noncanonical Binding Site in the EVH1 Domain of Vasodilator-Stimulated Phosphoprotein Regulates Its Interactions with the Proline Rich Region of Zyxin,published,journal,Biochemistry,Biochemistry,56,35,,1520-4995,,,,,,,,,,,,,,,,,,,,4626,4636,2017, citations,entry_citation,27194,151147,1,,entry citation,,,,,,Dynamics of Dehaloperoxidase-Hemoglobin A Derived from NMR Relaxation Spectroscopy and Molecular Dynamics Simulation,in preparation,journal,J. Biol. Inorg. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,27195,151165,1,,entry citation,,,29090418,10.1007/s12104-017-9790-3,,Chemical shift assignment of a thermophile frataxin.,published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,12,1,,1874-270X,,,,,,,,,,,,,,,,,,,,113,116,2018, citations,entry_citation,27196,151179,1,,entry citation,,,28792111,10.1002/cphc.201700572,,Solid-State NMR H-N-(C)-H and H-N-C-C 3D/4D Correlation Experiments for Resonance Assignment of Large Proteins.,published,journal,Chemphyschem,Chemphyschem : a European journal of chemical physics and physical chemistry,18,19,,1439-7641,,,,,,,,,,,,,,,,,,,,2697,2703,2017, citations,entry_citation,27197,151194,1,,entry citation,,,29440511,10.1126/scisignal.aam9899,,Structural basis for the interaction between the cell polarity proteins Par3 and Par6,published,journal,Sci. Signal.,Science signaling,11,517,,1937-9145,,,,,,,,,,,,,,,,,,,,9899,9899,2018, citations,entry_citation,27198,151209,1,,entry citation,,,29440511,10.1126/scisignal.aam9899,,Structural basis for the interaction between the cell polarity proteins Par3 and Par6,published,journal,Sci. Signal.,Science signaling,11,517,,1937-9145,,,,,,,,,,,,,,,,,,,,9899,9899,2018, citations,entry_citation,27199,151224,1,,entry citation,,,29963623,,,The neuronal S100B protein is a calcium-tuned suppressor of amyloid-beta aggregation.,published,journal,Sci. Adv.,Science advances,4,6,,2375-2548,,,,,,,,,,,,,,,,,,,,e1702,e1702,2018, citations,entry_citation,27201,151243,1,,entry citation,,,28792111,10.1002/cphc.201700572,,Solid-State NMR H-N-(C)-H and H-N-C-C 3D/4D Correlation Experiments for Resonance Assignment of Large Proteins.,published,journal,Chemphyschem,Chemphyschem : a European journal of chemical physics and physical chemistry,18,19,,1439-7641,,,,,,,,,,,,,,,,,,,,2697,2703,2017, citations,entry_citation,27202,151257,1,,entry citation,,,29168021,,,Application of methyl-TROSY to a large paramagnetic membrane protein without perdeuteration: 13C-MMTS-labeled NADPH-cytochrome P450 oxidoreductase,published,journal,J. Biomol. NMR,,70,1,,,,,,,,,,,,,,,,,,,,,,21,31,2018, citations,entry_citation,27203,151273,1,,entry citation,,,29440511,10.1126/scisignal.aam9899,,Structural basis for the interaction between the cell polarity proteins Par3 and Par6,published,journal,Sci. Signal.,Science signaling,11,517,,1937-9145,,,,,,,,,,,,,,,,,,,,9899,9899,2018, citations,entry_citation,27204,151287,1,,entry citation,,,29440511,10.1126/scisignal.aam9899,,Structural basis for the interaction between the cell polarity proteins Par3 and Par6,published,journal,Sci. Signal.,Science signaling,11,517,,1937-9145,,,,,,,,,,,,,,,,,,,,9899,9899,2018, citations,entry_citation,27205,151301,1,,entry citation,,,29440511,10.1126/scisignal.aam9899,,Structural basis for the interaction between the cell polarity proteins Par3 and Par6,published,journal,Sci. Signal.,Science signaling,11,517,,1937-9145,,,,,,,,,,,,,,,,,,,,9899,9899,2018, citations,entry_citation,27206,151315,1,,entry citation,,,29315319,10.1371/journal.pone.0190530,,The centrosomin CM2 domain is a multi-functional binding domain with distinct cell cycle roles,published,journal,PLoS ONE,PloS one,13,1,,1932-6203,,,,,,,,,,,,,,,,,,,,e0190530,e0190530,2018, citations,entry_citation,27207,151332,1,,entry citation,,,29562181,10.1016/j.celrep.2018.02.097,,Gcn4-Mediator Specificity Is Mediated by a Large and Dynamic Fuzzy Protein-Protein Complex.,published,journal,Cell Rep.,Cell reports,22,12,,2211-1247,,,,,,,,,,,,,,,,,,,,3251,3264,2018, citations,entry_citation,27208,151348,1,,entry citation,,,28953258,,,NMR Detection of Semi-Specific Antibody Interactions in Serum Environments.,published,journal,Molecules,"Molecules (Basel, Switzerland)",22,10,,1420-3049,,,,,,,,,,,,,,,,,,,,E1619,E1619,2017, citations,entry_citation,27209,151365,1,,entry citation,,,31093909,,,"1HN, 13C, and 15N backbone resonance assignments of the human DNA ligase 3 DNA-binding domain (residues 257-477)",published,journal,Biomol. NMR Assignments,,13,2,,1874-270X,,,,,,,,,,,,,,,,,,,,305,308,2019, citations,entry_citation,27210,151381,1,,entry citation,,,29299752,,,Backbone resonance assignment of the Escherichia coli protein mutation PhoBNF20D,published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,12,1,,1874-270X,,,,,,,,,,,,,,,,,,,,133,137,2018, citations,entry_citation,27211,151395,1,,entry citation,,,31217444,,,Integrated NMR and cryo-EM atomic-resolution structure determination of a half-megadalton enzyme complex,published,journal,Nat. 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Lett.,Bioorganic & medicinal chemistry letters,27,20,,1464-3405,,,,,,,,,,,,,,,,,,,,4705,4709,2017, citations,entry_citation,27228,151639,1,,entry citation,,,29489342,,,Sensitivity-Enhanced Four-Dimensional Amide-Amide Correlation NMR Experiments for Sequential Assignment of Proline-Rich Disordered Proteins,published,journal,J. Am. Chem. Soc.,,140,10,,,,,,,,,,,,,,,,,,,,,,3518,3522,2018, citations,entry_citation,27229,151655,1,,entry citation,,,32461691,10.1038/s41586-020-2336-3,,Base-pair Conformational Switch Modulates miR-34a Targeting of Sirt1 mRNA,published,journal,Nature,,583,7814,,1476-4687,,,,,,,,,,,,,,,,,,,,139,144,2020, citations,entry_citation,27230,151670,1,,entry citation,,,29642027,,,Modeling the Early Stages of Phase Separation in Disordered Elastin-like Proteins.,published,journal,Biophys. J.,Biophysical journal,114,7,,1542-0086,,,,,,,,,,,,,,,,,,,,1563,1578,2018, citations,entry_citation,27231,151685,1,,entry citation,,,29055659,,,Secondary structure and membrane topology of dengue virus NS4A protein in micelles,published,journal,Biochim. Biophys. Acta,,S0005-2736,17,,,,,,,,,,,,,,,,,,,,,,30334,30336,2017, citations,entry_citation,27232,151700,1,,entry citation,,,29197977,,,Direct assignment of 13C solid-state NMR signals of TFoF1 ATP synthase subunit c-ring in lipid membranes and its implication for the ring structure,published,journal,J. Biomol. NMR,,70,1,,,,,,,,,,,,,,,,,,,,,,53,65,2018, citations,entry_citation,27234,151718,1,,entry citation,,,28991265,10.1038/nsmb.3483,,A structural model for microtubule minus-end recognition and protection by CAMSAP proteins.,published,journal,Nat. Struct. Mol. Biol.,Nature structural & molecular biology,24,11,,1545-9985,,,,,,,,,,,,,,,,,,,,931,943,2017, citations,entry_citation,27235,151732,1,,entry citation,,,29582386,,,Solution NMR assignment of the C-terminal domain of human chTOG,published,journal,Biomol. NMR Assign.,,12,2,,,,,,,,,,,,,,,,,,,,,,221,224,2018, citations,citation_1,27236,151750,1,,entry citation,,,,,,Resonance assignment and spectral density mapping of the central conserved region of tropoelastin,in preparation,journal,J. Biomol. NMR,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,27237,151766,1,,entry citation,,,29392834,,,Structural mechanisms for the S-nitrosylation-derived protection of mouse galectin-2 from oxidation-induced inactivation revealed by NMR,published,journal,FEBS J.,,285,6,,,,,,,,,,,,,,,,,,,,,,1129,1145,2018, citations,entry_citation,27238,151781,1,,entry citation,,,29392834,,,Structural mechanisms for the S-nitrosylation-derived protection of mouse galectin-2 from oxidation-induced inactivation revealed by NMR,published,journal,FEBS J.,,285,6,,,,,,,,,,,,,,,,,,,,,,1129,1145,2018, citations,TF_dimer,27239,151797,1,,entry citation,,,29222465,10.1038/s41467-017-02196-7,,The dynamic dimer structure of the chaperone Trigger Factor.,published,journal,Nat. 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NMR Assign.,,,,,,,,,,,,,,,,,,,,,,,,,,,2019, citations,entry_citation,27255,152059,1,,entry citation,,,28813004,,,Lactose Binding Induces Opposing Dynamics Changes in Human Galectins Revealed by NMR-Based Hydrogen-Deuterium Exchange.,published,journal,Molecules,,22,8,,,,,,,,,,,,,,,,,,,,,,1357,,2017, citations,entry_citation,27256,152077,1,,entry citation,,,28813004,,,Lactose Binding Induces Opposing Dynamics Changes in Human Galectins Revealed by NMR-Based Hydrogen-Deuterium Exchange.,published,journal,Molecules,,22,8,,,,,,,,,,,,,,,,,,,,,,1357,,2017, citations,entry_citation,27257,152095,1,,entry citation,,,28813004,,,Lactose Binding Induces Opposing Dynamics Changes in Human Galectins Revealed by NMR-Based Hydrogen-Deuterium Exchange.,published,journal,Molecules,,22,8,,,,,,,,,,,,,,,,,,,,,,1357,,2017, citations,entry_citation,27258,152113,1,,entry citation,,,28813004,,,Lactose Binding Induces Opposing Dynamics Changes in Human Galectins Revealed by NMR-Based Hydrogen-Deuterium Exchange.,published,journal,Molecules,,22,8,,,,,,,,,,,,,,,,,,,,,,1357,,2017, citations,entry_citation,27259,152131,1,,entry citation,,,30181558,,,Structural basis for the complete resistance of the human prion protein mutant G127V to prion disease,published,journal,Sci. Rep.,Scientific reports,8,1,,2045-2322,,,,,,,,,,,,,,,,,,,,13211,13211,2018, citations,entry_citation,27260,152145,1,,entry citation,,,29728980,,,"Backbone resonance assignments of complexes of apo human calmodulin bound to IQ motif peptides of voltage-dependent sodium channels NaV1.1, NaV1.4 and NaV1.7",published,journal,Biomol. NMR Assignments,,12,2,,,,,,,,,,,,,,,,,,,,,,283,289,2018, citations,entry_citation,27261,152163,1,,entry citation,,,28984574,,,Ligand modulation of sidechain dynamics in a wild-type human GPCR,published,journal,Elife,,6,,,,,,,,,,,,,,,,,,,,,,,e28505,e28505,2017, citations,citation_1,27262,152182,1,,entry citation,,,29445910,,,"1H, 13C and 15N resonance assignment of domain 1 of trans-activation response element (TAR) RNA binding protein isoform 1 (TRBP2) and its comparison with that of isoform 2 (TRBP1)",published,journal,Biomol. 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Chem.,The Journal of biological chemistry,293,3,,1083-351X,,,,,,,,,,,,,,,,,,,,754,766,2018, citations,entry_citation,27287,152604,1,,entry citation,,,29934293,,,Mechanism of APTX nicked DNA sensing and pleiotropic inactivation in neurodegenerative disease,published,journal,EMBO J.,The EMBO journal,37,14,,1460-2075,,,,,,,,,,,,,,,,,,,,e98875,e98875,2018, citations,entry_citation,27288,152619,1,,entry citation,,,29225078,10.1016/j.str.2017.11.007,,Regulation of Androgen Receptor Activity by Transient Interactions of Its Transactivation Domain with General Transcription Regulators,published,journal,Structure,"Structure (London, England : 1993)",26,1,,1878-4186,,,,,,,,,,,,,,,,,,,,145,152,2018, citations,entry_citation,27289,152634,1,,entry citation,,,29398526,,,"Structure of the 30 kDa HIV-1 RNA Dimerization Signal by a Hybrid Cryo-EM, NMR, and Molecular Dynamics Approach",published,journal,Structure,,S0969-2126,18,,,,,,,,,,,,,,,,,,,,,,30001,30007,2018, citations,Assignment_paper,27290,152654,1,,entry citation,,,29372459,,,"1H, 13C, 15N resonance assignment of human YAP 50-171 fragment",published,journal,Biomol. 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Cell,,69,3,,,,,,,,,,,,,,,,,,,,,,465,479,2018, citations,entry_citation,27300,152799,1,,entry citation,,,30574775,,,UBC9 mutant reveals the impact of protein dynamics on substrate selectivity and SUMO chain linkages,published,journal,Biochemistry,,58,6,,,,,,,,,,,,,,,,,,,,,,621,632,2019, citations,entry_citation,27301,152814,1,,entry citation,,,30937734,,,Backbone and side-chain resonance assignments of centromeric protein Scm3 from Saccharomyces cerevisiae,published,journal,Biomol. NMR Assign.,,13,2,,,,,,,,,,,,,,,,,,,,,,267,273,2019, citations,entry_citation,27302,152829,1,,entry citation,,,29657132,10.1016/j.str.2018.03.013,,Structure of Radical-induced Cell Death1 hub domain reveals a common aa-scaffold for disorder in transcriptional networks,published,journal,Structure,,26,5,,,,,,,,,,,,,,,,,,,,,,734,746,2018, citations,reference_citation,27303,152846,1,,reference citation,,,27881680,10.1074/jbc.M116.753426,,Structures and Short Linear Motif of Disordered Transcription Factor Regions Provide Clues to the Interactome of the Cellular Hub Protein Radical-induced Cell Death1,published,journal,J. Biol. 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U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,115,23,,1091-6490,,,,,,,,,,,,,,,,,,,,5986,5991,2018, citations,entry_citation,27307,152915,1,,entry citation,,,29450823,,,NMR resonance assignments of RNase P protein from Thermotoga maritima,published,journal,Biomol. NMR Assign.,,12,1,,,,,,,,,,,,,,,,,,,,,,183,187,2018, citations,entry_citation,27312,152933,1,,entry citation,,,29572785,,,"Partial solid-state NMR 1H, 13C, 15N resonance assignments of a perdeuterated back-exchanged seven-transmembrane helical protein Anabaena Sensory Rhodopsin",published,journal,Biomol. NMR Assign.,,12,2,,,,,,,,,,,,,,,,,,,,,,237,242,2018, citations,entry_citation,27313,152948,1,,entry citation,,,30291238,10.1038/s41467-018-06470-0,,Structural properties of a haemophore facilitate targeted elimination of the pathogen Porphyromonas gingivalis,published,journal,Nat. Commun.,Nature communications,9,1,,2041-1723,,,,,,,,,,,,,,,,,,,,4097,4097,2018, citations,E1_ILs,27314,152972,1,,entry citation,,,29120187,,,Mechanism of Competitive Inhibition and Destabilization of Acidothermus cellulolyticus Endoglucanase 1 by Ionic Liquids,published,journal,J. Phys. Chem. B,,121,48,,,,,,,,,,,,,,,,,,,,,,10793,10803,2017, citations,entry_citation,27315,152988,1,,entry citation,,,30289706,10.1021/jacs.8b09188,,Lipid- and Cholesterol-Mediated Time-Scale-Specific Modulation of the Outer Membrane Protein X Dynamics in Lipid Bilayers,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,140,45,,1520-5126,,,,,,,,,,,,,,,,,,,,15402,15411,2018, citations,entry_citation,27316,153003,1,,entry citation,,,,,,Structural analysis of natively-folded membrane-anchored proteins obtained by SortaseA-mediated ligation,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,27317,153018,1,,entry citation,,,29450824,,,Solid-state [13C-15N] NMR resonance assignment of Hepatitis B Virus core protein,published,journal,Biomol. NMR Assignments,,12,1,,,,,,,,,,,,,,,,,,,,,,205,214,2018, citations,entry_citation,27320,153032,1,,entry citation,,,31308176,,,"AMPK and AKT protein kinases hierarchically phosphorylate the N-terminus of the FOXO1 transcription factor, modulating interactions with 14-3-3 proteins",published,journal,J. Biol. 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Cell,Molecular cell,S1097,18,,1097-4164,,,,,,,,,,,,,,,,,,,,30102,30103,2018, citations,entry_citation,27341,153277,1,,entry citation,,,,10.1038/s41598-018-33379-x,,Overlapping motifs on the herpes viral proteins ICP27 and ORF57 mediate interactions with the mRNA export adaptors ALYREF and UIF,published,journal,Sci. Rep.,,8,,,,,,,,,,,,,,,,,,,,,,,15005,15005,2018, citations,entry_citation,27342,153292,1,,entry citation,,,30349081,,,Cryo-EM structure of the bacteria-killing type IV secretion system core complex from Xanthomonas citri,published,journal,Nat. Microbiol.,,3,12,,,,,,,,,,,,,,,,,,,,,,1429,1440,2018, citations,entry_citation,27343,153311,1,,entry citation,,,29512300,,,Co-evolutionary fitness landscapes for sequence design,published,journal,Angew. Chem. Int. Ed. Engl.,,57,20,,,,,,,,,,,,,,,,,,,,,,5674,5678,2018, citations,entry_citation,27344,153328,1,,entry citation,,,29512300,,,Co-evolutionary fitness landscapes for sequence design,published,journal,Angew. Chem. Int. Ed. 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NMR Assignments,,12,2,,,,,,,,,,,,,,,,,,,,,,279,281,2018, citations,entry_citation,27406,154436,1,,entry citation,,,29876749,,,"1H, 13C, 15N resonance assignment of recombinant Euplotes raikovi protein Er-23",published,journal,Biomol. NMR Assignments,,12,2,,,,,,,,,,,,,,,,,,,,,,291,295,2018, citations,citation_1,27407,154450,1,,entry citation,,,29917149,,,Transitions in DNA polymerase beta microsecond-millisecond dynamics related to substrate binding and catalysis,published,journal,Nucleic Acids Res.,,46,14,,,,,,,,,,,,,,,,,,,,,,7309,7322,2018, citations,entry_citation,27408,154468,1,,entry citation,,,27294323,,,Small-molecule binding of the axin RGS domain promotes beta-catenin and Ras degradation.,published,journal,Nat. Chem. 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NMR Assignments,,12,2,,,,,,,,,,,,,,,,,,,,,,357,361,2018, citations,entry_citation,27412,154548,1,,entry citation,,,,,,Assigned Chemical Shifts for dASCIZ LC8 Binding Domain (241-388),submitted,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,27413,154565,1,,entry citation,,,29858729,,,"1H, 15N, 13C backbone resonance assignment of human Alkbh5",published,journal,Biomol. NMR Assign.,,12,2,,,,,,,,,,,,,,,,,,,,,,297,301,2018, citations,citation_1,27414,154579,1,,entry citation,,,29695509,10.1074/jbc.RA118.002709,,"Myc phosphorylation in its basic helix-loop-helix region destabilizes transient alpha-helical structures, disrupting Max and DNA binding",published,journal,J. Biol. Chem.,The Journal of biological chemistry,293,24,,1083-351X,,,,,,,,,,,,,,,,,,,,9301,9310,2018, citations,entry_citation,27415,154593,1,,entry citation,,,29960917,,,"Identification of major matrix metalloproteinase-20 proteolytic processing products of murine amelogenin and tyrosine-rich amelogenin peptide using a nuclear magnetic resonance spectroscopy based method",published,journal,Arch. Oral Biol.,Archives of oral biology,93,,,1879-1506,,,,,,,,,,,,,,,,,,,,187,194,2018, citations,entry_citation,27416,154610,1,,entry citation,,,29695509,10.1074/jbc.RA118.002709,,"Myc phosphorylation in its basic helix-loop-helix region destabilizes transient alpha-helical structures, disrupting Max and DNA binding",published,journal,J. Biol. Chem.,The Journal of biological chemistry,293,24,,1083-351X,,,,,,,,,,,,,,,,,,,,9301,9310,2018, citations,entry_citation,27417,154624,1,,entry citation,,,29868988,,,NMR assignments of the WBSCR27 protein related to Williams-Beuren syndrome,published,journal,Biomol. NMR Assignments,,12,2,,,,,,,,,,,,,,,,,,,,,,303,308,2018, citations,Citation_1,27449,155131,1,,entry citation,,,30159810,,,"Resonance assignments of wild-type and two cysteine-free variants of the four-helix bundle protein, Rop",published,journal,Biomol. NMR Assignments,,12,2,,,,,,,,,,,,,,,,,,,,,,345,350,2018, citations,entry_citation,27418,154649,1,,entry citation,,,29695509,10.1074/jbc.RA118.002709,,"Myc phosphorylation in its basic helix-loop-helix region destabilizes transient alpha-helical structures, disrupting Max and DNA binding",published,journal,J. Biol. Chem.,The Journal of biological chemistry,293,24,,1083-351X,,,,,,,,,,,,,,,,,,,,9301,9310,2018, citations,entry_citation,27419,154663,1,,entry citation,,,29695509,10.1074/jbc.RA118.002709,,"Myc phosphorylation in its basic helix-loop-helix region destabilizes transient alpha-helical structures, disrupting Max and DNA binding",published,journal,J. Biol. Chem.,The Journal of biological chemistry,293,24,,1083-351X,,,,,,,,,,,,,,,,,,,,9301,9310,2018, citations,entry_citation,27420,154677,1,,entry citation,,,30152054,,,"Cytosolic expression, solution structures, and molecular dynamics simulation of genetically encodable disulfide-rich de novo designed peptides",published,journal,Protein Sci.,Protein science : a publication of the Protein Society,27,9,,1469-896X,,,,,,,,,,,,,,,,,,,,1611,1623,2018, citations,entry_citation,27421,154693,1,,entry citation,,,29695509,10.1074/jbc.RA118.002709,,"Myc phosphorylation in its basic helix-loop-helix region destabilizes transient alpha-helical structures, disrupting Max and DNA binding",published,journal,J. Biol. 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Lett.,Protein and peptide letters,26,6,,1875-5305,,,,,,,,,,,,,,,,,,,,449,457,2019, citations,entry_citation,27426,154753,1,,entry citation,,,,,,Disruption of the MBD2-NuRD complex but not MBD3-NuRD induces high levels of expression in human adult erythroid cells,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,27429,154768,1,,entry citation,,,29724824,,,Distinctive phosphoinositide- and Ca2+-binding properties of normal and cognitive performance-linked variant forms of KIBRA C2 domain,published,journal,J. Biol. Chem.,,293,24,,,,,,,,,,,,,,,,,,,,,,9335,9344,2018, citations,entry_citation,27430,154785,1,,entry citation,,,29724824,,,Distinctive phosphoinositide- and Ca2+-binding properties of normal and cognitive performance-linked variant forms of KIBRA C2 domain,published,journal,J. Biol. Chem.,,293,24,,,,,,,,,,,,,,,,,,,,,,9335,9344,2018, citations,entry_citation,27431,154802,1,,entry citation,,,30125090,,,Sequence-Specific Solution NMR Assignments of the beta-Barrel Insertase BamA to Monitor Its Conformational Ensemble at the Atomic Level,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,140,36,,1520-5126,,,,,,,,,,,,,,,,,,,,11252,11260,2018, citations,entry_citation,27432,154836,1,,entry citation,,,30631134,,,Structure of the SLy1 SAM homodimer reveals a new interface for SAM domain self-association.,published,journal,Sci. Rep.,Scientific reports,9,1,,2045-2322,,,,,,,,,,,,,,,,,,,,54,54,2019, citations,entry_citation,27433,154855,1,,entry citation,,,,,,"Production and characterization of double knot toxin (DkTx), a TrpV1 channel agonist.",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,27434,154869,1,,entry citation,,,29740459,,,3D Structures of Plant Phytochrome A as Pr and Pfr From Solid-State NMR: Implications for Molecular Function,published,journal,Front. Plant Sci.,Frontiers in plant science,9,,,1664-462X,,,,,,,,,,,,,,,,,,,,498,498,2018, citations,entry_citation,27435,154887,1,,entry citation,,,30109462,,,NMR assignments for monomeric phage L decoration protein,published,journal,Biomol. NMR Assignments,,12,2,,,,,,,,,,,,,,,,,,,,,,339,343,2018, citations,entry_citation,27436,154906,1,,entry citation,,,30242623,,,Backbone and side-chain resonance assignments of the methyl-CpG-binding domain of MBD6 from Arabidopsis thaliana,published,journal,Biomol. NMR Assignments,,13,1,,,,,,,,,,,,,,,,,,,,,,59,62,2019, citations,entry_citation,27437,154923,1,,entry citation,,,,,,Insight into Small Molecule Binding to the Neonatal Fc Receptor by X-ray Crystallography and 100 kHz Magic-Angle-Spinning NMR,submitted,journal,PLOS Biology,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,27438,154939,1,,entry citation,,,29724821,,,Phosphoinositide-interacting regulator of TRP (PIRT) has opposing effects on human and mouse TRPM8 ion channels,published,journal,J. Biol. Chem.,The Journal of biological chemistry,293,24,,1083-351X,,,,,,,,,,,,,,,,,,,,9423,9434,2018, citations,entry_citation,27439,154955,1,,entry citation,,,30284185,10.1007/s12104-018-9853-0,,"1H, 13C and 15N NMR assignments of self-incompatibility protein homologue 15 from Arabidopsis thaliana",published,journal,Biomol. NMR Assignments,,13,1,,,,,,,,,,,,,,,,,,,,,,67,70,2019, citations,entry_citation,27440,154974,1,,entry citation,,,30135211,10.1074/jbc.RA118.003832,,Peptide-MHC (pMHC) binding to a human antiviral T cell receptor induces long-range allosteric communication between pMHC- and CD3-binding sites,published,journal,J. Biol. Chem.,The Journal of biological chemistry,293,41,,1083-351X,,,,,,,,,,,,,,,,,,,,15991,16005,2018, citations,entry_citation,27441,154990,1,,entry citation,,,30135211,10.1074/jbc.RA118.003832,,Peptide-MHC (pMHC) binding to a human antiviral T cell receptor induces long-range allosteric communication between pMHC- and CD3-binding sites,published,journal,J. Biol. Chem.,The Journal of biological chemistry,293,41,,1083-351X,,,,,,,,,,,,,,,,,,,,15991,16005,2018, citations,entry_citation,27442,155006,1,,entry citation,,,30177392,,,Solution structure of the N-terminal domain of proteasome lid subunit Rpn5,published,journal,Biochem. Biophys. Res. 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NMR Assignments,,12,2,,,,,,,,,,,,,,,,,,,,,,315,318,2018, citations,entry_citation,27447,155069,1,,entry citation,,,30328810,,,Tuning site-specific dynamics to drive allosteric activation in a pneumococcal zinc uptake regulator,published,journal,eLife,,7,,,,,,,,,,,,,,,,,,,,,,,e37268,e37268,2018, citations,entry_citation,27448,155101,1,,entry citation,,,30328810,,,Tuning site-specific dynamics to drive allosteric activation in a pneumococcal zinc uptake regulator,published,journal,eLife,,7,,,,,,,,,,,,,,,,,,,,,,,e37268,e37268,2018, citations,Citation_1,27450,155147,1,,entry citation,,,30159810,,,"Resonance assignments of wild-type and two cysteine-free variants of the four-helix bundle protein, Rop",published,journal,Biomol. NMR Assignments,,12,2,,,,,,,,,,,,,,,,,,,,,,345,350,2018, citations,Citation_1,27451,155163,1,,entry citation,,,30159810,,,"Resonance assignments of wild-type and two cysteine-free variants of the four-helix bundle protein, Rop",published,journal,Biomol. NMR Assignments,,12,2,,,,,,,,,,,,,,,,,,,,,,345,350,2018, citations,entry_citation,27452,155178,1,,entry citation,,,30051308,10.1007/s12104-018-9834-3,,NMR resonance assignments for the SAM/SAH-binding riboswitch RNA bound to S-adenosylhomocysteine,published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,12,2,,1874-270X,,,,,,,,,,,,,,,,,,,,329,334,2018, citations,entry_citation,27453,155212,1,,entry citation,,,29934867,,,NMR resonance assignments for a ProQ homolog from Legionella pneumophila,published,journal,Biomol. NMR Assignments,,12,2,,,,,,,,,,,,,,,,,,,,,,319,322,2018, citations,entry_citation,27455,155233,1,,entry citation,,,29953213,,,Functional Role of Solvent Entropy and Conformational Entropy of Metal Binding in a Dynamically Driven Allosteric System,published,journal,J. Am. Chem. Soc.,,140,29,,,,,,,,,,,,,,,,,,,,,,9108,9119,2018, citations,entry_citation,27457,155260,1,,entry citation,,,29905032,,,Structure and Dynamics in the Nucleosome Revealed by Solid-State NMR,published,journal,Angew. Chem. Int. Ed. Engl.,,57,,,,,,,,,,,,,,,,,,,,,,,9734,9738,2018, citations,entry_citation,27458,155276,1,,entry citation,,,30054867,10.1007/s12104-018-9835-2,,"Backbone and side-chain chemical shift assignments of MarH, a critical intermediary epimerase for biosynthesis of Maremycins in Streptomyces",published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,12,2,,1874-270X,,,,,,,,,,,,,,,,,,,,335,338,2018, citations,entry_citation,27459,155294,1,,entry citation,,,29953213,,,Functional Role of Solvent Entropy and Conformational Entropy of Metal Binding in a Dynamically Driven Allosteric System,published,journal,J. Am. Chem. Soc.,,140,29,,,,,,,,,,,,,,,,,,,,,,9108,9119,2018, citations,entry_citation,27460,155323,1,,entry citation,,,29844575,,,Conformation and dynamics of soluble repetitive domain elucidates the initial beta-sheet formation of spider silk,published,journal,Nat. Commun.,,9,1,,,,,,,,,,,,,,,,,,,,,,2121,2121,2018, citations,entry_citation,27461,155342,1,,entry citation,,,30060237,,,TGIF1 homeodomain interacts with Smad MH1 domain and represses TGF-beta signaling.,published,journal,Nucleic Acids Res.,Nucleic acids research,46,17,,1362-4962,,,,,,,,,,,,,,,,,,,,9220,9235,2018, citations,BLVRB_citaiton_1,27462,155358,1,,entry citation,,,29932944,,,Biliverdin Reductase B Dynamics Are Coupled to Coenzyme Binding.,published,journal,J. Mol. Biol.,Journal of molecular biology,430,18 Pt B,,1089-8638,,,,,,,,,,,,,,,,,,,,3234,3250,2018, citations,BLVRB_citaiton_1,27463,155374,1,,entry citation,,,29932944,,,Biliverdin Reductase B Dynamics Are Coupled to Coenzyme Binding.,published,journal,J. Mol. Biol.,Journal of molecular biology,430,18 Pt B,,1089-8638,,,,,,,,,,,,,,,,,,,,3234,3250,2018, citations,entry_citation,27464,155392,1,,entry citation,,,30770806,10.1038/s41467-019-08686-0,,ASPP proteins discriminate between PP1 catalytic subunits through their SH3 domain and the PP1 C-tail,published,journal,Nat. Commun.,Nature communications,10,1,,2041-1723,,,,,,,,,,,,,,,,,,,,771,771,2019, citations,entry_citation,27465,155405,1,,entry citation,,,32277554,10.1002/anie.202003527,,Membrane Proteins Have Distinct Fast Internal Motion and Residual Conformational Entropy,published,journal,Angew. Chem. Int. Ed. Engl.,Angewandte Chemie (International ed. in English),59,27,,1521-3773,,,,,,,,,,,,,,,,,,,,11108,11114,2020, citations,entry_citation,27466,155420,1,,entry citation,,,30127417,10.1038/s41467-018-05776-3,,The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation,published,journal,Nat. 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Commun.,Nature communications,9,1,,2041-1723,,,,,,,,,,,,,,,,,,,,3321,3321,2018, citations,entry_citation,27468,155450,1,,entry citation,,,29917302,,,Protein-Protein Interfaces Probed by Methyl Labeling and Proton-Detected Solid-State NMR Spectroscopy,published,journal,Chemphyschem,Chemphyschem : a European journal of chemical physics and physical chemistry,19,19,,1439-7641,,,,,,,,,,,,,,,,,,,,2457,2460,2018, citations,entry_citation,27469,155471,1,,entry citation,,,,10.1021/acscatal.8b02810,,"Nonequivalence of Second Sphere ""Noncatalytic"" Residues in Pentaerythritol Tetranitrate Reductase in Relation to Local Dynamics Linked to H-Transfer in Reactions with NADH and NADPH Coenzymes",published,journal,ACS Catal.,,8,,,,,,,,,,,,,,,,,,,,,,,11589,11599,2018, citations,entry_citation,27470,155488,1,,entry citation,,,,10.1021/acscatal.8b02810,,"Nonequivalence of Second Sphere ""Noncatalytic"" Residues in Pentaerythritol Tetranitrate Reductase in Relation to Local Dynamics Linked to H-Transfer in Reactions with NADH and NADPH Coenzymes",published,journal,ACS Catal.,,8,,,,,,,,,,,,,,,,,,,,,,,11589,11599,2018, citations,entry_citation,27471,155505,1,,entry citation,,,31476357,,,Structural insights into the AapA1 toxin of Helicobacter pylori,published,journal,Biochim. 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Commun.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,Citation_1,27476,155571,1,,entry citation,,,30659884,10.1016/j.bbagen.2019.01.008,,Structure and proteolytic susceptibility of the inhibitory C-terminal tail of cardiac troponin I.,published,journal,Biochim. Biophys. Acta Gen. Subj.,Biochimica et biophysica acta. General subjects,1863,4,,1872-8006,,,,,,,,,,,,,,,,,,,,661,671,2019, citations,entry_citation,27477,155585,1,,entry citation,,,30229450,,,"1H, 13C, and 15N resonance assignments of the C-terminal lobe of the human HECT E3 ubiquitin ligase ITCH",published,journal,Biomol. NMR Assignments,,13,1,,,,,,,,,,,,,,,,,,,,,,15,20,2019, citations,entry_citation,27478,155609,1,,entry citation,,,30627403,10.1039/c8sc03655a,,Structural studies suggest aggregation as one of the modes of action for teixobactin.,published,journal,Chem. Sci.,Chemical science,9,47,,2041-6520,,,,,,,,,,,,,,,,,,,,8850,8859,2018, citations,entry_citation,27479,155627,1,,entry citation,,,30627403,10.1039/c8sc03655a,,Structural studies suggest aggregation as one of the modes of action for teixobactin.,published,journal,Chem. Sci.,Chemical science,9,47,,2041-6520,,,,,,,,,,,,,,,,,,,,8850,8859,2018, citations,entry_citation,27480,155645,1,,entry citation,,,30627403,10.1039/c8sc03655a,,Structural studies suggest aggregation as one of the modes of action for teixobactin.,published,journal,Chem. Sci.,Chemical science,9,47,,2041-6520,,,,,,,,,,,,,,,,,,,,8850,8859,2018, citations,entry_citation,27481,155663,1,,entry citation,,,31509280,,,"Uno Ferro, a de novo designed protein, binds transition metals with high affinity and stabilizes semiquinone radical anion",published,journal,Chemistry,"Chemistry (Weinheim an der Bergstrasse, Germany)",25,67,,1521-3765,,,,,,,,,,,,,,,,,,,,15252,15256,2019, citations,SET-FTY720,27482,155678,1,,entry citation,,,30917007,,,The NMR-based characterization of the FTY720-SET complex reveals an alternative mechanism for the attenuation of the inhibitory SET-PP2A interaction,published,journal,FASEB J.,FASEB journal,33,6,,1530-6860,,,,,,,,,,,,,,,,,,,,7647,7666,2019, citations,entry_citation,27483,155694,1,,entry citation,,,,10.1038/s41598-018-33379-x,,Overlapping motifs on the herpes viral proteins ICP27 and ORF57 mediate interactions with the mRNA export adaptors ALYREF and UIF,published,journal,Sci. Rep.,,8,,,,,,,,,,,,,,,,,,,,,,,15005,15005,2018, citations,entry_citation,27484,155709,1,,entry citation,,,,10.1038/s41598-018-33379-x,,Overlapping motifs on the herpes viral proteins ICP27 and ORF57 mediate interactions with the mRNA export adaptors ALYREF and UIF,published,journal,Sci. Rep.,,8,,,,,,,,,,,,,,,,,,,,,,,15005,15005,2018, citations,citation_1,27485,155725,1,,entry citation,,,30249616,10.1074/jbc.RA118.005649,,Molecular determinants of alpha-conotoxin potency for inhibition of human and rat alpha6beta4 nicotinic acetylcholine receptors,published,journal,J. Biol. Chem.,The Journal of biological chemistry,293,46,,1083-351X,,,,,,,,,,,,,,,,,,,,17838,17852,2018, citations,citations_1,27488,155740,1,,entry citation,,,31623019,,,The redox-active site of thioredoxin is directly involved in apoptosis signal-regulating kinase 1 binding that is modulated by oxidative stress,published,journal,FEBS J.,,287,8,,,,,,,,,,,,,,,,,,,,,,1626,1644,2020, citations,entry_citation,27489,155755,1,,entry citation,,,30124944,,,Conformational switch in the ribosomal protein S1 guides unfolding of structured RNAs for translation initiation,published,journal,Nucleic Acids Res.,,46,20,,,,,,,,,,,,,,,,,,,,,,10917,10929,2018, citations,entry_citation,27490,155773,1,,entry citation,,,30124944,,,Conformational switch in the ribosomal protein S1 guides unfolding of structured RNAs for translation initiation,published,journal,Nucleic Acids Res.,,46,20,,,,,,,,,,,,,,,,,,,,,,10917,10929,2018, citations,entry_citation,27491,155789,1,,entry citation,,,30543823,,,Directed Evolution of Canonical Loops and Their Swapping between Unrelated Serine Proteinase Inhibitors Disprove the Interscaffolding Additivity Model,published,journal,J. Mol. Biol.,Journal of molecular biology,431,3,,1089-8638,,,,,,,,,,,,,,,,,,,,557,575,2019, citations,entry_citation,27492,155804,1,,entry citation,,,30543823,,,Directed Evolution of Canonical Loops and Their Swapping between Unrelated Serine Proteinase Inhibitors Disprove the Interscaffolding Additivity Model,published,journal,J. Mol. Biol.,Journal of molecular biology,431,3,,1089-8638,,,,,,,,,,,,,,,,,,,,557,575,2019, citations,entry_citation,27493,155819,1,,entry citation,,,30655293,10.1074/jbc.RA118.004723,,The copBL operon protects Staphylococcus aureus from copper toxicity: CopL is an extracellular membrane-associated copper-binding protein,published,journal,J. Biol. Chem.,The Journal of biological chemistry,294,11,,1083-351X,,,,,,,,,,,,,,,,,,,,4027,4044,2019, citations,entry_citation,27494,155844,1,,entry citation,,,32071088,,,Modulation of conformational equilibrium by phosphorylation underlies the activation of deubiquitinase A,published,journal,J. Biol. Chem.,The Journal of biological chemistry,,,,1083-351X,,,,,,,,,,,,,,,,,,,,,,2020, citations,entry_citation,27495,155859,1,,entry citation,,,32071088,,,Modulation of conformational equilibrium by phosphorylation underlies the activation of deubiquitinase A,published,journal,J. Biol. Chem.,The Journal of biological chemistry,,,,1083-351X,,,,,,,,,,,,,,,,,,,,,,2020, citations,entry_citation,27496,155875,1,,entry citation,,,29972810,,,Dynamic allostery in PLC 1 and its modulation by a cancer mutation revealed by MD simulation and NMR,published,journal,Biophys. J.,,115,1,,,,,,,,,,,,,,,,,,,,,,31,45,2018, citations,entry_citation,27497,155894,1,,entry citation,,,30289063,,,Structural Insights on the Obscurin-Binding Domains in Titin,published,journal,Protein Pept. Letter,,25,11,,,,,,,,,,,,,,,,,,,,,,973,979,2018, citations,entry_citation,27498,155908,1,,entry citation,,,27498,,,"1H, 15N and 13C resonance assignments of the C-terminal domain of the P protein of the Nishigahara strain of rabies virus",published,journal,Biomol. NMR Assignments,,,,,,,,,,,,,,,,,,,,,,,,,,,2018, citations,entry_citation,27499,155933,1,,entry citation,,,,,,NMR assignments of the the protein SFRS1-RRM1,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,275,155947,1,,entry citation,,,,,"Fogh, Rasmus H., Mabbutt, Bridget C., Kem, William R., Norton, Raymond S., ""Sequence-Specific 1H NMR Assignments and Secondary Structure in the Sea Anemone Stichodactyla helianthus Neurotoxin I,"" Biochemistry 28, 1826-1834 (1989).","Sequence-Specific 1H NMR Assignments and Secondary Structure in the Sea Anemone Stichodactyla helianthus Neurotoxin I",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,1826,1834,1989, citations,entry_citation,27500,155960,1,,entry citation,,,30543823,,,Directed Evolution of Canonical Loops and Their Swapping between Unrelated Serine Proteinase Inhibitors Disprove the Interscaffolding Additivity Model,published,journal,J. Mol. Biol.,Journal of molecular biology,431,3,,1089-8638,,,,,,,,,,,,,,,,,,,,557,575,2019, citations,entry_citation,27501,155978,1,,entry citation,,,30543823,,,Directed Evolution of Canonical Loops and Their Swapping between Unrelated Serine Proteinase Inhibitors Disprove the Interscaffolding Additivity Model,published,journal,J. Mol. Biol.,Journal of molecular biology,431,3,,1089-8638,,,,,,,,,,,,,,,,,,,,557,575,2019, citations,entry_citation,27502,155993,1,,entry citation,,,29771498,10.1021/jacs.7b09670,,"Structure and Function of the Transmembrane Domain of NsaS, an Antibiotic Sensing Histidine Kinase in Staphylococcus aureus.",published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,140,24,,1520-5126,,,,,,,,,,,,,,,,,,,,7471,7485,2018, citations,entry_citation,27503,156008,1,,entry citation,,,30099718,,,Backbone and side chain NMR assignments for the ribosome Elongation Factor P (EF-P) from Staphylococcus aureus,published,journal,Biomol. NMR Assignments,,12,2,,,,,,,,,,,,,,,,,,,,,,351,355,2018, citations,entry_citation,27506,156022,1,,entry citation,,,30242622,,,Chemical shift assignment of the viral protein genome-linked (VPg) from potato virus Y,published,journal,Biomol. NMR Assignments,,13,1,,,,,,,,,,,,,,,,,,,,,,9,13,2019, citations,entry_citation,27508,156043,1,,entry citation,,,29964046,,,Beta-Sheet Augmentation Is a Conserved Mechanism of Priming HECT E3 Ligases for Ubiquitin Ligation,published,journal,J. Mol. Biol.,,430,,,,,,,,,,,,,,,,,,,,,,,3218,3233,2018, citations,entry_citation,27509,156057,1,,entry citation,,,30598509,10.1074/jbc.RA118.006848,,A ligand-induced structural change in fatty acid-binding protein 1 is associated with potentiation of peroxisome proliferator-activated receptor alpha agonists,published,journal,J. Biol. Chem.,The Journal of biological chemistry,294,10,,1083-351X,,,,,,,,,,,,,,,,,,,,3720,3734,2019, citations,entry_citation,27510,156073,1,,entry citation,,,30598509,10.1074/jbc.RA118.006848,,A ligand-induced structural change in fatty acid-binding protein 1 is associated with potentiation of peroxisome proliferator-activated receptor alpha agonists,published,journal,J. Biol. Chem.,The Journal of biological chemistry,294,10,,1083-351X,,,,,,,,,,,,,,,,,,,,3720,3734,2019, citations,entry_citation,27511,156089,1,,entry citation,,,29964046,,,Beta-Sheet Augmentation Is a Conserved Mechanism of Priming HECT E3 Ligases for Ubiquitin Ligation,published,journal,J. Mol. Biol.,,430,,,,,,,,,,,,,,,,,,,,,,,3218,3233,2018, citations,entry_citation,27512,156103,1,,entry citation,,,29964046,,,Beta-Sheet Augmentation Is a Conserved Mechanism of Priming HECT E3 Ligases for Ubiquitin Ligation,published,journal,J. Mol. Biol.,,430,,,,,,,,,,,,,,,,,,,,,,,3218,3233,2018, citations,entry_citation,27513,156117,1,,entry citation,,,29972637,,,NMR Measurements Reveal the Structural Basis of Transthyretin Destabilization by Pathogenic Mutations,published,journal,Biochemistry,Biochemistry,57,30,,1520-4995,,,,,,,,,,,,,,,,,,,,4421,4430,2018, citations,entry_citation,27514,156131,1,,entry citation,,,29972637,,,NMR Measurements Reveal the Structural Basis of Transthyretin Destabilization by Pathogenic Mutations,published,journal,Biochemistry,Biochemistry,57,30,,1520-4995,,,,,,,,,,,,,,,,,,,,4421,4430,2018, citations,entry_citation,27515,156145,1,,entry citation,,,29972637,,,NMR Measurements Reveal the Structural Basis of Transthyretin Destabilization by Pathogenic Mutations,published,journal,Biochemistry,Biochemistry,57,30,,1520-4995,,,,,,,,,,,,,,,,,,,,4421,4430,2018, citations,entry_citation,27516,156159,1,,entry citation,,,29972637,,,NMR Measurements Reveal the Structural Basis of Transthyretin Destabilization by Pathogenic Mutations,published,journal,Biochemistry,Biochemistry,57,30,,1520-4995,,,,,,,,,,,,,,,,,,,,4421,4430,2018, citations,citation_1,27517,156173,1,,entry citation,,,30232260,,,Structural basis for cooperative regulation of KIX-mediated transcription pathways by the HTLV-1 HBZ activation domain,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,115,40,,1091-6490,,,,,,,,,,,,,,,,,,,,10040,10045,2018, citations,entry_citation,27518,156187,1,,entry citation,,,30328057,10.1007/s12104-018-9855-y,,Chemical shift assignments of a camelid nanobody against aflatoxin B,published,journal,Biomol NMR Assign,Biomolecular NMR assignments,13,1,,1874-270X,,,,,,,,,,,,,,,,,,,,75,78,2019, citations,entry_citation,27519,156203,1,,entry citation,,,,,,Solution NMR chemical shift assignments of nanobody Nb11 specific for aflatoxin B1,in preparation,journal,Structure,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,27520,156225,1,,entry citation,,,30375376,,,Mechanism of activating mutations and allosteric drug inhibition of the phosphatase SHP2,published,journal,Nat. Commun.,,9,1,,,,,,,,,,,,,,,,,,,,,,4507,4507,2018, citations,entry_citation,27521,156246,1,,entry citation,,,30375376,,,Mechanism of activating mutations and allosteric drug inhibition of the phosphatase SHP2,published,journal,Nat. Commun.,,9,1,,,,,,,,,,,,,,,,,,,,,,4507,4507,2018, citations,entry_citation,27522,156266,1,,entry citation,,,30375376,,,Mechanism of activating mutations and allosteric drug inhibition of the phosphatase SHP2,published,journal,Nat. Commun.,,9,1,,,,,,,,,,,,,,,,,,,,,,4507,4507,2018, citations,citation_hbd,27523,156285,1,,entry citation,,,,,,A small helical bundle prepares primer synthesis by binding two ATP nucleotides that enhance sequence-specific recognition of the DNA tempate,in preparation,journal,Cell,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,27524,156307,1,,entry citation,,,30232732,,,"Sequence specific 1H, 13C and 15N resonance assignments of the C-terminal domain of human Gamma S-crystallin",published,journal,Biomol. NMR Assignments,,13,1,,,,,,,,,,,,,,,,,,,,,,43,47,2019, citations,entry_citation,27525,156321,1,,entry citation,,,,,,High resolution X-ray and NMR structural study of human T-cell immunoglobulin and mucin domain containing protein-3,published,journal,Sci. Rep.,,8,,,,,,,,,,,,,,,,,,,,,,,17512,17512,2018, citations,entry_citation,27526,156337,1,,entry citation,,,30504777,10.1038/s41467-018-07481-7,,Force-dependent allostery of the alpha-catenin actin-binding domain controls adherens junction dynamics and functions,published,journal,Nat. Commun.,Nature communications,9,1,,2041-1723,,,,,,,,,,,,,,,,,,,,5121,5121,2018, citations,entry_citation,27527,156351,1,,entry citation,,,30127417,10.1038/s41467-018-05776-3,,The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation,published,journal,Nat. Commun.,Nature communications,9,1,,2041-1723,,,,,,,,,,,,,,,,,,,,3321,3321,2018, citations,entry_citation,27528,156365,1,,entry citation,,,31400120,,,The MLL1 trimeric catalytic complex is a dynamic conformational ensemble stabilized by multiple weak interactions,published,journal,Nucleic Acids Res.,Nucleic acids research,47,17,,1362-4962,,,,,,,,,,,,,,,,,,,,9433,9447,2019, citations,entry_citation,27529,156381,1,,entry citation,,,,,,NMR resonance assignment of ubiquitin specific protease 7 (USP7).,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,27530,156395,1,,entry citation,,,,,,ApoCaM bound to Cav1.2 IQ,in preparation,journal,Cell,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,27531,156410,1,,entry citation,,,30229449,,,Backbone chemical shift assignment of macrophage infectivity potentiator virulence factor of Trypanosoma cruzi,published,journal,Biomol. NMR Assignments,,13,1,,,,,,,,,,,,,,,,,,,,,,21,25,2019, citations,entry_citation,27532,156429,1,,entry citation,,,30225569,,,Backbone and side chain NMR assignments for the ribosome binding factor A (RbfA) from Staphylococcus aureus,published,journal,Biomol. NMR Assignments,,13,1,,,,,,,,,,,,,,,,,,,,,,27,30,2019, citations,entry_citation,27533,156444,1,,entry citation,,,31264103,10.1007/s12104-019-09902-0,,Solution NMR backbone assignment reveals interaction-free tumbling of human lineage-specific Olduvai protein domains,published,journal,Biomol. NMR Assign.,,13,2,,,,,,,,,,,,,,,,,,,,,,339,343,2019, citations,entry_citation,27534,156460,1,,entry citation,,,30289697,,,Antiparallel Coiled-Coil Interactions Mediate the Homodimerization of the DNA Damage-Repair Protein PALB2,published,journal,Biochemistry,,57,47,,,,,,,,,,,,,,,,,,,,,,6581,6591,2018, citations,entry_citation,27536,156499,1,,entry citation,,,30244308,,,"1H, 13C and 15N backbone and side-chain assignment of a carbohydrate binding module from a xylanase from Roseburia intestinalis",published,journal,Biomol. NMR Assignments,,13,1,,,,,,,,,,,,,,,,,,,,,,55,58,2018, citations,entry_citation,27537,156515,1,,entry citation,,,30414042,,,A CON-based NMR assignment strategy for pro-rich intrinsically disordered proteins with low signal dispersion: the C-terminal domain of histone H1.0 as a case study,published,journal,J. Biomol. NMR,,72,3,,,,,,,,,,,,,,,,,,,,,,139,148,2018, citations,entry_citation,27538,156534,1,,entry citation,,,30414042,,,A CON-based NMR assignment strategy for pro-rich intrinsically disordered proteins with low signal dispersion: the C-terminal domain of histone H1.0 as a case study,published,journal,J. Biomol. NMR,,72,3,,,,,,,,,,,,,,,,,,,,,,139,148,2018, citations,entry_citation,27539,156555,1,,entry citation,,,30076219,,,Structural analyses reveal the mechanism of inhibition of influenza virus NS1 by two antiviral compounds,published,journal,J. Biol. Chem.,,293,38,,,,,,,,,,,,,,,,,,,,,,14659,14668,2018, citations,entry_citation,27540,156573,1,,entry citation,,,30729401,10.1007/s12104-019-09880-3,,Backbone resonance assignments of innate immune evasion protein EapH2 from the S. aureus.,published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,13,1,,1874-270X,,,,,,,,,,,,,,,,,,,,219,222,2019, citations,entry_citation,27541,156589,1,,entry citation,,,30076219,,,Structural analyses reveal the mechanism of inhibition of influenza virus NS1 by two antiviral compounds,published,journal,J. Biol. Chem.,,293,38,,,,,,,,,,,,,,,,,,,,,,14659,14668,2018, citations,entry_citation,27542,156607,1,,entry citation,,,,,,Macaca fascicularis Eosinophil Cationic Protein backbone assignment,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,27543,156621,1,,entry citation,,,30554144,,,A serine in the first transmembrane domain of the human E3 ubiquitin ligase MARCH9 is critical for down-regulation of its protein substrates,published,journal,J. Biol. Chem.,The Journal of biological chemistry,294,7,,1083-351X,,,,,,,,,,,,,,,,,,,,2470,2485,2019, citations,entry_citation,27544,156636,1,,entry citation,,,,,,Pongo pygmaeus Eosinophil Cationic Protein backbone assignment,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,27545,156650,1,,entry citation,,,,,,Pongo abelii ribonuclease 3 backbone assignment,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,27546,156664,1,,entry citation,,,,,,Aotus trivirgatus Eosinophil-Derived Neurotoxin backbone assignment,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,27547,156678,1,,entry citation,,,30988309,,,Structural basis of specific H2A K13/K15 ubiquitination by RNF168.,published,journal,Nat. Commun.,Nature communications,10,1,,2041-1723,,,,,,,,,,,,,,,,,,,,1751,1751,2019, citations,entry_citation,27548,156693,1,,entry citation,,,30060237,,,TGIF1 homeodomain interacts with Smad MH1 domain and represses TGF-beta signaling.,published,journal,Nucleic Acids Res.,Nucleic acids research,46,17,,1362-4962,,,,,,,,,,,,,,,,,,,,9220,9235,2018, citations,manuscript,27549,156710,1,,entry citation,,,30309612,,,Characterization of TDP-43 RRM2 Partially Folded States and Their Significance to ALS Pathogenesis.,published,journal,Biophys. J.,Biophysical journal,115,9,,1542-0086,,,,,,,,,,,,,,,,,,,,1673,1680,2018, citations,entry_citation,27550,156726,1,,entry citation,,,30301765,,,The Streptococcus pyogenes Shr protein captures human hemoglobin using two structurally unique binding domains,published,journal,J. Biol. Chem.,,293,47,,1083-351X,,,,,,,,,,,,,,,,,,,,18365,18377,2018, citations,entry_citation,27552,156746,1,,entry citation,,,,,,Assigned Chemical Shifts for m62A-h45,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,27553,156760,1,,entry citation,,,30284668,,,"1H, 15N, and 13C resonance assignments of the intrinsically disordered SH4 and Unique domains of Hck",published,journal,Biomol. NMR Assignments,,13,1,,,,,,,,,,,,,,,,,,,,,,71,74,2019, citations,entry_citation,27554,156778,1,,entry citation,,,30284668,,,"1H, 15N, and 13C resonance assignments of the intrinsically disordered SH4 and Unique domains of Hck",published,journal,Biomol. NMR Assignments,,13,1,,,,,,,,,,,,,,,,,,,,,,71,74,2019, citations,citations_1,27555,156796,1,,entry citation,,,30279485,,,RIP2 filament formation is required for NOD2 dependent NF-B signalling,published,journal,Nat. Commun.,,9,1,,,,,,,,,,,,,,,,,,,,,,4043,4043,2018, citations,entry_citation,27556,156812,1,,entry citation,,,30879887,10.1016/j.str.2019.02.007,,Surface-Binding to Cardiolipin Nanodomains Triggers Cytochrome c Pro-apoptotic Peroxidase Activity via Localized Dynamics.,published,journal,Structure,"Structure (London, England : 1993)",27,5,,1878-4186,,,,,,,,,,,,,,,,,,,,806,815,2019, citations,entry_citation,27557,156828,1,,entry citation,,,30439429,10.1016/j.ijbiomac.2018.11.054,,Molecular interaction between human SUMO-I and histone like DNA binding protein of Helicobacter pylori (Hup) investigated by NMR and other biophysical tools,published,journal,Int. J. Biol. Macromol.,International journal of biological macromolecules,123,,,1879-0003,,,,,,,,,,,,,,,,,,,,446,456,2018, citations,Citation_q,27558,156844,1,,entry citation,,,30102405,,,p15PAF binding to PCNA modulates the DNA sliding surface.,published,journal,Nucleic Acids Res.,Nucleic acids research,46,18,,1362-4962,,,,,,,,,,,,,,,,,,,,9816,9828,2018, citations,citation_1,27559,156858,1,,entry citation,,,30239932,,,I260Q DNA polymerase beta highlights precatalytic conformational rearrangements critical for fidelity,published,journal,Nucleic Acids Res.,,46,20,,,,,,,,,,,,,,,,,,,,,,10740,10756,2018, citations,citation_1,27560,156873,1,,entry citation,,,30239932,,,I260Q DNA polymerase beta highlights precatalytic conformational rearrangements critical for fidelity,published,journal,Nucleic Acids Res.,,46,20,,,,,,,,,,,,,,,,,,,,,,10740,10756,2018, citations,citation_1,27561,156891,1,,entry citation,,,30239932,,,I260Q DNA polymerase beta highlights precatalytic conformational rearrangements critical for fidelity,published,journal,Nucleic Acids Res.,,46,20,,,,,,,,,,,,,,,,,,,,,,10740,10756,2018, citations,entry_citation,27562,156911,1,,entry citation,,,30070484,,,Simple and Robust Study of Backbone Dynamics of Crystalline Proteins Employing 1H-15N Dipolar Coupling Dispersion,published,journal,J. Phys. Chem. B.,,122,34,,,,,,,,,,,,,,,,,,,,,,8146,8156,2018, citations,entry_citation,27563,156925,1,,entry citation,,,30377945,,,Backbone chemical shift assignments of human 14-3-3sigma.,published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,13,1,,1874-270X,,,,,,,,,,,,,,,,,,,,103,107,2019, citations,entry_citation,27564,156940,1,,entry citation,,,31009467,,,A DNA aptamer reveals an allosteric site for inhibition in metallo-beta-lactamases,published,journal,PLoS One,,14,4,,,,,,,,,,,,,,,,,,,,,,,e0214440,e0214440,2019 citations,entry_citation,27565,156958,1,,entry citation,,,30332472,,,"TMEM106B, a risk factor for FTLD and aging, has an intrinsically disordered cytoplasmic domain",published,journal,PLoS One,,13,10,,,,,,,,,,,,,,,,,,,,,,e0205856,e0205856,2018, citations,entry_citation,27566,156973,1,,entry citation,,,30298375,,,Backbone resonance assignment for the N-terminal region of bacterial tRNA-(N'1G37) methyltransferase,published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,13,1,,1874-270X,,,,,,,,,,,,,,,,,,,,49,53,2019, citations,entry_citation,27567,156990,1,,entry citation,,,,,,Structural analyses of HIV-1 Tat interactions with cellular 7SK and viral TAR RNAs identifies molecular mimicry,in preparation,journal,Nat. Commun.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,27569,157019,1,,entry citation,,,31264103,10.1007/s12104-019-09902-0,,Solution NMR backbone assignment reveals interaction-free tumbling of human lineage-specific Olduvai protein domains,published,journal,Biomol. NMR Assign.,,13,2,,,,,,,,,,,,,,,,,,,,,,339,343,2019, citations,entry_citation,27570,157035,1,,entry citation,,,30850624,,,Global response of wild-type E.coli diacylglycerol kinase towards nucleotide and lipid substrate binding observed by 3D and 2D MAS NMR,published,journal,Sci. Rep.,,9,1,,,,,,,,,,,,,,,,,,,,,,3995,3995,2019, citations,citation_1,27571,157052,1,,entry citation,,,31260268,,,Crystal Structures and Nuclear Magnetic Resonance Studies of the Apo Form of the c-MYC:MAX bHLHZip Complex Reveal a Helical Basic Region in the Absence of DNA,published,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,,2019, citations,entry_citation,28001,163391,1,,entry citation,,,31604242,,,Structural basis for client recognition and activity of Hsp40 chaperones,published,journal,Science,,365,6459,,,,,,,,,,,,,,,,,,,,,,1313,1319,2019, citations,citation_2,27571,157053,2,,reference citation,,,30222246,,,The structure of INI1/hSNF5 RPT1 and its interactions with the c-MYC:MAX heterodimer provide insights into the interplay between MYC and the SWI/SNF chromatin remodeling complex,published,journal,FEBS J.,,285,22,,,,,,,,,,,,,,,,,,,,,,4165,4180,2018, citations,entry_citation,27572,157069,1,,entry citation,,,30262913,,,High-resolution NMR studies of antibiotics in cellular membranes,published,journal,Nat. Commun.,,9,1,,,,,,,,,,,,,,,,,,,,,,3963,3963,2018, citations,entry_citation,27573,157093,1,,entry citation,,,30824543,10.1074/jbc.RA118.006642,,A conserved and buried edge-to-face aromatic interaction in small ubiquitin-like modifier (SUMO) has a role in SUMO stability and function,published,journal,J. Biol. Chem.,The Journal of biological chemistry,294,17,,1083-351X,,,,,,,,,,,,,,,,,,,,6772,6784,2019, citations,entry_citation,27574,157107,1,,entry citation,,,30598510,,,TGF-b2 uses the concave surface of its extended finger region to bind betaglycan's ZP domain via three residues specific to TGF-b and Inhibin-a,published,journal,J. Biol. Chem.,,294,9,,,,,,,,,,,,,,,,,,,,,,3065,3080,2019, citations,entry_citation,27575,157122,1,,entry citation,,,31502419,,,Biophysical characterization and modulation of Transthyretin Ala97Ser,published,journal,Ann. Clin. Transl. Neurol.,Annals of clinical and translational neurology,6,10,,2328-9503,,,,,,,,,,,,,,,,,,,,1961,1970,2019, citations,entry_citation,27576,157138,1,,entry citation,,,31502419,,,Biophysical characterization and modulation of Transthyretin Ala97Ser,published,journal,Ann. Clin. Transl. Neurol.,Annals of clinical and translational neurology,6,10,,2328-9503,,,,,,,,,,,,,,,,,,,,1961,1970,2019, citations,citation_1,27577,157154,1,,entry citation,,,,,,Conformational landscape alternations promote oncogenic activities of Ras-related C3 botulinum toxin substrate 1 as revealed by NMR,published,journal,Sci. Adv.,,5,3,,,,,,,,,,,,,,,,,,,,,,8945,8945,2019, citations,citation_1,27578,157173,1,,entry citation,,,32255258,,,Williams-Beuren Syndrome-Related Methyltransferase WBSCR27: Cofactor Binding and Cleavage,published,journal,FEBS J.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,27579,157195,1,,entry citation,,,30353504,10.1007/s12104-018-9857-9,,"Backbone and side-chain chemical shift assignments of full-length, apo, human Pin1, a phosphoprotein regulator with interdomain allostery",published,journal,Biomol. NMR Assignments,,13,1,,,,,,,,,,,,,,,,,,,,,,85,89,2019, citations,entry_citation,27580,157210,1,,entry citation,,,30576065,10.1111/febs.14737,,Structural characterization of VapB46 antitoxin from Mycobacterium tuberculosis: insights into VapB46-DNA binding.,published,journal,FEBS J.,The FEBS journal,286,6,,1742-4658,,,,,,,,,,,,,,,,,,,,1174,1190,2019, citations,entry_citation,27581,157224,1,,entry citation,,,30630900,10.1126/science.aao4827,,Secreted amyloid-beta precursor protein functions as a GABA,published,journal,Science,"Science (New York, N.Y.)",363,6423,,1095-9203,,,,,,,,,,,,,,,,,,,,4827,4827,2019, citations,entry_citation,27582,157241,1,,entry citation,,,30449689,,,The Structure of the SPOP-Pdx1 Interface Reveals Insights into the Phosphorylation-Dependent Binding Regulation,published,journal,Structure,,27,2,,,,,,,,,,,,,,,,,,,,,,327,334,2019, citations,entry_citation,27583,157255,1,,entry citation,,,30393051,,,The structure of the Pro-domain of mouse proNGF in contact with the NGF domain,published,journal,Structure,,27,1,,,,,,,,,,,,,,,,,,,,,,78,89,2019, citations,entry_citation,27584,157269,1,,entry citation,,,30228183,10.1074/jbc.RA118.005475,,A single residue switch reveals principles of antibody domain integrity.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,293,44,,1083-351X,,,,,,,,,,,,,,,,,,,,17107,17118,2018, citations,entry_citation,27585,157285,1,,entry citation,,,30228183,10.1074/jbc.RA118.005475,,A single residue switch reveals principles of antibody domain integrity.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,293,44,,1083-351X,,,,,,,,,,,,,,,,,,,,17107,17118,2018, citations,entry_citation,27586,157300,1,,entry citation,,,30175546,,,XLSY: Extra-Large NMR Spectroscopy,published,journal,Angew. Chem. Int Ed Engl.,,57,43,,,,,,,,,,,,,,,,,,,,,,14043,14045,2018, citations,entry_citation,27587,157318,1,,entry citation,,,31160341,10.1074/jbc.RA119.008485,,E3 ubiquitin-protein ligase TRIM21-mediated lysine capture by UBE2E1 reveals substrate-targeting mode of a ubiquitin-conjugating E2,published,journal,J. Biol. 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NMR Assignments,,13,1,,,,,,,,,,,,,,,,,,,,,,63,66,2019, citations,entry_citation,27594,157434,1,,entry citation,,,30228191,,,Archaic and alternative chaperones preserve pilin folding energy by providing incomplete structural information,published,journal,J. Biol. Chem.,,293,44,,,,,,,,,,,,,,,,,,,,,,17070,17080,2018, citations,entry_citation,27595,157459,1,,entry citation,,,30535613,,,Sequential backbone resonance assignment of AT-rich interaction domain of human BAF200,published,journal,Biomol. NMR Assignments,,13,1,,,,,,,,,,,,,,,,,,,,,,115,119,2019, citations,entry_citation,27596,157477,1,,entry citation,,,30617945,,,"1H, 13C, 15N resonance assignment of the C-terminal domain of the bifunctional enzyme TraI of plasmid R1",published,journal,Biomol. NMR Assignments,,13,1,,,,,,,,,,,,,,,,,,,,,,121,125,2019, citations,entry_citation,27598,157491,1,,entry citation,,,30650352,10.1016/j.celrep.2018.12.082,,Efficient Single-Strand Break Repair Requires Binding to Both Poly(ADP-Ribose) and DNA by the Central BRCT Domain of XRCC1.,published,journal,Cell Rep.,Cell reports,26,3,,2211-1247,,,,,,,,,,,,,,,,,,,,573,581,2019, citations,entry_citation,27599,157505,1,,entry citation,,,30420502,,,Long-range regulation of p53 DNA binding by its intrinsically disordered N-terminal transactivation domain,published,journal,Proc. Natl. Acad. Sci. 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Cell,,56,3,,,,,,,,,,,,,,,,,,,,,,453,461,2014, citations,entry_citation,27619,157802,1,,entry citation,,,31175551,10.1007/s12104-019-09900-2,,Backbone resonance assignment for the full length tRNA-(N,published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,13,2,,1874-270X,,,,,,,,,,,,,,,,,,,,327,332,2019, citations,entry_citation,27620,157816,1,,entry citation,,,30395443,,,Assessing interactions between helical aromatic oligoamide foldamers and protein surfaces: a tethering approach,published,journal,Bioconjug. Chem.,,30,1,,,,,,,,,,,,,,,,,,,,,,54,62,2019, citations,entry_citation,27621,157832,1,,entry citation,,,30802457,10.1016/j.jmb.2019.02.021,,Dynamic Studies on Intrinsically Disordered Regions of Two Paralogous Transcription Factors Reveal Rigid Segments with Important Biological Functions,published,journal,J. Mol. Biol.,Journal of molecular biology,431,7,,1089-8638,,,,,,,,,,,,,,,,,,,,1353,1369,2019, citations,entry_citation,27622,157846,1,,entry citation,,,30802457,10.1016/j.jmb.2019.02.021,,Dynamic Studies on Intrinsically Disordered Regions of Two Paralogous Transcription Factors Reveal Rigid Segments with Important Biological Functions,published,journal,J. Mol. Biol.,Journal of molecular biology,431,7,,1089-8638,,,,,,,,,,,,,,,,,,,,1353,1369,2019, citations,entry_citation,27623,157860,1,,entry citation,,,31293000,,,Structural basis for -35 element recognition by sigma4 chimera proteins and their interactions with PmrA response regulator,published,journal,Proteins,,88,1,,,,,,,,,,,,,,,,,,,,,,69,81,2020, citations,entry_citation,27624,157874,1,,entry citation,,,31293000,,,Structural basis for -35 element recognition by sigma4 chimera proteins and their interactions with PmrA response regulator,published,journal,Proteins,,88,1,,,,,,,,,,,,,,,,,,,,,,69,81,2020, citations,entry_citation,27625,157888,1,,entry citation,,,30474821,,,"1H, 15N, 13C resonance assignment of the human CD44 cytoplasmic tail (669-742)",published,journal,Biomol. NMR Assignments,,13,1,,,,,,,,,,,,,,,,,,,,,,109,113,2019, citations,entry_citation,27626,157902,1,,entry citation,,,30593502,,,Dynamic ion pair behavior stabilizes single alpha-helices in proteins,published,journal,J. 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J.,,116,3,,1542-0086,,,,,,,,,,,,,,,,,,,,406,418,2019, citations,entry_citation,27631,157993,1,,entry citation,,,31796585,,,Molecular determinants of chaperone interactions on MHC-I for folding and antigen repertoire selection,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,116,51,,1091-6490,,,,,,,,,,,,,,,,,,,,25602,25613,2019, citations,entry_citation,27632,158012,1,,entry citation,,,31796585,,,Molecular determinants of chaperone interactions on MHC-I for folding and antigen repertoire selection,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,116,51,,1091-6490,,,,,,,,,,,,,,,,,,,,25602,25613,2019, citations,entry_citation,27633,158032,1,,entry citation,,,30301810,,,Highly disordered histone H1-DNA model complexes and their condensates,published,journal,Proc. Natl. Acad. Sci. 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NMR Assignments,,13,1,,,,,,,,,,,,,,,,,,,,,,143,147,2019, citations,entry_citation,27641,158195,1,,entry citation,,,30784592,,,Interactions between N-terminal Modules in MPS1 Enable Spindle Checkpoint Silencing.,published,journal,Cell Rep.,Cell reports,26,8,,2211-1247,,,,,,,,,,,,,,,,,,,,2101,2112,2019, citations,entry_citation,27642,158209,1,,entry citation,,,30784592,,,Interactions between N-terminal Modules in MPS1 Enable Spindle Checkpoint Silencing.,published,journal,Cell Rep.,Cell reports,26,8,,2211-1247,,,,,,,,,,,,,,,,,,,,2101,2112,2019, citations,entry_citation,27643,158222,1,,entry citation,,,30963726,,,Structural insight into the unique dsDNA binding topology of the human ORC2 wing helix domain,published,journal,FEBS J.,The FEBS journal,286,14,,1742-4658,,,,,,,,,,,,,,,,,,,,2726,2736,2019, citations,entry_citation,27645,158236,1,,entry citation,,,31092861,10.1038/s41598-019-43932-x,,Structural and functional characterization of the PDZ domain of the human phosphatase PTPN3 and its interaction with the human papillomavirus E6 oncoprotein,published,journal,Sci. Rep.,Scientific reports,9,1,,2045-2322,,,,,,,,,,,,,,,,,,,,7438,7438,2019, citations,entry_citation,27646,158256,1,,entry citation,,,31468366,,,"1H, 15N backbone assignment and comparative analysis of the wild type and G12C, G12D, G12V mutants of K-Ras bound to GDP at physiological pH",published,journal,Biomol. 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Chem.,The Journal of biological chemistry,293,51,,1083-351X,,,,,,,,,,,,,,,,,,,,19522,19531,2018, citations,entry_citation,27651,158331,1,,entry citation,,,30773397,,,Conformational Changes in the Cytoplasmic Region of KIR3DL1 upon Interaction with SHP-2,published,journal,Structure,,27,4,,,,,,,,,,,,,,,,,,,,,,639,650,2019, citations,citations_1,27652,158346,1,,entry citation,,,,,,1H Assigned Chemical Shifts for NZ118,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,27653,158360,1,,entry citation,,,31026448,10.1016/j.jmb.2019.04.018,,"The Tumor Suppressor ING5 Is a Dimeric, Bivalent Recognition Molecule of the Histone H3K4me3 Mark.",published,journal,J. Mol. Biol.,Journal of molecular biology,431,12,,1089-8638,,,,,,,,,,,,,,,,,,,,2298,2319,2019, citations,entry_citation,27654,158376,1,,entry citation,,,31026448,10.1016/j.jmb.2019.04.018,,"The Tumor Suppressor ING5 Is a Dimeric, Bivalent Recognition Molecule of the Histone H3K4me3 Mark.",published,journal,J. Mol. Biol.,Journal of molecular biology,431,12,,1089-8638,,,,,,,,,,,,,,,,,,,,2298,2319,2019, citations,entry_citation,27655,158394,1,,entry citation,,,30328810,,,Tuning site-specific dynamics to drive allosteric activation in a pneumococcal zinc uptake regulator,published,journal,eLife,,7,,,,,,,,,,,,,,,,,,,,,,,e37268,e37268,2018, citations,entry_citation,27656,158419,1,,entry citation,,,30328810,,,Tuning site-specific dynamics to drive allosteric activation in a pneumococcal zinc uptake regulator,published,journal,eLife,,7,,,,,,,,,,,,,,,,,,,,,,,e37268,e37268,2018, citations,entry_citation,27659,158442,1,,entry citation,,,31909602,,,Insights into Structural and Dynamical Changes Experienced by Human RNase 6 upon Ligand Binding,published,journal,Biochemistry,Biochemistry,59,6,,1520-4995,,,,,,,,,,,,,,,,,,,,755,765,2020, citations,entry_citation,27661,158458,1,,entry citation,,,30655288,10.1074/jbc.RA118.006391,,The p12 subunit of human polymerase delta uses an atypical PIP box for molecular recognition of proliferating cell nuclear antigen (PCNA),published,journal,J. Biol. Chem.,The Journal of biological chemistry,294,11,,1083-351X,,,,,,,,,,,,,,,,,,,,3947,3956,2019, citations,entry_citation,27662,158474,1,,entry citation,,,30655288,10.1074/jbc.RA118.006391,,The p12 subunit of human polymerase delta uses an atypical PIP box for molecular recognition of proliferating cell nuclear antigen (PCNA),published,journal,J. Biol. Chem.,The Journal of biological chemistry,294,11,,1083-351X,,,,,,,,,,,,,,,,,,,,3947,3956,2019, citations,entry_citation,27664,158489,1,,entry citation,,,,,,Synergistic Recruitment of UbcH7~Ub and Phosphorylated Ubl Domain Triggers Parkin Activation,submitted,journal,EMBO J.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,Citation_1,27666,158508,1,,entry citation,,,30632004,,,Resonance assignment of human LARP4A La module,published,journal,Biomol. NMR Assignments,,13,1,,,,,,,,,,,,,,,,,,,,,,169,172,2019, citations,entry_citation,27667,158528,1,,entry citation,,,,,,Backbone resonance assignment of the catalytic and ATP-binding domain of HK853 from Thermotoga maritime,in preparation,journal,Biomol. NMR Assignments,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,27668,158542,1,,entry citation,,,31459761,,,Alginate Trisaccharide Binding Sites on the Surface of beta-Lactoglobulin Identified by NMR Spectroscopy: Implications for Molecular Network Formation,published,journal,ACS Omega,ACS omega,4,4,,2470-1343,,,,,,,,,,,,,,,,,,,,6165,6174,2019, citations,entry_citation,27669,158560,1,,entry citation,,,30418581,,,HuR biological function involves RRM3-mediated dimerization and RNA binding by all three RRMs.,published,journal,Nucleic Acids Res.,Nucleic acids research,47,2,,1362-4962,,,,,,,,,,,,,,,,,,,,1011,1029,2019, citations,entry_citation,27670,158576,1,,entry citation,,,30418581,,,HuR biological function involves RRM3-mediated dimerization and RNA binding by all three RRMs.,published,journal,Nucleic Acids Res.,Nucleic acids research,47,2,,1362-4962,,,,,,,,,,,,,,,,,,,,1011,1029,2019, citations,entry_citation,27671,158592,1,,entry citation,,,30418581,,,HuR biological function involves RRM3-mediated dimerization and RNA binding by all three RRMs.,published,journal,Nucleic Acids Res.,Nucleic acids research,47,2,,1362-4962,,,,,,,,,,,,,,,,,,,,1011,1029,2019, citations,entry_citation,27672,158610,1,,entry citation,,,30539422,,,NMR Backbone and Methyl Resonance Assignments of an inhibitory G-alpha subunit in complex with GDP,published,journal,Biomol. NMR Assignments,,13,1,,,,,,,,,,,,,,,,,,,,,,131,137,2019, citations,journal_article,27673,158628,1,,entry citation,,,,,,Substrate modulates CYP-Adx interactions in mitochondria,in preparation,journal,JMB,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,27674,158646,1,,entry citation,,,31394100,,,"Structure, amphipathy, and topology of the membrane-proximal helix 8 influence apelin receptor plasma membrane localization",published,journal,Biochim. Biophys. Acta Biomembr.,Biochimica et biophysica acta. Biomembranes,1861,11,,1879-2642,,,,,,,,,,,,,,,,,,,,183036,183036,2019, citations,entry_citation,27676,158670,1,,entry citation,,,30631074,,,Shifts in the selectivity filter dynamics cause modal gating in K+ channels,published,journal,Nat. Commun.,,10,1,,2041-1723,,,,,,,,,,,,,,,,,,,,123,123,2019, citations,entry_citation,27677,158687,1,,entry citation,,,30666492,,,Resonance assignments for the tandem PWWP-ARID domains of human RBBP1,published,journal,Biomol. NMR Assignments,,13,1,,,,,,,,,,,,,,,,,,,,,,177,181,2019, citations,entry_citation,27678,158703,1,,entry citation,,,30631074,,,Shifts in the selectivity filter dynamics cause modal gating in K+ channels,published,journal,Nat. Commun.,,10,1,,2041-1723,,,,,,,,,,,,,,,,,,,,123,123,2019, citations,entry_citation,27679,158720,1,,entry citation,,,30631074,,,Shifts in the selectivity filter dynamics cause modal gating in K+ channels,published,journal,Nat. Commun.,,10,1,,2041-1723,,,,,,,,,,,,,,,,,,,,123,123,2019, citations,entry_citation,2768,158737,1,,entry citation,,,,,"Landry, Samuel J., Jordan, Robert, McMacken, Roger, Gierasch, Lila M., ""Different conformations for the same polypeptide bound to chaperones DnaK and GroEL,"" Nature 355, 455-457 (1992).","Different conformations for the same polypeptide bound to chaperones DnaK and GroEL",published,journal,Nature,,355,,,,,,,,,,,,,,,,,,,,,,,455,457,1992, citations,entry_citation,27680,158750,1,,entry citation,,,30631074,,,Shifts in the selectivity filter dynamics cause modal gating in K+ channels,published,journal,Nat. Commun.,,10,1,,2041-1723,,,,,,,,,,,,,,,,,,,,123,123,2019, citations,citation_1,27681,158767,1,,entry citation,,,31573509,,,Interplay of disordered and ordered regions of a human small heat shock protein yields an ensemble of 'quasi-ordered' states,published,journal,Elife,eLife,8,,,2050-084X,,,,,,,,,,,,,,,,,,,,e50259,e50259,2019, citations,entry_citation,27682,158787,1,,entry citation,,,31796585,,,Molecular determinants of chaperone interactions on MHC-I for folding and antigen repertoire selection,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,116,51,,1091-6490,,,,,,,,,,,,,,,,,,,,25602,25613,2019, citations,entry_citation,27683,158808,1,,entry citation,,,31558722,,,Methionine in a protein hydrophobic core drives tight interactions required for assembly of spider silk,published,journal,Nat. Commun.,Nature communications,10,1,,2041-1723,,,,,,,,,,,,,,,,,,,,4378,4378,2019, citations,entry_citation,27684,158825,1,,entry citation,,,30528777,,,An inter-switch between hydrophobic and charged amino acids generated druggable small molecule binding pocket in chemokine paralog CXCL3,published,journal,Arch. Biochem. Biophys.,Archives of biochemistry and biophysics,662,,,1096-0384,,,,,,,,,,,,,,,,,,,,121,128,2018, citations,entry_citation,27687,158839,1,,entry citation,,,30542820,,,NMR resonance assignments of the pathogenesis-related peach allergen Pru p 1.0101,published,journal,Biomol. NMR Assignments,,13,1,,,,,,,,,,,,,,,,,,,,,,127,130,2018, citations,entry_citation,27688,158854,1,,entry citation,,,30758717,,,"(1)H, (13)C, and (15)N resonance assignments of the cytokine interleukin-36beta isoform-2",published,journal,Biomol. NMR Assignments,,13,,,,,,,,,,,,,,,,,,,,,,,155,161,2019, citations,citation_1,30057,166260,1,,entry citation,,,,,,NMR structures and molecular dynamics simulation of hylin-a1 analogs bound to dodecylphosphocholine micelles.,in preparation,journal,,,,,,,0353,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,27690,158872,1,,entry citation,,,30879170,,,"Backbone and side chain 1H, 15N and 13C assignments of a putative peptidyl prolyl cis-trans isomerase FKBP12 from Mycobacterium tuberculosis",published,journal,Biomol. NMR Assignments,,13,1,,,,,,,,,,,,,,,,,,,,,,239,243,2019, citations,citation_1,27691,158888,1,,entry citation,,,30734154,,,"Backbone 1H, 13C, and 15N resonance assignments of BoMan26A, a beta-mannanase of the glycoside hydrolase family 26 from the human gut bacterium Bacteroides ovatus",published,journal,Biomol. NMR Assign.,,13,1,,,,,,,,,,,,,,,,,,,,,,213,218,2019, citations,entry_citation,27692,158904,1,,entry citation,,,30788773,10.1007/s12104-019-09883-0,,Chemical shift assignments of a calmodulin intermediate with two Ca2+ bound in complex with the IQ-motif of voltage-gated Ca2+ channels (CaV1.2),published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,13,1,,1874-270X,,,,,,,,,,,,,,,,,,,,233,237,2019, citations,entry_citation,27693,158921,1,,entry citation,,,30573682,,,"Structural basis and mechanism of the unfolding-induced activation of HdeA, a bacterial acid response chaperone",published,journal,J. Biol. Chem.,,294,9,,,,,,,,,,,,,,,,,,,,,,3192,3206,2019, citations,citation_1,27694,158936,1,,entry citation,,,27936610,,,Dynamics of Aromatic Side Chains in the Active Site of FKBP12.,published,journal,Biochemistry,,56,1,,,,,,,,,,,,,,,,,,,,,,334,343,2017, citations,citation_1,27695,158950,1,,entry citation,,,27936610,,,Dynamics of Aromatic Side Chains in the Active Site of FKBP12,published,journal,Biochemistry,,56,1,,,,,,,,,,,,,,,,,,,,,,334,343,2017, citations,entry_citation,27696,158964,1,,entry citation,,,31479228,,,Double Monoubiquitination Modifies the Molecular Recognition Properties of p15PAF Promoting Binding to the Reader Module of Dnmt1,published,journal,ACS Chem. Biol.,ACS chemical biology,14,10,,1554-8937,,,,,,,,,,,,,,,,,,,,2315,2326,2019, citations,entry_citation,27698,158979,1,,entry citation,,,31479228,,,Double Monoubiquitination Modifies the Molecular Recognition Properties of p15PAF Promoting Binding to the Reader Module of Dnmt1,published,journal,ACS Chem. Biol.,ACS chemical biology,14,10,,1554-8937,,,,,,,,,,,,,,,,,,,,2315,2326,2019, citations,Citation_high_ionic,27699,158993,1,,entry citation,,,30868366,10.1007/s12104-019-09886-x,,NMR assignments of human linker histone H1x N-terminal domain and globular domain in the presence and absence of perchlorate,published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,13,1,,1874-270X,,,,,,,,,,,,,,,,,,,,249,254,2019, citations,NGH1x_low_ionic,27700,159018,1,,entry citation,,,30868366,10.1007/s12104-019-09886-x,,NMR assignments of human linker histone H1x N-terminal domain and globular domain in the presence and absence of perchlorate,published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,13,1,,1874-270X,,,,,,,,,,,,,,,,,,,,249,254,2019, citations,entry_citation,27701,159042,1,,entry citation,,,31402220,,,Mapping Hidden Residual Structure within the Myc bHLH-LZ Domain Using Chemical Denaturant Titration,published,journal,Structure,"Structure (London, England : 1993)",27,10,,1878-4186,,,,,,,,,,,,,,,,,,,,1537,1546,2019, citations,entry_citation,27702,159056,1,,entry citation,,,31402220,,,Mapping Hidden Residual Structure within the Myc bHLH-LZ Domain Using Chemical Denaturant Titration,published,journal,Structure,"Structure (London, England : 1993)",27,10,,1878-4186,,,,,,,,,,,,,,,,,,,,1537,1546,2019, citations,entry_citation,27703,159070,1,,entry citation,,,31402220,,,Mapping Hidden Residual Structure within the Myc bHLH-LZ Domain Using Chemical Denaturant Titration,published,journal,Structure,"Structure (London, England : 1993)",27,10,,1878-4186,,,,,,,,,,,,,,,,,,,,1537,1546,2019, citations,entry_citation,27704,159084,1,,entry citation,,,31402220,,,Mapping Hidden Residual Structure within the Myc bHLH-LZ Domain Using Chemical Denaturant Titration,published,journal,Structure,"Structure (London, England : 1993)",27,10,,1878-4186,,,,,,,,,,,,,,,,,,,,1537,1546,2019, citations,citation_1,27705,159098,1,,entry citation,,,30559291,,,"Retinal degeneration 3 (RD3) protein, a retinal guanylyl cyclase regulator, forms a monomeric and elongated four helix bundle",published,journal,J. Biol. Chem.,The Journal of biological chemistry,94,7,,1083-351X,,,,,,,,,,,,,,,,,,,,2318,2328,2019, citations,entry_citation,27706,159115,1,,entry citation,,,30700785,,,The EZH2 SANT1 domains is a histone reader domain providing sensitivity to the modification state of the H4 tail,published,journal,Sci. Rep.,Scientific reports,9,1,,2045-2322,,,,,,,,,,,,,,,,,,,,987,987,2019, citations,entry_citation,27707,159132,1,,entry citation,,,,,,All major cholesterol-dependent cytolysins use glycans as cellular receptors.,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,27708,159146,1,,entry citation,,,30690395,,,A myristoyl binding site in the SH3 domain modulates c-Src membrane anchoring,published,journal,iScience,,12,,,2589-0042,,,,,,,,,,,,,,,,,,,,194,203,2019, citations,citations_1,27709,159163,1,,entry citation,,,30554144,,,A serine in the first transmembrane domain of the human E3 ubiquitin ligase MARCH9 is critical for down-regulation of its protein substrates,published,journal,J. Biol. Chem.,The Journal of biological chemistry,294,7,,1083-351X,,,,,,,,,,,,,,,,,,,,2470,2485,2019, citations,entry_citation,27711,159178,1,,entry citation,,,30753871,,,The KN-93 Molecule Inhibits Calcium/Calmodulin-Dependent Protein Kinase II (CaMKII) Activity by Binding to Ca,published,journal,J. Mol. Biol.,Journal of molecular biology,431,7,,1089-8638,,,,,,,,,,,,,,,,,,,,1440,1459,2019, citations,entry_citation,27712,159197,1,,entry citation,,,30753871,,,The KN-93 Molecule Inhibits Calcium/Calmodulin-Dependent Protein Kinase II (CaMKII) Activity by Binding to Ca,published,journal,J. Mol. Biol.,Journal of molecular biology,431,7,,1089-8638,,,,,,,,,,,,,,,,,,,,1440,1459,2019, citations,entry_citation,27713,159216,1,,entry citation,,,31048691,10.1038/s41467-019-09923-2,,Side chain to main chain hydrogen bonds stabilize a polyglutamine helix in a transcription factor.,published,journal,Nat. Commun.,Nature communications,10,1,,2041-1723,,,,,,,,,,,,,,,,,,,,2034,2034,2019, citations,entry_citation,27714,159230,1,,entry citation,,,31048691,10.1038/s41467-019-09923-2,,Side chain to main chain hydrogen bonds stabilize a polyglutamine helix in a transcription factor.,published,journal,Nat. Commun.,Nature communications,10,1,,2041-1723,,,,,,,,,,,,,,,,,,,,2034,2034,2019, citations,entry_citation,27715,159246,1,,entry citation,,,31048691,10.1038/s41467-019-09923-2,,Side chain to main chain hydrogen bonds stabilize a polyglutamine helix in a transcription factor.,published,journal,Nat. Commun.,Nature communications,10,1,,2041-1723,,,,,,,,,,,,,,,,,,,,2034,2034,2019, citations,entry_citation,27716,159262,1,,entry citation,,,31048691,10.1038/s41467-019-09923-2,,Side chain to main chain hydrogen bonds stabilize a polyglutamine helix in a transcription factor.,published,journal,Nat. Commun.,Nature communications,10,1,,2041-1723,,,,,,,,,,,,,,,,,,,,2034,2034,2019, citations,entry_citation,27717,159278,1,,entry citation,,,31048691,10.1038/s41467-019-09923-2,,Side chain to main chain hydrogen bonds stabilize a polyglutamine helix in a transcription factor.,published,journal,Nat. Commun.,Nature communications,10,1,,2041-1723,,,,,,,,,,,,,,,,,,,,2034,2034,2019, citations,entry_citation,27718,159294,1,,entry citation,,,31468366,,,"1H, 15N backbone assignment and comparative analysis of the wild type and G12C, G12D, G12V mutants of K-Ras bound to GDP at physiological pH",published,journal,Biomol. NMR Assignments,,14,1,,,,,,,,,,,,,,,,,,,,,,1,7,2020, citations,entry_citation,27719,159313,1,,entry citation,,,31468366,,,"1H, 15N backbone assignment and comparative analysis of the wild type and G12C, G12D, G12V mutants of K-Ras bound to GDP at physiological pH",published,journal,Biomol. 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Soc.,Journal of the American Chemical Society,141,5,,1520-5126,,,,,,,,,,,,,,,,,,,,2012,2026,2019, citations,entry_citation,27724,159439,1,,entry citation,,,32094450,,,Aedes aegypti Odorant Binding Protein 22 selectively binds fatty acids through a conformational change in its C-terminal tail,published,journal,Sci. Rep.,Scientific reports,10,1,,2045-2322,,,,,,,,,,,,,,,,,,,,3300,3300,2020, citations,entry_citation,27725,159459,1,,entry citation,,,30684235,,,"1H, 13C and 15N resonance assignments of the second peptidyl-prolyl isomerase domain of chaperone SurA from Escherichia coli",published,journal,Biomol. NMR Assignments,,13,1,,,,,,,,,,,,,,,,,,,,,,183,186,2019, citations,entry_citation,27726,159476,1,,entry citation,,,30735034,,,Functional Expression and Characterization of Human Myristoylated-Arf1 in Nanodisc Membrane Mimetics.,published,journal,Biochemistry,Biochemistry,58,10,,1520-4995,,,,,,,,,,,,,,,,,,,,1423,1431,2019, citations,entry_citation,27728,159494,1,,entry citation,,,30772281,10.1016/j.bbamem.2019.02.005,,Structure determination of UL49.5 transmembrane protein from bovine herpesvirus 1 by NMR spectroscopy and molecular dynamics.,published,journal,Biochim. Biophys. Acta Biomembr.,Biochimica et biophysica acta. Biomembranes,1861,5,,1879-2642,,,,,,,,,,,,,,,,,,,,926,938,2019, citations,entry_citation,27729,159513,1,,entry citation,,,30819901,,,Interleukin-37 monomer is the active form for reducing innate immunity.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,116,12,,1091-6490,,,,,,,,,,,,,,,,,,,,5514,5522,2019, citations,entry_citation,27730,159529,1,,entry citation,,,30772281,10.1016/j.bbamem.2019.02.005,,Structure determination of UL49.5 transmembrane protein from bovine herpesvirus 1 by NMR spectroscopy and molecular dynamics.,published,journal,Biochim. Biophys. Acta Biomembr.,Biochimica et biophysica acta. Biomembranes,1861,5,,1879-2642,,,,,,,,,,,,,,,,,,,,926,938,2019, citations,entry_citation,27732,159548,1,,entry citation,,,30707421,,,"15N, 13C and 1H resonance assignments of FKBP12 proteins from the pathogenic fungi Mucor circinelloides and Aspergillus fumigatus",published,journal,Biomol. NMR Assignments,,13,1,,,,,,,,,,,,,,,,,,,,,,207,212,2019, citations,entry_citation,27733,159569,1,,entry citation,,,30707421,,,"15N, 13C and 1H resonance assignments of FKBP12 proteins from the pathogenic fungi Mucor circinelloides and Aspergillus fumigatus",published,journal,Biomol. NMR Assignments,,13,1,,,,,,,,,,,,,,,,,,,,,,207,212,2019, citations,entry_citation,27734,159592,1,,entry citation,,,30707421,,,"15N, 13C and 1H resonance assignments of FKBP12 proteins from the pathogenic fungi Mucor circinelloides and Aspergillus fumigatus",published,journal,Biomol. NMR Assignments,,13,1,,,,,,,,,,,,,,,,,,,,,,207,212,2019, citations,entry_citation,27737,159613,1,,entry citation,,,30707421,,,"15N, 13C and 1H resonance assignments of FKBP12 proteins from the pathogenic fungi Mucor circinelloides and Aspergillus fumigatus",published,journal,Biomol. NMR Assignments,,13,1,,,,,,,,,,,,,,,,,,,,,,207,212,2019, citations,entry_citation,27738,159636,1,,entry citation,,,30707421,,,"15N, 13C and 1H resonance assignments of FKBP12 proteins from the pathogenic fungi Mucor circinelloides and Aspergillus fumigatus",published,journal,Biomol. NMR Assignments,,13,1,,,,,,,,,,,,,,,,,,,,,,207,212,2019, citations,entry_citation,27739,159657,1,,entry citation,,,30707421,,,"15N, 13C and 1H resonance assignments of FKBP12 proteins from the pathogenic fungi Mucor circinelloides and Aspergillus fumigatus",published,journal,Biomol. NMR Assignments,,13,1,,,,,,,,,,,,,,,,,,,,,,207,212,2019, citations,entry_citation,27741,159680,1,,entry citation,,,30655293,10.1074/jbc.RA118.004723,,The,published,journal,J. Biol. Chem.,The Journal of biological chemistry,294,11,,1083-351X,,,,,,,,,,,,,,,,,,,,4027,4044,2019, citations,entry_citation,27742,159703,1,,entry citation,,,31582430,,,Structural basis for distinct roles of SMAD2 and SMAD3 in FOXH1 pioneer-directed TGF-beta signaling,published,journal,Genes Dev.,Genes & Development,33,21-22,,1549-5477,,,,,,,,,,,,,,,,,,,,1506,1524,2019, citations,entry_citation,27743,159719,1,,entry citation,,,31582430,,,Structural basis for distinct roles of SMAD2 and SMAD3 in FOXH1 pioneer-directed TGF-beta signaling,published,journal,Genes Dev.,Genes & Development,33,21-22,,1549-5477,,,,,,,,,,,,,,,,,,,,1506,1524,2019, citations,entry_citation,27744,159735,1,,entry citation,,,31902070,,,Backbone chemical shift assignments of translation initiation factor 3 from Pseudomonas aeruginosa,published,journal,Biomol. NMR Assignments,,14,1,,,,,,,,,,,,,,,,,,,,,,93,97,2020, citations,entry_citation,27746,159750,1,,entry citation,,,,10.1126/sciadv.aaw6756,,The conduction pathway of potassium channels is water free under physiological conditions,published,journal,Sci. Adv.,,5,7,,,,,,,,,,,,,,,,,,,,,,,,2019, citations,entry_citation,27747,159768,1,,entry citation,,,30847846,,,Assignment of the ARC4 domain of human Tankyrase,published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,13,1,,1874-270X,,,,,,,,,,,,,,,,,,,,255,260,2019, citations,entry_citation,27750,159785,1,,entry citation,,,32132204,,,TDP-43 alpha-helical structure tunes liquid-liquid phase separation and function,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,117,11,,1091-6490,,,,,,,,,,,,,,,,,,,,5883,5894,2020, citations,entry_citation,27751,159801,1,,entry citation,,,32132204,,,TDP-43 alpha-helical structure tunes liquid-liquid phase separation and function,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,117,11,,1091-6490,,,,,,,,,,,,,,,,,,,,5883,5894,2020, citations,citation_1,27752,159817,1,,entry citation,,,,,,"Comparison of four cyclosporin variants A, B, C and D based on NMR spectroscopy",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,27753,159839,1,,entry citation,,,31181288,,,The Cytoplasm-Entry Domain of Antibacterial CdiA Is a Dynamic alpha-Helical Bundle with Disulfide-Dependent Structural Features,published,journal,J. Mol. Biol.,,431,17,,,,,,,,,,,,,,,,,,,,,,,3203,3216,2019 citations,entry_citation,27754,159854,1,,entry citation,,,31181288,,,The Cytoplasm-Entry Domain of Antibacterial CdiA Is a Dynamic alpha-Helical Bundle with Disulfide-Dependent Structural Features,published,journal,J. Mol. Biol.,,431,17,,,,,,,,,,,,,,,,,,,,,,,3203,3216,2019 citations,entry_citation,27755,159869,1,,entry citation,,,31181288,,,The Cytoplasm-Entry Domain of Antibacterial CdiA Is a Dynamic alpha-Helical Bundle with Disulfide-Dependent Structural Features,published,journal,J. Mol. Biol.,,431,17,,,,,,,,,,,,,,,,,,,,,,,3203,3216,2019 citations,In_Preparation,27756,159884,1,,entry citation,,,31538782,,,Sequential and Environmental Dependence of Conformation in a Small Opioid Peptide,published,journal,J. Org. Chem.,,84,21,,,,,,,,,,,,,,,,,,,,,,13299,13312,2019, citations,entry_citation,27757,159905,1,,entry citation,,,31227800,10.1038/s41598-019-45565-6,,Studies of the oligomerisation mechanism of a cystatin-based engineered protein scaffold.,published,journal,Sci. Rep.,Scientific reports,9,1,,2045-2322,,,,,,,,,,,,,,,,,,,,9067,9067,2019, citations,entry_citation,27759,159920,1,,entry citation,,,30707944,,,The isolated C-terminal nuclear localization sequence of the breast cancer metastasis suppressor 1 is disordered,published,journal,Arch. Biochem. Biophys.,Archives of Biochemistry and Biophysics,664,,,0003-9861,,,,,,,,,,,,,,,,,,,,95,101,2019, citations,entry_citation,27761,159939,1,,entry citation,,,31780432,,,"Molecular Architecture of a Network of Potential Intracellular EGFR Modulators: ARNO, CaM, Phospholipids, and the Juxtamembrane Segment",published,journal,Structure,"Structure (London, England : 1993)",28,1,,1878-4186,,,,,,,,,,,,,,,,,,,,54,62.e5,2020, citations,entry_citation,27762,159953,1,,entry citation,,,31025174,,,Resonance assignment of the 128 kDa enzyme I dimer from Thermoanaerobacter tengcongensis,published,journal,Biomol. NMR Assignments,,13,2,,,,,,,,,,,,,,,,,,,,,,287,293,2019, citations,entry_citation,27763,159969,1,,entry citation,,,31134895,,,An order-to-disorder structural switch activates the FoxM1 transcription factor.,published,journal,Elife,eLife,8,,,2050-084X,,,,,,,,,,,,,,,,,,,,e46131,e46131,2019, citations,entry_citation,27764,159985,1,,entry citation,,,31134895,,,An order-to-disorder structural switch activates the FoxM1 transcription factor.,published,journal,Elife,eLife,8,,,2050-084X,,,,,,,,,,,,,,,,,,,,e46131,e46131,2019, citations,entry_citation,27767,160004,1,,entry citation,,,30830594,,,"1H, 13C and 15N NMR assignments of Bacillus subtilis bacteriophage SPO1 protein Gp46",published,journal,Biomol. 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NMR Assign.,Biomolecular NMR assignments,13,2,,1874-270X,,,,,,,,,,,,,,,,,,,,383,390,2019, citations,Letter,27853,161355,1,,entry citation,,,31432400,,,NMR resonance assignments for the GSPII-B domain of the traffic ATPase PilF from Thermus thermophilus in the apo and the c-di-GMP-bound state,published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,13,2,,1874-270X,,,,,,,,,,,,,,,,,,,,383,390,2019, citations,entry_citation,27854,161374,1,,entry citation,,,31283166,,,Molecular Insights into DC-SIGN Binding to Self-Antigens: The Interaction with the Blood Group A/B Antigens,published,journal,ACS Chem Biol.,,14,7,,,,,,,,,,,,,,,,,,,,,,1660,1671,2019, citations,entry_citation,27856,161393,1,,entry citation,,,31228091,10.1007/s12104-019-09901-1,,Resonance assignments of N-terminal receiver domain of sigma factor S regulator RssB from Escherichia coli.,published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,13,2,,1874-270X,,,,,,,,,,,,,,,,,,,,333,337,2019, citations,entry_citation,27857,161410,1,,entry citation,,,32671633,,,Backbone and sidechain NMR assignments for the ribosome maturation factor RbfA from Escherichia coli,published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,14,2,,1874-270X,,,,,,,,,,,,,,,,,,,,317,321,2020, citations,entry_citation,27859,161427,1,,entry citation,,,31183057,10.1039/c8sc05683h,,Localization of ligands within human carbonic anhydrase II using,published,journal,Chem. Sci.,Chemical science,10,19,,2041-6520,,,,,,,,,,,,,,,,,,,,5064,5072,2019, citations,entry_citation,2786,161442,1,,entry citation,,,,,"Dobson, Christopher M., Ferguson, Stuart J., Poulsen, Flemming M., Williams, Robert J. P., ""Complete Assignment of Aromatic 1H Nuclear Magnetic Resonances of the Tyrosine Residues of Hen Lysozyme,"" Eur. J. 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Chem.,The Journal of biological chemistry,295,1,,1083-351X,,,,,,,,,,,,,,,,,,,,170,180,2020, citations,entry_citation,27866,161546,1,,entry citation,,,31406020,,,A ubiquitin-like dimerization domain controls protein kinase D activation by trans-autophosphorylation,published,journal,J. Biol. Chem.,The Journal of biological chemistry,294,39,,1083-351X,,,,,,,,,,,,,,,,,,,,14422,14441,2019, citations,citation_1,27867,161565,1,,entry citation,,,31388821,,,Backbone and side chain resonance assignments of the C-terminal domain of human TGIF1,published,journal,Biomol. NMR Assignments,,13,2,,1874-270X,,,,,,,,,,,,,,,,,,,,357,360,2019, citations,entry_citation,27868,161579,1,,entry citation,,,31493651,,,Structural characterization and biological function of bivalent binding of CD2AP to intrinsically disordered domain of chikungunya virus nsP3 protein,published,journal,Virology,Virology,537,,,1096-0341,,,,,,,,,,,,,,,,,,,,130,142,2019, citations,entry_citation,27869,161595,1,,entry citation,,,31119489,,,"Backbone assignment of cytochrome PccH, a crucial protein for microbial electrosynthesis in Geobacter sulfurreducens",published,journal,Biomol. NMR Assignments,,13,2,,,,,,,,,,,,,,,,,,,,,,321,326,2019, citations,entry_citation,2787,161613,1,,entry citation,,,,,"Hosur, Ramakrishna V., Wider, Gerhard, Wuthrich, Kurt, ""Sequential Individual Resonance Assignments in the 1H Nuclear-Magnetic-Resonance Spectrum of Cardiotoxin VII 2 from Naja mossambica mossambica,"" Eur. J. 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NMR Assignments,,13,2,,,,,,,,,,,,,,,,,,,,,,361,366,2019, citations,entry_citation,27878,161755,1,,entry citation,,,31724398,,,Amyloid formation under complicated conditions in which beta2-microglobulin coexists with its proteolytic fragments,published,journal,Biochemistry,,58,49,,,,,,,,,,,,,,,,,,,,,,4925,4934,2019, citations,entry_citation,27879,161775,1,,entry citation,,,31310428,,,Nucleotide binding modes in a motor protein revealed by 31P and 1H-detected MAS solid-state NMR,published,journal,Chembiochem,Chembiochem : a European journal of chemical biology,21,3,,1439-7633,,,,,,,,,,,,,,,,,,,,324,330,2020, citations,entry_citation,27880,161796,1,,entry citation,,,31346897,,,NMR chemical shift backbone assignment of the viral protein P1 encoded by the African Rice Yellow Mottle Virus,published,journal,Biomol. NMR Assignments,,13,2,,,,,,,,,,,,,,,,,,,,,,345,348,2019, citations,entry_citation,27881,161814,1,,entry citation,,,32241912,,,Iron is a ligand of SecA-like metal-binding domains in vivo,published,journal,J. Biol. Chem.,The Journal of biological chemistry,295,21,,1083-351X,,,,,,,,,,,,,,,,,,,,7516,7528,2020, citations,entry_citation,27882,161829,1,,entry citation,,,,,,Hybrid Histidine kinase activation by cyclic-di-GMP induced domain liberation,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,27883,161845,1,,entry citation,,,31340016,,,Phosphorylation orchestrates the structural ensemble of the intrinsically disordered protein HMGA1a and modulates its DNA binding to the NFkB promoter,published,journal,Nucleic Acids Res.,,47,22,,,,,,,,,,,,,,,,,,,,,,11906,11920,2019, citations,entry_citation,27884,161861,1,,entry citation,,,31340016,,,Phosphorylation orchestrates the structural ensemble of the intrinsically disordered protein HMGA1a and modulates its DNA binding to the NFkB promoter,published,journal,Nucleic Acids Res.,,47,22,,,,,,,,,,,,,,,,,,,,,,11906,11920,2019, citations,entry_citation,27886,161878,1,,entry citation,,,31301804,,,NMR Structural Analysis of Isolated Shaker Voltage-Sensing Domain in LPPG Micelles,published,journal,Biophys. J.,Biophysical journal,117,2,,1542-0086,,,,,,,,,,,,,,,,,,,,388,398,2019, citations,entry_citation,27887,161893,1,,entry citation,,,31270472,,,Molecular interactions underlying liquid-liquid phase separation of the FUS low complexity domain,published,journal,Nat. Struct. Mol. Biol.,Nature structural & molecular biology,26,7,,1545-9985,,,,,,,,,,,,,,,,,,,,637,648,2019, citations,CcpNmr,27888,161910,1,,reference citation,,,15815974,10.1002/prot.20449,,The CCPN data model for NMR spectroscopy: Development of a software pipeline,published,journal,Proteins,,59,4,,,,,,,,,,,,,,,,,,,,,,687,696,2005, citations,citations_1,27888,161911,2,,entry citation,,,31871087,,,Beta-Lactamase of Mycobacterium tuberculosis Shows Dynamics in the Active Site That Increase upon Inhibitor Binding,published,journal,Antimicrob. Agents. 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J.,,276,,,,,,,,,,,,,,,,,,,,,,,269,272,1991, citations,entry_citation,27893,161962,1,,entry citation,,,31612430,,,NMR chemical shift assignment of a constitutively active fragment of the antitermination protein LicT,published,journal,Biomol. NMR Assignments,,14,1,,,,,,,,,,,,,,,,,,,,,,19,23,2020, citations,citation_1,27894,161980,1,,entry citation,,,31913281,,,Mechanistic insights into transcription factor cooperativity and its impact on protein-phenotype interactions,published,journal,Nat. Commun.,Nature communications,11,1,,2041-1723,,,,,,,,,,,,,,,,,,,,124,124,2020, citations,entry_citation,27895,161994,1,,entry citation,,,31446566,,,Backbone resonance assignments of the dimeric domain of the p50 NF-kappaB subunit,published,journal,Biomol. NMR Assignments,,14,1,,,,,,,,,,,,,,,,,,,,,,9,11,2019, citations,citations_1,27900,162012,1,,entry citation,,,32157247,,,A short motif in the N-terminal region of alpha-synuclein is critical for both aggregation and function,published,journal,Nat. Struct. Mol. Biol.,Nature structural & molecular biology,27,3,,1545-9985,,,,,,,,,,,,,,,,,,,,249,259,2020, citations,citations_1,27901,162028,1,,entry citation,,,32157247,,,A short motif in the N-terminal region of alpha-synuclein is critical for both aggregation and function,published,journal,Nat. Struct. Mol. Biol.,Nature structural & molecular biology,27,3,,1545-9985,,,,,,,,,,,,,,,,,,,,249,259,2020, citations,citations_1,27903,162044,1,,entry citation,,,31165882,,,Disordered region of H3K9 methyltransferase Clr4 binds the nucleosome and contributes to its activity,published,journal,Nucleic Acids Res.,Nucleic acids research,47,13,,1362-4962,,,,,,,,,,,,,,,,,,,,6726,6736,2019, citations,entry_citation,27904,162058,1,,entry citation,,,29239081,,,Development and Validation of 2D Difference Intensity Analysis for Chemical Library Screening by Protein- Detected NMR Spectroscopy,published,journal,ChemBioChem,,19,5,,,,,,,,,,,,,,,,,,,,,,448,458,2018, citations,citations_1,27905,162074,1,,entry citation,,,31165882,,,Disordered region of H3K9 methyltransferase Clr4 binds the nucleosome and contributes to its activity,published,journal,Nucleic Acids Res.,Nucleic acids research,47,13,,1362-4962,,,,,,,,,,,,,,,,,,,,6726,6736,2019, citations,entry_citation,27911,162088,1,,entry citation,,,32468417,,,"1H, 13C and 15N NMR chemical shift assignments of cAMP-regulated phosphoprotein-19 and -16 (ARPP19 and ARPP16)",published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,14,2,,1874-270X,,,,,,,,,,,,,,,,,,,,227,231,2020, citations,entry_citation,27912,162103,1,,entry citation,,,32468417,,,"1H, 13C and 15N NMR chemical shift assignments of cAMP-regulated phosphoprotein-19 and -16 (ARPP19 and ARPP16)",published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,14,2,,1874-270X,,,,,,,,,,,,,,,,,,,,227,231,2020, citations,entry_citation,27913,162118,1,,entry citation,,,32195664,,,A dynamic charge:charge interaction modulates PP2A:B56 interactions,in preparation,journal,Elife,eLife,9,,,2050-084X,,,,,,,,,,,,,,,,,,,,,,2020, citations,entry_citation,27914,162134,1,,entry citation,,,31792442,,,Targeting the interaction of AIMP2-DX2 with HSP70 suppresses cancer development,published,journal,Nat. Chem. Biol.,Nature chemical biology,16,1,,1552-4469,,,,,,,,,,,,,,,,,,,,31,41,2020, citations,entry_citation,27915,162151,1,,entry citation,,,31587407,,,Comparison of backbone dynamics of the p50 dimerization domain of NFkB in the homodimeric transcription factor NFkB1 and in its heterodimeric complex with RelA (p65),published,journal,Protein Sci.,,28,12,,,,,,,,,,,,,,,,,,,,,,2064,2072,2019, citations,entry_citation,27916,162175,1,,entry citation,,,31587407,,,Comparison of backbone dynamics of the p50 dimerization domain of NFkB in the homodimeric transcription factor NFkB1 and in its heterodimeric complex with RelA (p65),published,journal,Protein Sci.,,28,12,,,,,,,,,,,,,,,,,,,,,,2064,2072,2019, citations,entry_citation,27917,162197,1,,entry citation,,,31625047,,,"1H, 13C, and 15N backbone and side chain chemical shift assignment of YdaS, a monomeric member of the HigA family",published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,14,1,,1874-270X,,,,,,,,,,,,,,,,,,,,25,30,2020, citations,entry_citation,27920,162213,1,,entry citation,,,31396843,,,"1H, 15N and 13C backbone resonance assignments of the P146A variant of beta-phosphoglucomutase from Lactococcus lactis in its substrate-free form",published,journal,Biomol. NMR Assignments,,13,2,,,,,,,,,,,,,,,,,,,,,,349,356,2019, citations,entry_citation,27922,162230,1,,entry citation,,,31399562,,,A switch element in the autophagy E2 Atg3 mediates allosteric regulation across the lipidation cascade,published,journal,Nat. Commun.,Nature communications,10,1,,2041-1723,,,,,,,,,,,,,,,,,,,,3600,3600,2019, citations,entry_citation,27923,162247,1,,entry citation,,,31399562,,,A switch element in the autophagy E2 Atg3 mediates allosteric regulation across the lipidation cascade,published,journal,Nat. Commun.,Nature communications,10,1,,2041-1723,,,,,,,,,,,,,,,,,,,,3600,3600,2019, citations,entry_citation,27924,162262,1,,entry citation,,,31399562,,,A switch element in the autophagy E2 Atg3 mediates allosteric regulation across the lipidation cascade,published,journal,Nat. Commun.,Nature communications,10,1,,2041-1723,,,,,,,,,,,,,,,,,,,,3600,3600,2019, citations,entry_citation,27925,162278,1,,entry citation,,,31848940,,,"1H, 13C, and 15N resonance assignments of the capsid protrusion domain of dragon grouper nervous necrosis virus",published,journal,Biomol. NMR Assignments,,14,1,,,,,,,,,,,,,,,,,,,,,,63,66,2020, citations,entry_citation,27926,162293,1,,entry citation,,,31874147,,,Revealing the mechanism of protein-lipid interactions for a putative membrane curvature sensor in plant endoplasmic reticulum,published,journal,Biochim. Biophys. Acta Biomembr.,Biochimica et biophysica acta. Biomembranes,1862,3,,1879-2642,,,,,,,,,,,,,,,,,,,,183160,183160,2020, citations,entry_citation,27927,162310,1,,entry citation,,,31874147,,,Revealing the mechanism of protein-lipid interactions for a putative membrane curvature sensor in plant endoplasmic reticulum,published,journal,Biochim. Biophys. Acta Biomembr.,Biochimica et biophysica acta. Biomembranes,1862,3,,1879-2642,,,,,,,,,,,,,,,,,,,,183160,183160,2020, citations,entry_citation,27928,162327,1,,entry citation,,,31874147,,,Revealing the mechanism of protein-lipid interactions for a putative membrane curvature sensor in plant endoplasmic reticulum,published,journal,Biochim. Biophys. Acta Biomembr.,Biochimica et biophysica acta. Biomembranes,1862,3,,1879-2642,,,,,,,,,,,,,,,,,,,,183160,183160,2020, citations,CcpNmr,27929,162344,1,,reference citation,,,15815974,10.1002/prot.20449,,The CCPN data model for NMR spectroscopy: Development of a software pipeline,published,journal,Proteins,,59,4,,,,,,,,,,,,,,,,,,,,,,687,696,2005, citations,entry,27929,162345,2,,entry citation,,,31871087,,,Beta-Lactamase of Mycobacterium tuberculosis Shows Dynamics in the Active Site That Increase upon Inhibitor Binding,published,journal,Antimicrob. Agents. Chemother.,,64,3,,,,,,,,,,,,,,,,,,,,,,e02025,e02025,2020, citations,Ambler1991,27929,162346,3,,reference citation,,,6109327,10.1042/bj2760269,,A standard numbering scheme for the Class A beta-lactamases,published,journal,Biochem. J.,,276,,,,,,,,,,,,,,,,,,,,,,,269,272,1991, citations,entry_citation,27930,162371,1,,entry citation,,,31597702,,,Intrinsic disorder and amino acid specificity modulate binding of the WW2 domain in kidney and brain protein (KIBRA) to synaptopodin,published,journal,J. Biol. Chem.,The Journal of biological chemistry,294,46,,1083-351X,,,,,,,,,,,,,,,,,,,,17383,17394,2019, citations,Citation_1,27931,162385,1,,entry citation,,,31188823,,,A unified mechanism for LLPS of ALS/FTLD-causing FUS as well as its modulation by ATP and oligonucleic acids,published,journal,PLoS Biol.,PLoS biology,17,6,,1545-7885,,,,,,,,,,,,,,,,,,,,e3000327,e3000327,2019, citations,entry_citation,27932,162399,1,,entry citation,,,31188823,,,A unified mechanism for LLPS of ALS/FTLD-causing FUS as well as its modulation by ATP and oligonucleic acids,published,journal,PLoS Biol.,PLoS biology,17,6,,1545-7885,,,,,,,,,,,,,,,,,,,,e3000327,e3000327,2019, citations,entry_citation,27934,162415,1,,entry citation,,,31570709,,,The structural basis for RNA selectivity by the IMP family of RNA binding proteins,published,journal,Nat. Comm.,,10,1,,2041-1723,,,,,,,,,,,,,,,,,,,,4440,4440,2019, citations,entry_citation,27935,162435,1,,entry citation,,,31782893,,,Characterization of an intermolecular quaternary interaction between discrete segments of the Streptococcus mutans adhesin P1 by NMR Spectroscopy,published,journal,FEBS J.,The FEBS journal,,,,1742-4658,,,,,,,,,,,,,,,,,,,,,,2019, citations,entry_citation,27943,162450,1,,entry citation,,,31377986,,,Backbone resonance assignment of human DJ-1 in the reduced state and in the cysteine sulfinic acid state,published,journal,Biomol. NMR Assignments,,13,2,,,,,,,,,,,,,,,,,,,,,,371,376,2019, citations,citations_1,27944,162466,1,,entry citation,,,31537834,,,Probing the dynamic stalk region of the ribosome using solution NMR,published,journal,Sci. Rep.,,9,1,,,,,,,,,,,,,,,,,,,,,,13528,13528,2019, citations,entry_citation,27945,162480,1,,entry citation,,,31566355,,,Retinoic Acid Binding Leads to CRABP2 Rigidification and Dimerization,published,journal,Biochemistry,Biochemistry,58,41,,1520-4995,,,,,,,,,,,,,,,,,,,,4183,4194,2019, citations,entry_citation,27946,162494,1,,entry citation,,,31566355,,,Retinoic Acid Binding Leads to CRABP2 Rigidification and Dimerization,published,journal,Biochemistry,Biochemistry,58,41,,1520-4995,,,,,,,,,,,,,,,,,,,,4183,4194,2019, citations,entry_citation,27947,162510,1,,entry citation,,,31377986,,,Backbone resonance assignment of human DJ-1 in the reduced state and in the cysteine sulfinic acid state,published,journal,Biomol. NMR Assignments,,13,2,,,,,,,,,,,,,,,,,,,,,,371,376,2019, citations,citations_1,27948,162527,1,,entry citation,,,31537834,,,Probing the dynamic stalk region of the ribosome using solution NMR,published,journal,Sci. Rep.,,9,1,,,,,,,,,,,,,,,,,,,,,,13528,13528,2019, citations,citation_1,27949,162541,1,,entry citation,,,31377985,,,"1H, 13C, 15N backbone and side chain resonance assignment of the HNH nuclease from Streptococcus pyogenes CRISPR-Cas9",published,journal,Biomol. NMR Assignments,,13,2,,,,,,,,,,,,,,,,,,,,,,367,370,2019, citations,citation_1,27950,162557,1,,entry citation,,,,,,Solution state backbone assignments of Vaccinia H1-Related (VHR) protein tyrosine phosphatase (PTP),in preparation,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,27951,162574,1,,entry citation,,,32877603,,,Ligand- and pH-Induced Structural Transition of Gypsy Moth Lymantria dispar Pheromone-Binding Protein 1 (LdisPBP1),published,journal,Biochemistry,Biochemistry,,,,1520-4995,0353,,,,,,,,,,,,,,,,,,,,,2020, citations,entry_citation,27952,162590,1,,entry citation,,,31690116,,,The Plasmodium falciparum Hsp70-x chaperone assists the heat stress response of the malaria parasite,published,journal,FASEB J.,FASEB journal : official publication of the Federation of American Societies for Experimental Biology,33,12,,1530-6860,,,,,,,,,,,,,,,,,,,,14611,14624,2019, citations,entry_citation,27953,162606,1,,entry citation,,,31690116,,,The Plasmodium falciparum Hsp70-x chaperone assists the heat stress response of the malaria parasite,published,journal,FASEB J.,FASEB journal : official publication of the Federation of American Societies for Experimental Biology,33,12,,1530-6860,,,,,,,,,,,,,,,,,,,,14611,14624,2019, citations,entry_citation,27954,162622,1,,entry citation,,,31339702,,,Nucleation of an Activating Conformational Change by a Cation-pi Interaction,published,journal,Biochemistry,Biochemistry,58,32,,1520-4995,,,,,,,,,,,,,,,,,,,,3408,3412,2019, citations,entry_citation,27955,162640,1,,entry citation,,,31889185,,,Adjacent mutations in the archaeal Rad50 ABC ATPase D-loop disrupt allosteric regulation of ATP hydrolysis through different mechanisms,published,journal,Nucleic Acids Res.,,48,5,,,,,,,,,,,,,,,,,,,,,,2457,2472,2020, citations,entry_citation,27956,162656,1,,entry citation,,,31889185,,,Adjacent mutations in the archaeal Rad50 ABC ATPase D-loop disrupt allosteric regulation of ATP hydrolysis through different mechanisms,published,journal,Nucleic Acids Res.,,48,5,,,,,,,,,,,,,,,,,,,,,,2457,2472,2020, citations,entry_citation,27957,162672,1,,entry citation,,,31889185,,,Adjacent mutations in the archaeal Rad50 ABC ATPase D-loop disrupt allosteric regulation of ATP hydrolysis through different mechanisms,published,journal,Nucleic Acids Res.,,48,5,,,,,,,,,,,,,,,,,,,,,,2457,2472,2020, citations,entry_citation,27958,162688,1,,entry citation,,,32052020,,,2'-Alkynyl spin-labelling is a minimally perturbing tool for DNA structural analysis,published,journal,Nucleic Acids Res.,,48,6,,,,,,,,,,,,,,,,,,,,,,2830,2840,2020, citations,citation_1,27959,162708,1,,entry citation,,,31637245,,,Including protons in solid-state NMR resonance assignment and secondary structure analysis: The example of RNA polymerase II subunits Rpo4/7,published,journal,Front. Mol. Biosci.,,6,,,,,,,,,,,,,,,,,,,,,,,100,100,2019, citations,citation_1,27960,162724,1,,entry citation,,,32962519,,,Identification and validation of a novel anti-virulent that binds to pyoverdine and inhibits its function,published,journal,Virulence,,11,1,,2150-5608,,,,,,,,,,,,,,,,,,,,1293,1309,2020, citations,entry_citation,27961,162742,1,,entry citation,,,31691092,,,NMR resonance assignments of the four isoforms of the hazelnut allergen Cor a 1.04,published,journal,Biomol. NMR Assignments,,14,1,,,,,,,,,,,,,,,,,,,,,,45,49,2020, citations,entry_citation,27962,162757,1,,entry citation,,,31868593,,,Indirect sexual selection drives rapid sperm protein evolution in abalone,published,journal,Elife,,8,,,,,,,,,,,,,,,,,,,,,,,e52628,e52628,2019, citations,entry_citation,27963,162775,1,,entry citation,,,31550880,,,Quantitative Conformational Analysis of Functionally Important Electrostatic Interactions in the Intrinsically Disordered Region of Delta Subunit of Bacterial RNA Polymerase,published,journal,J. Am. Chem. Soc.,,141,42,,,,,,,,,,,,,,,,,,,,,,16817,16828,2019, citations,entry_citation,27964,162790,1,,entry citation,,,31550880,,,Quantitative Conformational Analysis of Functionally Important Electrostatic Interactions in the Intrinsically Disordered Region of Delta Subunit of Bacterial RNA Polymerase,published,journal,J. Am. Chem. Soc.,,141,42,,,,,,,,,,,,,,,,,,,,,,16817,16828,2019, citations,entry_citation,27965,162809,1,,entry citation,,,31691092,,,NMR resonance assignments of the four isoforms of the hazelnut allergen Cor a 1.04,published,journal,Biomol. NMR Assignments,,14,1,,,,,,,,,,,,,,,,,,,,,,45,49,2020, citations,entry_citation,27967,162824,1,,entry citation,,,31691092,,,NMR resonance assignments of the four isoforms of the hazelnut allergen Cor a 1.04,published,journal,Biomol. NMR Assignments,,14,1,,,,,,,,,,,,,,,,,,,,,,45,49,2020, citations,entry_citation,27968,162839,1,,entry citation,,,31445682,,,Conformational Flexibility of p150Glued(1-191) Subunit of Dynactin Assembled with Microtubules,published,journal,Biophys. J.,,117,5,,,,,,,,,,,,,,,,,,,,,,938,949,2019, citations,entry_citation,27969,162854,1,,entry citation,,,32184322,,,Interleukin-2 druggability is modulated by global conformational transitions controlled by a helical capping switch,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,117,13,,1091-6490,,,,,,,,,,,,,,,,,,,,7183,7192,2020, citations,entry_citation,27970,162869,1,,entry citation,,,32184322,,,Interleukin-2 druggability is modulated by global conformational transitions controlled by a helical capping switch,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,117,13,,1091-6490,,,,,,,,,,,,,,,,,,,,7183,7192,2020, citations,entry_citation,27971,162883,1,,entry citation,,,32184322,,,Interleukin-2 druggability is modulated by global conformational transitions controlled by a helical capping switch,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,117,13,,1091-6490,,,,,,,,,,,,,,,,,,,,7183,7192,2020, citations,entry_citation,27972,162897,1,,entry citation,,,31896592,,,The Connector Domain of Vesicular Stomatitis Virus Large Protein Interacts with the Viral Phosphoprotein,published,journal,J. Virol.,Journal of virology,94,6,,1098-5514,,,,,,,,,,,,,,,,,,,,e01729-19,e01729-19,2020, citations,entry_citation,27973,162911,1,,entry citation,,,31445682,,,Conformational Flexibility of p150Glued(1-191) Subunit of Dynactin Assembled with Microtubules,published,journal,Biophys. J.,,117,5,,,,,,,,,,,,,,,,,,,,,,938,949,2019, citations,entry_citation,27974,162929,1,,entry citation,,,32184322,,,Interleukin-2 druggability is modulated by global conformational transitions controlled by a helical capping switch,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,117,13,,1091-6490,,,,,,,,,,,,,,,,,,,,7183,7192,2020, citations,entry_citation,27975,162944,1,,entry citation,,,32246827,,,"Structure, dynamics and function of the evolutionarily changing biliverdin reductase B family",published,journal,J. Biochem.,Journal of biochemistry,168,2,,1756-2651,,,,,,,,,,,,,,,,,,,,191,202,2020, citations,entry_citation,27976,162959,1,,entry citation,,,32246827,,,"Structure, dynamics and function of the evolutionarily changing biliverdin reductase B family",published,journal,J. Biochem.,Journal of biochemistry,168,2,,1756-2651,,,,,,,,,,,,,,,,,,,,191,202,2020, citations,citation_1,27977,162976,1,,entry citation,,,,10.3390/biom9120876,,Structure of the PUB Domain from Ubiquitin Regulatory X Domain Protein 1 (UBXD1) and Its Interaction with the p97 AAA+ ATPase,published,journal,Biomolecules,,9,12,,,,,,,,,,,,,,,,,,,,,,876,876,2019, citations,citation_1,27978,162996,1,,entry citation,,,31463759,,,"Complete 1H, 13C, 15N resonance assignments and secondary structure of the Vpr binding region of hHR23A (residues 223-363)",published,journal,Biomol. NMR Assign.,,14,1,,,,,,,,,,,,,,,,,,,,,,13,17,2020, citations,entry_citation,27979,163019,1,,entry citation,,,31487494,,,Structure and membrane-targeting of a Bordetella pertussis effector N-terminal domain,published,journal,Biochim. Biophys. 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Chem.,,295,2,,,,,,,,,,,,,,,,,,,,,,458,467,2020, citations,citation_1,27981,163060,1,,entry citation,,,31626806,,,Coordination of a single calcium ion in the EF-hand maintains the off state of the stromal interaction molecule luminal domain,published,journal,J. Mol. Biol.,,432,2,,,,,,,,,,,,,,,,,,,,,,367,383,2020, citations,citation_1,27982,163080,1,,entry citation,,,31626806,,,Coordination of a single calcium ion in the EF-hand maintains the off state of the stromal interaction molecule luminal domain,published,journal,J. Mol. Biol.,,432,2,,,,,,,,,,,,,,,,,,,,,,367,383,2020, citations,citation_1,27983,163100,1,,entry citation,,,31626806,,,Coordination of a single calcium ion in the EF-hand maintains the off state of the stromal interaction molecule luminal domain,published,journal,J. Mol. Biol.,,432,2,,,,,,,,,,,,,,,,,,,,,,367,383,2020, citations,entry_citation,27984,163120,1,,entry citation,,,31937588,,,Oxygen-dependent asparagine hydroxylation of the ubiquitin-associated (UBA) domain in Cezanne regulates ubiquitin binding,published,journal,J. Biol. Chem.,,295,8,,,,,,,,,,,,,,,,,,,,,,2160,2174,2020, citations,entry_citation,27986,163135,1,,entry citation,,,32289428,,,Dissecting the differential structural and dynamics features of CCL2 chemokine orthologs,published,journal,Int. J. Biol. Macromol.,International journal of biological macromolecules,156,,,1879-0003,,,,,,,,,,,,,,,,,,,,239,251,2020, citations,entry_citation,27987,163149,1,,entry citation,,,31617060,,,"Backbone, side chain and heme resonance assignment of the triheme cytochrome PpcA from Geobacter metallireducens in the oxidized state",published,journal,Biomol. NMR Assignments,,14,1,,,,,,,,,,,,,,,,,,,,,,31,36,2019, citations,entry_citation,27988,163167,1,,entry citation,,,,,,The CRY1 tail controls circadian timing by regulating its association with CLOCK:BMAL1,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,27989,163187,1,,entry citation,,,31734904,,,Backbone and side-chain chemical shift assignments for the ribosome-inactivating protein trichobakin (TBK),published,journal,Biomol. NMR Assignments,,14,1,,,,,,,,,,,,,,,,,,,,,,55,61,2020, citations,entry_citation,2799,163203,1,,entry citation,,,,,"Krishnamoorthi, Ramaswamy, Sun Lin, Chan-Lan, Gong, YuXi, VanderVelde, David, Hahn, Karl, ""Proton NMR Studies of Cucurbita maxima Trypsin Inhibitors: Evidence for pH-Dependent Conformational Change and His25-Tyr27 Interaction,"" Biochemistry 31 (3), 905-910 (1992).","Proton NMR Studies of Cucurbita maxima Trypsin Inhibitors: Evidence for pH-Dependent Conformational Change and His25-Tyr27 Interaction",published,journal,Biochemistry,,31,3,,,,,,,,,,,,,,,,,,,,,,905,910,1992, citations,citation_1,27990,163216,1,,entry citation,,,32611811,,,Intercepting second-messenger signaling by rationally designed peptides sequestering c-di-GMP,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,117,29,,1091-6490,,,,,,,,,,,,,,,,,,,,17211,17220,2020, citations,entry_citation,27992,163234,1,,entry citation,,,31642121,,,IDDomainSpotter: Compositional bias reveals domains in long disordered protein regions - insights from transcription factors,published,journal,Protein Sci.,,29,1,,,,,,,,,,,,,,,,,,,,,,169,183,2020, citations,entry_citation,27993,163250,1,,entry citation,,,31642121,,,IDDomainSpotter: Compositional bias reveals domains in long disordered protein regions - insights from transcription factors,published,journal,Protein Sci.,,29,1,,,,,,,,,,,,,,,,,,,,,,169,183,2020, citations,entry_citation,27994,163266,1,,entry citation,,,32936779,10.1126/sciadv.aba3681,,The structure of the RCAN1:CN complex explains the inhibition of and substrate recruitment by calcineurin,published,journal,Sci. Adv.,Science Advances,6,27,,,,,,,,,,,,,,,,,,,,,,3681,3681,2020, citations,entry_citation,27995,163281,1,,entry citation,,,32936779,10.1126/sciadv.aba3681,,The structure of the RCAN1:CN complex explains the inhibition of and substrate recruitment by calcineurin,published,journal,Sci. Adv.,Science Advances,6,27,,,,,,,,,,,,,,,,,,,,,,3681,3681,2020, citations,entry_citation,27996,163298,1,,entry citation,,,32936779,10.1126/sciadv.aba3681,,The structure of the RCAN1:CN complex explains the inhibition of and substrate recruitment by calcineurin,published,journal,Sci. Adv.,Science Advances,6,27,,,,,,,,,,,,,,,,,,,,,,3681,3681,2020, citations,entry_citation,27997,163314,1,,entry citation,,,32936779,10.1126/sciadv.aba3681,,The structure of the RCAN1:CN complex explains the inhibition of and substrate recruitment by calcineurin,published,journal,Sci. 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Rep.,Scientific reports,10,1,,2045-2322,,,,,,,,,,,,,,,,,,,,4051,4051,2020, citations,entry_citation,28006,163457,1,,entry citation,,,32132631,,,Structural features of the interaction of MapZ with FtsZ and membranes in Streptococcus pneumoniae,published,journal,Sci. Rep.,Scientific reports,10,1,,2045-2322,,,,,,,,,,,,,,,,,,,,4051,4051,2020, citations,entry_citation,28011,163473,1,,entry citation,,,,,,Phosphorylation of Mdm2 by DNA-Damage Response Kinases in physiological conditions monitored using 13C-NMR,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,28012,163490,1,,entry citation,,,31540099,,,Development of a fragment-based screening assay for the focal adhesion targeting domain using SPR and NMR,published,journal,Molecules,"Molecules (Basel, Switzerland)",24,18,,1420-3049,,,,,,,,,,,,,,,,,,,,E3352,E3352,2019, citations,entry_citation,28015,163508,1,,entry citation,,,,10.1039/D0SC03441J,,Structural impact of GTP binding on downstream KRAS signaling,accepted,journal,Chem. Sci.,,,,,,,,,,,,,,,,,,,,,,,,,,,2020, citations,entry_citation,28016,163529,1,,entry citation,,,31691092,,,NMR resonance assignments of the four isoforms of the hazelnut allergen Cor a 1.04,published,journal,Biomol. NMR Assignments,,14,1,,,,,,,,,,,,,,,,,,,,,,45,49,2020, citations,Citation1,28017,163544,1,,entry citation,,,31568752,,,Molecular mechanism of the inhibition of TDP-43 amyloidogenesis by QBP1,published,journal,Arch. Biochem. 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U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,117,15,,1091-6490,,,,,,,,,,,,,,,,,,,,8503,8514,2020, citations,entry_citation,28027,163677,1,,entry citation,,,32234784,,,Nonclassical nuclear localization signals mediate nuclear import of CIRBP,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,117,15,,1091-6490,,,,,,,,,,,,,,,,,,,,8503,8514,2020, citations,entry_citation,28028,163691,1,,entry citation,,,31792831,,,"1H, 13C, 15N backbone and side-chain resonance assignment of the native form of UbcH7 (UBE2L3) through solution NMR spectroscopy",published,journal,Biomol. NMR Assignments,,14,1,,,,,,,,,,,,,,,,,,,,,,73,78,2020, citations,citation_1,28030,163707,1,,entry citation,,,31993958,,,"Complete assignment of Ala, Ile, LeuProS, Met and ValProS methyl groups of the protruding domain from human norovirus GII.4 Saga",published,journal,Biomol. NMR Assignments,,14,1,,1874-270X,,,,,,,,,,,,,,,,,,,,123,130,2020, citations,citation_1,28031,163734,1,,entry citation,,,31963646,,,Disulfide-Linked Peptides for Blocking BTLA/HVEM Binding,published,journal,Int. J. Mol. Sci.,International journal of molecular sciences,21,2,,1422-0067,,,,,,,,,,,,,,,,,,,,,,2020, citations,entry_citation,28033,163748,1,,entry citation,,,32139510,,,"The dynein light chain 8 (LC8) binds predominantly ""in-register"" to a multivalent intrinsically disordered partner",published,journal,J. Biol. Chem.,The Journal of biological chemistry,295,15,,1083-351X,,,,,,,,,,,,,,,,,,,,4912,4922,2020, citations,entry_citation,28034,163765,1,,entry citation,,,32081587,,,Conditional disorder in small heat-shock proteins,published,journal,J. Mol. Biol.,,432,9,,,,,,,,,,,,,,,,,,,,,,3033,3049,2020, citations,entry_citation,28035,163781,1,,entry citation,,,,10.1007/s12104-020-09927-w,,"Solid-state NMR 13C, 15N assignments of human histone H3 in the nucleosome core particle",published,journal,Biomol. NMR Assignments,,14,1,,,,,,,,,,,,,,,,,,,,,,99,104,2020, citations,entry_citation,28036,163798,1,,entry citation,,,,,,"1H, 15N and 13C backbone chemical shift assignment of Shaker-VSD(S2bot_mutant)",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,28037,163813,1,,entry citation,,,31950462,,,"1H, 13C, 15 N chemical shift assignments of the FKBP12 protein from the pathogenic fungi Candida auris and Candida glabrata",published,journal,Biomol. NMR Assignments,,14,1,,,,,,,,,,,,,,,,,,,,,,105,109,2020, citations,entry_citation,28038,163830,1,,entry citation,,,31950462,,,"1H, 13C, 15 N chemical shift assignments of the FKBP12 protein from the pathogenic fungi Candida auris and Candida glabrata",published,journal,Biomol. NMR Assignments,,14,1,,,,,,,,,,,,,,,,,,,,,,105,109,2020, citations,entry_citation,2804,163847,1,,entry citation,,,,,"Mills, Robyn G., O'Donoghue, Sean I., Smith, Ross, King, Glenn F., ""Solution Structure of Endothelin-3 Determined Using NMR Spectroscopy,"" Biochemistry 31 (24), 5640-5645 (1992).",Solution Structure of Endothelin-3 Determined Using NMR Spectroscopy,published,journal,Biochemistry,,31,24,,,,,,,,,,,,,,,,,,,,,,5640,5645,1992, citations,entry_citation,28042,163860,1,,entry citation,,,32160516,,,An Extended Conformation for K48 Ubiquitin Chains Revealed by the hRpn2:Rpn13:K48-Diubiquitin Structure,published,journal,Structure,"Structure (London, England : 1993)",28,5,,1878-4186,,,,,,,,,,,,,,,,,,,,495,506.e3,2020, citations,citations_1,28045,163886,1,,entry citation,,,32157247,,,A short motif in the N-terminal region of alpha-synuclein is critical for both aggregation and function,published,journal,Nat. Struct. Mol. Biol.,Nature structural & molecular biology,27,3,,1545-9985,,,,,,,,,,,,,,,,,,,,249,259,2020, citations,entry_citation,28046,163909,1,,entry citation,,,31916136,,,NMR resonance assignments for the active and inactive conformations of the small G protein RalA,published,journal,Biomol. NMR Assignments,,14,1,,,,,,,,,,,,,,,,,,,,,,87,91,2020, citations,entry_citation,28047,163928,1,,entry citation,,,31916136,,,NMR resonance assignments for the active and inactive conformations of the small G protein RalA,published,journal,Biomol. NMR Assignments,,14,1,,,,,,,,,,,,,,,,,,,,,,87,91,2020, citations,entry_citation,28048,163945,1,,entry citation,,,32376391,,,The molecular basis of specific DNA binding by the BRG1 AT-hook and bromodomain,published,journal,Biochim. Biophys. Acta Gene Regul. Mech.,Biochimica et biophysica acta. Gene regulatory mechanisms,,,,1876-4320,,,,,,,,,,,,,,,,,,,,194566,194566,2020, citations,entry_citation,28049,163959,1,,entry citation,,,31889185,,,Adjacent mutations in the archaeal Rad50 ABC ATPase D-loop disrupt allosteric regulation of ATP hydrolysis through different mechanisms,published,journal,Nucleic Acids Res.,,48,5,,,,,,,,,,,,,,,,,,,,,,2457,2472,2020, citations,entry_citation,28050,163975,1,,entry citation,,,31896582,,,Structure of the cell-binding component of the Clostridium difficile binary toxin reveals a novel macromolecular assembly,published,journal,Proc. Natl. Acad. Sci. 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Chem.,Analytical chemistry,92,11,,1520-6882,,,,,,,,,,,,,,,,,,,,7786,7793,2020, citations,entry_citation,28054,164042,1,,entry citation,,,32246962,,,Mutation of Conserved Mre11 Residues Alter Protein Dynamics to Separate Nuclease Functions,published,journal,J. Mol. Biol.,Journal of molecular biology,432,10,,1089-8638,,,,,,,,,,,,,,,,,,,,3289,3308,2020, citations,entry_citation,28056,164057,1,,entry citation,,,32495035,,,"1H, 13C, 15N backbone resonance assignments of the apo and holo forms of the solute binding protein PiuA from Streptococcus pneumoniae",published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,,,,1874-270X,,,,,,,,,,,,,,,,,,,,,,2020, citations,entry_citation,28057,164073,1,,entry citation,,,32495035,,,"1H, 13C, 15N backbone resonance assignments of the apo and holo forms of the solute binding protein PiuA from Streptococcus pneumoniae",published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,,,,1874-270X,,,,,,,,,,,,,,,,,,,,,,2020, citations,entry_citation,28058,164093,1,,entry citation,,,32184239,10.1128/mBio.00226-20,,Structural basis of Ca 2+ -dependent self-processing activity of repeat-in-toxin proteins,published,journal,mBio,,11,2,,,,,,,,,,,,,,,,,,,,,,e00226-20,e00226-20,2020, citations,entry_citation,28059,164125,1,,entry citation,,,32710623,,,Structural basis of DNA binding to human YB-1 cold shock domain regulated by phosphorylation,published,journal,Nucleic Acids Res.,Nucleic acids research,48,16,,1362-4962,,,,,,,,,,,,,,,,,,,,9361,9371,2020, citations,citations_1,28060,164142,1,,entry citation,,,,,,HP1,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,28065,164157,1,,entry citation,,,32832664,,,PProteasomal degradation of the intrinsically disordered protein tau at single-residue resolution,published,journal,Sci. Adv.,Science advances,6,30,,2375-2548,,,,,,,,,,,,,,,,,,,,eaba3916,eaba3916,2020, citations,entry_citation,28066,164172,1,,entry citation,,,,,,Comparison of the spatial structures of cyclosporin D in different media (chloroform and micellar solution) using NMR spectroscopy,in preparation,journal,J. Biomol. Struct. Dyn.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,28077,164194,1,,entry citation,,,,,,"'Backbone 1H, 13C, 15N chemical shift assignments of BRCT'",na,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,28086,164208,1,,entry citation,,,32697992,,,Pseudo-RNA binding domains mediate RNA structure specificity in Upstream of N-Ras,published,journal,Cell Rep.,Cell reports,32,3,,2211-1247,0353,,,,,,,,,,,,,,,,,,,107930,107930,2020, citations,entry_citation,28088,164224,1,,entry citation,,,32697992,,,Pseudo-RNA binding domains mediate RNA structure specificity in Upstream of N-Ras,published,journal,Cell Rep.,Cell reports,32,3,,2211-1247,0353,,,,,,,,,,,,,,,,,,,107930,107930,2020, citations,paper,28092,164240,1,,entry citation,,,,,,Hydrogen/deuterium exchange memory NMR reveals structural epitopes involved in IgE cross-reactivity of allergenic lipid transfer proteins,in preparation,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,28094,164257,1,,entry citation,,,32807496,,,NMR structure of Dengue West Nile viruses stem-loop B: A key cis-acting element for flavivirus replication,published,journal,Biochem. Biophys. Res. Commun.,,,,,,,,,,,,,,,,,,,,,,,,,,,2020, citations,entry_citation,28095,164272,1,,entry citation,,,,,,Allomorphy as a mechanism of post-translational control of enzyme activity,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,28096,164289,1,,entry citation,,,,,,Allomorphy as a mechanism of post-translational control of enzyme activity,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,28097,164306,1,,entry citation,,,,,,Allomorphy as a mechanism of post-translational control of enzyme activity,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,28098,164329,1,,entry citation,,,,,,Spindly: A dynein adaptor with a significant role in mitotic division,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,28107,164346,1,,entry citation,,,,,,TAPBPR Promotes Loading of Cargo on MHC-I Molecules Using a Peptide Trap,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,28108,164363,1,,entry citation,,,,,,TAPBPR Promotes Loading of Cargo on MHC-I Molecules Using a Peptide Trap,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,28111,164380,1,,entry citation,,,,,,Proline-rich domain of human ALIX contains multiple TSG101-UEV interaction sites and forms phosphorylation-mediated reversible amyloids,accepted,journal,Proc. Natl. Acad. Sci. U. S. A.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,28113,164395,1,,entry citation,,,32611767,,,Hairpin RNA-induced conformational change of a eukaryotic-specific lysyl-tRNA synthetase extension and role of adjacent anticodon-binding domain,published,journal,J. Biol. Chem.,The Journal of biological chemistry,295,34,,1083-351X,,,,,,,,,,,,,,,,,,,,12071,12085,2020, citations,entry_citation,28114,164411,1,,entry citation,,,,,,"AILVproS stereospecific methyl chemical shift assignments of HLA-A*01:01, a human class I major histocompatibility complex heavy chain, bound to NRASQ61K neoepitope and human beta-2 microglobulin",na,BMRB only,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,28123,164430,1,,entry citation,,,32530275,,,Identification and Quantification of Oxidation Products in Full-Length Biotherapeutic Antibodies by NMR Spectroscopy,published,journal,Anal. 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Chem.,,92,14,,,,,,,,,,,,,,,,,,,,,,9666,9673,2020, citations,entry_citation,28127,164514,1,,entry citation,,,32530275,,,Identification and Quantification of Oxidation Products in Full-Length Biotherapeutic Antibodies by NMR Spectroscopy,published,journal,Anal. Chem.,,92,14,,,,,,,,,,,,,,,,,,,,,,9666,9673,2020, citations,entry_citation,28128,164536,1,,entry citation,,,32530275,,,Identification and Quantification of Oxidation Products in Full-Length Biotherapeutic Antibodies by NMR Spectroscopy,published,journal,Anal. Chem.,,92,14,,,,,,,,,,,,,,,,,,,,,,9666,9673,2020, citations,entry_citation,28129,164556,1,,entry citation,,,32530275,,,Identification and Quantification of Oxidation Products in Full-Length Biotherapeutic Antibodies by NMR Spectroscopy,published,journal,Anal. Chem.,,92,14,,,,,,,,,,,,,,,,,,,,,,9666,9673,2020, citations,entry_citation,28130,164577,1,,entry citation,,,32530275,,,Identification and Quantification of Oxidation Products in Full-Length Biotherapeutic Antibodies by NMR Spectroscopy,published,journal,Anal. Chem.,,92,14,,,,,,,,,,,,,,,,,,,,,,9666,9673,2020, citations,entry_citation,28133,164599,1,,entry citation,,,32898583,,,Structural Analysis of the Regulatory GAF Domains of cGMP Phosphodiesterase Elucidates the Allosteric Communication Pathway,published,journal,J. Mol. Biol.,,,,,,,,,,,,,,,,,,,,,,,,,,,2020, citations,entry_citation,28136,164617,1,,entry citation,,,31634467,,,The LC8-RavP Ensemble Structure Evinces A Role for LC8 in Regulating Lyssavirus Polymerase Functionality,published,journal,J. Mol. Biol.,,431,24,,,,,,,,,,,,,,,,,,,,,,4959,4977,2019, citations,entry_citation,28137,164631,1,,entry citation,,,31634467,10.1016/j.jmb.2019.10.011,,The LC8-RavP ensemble Structure Evinces A Role for LC8 in Regulating Lyssavirus Polymerase Functionality,published,journal,J. Mol. Biol.,,431,24,,,,,,,,,,,,,,,,,,,,,,4959,4977,2019, citations,entry_citation,28138,164645,1,,entry citation,,,31634467,10.1016/j.jmb.2019.10.011,,The LC8-RavP ensemble Structure Evinces A Role for LC8 in Regulating Lyssavirus Polymerase Functionality,published,journal,J. Mol. Biol.,,431,24,,,,,,,,,,,,,,,,,,,,,,4959,4977,2019, citations,entry_citation,283,164659,1,,entry citation,,,,,"Forman-Kay, Julie D., Gronenborn, Angela M., Kay, Lewis E., Wingfield, Paul, Clore, G. 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Walter, ""Assignment of paramagnetically shifted resonances in the 1H NMR spectrum of horse ferricytochrome c,"" Biophys. J. 57, 15-22 (1990).","Assignment of paramagnetically shifted resonances in the 1H NMR spectrum of horse ferricytochrome c",published,journal,Biophys. J.,,57,,,,,,,,,,,,,,,,,,,,,,,15,22,1990, citations,entry_citation,2852,164701,1,,entry citation,,,,,"Constantine, Keith L., Brew, Shelesa A., Ingham, Kenneth C., Llinas, M., ""1H-n.m.r. studies of the fibronectin 13kDa collagen-binding fragment Evidence for autonomous conserved typeI and type II domain folds,"" Biochem. J. 283, 247-254 (1992).","1H-n.m.r. studies of the fibronectin 13kDa collagen-binding fragment Evidence for autonomous conserved typeI and type II domain folds",published,journal,Biochem. J.,,283,,,,,,,,,,,,,,,,,,,,,,,247,254,1992, citations,entry_citation,2853,164714,1,,entry citation,,,,,"Constantine, Keith L., Brew, Shelesa A., Ingham, Kenneth C., Llinas, M., ""1H-n.m.r. studies of the fibronectin 13kDa collagen-binding fragment Evidence for autonomous conserved typeI and type II domain folds,"" Biochem. J. 283, 247-254 (1992).","1H-n.m.r. studies of the fibronectin 13kDa collagen-binding fragment Evidence for autonomous conserved typeI and type II domain folds",published,journal,Biochem. J.,,283,,,,,,,,,,,,,,,,,,,,,,,247,254,1992, citations,entry_citation,2856,164727,1,,entry citation,,,,,"Adler, Marc, Wagner, Gerhard, ""Sequential 1H NMR Assignments of Kistrin, a Potent Platelet Aggregation Inhibitor and Glycoprotein IIB-IIIa Antagonist,"" Biochemistry 31 (4), 1031-1039 (1992).","Sequential 1H NMR Assignments of Kistrin, a Potent Platelet Aggregation Inhibitor and Glycoprotein IIB-IIIa Antagonist",published,journal,Biochemistry,,31,4,,,,,,,,,,,,,,,,,,,,,,1031,1039,1992, citations,entry_citation,2858,164740,1,,entry citation,,,,,"Perkins, Stephen J., Dwek, Raymond A., ""Comparisons of Ring-Current Shifts Calculated from the Crystal Structure of Egg White Lysozyme of Hen with the Proton Nuclear Magnetic Resonance Spectrum of Lysozyme in Solution,"" Biochemistry 19 (2), 246-258 (1980).","Comparisons of Ring-Current Shifts Calculated from the Crystal Structure of Egg White Lysozyme of Hen with the Proton Nuclear Magnetic Resonance Spectrum of Lysozyme in Solution",published,journal,Biochemistry,,19,2,,,,,,,,,,,,,,,,,,,,,,246,258,1980, citations,entry_citation,286,164753,1,,entry citation,,,,,"Feng, Yiqing, Roder, Heinrich, Englander, S. Walter, ""Assignment of paramagnetically shifted resonances in the 1H NMR spectrum of horse ferricytochrome c,"" Biophys. J. 57, 15-22 (1990).","Assignment of paramagnetically shifted resonances in the 1H NMR spectrum of horse ferricytochrome c",published,journal,Biophys. J.,,57,,,,,,,,,,,,,,,,,,,,,,,15,22,1990, citations,entry_citation,2868,164769,1,,entry citation,,,,,"Martineau, Laure, Craescu, Constantin T., ""Sequential assignment of the proton NMR spectrum of isolated alpha(CO) chains from human adult hemoglobin,"" Eur. J. Biochem. 205, 661-670 (1992).","Sequential assignment of the proton NMR spectrum of isolated alpha(CO) chains from human adult hemoglobin",published,journal,Eur. J. Biochem.,,205,,,,,,,,,,,,,,,,,,,,,,,661,670,1992, citations,entry_citation,287,164782,1,,entry citation,,,,,"Gronenborn, Angela M., Wingfield, Paul, Clore, G. Marius, ""Determination of The Secondary Structure of the DNA Binding Protein Ner from Phage Mu Using 1H Homonuclear and 15N-1H Heteronuclear NMR Spectroscopy,"" Biochemistry 28, 5081-5089 (1989).","Determination of The Secondary Structure of the DNA Binding Protein Ner from Phage Mu Using 1H Homonuclear and 15N-1H Heteronuclear NMR Spectroscopy",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,5081,5089,1989, citations,entry_citation,288,164795,1,,entry citation,,,,,"Gronenborn, Angela M., Wingfield, Paul, Clore, G. Marius, ""Determination of The Secondary Structure of the DNA Binding Protein Ner from Phage Mu Using 1H Homonuclear and 15N-1H Heteronuclear NMR Spectroscopy,"" Biochemistry 28, 5081-5089 (1989).","Determination of The Secondary Structure of the DNA Binding Protein Ner from Phage Mu Using 1H Homonuclear and 15N-1H Heteronuclear NMR Spectroscopy",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,5081,5089,1989, citations,entry_citation,289,164808,1,,entry citation,,,,,"Hyberts, Sven G., Wagner, Gerhard, ""Sequence-Specific 1H NMR Assignments and Secondary Structure of Eglin c,"" Biochemistry 29, 1465-1474 (1990).",Sequence-Specific 1H NMR Assignments and Secondary Structure of Eglin c,published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,1465,1474,1990, citations,entry_citation,29,164822,1,,entry citation,,,,,"Klevit, Rachel E., Drobny, Gary P., Waygood, E. Bruce, ""Two-Dimensional 1H NMR studies of Histidine-Containing Protein from Escherichia coli. 1. Sequential Resonance Assignments,"" Biochemistry 25, 7760-7769 (1986).","Two-Dimensional 1H NMR studies of Histidine-Containing Protein from Escherichia coli. 1. Sequential Resonance Assignments",published,journal,Biochemistry,,25,,,,,,,,,,,,,,,,,,,,,,,7760,7769,1986, citations,entry_citation,290,164835,1,,entry citation,,,,,"Marsden, Brian J., Hodges, Robert S., Sykes, Brian D., ""A 1H NMR Determination of the Solution Conformation of a Synthetic Peptide Analogue of Calcium-Binding Site III of Rabbit Skeletal Troponin C,"" Biochemistry 28, 8839-8847 (1989).","A 1H NMR Determination of the Solution Conformation of a Synthetic Peptide Analogue of Calcium-Binding Site III of Rabbit Skeletal Troponin C",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,8839,8847,1989, citations,entry_citation,291,164848,1,,entry citation,,,,,"Emerson, S. Donald, La Mar, Gerd N., ""Solution Structural Characterization of Cyanometmyoglobin: Resonance Assignment of Heme Cavity Residues by Two-Dimensional NMR,"" Biochemistry 29, 1545-1556 (1990).","Solution Structural Characterization of Cyanometmyoglobin: Resonance Assignment of Heme Cavity Residues by Two-Dimensional NMR",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,1545,1556,1990, citations,entry_citation,2917,164861,1,,entry citation,,,,,"Cassels, Robert, Dobson, Christopher M., Poulsen, Flemming M., Williams, Robert J. P., ""Study of Tryptophan Residues of Lysozyme Using 1H Nuclear Magnetic Resonance,"" Eur. J. Biochem. 92, 81-97 (1978).",Study of Tryptophan Residues of Lysozyme Using 1H Nuclear Magnetic Resonance,published,journal,Eur. J. Biochem.,,92,,,,,,,,,,,,,,,,,,,,,,,81,97,1978, citations,entry_citation,292,164874,1,,entry citation,,,,,"Emerson, S. Donald, La Mar, Gerd N., ""Solution Structural Characterization of Cyanometmyoglobin: Resonance Assignment of Heme Cavity Residues by Two-Dimensional NMR,"" Biochemistry 29, 1545-1556 (1990).","Solution Structural Characterization of Cyanometmyoglobin: Resonance Assignment of Heme Cavity Residues by Two-Dimensional NMR",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,1545,1556,1990, citations,entry_citation,2928,164887,1,,entry citation,,,,,"Rico, Manuel, Santoro, Jorge, Gonzalez, Carlos, Bruix, Marta, Neira, Jose Luis, Nieto, Jose Luis, Herranz, Jose, ""3D structure of bovine pancreatic ribonuclease A in aqueous solution: An approach to tertiary structure determination from a small basis of 1H NMR NOE correlations,"" J. Biomol. NMR 1 (3), 283-298 (1991).","3D structure of bovine pancreatic ribonuclease A in aqueous solution: An approach to tertiary structure determination from a small basis of 1H NMR NOE correlations",published,journal,J. Biomol. NMR,,1,3,,,,,,,,,,,,,,,,,,,,,,283,298,1991, citations,entry_citation,293,164900,1,,entry citation,,,,,"Emerson, S. Donald, La Mar, Gerd N., ""Solution Structural Characterization of Cyanometmyoglobin: Resonance Assignment of Heme Cavity Residues by Two-Dimensional NMR,"" Biochemistry 29, 1545-1556 (1990).","Solution Structural Characterization of Cyanometmyoglobin: Resonance Assignment of Heme Cavity Residues by Two-Dimensional NMR",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,1545,1556,1990, citations,entry_citation,2935,164913,1,,entry citation,,,,,"Keating, Kelly A., La Mar, Gerd N., Shiau, Fuu-Yau, Smith, Kevin M., ""1H NMR Study of the Molecular and Electronic Structure of Paramagnetic Iron Chlorin Complexes of Myoglobin: Dynamic Heterogeneity of the Heme Pocket,"" J. Am. Chem. Soc. 114 (16), 6513-6520 (1992).","1H NMR Study of the Molecular and Electronic Structure of Paramagnetic Iron Chlorin Complexes of Myoglobin: Dynamic Heterogeneity of the Heme Pocket",published,journal,J. Am. Chem. Soc.,,114,16,,,,,,,,,,,,,,,,,,,,,,6513,6520,1992, citations,entry_citation,2936,164926,1,,entry citation,,,,,"Keating, Kelly A., La Mar, Gerd N., Shiau, Fuu-Yau, Smith, Kevin M., ""1H NMR Study of the Molecular and Electronic Structure of Paramagnetic Iron Chlorin Complexes of Myoglobin: Dynamic Heterogeneity of the Heme Pocket,"" J. Am. Chem. Soc. 114 (16), 6513-6520 (1992).","1H NMR Study of the Molecular and Electronic Structure of Paramagnetic Iron Chlorin Complexes of Myoglobin: Dynamic Heterogeneity of the Heme Pocket",published,journal,J. Am. Chem. Soc.,,114,16,,,,,,,,,,,,,,,,,,,,,,6513,6520,1992, citations,entry_citation,2939,164939,1,,entry citation,,,,,"Fry, David C., Madison, Vincent S., Greeley, David N., Felix, Arthur M., Heimer, Edgar P., Frohman, Lawrence, Campbell, Robert M., Mowles, Thomas F., Toome, Voldemar, Wegrzynski, Bogda B., ""Solution Structures of Cyclic and Dicyclic Analogues of Growth Hormone Releasing factor as Determined by Two-Dimensional NMR an CD Spectroscopies and Constrained Molecular Dynamics,"" Biopolymers 32, 649-666 (1992).","Solution Structures of Cyclic and Dicyclic Analogues of Growth Hormone Releasing factor as Determined by Two-Dimensional NMR an CD Spectroscopies and Constrained Molecular Dynamics",published,journal,Biopolymers,,32,,,,,,,,,,,,,,,,,,,,,,,649,666,1992, citations,entry_citation,294,164952,1,,entry citation,,,,,"Guiles, R.D., Altman, John, Lipka, James J., Kuntz, Irwin D., Waskell, Lucy, ""Structural Studies of Cytochrome b5: Complete Sequence-Specific Resonance Assignments for the Trypsin-Solubilized Microsomal Ferrocytochrome b5 Obtained from Pig and Calf,"" Biochemistry 29, 1276-1289 (1990).","Structural Studies of Cytochrome b5: Complete Sequence-Specific Resonance Assignments for the Trypsin-Solubilized Microsomal Ferrocytochrome b5 Obtained from Pig and Calf",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,1276,1289,1990, citations,entry_citation,3,165177,1,,entry citation,,,,,"Holak, Tadeusz A., Prestegard, J.H., ""Secondary Structure of Acyl Carrier Protein as Derived from Two-Dimensional 1H NMR Spectroscopy,"" Biochemistry 25, 5766-5774 (1986).","Secondary Structure of Acyl Carrier Protein as Derived from Two-Dimensional 1H NMR Spectroscopy",published,journal,Biochemistry,,25,,,,,,,,,,,,,,,,,,,,,,,5766,5774,1986, citations,entry_citation,2940,164965,1,,entry citation,,,,,"Fry, David C., Madison, Vincent S., Greeley, David N., Felix, Arthur M., Heimer, Edgar P., Frohman, Lawrence, Campbell, Robert M., Mowles, Thomas F., Toome, Voldemar, Wegrzynski, Bogda B., ""Solution Structures of Cyclic and Dicyclic Analogues of Growth Hormone Releasing factor as Determined by Two-Dimensional NMR an CD Spectroscopies and Constrained Molecular Dynamics,"" Biopolymers 32, 649-666 (1992).","Solution Structures of Cyclic and Dicyclic Analogues of Growth Hormone Releasing factor as Determined by Two-Dimensional NMR an CD Spectroscopies and Constrained Molecular Dynamics",published,journal,Biopolymers,,32,,,,,,,,,,,,,,,,,,,,,,,649,666,1992, citations,entry_citation,2941,164978,1,,entry citation,,,,,"Fry, David C., Madison, Vincent S., Greeley, David N., Felix, Arthur M., Heimer, Edgar P., Frohman, Lawrence, Campbell, Robert M., Mowles, Thomas F., Toome, Voldemar, Wegrzynski, Bogda B., ""Solution Structures of Cyclic and Dicyclic Analogues of Growth Hormone Releasing factor as Determined by Two-Dimensional NMR an CD Spectroscopies and Constrained Molecular Dynamics,"" Biopolymers 32, 649-666 (1992).","Solution Structures of Cyclic and Dicyclic Analogues of Growth Hormone Releasing factor as Determined by Two-Dimensional NMR an CD Spectroscopies and Constrained Molecular Dynamics",published,journal,Biopolymers,,32,,,,,,,,,,,,,,,,,,,,,,,649,666,1992, citations,entry_citation,2948,164991,1,,entry citation,,,,,"Paolillo, Livio, Simonetti, Mario, Brakch, Noureddine, D'Auria, Gabriella, Saviano, Michele, Dettin, Monica, Rholam, Mohamed, Scatturin, A., Di Bello, C., Cohen, Paul, ""Evidence for the presence of a secondary structure at the dibasic processing site of prohormone: the pro-ocytocin model,"" EMBO J. 11 (7), 2399-2405 (1992).","Evidence for the presence of a secondary structure at the dibasic processing site of prohormone: the pro-ocytocin model",published,journal,EMBO J.,,11,7,,,,,,,,,,,,,,,,,,,,,,2399,2405,1992, citations,entry_citation,295,165004,1,,entry citation,,,,,"Guiles, R.D., Altman, John, Lipka, James J., Kuntz, Irwin D., Waskell, Lucy, ""Structural Studies of Cytochrome b5: Complete Sequence-Specific Resonance Assignments for the Trypsin-Solubilized Microsomal Ferrocytochrome b5 Obtained from Pig and Calf,"" Biochemistry 29, 1276-1289 (1990).","Structural Studies of Cytochrome b5: Complete Sequence-Specific Resonance Assignments for the Trypsin-Solubilized Microsomal Ferrocytochrome b5 Obtained from Pig and Calf",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,1276,1289,1990, citations,entry_citation,2950,165017,1,,entry citation,,,,,"Kar, L., de Croos, P.Z., Roman, S.J., Matsumura, P., Johnson, M. 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Engl.,,,,ACIEAY,1521-3773,0179,,,,,,,,,,,,,,,,,,,,,2020, citations,citation_1,30738,178857,1,,entry citation,,,,,,Solution NMR structure of the myristoylated feline immunodeficiency virus matrix protein,in preparation,journal,,,,,,,0353,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,30739,178883,1,,entry citation,,,,,,Solution NMR structure of the unmyristoylated feline immunodeficiency virus matrix protein,in preparation,journal,,,,,,,0353,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,30740,178909,1,,entry citation,,,,,,Solution NMR Structure of the G4L/Q5K/G6S (NOS) Unmyristoylated Feline Immunodeficiency Virus Matrix Protein,in preparation,journal,,,,,,,0353,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,30741,178935,1,,entry citation,,,,,,Atomic-Resolution Structure of HIV-1 Capsid Tubes by Magic Angle Spinning NMR,in preparation,journal,,,,,,,0353,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,30744,178965,1,,entry citation,,,32828849,,,Membrane interactions of the anuran antimicrobial peptide HSP1-NH 2: Different aspects of the association to anionic and zwitterionic biomimetic systems,published,journal,Biochim. 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Biol. 250, 134-143 (1995).","NMR Structure of a Stable ""OB-fold"" Sub-domain Isolated from Staphylococcal Nuclease",published,journal,J. Mol. Biol.,Journal of Molecular Biology,250,2,,,,,,,,,,,,,,,,,,,,,,134,143,1995, citations,entry_citation,4011,192389,1,,entry citation,,96067700,,,"Jacks, A.J., Sorimachi, K., Le Gal-Coeffe, M-F., Williamson, G., Archer, D.B., and Williamson, M.P., ""1H and 15N Assignments and Secondary Structure of the Starch-binding Domain of Glucoamylase from Aspergillus niger,"" Eur. J. Biochem., 233, 568-578 (1995).","1H and 15N Assignments and Secondary Structure of the Starch-binding Domain of Glucoamylase from Aspergillus niger",published,journal,Eur. J. Biochem.,European Journal of Biochemistry,233,,,,,,,,,,,,,,,,,,,,,,,568,578,1995, citations,entry_citation,4012,192409,1,,entry citation,,,8810899,,,Structure of the Acid State of E. coli Ribonuclease H1,published,journal,Biochemistry,,35,,,,,,,,,,,,,,,,,,,,,,,11951,11958,1996, citations,entry_citation,4019,192423,1,,entry citation,,,,,"Koide, S., Gippert, G.P., Reymond, M., and Wright P.E., ""1H, 13C and 15N Resonance Assignments of Recombinant Poplar Plastocyanin.""","1H, 13C and 15N Resonance Assignments of Recombinant Poplar Plastocyanin",published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,secondary_citation,4019,192424,2,,reference citation,,,,,"Gippert, G. P., ""New Computational Methods for 3D NMR Data Analysis and Protein Structure Determination in High-Dimensional Internal Coordinate Space,"" Thesis, The Scripps Research Institute, La Jolla, CA USA (1995).","New Computational Methods for 3D NMR Data Analysis and Protein Structure Determination in High-Dimensional Internal Coordinate Space",,thesis,,,,,,,,,,,,,,,,,,,,,,The Scripps Research Institute,La Jolla,USA,,4-1,4-88,1995, citations,entry_citation,402,192443,1,,entry citation,,,,,"Ni, Feng, Konishi, Yasuo, Bullock, Lea Doerr, Rivetna, Meheryar N., Scheraga, H.A., ""High-Resolution NMR Studies of Fibrinogen-like Peptides in Solution: Structural Basis for the Bleeding Disorder Caused by a Single Mutation of Gly(12) to Val(12) in the Aalpha Chain of Human Fibrinogen Rouen,"" Biochemistry 28, 3106-3119 (1989).","High-Resolution NMR Studies of Fibrinogen-like Peptides in Solution: Structural Basis for the Bleeding Disorder Caused by a Single Mutation of Gly(12) to Val(12) in the Aalpha Chain of Human Fibrinogen Rouen",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,3106,3119,1989, citations,entry_citation,4020,192456,1,,entry citation,,97098087,,,"Doreleijers, J.F., Langedijk, J.P.M., Herd, K., Boelens, R., Rullmann, J.A.C., Schaaper, W. M., van Oirschot, J.T., and Kaptein, R., ""Solution Structure of the Immunodominant Region of Protein G of Bovine Respiratory Syncytial Virus,"" Biochemistry 35, 14684-14688 (1996).","Solution Structure of the Immunodominant Region of Protein G of Bovine Respiratory Syncytial Virus",published,journal,Biochemistry,,35,47,,,,,,,,,,,,,,,,,,,,,,14684,14688,1996,"ABSTRACT The three-dimensional solution structure of the immunodominant central conserved region of the attachment protein G (BRSV-G) of bovine respiratory syncytial virus has been determined by nuclear magnetic resonance (NMR) spectroscopy. In the 32-residue peptide studied, 19 residues form a small rigid core composed of two short helices, connected by a type I' turn, and linked by two disulfide bridges. This unique fold is among the smallest stable tertiary structures known and could therefore serve as an ideal building block for the design of de novo proteins and as a test case for modeling studies. A characteristic hydrophobic pocket, lined by conserved residues lies at the surface of the peptide and may play a role in receptor binding. This work provides a structural basis for further peptide vaccine development against the severe diseases associated with the respiratory syncytial viruses both in cattle and man. Bovine respiratory syncytial virus (BRSV) accounts for a high proportion of morbidity and mortality in cattle (Stott & Taylor, 1985; Baker et al., 1986) resulting in considerable economic losses. Furthermore, human RSV (HRSV) is a major cause of serious respiratory infections including bronchiolitis and pneumonia in infants and young children: these conditions are responsible for almost 100,000 hospitalizations yearly in the USA alone (Heilman, 1990). The development of efficacious vaccines against HRSV infections has a very high priority according to the World Health Organization (World Health Organization, 1995), and has lately received much attention (Hall, 1994; McIntosh & Chanock, 1990). Respiratory syncytial virus carries two glycoproteins on its surface: the fusion protein F and the attachment protein G. The latter is an integral membrane protein and is functionally distinct from other viral attachment proteins. The focus of the present study is the small conserved hydrophobic domain (Figure 1) that is located in the ectodomain and is presumably flanked in the intact protein G by two extended mucin-like regions (Langedijk et al., 1996b). This domain contains four conserved cysteines which form two disulfide bridges. Peptides based on this domain were found to be immunodominant in protein G of both HRSV (Norrby et al., 1987; Ekerlind-Stopner et al., 1990) and BRSV (Langedijk et al., 1996b); they can be used as antigens in highly specific and sensitive immunoassays (Langedijk et al., 1996a) and have conferred protection against HRSV challenge in mice (Trudel et al., 1991). We have studied a 32-residue synthetic peptide representing the conserved central region of protein G of BRSV using two-dimensional (2D) NMR, distance geometry (DG), and restrained molecular dynamics (RMD)." citations,entry_citation,4038,192683,1,,entry citation,,98344234,,,"Alam, S. L., Volkman, B. F., Markley, J. L., and Satterlee, J. D., ""Detailed NMR Analysis of the Heme-Protein Interactions in Component IV Glycera dibranchiata Monomeric Hemoglobin-CO, J. Biomol. NMR 11, 119-133 (1998)""","Detailed NMR Analysis of the Heme-Protein Interactions in Component IV Glycera dibranchiata Monomeric Hemoglobin-CO",published,journal,J. Biomol. NMR,,11,,,,,,,,,,,,,,,,,,,,,,,119,133,1998, citations,entry_citation,4022,192469,1,,entry citation,,97161090,,,"Sethson, I., Edlund, U., Holak, T.A., Ross, A., and Johnson, B-H., ""Sequential Assignment of 1H, 13C and 15N Resonances of Human Carbonic Anhydrase I by Triple-resonance NMR Techniques and Extensive Amino Acid-Specific 15N-Labeling,"" J. Biomol. NMR 8, 417-428 (1996).","Sequential Assignment of 1H, 13C and 15N Resonances of Human Carbonic Anhydrase I by Triple-Resonance NMR Techniques and Extensive Amino Acid-Specific 15N-Labeling",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,8,4,,,,,,,,,,,,,,,,,,,,,,417,428,1996, citations,entry_citation,4023,192484,1,,entry citation,,,9325113,,,"High Resolution Solution NMR Structure of the Z Domain of Staphylococcal Protein A",published,journal,J. Mol. Biol.,,272,,,,,,,,,,,,,,,,,,,,,,,573,590,1997, citations,entry_citation,4024,192497,1,,entry citation,,96347358,,,"Dutnall, R.N., Neuhaus, D., and Rhodes, D., ""The Solution Structure of the First Zinc Finger Domain of SWI5: A Novel Extension to a Common Fold,"" Structure 4, 599-611 (1996).","The Solution Structure of the First Zinc Finger Domain of SWI5: A Novel Extension to a Common Fold",published,journal,Structure,Structure,4,5,,,,,,,,,,,,,,,,,,,,,,599,611,1996, citations,entry_citation,4027,192513,1,,entry citation,,97399849,,,"Altmann, S., Labhardt, A. M., Senn, H., and Wuthrich, K., ""Sequence-Specific 1H, 13C, and 15N assignment of the TMP-resistant dihydrofolate reductase mutant DHFR(F98Y) in the ternary complex with TMP and NADPH,"" J. Biomol. NMR 9, 445-446 (1997).","Sequence-Specific 1H, 13C, and 15N assignment of the TMP-resistant dihydrofolate reductase mutant DHFR(F98Y) in the ternary complex with TMP and NADPH",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,9,4,,,,,,,,,,,,,,,,,,,,,,445,446,1997, citations,entry_citation,4028,192534,1,,entry citation,,98062897,,,"Lee, A.L., Volkman, B.F., Rudner, D.Z., Barbash, D.A., Cline, T.W, Kanaar, R., Rio D.C., and Wemmer, D.E., ""Chemical Shift Mapping of the RNA-binding Interface to the Multiple-RBD Protein Sex-Lethal,"" Biochemistry 36, 14306-14317 (1997).","Chemical Shift Mapping of the RNA-binding Interface to the Multiple-RBD Protein Sex-Lethal",submitted,journal,Biochemistry,,36,,,,,,,,,,,,,,,,,,,,,,,14306,14317,1997, citations,entry_citation,4029,192551,1,,entry citation,,98062897,,,"Lee, A.L., Volkman, B.F., Rudner, D.Z., Barbash, D.A., Cline, T.W, Kanaar, R., Rio D.C., and Wemmer, D.E., ""Chemical Shift Mapping of the RNA-binding Interface to the Multiple-RBD Protein Sex-Lethal,"" Biochemistry 36, 14306-14317 (1997).","Chemical Shift Mapping of the RNA-binding Interface to the Multiple-RBD Protein Sex-Lethal",published,journal,Biochemistry,,36,,,,,,,,,,,,,,,,,,,,,,,14306,14317,1997, citations,entry_citation,4030,192567,1,,entry citation,,99032118,,,"Tanaka, T., Ames, J.B., Kainosho, M., Stryer, L., and Ikura, M., ""Differential isotype labeling strategy for determining the structure of myristoylated recoverin by NMR spectroscopy,"" J. Biomol NMR 11, 135-152 (1998).","Differential isotype labeling strategy for determining the structure of myristoylated recoverin by NMR spectroscopy",published,journal,J. Biomol. NMR,,11,2,,,,,,,,,,,,,,,,,,,,,,135,152,1998, citations,entry_citation,4031,192585,1,,entry citation,,,,,"Shimotakahara, S., Rios, C. B., Laity, J. H., Zimmerman, D. E., Scheraga, H. A., Montelione, G. T., ""NMR Structural Analysis of an Analog of an Intermediate Formed in the Rate-Determining Step of One Pathway in the Oxidative Folding of Bovine Pancreatic Ribonuclease A: Automated Analysis of 1H, 13C and 15N Resonance Assignments for Wild-Type and [C65S, C72S] Mutant Forms,"" Biochemistry 36, 6915-6929 (1997).","NMR Structural Analysis of an Analog of an Intermediate Formed in the Rate-Determining Step of One Pathway in the Oxidative Folding of Bovine Pancreatic Ribonuclease A: Automated Analysis of 1H, 13C and 15N Resonance Assignments for Wild-Type and [C65S, C72S] Mutant Forms.",published,journal,Biochemistry,,36,,,,,,,,,,,,,,,,,,,,,,,6915,6929,1997, citations,entry_citation,4032,192599,1,,entry citation,,,9188686,,,"NMR Structural Analysis of an Analog of an Intermediate Formed in the Rate-Determining Step of One Pathway in the Oxidative Folding of Bovine Pancreatic Ribonuclease A: Automated Analysis of 1H, 13C and 15N Resonance Assignments for Wild-Type and [C65S, C72S] Mutant Forms.",published,journal,Biochemistry,,36,,,,,,,,,,,,,,,,,,,,,,,6915,6929,1997, citations,entry_citation,4033,192613,1,,entry citation,,,,,"Sem, D., Casimiro, D., Kliewer, S., Provencal, J., Evans, R., and Wright, P., ""NMR Spectroscopic Studies of the DNA-Binding Domain of the Monomer-Binding Nuclear Orphan Receptor, Human ERR2. The Carboxy Terminal Extension to the Zinc-Finger Region is Unstructured in the Free Form of the Protein,"" J. Biol. Chem., in press (1997).","NMR Spectroscopic Studies of the DNA-Binding Domain of the Monomer-Binding Nuclear Orphan Receptor, Human ERR2. The Carboxy Terminal Extension to the Zinc-Finger Region is Unstructured in the Free Form of the Protein.",in press,journal,J. Biol. Chem.,Journal of Biological Chemistry,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4034,192626,1,,entry citation,,,,,"Sem, D., Casimiro, D., Kliewer, S., Provencal, J., Evans, R., and Wright, P., ""NMR Spectroscopic Studies of the DNA-Binding Domain of the Monomer-Binding Nuclear Orphan Receptor, Human ERR2. The Carboxy Terminal Extension to the Zinc-Finger Region is Unstructured in the Free Form of the Protein,"" J. Biol. Chem. (in press) (1997).","NMR Spectroscopic Studies of the DNA-Binding Domain of the Monomer-Binding Nuclear Orphan Receptor, Human ERR2. The Carboxy Terminal Extension to the Zinc-Finger Region is Unstructured in the Free Form of the Protein.",in press,journal,J. Biol. Chem.,Journal of Biological Chemistry,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4035,192639,1,,entry citation,,96194130,,,"Liang, H., Petros, A. M., Meadows, R. P., Yoon, H. S., Egan, D. A., Walter, K., Holzman, T. F., Robins, T., and Fesik, S. W., ""Solution Structure of the DNA-Binding Domain of a Human Papillomavirus E2 Protein: Evidence for Flexible DNA-Binding Regions,"" Biochemistry 35, 2095-2103 (1996).","Solution Structure of the DNA-Binding Domain of a Human Papillomavirus E2 Protein: Evidence for Flexible DNA-Binding Regions",published,journal,Biochemistry,,35,7,,,,,,,,,,,,,,,,,,,,,,2095,2103,1996, citations,entry_citation,4036,192655,1,,entry citation,,95001848,,,"Constantine, K.L., Colson, K.L., Wittekind, M., Friedrichs, M.S., Zein, N., Tuttle, J., Langley, D.R., Leet, J.E., Schroeder, D.R., Lam, K.S., Farmer, B.T., II, Metzler, W.J., Bruccoleri, R.E., and Mueller, L., ""Sequential 1H, 13C, and 15N, NMR Assignments and Solution Conformation of Apokedarcidin,"" Biochemistry 33, 11438-11452 (1994).","Sequential 1H, 13C, and 15N, NMR Assignments and Solution Conformation of Apokedarcidin",published,journal,Biochemistry,,33,38,,,,,,,,,,,,,,,,,,,,,,11438,11452,1994, citations,entry_citation,4037,192668,1,,entry citation,,93298762,,,"Clubb, R. T., Thanabal, V., Fejzo, J., Ferguson, S. B., Zydowsky, L., Baker, C. H., Walsh, C. T., and Wagner, G., ""Secondary Structure and Backbone Resonance Assignments of the Periplasmic Cyclophilin Type Peptidyl-Prolyl Isomerase from Escherichia Coli,"" Biochemistry 32, 6391-6401 (1993).","Secondary Structure and Backbone Resonance Assignments of the Periplasmic Cyclophilin Type Peptidyl-Prolyl Isomerase from Escherichia Coli",published,journal,Biochemistry,,32,25,,,,,,,,,,,,,,,,,,,,,,6391,6401,1993, citations,entry_citation,4762,206309,1,,entry citation,,,,,,Two-state allosteric behavior in a single domain signaling protein,published,journal,Science,,291,,,,,,,,,,,,,,,,,,,,,,,2429,2433,2001, citations,entry_citation,4039,192698,1,,entry citation,,,,,"Shao, X., Sudhof, T., and Rizo, J., ""Assignments of the 1H, 15N and 13C resonances of the calcium-free and calcium-bound forms of the first C2-domain of synaptotagmin I,""","Assignments of the 1H, 15N and 13C resonances of the calcium-free and calcium-bound forms of the first C2-domain of synaptotagmin I",submitted,journal,J. Biomol. NMR,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4040,192711,1,,entry citation,,,,,"Urbauer J. L., Adelman K., and Brody E. N., ""Main-Chain NMR Assignments for AsiA,"" J. Biomol. NMR 10, 205-206 (1997).",Main-Chain NMR Assignments for AsiA,published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,10,,,,,,,,,,,,,,,,,,,,,,,205,206,1997, citations,citation_one,4040,192712,2,,reference citation,,,8589602,,"Wishart D. S., Bigam C. G., Yao J., Abildgaard F., Dyson H. J., Oldfield E., Markley J. L., Sykes B.D., J. Biomol. NMR 6, 135-140 (1995)","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4041,192727,1,,entry citation,,,,,"Shao, X., Sudhof, T., and Rizo, J., ""Assignments of the 1H, 15N and 13C resonances of the calcium-free and calcium-bound forms of the first C2-domain of synaptotagmin I,""","Assignments of the 1H, 15N and 13C resonances of the calcium-free and calcium-bound forms of the first C2-domain of synaptotagmin I",submitted,journal,J. Biomol. NMR,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4042,192742,1,,entry citation,,95045521,,,"Bertini, I., Felli, I. C., Kastrau, D. H.W., Luchinat, C., Piccioli, M., and Viezzoli, M. S., ""Sequence-specific assignment of the 1H and 15N nuclear magnetic resonance spectra of the reduced recombinant high potential iron-sulfur protein I from Ectothiorhodospira halophila,"" European Journal of Biochemistry 225, 703-714 (1994).","Sequence-specific assignment of the 1H and 15N Nuclear Magnetic Resonance Spectra of the Reduced Recombinant High-potential Iron-sulfur Protein I from Ectothiorhodospira halophila",published,journal,Eur. J. Biochem.,European Journal of Biochemistry,225,,,,,,,,,,,,,,,,,,,,,,,703,714,1994, citations,entry_citation,4043,192759,1,,entry citation,,95257401,,,"Jablonsky, M. J., Watt, D. W., and Krishna, N. R., ""Solution Structure of an Old World-like Neurotoxin from the Venom of the New World Scorpion Centrurodies Sculpturatus Ewing,"" J. Mol. Biol. 248, 449-458 (1995).","Solution Structure of an Old World-like Neurotoxin from the Venom of the New World Scorpion Centrurodies Sculpturatus Ewing",published,journal,J. Mol. Biol.,Journal of Molecular Biology,248,,,,,,,,,,,,,,,,,,,,,,,449,458,1995, citations,entry_citation,4044,192773,1,,entry citation,,95113840,,,"Balasubramanian, S., Beger, R. D., Bennett, S. E., Mosbaugh, D. W., and Bolton, P. H., ""Secondary Structure of Uracil-DNA Glycosylase Inhibitor Protein,"" J. Biol. Chem. 270, 296-303 (1995).",Secondary Structure of Uracil-DNA Glycosylase Inhibitor Protein,published,journal,J. Biol. Chem.,,270,1,,,,,,,,,,,,,,,,,,,,,,296,303,1995, citations,entry_citation,4045,192786,1,,entry citation,,95298771,,,"Yu, L., Zhu, C-X., Tse-Dinh, Y-C., and Fesik, S. W., ""Solution Structure of the C-Terminal Single-Stranded DNA-Binding Domain of Escherichia coli Topoisomerase I,"" Biochemistry 34, 7622-7628 (1995).","Solution Structure of the C-Terminal Single-Stranded DNA-Binding Domain of Escherichia coli Topoisomerase I",published,journal,Biochemistry,Biochemistry,34,23,,,,,,,,,,,,,,,,,,,,,,7622,7628,1995, citations,entry_citation,4046,192800,1,,entry citation,,94114471,,,"Vuister, G. W., Kim, S-J., Wu, C., and Bax, A., ""NMR Evidence for Similarities between the DNA-Binding Regions of Drosophila melanogaster Heat Shock Factor and the Helix-Turn-Helix and HNF-3/forkhead Families of Transcription Factors,"" Biochemistry 33, 10-16 (1994).","NMR Evidence for Similarities between the DNA-Binding Regions of Drosophila melanogaster Heat Shock Factor and the Helix-Turn-Helix and HNF-3/forkhead Families of Transcription Factors",published,journal,,Biochemistry,33,1,,,,,,,,,,,,,,,,,,,,,,10,16,1994, citations,entry_citation,4047,192814,1,,entry citation,,95086081,,,"Vis, H., Boelens, R., Mariani, M., Stroop, R., Vorgias, C. E., Wilson, K., and Kaptein, R., '1H, 13C, 15N Resonance Assignments and Secondary Structure Analysis of the HU Protein from Bacillus stearothermophilus Using Two- and Three-Dimensional Double- and Triple-Resonance Heteronuclear Magnetic Resonance Spectroscopy,"" Biochemistry 33, 14858-14870, (1994).","1H, 13C, 15N Resonance Assignments and Secondary Structure Analysis of the HU Protein from Bacillus stearothermophilus Using Two- and Three- Dimensional Double- and Triple-Resonance Heteronuclear Magnetic Resonance Spectroscopy",published,journal,Biochemistry,Biochemistry,33,49,,,,,,,,,,,,,,,,,,,,,,14858,14870,1994, citations,entry_citation,4048,192828,1,,entry citation,,95292092,,,"Lee, W., Harvey, T. S., Yin, Y., Yau, P., Litchfield, D., and Arrowsmith, C. H., ""Solution Structure of the tetrameric minimum transforming domain of p53,"" Nat. Struct. Biol. 1, 877-890 (1994).",Solution Structure of the tetrameric minimum transforming domain of p53,published,journal,Nat. Struct. Biol.,Nature Structural Biology,1,12,,,,,,,,,,,,,,,,,,,,,,877,890,1994, citations,entry_citation,4049,192844,1,,entry citation,,94213863,,,"Hansen, A. P., Petros, A. M., Meadows, R. P., Nettesheim D. G., Mazar, A. P., Olejniczak, E. T., Xu, R. X., Pederson, T. M., Henkin, J., and Fesik, S. W., ""Solution Structure of the Amino-Terminal Fragment of Urokinase-Type Plasminogen Activator,"" Biochemistry 33, 4847-4864 (1994).","Solution Structure of the Amino-Terminal Fragment of Urokinase-Type Plasminogen Activator",published,journal,Biochemistry,Biochemistry,33,16,,,,,,,,,,,,,,,,,,,,,,4847,4864,1994, citations,entry_citation,405,192862,1,,entry citation,,,,,"King, Garry C., Coleman, Joseph E., ""Two-Dimensional 1H NMR of Gene 5 Protein Indicates That Only Two Aromatic Rings Interact Significantly with Oligodeoxynucleotide Bases,"" Biochemistry 26, 2929-2937 (1987).","Two-Dimensional 1H NMR of Gene 5 Protein Indicates That Only Two Aromatic Rings Interact Significantly with Oligodeoxynucleotide Bases",published,journal,Biochemistry,,26,,,,,,,,,,,,,,,,,,,,,,,2929,2937,1987, citations,entry_citation,4050,192875,1,,entry citation,,98121548,,,"Prantner, A. M., Volkman, B. F., Wilkens, S. J., Xia, B., and Markley, J. L., ""Assignment of 1H, 13C, 15N Signals of Reduced Clostridium Pasteurianum Rubredoxin: Oxidation State-Dependent Changes in Chemical Shifts and Relaxation Rates,"" J. Biomol. NMR 10, 411-412 (1997).","Assignment of 1H, 13C, 15N Signals of Reduced Clostridium Pasteurianum Rubredoxin: Oxidation State-Dependent Changes in Chemical Shifts and Relaxation Rates",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,10,,,,,,,,,,,,,,,,,,,,,,,411,412,1997, citations,entry_citation,4051,192890,1,,entry citation,,98121547,,,"Volkman, B. F., Prantner, A. M., Wilkens, S. J., Xia, B., and Markley, J. L., ""Assignment of 1H, 13C, 15N Signals of Oxidized Clostridium Pasteurianum Rubredoxin,"" J. Biomol. NMR 10, 409-410 (1997).","Assignment of 1H, 13C, 15N Signals of Oxidized Clostridium Pasteurianum Rubredoxin",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,10,,,,,,,,,,,,,,,,,,,,,,,409,410,1997, citations,entry_citation,4053,192924,1,,entry citation,,,,,,"Solution structures of Staphylococcal Nuclease from multidimensional, multinuclear NMR: nuclease-H124L and its ternary complex with Ca2+ and Thymidine-3'-5'-bisphosphate",published,journal,J. Biomol. NMR,,10,2,,,,,,,,,,,,,,,,,,,,,,143,164,1997, citations,entry_citation,4054,192947,1,,entry citation,,97406913,,,"Wiltscheck, R., Kammerer, R. A., Dames, S. A., Schulthess, T., Blommers, M. J.J., Engel, J., and Alexandrescu, A. T., ""Heteronuclear NMR Assignments and Secondary Structure of the Coiled Coil Trimerization Domain from Cartilage Matrix Protein in Oxidized and Reduced Forms,"" Protein Sci. 6, 1734-1745 (1997).","Heteronuclear NMR Assignments and Secondary Structure of the Coiled Coil Trimerization Domain from Cartilage Matrix Protein in Oxidized and Reduced Forms.",published,journal,Protein Sci.,Protein Science,6,8,,,,,,,,,,,,,,,,,,,,,,1734,1745,1997, citations,entry_citation,4055,192960,1,,entry citation,,97406913,,,"Wiltscheck, R., Kammerer, R. A., Dames, S. A., Schulthess, T., Blommers, M. J.J., Engel, J., and Alexandrescu, A. T., ""Heteronuclear NMR Assignments and Secondary Structure of the Coiled Coil Trimerization Domain from Cartilage Matrix Protein in Oxidized and Reduced Forms,"" Protein Sci. 6, 1734-1745 (1997).","Heteronuclear NMR Assignments and Secondary Structure of the Coiled Coil Trimerization Domain from Cartilage Matrix Protein in Oxidized and Reduced Forms.",published,journal,Protein Sci.,Protein Science,6,8,,,,,,,,,,,,,,,,,,,,,,1734,1745,1997, citations,entry_citation,4056,192976,1,,entry citation,,,,,"Osawa, M., Swindells, M. B., Tanikawa, J., Toshiyuki, T., Toshiyasu, M., Toshio, F., and Mitsuhiko, I., ""Solution Structure of Calmodulin-W-7 Complex: The Basis of Diversity in Molecular Recognition,"" J. Mol. Biol., submitted (1997).","Solution Structure of Calmodulin-W-7 Complex: The Basis of Diversity in Molecular Recognition",submitted,journal,J. Mol. Biol.,,,,,,,,,,,,,,,,,,,,,,,,,,,1998, citations,entry_citation,4057,192991,1,,entry citation,,97194052,,,"Mattinen, M-L. M., Kontteli, M., Kerovuo, J., Linder, M., Lindeberg, G., Reinikainen, T., and Drakenberg T., ""Three-Dimensional Structures of Three Engineered Cellulose-Binding Domains of Cellobiohydrolase I from Trichoderma reesei,"" Protein Sci. 6, 294-303 (1997).","Three-Dimensional Structures of Three Engineered Cellulose-Binding Domains of Cellobiohydrolase I from Trichoderma reesei",published,journal,Protein Sci.,Protein Science,6,,,,,,,,,,,,,,,,,,,,,,,294,303,1997, citations,entry_citation,4058,193004,1,,entry citation,,97194052,,,"Mattinen, M-L. M., Kontteli, M., Kerovuo, J., Linder, M., Lindeberg, G., Reinikainen, T., and Drakenberg T., ""Three-Dimensional Structures of Three Engineered Cellulose-Binding Domains of Cellobiohydrolase I from Trichoderma reesei,"" Protein Sci. 6, 294-303 (1997).","Three-Dimensional Structures of Three Engineered Cellulose-Binding Domains of Cellobiohydrolase I from Trichoderma reesei",published,journal,Protein Sci.,Protein Science,6,,,,,,,,,,,,,,,,,,,,,,,294,303,1997, citations,entry_citation,4059,193017,1,,entry citation,,97194052,,,"Mattinen, M-L. M., Kontteli, M., Kerovuo, J., Linder, M., Lindeberg, G., Reinikainen, T., and Drakenberg T., ""Three-Dimensional Structures of Three Engineered Cellulose-Binding Domains of Cellobiohydrolase I from Trichoderma reesei,"" Protein Sci. 6, 294-303 (1997).","Three-Dimensional Structures of Three Engineered Cellulose-Binding Domains of Cellobiohydrolase I from Trichoderma reesei",published,journal,Protein Sci.,Protein Science,6,,,,,,,,,,,,,,,,,,,,,,,294,303,1997, citations,entry_citation,4060,193030,1,,entry citation,,,,,,"Multinuclear Backbone NMR Resonance Assignments and the Secondary Structure of Escherichia coli Thioesterase/Protease I - A Member of a New Subclass of Lipolytic Enzymes",in press,,J. Biomol. NMR,Journal of Biomolecular NMR,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4061,193045,1,,entry citation,,96088117,,,"Jennings, P. A., Stone, M. J., and Wright, P. E., ""Overexpession of Myoglobin and Assignment of Its amide, C Alpha and C Beta Resonances,"" J. Biomol. NMR 6, 271-276 (1995).","Overexpression of Myoglobin and Assignment of Its Amide, C Alpha and C Beta Resonances",published,journal,J. Biomol. NMR,,6,,,,,,,,,,,,,,,,,,,,,,,271,276,1995, citations,entry_citation,4062,193064,1,,entry citation,,94355813,,,"Theriault, Y., Pochapsky T. C., Dalvit, C., Chiu, M., Sligar, S. G., and Wright, P. E., ""1H and 15N Resonance Assignments and Secondary Structure of the Carbon Monoxide Complex of Sperm Whale Myoglobin,"" J. Biomol. NMR 4, 491-504 (1994).","1H and 15N Resonance Assignments and Secondary Structure of the Carbon Monoxide Complex of Sperm Whale Myoglobin",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,4,,,,,,,,,,,,,,,,,,,,,,,491,504,1994, citations,entry_citation,4063,193083,1,,entry citation,,96329605,,,"Hoffman, R. C., Moy, F. J., Price, V., Richardson, J., Kaubisch, D., Frieden, E. A., Krakover, J. D., Castner, B. J., King, J., March, C. J., and Powers, R., ""Resonance Assignments for Oncostatin M, a 24-kDa Alpha-Helical Protein,"" J. Biomol. NMR 7, 273-282 (1996).","Resonance Assignments for Oncostatin M, a 24-kDa Alpha-Helical Protein",published,journal,J. Biomol. NMR,,7,,,,,,,,,,,,,,,,,,,,,,,273,282,1996, citations,entry_citation,4064,193096,1,,entry citation,,97475657,,,"Moy, F. J., Pisano, M. R., Chanda, P. K., Urbano, C., Killar, L. M., Sung, M-L., and Powers, R., ""Assignments, Secondary Structure and Dynamics of the Inhibitor- Free Catalytic Fragment of Human Fibroblast Collagenase,"" J. Biomol. NMR, 10, 9-19 (1997).","Assignments, Secondary Structure and Dynamics of the Inhibitor-Free Catalytic Fragment of Human Fibroblast Collagenase",published,journal,J. Biomol. NMR,,10,,,,,,,,,,,,,,,,,,,,,,,9,19,1997, citations,entry_citation,4065,193110,1,,entry citation,,,,,"Skalicky, J. J., Bieber, R. J., Gibney, B. R., Rabanal, F. , Dutton, L. P., and Wand, J. A., ""Sequence-Specific Resonance Assignments for a Designed Four-Alpha-Helix-Bundle Protein,"" J. Biomol. NMR 11, 227-228 (1998).","Sequence-Specific Resonance Assignments for a Designed Four-Alpha-Helix-Bundle Protein",published,journal,J. Biomol. NMR,,11,2,,,,,,,,,,,,,,,,,,,,,,227,228,1998, citations,entry_citation,4066,193124,1,,entry citation,,,,,"Xia, B., Wilkens, S.J., Westler, W.M., Markley, J.L., ""Amplification of One-Bond 1H/2H Isotope Efects on 15N Chemical Shifts in Clostridium pasteurianum Rubredoxin by Fermi-Contact Effects through Hydrogen Bonds,"" J. Am. Chem. Soc. 120, 4893-4894 (1998).","Amplification of One-Bond 1H/2H Isotope Efects on 15N Chemical Shifts in Clostridium pasteurianum Rubredoxin by Fermi-Contact Effects through Hydrogen Bonds",published,journal,J. Am. Chem. Soc.,,120,19,,,,,,,,,,,,,,,,,,,,,,4893,4894,1998, citations,citation_one,4066,193125,2,,reference citation,,,,,"Xia, B., Westler, W.M., Cheng, H., Moulis, J.-M., and Markley, J.L. J. Am. Chem. Soc. 117, 5347 (1995).",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4067,193142,1,,entry citation,,98344242,,,"Caldwell, J. E., Abildgaard, F., Ming, D., Hellekant, G., and Markley, J. L., ""Complete 1H and Partial 13C Resonance Assignments at 37 and 22 C for Brazzein, an Intensely Sweet Protein,"" J. Biomol. NMR 11, 231-232 (1998).","Complete 1H and Partial 13C Resonance Assignments at 37 and 22 C for Brazzein, an Intensely Sweet Protein",submitted,journal,J. Biomol. NMR,,11,,,,,,,,,,,,,,,,,,,,,,,231,232,1998, citations,entry_citation,4134,194271,1,,entry citation,,,,,"Alexandrescu, A. T., Jaravine, Viktor A., and Lamour, F. P., ""NMR Assignments for Denatured LysN,""",NMR Assignments for denatured LysN,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,1999, citations,entry_citation,4068,193166,1,,entry citation,,,,,"Choe, S., Dzakula, Z., Kuloglu, E. S., and Markley, J. L., ""Assignment of 1H, 13C, and 15N Signals of Turkey Ovomucoid Third Domain at pH 2.0,"" J. Biomol. NMR, in press (1998).","Assignment of 1H, 13C, and IN Signals of Turkey Ovomucoid Third Domain at pH 2.0",in press,journal,J. Biomol. NMR,,,,,,,,,,,,,,,,,,,,,,,,,,,1998, citations,entry_citation,4069,193184,1,,entry citation,,,,,"Laajoki, L. G., Le Breton, E., Shooter, G., Wallace, J. C., Francis, G. L., Carver, J. A., and Keniry, M. A., ""Secondary Structure Determination of 15N-Labelled Human Long-[Arg-3]-Insulin-Like Growth Factor-I by Multidimensional NMR Spectroscopy,"" FEBS Letters, submitted (1997).","Secondary Structure Determination of 15N-Labelled Human Long-[Arg-3]-Insulin-Like Growth Factor-I by Multidimensional NMR Spectroscopy",submitted,journal,FEBS Lett.,Federation of European Biochemical Societies Letters,,,,,,,,,,,,,,,,,,,,,,,,,,1997, citations,entry_citation,407,193199,1,,entry citation,,,,,"Carver, John A., Collins, J. Grant, ""NMR identification of a partial helical conformation for bombesin in solution,"" Eur. J. Biochem. 187, 645-650 (1990).",NMR identification of a partial helical conformation for bombesin in solution,published,journal,Eur. J. Biochem.,,187,,,,,,,,,,,,,,,,,,,,,,,645,650,1990, citations,entry_citation,4070,193214,1,,entry citation,,98344241,,,"Pellecchia, M., Guntert, P., Glockshuber, R., and Wuthrich, K., ""Sequence-Specific 1H, 15N and 13C Assignments of the 23 kDa Chaperone FimC from Escherichia coli,"" J. Biomol. NMR 11, 229-230 (1998).","Sequence-Specific 1H, 15N and 13C Assignments of the 23 kDa Chaperone FimC from Escherichia coli",published,journal,J. Biomol. NMR,,11,,,,,,,,,,,,,,,,,,,,,,,229,230,1998, citations,entry_citation,4071,193230,1,,entry citation,,,,,"Fant, F., Vranken, W. F., Martins, J. C., and Borremans F. A.M., ""1H Chemical Shift Assignments and Interproton 3JNHA Coupling Constants of Raphanus sativus Antifungal Protein 1 (Rs-AFP1), a Plant Defensin Isolated from Seeds of Radish,"" Bull. Soc. Chim. Belg. 106, 51-57 (1997).","1H Chemical Shift Assignments and Interproton 3JNHA Coupling Constants of Raphanus sativus Antifungal Protein 1 (Rs-AFP1), a Plant Defensin Isolated from Seeds of Radish",published,journal,Bull. Soc. Chim. Belg.,,106,1,,,,,,,,,,,,,,,,,,,,,,51,57,1997, citations,entry_citation,4072,193244,1,,entry citation,,98356295,,,"Pelton, J. G., Chang, K-Y., and Comolli, L.R., ""Sequence Specific 1HN, 15N, 1H Alpha, 13C Alpha, and 13C Beta Assignments for RNA-1 Modulator Protein ROM,"" J. Biomol. NMR 11, 463-464 (1998).","Sequence Specific 1HN, 15N, 1H Alpha, 13C Alpha, and 13C Beta Assignments for RNA-1 Modulator Protein ROM",published,journal,J. Biomol. NMR,,11,4,,,,,,,,,,,,,,,,,,,,,,463,464,1998, citations,citation_one,4072,193245,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, J. H., Oldfield, E., Markley, J. L., and Sykes, B. D., J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4073,193258,1,,entry citation,,98191359,,,"Xia, B., Volkman, B. F. , and Markley, J. L., ""Evidence for Oxidation-State-Dependent Conformational Changes in Human Ferredoxin from Multinuclear, Multidimensional NMR Spectroscopy,"" Biochemistry 37, 3965-3973 (1998).","Evidence for Oxidation-State-Dependent Conformational Changes in Human Ferredoxin from Multinuclear, Multidimensional NMR Spectroscopy",published,journal,Biochemistry,,37,,,,,,,,,,,,,,,,,,,,,,,3965,3973,1998, citations,citation_one,4073,193259,2,,reference citation,,,7819194,,"Xia, B., Cheng, H., Skjeldal, L., Coghlan, V. M., Vickery, L. E., and Markley, J. L., Biochemistry 34, 180-187, (1995).",Multinuclear magnetic resonance and mutagenesis studies of the histidine residues of human mitochondrial ferredoxin.,published,journal,Biochemistry,Biochemistry,34,1,,0006-2960,,,,,,,,,,,,,,,,,,,,180,187,1995,"Human mitochondrial ferredoxin is a [2Fe-2S] protein that functions to transfer electrons from NADPH-dependent ferredoxin reductase to cytochrome P450 enzymes. Two of the three histidines of human ferredoxin are strictly conserved in the sequences of all known vertebrate ferredoxins, and one of these (His56) is adjacent to Cys55, which serves as one of the ligands to the iron-sulfur cluster. All but 16 of its residues show sequence identity with those of bovine ferredoxin. It has been proposed for bovine ferredoxin that His56 hydrogen bonds with a labile sulfur and that the reduction of the iron-sulfur center is accompanied by the uptake of a proton by this histidine [Lambeth, J. D., Seybert, D. W., Lancaster, J. R., Jr., Salerno, J. C., & Kamin, H. (1982) Mol. Cell. Biochem. 45, 13-31]. In this paper, we report procedures for labeling human ferredoxin uniformly with 15N using 15NH4Cl and selectively with 13C by the incorporation of [U-13C]histidine. Most of the imidazole 1H, 13C, and 15N resonances of the three histidines have been assigned by heteronuclear two-dimensional single- and multiple-bond correlation spectroscopy. Site-directed mutagenesis was used in assigning the NMR signals from His56. The pKa values of His10 (6.5) and His62 (5.8) in oxidized human ferredoxin were found to be similar to those reported previously for the corresponding residues of bovine ferredoxin [Greenfield, N. J., Wu, X., & Jordan, F. (1989) Biochim. Biophys. Acta 995, 246-254; Miura, S., Tamita, S., & Ichikawa, Y. (1991) J. Biol. Chem. 266, 19212-19216].(ABSTRACT TRUNCATED AT 250 WORDS)" citations,citation_two,4073,193260,3,,reference citation,,,8755728,,"Xia B., Cheng H., Bandarian V., Reed G. H., & Markley J. L., Biochemistry 35, 9488-9495,(1996).","Human ferredoxin: overproduction in Escherichia coli, reconstitution in vitro, and spectroscopic studies of iron-sulfur cluster ligand cysteine-to-serine mutants.",published,journal,Biochemistry,Biochemistry,35,29,,0006-2960,,,,,,,,,,,,,,,,,,,,9488,9495,1996,"Human ferredoxin, the human equivalent of bovine adrenodoxin, is a small iron-sulfur protein with one [2Fe-2S] cluster. It functions, as do other vertebrate ferredoxins, to transfer electrons during the processes of steroid hormone synthesis. A DNA fragment encoding the mature form of human ferredoxin was cloned into an expression vector under control of the T7 RNA polymerase/promoter system. The protein was overproduced in Escherichia coli, and the [2Fe-2S] cluster was incorporated into the protein by in vitro reconstitution. The overall yield was approximately 30 mg of purified, reconstituted ferredoxin per liter of culture. Four of the five cysteines in human ferredoxin are coordinated to the iron-sulfur cluster. First, the non-ligand cysteine (cysteine-95) was mutated to alanine, and then double mutants were created in which each of the other four cysteines (at positions 46, 52, 55, and 92) were mutated individually to serine. The wild-type ferredoxin and each of the five mutant proteins were studied by UV-visible spectroscopy and electron paramagnetic resonance spectroscopy. The EPR gav values of all five mutants were very similar to that of wild-type human ferredoxin. In the reduced state, three of the cysteine-to-serine mutants exhibited axial EPR spectra similar to that of wild-type, but one of the double mutants (C52S/C95A) exhibited a rhombic EPR spectrum. The UV-visible spectroscopic properties of the wild-type and the C95A mutant ferredoxins were identical, but those of the other cysteine-to-serine mutant proteins of human ferredoxin were quite different from those of the wild-type protein and each other. These results, along with those from cysteine-to-serine mutations in other ferredoxins, provide the basis for a more comprehensive theoretical and practical understanding of the features important to the ligation of [2Fe-2S] clusters, although they do not yet permit determination of which two cysteines ligate Fe(II) and which ligate Fe(III) in the reduced protein." citations,entry_citation,4074,193282,1,,entry citation,,98191359,,,"Xia, B., Volkman, B. F. , and Markley, J. L., ""Evidence for Redidation-State-Dependent Conformational Changes in Human Ferredoxin from Multinuclear, Multidimensional NMR Spectroscopy,"" Biochemistry 37, 3965-3973 (1998).","Evidence for Redidation-State-Dependent Conformational Changes in Human Ferredoxin from Multinuclear, Multidimensional NMR Spectroscopy",published,journal,Biochemistry,,37,,,,,,,,,,,,,,,,,,,,,,,3965,3973,1998, citations,citation_one,4074,193283,2,,reference citation,,,7819194,,"Xia, B., Cheng, H., Skjeldal, L., Coghlan, V. M., Vickery, L. E., and Markley, J. L., Biochemistry 34, 180-187, (1995).",Multinuclear magnetic resonance and mutagenesis studies of the histidine residues of human mitochondrial ferredoxin.,published,journal,Biochemistry,Biochemistry,34,1,,0006-2960,,,,,,,,,,,,,,,,,,,,180,187,1995,"Human mitochondrial ferredoxin is a [2Fe-2S] protein that functions to transfer electrons from NADPH-dependent ferredoxin reductase to cytochrome P450 enzymes. Two of the three histidines of human ferredoxin are strictly conserved in the sequences of all known vertebrate ferredoxins, and one of these (His56) is adjacent to Cys55, which serves as one of the ligands to the iron-sulfur cluster. All but 16 of its residues show sequence identity with those of bovine ferredoxin. It has been proposed for bovine ferredoxin that His56 hydrogen bonds with a labile sulfur and that the reduction of the iron-sulfur center is accompanied by the uptake of a proton by this histidine [Lambeth, J. D., Seybert, D. W., Lancaster, J. R., Jr., Salerno, J. C., & Kamin, H. (1982) Mol. Cell. Biochem. 45, 13-31]. In this paper, we report procedures for labeling human ferredoxin uniformly with 15N using 15NH4Cl and selectively with 13C by the incorporation of [U-13C]histidine. Most of the imidazole 1H, 13C, and 15N resonances of the three histidines have been assigned by heteronuclear two-dimensional single- and multiple-bond correlation spectroscopy. Site-directed mutagenesis was used in assigning the NMR signals from His56. The pKa values of His10 (6.5) and His62 (5.8) in oxidized human ferredoxin were found to be similar to those reported previously for the corresponding residues of bovine ferredoxin [Greenfield, N. J., Wu, X., & Jordan, F. (1989) Biochim. Biophys. Acta 995, 246-254; Miura, S., Tamita, S., & Ichikawa, Y. (1991) J. Biol. Chem. 266, 19212-19216].(ABSTRACT TRUNCATED AT 250 WORDS)" citations,citation_two,4074,193284,3,,reference citation,,,8755728,,"Xia B., Cheng H., Bandarian V., Reed G. H., & Markley J. L., Biochemistry 35, 9488-9495,(1996).","Human ferredoxin: overproduction in Escherichia coli, reconstitution in vitro, and spectroscopic studies of iron-sulfur cluster ligand cysteine-to-serine mutants.",published,journal,Biochemistry,Biochemistry,35,29,,0006-2960,,,,,,,,,,,,,,,,,,,,9488,9495,1996,"Human ferredoxin, the human equivalent of bovine adrenodoxin, is a small iron-sulfur protein with one [2Fe-2S] cluster. It functions, as do other vertebrate ferredoxins, to transfer electrons during the processes of steroid hormone synthesis. A DNA fragment encoding the mature form of human ferredoxin was cloned into an expression vector under control of the T7 RNA polymerase/promoter system. The protein was overproduced in Escherichia coli, and the [2Fe-2S] cluster was incorporated into the protein by in vitro reconstitution. The overall yield was approximately 30 mg of purified, reconstituted ferredoxin per liter of culture. Four of the five cysteines in human ferredoxin are coordinated to the iron-sulfur cluster. First, the non-ligand cysteine (cysteine-95) was mutated to alanine, and then double mutants were created in which each of the other four cysteines (at positions 46, 52, 55, and 92) were mutated individually to serine. The wild-type ferredoxin and each of the five mutant proteins were studied by UV-visible spectroscopy and electron paramagnetic resonance spectroscopy. The EPR gav values of all five mutants were very similar to that of wild-type human ferredoxin. In the reduced state, three of the cysteine-to-serine mutants exhibited axial EPR spectra similar to that of wild-type, but one of the double mutants (C52S/C95A) exhibited a rhombic EPR spectrum. The UV-visible spectroscopic properties of the wild-type and the C95A mutant ferredoxins were identical, but those of the other cysteine-to-serine mutant proteins of human ferredoxin were quite different from those of the wild-type protein and each other. These results, along with those from cysteine-to-serine mutations in other ferredoxins, provide the basis for a more comprehensive theoretical and practical understanding of the features important to the ligation of [2Fe-2S] clusters, although they do not yet permit determination of which two cysteines ligate Fe(II) and which ligate Fe(III) in the reduced protein." citations,citation_three,4074,193285,4,,reference citation,,,,,"Chylla, R. A. & Markley, J. L. J. Magn. Reson. (Series B) 102, 148-154, (1993)",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4075,193306,1,,entry citation,,98344243,,,"Weigelt, J., Miles, C. S., Dixon, N. E., and Otting, G., ""Backbone NMR Assignments and Secondary Structure of the N Terminal Domain of DnaB Helicase from E. coli,"" J. Biomol. NMR 11, 233-234 (1998).","Backbone NMR Assignments and Secondary Structure of the N Terminal Domain of DnaB Helicase from E. coli",published,journal,J. Biomol. NMR,,11,,,,,,,,,,,,,,,,,,,,,,,233,234,1998, citations,citation_one,4075,193307,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, J. H., Oldfield, E., Markley, J. L., and Sykes, B. D., J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4076,193320,1,,entry citation,,98356289,,,"Pham, T-N., and Koide, S., ""NMR Studies of Borrelia burgdorferi OspA, a 28 KDa Protein Containing a Single-Layer Beta-sheet,"" J. Biomol. NMR 11, 407-414 (1998)","NMR Studies of Borrelia burgdorferi OspA, a 28 kDa Protein Containing a Single-Layer Beta-sheet",published,journal,J. Biomol. NMR,,11,,,,,,,,,,,,,,,,,,,,,,,407,414,1998, citations,entry_citation,4078,193333,1,,entry citation,,96202132,,,"Jerala, R., Almeida, P. F.F., Ye, Q., Biltonen, R. L., and Rule, G. S, ""1H, 15N and 13C Resonance Assignments and Secondary Structure of Group II Phospholipase A2 from Agkistrodon piscivorus piscivorus: Presence of an Amino-Terminal Helix in Solution,"" J. Biomol. NMR 7, 107-120 , (1996).","1H, 15N and 13C Resonance Assignments and Secondary Structure of Group II Phospholipase A2 from Agkistrodon piscivorus piscivorus: Presence of an Amino-Terminal Helix in Solution",published,journal,J. Biomol. NMR,,7,,,,,,,,,,,,,,,,,,,,,,,107,120,1996, citations,entry_citation,4079,193347,1,,entry citation,,,,,"Hardman, C. H., Broadhurst, R. W., Raine, A. R.C., Grasser , K. D., Thomas, J. O.,and Laue, E. D., ""Structure of the A-Domain of HMG1 and Its Interaction with DNA As Studied by Heteronuclear Three- and Four-Dimensional NMR Spectroscopy,"" Biochemistry 34, 16596-16607 (1995).","Structure of the A-Domain of HMG1 and Its Interaction with DNA As Studied by Heteronuclear Three- and Four-Dimensional NMR Spectroscopy",published,journal,Biochemistry,,34,51,,,,,,,,,,,,,,,,,,,,,,16596,16607,1995, citations,entry_citation,408,193363,1,,entry citation,,,,,"Martins, Jose C., Zhang, Weiguo, Tartar, Andre, Lazdunski, Michel, Borremans, Frans A.M., ""Solution conformation of leiurotoxin I (scyllatoxin) by 1H nuclear magnetic resonance Resonance assignment and secondary structure,"" FEBS Lett. 260 (2), 249-253 (1990).","Solution conformation of leiurotoxin I (scyllatoxin) by 1H nuclear magnetic resonance Resonance assignment and secondary structure",published,journal,FEBS Lett.,,260,2,,,,,,,,,,,,,,,,,,,,,,249,253,1990, citations,entry_citation,4470,201273,1,,entry citation,,20577274,,,,"Solution Structure of ThiS and Implications for the Evolutionary Roots of Ubiquitin",published,journal,Nat. Struct. Biol.,Nature Structural Biology,8,,,,,,,,,,,,,,,,,,,,,,,47,51,2001, citations,entry_citation,4080,193377,1,,entry citation,,,,,"Slupsky, C. M. and Sykes, B. D., ""NMR Solution Structure of Calcium-Saturated Skeletal Muscle Troponin C,"" Biochemistry 34, 15953-15964 (1995).",NMR Solution Structure of Calcium-Saturated Skeletal Muscle Troponin C,published,journal,Biochemistry,,34,,,,,,,,,,,,,,,,,,,,,,,14953,15964,1995, citations,entry_citation,4081,193390,1,,entry citation,,98118493,,,"Werner, K., Gsell, B., Labhardt, A. M., Wipf, B., and Senn, H., ""The Three-dimensional High Resolution Structure of Human Interferon alpha-2a Determined by Hetero-nuclear NMR Spectroscopy in Solution,"" J. Mol. Biol. 274, 661-675 (1997).","The Three-dimensional High Resolution Structure of Human Interferon alpha-2a Determined by Hetero-nuclear NMR Spectroscopy in Solution",published,journal,J. Mol. Biol.,,274,,,,,,,,,,,,,,,,,,,,,,,661,675,1997, citations,citation_one,4081,193391,2,,reference citation,,,9417943,,"J. Mol. Biol. , vol. 274(4), 661-675""",The three-dimensional high resolution structure of human interferon alpha-2a determined by heteronuclear NMR spectroscopy in solution.,published,journal,J. Mol. Biol.,Journal of molecular biology,274,4,,0022-2836,,,,,,,,,,,,,,,,,,,,661,675,1997,"The solution structure of recombinant human interferon alpha-2a (Roferon-A) has been determined by multidimensional heteronuclear NMR spectroscopy. The calculations using simulated annealing produced a family of 24 convergent structures which satisfy the experimental restraints comprising 1541 NOE-derived inter-proton distances, 187 dihedral restraints, 66 pairs of hydrogen bond restraints, and six upper and lower limits for two disulfide bridges. The fractional labeling of methyl groups allowed their direct and unambiguous stereospecific assignment which proved to be essential for obtaining a high resolution of the structures. A best fit superposition of residues 10 to 47, 50 to 101 and 111 to 157 gives an rms deviation of 0.62 A for the backbone heavy atoms and 1.39 A for all heavy atoms of these segments. The dominant feature of the structure is a cluster of five alpha-helices, four of which are arranged to form a left-handed helix bundle with an up-up-down-down topology and two over-hand connections. The interpretation of heteronuclear 15N-1H NOE data shows the co-existence of flexible regions within an otherwise rigid framework of the protein. Four stretches of pronounced flexibility can be located: Cys1-Ser8, Gly44-Ala50, Ile100-Lys112, and Ser160-Glu165. Among the structurally related four-helical bundle cytokines, the structure of IFN alpha-2a is most similar to that of human interferon alpha-2b and murine interferon-beta. From this structural information and mutagenesis data, areas on the surface of the protein are identified which seem to be important in receptor interactions." citations,citation_two,4081,193392,3,,reference citation,,,8589602,,"J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4082,193408,1,,entry citation,,,,,"Metzler, W. J., Constantine, K. L., Friedrichs, M. S., Bell, A. J., Ernst, E. G., Lavoie, T. S., and Mueller, L., ""Characterization of the Three-Dimensional Solution Structure of Human Profilin: 1H, 13C, and 15N Assignments and Global Folding Pattern,"" Biochemistry 32, 13818-13829 (1993).","Characterization of the Three-Dimensional Solution Structure of Human Profilin: 1H, 13C, and 15N Assignments and Global Folding Pattern",published,journal,Biochemistry,,32,,,,,,,,,,,,,,,,,,,,,,,13818,13829,1993, citations,entry_citation,4083,193426,1,,entry citation,,,,,"Moy, F. L., Lowry, D. F., Matsumura, P., Dahlquist, F. W., Krywko, J. E., and Domaille, P. J., ""Assignments, Secondary Structure, Global Fold, and Dynamics of Chemotaxis Y Protein Using Three- and Four-Dimensional Heteronuclear (13C, 15N) NMR Spectroscopy,"" Biochemistry 33, 10731-10742 (1994).","Assignments, Secondary Structure, Global Fold, and Dynamics of Chemotaxis Y Protein Using Three- and Four-Dimensional Heteronuclear (13C, 15N) NMR Spectroscopy",published,journal,Biochemistry,,33,35,,,,,,,,,,,,,,,,,,,,,,10731,10742,1994, citations,entry_citation,4084,193443,1,,entry citation,,,,,"Garrett, D. S., Lodi, P. J., Shamoo, Y., Williams, K. R., Clore, G. M., and Gronenborn, A. M., ""Determination of the Secondary Structure and Folding Topology of an RNA Binding Domain of Mammalian nhRNP A1 Protein Using Three-Dimensional Heteronuclear Magnetic Resonance Spectroscopy,"" Biochemistry 33, 2852-2858, (1994).","Determination of the Secondary Structure and Folding Topology of an RNA Binding Domain of Mammalian nhRNP A1 Protein Using Three-Dimensional Heteronuclear Magnetic Resonance Spectroscopy",published,journal,Biochemistry,,33,10,,,,,,,,,,,,,,,,,,,,,,2852,2858,1994, citations,entry_citation,4085,193460,1,,entry citation,,,7524663,,"Lee, A. L., Kannar, R., Rio, D. C., and Wemmer, D. E., ""Resonance Assignments and Solution Structure of the Second RNA-Binding Domain of Sex-lethal Determined by Multidimensional Heteronuclear Magnetic Resonance,"" Biochemistry 33, 13775-13786 (1994).","Resonance Assignments and Solution Structure of the Second RNA-Binding Domain of Sex-lethal Determined by Multidimensional Heteronuclear Magnetic Resonance",published,journal,Biochemistry,,33,46,,,,,,,,,,,,,,,,,,,,,,13775,13786,1994, citations,entry_citation,4086,193476,1,,entry citation,,,8755727,,"Tevlev, A., Byeion, I. L., Selby, T., Ericson, K., Kim, H-J., Kraynov, V., and Tsai M-D., ""Tumor Suppressor p16ink4a: Structural Characterization of Wild-Type and Mutant Proteins by NMR and Circular Dichroism,"" Biochemistry 35, 9475-9487 (1996).","Tumor Suppressor p16ink4a: Structural Characterization of Wild-Type and Mutant Proteins by NMR and Circular Dichroism",published,journal,Biochemistry,,35,29,,,,,,,,,,,,,,,,,,,,,,9475,9487,1996, citations,entry_citation,4087,193490,1,,entry citation,,20056031,,,,"Structural Correlates for Enhanced Stability in the E2 DNA-Binding Domain from Bovine Papillomavirus",published,journal,Biochemistry,Biochemistry,38,,,,,,,,,,,,,,,,,,,,,,,16115,16124,1999, citations,citation_one,4087,193491,2,,reference citation,,,9691287,,"Veeraraghavan, S.; Mello, C. C.; Lee, K. M.; Androphy, E. J. and Baleja, J. D. ""1H, 15N, and 13C NMR resonance assignments for the DNA-binding domain of the BPV-1 E2 protein"". J. Biomol. NMR, 11, 457-458 (1998).","1H, 15N, and 13C NMR resonance assignments for the DNA-binding domain of the BPV-1 E2 protein.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,11,4,,0925-2738,,,,,,,,,,,,,,,,,,,,457,458,1998, citations,entry_citation,4088,193506,1,,entry citation,,,9541394,,,"Solution Structure of Compstatin, a Potent Complement Inhibitor",published,journal,Protein Sci.,,7,,,,,,,,,,,,,,,,,,,,,,,619,627,1998, citations,entry_citation,4089,193520,1,,entry citation,,98332750,,,"DARDEL, F., RAGUSA, S., LAZENNEC, C., BLANQUET, S., and MEINNEL, T., ""Solution Structure of Nickel-peptide Deformylase,"" J. Mol. Biol. 280, 501-513 (1998).",Solution Structure of Nickel-peptide Deformylase,published,journal,J. Mol. Biol.,,280,,,,,,,,,,,,,,,,,,,,,,,501,513,1998, citations,entry_citation,4090,193536,1,,entry citation,,98035037,,,,"Solution structure of the I gamma subdomain of the Mu end DNA-binding domain of phage Mu transposase",published,journal,J. Mol. Biol.,,273,,,,,,,,,,,,,,,,,,,,,,,19,25,1997, citations,entry_citation,4091,193550,1,,entry citation,,,,,"Moy, F. J., Seddon, A. P., Campbell, E. B., Bohlen, P., and Powers, R., ""1H, 15N, 13C, and 13CO Assignments and Secondary Structure Determination of Basic Fibroblast Growth Factor using 3D Heteronuclear NMR Spectroscopy,"" J. Biomol. NMR 6, 245-254 (1995).","1H, 15N, 13C, and 13CO Assignments and Secondary Structure Determination of Basic Fibroblast Growth Factor using 3D Heteronuclear NMR Spectroscopy",published,journal,J. Biomol. NMR,,6,,,,,,,,,,,,,,,,,,,,,,,245,254,1995, citations,entry_citation,4092,193564,1,,entry citation,,99052119,,,"Huang, X., Speck, N. A., and Bushweller, J. H., ""Complete Heteronuclear NMR Resonance Assignments and Secondary Structure of Core Binding Factor b (1-141),"" J. Biomol. NMR 12, 459-460 (1998).","Complete Heteronuclear NMR Resonance Assignments and Secondary Structure of Core Binding Factor b (1-141)",published,journal,J. Biomol. NMR,,12,3,,,,,,,,,,,,,,,,,,,,,,459,460,1998, citations,entry_citation,4093,193577,1,,entry citation,,92046051,,,"Powers, R., Clore, M. G., Bax, A., Garrett, D. S., Stahl, S. J., Wingfield, P. T., and Gronenborn A. M., ""Secondary Structure of the Ribonuclease H Domain of the Human Immunodeficiency Virus Reverse Transcriptase in Solution Using Three-Dimensional Double and Triple Resonance Heteronuclear Magnetic Resonance Spectroscopy,"" J. Biomol. NMR, 221, 1081-1090 (1991).","Secondary Structure of the Ribonuclease H Domain of the Human Immunodeficiency Virus Reverse Transcriptase in Solution Using Three-Dimensional Double and Triple Resonance Heteronuclear Magnetic Resonance Spectroscopy",published,journal,J. Biomol. NMR,,221,,,,,,,,,,,,,,,,,,,,,,,1081,1090,1991, citations,entry_citation,4094,193590,1,,entry citation,,92232741,,,"Powers, R., Garrett, D. S., March, C. J., Frieden, E. A., Gronenborn A. M., and Clore G. M., ""1H, 15N, and 13CO Assignments of Human Interleukin-4 Using Three Dimensional Double- and Triple-Resonance Heteronuclear Magnetic Resonance Spectroscopy,"" Biochemistry 31, 4334-4346 (1992).","1H, 15N, and 13CO Assignments of Human Interleukin-4 Using Three Dimensional Double- and Triple-Resonance Heteronuclear Magnetic Resonance Spectroscopy",published,journal,Biochemistry,,31,,,,,,,,,,,,,,,,,,,,,,,4334,4346,1992, citations,entry_citation,4095,193604,1,,entry citation,,97449147,,,"Manival, X., Yang, Y., Strub, M-P., Kochoyan, M., Steinmetz, M., and Aymerich, S., ""From Genetic to Structural Characterization of a New Class of RNA-Binding Domain Within the SacY/BglG family of Antiterminator,"" EMBO J. 16, 5019-5029 (1997).","From Genetic to Structural Characterization of a New Class of RNA-Binding Domain Within the SacY/BglG family of Antiterminator",published,journal,EMBO J.,,16,,,,,,,,,,,,,,,,,,,,,,,5019,5029,1997, citations,entry_citation,4097,193617,1,,entry citation,,99006568,,,"Kern, G., Handel, T., and Marqusee, S. ""Characterization of a Folding Intermediate from HIV-1 Ribonuclease H,"" Protein Sci. 7, 2164-2174 (1998).",Characterization of a Folding Intermediate from HIV-1 Ribonuclease H,published,journal,Protein Sci.,,7,,,,,,,,,,,,,,,,,,,,,,,2164,2174,1998, citations,citation_one,4097,193618,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,citation_two,4097,193619,3,,reference citation,,,1719214,,"Assignment for a mutant RNase H from HIV-1 strain HXB2 is available Powers et al. 1991, J. Mol. Biol. 221 1081-90",Secondary structure of the ribonuclease H domain of the human immunodeficiency virus reverse transcriptase in solution using three-dimensional double and triple resonance heteronuclear magnetic resonance spectroscopy.,published,journal,J. Mol. Biol.,Journal of molecular biology,221,4,,0022-2836,,,,,,,,,,,,,,,,,,,,1081,1090,1991,"The solution structure of the ribonuclease H domain of HIV-1 reverse transcriptase has been investigated by three-dimensional double and triple resonance heteronuclear magnetic resonance spectroscopy. The domain studied has 138 residues and comprises residues 427 to 560 of the 66 kDa reverse transcriptase with an additional four residues at the N terminus. Initial studies on the wild-type protein were hindered by severe differential line broadening, presumably due to conformational averaging. Mutation of the single tryptophan residue located in a loop at position 113 (position 535 in the reverse transcriptase sequence) to an alanine resulted in much improved spectral properties with no apparent change in structure. 1H, 15N and 13C backbone resonances were assigned sequentially using a range of three-dimensional double and triple resonance heteronuclear experiments on samples of uniformly (greater than 95%) 15N and 15N/13C-labeled protein, and the secondary structure was elucidated from a qualitative analysis of data derived from three-dimensional 15N- and 13C-edited nuclear Overhauser enhancement spectra. The secondary structure comprises three alpha-helices and five strands arranged in a mixed parallel/antiparallel beta-sheet with a +1, +1, -3x, -1x topology. The C-terminal region from residue 114 onwards appears to be conformationally disordered in solution as evidenced by an almost complete absence of sequential and medium range nuclear Overhauser effects." citations,entry_citation,4098,193635,1,,entry citation,,98399498,,,"Wang, H., He, Y., Hsu, K.T., Magliocca, J.F., Storch, J., and Stark, R. E., ""1H, 15N and 13C Resonance Assignments and Secondary Structure of Apo Liver Fatty Acid-Binding Protein,"" J. Biomol. NMR 12, 197-199 (1998).","1H, 15N and 13C Resonance Assignments and Secondary Structure of Apo Liver Fatty Acid-Binding Protein",published,journal,J. Biomol. NMR,,12,,,,,,,,,,,,,,,,,,,,,,,197,199,1998, citations,citation_one,4098,193636,2,,reference citation,,,,,"Johnson, B. A. and Blevins, R. A. (1994) J. Biomol. NMR 4, 603-614",,,,J. Biomol. NMR,,4,,,,,,,,,,,,,,,,,,,,,,,603,614,1994, citations,entry_citation,4104,193774,1,,entry citation,,,,,"Fernandez, C., Szyperski, T., Ono, A., Iwai, H., Tate, S., Kainosho, M. and Wuthrich, K., ""NMR with 13C,15N-doubly-labeled DNA: the Antennapedia Homeodomain Complex with a 14mer DNA Duplex,"" J. Biomol. NMR, in press (1998).","NMR with 13C,15N-doubly-labeled DNA: the Antennapedia Homeodomain Complex with a 14mer DNA Duplex",in press,journal,J. Biomol. NMR,,,,,,,,,,,,,,,,,,,,,,,,,,,1998, citations,entry_citation,4105,193791,1,,entry citation,,98153156,,,"Drohat, A. C., Baldisseri, D. M., Rustandi, R. R., and Weber, D. J., ""Solution Structure of Calcium-Bound S100B(Beta Beta) as Determined by Nuclear Magnetic Resonance Spectroscopy,"" Biochemistry 37, 1951-1960 (1998).","Solution Structure of Calcium-Bound S100B(Beta Beta) as Determined by Nuclear Magnetic Resonance Spectroscopy",published,journal,Biochemistry,,37,9,,,,,,,,,,,,,,,,,,,,,,1951,1960,1998, citations,entry_citation,4106,193807,1,,entry citation,,97207064,,,,"Solution Structure of the 30 Kda N-terminal Domain of Enzyme I of the Escherichia coli Phosphoenolpyruvate:Sugar Phosphotransferase System by Multidimensional NMR",published,journal,Biochemistry,,36,9,,,,,,,,,,,,,,,,,,,,,,2517,2530,1997, citations,citation_two,4098,193637,3,,reference citation,,,8520220,,"Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G. Pfeifer, J. and Bax, A (1995) J. Biomol. NMR 6, 277-293.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,citation_three,4098,193638,4,,reference citation,,,8574703,,"Zimmerman, D. E. and Montelione, G. T. (1995) Curr. Opin. Struct. Biol. 5, 664-673.",Automated analysis of nuclear magnetic resonance assignments for proteins.,published,journal,Curr. Opin. Struct. Biol.,Current opinion in structural biology,5,5,,0959-440X,,,,,,,,,,,,,,,,,,,,664,673,1995,"Recent developments in protein NMR technology provide spectral data that are highly amendable to analysis by computer software systems. Automated methods of analysis use constraint satisfaction, pseudoenergy minimization, directed search, neural net, simulated annealing, and/or genetic algorithms to establish sequential links and sequence-specific assignments. The most advanced systems provide automated analysis of complete backbone and extensive side-chain resonance assignments for proteins of 50-150 amino acids." citations,citation_four,4098,193639,5,,reference citation,,,,,"Garrett, D. S., Powers, R., Gronenborn, A. M. and Clore, G. M. (1991) J. Mag. Reson. 95, 214-220.",,,,J. Mag. Reson.,,95,,,,,,,,,,,,,,,,,,,,,,,214,220,1991, citations,citation_NMR_Pulse_Sequence_Reference,4098,193640,6,,reference citation,,,7812156,,"Grzesiek, S. and Bax, A. (1992) J. Am. Chem. Soc. 114, 6291-6293. Wittekind, M. and Mueller, L. (1993) J. Magn. Reson. Ser. B, 101, 201-205. Muhandiram, D.R. and Kay, L.E. (1994) J. Magn. Reson. Ser. B, 103, 203-216. Kay, L.E., Ikura, M., Tschudin, R. and Bax, A. (1990) J. Magn. Reson. 89, 496-514. Kay, L.E. (1993) J. Am. Chem. Soc. 115, 2055-2057. Logan, T.M., Olejniczak, E.T., Xu, R.X. and Fesik, S. (1993) J. Biomol. NMR 3, 225-231. Grzesiek, S. and Bax, A. (1993) J. Biomol. NMR 3, 185-204. Bax, A., Clore, G.M., and Gronenborn, A.M. (1990) J. Magn. Reson. 88, 425-431. Kay, L.E., Keifer, P. and Saarinen, T. (1992) J. Am. Chem. Soc. 114, 10663-10665. Kay, L.E., Marion, D. and Bax, A. (1989) J. Magn. Reson. 84, 72-84. Zhang, O., Kay, L.E., Olivier, J.P. and Forman-Kay, J.D. (1994) J. Biomol. NMR 4, 845-858.",Backbone 1H and 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,4,6,,0925-2738,,,,,,,,,,,,,,,,,,,,845,858,1994,"The backbone 1H and 15N resonances of the N-terminal SH3 domain of the Drosophila signaling adapter protein, drk, have been assigned. This domain is in slow exchange on the NMR timescale between folded and predominantly unfolded states. Data were collected on both states simultaneously, on samples of the SH3 in near physiological buffer exhibiting an approximately 1:1 ratio of the two states. NMR methods which exploit the chemical shift dispersion of the 15N resonances of unfolded states and pulsed field gradient water suppression approaches for avoiding saturation and dephasing of amide protons which rapidly exchange with solvent were utilized for the assignment." citations,entry_citation,4099,193668,1,,entry citation,,,,,"Rustandi, R. R., Drohat, A. C., Baldisseri, D. M., Wilder, P. T., and Weber, D. J., ""The Ca2+-Dependent Interaction of S100B(bb)with a Peptide Derived from p53,"" Biochemistry, 37, 1951-1960 (1998).",The Ca2+-Dependent Interaction of S100B(bb)with a Peptide Derived from p53,published,journal,Biochemistry,,37,,,,,,,,,,,,,,,,,,,,,,,1951,1960,1998, citations,entry_citation,41,193689,1,,entry citation,,,,,"Bach, II, Alvin C., Selsted, Michael E., Pardi, Arthur, ""Two-Dimensional NMR Studies of the Antimicrobial Peptide NP-5,"" Biochemistry 26, 4389-4397 (1987).",Two-Dimensional NMR Studies of the Antimicrobial Peptide NP-5,published,journal,Biochemistry,,26,,,,,,,,,,,,,,,,,,,,,,,4389,4397,1987, citations,entry_citation,410,193702,1,,entry citation,,,,,"Stassinopoulou, Chariclia I., Wagner, Gerhard, Wuthrich, Kurt, ""Two-dimensional 1H NMR spectroscopy of two chemically modified analogs of the basic pancreatic trypsin inhibitor Sequence-specific resonance assignments and sequence location of conformation changes relative to the native protein,"" Eur. J. Biochem. 145, 423-430 (1984).","Two-dimensional 1H NMR spectroscopy of two chemically modified analogs of the basic pancreatic trypsin inhibitor Sequence-specific resonance assignments and sequence location of conformation changes relative to the native protein",published,journal,Eur. J. Biochem.,,145,,,,,,,,,,,,,,,,,,,,,,,423,430,1984, citations,entry_citation,4100,193715,1,,entry citation,,98356293,,,"Yuan, Y-C., Whitson, R. H., Itakura, K., and Chen, Y., ""Resonance Assignments of the Mrf-2 DNA-binding Domain,"" J. Biomol. NMR 11, 459-460 (1998).",Resonance Assignments of the Mrf-2 DNA-binding Domain,published,journal,J. Biomol. NMR,,11,4,,,,,,,,,,,,,,,,,,,,,,459,460,1998, citations,entry_citation,4101,193728,1,,entry citation,,98046750,,,"Prompers, J., Groenewegen, A., van Schaik, R. C., Pepermans, H. A.M., and Hilbers, C. W., ""1H, 13C, and 15N Resonance Assignments of Fusarium Solani Pisi Cutinase and Preliminary Features of the Structure in Solution,"" Protein Sci. 6, 2375-2384 (1997).","1H, 13C, and 15N Resonance Assignments of Fusarium Solani Pisi Cutinase and Preliminary Features of the Structure in Solution",published,journal,Protein Sci.,,6,11,,,,,,,,,,,,,,,,,,,,,,2374,2384,1997, citations,entry_citation,4102,193739,1,,entry citation,,98399499,,,"Scrofani, S. D.B., Wright, P. E., and Dyson, J. H., ""1H, 13C and 15N NMR Backbone Assignments of 25.5 kDa Metallo-b-lactamase from Bacteroides fragilis,"" J. Biomol. NMR 12, 201-202 (1998).","1H, 13C and 15N NMR Backbone Assignments of 25.5 kDa Metallo-b-lactamase from Bacteroides fragilis",published,journal,J. Biomol. NMR,,12,1,,,,,,,,,,,,,,,,,,,,,,201,202,1998, citations,entry_citation,4103,193758,1,,entry citation,,,,,"Fernandez, C., Szyperski, T., Ono, A., Iwai, H., Tate, S., Kainosho, M. and Wuthrich, K., ""NMR with 13C,15N-doubly-labeled DNA: the Antennapedia Homeodomain Complex with a 14mer DNA Duplex,"" J. Biomol. NMR, in press (1998).","NMR with 13C,15N-doubly-labeled DNA: the Antennapedia Homeodomain Complex with a 14mer DNA Duplex",in press,journal,J. Biomol. NMR,,,,,,,,,,,,,,,,,,,,,,,,,,,1998, citations,citation_one,4106,193808,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4107,193829,1,,entry citation,,98356294,,,"Alexandrescu, A. T., and Rathgeb-Szabo, K., ""NMR Assignments for Acid-Denatured Cold Shock Protein A,"" J. Biomol. NMR 11, 461-462 (1998).",NMR Assignments for Acid-Denatured Cold Shock Protein A,published,journal,J. Biomol. NMR,,11,4,,,,,,,,,,,,,,,,,,,,,,461,462,1998, citations,citation_one,4107,193830,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., Sykes, B. D., ""1H, 13C and 15N Chemical Shift Referencing in Biomolecular NMR,"" J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4108,193844,1,,entry citation,,98356294,,,"Alexandrescu, A. T., and Rathgeb-Szabo, K., ""NMR Assignments for Acid-Denatured Cold Shock Protein A,"" J. Biomol. NMR 11, 461-462 (1998).",NMR Assignments for Acid-Denatured Cold Shock Protein A,published,journal,J. Biomol. NMR,,11,4,,,,,,,,,,,,,,,,,,,,,,461,462,1998, citations,citation_one,4108,193845,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., Sykes, B. D., ""1H, 13C and 15N Chemical Shift Referencing in Biomolecular NMR,"" J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4109,193859,1,,entry citation,,99052118,,,"Chen, H. A., Pfuhl, M., Davis, B., and Driscoll, P. C., ""Sequence Specific 1H, 13C and 15N Resonance Assignment of Rat CD2 Domain 1,"" J. Biomol. NMR 12, 457-458 (1998).","Sequence Specific 1H, 13C and 15N Resonance Assignment of Rat CD2 Domain 1",published,journal,J. Biomol. NMR,,12,,,,,,,,,,,,,,,,,,,,,,,457,458,1998, citations,citation_one,4109,193860,2,,reference citation,,,8520220,,"Delaglio et.al, J. Biomol. NMR 6, 277-293, (1995).",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,entry_citation,411,193889,1,,entry citation,,,,,"Brown, Larry R., De Marco, A., Richarz, Rene, Wagner, Gerhard, Wuthrich, Kurt, ""The Influence of a Single Salt Bridge on Static and Dynamic Features of the Globular Solution Conformation of the Basic Pancreatic Trypsin Inhibitor 1H and 13C Nuclear-Magnetic-Resonance Studies of the Native and the Transaminated Inhibitor,"" Eur. J. Biochem. 88, 87-95 (1978).","The Influence of a Single Salt Bridge on Static and Dynamic Features of the Globular Solution Conformation of the Basic Pancreatic Trypsin Inhibitor 1H and 13C Nuclear-Magnetic-Resonance Studies of the Native and the Transaminated Inhibitor",published,journal,Eur. J. Biochem.,,88,,,,,,,,,,,,,,,,,,,,,,,87,95,1978, citations,entry_citation,4110,193902,1,,entry citation,,98424558,,,"Nanduri, S., Carpick, B., Yang, Y.W., Williams, B.R.G., and Qin, J. ""1H, 13C, 15N Resonance Assignment of the 20 KDa Double Stranded RNA Binding Domain of PKR,"" J. Biomol. NMR 12, 349-351 (1998).","1H, 13C, 15N Resonance Assignment of the 20 KDa Double Stranded RNA Binding Domain of PKR",published,journal,J. Biomol. NMR,,12,,,,,,,,,,,,,,,,,,,,,,,349,351,1998, citations,entry_citation,4124,194108,1,,entry citation,,99052117,,,"Ekiel, I., Banville, D., Shen, S. H., Slon-Usakiewicz, J. J., Koshy, A., Gehring, K., ""Main-chain Signal Assignment for the PDZ2 Domain from Human Protein Tyrosine Phosphatase hPTP1E and its Complex with a C-terminal Peptide from the Fas Receptor,"" J. Biomol. NMR 12, 455-456 (1998).","Main-chain Signal Assignment for the PDZ2Domain from Human Protein Tyrosine Phosphatase hPTP1E and its Complex with a C-terminal Peptide from the Fas Receptor",published,journal,J. Biomol. NMR,,12,,,,,,,,,,,,,,,,,,,,,,,455,456,1998, citations,citation_one,4124,194109,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, J. H., Oldfield, E., Markley, J. L., and Sykes, B. D., J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,citation_one,4110,193903,2,,reference citation,,,8520220,,"Delaglio, F., Grzesiek, S. Vuister, G. W., Zhu, G., Pfeifer, J. and Bax, A. J. Biomol NMR 6, 277-293 (1995).",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,entry_citation,4111,193919,1,,entry citation,,98399496,,,"Kelly, G., Prasannan, S., Daniel, S., Frankel, G., Dougan, G., Connerton, I., and Matthews, S., ""Sequential Assignment of the Triple Labelled 30.1 kDa Cell-adhesion Domain of Intimin from Enteropathogenic E. coli,"" J. Biomol. NMR 12, 189-191 (1998).","Sequential Assignment of the Triple Labelled 30.1 kDa Cell-adhesion Domain of Intimin from Enteropathogenic E. coli",published,journal,J Biomol. NMR,Journal of Biomolecular NMR,12,,,,,,,,,,,,,,,,,,,,,,,189,191,1998, citations,entry_citation,4112,193932,1,,entry citation,,98399494,,,"Langdon, G.M., Bruix, M., Galvez, A., Valdivia, E., Maqueda, M., and Rico, M., ""Sequence-specific 1H Assignment and Secondary Structure of the Bacteriocin AS-48 Cyclic Peptide,"" J. Biomol. NMR 12, 173-175 (1998).","Sequence-specific 1H Assignment and Secondary Structure of the Bacteriocin AS-48 Cyclic Peptide.",published,journal,J. Biomol. NMR,,12,,,,,,,,,,,,,,,,,,,,,,,173,175,1998, citations,entry_citation,4113,193943,1,,entry citation,,9752005,,,"Kelley, J. J. III, Bushweller, J., ""1H, 13C, and 15N NMR Resonance Assignments of Vaccinia Glutaredoxin-1 in the Fully Reduced Form,"" J. Biomol. NMR 12, 353-355 (1998).","1H, 13C, and 15N NMR Resonance Assignments of Vaccinia Glutaredoxin-1 in the Fully Reduced Form",published,journal,J. Biomol. NMR,,12,2,,,,,,,,,,,,,,,,,,,,,,353,355,1998, citations,entry_citation,4114,193956,1,,entry citation,,,9657674,,,"Solution Structure of the B-MYB DNA-binding Domain: Evidence for a Key Role for Conformational Instability of the Protein in DNA-binding and Control of Gene Expression",published,journal,Biochemistry,,37,,,,,,,,,,,,,,,,,,,,,,,9619,9629,1998, citations,entry_citation,4115,193987,1,,entry citation,,99109973,,,"Boetzel, R., Czisch, M., MacDonald, C. J., Kaptein, R., Hemmings, A., James, R., Kleanthous, C., and Moore, G. R., ""Assignment of 1H, 13C and 15N Signals of the Inhibitor Protein Im9 Bound to the DNase Domain of Colicin E9,"" J. Biomol. NMR 12, 567-568 (1998).","Assignment of 1H, 13C and 15N Signals of the Inhibitor Protein Im9 Bound to the DNase Domain of Colicin E9",published,journal,J. Biomol. NMR,,12,4,,,,,,,,,,,,,,,,,,,,,,567,568,1998, citations,entry_citation,4116,194002,1,,entry citation,,99109973,,,"Boetzel, R., Czisch, M., MacDonald, C. J., Kaptein, R., Hemmings, A.M., James, R., Kleanthous, C., Moore, G. R., ""Assignment of 1H, 13C and 15N Signals of the Inhibitor Protein Im9 Bound to the DNase Domain of Colicin E9,"" J. Biomol. NMR 12, 567-568 (1998).","Assignment of 1H, 13C and 15N Signals of the Inhibitor Protein Im9 Bound to the DNase Domain of Colicin E9",published,journal,J. Biomol. NMR,,12,4,,,,,,,,,,,,,,,,,,,,,,567,568,1998, citations,entry_citation,4117,194016,1,,entry citation,,99052123,,,"Perez, J. M. J., Kriek, J., Dijk, J., Moller, W., Siegal, G., Hard, K., Kalverda, A. P., and Canters, G. W., ""1H, 15N and 13C Chemical Shift Assignment of the Guanine Nucleotide Exchange Domain of Human Elongation Factor-one Beta,"" J. Biomol. NMR 12, 467-468 (1998).","1H, 15N and 13C Chemical Shift Assignment of the Guanine Nucleotide Exchange Domain of Human Elongation Factor-one Beta",published,journal,J. Biomol. NMR,,12,,,,,,,,,,,,,,,,,,,,,,,467,468,1998, citations,citation_one,4117,194017,2,,reference citation,,,7830591,,"Wishart and Sykes, Meth. Enzymol. 239, 363-392 (1994).",Chemical shifts as a tool for structure determination.,published,journal,Meth. Enzymol.,Methods in enzymology,239,,,0076-6879,,,,,,,,,,,,,,,,,,,,363,392,1994, citations,entry_citation,412,194030,1,,entry citation,,,,,"Brown, Larry R., De Marco, A., Richarz, Rene, Wagner, Gerhard, Wuthrich, Kurt, ""The Influence of a Single Salt Bridge on Static and Dynamic Features of the Globular Solution Conformation of the Basic Pancreatic Trypsin Inhibitor 1H and 13C Nuclear-Magnetic-Resonance Studies of the Native and the Transaminated Inhibitor,"" Eur. J. Biochem. 88, 87-95 (1978).","The Influence of a Single Salt Bridge on Static and Dynamic Features of the Globular Solution Conformation of the Basic Pancreatic Trypsin Inhibitor 1H and 13C Nuclear-Magnetic-Resonance Studies of the Native and the Transaminated Inhibitor",published,journal,Eur. J. Biochem.,,88,,,,,,,,,,,,,,,,,,,,,,,87,95,1978, citations,entry_citation,4120,194043,1,,entry citation,,,9545221,,,"NMR Structure of a Classical Pseudoknot: Interplay of Single- and Double-Stranded RNA",published,journal,Science,,280,,,,,,,,,,,,,,,,,,,,,,,434,438,1998, citations,entry_citation,4121,194066,1,,entry citation,,98424560,,,"Ippel, J.H., Larsson, G., Behravan, G., Lundqvist, M., Lycksell , P.-O., Schleucher, J., Zdunek, J., and Wijmenga, S.S., ""1H, 13C and 15N Assignment of the Isl-1 Homeodomain,"" J. Biomol. NMR 12, 357-359 (1998).","1H, 13C and 15N Assignment of the Isl-1 Homeodomain",published,journal,J. Biomol. NMR,,12,2,,,,,,,,,,,,,,,,,,,,,,357,359,1998, citations,entry_citation,4122,194082,1,,entry citation,,98239731,,,"Horita, D.A., Baldisseri, D.M., Zhang, W., Altieri, A.S. Smithgall, T.E., Gmeiner, W.H., and Byrd, R.A., ""Solution Structure of the Human Hck SH3 Domain and Identification of its Ligand Binding Site,"" J. Mol. Biol. 278, 253-265 (1998).","Solution Structure of the Human Hck SH3 Domain and Identification of its Ligand Binding Site",published,journal,J. Mol. Biol.,,278,,,,,,,,,,,,,,,,,,,,,,,253,265,1998, citations,entry_citation,4123,194095,1,,entry citation,,99052117,,,"Ekiel, I., Banville, D., Shen, S. H., Slon-Usakiewicz, J. J., Koshy, A., Gehring, K., ""Main-chain Signal Assignment for the PDZ2 Domain from Human Protein Tyrosine Phosphatase hPTP1E and its Complex with a C-terminal Peptide from the Fas Receptor,"" J. Biomol. NMR 12, 455-456 (1998).","Main-chain Signal Assignment for the PDZ2Domain from Human Protein Tyrosine Phosphatase hPTP1E and its Complex with a C-terminal Peptide from the Fas Receptor",submitted,journal,J. Biomol. NMR,,12,,,,,,,,,,,,,,,,,,,,,,,455,456,1998, citations,entry_citation,4125,194123,1,,entry citation,,96251082,,,"Glemarec, C., Kufel, J., Foldesi, A., Maltseva, T., Sandstrom, A., Kirsebom, L., Chattopadhyaya, J., ""The NMR Structure of 31mer RNA Domain of Escherichia Coli RNase P RNA Using Its Non-uniformly Deuterium Labelled Counterpart [the 'NMR-window' concept],"" Nucleic Acids Res. 24, 2022-2035 (1996).","The NMR Structure of 31mer RNA Domain of Escherichia Coli RNase P RNA Using Its Non-uniformly Deuterium Labelled Counterpart [the 'NMR-window' concept]",published,journal,Nucleic Acids Res.,Nucleic Acids Research,24,11,,,,,,,,,,,,,,,,,,,,,,2022,2035,1996, citations,entry_citation,4126,194137,1,,entry citation,,99254067,,,"Walsh, S.T.R., Cheng, H., Bryson, J.W., Roder, H., and DeGrado, W.F., ""Solution Structure and Dynamics of a De Novo Designed Three-helix Bundle Protein,"" Proc. Natl. Acad. Sci. USA 96, 5486-5491 (1999).",Solution Structure and Dynamics of a De Novo Designed Three-helix Bundle Protein,published,journal,Proc. Natl. Acad. Sci. U. S. A.,,96,10,,,,,,,,,,,,,,,,,,,,,,5486,5491,1999, citations,entry_citation,4127,194150,1,,entry citation,,97102430,,,"Luo, X., Sanford, D. G., Bullock, P. A., Bachovchin, W. W., ""Solution Structure of the Origin DNA-binding Domain of SV40 T-antigen,"" Nature Struct. Biol. 3, 1034-1039, (1996).",Solution Structure of the Origin DNA-binding Domain of SV40 T-antigen,published,journal,Nat. Struct. Biol.,Nature Structural Biology,3,12,,,,,,,,,,,,,,,,,,,,,,1034,1039,1996,"The data reported here represents the origin DNA-binding domain (residues 131-260) of simian virus 40 large T antigen." citations,entry_citation,4128,194163,1,,entry citation,,,,,"Morita, H., Kosada, T., Yamazaki, T., Kyogoku, Y., Hayashi, H., ""NMR Backbone Assignments of the Cyanobacterial Transcriptional Factor, SmtB, that Senses the Zinc Concentration in the Cell,"" J. Biomol. NMR 12, 453-454 (1998).","NMR Backbone Assignments of the Cyanobacterial Transcriptional Factor, SmtB, that Senses the Zinc Concentration in the Cell",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,12,,,,,,,,,,,,,,,,,,,,,,,453,454,1998, citations,entry_citation,4129,194178,1,,entry citation,,99079125,9862132,,,"1H and 15N Resonance Assignment of the Calcium-bound Form of the Nereis Diversicolor Sarcoplasmic Calcium(2+)-binding Protein.",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,12,4,,,,,,,,,,,,,,,,,,,,,,565,566,1998, citations,entry_citation,413,194198,1,,entry citation,,,,,"Brown, Larry R., De Marco, A., Richarz, Rene, Wagner, Gerhard, Wuthrich, Kurt, ""The Influence of a Single Salt Bridge on Static and Dynamic Features of the Globular Solution Conformation of the Basic Pancreatic Trypsin Inhibitor 1H and 13C Nuclear-Magnetic-Resonance Studies of the Native and the Transaminated Inhibitor,"" Eur. J. Biochem. 88, 87-95 (1978).","The Influence of a Single Salt Bridge on Static and Dynamic Features of the Globular Solution Conformation of the Basic Pancreatic Trypsin Inhibitor 1H and 13C Nuclear-Magnetic-Resonance Studies of the Native and the Transaminated Inhibitor",published,journal,Eur. J. Biochem.,,88,,,,,,,,,,,,,,,,,,,,,,,87,95,1978, citations,entry_citation,4130,194211,1,,entry citation,,98285557,,,"Dangi, B., Sarma, S., Yan, C., Banville, D., Guiles, R.D., ""The Origin of Difference in the Physical Properties of the Equilibrium Forms of Cytochrome b5 Revealed Through High Resolution NMR Structures and Backbone Dynamic Analyses,"" Biochemistry 37, 8289-8302 (1998).","The Origin of Difference in the Physical Properties of the Equilibrium Forms of Cytochrome b5 Revealed Through High Resolution NMR Structures and Backbone Dynamic Analyses",published,journal,Biochemistry,Biochemistry,37,,,,,,,,,,,,,,,,,,,,,,,8289,8302,1998, citations,citation_one,4130,194212,2,,reference citation,,,8019132,,"Wishart and Sykes, (1994), J.B. NMR, 4 171-18",The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,4,2,,0925-2738,,,,,,,,,,,,,,,,,,,,171,180,1994,"A simple technique for identifying protein secondary structures through the analysis of backbone 13C chemical shifts is described. It is based on the Chemical-Shift Index [Wishart et al. (1992) Biochemistry, 31, 1647-1651] which was originally developed for the analysis of 1H(alpha) chemical shifts. By extending the Chemical-Shift Index to include 13C(alpha), 13C(beta) and carbonyl 13C chemical shifts, it is now possible to use four independent chemical-shift measurements to identify and locate protein secondary structures. It is shown that by combining both 1H and 13C chemical-shift indices to produce a 'consensus' estimate of secondary structure, it is possible to achieve a predictive accuracy in excess of 92%. This suggests that the secondary structure of peptides and proteins can be accurately obtained from 1H and 13C chemical shifts, without recourse to NOE measurements." citations,entry_citation,4131,194227,1,,entry citation,,98285557,,,"Dangi, B., Sarma, S., Yan, C., Banville, D., Guiles, R.D., ""The Origin of Difference in the Physical Properties of the Equilibrium Forms of Cytochrome b5 Revealed Through High Resolution NMR Structures and Backbone Dynamic Analyses,"" Biochemistry 37, 8289-8302 (1998).","The Origin of Difference in the Physical Properties of the Equilibrium Forms of Cytochrome b5 Revealed Through High Resolution NMR Structures and Backbone Dynamic Analyses",published,journal,Biochemistry,Biochemistry,37,,,,,,,,,,,,,,,,,,,,,,,8289,8302,1998, citations,citation_one,4131,194228,2,,reference citation,,,8019132,,"Wishart and Sykes, (1994), J.B. NMR, 4 171-18",The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,4,2,,0925-2738,,,,,,,,,,,,,,,,,,,,171,180,1994,"A simple technique for identifying protein secondary structures through the analysis of backbone 13C chemical shifts is described. It is based on the Chemical-Shift Index [Wishart et al. (1992) Biochemistry, 31, 1647-1651] which was originally developed for the analysis of 1H(alpha) chemical shifts. By extending the Chemical-Shift Index to include 13C(alpha), 13C(beta) and carbonyl 13C chemical shifts, it is now possible to use four independent chemical-shift measurements to identify and locate protein secondary structures. It is shown that by combining both 1H and 13C chemical-shift indices to produce a 'consensus' estimate of secondary structure, it is possible to achieve a predictive accuracy in excess of 92%. This suggests that the secondary structure of peptides and proteins can be accurately obtained from 1H and 13C chemical shifts, without recourse to NOE measurements." citations,entry_citation,4132,194243,1,,entry citation,,99169955,,,"Liu, Q., Shen, B., Chen, D., and Chen, Y., ""Backbone Resonance Assignments of Human UBC9,"" J. Biomol. NMR 13, 89-90 (1999).",Backbone Resonance Assignments of Human UBC9,published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,13,1,,,,,,,,,,,,,,,,,,,,,,89,90,1999, citations,entry_citation,4133,194258,1,,entry citation,,98263181,,,"Greenfield, N. J., Montelione, G. T., Farid, R. S. and Hitchcock-DeGregori, S. E., ""The Structure of the N-terminus of Striated Muscle Alpha-Tropomyosin in a Chimeric Peptide: Solution Nuclear Magnetic Resonance Structure and Circular Dichroism Studies,"" Biochemistry 37, 7834-7843 (1998).","The Structure of the N-terminus of Striated Muscle Alpha-Tropomyosin in a Chimeric Peptide: Solution Nuclear Magnetic Resonance Structure and Circular Dichroism Studies.",published,journal,Biochemistry,,37,,,,,,,,,,,,,,,,,,,,,,,7834,7843,1998, citations,citation_one,4134,194272,2,,reference citation,,,8589602,,"Wishart D. S., Bigam C .G., Yao J., Abildgaard F., Dyson H. J., Oldfield E., Markley J. L., Sykes B. D. , '1H, 13C and 15N chemical shift referencing in biomolecular NMR,' J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4135,194288,1,,entry citation,,20311269,,,"Tanaka, Y., Kojima, C., Yamazaki, T., Kodama, T.S., Yasuno, K., Miyashita, S., Ono, A., Ono, A., Kainosho, M., and Kyogoku, Y., ""Solution Structure of an RNA Duplex Including a C-U Base Pair,"" Biochemistry 39, 7074-7080 (2000).",Solution Structure of an RNA Duplex Including a C-U Base Pair,published,journal,Biochemistry,Biochemistry,39,24,,,,,,,,,,,,,,,,,,,,,,7074,7080,2000, citations,entry_citation,4136,194307,1,,entry citation,,98351559,,,"Schwaiger, M., Lebendiker, M., Yerushalmi, H., Coles, M., Groeger, A., Schwarz, C., Schuldiner, S., Horst, K. , ""NMR-Investigations of the Multidrug Transporter EmrE, an Integral Membrane Protein,"" Eur. J. Biochem. 254, 610-619 (1998).","NMR-Investigations of the Multidrug Transporter EmrE, an Integral Membrane Protein",published,journal,Eur. J. Biochem.,,,254,,,,,,,,,,,,,,,,,,,,,,610,619,1998, citations,citation_1,4136,194308,2,,reference citation,,,,,"Schwaiger, M., Riemer,C., Kessler,H. (1998) Random coil 1H and 13C chemical shifts in chloroform/methanol mixtures. Submitted for publication",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4137,194325,1,,entry citation,,,,,"Xia, B., Wilkens, S. J., Westler, W. M., Markley, J. L., ""Amplification of One-Bond 1H/2H Isotope Efects on 15N Chemical Shifts in Clostridium pasteurianum Rubredoxin by Fermi-Contact Effects Through Hydrogen Bonds,"" J. Am. Chem. Soc. 120, 4893-4894 (1998).","Amplification of One-Bond 1H/2H Isotope Efects on 15N Chemical Shifts in Clostridium pasteurianum Rubredoxin by Fermi-Contact Effects Through Hydrogen Bonds",published,journal,J. Am. Chem. Soc.,,120,19,,,,,,,,,,,,,,,,,,,,,,4893,4894,1998, citations,citation_one,4137,194326,2,,reference citation,,,,,"Xia, B., Westler, W.M., Cheng, H., Moulis, J.-M., and Markley, J.L. J. Am. Chem. Soc. 117, 5347 (1995).",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4138,194344,1,,entry citation,,97111348,,,"Chen, C., Hom, K., Huang, R.-F., Chou, P.-J., Laio, Y.-D., Huang, T.-H., ""The Secondary Structure of a Pyrimidine-Guanine Sequence-Specific Ribonuclease Possessing Cytotoxic Activity from the Oocytes of Rana catesbeiana,"" J. Biomol NMR, 331-344 (1996).","The Secondary Structure of a Pyrimidine-Guanine Sequence-Specific Ribonuclease Possessing Cytotoxic Activity from the Oocytes of Rana catesbeiana",published,journal,J. Biomol NMR,Journal of Biomolecular NMR,8,,,,,,,,,,,,,,,,,,,,,,,331,344,1996, citations,entry_citation,414,194359,1,,entry citation,,,,,"Brown, Larry R., De Marco, A., Richarz, Rene, Wagner, Gerhard, Wuthrich, Kurt, ""The Influence of a Single Salt Bridge on Static and Dynamic Features of the Globular Solution Conformation of the Basic Pancreatic Trypsin Inhibitor 1H and 13C Nuclear-Magnetic-Resonance Studies of the Native and the Transaminated Inhibitor,"" Eur. J. Biochem. 88, 87-95 (1978).","The Influence of a Single Salt Bridge on Static and Dynamic Features of the Globular Solution Conformation of the Basic Pancreatic Trypsin Inhibitor 1H and 13C Nuclear-Magnetic-Resonance Studies of the Native and the Transaminated Inhibitor",published,journal,Eur. J. Biochem.,,88,,,,,,,,,,,,,,,,,,,,,,,87,95,1978, citations,entry_citation,4140,194372,1,,entry citation,,99052122,,,"Whitehead, B., Tessari, M., Versteeg, H. H., van Delft, S., van Bergen en Henegouwen, P.M.P., and Vuister, G.W., ""Sequence-specific 1H, 13C and 15N Assignment of the EH1 Domain of Mouse Eps15,"" J. Biomol. NMR 12, 465-466 (1998).","Sequence-specific 1H, 13C and 15N Assignment of the EH1 Domain of Mouse Eps15",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,12,,,,,,,,,,,,,,,,,,,,,,,465,466,1998, citations,entry_citation,4141,194387,1,,entry citation,,,10356327,,,"The three-dimensional structure of the vnd/NK-2 homeodomain-DNA complex by NMR spectroscopy",published,journal,J. Mol. Biol.,Journal of Molecular Biology,289,,,,,,,,,,,,,,,,,,,,,,,529,545,1999, citations,ref_1,4141,194388,2,,reference citation,,,9154919,,"J. M. Gruschus, D. H. H. Tsao, L.-H. Wang, M. Nirenberg, J. A. Ferretti, ""Interactions of the vnd/NK-2 Homeodomain with DNA by NMR: Basis of Binding Specificit,"" Biochemistry, 36, 5327-5380 (1997).",Interactions of the vnd/NK-2 homeodomain with DNA by nuclear magnetic resonance spectroscopy: basis of binding specificity.,published,journal,Biochemistry,Biochemistry,36,18,,0006-2960,,,,,,,,,,,,,,,,,,,,5372,5380,1997,"The interactions responsible for the nucleotide sequence-specific binding of the vnd/NK-2 homeodomain of Drosophila melanogaster to its consensus DNA binding site have been identified. A three-dimensional structure of the vnd/NK-2 homeodomain-DNA complex is presented, with emphasis on the structure of regions of observed protein-DNA contacts. This structure is based on protein-DNA distance restraints derived from NMR data, along with homology modeling, solvated molecular dynamics, and results from methylation and ethylation interference experiments. Helix III of the homeodomain binds in the major groove of the DNA and the N-terminal arm binds in the minor groove, in analogy with other homeodomain-DNA complexes whose structures have been reported. The vnd/NK-2 homeodomain recognizes the unusual DNA consensus sequence 5'-CAAGTG-3'. The roles in sequence specificity and strength of binding of individual amino acid residues that make contact with the DNA are described. We show, based primarily on the observed protein-DNA contacts, that the interaction of Y54 with the DNA is the major determinant of this uncommon nucleotide binding specificity in the vnd/NK-2 homeodomain-DNA complex." citations,entry_citation,4149,194525,1,,entry citation,,99052113,,,"Pochapsky, T.C., Kuti, M., Kazanis, S., ""Solution Structure of Gallium-Substituted Putidaredoxin Mutant: GaPdx C85S,"" J. Biomol. NMR 12, 407-415 (1998).","Solution Structure of Gallium-Substituted Putidaredoxin Mutant: GaPdx C85S",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,12,,,,,,,,,,,,,,,,,,,,,,,407,415,1998, citations,entry_citation,415,194545,1,,entry citation,,,,,"Brown, Larry R., De Marco, A., Richarz, Rene, Wagner, Gerhard, Wuthrich, Kurt, ""The Influence of a Single Salt Bridge on Static and Dynamic Features of the Globular Solution Conformation of the Basic Pancreatic Trypsin Inhibitor 1H and 13C Nuclear-Magnetic-Resonance Studies of the Native and the Transaminated Inhibitor,"" Eur. J. Biochem. 88, 87-95 (1978).","The Influence of a Single Salt Bridge on Static and Dynamic Features of the Globular Solution Conformation of the Basic Pancreatic Trypsin Inhibitor 1H and 13C Nuclear-Magnetic-Resonance Studies of the Native and the Transaminated Inhibitor",published,journal,Eur. J. Biochem.,,88,,,,,,,,,,,,,,,,,,,,,,,87,95,1978, citations,entry_citation,4161,194761,1,,entry citation,,98230747,9562558,,,"Solution structure of the IRF-2 DNA-binding domain: a novel subgroup of the winged helix-turn-helix family",published,journal,Structure,Structure,6,,,,,,,,,,,,,,,,,,,,,,,491,500,1998, citations,ref_2,4141,194389,3,,reference citation,,,7643404,,"D. H. H. Tsao, J. M. Gruschus, L.-H. Wang, M. Nirenberg, J. A. Ferretti, ""The Three- dimensional Solution Structure of the NK-2 Homeodomain from Drosophila,"" J. Mol. Biol., 251, 297-307 (1995).",The three-dimensional solution structure of the NK-2 homeodomain from Drosophila.,published,journal,J. Mol. Biol.,Journal of molecular biology,251,2,,0022-2836,,,,,,,,,,,,,,,,,,,,297,307,1995,"We describe the NMR determination of the three-dimensional structure of a 77 amino acid residue protein, which consists of the 60 residue NK-2 homeodomain from Drosophila melanogaster and adjacent amino acid residues. The NK-2 homeodomain protein is part of a 723 amino acid residue protein which is expressed early in embryonic development in part of the central nervous system. NK-2 was characterized using both a natural abundance and a uniformly 15N enriched sample by two-dimensional and three-dimensional NMR experiments. The average root-mean-square deviation for 30 structures for residues 8 to 53 is 0.40 A for the backbone heavy-atoms and 0.72 A for the backbone and side-chain heavy-atoms. These structures were obtained from 986 NOE-derived upper and lower bound restraints. The three-dimensional structure contains three helices which consist of homeodomain amino acid residues 10 to 22, 28 to 38 and 42 to 52, as well as a turn between helix II and III, characteristic of homeodomains. Residues 53 to 60 of the DNA recognition helix are not fully ordered in the absence of DNA. In the free state this segment adopts a flexible but helix-like structure between residues 53 and 56 and is disordered from residues 57 to 60 although, as shown previously, the helix elongates by eight residues upon binding to DNA. The role of variable residues 52, 54 and 56 in determining the structure and flexibility of the recognition helix, as well as the stability of the NK-2 homeodomain as manifested by its thermal denaturation, are discussed." citations,ref_3,4141,194390,4,,reference citation,,,7999763,,"D. H. H. Tsao, J. M. Gruschus, L.-H. Wang, M. Nirenberg, J. A. Ferretti, ""Elongation of Helix III of the NK-2 Homeodomain upon Binding to DNA: A Secondary Structure Study by NMR,"" Biochemistry, 33, 15053-15060 (1994).",Elongation of helix III of the NK-2 homeodomain upon binding to DNA: a secondary structure study by NMR.,published,journal,Biochemistry,Biochemistry,33,50,,0006-2960,,,,,,,,,,,,,,,,,,,,15053,15060,1994,"The secondary structure of the homeodomain encoded by the NK-2 gene from Drosophila melanogaster, in both the free and DNA-bound states, was determined in solution using two- and three-dimensional (2D and 3D) NMR spectroscopy. Proton and 15N studies were carried out on a 77 amino acid residue protein that contains the homeodomain, which was synthesized in Escherichia coli. On the basis of NOE connectivities, vicinal coupling constants, and proton-deuterium exchange behavior, three helical segments were found that consist of homeodomain amino acid residues 10-22, 28-38, and 42-52 for the protein in the absence of DNA. The major structural differences between free NK-2 and other homeodomains are the increased internal mobility of the second helix and the shorter length of the third helix, also termed the recognition helix. Despite this shorter helix, NK-2 exhibits high-affinity binding to DNA compared to other homeodomains (kD = 2.0 x 10(-10) M; L.-H. Wang and M. Nirenberg, unpublished results). The formation of the complex of NK-2 with the duplex DNA (TGTGTCAAGTG-GCTGT) significantly increases the thermal stability of the protein. The Tm increases from 25 degrees C (free NK-2) to > 47 degrees C (DNA-bound NK-2). Also, a dramatic increase in the length of helix III is observed. In the absence of DNA, the DNA recognition helix is 11 amino acid residues long (residues 42-52), whereas in the presence of DNA, the length of this helix extends to 19 amino acids (residues 42-60).(ABSTRACT TRUNCATED AT 250 WORDS)" citations,entry_citation,4142,194417,1,,entry citation,,99079127,,,"Lerche, M. H., and Poulsen, F. M., ""Assignments of 1H and 13C Resonances in the Complex of Palmitate and a Non-specific Lipid Transfer Protein (ns-LTP) Isolated from Barley Seeds,"" J. Biomol. NMR. 12, 571-572 (1998).","Assignments of 1H and 13C Resonances in the Complex of Palmitate and a Non-specific Lipid Transfer Protein (ns-LTP) Isolated from Barley Seeds.",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,12,4,,,,,,,,,,,,,,,,,,,,,,571,572,1998, citations,entry_citation,4143,194432,1,,entry citation,,99079126,,,"Jensen, P. H., Thomsen, N. K., Soroka, V., Berezin, V., Bock, E., and Poulsen, F. M., ""1H and 15N Resonance Assignment of Neural Cell Adhesion Molecule Module-2,"" J. Biomol. NMR. 12, 569-570 (1998).",1H and 15N Resonance Assignment of Neural Cell Adhesion Molecule module 2,published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,12,4,,,,,,,,,,,,,,,,,,,,,,569,570,1998, citations,entry_citation,4144,194446,1,,entry citation,,,,,"Hodach, M., Elorante, J., Kostourou, V., Wienzierl, R., and Matthews, S., ""1H, 13C, 15N Sequential Assignment of the RNA Polymerase 'H' Subunit from Methanococcus jannaschii,"" J. Biomol. NMR, submitted (1998).","1H, 13C, 15N Sequential Assignment of the RNA Polymerase 'H' Subunit from Methanococcus jannaschii",submitted,journal,J Biomol. NMR,Journal of Biomolecular NMR,,,,,,,,,,,,,,,,,,,,,,,,,,1998, citations,entry_citation,4145,194459,1,,entry citation,,99052120,,,"Pursglove, S. E., Mulhern, T. D., Hinds, M. G., Norton, R. S., and Booker, G. W., ""Assignment of 1H and 15N Resonances of Murine Tec SH3 Domain,"" J. Biomol. NMR 12, 461-462 (1998).",Assignment of 1H and 15N Resonances of Murine Tec SH3 Domain,published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,12,,,,,,,,,,,,,,,,,,,,,,,461,462,1998, citations,citation_one,4145,194460,2,,reference citation,,,,,"Bartel, Ch., Xia, T.H., Billeter, P., Guntert, P. and Wuthrich K. J. Biomol. NMR 5, 1-10 (1995).",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_two,4145,194461,3,,reference citation,,,,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4146,194481,1,,entry citation,,98301362,,,"Girvin, M. E., Rastogi, V. K., Abildgaard, F., Markley, J. L., and Fillingame, R. H., ""Solution Structure of the Transmembrane H+-Transporting Subunit c of the F1Fo ATP Synthase,"" Biochemistry 37, 8817-8824 (1998).","Solution Structure of the Transmembrane H+-Transporting Subunit c of the F1Fo ATP Synthase",published,journal,Biochemistry,Biochemistry,37,25,,,,,,,,,,,,,,,,,,,,,,8817,8824,1998, citations,entry_citation,4147,194497,1,,entry citation,,99052121,,,"Kloks, C.P.A.M., Hoffmann, A., Omichinski, J. G., Vuister, G. W., Hilbers, C. W., Grzesiek, S., ""Resonance Assignment and Secondary Structure of the Cold Shock Domain of the Human YB-1 Protein,"" J. Biomol. NMR. 12, 463-464 (1998).","Resonance Assignment and Secondary Structure of the Cold Shock Domain of the Human YB-1 Protein",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,12,,,,,,,,,,,,,,,,,,,,,,,463,464,1998, citations,citation_one,4147,194498,2,,reference citation,,,,,"Bax, A. and Subramanian, S. J. Magn. Reson., 67, 565-570 (1986).",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4148,194514,1,,entry citation,,98430965,,,,"Solution Structure of the Cellulose-binding Domain of Endoglucanase I from Trichoderma reesei and its Interaction with Cello-oligosaccharides",published,journal,Eur. J. Biochem.,European Journal of Biochemistry,256,2,,,,,,,,,,,,,,,,,,,,,,279,286,1998, citations,entry_citation,5555,227109,1,,entry citation,,22728194,12842043,,,Engineering a Protein Scaffold from a PHD Finger,published,journal,Structure,Structure,11,7,,,,,,,,,,,,,,,,,,,,,,803,813,2003, citations,entry_citation,4150,194558,1,,entry citation,,99224884,,,"and Grotzinger, J., ""The Signal Transducer gp130: Solution Structure of the Carboxy-terminal Domain of the Cytokine Receptor Homology Region,"" Protein Sci. 8, 5-12 (1999).","The Signal Transducer gp130: Solution Structure of the Carboxy-terminal Domain of the Cytokine Receptor Homology Region",published,journal,Protein Sci.,Protein Science,8,,,,,,,,,,,,,,,,,,,,,,,5,12,1999, citations,entry_citation,4151,194575,1,,entry citation,,99169956,,,"Rastogi, V. K., Girvin, M. E. ""1H, 13C, and 15N Assignments and Secondary Structure of the High pH Form of Subunit c of the F1FO ATP Synthase,"" J. Biomol. NMR 13, 91-92 (1999).","1H, 13C, and 15N Assignment and Secondary Structure of the High pH Form of Subunit c of the F1FO ATP Synthase",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,13,1,,,,,,,,,,,,,,,,,,,,,,91,92,1999, citations,citation_one,4151,194576,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4152,194591,1,,entry citation,,99169957,,,,"1H, 13C and 15N Backbone Resonance Assignment of Escherichia coli Adenylate Kinase, a 23.6 kDa Protein",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,13,,,,,,,,,,,,,,,,,,,,,,,93,94,1999, citations,entry_citation,4153,194607,1,,entry citation,,98365498,,,,High-Resolution Solution Structure of the Retinoid X Receptor DNA-Binding Domain,published,journal,J. Mol. Biol.,Journal of Molecular Biology,281,,,,,,,,,,,,,,,,,,,,,,,271,284,1998, citations,entry_citation,4154,194624,1,,entry citation,,99218076,,,"Pochapsky, T. C., Jain, N. U., Kuti, M., Lyons, T. A., and Heymont, J., ""A Refined Model for the Solution Structure of Oxidized Putidaredoxin"", Biochemistry, 38, 4681-4690 (1999).",A Refined Model for the Solution Structure of Oxidized Putidaredoxin,published,journal,Biochemistry,Biochemistry,38,,,,,,,,,,,,,,,,,,,,,,,4681,4690,1999, citations,citation_one,4154,194625,2,,reference citation,,,1536837,,"Ye, X. M., Pochapsky, T. C. and Pochapsky, S. S., ""1H NMR Sequential Assignments and Identification of Secondary Structural Elements in Oxidized Putidaredoxin, an Electron-transfer Protein from Pseudomonas,"" Biochemistry 31, 1961-1968 (1992)","1H NMR sequential assignments and identification of secondary structural elements in oxidized putidaredoxin, an electron-transfer protein from Pseudomonas.",published,journal,Biochemistry,Biochemistry,31,7,,0006-2960,,,,,,,,,,,,,,,,,,,,1961,1968,1992,"Sequential 1H resonance assignments and secondary structural features of putidaredoxin (Pdx), a 106-residue globular protein consisting of a single polypeptide chain and a [2Fe-2S] cluster, are reported. No crystal structure has been obtained for Pdx or for any closely homologous protein. The sequentially assigned resonances represent ca. 83% of all the protons in Pdx and a large majority of those protons which are unaffected by the paramagnetism of the iron-sulfur cluster. A total of three alpha-helices, two beta-sheets, and two type I beta-turns have been identified from NOE (nuclear Overhauser effect) patterns. Besides the extensive beta-sheet described previously, a second sheet is identified, consisting of two short antiparallel strands (Ile 89-Thr 91 and Val 21-Leu 23), one of which ends in a tight type I turn (Thr 91-Pro 92-Glu 93-Leu 94). One short helix (Ala 26-Gly 31) and a second longer helical region (Glu 54-Cys 73) are present. This second helical region is discontinuous, breaking at Pro 61, resuming at Glu 65, and ending at Cys 73. The functionally important C-terminal tryptophan residue has been identified, and some structural constraints on this residue are described. Previously reported functional data concerning Pdx are discussed in light of present structural information. Finally, approaches to the determination of a high-resolution solution structure of the protein are discussed." citations,citation_two,4154,194626,3,,reference citation,,,8845752,,"Lyons, T. A., Ratnaswamy, G. and Pochapsky, T. C., ""Redox-dependent Dynamics of Putidaredoxin Characterized by Amide Proton Exchange,"" Protein Sci. 5, 627-639 (1996).",Redox-dependent dynamics of putidaredoxin characterized by amide proton exchange.,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,5,4,,0961-8368,,,,,,,,,,,,,,,,,,,,627,639,1996,"Multidimensional NMR methods were used to obtain 1H-15N correlations and 15N resonance assignments for amide and side-chain nitrogens of oxidized and reduced putidaredoxin (Pdx), the Fe2S2 ferredoxin, which acts as the physiological reductant of cytochrome P-450cam (CYP101). A model for the solution structure of oxidized Pdx has been determined recently using NMR methods (Pochapsky TC, Ye XM, Ratnaswamy G, Lyons TA, 1994, Biochemistry 33:6424-6432) and redox-dependent 1H NMR spectral features have been described (Pochapsky TC, Ratnaswamy G, Patera A, 1994, Biochemistry 33:6433-6441). 15N assignments were made with NOESY-(1H/15N) HMQC and TOCSY-(1H/15N) HSQC spectra obtained using samples of Pdx uniformly labeled with 15N. Local dynamics in both oxidation states of Pdx were then characterized by comparison of residue-specific amide proton exchange rates, which were measured by a combination of saturation transfer and H2O/D2O exchange methods at pH 6.4 and 7.4 (uncorrected for isotope effects). In general, where exchange rates for a given site exhibit significant oxidation-state dependence, the oxidized protein exchanges more rapidly than the reduced protein. The largest dependence of exchange rate upon oxidation state is found for residues near the metal center and in a region of compact structure that includes the loop-turn Val 74-Ser 82 and the C-terminal residues (Pro 102-Trp 106). The significance of these findings is discussed in light of the considerable dependence of the binding interaction between Pdx and CYP101 upon the oxidation state of Pdx." citations,citation_three,4154,194627,4,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,citation_four,4154,194628,5,,reference citation,,,,,"""Recommendations for Presentations of NMR Structures of Proteins and Nucleic Acids,"" IUPAC/IUB Draft version.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4155,194645,1,,entry citation,,98380469,,,"Crump, M. P., Rajarathnam, K., Kim, K.-S., and Sykes, B. D., ""Solution Structure of Eotaxin: a Chemokine That Selectively Recruits Eosinophils in Allergic Inflammation,"" J. Biol. Chem. 273, 22471-22479 (1998).","Solution Structure of Eotaxin: a Chemokine That Selectively Recruits Eosinophils in Allergic Inflammation",published,journal,J. Biol. Chem.,Journal of Biological Chemistry,273,,,,,,,,,,,,,,,,,,,,,,,22471,22479,1998, citations,citation_one,4155,194646,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4156,194664,1,,entry citation,,99309858,,,"Kemmink, J., Dijkstra, K., Mariani, M., Scheek, R.M., Penka, E., Nilges, M., and Darby, N.J., ""The Structure in Solution of the b Domain of Protein Disulfide Isomerase,"" J. Biomol. NMR 13, 357-368 (1999).","The Structure in Solution of the b Domain of Protein Disulfide Isomerase",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,13,,,,,,,,,,,,,,,,,,,,,,,357,368,1999, citations,citation_one,4156,194665,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4157,194679,1,,entry citation,,98190007,,,,"Three-dimensional Solution Structure of Lactoferricin B, an Antimicrobial Peptide Derived from Bovine Lactoferrin",published,journal,Biochemistry,,37,,,,,,,,,,,,,,,,,,,,,,,4288,4298,1998, citations,citation_one,4157,194680,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4158,194693,1,,entry citation,,96303820,,,,"1H and 15N Nuclear Magnetic Resonance Assignment and Secondary Structure of the Cytotoxic Ribonuclease Alpha-sarcin",published,journal,Protein Sci.,,5,,,,,,,,,,,,,,,,,,,,,,,969,972,1996, citations,citation_one,4158,194694,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D., ""1H, 13C and 15N Chemical Shift Referencing in Biomolecular NMR,"" J. Biomol. NMR 6, 135-140 (1995)","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,citation_two,4158,194695,3,,reference citation,,,,,,"Campos-Olivas, R., ""Estructura y Dinamica de Proteinas por Resonancia Magnetica Nuclear: Proteina Antifungica y Alpha Sarcina,"" Thesis, 85-142, Universidad Complutense de Madrid (1997)",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4159,194708,1,,entry citation,,96140214,,,,"Solution Structure of LSIII, a Long Neurotoxin from the Venom of Laticauda semifasciata",published,journal,Biochemistry,,35,,,,,,,,,,,,,,,,,,,,,,,418,426,1996, citations,citation_one,4159,194709,2,,reference citation,,,,,"Hoch, J. C., and Stern, A.S., The Rowland NMR Toolkit v3, The Rowland Institute for Science, Cambridge MA.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_two,4159,194710,3,,reference citation,,,1726780,,"Eccles, C., Guntert, P., Billeter, M., and Wutrich, K. J. Biol. NMR, 1, 111-130, (1991).",Efficient analysis of protein 2D NMR spectra using the software package EASY.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,1,2,,0925-2738,,,,,,,,,,,,,,,,,,,,111,130,1991,"The program EASY supports the spectral analysis of biomacromolecular two-dimensional (2D) nuclear magnetic resonance (NMR) data. It provides a user-friendly, window-based environment in which to view spectra for interactive interpretation. In addition, it includes a number of automated routines for peak-picking, spin-system identification, sequential resonance assignment in polypeptide chains, and cross peak integration. In this uniform environment, all resulting parameter lists can be recorded on disk, so that the paper plots and handwritten notes which normally accompany manual assignment of spectra can be largely eliminated. For example, in a protein structure determination by 2D 1H NMR, EASY accepts the frequency domain datasets as input, and after combined use of the automated and interactive routines it can yield a listing of conformational constraints in the format required as input for the calculation of the 3D structure. The program was extensively tested with current protein structure determinations in our laboratory. In this paper, its main features are illustrated with data on the protein basic pancreatic trypsin inhibitor." citations,citation_three,4159,194711,4,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,416,194734,1,,entry citation,,,,,"Brown, Larry R., De Marco, A., Richarz, Rene, Wagner, Gerhard, Wuthrich, Kurt, ""The Influence of a Single Salt Bridge on Static and Dynamic Features of the Globular Solution Conformation of the Basic Pancreatic Trypsin Inhibitor 1H and 13C Nuclear-Magnetic-Resonance Studies of the Native and the Transaminated Inhibitor,"" Eur. J. Biochem. 88, 87-95 (1978).","The Influence of a Single Salt Bridge on Static and Dynamic Features of the Globular Solution Conformation of the Basic Pancreatic Trypsin Inhibitor 1H and 13C Nuclear-Magnetic-Resonance Studies of the Native and the Transaminated Inhibitor",published,journal,Eur. J. Biochem.,,88,,,,,,,,,,,,,,,,,,,,,,,87,95,1978, citations,entry_citation,4160,194747,1,,entry citation,,99311323,,,,"Resonance Assignments of the Tn916 Integrase DNA-Binding Domain and Integrase: DNA Complex",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,14,,,,,,,,,,,,,,,,,,,,,,,95,96,1999, citations,citation_one,4160,194748,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,5556,227133,1,,entry citation,,22728194,12842043,,,Engineering a Protein Scaffold from a PHD Finger,published,journal,Structure,Structure,11,7,,,,,,,,,,,,,,,,,,,,,,803,813,2003, citations,citation_one,4161,194762,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., Sykes, B. D., ""1H, 13C and 15N Chemical Shift Referencing in Biomolecular NMR,"" J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4162,194781,1,,entry citation,,99356752,,,"Jensen, P. H., Thomsen, N. K., Soroka, V., Berezin, V., Bock, E., and Poulsen, F. M., ""1H, 13C and 15N Resonance Assignment of the Neural Cell Adhesion Molecule Module-1,"" J. Biomol. NMR 14, 185-186 (1999).","1H, 13C and 15N Resonance Assignment of the Neural Cell Adhesion Molecule Module-1",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,14,,,,,,,,,,,,,,,,,,,,,,,185,186,1999, citations,entry_citation,4163,194797,1,,entry citation,,20058644,,,"Fant, F., Vranken, W., and Borremans F., ""The Three-dimensional Solution Structure of Aesculus hippocastanum Antimicrobial Protein 1 Determined by 1H Nuclear Magnetic Resonance,"" Proteins 37, 388-403 (1999).","The Three-dimensional Solution Structure of Aesculus hippocastanum Antimicrobial Protein 1 Determined by 1H Nuclear Magnetic Resonance",published,journal,Proteins,Proteins,37,,,,,,,,,,,,,,,,,,,,,,,388,403,1999, citations,entry_citation,4164,194812,1,,entry citation,,99060075,9843403,,,"Bacterial Iron Transport: 1H NMR Determination of the Three-dimensional Structure of the Gallium Complex of Pyoverdin G4R, the Peptidic Siderophore of Pseudomonas putida G4R",published,journal,Biochemistry,,37,,,,,,,,,,,,,,,,,,,,,,,15965,15973,1998, citations,citation_one,4164,194813,2,,reference citation,,,,,"Salah El Din, A.M., Kyslik, P., Stephan, D. and Abdallah, M.A. Tetrahedron, 53, 12539-12552 (1997).",,published,journal,,,,,,,,,,,,,,,,,,,,,,,,,,12539,12552,1997, citations,entry_citation,4165,194836,1,,entry citation,,99315213,10382314,,,"Resonance assignments of the Tn916 integrase DNA-binding domain and the integrase:DNA complex",published,journal,J. Biomol. NMR,,14,,,,,,,,,,,,,,,,,,,,,,,95,96,1999, citations,citation_one,4165,194837,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4166,194856,1,,entry citation,,9748232,,,,"Lipid-induced Local Conformational Changes in the C2A-domain of Synaptotagmin I as Revealed by NMR Spectroscopy",published,journal,J. Biol. Chem.,Journal of Biological Chemistry,273,40,,,,,,,,,,,,,,,,,,,,,,25659,25663,1998, citations,citation_one,4166,194857,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4167,194875,1,,entry citation,,9748232,,,,"Lipid-induced Local Conformational Changes in the C2A-domain of Synaptotagmin I as Revealed by NMR Spectroscopy",published,journal,J. Biol. Chem.,Journal of Biological Chemistry,273,40,,,,,,,,,,,,,,,,,,,,,,25659,25663,1998, citations,citation_one,4167,194876,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4168,194896,1,,entry citation,,99081553,,,,"Localization of Basic Residues Required for Receptor Binding to the Single Alpha-helix of the Receptor Binding Domain of Human Alpha-2-macroglobulin",published,journal,Protein Sci.,Protein Science,7,,,,,,,,,,,,,,,,,,,,,,,2602,2612,1998, citations,entry_citation,4169,194910,1,,entry citation,,99060075,9843403,,,"Bacterial Iron Transport: 1H NMR Determination of the Three-dimensional Structure of the Gallium Complex of Pyoverdin G4R, the Peptidic Siderophore of Pseudomonas putida G4R",published,journal,Biochemistry,,37,,,,,,,,,,,,,,,,,,,,,,,15965,15973,1998, citations,citation_one,4169,194911,2,,reference citation,,,,,"Salah El Din, A.M., Kyslik, P., Stephan, D. and Abdallah, M.A. Tetrahedron, 53, 12539-12552 (1997).",,published,journal,,,,,,,,,,,,,,,,,,,,,,,,,,12539,12552,1997, citations,entry_citation,417,194931,1,,entry citation,,,,,"Ni, Feng, Konishi, Yasuo, Bullock, Lea Doerr, Rivetna, Meheryar N., Scheraga, H.A., ""High-Resolution NMR Studies of Fibrinogen-like Peptides in Solution: Structural Basis for the Bleeding Disorder Caused by a Single Mutation of Gly(12) to Val(12) in the Aalpha Chain of Human Fibrinogen Rouen,"" Biochemistry 28, 3106-3119 (1989).","High-Resolution NMR Studies of Fibrinogen-like Peptides in Solution: Structural Basis for the Bleeding Disorder Caused by a Single Mutation of Gly(12) to Val(12) in the Aalpha Chain of Human Fibrinogen Rouen",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,3106,3119,1989, citations,entry_citation,4170,194944,1,,entry citation,,98359763,,,,"2'-Deoxyisoguanosine Adopts more than one Tautomer to Base Pair with Thymidine Observed by High Resolution Crystal Structure Analysis",published,journal,Biochemistry,Biochemistry,37,,,,,,,,,,,,,,,,,,,,,,,10897,10905,1998, citations,entry_citation,4229,196101,1,,entry citation,,99089613,,,,"Solution structure of an artficial Fe8S8 ferredoxin: the D13C variant of Bacillus schlegelii Fe7S8 ferredoxin""",published,journal,Eur. J. Biochem.,European Journal of Biochemistry,258,2,,,,,,,,,,,,,,,,,,,,,,502,514,1998, citations,entry_citation,4493,201575,1,,entry citation,,99404942,10467150,,,"Solution structure and dynamics of a designed hydrophobic core variant of ubiquitin",published,journal,Structure,,7,,,,,,,,,,,,,,,,,,,,,,,967,976,1999, citations,citation_one,4170,194945,2,,reference citation,,,1554732,,"Robinson, H., and Wang, A.H.-J, Biochemistry 31, 3524-3533 (1992).",A simple spectral-driven procedure for the refinement of DNA structures by NMR spectroscopy.,published,journal,Biochemistry,Biochemistry,31,13,,0006-2960,,,,,,,,,,,,,,,,,,,,3524,3533,1992,"We have developed a simple and quantitative procedure (SPEDREF) for the refinement of DNA structures using experimental two-dimensional nuclear Overhauser effect (2D NOE) data. The procedure calculates the simulated 2D NOE spectrum using the full matrix relaxation method on the basis of a molecular model. The volume of all NOE peaks is measured and compared between the experimental and the calculated spectra. The difference of the experimental and simulated volumes is minimized by a conjugated gradient procedure to adjust the interproton distances in the model. An agreement factor (analogous to the crystallographic R-factor) is used to monitor the progress of the refinement. The procedure is an The agreement is considered to be complete when several parameters, including the R-factor, the energy associated with the molecule, the local conformation (as judged by the sugar pseudorotation), and the global conformation (as judged by the helical x-displacement), are refined to their respective convergence. With the B-DNA structure of d(CGATCG) as an example, we show that DNA structure may be refined to produce calculated NOE spectra that are in excellent agreement with the experimental 2D NOE spectra. This is judged to be effective by the low R-factor of approximately 15%. Moreover, we demonstrate that not only are NOE data very powerful in providing details of the local structure but, with appropriate weighting of the NOE constraints, the global structure of the DNA double helix can also be determined, even when starting with a grossly different model. The reliability and limitations of a DNA structure as determined by NMR spectroscopy are discussed." citations,citation_two,4170,194946,3,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4171,194964,1,,entry citation,,99169966,,,,"Backbone and C beta Assignments of the Anti-gp120 Antibody Fv Fragment Complexed with an Antigenic Peptide",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,13,,,,,,,,,,,,,,,,,,,,,,,193,194,1999, citations,citation_one,4171,194965,2,,reference citation,,,7538073,,"Zvi, A., Kustanovich, I., Levy, R., Matsushita, M., Richalet-Secordel, P., Regenmortel, M. H. V., and Anglister, J., ""Mapping of the Antigenic Determinant Recognized by an Anti-Gp120 HIV Neutralizing Antibody by Two-Dimensional NMR. Eur. J. Biochem. 119: 178-187 (1995).","NMR mapping of the antigenic determinant recognized by an anti-gp120, human immunodeficiency virus neutralizing antibody.",published,journal,Eur. J. Biochem.,European journal of biochemistry / FEBS,229,1,,0014-2956,,,,,,,,,,,,,,,,,,,,178,187,1995,"The 24-amino-acid peptide RP135 (NNTRKSIRIQRGPGRAFVTIGKIG) corresponds in its amino acid sequence to the principal neutralizing determinant of the human immunodeficiency virus type-1, IIIB isolate (HIV-1IIIB, residues 308-331 of the envelope glycoprotein gp120). In order to map the antigenic determinant recognized by 0.5 beta, the complex of RP135 with an anti-gp120 HIV neutralizing antibody, 0.5 beta, which cross reacts with the peptide, was studied by using two-dimensional NMR spectroscopy. A combination of homonuclear Hartmann Hahn two-dimensional experiment and roating-frame Overhauser enhancement spectroscopy of the Fab/peptide complex measured in H2O was used to eliminate the resonances of the Fab and the tightly bound peptide residues and to obtain sequential assignments for those parts of the peptide which retain considerable mobility upon binding. In this manner, a total of 14 residues (Ser6-Thr19) were shown to be part of the antigenic determinant recognized by the antibody 0.5 beta. Lys5 and Ile20 were found to retain considerable mobility in the bound peptide while their amide protons undergo significant change in chemical shift upon binding. This observation suggests that these two residues are at the boundaries of the determinant recognized by the antibody. Competitive binding experiments using truncated peptides strongly support the NMR observations." citations,entry_citation,4172,194981,1,,entry citation,,,,,,"Solution Structure of the Orphan Nuclear Receptor Rev-erb Beta Response Element by 1H, 31P NMR and Molecular Simulation",published,journal,Biochimie,Biochimie,82,,,,,,,,,,,,,,,,,,,,,,,739,748,2000, citations,citation_one,4172,194982,2,,reference citation,,,,,"R. Lavery in structure and expression,vol 3, DNA bending and curvature (Olson et al., Eds) pp 191-211, Adenine Press, NY (1988)",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4173,195001,1,,entry citation,,98434377,9760240,,,"Solution Structure of the Catalytic Domain of Human Stromelysin-1 Complexed to a Potent, Non-peptidic Inhibitor",published,journal,Biochemistry,Biochemistry,37,,,,,,,,,,,,,,,,,,,,,,,14048,14056,1998, citations,entry_citation,4174,195028,1,,entry citation,,9748232,,,,"When Size is Important: Accommodation of Magnesium in a Calcium Binding Regulatory Domain",published,journal,J. Biol. Chem.,Journal of Biological Chemistry,273,44,,,,,,,,,,,,,,,,,,,,,,28994,29001,1998, citations,citation_one,4174,195029,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4175,195045,1,,entry citation,,98417646,,,,Three-dimensional Folding of an RNA Hairpin Required for Packaging HIV-1,published,journal,J. Mol. Biol.,Journal of Molecular Biology,282,,,,,,,,,,,,,,,,,,,,,,,801,818,1998, citations,entry_citation,4176,195061,1,,entry citation,,98451587,,,,NMR Solution Structure of a DNA Dodecamer Containing Single G:T Mismatches,published,journal,Nucleic Acids Res.,Nucleic Acids Research,26,,,,,,,,,,,,,,,,,,,,,,,4925,4934,1998, citations,entry_citation,4195,195432,1,,entry citation,,97322323,,,"Scherf, T., Balass M., Fuchs, S., Katchalski-Katzir, E., and Anglister, J., ""Three-Dimensional Solution Structure of the Complex of Alpha-Bungarotoxin with a Library-Derived Peptide"", Proc. Natl. Acad. Sci. U.S.A. 94, 6059-6064 (1997).","Three-Dimensional Solution Structure of the Complex of Alpha-Bungarotoxin with a Library-Derived Peptide",published,journal,Proc. Natl. Acad. Sci. U.S.A.,"Proceedings of the National Academy of Sciences,USA",94,,,,,,,,,,,,,,,,,,,,,,,6059,6064,1997, citations,citation_one,4176,195062,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4177,195078,1,,entry citation,,,,,,"Structural Characterization of a Monomeric Chemokine: Monocyte Chemoattractant Protein-3",published,journal,FEBS Lett.,,395,,,,,,,,,,,,,,,,,,,,,,,277,,1996, citations,citation_one,4177,195079,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4179,195101,1,,entry citation,,99169414,,,,"Conformational Analysis of Peptide Fragments Derived from the Peripheral Subunit-binding Domain from the Pyruvate Dehydrogenase Multienzyme Complex of Bacillus stearothermophilus: Evidence for Non-random Structure in the Unfolded State",published,journal,Biopolymers,Biopolymers,49,,,,,,,,,,,,,,,,,,,,,,,29,40,1999, citations,entry_citation,418,195117,1,,entry citation,,,,,"Pease, Joseph H.B., Wemmer, David, ""Solution Structure of Apamin Determined by Nuclear Magnetic Resonance and Distance Geometry,"" Biochemistry 27, 8491-8498 (1988).","Solution Structure of Apamin Determined by Nuclear Magnetic Resonance and Distance Geometry",published,journal,Biochemistry,,27,,,,,,,,,,,,,,,,,,,,,,,8491,8498,1988, citations,entry_citation,4180,195130,1,,entry citation,,99169414,,,,"Conformational Analysis of Peptide Fragments Derived from the Peripheral Subunit-binding Domain from the Pyruvate Dehydrogenase Multienzyme Complex of Bacillus stearothermophilus: Evidence for Non-random Structure in the Unfolded State",published,journal,Biopolymers,Biopolymers,49,,,,,,,,,,,,,,,,,,,,,,,29,40,1999, citations,entry_citation,4181,195146,1,,entry citation,,99089609,,,"Im, S-C., Liu, G., Luchinat, C., Sykes, A.G., and Bertini, I.,""The Solution Structure of Parsley [2Fe-2S] Ferredoxin,"" Eur. J. Biochem. 258, 465-477 (1998).",The Solution Structure of Parsley [2Fe-2S] Ferredoxin,published,journal,Eur. J. Biochem.,European Journal Biochemistry,258,,,,,,,,,,,,,,,,,,,,,,,465,477,1998, citations,entry_citation,4182,195167,1,,entry citation,,,,,,Solution Structure of Reduced Clostridium pasteurianum Rubredoxin,published,journal,J. Biol. Inorg. Chem.,Journal of Biological Inorganic Chemistry,3,4,,,,,,,,,,,,,,,,,,,,,,401,410,1998, citations,entry_citation,4183,195183,1,,entry citation,,,,,"Twigg, P. D., Wylie, G. P., Wang, G., Caspar, D. L.D., Murphy, J. R., and Logan, T. M.,""Expression and Assignment of 1H, 15N,and 13C Resonances of the C-terminal Domain of the Diphtheria Toxin Repressor,"" J. Biomol. NMR 13, 197-198 (1999).","Expression and Assignment of 1H, 15N,and 13C Resonances of the C-terminal Domain of the Diphtheria Toxin Repressor",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,13,,,,,,,,,,,,,,,,,,,,,,,197,198,1999, citations,citation_one,4183,195184,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4184,195198,1,,entry citation,,98387926,,,,Structure and Asn-Pro-Phe Binding Pocket of the Eps15 Homology Domain,published,journal,Science,Science,281,,,,,,,,,,,,,,,,,,,,,,,1357,1360,1998, citations,citation_one,4184,195199,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4185,195233,1,,entry citation,,99421659,,,,"High-Resolution Solution Structure of Gurmarin,a Sweet-Taste-Suppressing Plant Polypeptide",published,journal,Eur. J. Biochem.,European Journal of Biochemistry,264,,,,,,,,,,,,,,,,,,,,,,,525,533,1999, citations,citation_one,4185,195234,2,,reference citation,,,,,"Bartels, C.,Xia, T-H., Billeter,M., Guentert, P., Wuthrich, K., ""The Program XEASY for Computer-Supported NMR Spectral Analysis of Biological Macromolecules,"" J.Biomol.NMR 5 pp 1-10 (1995).",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_two,4185,195235,3,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4186,195251,1,,entry citation,,98409425,,,"Wang, L., Li, Y., Abildgaard, F., Markley, J.L., and Yan, H., ""NMR Solution Structure of type II Human Cellular Retinoic Acid Binding Protein: Implications for Ligand Binding,"" Biochemistry 37, 12727-12736 (1998).","NMR Solution Structure of type II Human Cellular Retinoic Acid Binding Protein: Implications for Ligand Binding",published,journal,Biochemistry,,37,37,,,,,,,,,,,,,,,,,,,,,,12727,12736,1998, citations,citation_one,4186,195252,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4187,195267,1,,entry citation,,98384140,,,"Tonelli, M., Ragg, E., Bianucci, A. M., Lesiak, K., and James, T. L., ""Nuclear Magnetic Resonance Structure of d(GCATATGATAG).d(CTATCATATGC): A Consensus Sequence for Promoters Recognized by Sigma-K RNA Polymerase,"" Biochemistry 37, 11745-11761 (1998).","Nuclear Magnetic Resonance Structure of d(GCATATGATAG).d(CTATCATATGC): A Consensus Sequence for Promoters Recognized by Sigma-K RNA Polymerase",published,journal,Biochemistry,Biochemistry,37,,,,,,,,,,,,,,,,,,,,,,,11745,11761,1998, citations,entry_citation,4188,195290,1,,entry citation,,98332749,,,,"Solution Structure and Membrane Interactions of the C2 Domain of Cytosolic Phospholipase A2",published,journal,J. Mol. Biol.,Journal of Molecular Biology,280,,,,,,,,,,,,,,,,,,,,,,,485,500,1998, citations,citation_one,4188,195291,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4189,195305,1,,entry citation,,99428887,,,,Solution Structure of Reduced Horse Heart Cytochrome C,published,journal,J. Biol. Inorg. Chem.,,4,,,,,,,,,,,,,,,,,,,,,,,21,31,1999, citations,citation_one,4189,195306,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,419,195326,1,,entry citation,,,,,"Wagner, Gerhard, Kumar, Anil, Wuthrich, Kurt, ""Systematic Application of Two-Dimensional 1H Nuclear-Magnetic-Resonance Techniques for Studies of Proteins 2. Combined Use of Correlated Spectroscopy and Nuclear Overhauser Spectroscopy for Sequential Assignments of Backbone Resonances and,"" Eur. J. Biochem. 114, 375-384 (1981).","Systematic Application of Two-Dimensional 1H Nuclear-Magnetic-Resonance Techniques for Studies of Proteins 2. Combined Use of Correlated Spectroscopy and Nuclear Overhauser Spectroscopy for Sequential Assignments of Backbone Resonances and",published,journal,Eur. J. Biochem.,,114,,,,,,,,,,,,,,,,,,,,,,,375,384,1981, citations,entry_citation,4190,195339,1,,entry citation,,98400946,,,,"Solution Structure of two new Toxins from the Venom of the Chinese Scorpion Buthus martensii Karsch Blockers of Potassium Channels",published,journal,Biochemistry,Biochemistry,37,,,,,,,,,,,,,,,,,,,,,,,12412,12418,1998, citations,citation_one,4190,195340,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4191,195354,1,,entry citation,,98400946,,,,"Solution Structure of two new Toxins from the Venom of the Chinese Scorpion Buthus martensii Karsch Blockers of Potassium Channels",published,journal,Biochemistry,Biochemistry,37,,,,,,,,,,,,,,,,,,,,,,,12412,12418,1998, citations,entry_citation,4192,195368,1,,entry citation,,,,,"Yao, S., Azad, A.A., Macreadie I.G., and Norton, R.S., ""Helical Structure of Polypeptides from the C-terminal Half of HIV-1 Vpr,"" Protein Pept. Lett. 5, 127-134 (1998).",Helical Structure of Polypeptides from the C-terminal Half of HIV-1 Vpr,published,journal,Protein Pept. Lett.,Protein and Peptide Letters,5,,,,,,,,,,,,,,,,,,,,,,,127,134,1998, citations,entry_citation,4193,195384,1,,entry citation,,99169967,,,"Meirovitch, E., Sinev, M. A., and Sineva, E. V., ""Letter to the Editor: Sequence-Specific 1H, 15N and 13C Assignment of Adenylate Kinase from Escherichia coli in Complex with the Inhibitor AP5A,"" J. Biomol. NMR 13, 195-196 (1999).","Letter to the Editor: Sequence-Specific 1H, 15N and 13C Assignment of Adenylate Kinase from Escherichia coli in Complex with the Inhibitor AP5A",published,journal,J. Biomol. NMR,,13,,,,,,,,,,,,,,,,,,,,,,,195,196,1999, citations,entry_citation,4194,195412,1,,entry citation,,,12168695,,,Structure-Functional Activity Studies of D-Pro Melittin,published,journal,J. Protein Chem.,,21,4,,,,,,,,,,,,,,,,,,,,,,243,253,2002, citations,citation_one,4194,195413,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4241,196332,1,,entry citation,,99354418,,,,"The Three-Dimensional Structure of a Family IIb Xylan Binding Domain: Evidence that the Orientation of the Solvent-Exposed Tryptophans Determines the Ligand Specificity of Type II Polysaccharide Binding Domains.",published,journal,Structure,,7,,,,,,,,,,,,,,,,,,,,,,,853,864,1999, citations,citation_one,4195,195433,2,,reference citation,,,3653402,,FEBS LETTERS V. 222 79-82 1987,Primary structure of alpha-bungarotoxin. Six amino acid residues differ from the previously reported sequence.,published,journal,FEBS Lett.,FEBS letters,222,1,,0014-5793,,,,,,,,,,,,,,,,,,,,79,82,1987,"alpha-Bungarotoxin (alpha-BuTx) was isolated from the venom of the Formosan banded krait (Bungarus multicinctus). The amino acid sequence was determined by a combination of conventional methods. In contrast to the sequence of alpha-BuTx reported by Mebs et al. ([1971) Biochem. Biophys. Res. Commun. 44, 711-716], our results revealed the presence of Ser-Pro-Ile, Pro-His and Gln-Arg at positions 9-11, 67-68 and 71-72 from the amino-terminal, respectively, and not Ile-Pro-Ser, His-Pro and Arg-Gln as reported previously." citations,entry_citation,4197,195448,1,,entry citation,,98407983,,,,"Solution Structure of the M13 Major Coat Protein in Detergent Micelles: A Basis for a Model of Phage Assembly Involving Specific Residues.",published,journal,J. Mol. Biol.,Journal of Molecular Biology,282,2,,,,,,,,,,,,,,,,,,,,,,401,419,1998, citations,citation_one,4197,195449,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,ref_1,4197,195450,3,,reference citation,,,7947703,,,Location of M13 coat protein in sodium dodecyl sulfate micelles as determined by NMR.,published,journal,Biochemistry,Biochemistry,33,44,,0006-2960,,,,,,,,,,,,,,,,,,,,12990,12997,1994,"The major coat protein (gVIIIp) of bacteriophage M13 solubilized in sodium dodecyl sulfate (SDS) detergent micelles was used as a model system to study this protein in the lipid-bound form. In order to probe the position of gVIIIp relative to the SDS micelles, stearate was added, spin-labeled at the 5- or 16-position with a doxyl group containing a stable nitroxide radical. The average position of the spin-labels in the micelles was derived from the line broadening of the resonances in the 13C spectrum of SDS. Subsequently, we derived a model of the relative position of gVIIIp in the SDS micelle from the effect of the spin-labels on the gVIIIp resonances, monitored via 1H-15N HSQC and TOCSY experiments. The results are consistent with the structure of gVIIIp having two helical strands. One strand is a long hydrophobic helix that spans the micelle, and the other is a shorter amphipathic helix on the surface of the micelle. These results are in good agreement with the structure of gVIIIp in membranes proposed by McDonnell et al. on the basis of solid state NMR data [McDonnell, P. A., Shon, K., Kim, Y., & Opella, S. J. (1993) J. Mol. Biol. 233, 447-463]. This study indicates that high-resolution NMR on this membrane protein, solubilized in detergent micelles, is a very suitable technique for mimicking these proteins in their natural environment. Furthermore, the data indicate that the structure of the micelle near the C-terminus of the major coat protein is distorted.(ABSTRACT TRUNCATED AT 250 WORDS)" citations,ref_2,4197,195451,4,,reference citation,,,7556198,,,NMR studies of the major coat protein of bacteriophage M13. Structural information of gVIIIp in dodecylphosphocholine micelles.,published,journal,Eur. J. Biochem.,European journal of biochemistry / FEBS,232,2,,0014-2956,,,,,,,,,,,,,,,,,,,,490,500,1995,"The membrane-bound form of the major coat protein (gVIIIp) of bacteriophage M13 has been studied using nuclear magnetic resonance spectroscopy. As membrane mimetics, we used dodecylphosphocholine (DodPCho) detergent micelles to solubilize the protein. We were able to nearly completely assign all resonances of the protein solubilized in DodPCho micelles by using both homonuclear and heteronuclear multidimensional experiments. Based on the patterns of the nuclear Overhauser enhancements and the chemical shifts of the resonances, we deduced the secondary structure of the protein. Additional structural information was obtained from amide proton exchange data and J-coupling constants. The protein consists of two alpha-helices which are connected by a hinge region around residue 21. From spin-label experiments, the location of the protein relative to the DodPCho micelles was determined. One, hydrophobic, helix spans the micelle, and another, amphipathic, helix, is located beneath the surface of the micelle. Comparison of the data of gVIIIp in DodPCho micelles with those of gVIIIp in sodium dodecyl sulfate (SDS) micelles [Van de Ven, F. J. M., van Os, J. W. M., Aelen, J. M. A., Wymenga, S. S., Remerowski, M. L., Konings, R. N. H. & Hilbers, C. W. (1993) Biochemistry 32, 8322-8328; Papavoine, C. H. M., Konings, R. N. H., Hilbers, C. W. & Van de Ven, F. J. M. (1994) Biochemistry 33, 12,990-12,997] reveals that the structures of the protein in the two detergent micelles are very similar. They differ only in the arrangement of the detergent molecules around the protein. For gVIIIp in SDS micelles, we found a micellar structure which is distorted near the C-terminus of the protein; whereas for DodPCho micelles, both distorted and regular elliptical micelles occur. This distortion is probably due to the interaction of the positively charged lysine side chains with the negatively charged head group of the detergent molecules." citations,ref_3,4197,195452,5,,reference citation,,,9092832,,,Backbone dynamics of the major coat protein of bacteriophage M13 in detergent micelles by 15N nuclear magnetic resonance relaxation measurements using the model-free approach and reduced spectral density mapping.,published,journal,Biochemistry,Biochemistry,36,13,,0006-2960,,,,,,,,,,,,,,,,,,,,4015,4026,1997,"The backbone dynamics of the major coat protein (gVIIIp) of the filamentous bacteriophage M13, solubilized in detergent micelles, have been studied using 15N nuclear magnetic resonance spectroscopy at three frequencies. Motional parameters and overall and internal correlation times were derived with the model-free approach. It was also checked whether these parameters had to be modified due to anisotropic motion of the protein/micelle complex. Reduced spectral density mapping was used to calculate the spectral densities at J(O), J(omegaN), and [J(omegaH)]. The spectral densities were interpreted by mapping a linear or scaled linear combination of two Lorentzians onto a J(O)-J(omega) plot. The major coat protein of bacteriophage M13 consists of two alpha-helices, one of which is hydrophobic and located within the micelle, while the other is amphipathic and located on the surface of the micelle. Our results indicate that the motion of the hydrophobic helix is restricted such that it corresponds to the overall tumbling of the protein/micelle complex. The interpretation of the relaxation data of the amphipathic helix by means of the model-free approach and the reduced spectral density mapping indicate that in addition to the overall motion all residues in this helix are subject to motion on the fast nanosecond and picosecond time scales. The motions of the vectors in the low nanosecond range are characterized by similar values of the spectral densities and correlation times and represent the motion of the amphipathic helix on and away from the surface of the micelle. The relaxation data of the residues in the hinge region connecting the helices show that there is an abrupt change from highly restricted to less restricted motion. Both the C-terminal and N-terminal residues are very mobile." citations,citation_one,4203,195589,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4333,198220,1,,entry citation,,20422733,,,,"The Three-dimensional Solution Structure and Dynamic Properties of the Human FADD Death Domain",published,journal,J. Mol. Biol.,Journal of Molecular Biology,302,,,,,,,,,,,,,,,,,,,,,,,171,188,2000, citations,ref_4,4197,195453,6,,reference citation,,,8347628,,,"Assignment of 1H, 15N, and backbone 13C resonances in detergent-solubilized M13 coat protein via multinuclear multidimensional NMR: a model for the coat protein monomer.",published,journal,Biochemistry,Biochemistry,32,32,,0006-2960,,,,,,,,,,,,,,,,,,,,8322,8328,1993,"The major coat protein (gVIIIp) of bacteriophage M13 complexed with SDS detergent micelles was used as a model system to study the lipid-bound conformation of the protein. Conditions were found that allowed the recording of good quality of NMR spectra. By making extensive use of three-dimensional heteronuclear (13C, 15N) NMR, we obtained a complete set of resonance assignments for 1HN, 1H alpha, 1H beta, 13C alpha, CO, and 15N and partially assigned the rest of the 1H spectrum. Analysis of NOE and chemical shift data reveals that gVIIIp is composed of two alpha-helical domains, one ranging from Pro-6 to Glu20 and the other ranging from Tyr-24 all the way to the C-terminus Ser-50. In contrast to the results reported by Henry and Sykes [Henry, G.D., & Sykes, B.D. (1992) Biochemistry 31, 5285-5297], at a high SDS to protein ratio the protein appears to be monomeric." citations,ref_5,4197,195454,7,,reference citation,,,8411155,,,fd coat protein structure in membrane environments.,published,journal,J. Mol. Biol.,Journal of molecular biology,233,3,,0022-2836,,,,,,,,,,,,,,,,,,,,447,463,1993,"The membrane bound form of bacteriophage fd coat protein has a long hydrophobic membrane spanning helix and a shorter amphipathic helix in the plane of the bilayer. Residues near the N and C termini and in the turn connecting the two helices are mobile. The locations and orientations of the helical secondary structure elements and the protein backbone dynamics were characterized by combining results from multidimensional solution NMR experiments on protein samples in micelles and high resolution solid-state NMR experiments on protein samples in oriented and unoriented lipid bilayers. The coat protein is a monomer in micelles. The secondary structure of the membrane bound form of fd coat protein is very similar to that of the structural form found in the virus particles, since it is nearly all alpha helix. However, the membrane bound form of the protein differs from the structural form of the protein in virus particles in the arrangement of the secondary structure, since the membrane bound form of the protein has two distinct helical domains oriented perpendicular to each other and the structural form of the protein in the virus particles has a nearly continuous helix aligned approximately along the filament axis. In addition, there are substantial differences in the dynamics of residues in the bend between the two helices and near the C terminus, since they are mobile in the membrane bound form of the protein and not in the virus particles. Residues 1 to 5 at the N terminus are highly mobile and unstructured in both the membrane bound and structural forms of the coat protein." citations,entry_citation,4198,195471,1,,entry citation,,98424252,,,,"Three-dimensional Structure of an Evolutionarily Conserved N-terminal Domain of Syntaxin 1A",published,journal,Cell,,94,,,,,,,,,,,,,,,,,,,,,,,841,849,1998, citations,entry_citation,4199,195485,1,,entry citation,,99353969,,,,"Determination of the Solution Structure of the N-Domain Plus Linker of Antarctic Eel Pout Antifreeze Protein RD3",published,journal,J. Biochem.,Journal of Biochemistry,126,2,,,,,,,,,,,,,,,,,,,,,,387,394,1999, citations,citation_one,4199,195486,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,42,195502,1,,entry citation,,,,,"Robertson, Andrew D., Westler, William M., Markley, John L., ""Two-Dimensional NMR Studies of Kazal Proteinase Inhibitors. 1. Sequence-Specific Assignments and Secondary Structure of Turkey Ovomucoid Third Domain,"" Biochemistry 27, 2519-2529 (1988).","Two-Dimensional NMR Studies of Kazal Proteinase Inhibitors. 1. Sequence-Specific Assignments and Secondary Structure of Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,27,,,,,,,,,,,,,,,,,,,,,,,2519,2529,1988, citations,entry_citation,420,195515,1,,entry citation,,,,,"Lee, Min S., Cavanagh, John, Wright, Peter E., ""Complete assignment of the 1H NMR spectrum of a synthetic zinc finger from Xfin Sequential resonance assignments and secondary structure,"" FEBS Lett. 254, 159-164 (1989).","Complete assignment of the 1H NMR spectrum of a synthetic zinc finger from Xfin Sequential resonance assignments and secondary structure",published,journal,FEBS Lett.,,254,,,,,,,,,,,,,,,,,,,,,,,159,164,1989, citations,entry_citation,4200,195530,1,,entry citation,,98347001,,,,"Insights into the Mechanism of Heterodimerization from the 1H-NMR Solution Structure of the c-Myc-Max Heterodimeric Leucine Zipper",published,journal,J. Mol. Biol.,,281,1,,,,,,,,,,,,,,,,,,,,,,165,181,1998, citations,reference_one,4200,195531,2,,reference citation,,,,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).",,published,journal,J. Biomol. NMR,,6,,,,,,,,,,,,,,,,,,,,,,,135,140,1995, citations,entry_citation,4201,195551,1,,entry citation,,99180407,,,"Barnham, K.J., Torres, A.M., Alewood, D., Alewood, P.F., Domagala, T., Nice, E.C., and Norton, R.S., ""Role of the 6-20 Disulfide Bridge in the Structure and Activity of Epidermal Growth Factor,"" Protein Sci. 7, 1738-1749 (1998).","Role of the 6-20 Disulfide Bridge in the Structure and Activity of Epidermal Growth Factor",published,journal,Protein Sci.,Protein Science,7,,,,,,,,,,,,,,,,,,,,,,,1738,1749,1998, citations,reference_one,4201,195552,2,,reference citation,,,,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4202,195568,1,,entry citation,,98384143,,,,"Solution Structure of Reduced Monomeric Q133M2 Copper, Zinc Superoxide Dismutase (SOD). Why SOD is a Dimeric Enzyme?",published,journal,Biochemistry,,37,34,,,,,,,,,,,,,,,,,,,,,,11780,11791,1998, citations,entry_citation,4203,195588,1,,entry citation,,99179484,,,,"An NMR Conformational Analysis of Synthetic Peptide Cn2(1-15)NH2-S-S-AcetylCn2(52-66)NH2 from the New World Centruroides Noxius 2(Cn2) Scorpion Toxin. Comparison of the Structure with those of the Centruroides Scorpion Toxins.",published,journal,Biopolymers,,49,4,,,,,,,,,,,,,,,,,,,,,,277,286,1999, citations,entry_citation,4204,195612,1,,entry citation,,93307857,,,"Sato, A., Nishumura, S., Ohkubo, T.,Kyogoku, Y., Koyama, S., Kobatashi, M., Yasuda,T., Kobayashi, Y., ""Three-Dimensional Structure of Human Insulin-like Growth Factor-I (IGF-I) Determined by 1H-NMR and Distance Geometry,"" Int. J. Pept Protein Res. 41, 433-440 (1993).","Three-Dimensional Structure of Human Insulin-like Growth Factor-I (IGF-I) Determined by 1H-NMR and Distance Geometry",published,journal,Int. J. Pept. Protein Res.,International Journal of Peptide and Protein Research,41,,,,,,,,,,,,,,,,,,,,,,,433,440,1993, citations,entry_citation,4205,195629,1,,entry citation,,98445336,,,"Slupsky, C.M., Gentile, L.N., Donaldson, L.W., Mackereth, C.D., Seidel, J.J., Graves, B.J., and McIntosh, L.P., ""Structure of the Ets-1 Pointed Domain and Mitogen-activiated Protein Kinase Phosphorylation Site,"" Proc. Natl. Acad. Sci. U.S.A. 95, 12129-12134 (1998).","Structure of the Ets-1 Pointed Domain and Mitogen-activiated Protein Kinase Phosphorylation Site.",published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences USA,95,,,,,,,,,,,,,,,,,,,,,,,12129,12134,1998, citations,entry_citation,4206,195661,1,,entry citation,,98202578,9533887,,"Copie, V., Tomita, Y., Akiyama, S.K., Aota, S., Yamada, K.M., Venable, R.M., Pastor, R.W., Krueger, S., and Torchia, D.A., ""Solution Structure and Dynamics of Linked Cell Attachment Modules of Mouse Fibronectin Containing the RGD and Synergy Regions: Comparison with the Human Fibronectin Crystal Structure,"" J. Mol. Biol. 277, 663-682 (1998).","Solution Structure and Dynamics of Linked Cell Attachment Modules of Mouse Fibronectin Containing the RGD and Synergy Regions: Comparison with the Human Fibronectin Crystal Structure",published,journal,J. Mol. Biol.,Journal of Molecular Biology,277,3,,,,,,,,,,,,,,,,,,,,,,663,682,1998, citations,entry_citation,4207,195676,1,,entry citation,,98227860,,,"Mossing, M.C., ""Solution Structure and Dynamics of a Designed Monomeric Variant of the Lambda CRO Repressor,"" Protein Sci. 7, 983-993 (1998).","Solution Structure and Dynamics of a Designed Monomeric Variant of the Lambda CRO Repressor",published,journal,Protein Sci.,Protein Science,7,,,,,,,,,,,,,,,,,,,,,,,983,993,1998, citations,citation_one,4207,195677,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4208,195696,1,,entry citation,,95147286,7844834,,,"Structure and Dynamics of Ferrocytochrome c553 from Desulfovibrio vulgaris Studied by Spectroscopy and Restrained Molecular Dynamics NMR",published,journal,J. Mol. Biol.,Journal of Molecular Biology,245,5,,,,,,,,,,,,,,,,,,,,,,661,681,1995, citations,entry_citation,4209,195711,1,,entry citation,,98407983,,,,"Solution structure of the M13 major coat protein in detergent micelles: A basis for a model of phage assembly involving specific residues",published,journal,J. Mol. Biol.,Journal of Molecular Biology,282,,,,,,,,,,,,,,,,,,,,,,,401,419,1998, citations,ref_1,4209,195712,2,,reference citation,,,7947703,,"Biochemistry 1994 Nov 8;33(44):12990-7 Location of M13 coat protein in sodium dodecyl sulfate micelles as determined by NMR. Papavoine CH, Konings RN, Hilbers CW, van de Ven FJ",Location of M13 coat protein in sodium dodecyl sulfate micelles as determined by NMR.,published,journal,Biochemistry,Biochemistry,33,44,,0006-2960,,,,,,,,,,,,,,,,,,,,12990,12997,1994,"The major coat protein (gVIIIp) of bacteriophage M13 solubilized in sodium dodecyl sulfate (SDS) detergent micelles was used as a model system to study this protein in the lipid-bound form. In order to probe the position of gVIIIp relative to the SDS micelles, stearate was added, spin-labeled at the 5- or 16-position with a doxyl group containing a stable nitroxide radical. The average position of the spin-labels in the micelles was derived from the line broadening of the resonances in the 13C spectrum of SDS. Subsequently, we derived a model of the relative position of gVIIIp in the SDS micelle from the effect of the spin-labels on the gVIIIp resonances, monitored via 1H-15N HSQC and TOCSY experiments. The results are consistent with the structure of gVIIIp having two helical strands. One strand is a long hydrophobic helix that spans the micelle, and the other is a shorter amphipathic helix on the surface of the micelle. These results are in good agreement with the structure of gVIIIp in membranes proposed by McDonnell et al. on the basis of solid state NMR data [McDonnell, P. A., Shon, K., Kim, Y., & Opella, S. J. (1993) J. Mol. Biol. 233, 447-463]. This study indicates that high-resolution NMR on this membrane protein, solubilized in detergent micelles, is a very suitable technique for mimicking these proteins in their natural environment. Furthermore, the data indicate that the structure of the micelle near the C-terminus of the major coat protein is distorted.(ABSTRACT TRUNCATED AT 250 WORDS)" citations,ref_2,4209,195713,3,,reference citation,,,7556198,,"Eur J Biochem 1995 Sep 1;232(2):490-500 NMR studies of the major coat protein of bacteriophage M13. Structural information of gVIIIp in dodecylphosphocholine micelles. Papavoine CH, Aelen JM, Konings RN, Hilbers CW, Van de Ven FJ",NMR studies of the major coat protein of bacteriophage M13. Structural information of gVIIIp in dodecylphosphocholine micelles.,published,journal,Eur. J. Biochem.,European journal of biochemistry / FEBS,232,2,,0014-2956,,,,,,,,,,,,,,,,,,,,490,500,1995,"The membrane-bound form of the major coat protein (gVIIIp) of bacteriophage M13 has been studied using nuclear magnetic resonance spectroscopy. As membrane mimetics, we used dodecylphosphocholine (DodPCho) detergent micelles to solubilize the protein. We were able to nearly completely assign all resonances of the protein solubilized in DodPCho micelles by using both homonuclear and heteronuclear multidimensional experiments. Based on the patterns of the nuclear Overhauser enhancements and the chemical shifts of the resonances, we deduced the secondary structure of the protein. Additional structural information was obtained from amide proton exchange data and J-coupling constants. The protein consists of two alpha-helices which are connected by a hinge region around residue 21. From spin-label experiments, the location of the protein relative to the DodPCho micelles was determined. One, hydrophobic, helix spans the micelle, and another, amphipathic, helix, is located beneath the surface of the micelle. Comparison of the data of gVIIIp in DodPCho micelles with those of gVIIIp in sodium dodecyl sulfate (SDS) micelles [Van de Ven, F. J. M., van Os, J. W. M., Aelen, J. M. A., Wymenga, S. S., Remerowski, M. L., Konings, R. N. H. & Hilbers, C. W. (1993) Biochemistry 32, 8322-8328; Papavoine, C. H. M., Konings, R. N. H., Hilbers, C. W. & Van de Ven, F. J. M. (1994) Biochemistry 33, 12,990-12,997] reveals that the structures of the protein in the two detergent micelles are very similar. They differ only in the arrangement of the detergent molecules around the protein. For gVIIIp in SDS micelles, we found a micellar structure which is distorted near the C-terminus of the protein; whereas for DodPCho micelles, both distorted and regular elliptical micelles occur. This distortion is probably due to the interaction of the positively charged lysine side chains with the negatively charged head group of the detergent molecules." citations,entry_citation,4225,196027,1,,entry citation,,99141205,,,"Nordstrand, K., Aslund, F., Holmgren, A., Otting, G., and Berndt, K.D., ""NMR Structure of Escherichia coli Glutaredoxin 3-glutathione Mixed Disulfide Complex: Implications for the Enzymatic Mechanism,"" J. Mol. Biol. 286, 541-552 (1999).","NMR Structure of Escherichia coli Glutaredoxin 3-glutathione Mixed Disulfide Complex: Implications for the Enzymatic Mechanism",published,journal,J. Mol. Biol.,Journal of Molecular Biology,286,,,,,,,,,,,,,,,,,,,,,,,541,552,1999, citations,ref1,4225,196028,2,,reference citation,,,,,"Bartels, C. et al. J. Biomol. NMR 5, 1-10 (1995)",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref2,4225,196029,3,,reference citation,,,,,"Guntert, P. et al. J. Biomol. NMR 2, 619-629 (1992)",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_3,4209,195714,4,,reference citation,,,9092832,,"Biochemistry 1997 Apr 1;36(13):4015-26 Backbone dynamics of the major coat protein of bacteriophage M13 in detergent micelles by 15N nuclear magnetic resonance relaxation measurements using the model-free approach and reduced spectral density mapping. Papavoine CH, Remerowski ML, Horstink LM, Konings RN, Hilbers CW, van de Ven FJ",Backbone dynamics of the major coat protein of bacteriophage M13 in detergent micelles by 15N nuclear magnetic resonance relaxation measurements using the model-free approach and reduced spectral density mapping.,published,journal,Biochemistry,Biochemistry,36,13,,0006-2960,,,,,,,,,,,,,,,,,,,,4015,4026,1997,"The backbone dynamics of the major coat protein (gVIIIp) of the filamentous bacteriophage M13, solubilized in detergent micelles, have been studied using 15N nuclear magnetic resonance spectroscopy at three frequencies. Motional parameters and overall and internal correlation times were derived with the model-free approach. It was also checked whether these parameters had to be modified due to anisotropic motion of the protein/micelle complex. Reduced spectral density mapping was used to calculate the spectral densities at J(O), J(omegaN), and [J(omegaH)]. The spectral densities were interpreted by mapping a linear or scaled linear combination of two Lorentzians onto a J(O)-J(omega) plot. The major coat protein of bacteriophage M13 consists of two alpha-helices, one of which is hydrophobic and located within the micelle, while the other is amphipathic and located on the surface of the micelle. Our results indicate that the motion of the hydrophobic helix is restricted such that it corresponds to the overall tumbling of the protein/micelle complex. The interpretation of the relaxation data of the amphipathic helix by means of the model-free approach and the reduced spectral density mapping indicate that in addition to the overall motion all residues in this helix are subject to motion on the fast nanosecond and picosecond time scales. The motions of the vectors in the low nanosecond range are characterized by similar values of the spectral densities and correlation times and represent the motion of the amphipathic helix on and away from the surface of the micelle. The relaxation data of the residues in the hinge region connecting the helices show that there is an abrupt change from highly restricted to less restricted motion. Both the C-terminal and N-terminal residues are very mobile." citations,ref_4,4209,195715,5,,reference citation,,,8347628,,"Biochemistry 1993 Aug 17;32(32):8322-8 Assignment of 1H, 15N, and backbone 13C resonances in detergent-solubilized M13 coat protein via multinuclear multidimensional NMR: a model for the coat protein monomer. van de Ven FJ, van Os JW, Aelen JM, Wymenga SS, Remerowski ML, Konings RN, Hilbers CW","Assignment of 1H, 15N, and backbone 13C resonances in detergent-solubilized M13 coat protein via multinuclear multidimensional NMR: a model for the coat protein monomer.",published,journal,Biochemistry,Biochemistry,32,32,,0006-2960,,,,,,,,,,,,,,,,,,,,8322,8328,1993,"The major coat protein (gVIIIp) of bacteriophage M13 complexed with SDS detergent micelles was used as a model system to study the lipid-bound conformation of the protein. Conditions were found that allowed the recording of good quality of NMR spectra. By making extensive use of three-dimensional heteronuclear (13C, 15N) NMR, we obtained a complete set of resonance assignments for 1HN, 1H alpha, 1H beta, 13C alpha, CO, and 15N and partially assigned the rest of the 1H spectrum. Analysis of NOE and chemical shift data reveals that gVIIIp is composed of two alpha-helical domains, one ranging from Pro-6 to Glu20 and the other ranging from Tyr-24 all the way to the C-terminus Ser-50. In contrast to the results reported by Henry and Sykes [Henry, G.D., & Sykes, B.D. (1992) Biochemistry 31, 5285-5297], at a high SDS to protein ratio the protein appears to be monomeric." citations,ref_5,4209,195716,6,,reference citation,,,8411155,,"J Mol Biol 1993 Oct 5;233(3):447-63 fd coat protein structure in membrane environments. McDonnell PA, Shon K, Kim Y, Opella SJ",fd coat protein structure in membrane environments.,published,journal,J. Mol. Biol.,Journal of molecular biology,233,3,,0022-2836,,,,,,,,,,,,,,,,,,,,447,463,1993,"The membrane bound form of bacteriophage fd coat protein has a long hydrophobic membrane spanning helix and a shorter amphipathic helix in the plane of the bilayer. Residues near the N and C termini and in the turn connecting the two helices are mobile. The locations and orientations of the helical secondary structure elements and the protein backbone dynamics were characterized by combining results from multidimensional solution NMR experiments on protein samples in micelles and high resolution solid-state NMR experiments on protein samples in oriented and unoriented lipid bilayers. The coat protein is a monomer in micelles. The secondary structure of the membrane bound form of fd coat protein is very similar to that of the structural form found in the virus particles, since it is nearly all alpha helix. However, the membrane bound form of the protein differs from the structural form of the protein in virus particles in the arrangement of the secondary structure, since the membrane bound form of the protein has two distinct helical domains oriented perpendicular to each other and the structural form of the protein in the virus particles has a nearly continuous helix aligned approximately along the filament axis. In addition, there are substantial differences in the dynamics of residues in the bend between the two helices and near the C terminus, since they are mobile in the membrane bound form of the protein and not in the virus particles. Residues 1 to 5 at the N terminus are highly mobile and unstructured in both the membrane bound and structural forms of the coat protein." citations,entry_citation,421,195749,1,,entry citation,,,,,"Williamson, Michael P., ""1H Nuclear Magnetic Resonance Assignments and Secondary Structure of Porcine C5ades Arg,"" J. Mol. Biol. 206, 407-410 (1989).","1H Nuclear Magnetic Resonance Assignments and Secondary Structure of Porcine C5ades Arg",published,journal,J. Mol. Biol.,,206,,,,,,,,,,,,,,,,,,,,,,,407,410,1989, citations,entry_citation,4210,195762,1,,entry citation,,98416700,,,"Nishikawa T, Nagadoi A, Yoshimura S, Aimoto S, Nishimura Y. Solution structure of the DNA-binding domain of human telomeric protein, hTRF1. Structure 6, 1057-1065 (1998).","Solution structure of the DNA-binding domain of human telomeric protein, hTRF1",published,journal,Structure,,6,,,,,,,,,,,,,,,,,,,,,,,1057,1065,1998, citations,entry_citation,4211,195776,1,,entry citation,,,,,,A highly precise solution 1H NMR structure of ragweed allergen Amb. t. V,submitted,journal,J. Mol. Biol.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4212,195792,1,,entry citation,,99121111,,,,"Solution structure of a retro-inverso peptide analogue mimicking the foot-and-mouth disease virus major antigenic site : structural basis for its antigenic crossreactivity with the parent peptide",published,journal,J. Biol. Chem.,Journal of Biological Chemistry,274,,,,,,,,,,,,,,,,,,,,,,,3686,3692,1999, citations,entry_citation,4213,195805,1,,entry citation,,99121111,,,,"Solution structure of a retro-inverso peptide analogue mimicking the foot-and-mouth disease virus major antigenic site. Structural basis for its antigenic cross-reactivity with the parent peptide.",published,journal,J. Biol. Chem.,Journal of Biological Chemistry,274,,,,,,,,,,,,,,,,,,,,,,,3686,3692,1999, citations,entry_citation,4214,195830,1,,entry citation,,98371010,9705310,,,"High resolution structure of the N-terminal domain of tissue inhibitor of metalloproteinases-2 and characterization of its interaction site with matrix metalloproteinase-3",published,journal,J. Biol. Chem.,Journal of Biological Chemistry,273,34,,,,,,,,,,,,,,,,,,,,,,21736,21743,1998, citations,entry_citation,4226,196047,1,,entry citation,,99033050,,,,"Order, Dynamics, and Metal-Binding in the Lead-Dependent Ribozyme",published,journal,J. Mol. Biol.,Journal of Molecular Biology,284,,,,,,,,,,,,,,,,,,,,,,,325,335,1998,"Solution structure of the leadzyme reported in accompanying paper in same issue, Hoogstraten et al." citations,entry_citation,4227,196073,1,,entry citation,,99224904,,,,"The influence of C-terminal extension on the structure of the J-domain in E. Coli DNAJ",published,journal,Protein Sci.,,8,,,,,,,,,,,,,,,,,,,,,,,203,214,1999, citations,ref_1,4214,195831,2,,reference citation,,,8520220,,"Delaglio,F. et al (1995) J. Biomol NMR 6, 277-293",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref_2,4214,195832,3,,reference citation,,,,,"Bartels, C. et al., (1995) J. Biomol NMR 6, 1-10",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_3,4214,195833,4,,reference citation,,,9367762,,"Guntert, P. et al., (1997) J. Mol. Biol. 273, 283-298",Torsion angle dynamics for NMR structure calculation with the new program DYANA.,published,journal,J. Mol. Biol.,Journal of molecular biology,273,1,,0022-2836,,,,,,,,,,,,,,,,,,,,283,298,1997,"The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from distance constraints and torsion angle constraints collected by nuclear magnetic resonance (NMR) experiments performs simulated annealing by molecular dynamics in torsion angle space and uses a fast recursive algorithm to integrate the equations of motions. Torsion angle dynamics can be more efficient than molecular dynamics in Cartesian coordinate space because of the reduced number of degrees of freedom and the concomitant absence of high-frequency bond and angle vibrations, which allows for the use of longer time-steps and/or higher temperatures in the structure calculation. It also represents a significant advance over the variable target function method in torsion angle space with the REDAC strategy used by the predecessor program DIANA. DYANA computation times per accepted conformer in the ""bundle"" used to represent the NMR structure compare favorably with those of other presently available structure calculation algorithms, and are of the order of 160 seconds for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300 computer. Test calculations starting from conformers with random torsion angle values further showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures." citations,entry_citation,4215,195851,1,,entry citation,,98367505,,,,NMR Solution Structure of the Plasminogen-Activator Protein Staphylokinase,published,journal,Biochemistry,,37,30,,,,,,,,,,,,,,,,,,,,,,10635,10642,1998, citations,citation_1,4215,195852,2,,reference citation,,,,,"Bartels et al. (1995) J. Biomol. Nmr 6, 1-10.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4216,195867,1,,entry citation,,99194861,,,,"Solution structure of the transactivation domain of ATF-2 comprising a zinc finger-like subdomain and a flexible subdomain.",published,journal,J. Mol. Biol.,,287,3,,,,,,,,,,,,,,,,,,,,,,593,607,1999, citations,entry_citation,4217,195880,1,,entry citation,,98407984,,,,"NMR structure of the streptomyces metalloproteinase inhibitor, SMPI, isolated from Streptomyces nigrescens TK-23: another example of an ancestral beta gamma-crystallin precursor structure.",published,journal,J. Mol. Biol.,Journal of Molecular Biology,282,,,,,,,,,,,,,,,,,,,,,,,421,433,1998, citations,entry_citation,4218,195894,1,,entry citation,,99182423,10080898,,,"Solution structure of toxin 2 from centruroides noxius Hoffmann, a beta-scorpion neurotoxin acting on sodium channels",published,journal,J. Mol. Biol.,Journal of Molecular biology,287,,,,,,,,,,,,,,,,,,,,,,,359,367,1999, citations,entry_citation,4219,195908,1,,entry citation,,99315214,,,"Hashimoto, Y., Toma, K., Nishikido, J., Yamamoto, K., Haneda, K., Inazu, T., Valentine, K.G., and Opella, S.J., ""Effects of Glycosylation on the Structure and Dynamics of Eel Calcitonin in Micelles and Lipid Bilayers Determined by Nuclear Magnetic Resonance Spectroscopy,"" Biochemistry 38, 8377-8384 (1999).","Effects of Glycosylation on the Structure and Dynamics of Eel Calcitonin in Micelles and Lipid Bilayers Determined by Nuclear Magnetic Resonance Spectroscopy",published,journal,Biochemistry,Biochemistry,38,26,,,,,,,,,,,,,,,,,,,,,,8377,8384,1999, citations,entry_citation,422,195927,1,,entry citation,,,,,"Kobayashi, Yuji, Ohkubo, Tadayasu, Kyogoku, Yoshimasa, Nishiuchi, Yuji, Sakakibara, Shumpei, Braun, Werner, Go, Nobuhiro, ""Solution Conformation of Conotoxin GI Determined by 1H Nuclear Magnetic Resonance Spectroscopy and Distance Geometry Calculations,"" Biochemistry 28, 4853-4860 (1989).","Solution Conformation of Conotoxin GI Determined by 1H Nuclear Magnetic Resonance Spectroscopy and Distance Geometry Calculations",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,4853,4860,1989, citations,entry_citation,4220,195941,1,,entry citation,,99013448,,,,"Solution structures of human immunodeficiency virus type 1 (HIV-1) and moloney murine leukemia virus (MoMLV) capsid protein major-homology-region peptide analogs by NMR spectroscopy",published,journal,Eur. J. Biochem.,,257,,,,,,,,,,,,,,,,,,,,,,,69,77,1998, citations,entry_citation,4221,195957,1,,entry citation,,99013448,,,,"Solution Structures of Human Immunodeficiency Virus Type 1 (HIV-1) and Moloney Murine Leukemia Virus (MoMLV) Capsid Protein Major Homology Region Peptide Analogs by NMR Spectroscopy",published,journal,Eur. J. Biochem.,European Journal of Biochemistry,257,,,,,,,,,,,,,,,,,,,,,,,69,77,1998, citations,entry_citation,4222,195973,1,,entry citation,,99155206,10029527,,,"Solution structure of a sweet protein single-chain monellin determined by nuclear magnetic resonance and dynamical simulated annealing calculations",published,journal,Biochemistry,Biochemistry,38,,,,,,,,,,,,,,,,,,,,,,,2340,2346,1999, citations,entry_citation,4223,195993,1,,entry citation,,98412653,,,,"Solution Structure of a TBP-TAFII230 Complex: Protein Mimicry of the Minor Groove Surface of the TATA Box Unwound by TB",published,journal,Cell,,94,,,,,,,,,,,,,,,,,,,,,,,573,583,1998, citations,entry_citation,4224,196007,1,,entry citation,,97337457,,,,"Nuclear Magnetic Resonance Assignment and Secondary Structure of Ankyrin-like Repeat-bearing protein: Myotrophin",published,journal,Protein Sci.,Protein Science,6,,,,,,,,,,,,,,,,,,,,,,,1347,1351,1997, citations,entry_citation,4228,196087,1,,entry citation,,,,,,"The influence of c-terminal extension on the structure of the j-domain in e. coli dnaj""",published,journal,Protein Sci.,,,,,,,,,,,,,,,,,,,,,,,,,5587,5596,1998, citations,entry_citation,423,196120,1,,entry citation,,,,,"Kobayashi, Yuji, Ohkubo, Tadayasu, Kyogoku, Yoshimasa, Nishiuchi, Yuji, Sakakibara, Shumpei, Braun, Werner, Go, Nobuhiro, ""Solution Conformation of Conotoxin GI Determined by 1H Nuclear Magnetic Resonance Spectroscopy and Distance Geometry Calculations,"" Biochemistry 28, 4853-4860 (1989).","Solution Conformation of Conotoxin GI Determined by 1H Nuclear Magnetic Resonance Spectroscopy and Distance Geometry Calculations",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,4853,4860,1989, citations,entry_citation,4230,196134,1,,entry citation,,98453317,9778345,,,Solution structure of Delta 5-3-ketosteroid isomerase complexed with the steroid 19-nortestosterone hemisuccinate,published,journal,Biochemistry,,37,44,,,,,,,,,,,,,,,,,,,,,,14701,14712,1998, citations,ref_1,4230,196135,2,,reference citation,,,,,Biosym Technologies,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_2,4230,196136,3,,reference citation,,,,,"Johnson, B; Blevins, R,A J. Biomol. NMR (1994), 4, 603",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4231,196154,1,,entry citation,,,9874217,,,"Solution structure of the first artficial Fe8S8 ferredoxin: the D13C variant of Bacillus schlegelii Fe7S8 ferredoxin",published,journal,Eur. J. Biochem.,,258,,,,,,,,,,,,,,,,,,,,,,,502,514,1998, citations,entry_citation,4232,196174,1,,entry citation,,,,,"Tsuda, S., Miura, A., Gagne, S. M., Spyracopoulos, L., and Sykes, B.D., ""Low Temperature-Induced Structural Changes in the Apo Regulatory Domain of Skeletal Muscle Troponin C,"" Biochemistry 38, 5693-5700 (1999).","Low Temperature-Induced Structural Changes in the Apo Regulatory Domain of Skeletal Muscle Troponin C",published,journal,Biochemistry,Biochemistry,38,,,,,,,,,,,,,,,,,,,,,,,5693,5700,1999, citations,citation_one,4232,196175,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4233,196194,1,,entry citation,,,,,"Fletcher, J. I., Smith, R., O'Donoghue, S. I., Nilges, M., Connor, M., Howden, M. E. H., Christie, M. J., and King, G. F., ""The Structure of a Novel Insecticidal Neurotoxin, Omega-Atracotoxin-Hv1, from the Venom of an Australian Funnel Web Spider,"" Nature Struct. Biol. 4, 559-566 (1997).","The Structure of a Novel Insecticidal Neurotoxin, Omega-Atracotoxin-Hv1a, from the Venom of an Australian Funnel Web Spider",published,journal,Nature Struct. Biol.,Nature Structure Biology,4,7,,,,,,,,,,,,,,,,,,,,,,559,566,1997, citations,entry_citation,4234,196212,1,,entry citation,,98046100,,,"Fletcher, J. I., Chapman, B. E., Mackay, J. P., Howden, M. E. H., and King, G. F., ""The Structure of Versutoxin (Delta-Atracotoxin-Hv1) Provides Insights into the Binding of Site 3 Neurotoxins to the Voltage-gated Sodium Channel,"" Structure 5, 1525-1535 (1997).","The Structure of Versutoxin (Delta-Atracotoxin-Hv1) Provides Insights into the Binding of Site 3 Neurotoxins to the Voltage-gated Sodium Channel",published,journal,Structure,Structure,5,,,,,,,,,,,,,,,,,,,,,,,1525,1535,1997, citations,entry_citation,4235,196230,1,,entry citation,,99058075,,,"Aramini, J. M., Mujeeb, A., and Germann, M. W., ""NMR Solution Structures of [d(GCGAAT-3'-3'-alphaT-5'-5'-CGC)2] and its Unmodified Control,"" Nucleic Acids Res. 15, 5644-5654 (1998).","NMR Solution Structures of [d(GCGAAT-3'-3'-alphaT-5'-5'-CGC)2] and its Unmodified Control",published,journal,Nucleic Acids Res.,Nucleic Acids Research,15,,,,,,,,,,,,,,,,,,,,,,,5644,5654,1998, citations,entry_citation,4236,196245,1,,entry citation,,,11004437,,,"Solution structure of the NADP(H)-binding component (dIII) of proton-translocating transhydrogenase from Rhodospirillum rubrum",published,journal,Biochim. Biophys. Acta,,1459,,,,,,,,,,,,,,,,,,,,,,,248,257,2000, citations,entry_citation,4237,196260,1,,entry citation,,99281466,,,,"Backbone and side-chain 1H, 15N, and 13C Assignments for the Topological Specificity Domain of the MinE cell Division Protein",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,13,4,,,,,,,,,,,,,,,,,,,,,,395,396,1999, citations,entry_citation,4239,196286,1,,entry citation,,98407983,,,,"Sequence-specific 1H, 13C and 15N assignment of the single-stranded DNA binding protein of the bacteriophage phi 29.",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,13,,,,,,,,,,,,,,,,,,,,,,,303,304,1999, citations,entry_citation,4240,196303,1,,entry citation,,97470529,,,,"Solution structure of the minor conformer of a DNA duplex containing a DG mismatch opposite a benzo[a]pyrene diol epoxide/DA adduct: glycosidic rotation from syn to anti at the modified deoxyadenosine",published,journal,Biochemistry,,36,37,,,,,,,,,,,,,,,,,,,,,,11069,11076,1997, citations,ref_1,4240,196304,2,,reference citation,,97470529,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_2,4240,196305,3,,reference citation,,96027474,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_3,4240,196306,4,,reference citation,,,,,"Meadows, R., Post, C. B., Luxon B. A., & Gorenstein, D. G. (1996) MORASS",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_4,4240,196307,5,,reference citation,,,,,"Pearlman, D. A., Case, D. A., Caldwell, J. C., Ross, W. L., Cheatham, T. E., Ferguson, D. M., Seibel, G. L., Singh, U. C., Weiner, P. K., & Kollman, P. A. (1995) AMBER 4.1",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_5,4240,196308,6,,reference citation,,,7827084,,"Yeh, H. J. C. et al. (1995) Biochemistry 34, 1364-1375.","NMR solution structure of a nonanucleotide duplex with a dG mismatch opposite a 10R adduct derived from trans addition of a deoxyadenosine N6-amino group to (-)-(7S,8R,9R,10S)-7,8-dihydroxy-9,10-epoxy-7,8,9,10- tetrahydrobenzo[a]pyrene.",published,journal,Biochemistry,Biochemistry,34,4,,0006-2960,,,,,,,,,,,,,,,,,,,,1364,1375,1995,"A nonanucleotide in which (-)-(7S,8R,9R,10S)-7,8-dihydroxy-9,10-epoxy- 7,8,9,10-tetrahydrobenzo[a]pyrene (7-hydroxy group and epoxide oxygen are trans) is covalently bonded to the exocyclic N6-amino group of deoxyadenosine through trans addition at C10 of the epoxide (10R adduct) has been synthesized. The modified oligonucleotide d(GGTCA*CGAG) was incorporated into the duplex d(GGTCA*CGAG).d(CTCGGGACC), containing a dG mismatch opposite the modified base (dA*). Proton assignments for the solution structure of the duplex containing the 10R adduct were made using 2D TOCSY and NOESY NMR spectra. The complete hybrid relaxation matrix program, MORASS2.0, was used to generate NOESY distance constraints for iterative refinement using distance-restrained molecular dynamics calculations with AMBER4.0. The iteratively refined structure showed the hydrocarbon intercalated from the major groove immediately below the dC4-dG15 base pair and oriented toward the 5'-end of the modified strand. The modified dA is in an anti configuration, with the dG of the GA mismatch turned out into the major groove. Chemical shifts of the hydrocarbon protons and unusual chemical shifts of sugar protons were accounted for by this orientation of the adduct. The information available currently provides the foundation for the rational explanation of observed benzo[a]pyrene (BaP) structures and predictions for other BaP dG and dA adducts." citations,citation_one,4241,196333,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4242,196358,1,,entry citation,,,,,"Haaf, A., LeClaire, L. III, Roberts, G., Kent, H. M., Roberts, T. M., Stewart, M., and Neuhaus, D., ""Solution Structure of the Motile Major Sperm Protein (MSP) of Ascaris suum - Evidence for Two Manganese Binding Sites and the Possible Role of Divalent Cations in Filament Formation,"" J. Mol. Biol. 284, 1611-1623 (1998).","Solution Structure of the Motile Major Sperm Protein (MSP) of Ascaris suum - Evidence for Two Manganese Binding Sites and the Possible Role of Divalent Cations in Filament Formation.",published,journal,J. Mol. Biol.,,284,5,,,,,,,,,,,,,,,,,,,,,,1611,1623,1998, citations,citation_one,4242,196359,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4243,196376,1,,entry citation,,98035724,,,,"Centromeric pyrimidine strands fold into an intercalated motif by forming a double hairpin with a novel T:G:G:T tetrad: solution structure of the D(TCCCGTTTCCA) dimer",published,journal,J. Mol. Biol.,Journal of Molecular Biology,273,,,,,,,,,,,,,,,,,,,,,,,840,856,1997, citations,citation_one,4243,196377,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4244,196400,1,,entry citation,,99058075,9837995,,"Aramini J. M., Mujeeb A., and Germann M. W., ""NMR Solution Structures of [d(GCGAAT-3'-3'-alphaT-5'-5'-CGC)2] and its Unmodified Control,"" Nucleic Acids Res. 26, 5644-5654 (1998).","NMR Solution Structures of [d(GCGAAT-3'-3'-alphaT-5'-5'-CGC)2] and its Unmodified Control",published,journal,Nucleic Acids Res.,,26,24,,,,,,,,,,,,,,,,,,,,,,5644,5654,1998, citations,primary_citation,4245,196417,1,,entry citation,,99169958,,,"Lee, A. L. and Wand, A. J., ""Assessing Potential Bias in the Determination of Rotational Correlation Times of Proteins by NMR Relaxation"", J. Biomol. NMR, 13, 101-112 (1999).","Assessing Potential Bias in the Determination of Rotational Correlation Times of Proteins by NMR Relaxation",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,13,2,,,,,,,,,,,,,,,,,,,,,,101,112,1999, citations,citation_one,4245,196418,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR",,journal,J. Biomol. NMR,,6,2,,,,,,,,,,,,,,,,,,,,,,135,140,1995, citations,entry_citation,4246,196443,1,,entry citation,,20178923,,,"Zhukov, I., Bolewska, K., and Bierzynski, A., ""Conservative Mutation Met8-->Leu Affects the Folding Process and Structural Stability of Squash Trypsin Inhibitor CMTI-I,"" Protein Sci. 9, 273-279 (2000).","Conservative Mutation Met8-->Leu Affects the Folding Process and Structural Stability of Squash Trypsin Inhibitor CMTI-I",published,journal,Protein Sci.,Protein Science,9,,,,,,,,,,,,,,,,,,,,,,,273,279,2000, citations,citation_one,4246,196444,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,citation_two,4246,196445,3,,reference citation,,,,,"Bartels, C., Xia, T., Guntert, P., Billeter, M. & Wuthrich,K. The program Xeasy for computer-supported NMR spectral analysis. J. Biomol. NMR 5, 1-10 (1995).",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4247,196462,1,,entry citation,,99281462,,,"Szyperski, T., Goette, M., Billeter, M., Perola, E., Celai, L., Heumann, H., and Wuthrich, K., ""NMR Structure of the Chimeric Hybrid Duplex r(gcaguggc). r(gcca)d(CTGC) Comprising the tRNA-DNA Junction Formed During Initiation of HIV-1 Reverse Trancription."" J. Biomol. NMR, 13(4), 343-355 (1999).","NMR Structure of the Chimeric Hybrid Duplex r(gcaguggc). r(gcca)d(CTGC) Comprising the tRNA-DNA Junction Formed During Initiation of HIV-1 Reverse Trancription",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,13,4,,,,,,,,,,,,,,,,,,,,,,343,355,1999, citations,entry_citation,4248,196481,1,,entry citation,,,,,,"Structural basis for DNA bending by the architectural transcription factor LEF-1",published,journal,Nature,,376,,,,,,,,,,,,,,,,,,,,,,,791,,1995, citations,entry_citation,4249,196521,1,,entry citation,,98363214,,,"Ikegami, T., Kuraoka, I., Saijo, M., Kodo, N., Kyogoku, Y., Morikawa, K., Tanaka, K., and Shirakawa, M., ""Solution Structure of the DNA- and RPA-binding Domain of the Human Repair Factor XPA,"" Nat. Struct. Biol. 5, 701-706 (1998).","Solution Structure of the DNA- and RPA-binding Domain of the Human Repair Factor XPA",published,journal,Nat. Struct. Biol.,,5,8,,,,,,,,,,,,,,,,,,,,,,701,706,1998, citations,citation_one,4249,196522,2,,reference citation,,,,,"Cavanagh, J., Fairbrother, W. J., Palmer III, A. G., and Skelton, N. J. Protein NMR Spectroscopy, p. 176, Academic Press, Inc. (1996).",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,4373,199086,2,,reference citation,,,,,"Bartels, C., T. Xia, M. Billeter, P. Guntert, and K. Wutrich, `The program {Xeasy} for computer -supported {NMR} spectral analysis of biological macromolecules', J. Biol. NMR, 6, 1-10 (1994).",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_two,4249,196523,3,,reference citation,,,8520220,,"Delaglio, F. et al. (1994) J. Biomol. NMR 6, 277-293.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,citation_three,4249,196524,4,,reference citation,,,,,"Garrett, D.S. (1991) J. Magn. Reson. 95, 214-220.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4250,196545,1,,entry citation,,9857204,,,,Structure of the 3' hairpin of the TYMV pseudoknot: Preformation in RNA folding,published,journal,EMBO J.,,17,24,,,,,,,,,,,,,,,,,,,,,,7498,7504,1998, citations,citation_one,4250,196546,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,citation_two,4250,196547,3,,reference citation,,,8520220,,"Delaglio, F. et al. J.Biomol.NMR 6, 277-293 (1994).",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,citation_three,4250,196548,4,,reference citation,,,,,"Garrett, D.S. J.Magn.Reson. 95, 214-220 (1991).",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4251,196566,1,,entry citation,,99356753,,,,"Triple resonance-based assignment for Abl SH(32) and its complex with a consolidated ligand",published,journal,J. Biomol. NMR,,14,2,,,,,,,,,,,,,,,,,,,,,,187,188,1999, citations,citation_one,4251,196567,2,,reference citation,,,,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).",,published,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4252,196578,1,,entry citation,,99356753,,,,"Triple resonance-based assignment for Abl SH(32) and its complex with a consolidated ligand",published,journal,J. Biomol. NMR,,14,2,,,,,,,,,,,,,,,,,,,,,,187,188,1999, citations,citation_one,4252,196579,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4253,196595,1,,entry citation,,99146782,,,"Holland, J.A., Hansen, M.R., Du, Z., and Hoffman, D.W., ""An Examination of Coaxial Stacking of Helical Stems in a Pseudoknot Motif: the Gene 32 Messenger RNA Pseudoknot of Bacteriophage T2,"" RNA 5, 257-271 (1999).","An Examination of Coaxial Stacking of Helical Stems in a Pseudoknot Motif: the Gene 32 Messenger RNA Pseudoknot of Bacteriophage T2",published,journal,RNA,RNA,5,2,,,,,,,,,,,,,,,,,,,,,,257,271,1999, citations,citation_one,4253,196596,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4263,196797,1,,entry citation,,99061335,,,"Li, S. C., Zwahlen, C., Vincent, S. J., McGlade, C. J., Kay, L. E., Pawson, T., and Forman-Kay, J. D., ""Structure of a Numb PTB Domain-peptide Complex Suggests a Basis for Diverse Binding Specificity,"" Nat. Struct. Biol. 5, 1075-1083 (1998).","Structure of a Numb PTB Domain-peptide Complex: A Basis for Diverse Binding Specificity",published,journal,Nat. Struct. Biol.,Nature Structural Biology,5,,,,,,,,,,,,,,,,,,,,,,,1075,1083,1998, citations,entry_citation,4254,196620,1,,entry citation,,99281467,,,"McIntosh, P.B., Taylor, I.A., Smerdon, S.J., Frenkiel, T.A., and Lane, A.N., ""1H, 15N and 13C Assignments of the DNA Binding Domain of Transcription Factor Mbp1 from Saccharomyces cerevisiae in Both Its Free and DNA Bound Forms and 1H Assignments of the Free DNA"", J. Biomol. NMR, 13(4), 397-398,(1999).","1H, 15N and 13C Assignments of the DNA Binding Domain of Transcription Factor Mbp1 from Saccharomyces cerevisiae in Both Its Free and DNA Bound Forms and 1H Assignments of the Fee DNA",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,13,4,,,,,,,,,,,,,,,,,,,,,,397,398,1999, citations,citation_one,4254,196621,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,citation_two,4254,196622,3,,reference citation,,,,,"Bartels, C., Xia, T., Guntert, P., Billeter, M. & Wuthrich,K. The Program Xeasy for Computer-Supported NMR Spectral Analysis. J. Biomol. NMR 5, 1-10 (1995).",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4255,196635,1,,entry citation,,99246285,,,,Structure and interactions of the translation initiation factor eIF1,published,journal,EMBO J.,,4,18,,,,,,,,,,,,,,,,,,,,,,2631,2637,1999, citations,entry_citation,4256,196650,1,,entry citation,,99281467,,,"McIntosh, P.B., Taylor, I.A., Smerdon, S.J., Frenkiel, T.A., and Lane, A.N., ""1H, 15N and 13C Assignments of the DNA Binding Domain of Transcription Factor Mbp1 from S. cerevisiae in Both its Free and DNA Bound Forms, and 1H Assignments of the Free DNA,"" J. Biomol. NMR 13, 397-398 (1999).","1H, 15N and 13C Assignments of the DNA Binding Domain of Transcription Factor Mbp1 from S. cerevisiae in Both Its Free and DNA Bound Forms, and 1H Assignments of the Free DNA",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,13,4,,,,,,,,,,,,,,,,,,,,,,397,398,1999, citations,citation_one,4256,196651,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,citation_two,4256,196652,3,,reference citation,,,,,"Bartels, C., Xia, T., Guntert, P., Billeter, M. & Wuthrich,K. The program Xeasy for computer-supported NMR spectral analysis. J. Biomol. NMR 5, 1-10 (1995).",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4257,196665,1,,entry citation,,99126539,,,,"NMR Structure of the (52-96) C-Terminal Domain of the HIV-1 Regulatory Protein Vpr : Molecular Insights into its Biological Functions",published,journal,J. Mol. Biol.,Journal of Molecular Biology,285,5,,,,,,,,,,,,,,,,,,,,,,2105,2117,1999, citations,cit1,4257,196666,2,,reference citation,,,,,"Bruker Spectrospin, Karlsruhe, Germany",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,cit2,4257,196667,3,,reference citation,,,,,MSI Molecular Simulations Inc.,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4258,196688,1,,entry citation,,99281467,,,,"1H, 15N and 13C Assignments of the DNA Binding Domain of Transcription Factor Mbp1 from Saccharomyces cerevisiae in Both Its Free and DNA Bound Forms and H1 Assignments of the Free DNA",published,journal,J. Biomol. NMR,,13,4,,,,,,,,,,,,,,,,,,,,,,397,398,1999, citations,entry_citation,4259,196701,1,,entry citation,,99311320,,,,"Sequential Assignment and Solution Secondary Structure of Doubly Labelled Ribonuclease Sa",published,journal,J. Biomol. NMR,,14,1,,,,,,,,,,,,,,,,,,,,,,89,90,1999, citations,citation_one,4259,196702,2,,reference citation,,,10382311,,"Laurents, DV, Perez-Ca?adillas, JM, Santoro, J, Rico, M. Schell, D, Hebert, EJ, Pace, CN & Bruix, M. ""Sequential Assignment and Solution Secondary Strucuture of Doubly Labbelled Ribonuclease Sa"" for submission to J. Biomol. NMR (1998)",Sequential assignment and solution secondary structure of doubly labelled ribonuclease Sa.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,14,1,,0925-2738,,,,,,,,,,,,,,,,,,,,89,90,1999, citations,citation_two,4259,196703,3,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,426,196721,1,,entry citation,,,,,"Simonneaux, Gerard, Bondon, Arnaud, Sodano, Patrick, Sinbandhit, Sourisak, ""Proton nuclear Overhauser effect investigation of the heme pocket expansion in trimethyl phosphine sperm whale myoglobin,"" Biochim. Biophys. Acta 999, 42-45 (1989).","Proton nuclear Overhauser effect investigation of the heme pocket expansion in trimethyl phosphine sperm whale myoglobin",published,journal,Biochim. Biophys. Acta,,999,,,,,,,,,,,,,,,,,,,,,,,42,45,1989, citations,entry_citation,4260,196734,1,,entry citation,,99315214,,,"Hashimoto, Y., Toma, K., Nishikido, J., Yamamoto, K., Haneda, K., Inazu, T., Valentine, K.G., and Opella, S.J., ""Effects of Glycosylation on the Structure and Dynamics of Eel Calcitonin in Micelles and Lipid Bilayers Determined by Nuclear Magnetic Resonance Spectroscopy,"" Biochemistry 38, 8377-8384 (1999).","Effects of Glycosylation on the Structure and Dynamics of Eel Calcitonin in Micelles and Lipid Bilayers Determined by Nuclear Magnetic Resonance Spectroscopy",published,journal,Biochemistry,Biochemistry,38,26,,,,,,,,,,,,,,,,,,,,,,8377,8384,1999, citations,entry_citation,4261,196754,1,,entry citation,,99315214,,,,Effects of Glycosylation on the Structure and Dynamics of Eel Calcitonin in Micelles and Lipid Bilayers Determined by NMR Spectroscopy,published,journal,Biochemistry,Biochemistry,38,26,,,,,,,,,,,,,,,,,,,,,,8377,8384,1999, citations,entry_citation,4262,196770,1,,entry citation,,10091649,,,,"Structure and dynamics in solution of the complex of Lactobillus casei dihydrofolate reductase with the new lipophilic antifolate drug trimetrexate""",published,journal,Protein Sci.,Protein Science,8,,,,,,,,,,,,,,,,,,,,,,,467,481,1999, citations,ref_1,4263,196798,2,,reference citation,,9207069,,,"Li SC, Songyang Z, Vincent SJ, Zwahlen C, Wiley S, Cantley L, Kay LE, Forman-Kay J, Pawson T, ""High-affinity binding of the Drosophila Numb phosphotyrosine-binding domain to peptides containing a Gly-Pro-(p)Tyr motif,"" Proc Natl Acad Sci U S A 1997 Jul 8;94(14):7204-9","High-affinity binding of the Drosophila Numb phosphotyrosine-binding domain to peptides containing a Gly-Pro-(p)Tyr motif",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,94,14,,,,,,,,,,,,,,,,,,,,,,7204,7209,1997, citations,entry_citation,4264,196820,1,,entry citation,,99140298,,,,"Solution structure of the 40,000 Mr phosphoryl transfer complex between the N-terminal domain of enzyme I and HPr.",published,journal,Nat. Struct. Biol.,Nature Structural Biology,6,,,,,,,,,,,,,,,,,,,,,,,166,173,1999, citations,entry_citation,4265,196846,1,,entry citation,,,,,"Wu, H., Maciejewski, M.W., Benashski, S.E., Mullen, G.P., and King, S.M., ""1H, 15N and 13C Resonance Assignments for the 22KDa LC1 Light Chain from Chlamydomonas Outer Arm Dynein,"" in preparation (1999)","1H, 15N and 13C Resonance Assignments for the 22KDa LC1 Light Chain from Chlamydomonas Outer Arm Dynein",submitted,journal,to be published,,,,,,,,,,,,,,,,,,,,,,,,,,,1999, citations,entry_citation,4266,196877,1,,entry citation,,99190073,,,"Kurapkat, G., Siedentop, M., Gattner, H-G., Hagelstein, M., Brandenburg, D., Grotzinger, J., and Wollmer, A., ""The Solution Structure of a Superpotent B-chain-shortened Single-replacement Insulin Analogue,"" Protein Sci. 8, 499- 508 (1999).","The Solution Structure of a Superpotent B-chain-shortend Single-replacement Insulin Analogue",published,journal,Protein Sci.,Protein Science,8,,,,,,,,,,,,,,,,,,,,,,,499,508,1999, citations,entry_citation,4267,196890,1,,entry citation,,99272561,,,"Coles, M., Diercks, T., Muehlenweg, B., Bartsch, S., Zoelzer, V., Tschesche, H., and Kessler, H., ""The Solution Structure and Dynamics of Human Neutrophil Gelatinase-associated Lipocalin,"" J. Mol. Biol. 289, 139-157 (1999).","The Solution Strucuture and Dynamics of Human Neutrophil Gelatinase-associated Lipocalin.",published,journal,J. Mol. Biol.,Journal of Molecular Biology,289,1,,,,,,,,,,,,,,,,,,,,,,139,157,1999, citations,entry_citation,4268,196922,1,,entry citation,,98322084,,,"Aono, S., Bentrop, D., Bertini, I., Donaire, A., Luchinat, C., Niikura, Y., and Rosato, A., ""Solution Structure of the Oxidized Fe7S8 Ferredoxin from the Thermophilic Bacterium Bacillus Schlegelii by 1H NMR Spectroscopy,"" Biochemistry 37, 9812-9826 (1998).","Solution Structure of the Oxidized Fe7S8 Ferredoxin from the Thermophilic Bacterium Bacillus Schlegelii by 1H NMR Spectroscopy",published,journal,Biochemistry,,37,,,,,,,,,,,,,,,,,,,,,,,9812,9826,1998, citations,entry_citation,4269,196941,1,,entry citation,,99229459,,,"Pan, B., and Mullen, G. P., ""1H, 15N and 13C Chemical Shift Assignments for the Catalytic Core of Resolvase,"" J. Biomol. NMR 13, 307-308 (1999).","1H, 15N and 13C Chemical Shift Assignments for the Catalytic Core of Resolvase",published,journal,J. Biomol. NMR,,13,,,,,,,,,,,,,,,,,,,,,,,307,308,1999, citations,entry_citation,4270,196967,1,,entry citation,,99396734,,,"Osawa, M., Tokumitsu, H., Swindells, M.B., Kurihara, H., Orita, M., Shibanuma, T., Furuya, T., Ikura, M., ""A Novel Target Recognition Revealed by Calmodulin in Complex with Ca2+-calmodulin-dependent Kinase Kinase,"" Nat. Struct. Biol. 6, 819-824 (1999).",A Novel Target Recognition Revealed by Calmodulin in Complex with Ca2+-calmodulin-dependent Kinase Kinase,published,journal,Nat. Struct. Biol.,,6,9,,,,,,,,,,,,,,,,,,,,,,819,824,1999, citations,entry_citation,4271,196985,1,,entry citation,,99311322,,,,"Sequence Specific 1H, 13C and 15N Assignments of a Calcium Binding Protein from Entamoeba Histolytica",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,14,1,,,,,,,,,,,,,,,,,,,,,,93,94,1999, citations,entry_citation,4272,197010,1,,entry citation,,99410887,,,"Hazzard, J., Sudhof, T. C., and Rizo, J., ""NMR analysis of the structure of synaptobrevin and of its interaction with syntaxin,"" J. Biomol. NMR, 14, 203-207 (1999).","NMR analysis of the structure of synaptobrevin and of its interaction with syntaxin",published,journal,J. Biomol. NMR,Journal of Biomoelcular NMR,14,,,,,,,,,,,,,,,,,,,,,,,203,207,1999, citations,entry_citation,4273,197032,1,,entry citation,,99227076,,,,"Candidacidal Activity Prompted by N-terminus Histatin-like Domain of Human Salivary Mucin (MUC7)",published,journal,Biochim. Biophys. Acta,Biochimica et Biophysica Acta,1431,1,,,,,,,,,,,,,,,,,,,,,,107,119,1999, citations,citation_1,4273,197033,2,,reference citation,,,3286634,,"F.G. Oppenheim, T. Xu, F.M. McMillan, S.M. Levitz, R.D. Diamond, G.D. Offner, R.F. Troxler, J. Biol. Chem. 263 (1988) 7472-7477.","Histatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans.",published,journal,J. Biol. Chem.,The Journal of biological chemistry,263,16,,0021-9258,,,,,,,,,,,,,,,,,,,,7472,7477,1988,"Histatins 1, 3, and 5 from human parotid secretion were isolated by gel filtration on Bio-Gel P-2 and reverse phase high performance liquid chromatography. The complete amino acid sequences of histatins determined by automated Edman degradation of the proteins, Staphylococcus aureus V8 protease, and tryptic peptides, are as follows: (Sequence: see text). Histatins 1, 3, and 5 contain 38, 32, and 24 amino acid residues, have molecular weights of 4929, 4063, and 3037, respectively, and contain 7 residues of histidine. Histatin 1 contains 1 mol of phosphate/mol of protein; histatins 3 and 5 lack phosphate. With the exception of Glu (residue 4) and Arg (residue 11) in histatin 1, the first 22 amino acid residues of all three histatins are identical, and the carboxyl-terminal 7 residues of histatins 1 and 3 are also identical. The sequence, -Glu-Phe-Pro-Phe-Tyr-Gly-Asp-Tyr-Gly- (residues 23-29), in histatin 1 is absent in histatin 3; and the sequence, -Gly-Tyr-Arg- (residues 23-25), in histatin 3 is absent in histatin 1. The complete sequence of histatin 5 is contained within the amino terminal 24 residues of histatin 3. The structural data suggest that histatins 1 and 3 are derived from different structural genes, whereas histatin 5 is a proteolytic product of histatin 3. All three histatins exhibit the ability to kill the pathogenic yeast, Candida albicans." citations,ref_1,4281,197144,2,,reference citation,,,,,"Hartel et al, Eur. J. Biochem v. 129, 343-357 (1982) and Orbons, et al, IBID, v 170, 225-239 (1987).",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_2,4281,197145,3,,reference citation,,,,,"Live, D.H. et al, JACS, v. 106, 1939-1941 (1984) and Bax and Subramanian, J. Mag. Res., v. 67, 565-569 (1986)",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4282,197173,1,,entry citation,,99281465,,,,"1H, 15N, and 13C Resonance Assignments for the N-terminal 20 kDa Domain of the DNA Single-Strand Break Repair Protein XRCC1",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,13,,,,,,,,,,,,,,,,,,,,,,,393,394,1999, citations,entry_citation,4283,197204,1,,entry citation,,99216534,,,"Fattorusso, R., Pellecchia, M., Viti, F., Neri, P., Neri, D. and Wuthrich, K. ""NMR structure of the human oncofoetal fibronectin ED-B domain, a specific marker for angiogenesis,"" Structure 7, 381-390 (1999).",NMR Structure of the Angiogenesis Marker Oncofoetal Fibronectin ED-B Domain,published,journal,Structure,,7,4,,,,,,,,,,,,,,,,,,,,,,381,390,1999, citations,ref-3,4293,197412,4,,reference citation,,,2646600,,"Eaton, T. & James, R. Nucleic Acids Res. 17, 1761-1761 (1989).",Complete nucleotide sequence of the colicin E9 (cei) gene.,published,journal,Nucleic Acids Res.,Nucleic acids research,17,4,,0305-1048,,,,,,,,,,,,,,,,,,,,1761,1761,1989, citations,citation_2,4273,197034,3,,reference citation,,,1747107,,"N. Ramasubbu, M.S. Reddy, E.J. Bergey, G. Haraszthy, S-D. Soni, M.J. Levine, Biochem. J. 280 (1991) 341-352.",Large-scale purification and characterization of the major phosphoproteins and mucins of human submandibular-sublingual saliva.,published,journal,Biochem. J.,The Biochemical journal,280 ( Pt 2),,,0264-6021,,,,,,,,,,,,,,,,,,,,341,352,1991,"The major components of human submandibular-sublingual saliva (HSMSL) are mucins, amylases, cystatins, proline-rich proteins and statherin. Structure-function studies of these molecules have been hampered by the small amounts of purified materials that can be isolated from human secretions. The present study describes an integrated purification protocol for the large-scale preparation of many of these molecules. To dissociate partially heterotypic complexes among salivary molecules, HSMSL was initially fractionated into four pools by gel filtration with 6 M-guanidine hydrochloride. Subsequent fractionation of these four pools by gel-filtration and ion-exchange chromatography resulted in the purification of high- and low-Mr mucins, neutral and acidic cystatins, acidic and basic proline-rich proteins and statherin. Many variants or isoforms of these salivary molecules have been identified and biochemically characterized. Biochemical studies indicated that the low-Mr mucin exists as two isoforms which vary in their sialic acid to fucose ratios. Three isoforms of acidic cystatin S were characterized which differ in their phosphate content. Two isoforms of a basic proline-rich peptide were identified; the smaller peptide was a truncated form missing the first seven amino acids." citations,citation_3,4273,197035,4,,reference citation,,,7690757,,"L.A. Bobek, H. Tsai, A.R. Biesbrock, M.J. Levine, J. Biol. Chem. 268 (1993) 20563-20569.","Molecular cloning, sequence, and specificity of expression of the gene encoding the low molecular weight human salivary mucin (MUC7).",published,journal,J. Biol. Chem.,The Journal of biological chemistry,268,27,,0021-9258,,,,,,,,,,,,,,,,,,,,20563,20569,1993,"Previous biochemical studies have determined that human saliva contains high and low molecular weight mucin glycoproteins (MG1 and MG2, respectively) that are structurally distinct. In this study, we describe the isolation and characterization of overlapping cDNA clones which code for the MG2 protein core. DNA sequencing revealed a translated region of 1131 nucleotides encoding a protein of 377 amino acid residues with a molecular mass of 39 kDa. The first 20 N-terminal residues were very hydrophobic and probably comprise the MG2 leader peptide. The region encoding the secreted protein can be divided into three distinct domains; unique 5'- and 3'-translated regions containing 4 and 1 potential N-glycosylation sites, respectively, and a central region of six almost perfect tandem repeats of 23 amino acid residues with a high number of Thr and Ser. No sequence homology with any other human or animal mucins, and no significant homology to any other proteins was found. MG2 mRNA is about 2.5 kilobases long, and its expression appears to be species-, tissue-, and cell-specific. We propose to name this gene MUC7 in accordance with the mucin genes cloned to date named MUC1-MUC6." citations,citation_4,4273,197036,5,,reference citation,,,9881747,,"T.L. Gururaja, N. Ramasubbu, P. Venugopalan, M.S. Reddy, K. Ramalingam, M.J. Levine, Glycoconjugate J. 15 (1998) 457-467.","Structural features of the human salivary mucin, MUC7.",published,journal,Glycoconj. J.,Glycoconjugate journal,15,5,,0282-0080,,,,,,,,,,,,,,,,,,,,457,467,1998,"Human salivary mucin (MUC7) is characterized by a single polypeptide chain of 357 aa. Detailed analysis of the derived MUC7 peptide sequence reveals five distinct regions or domains: (1) an N-terminal basic, histatin-like domain which has a leucine-zipper segment, (2) a moderately glycosylated domain, (3) six heavily glycosylated tandem repeats each consisting of 23 aa, (4) another heavily glycosylated MUC1- and MUC2-like domain, and (5) a C-terminal leucine-zipper segment. Chemical analysis and semi-empirical prediction algorithms for O-glycosylation suggested that 86/105 (83%) Ser/Thr residues were O-glycosylated with the majority located in the tandem repeats. The high (approximately 25%) proline content of MUC7 including 19 diproline segments suggested the presence of polyproline type structures. CD studies of natural and synthetic diproline-rich peptides and glycopeptides indicated that polyproline type structures do play a significant role in the conformational dynamics of MUC7. In addition, crystal structure analysis of a synthetic diproline segment (Boc-Ala-Pro-OBzl) revealed a polyproline type II extended structure. Collectively, the data indicate that the polyproline type II structure, dispersed throughout the tandem repeats, may impart a stiffening of the backbone and could act in consort with the glycosylated segments to keep MUC7 in a semi-rigid, rod shaped conformation resembling a 'bottle-brush' model." citations,entry_citation,4276,197053,1,,entry citation,,20093118,10625440,,,"Solution structure and dynamics of the plasminogen kringle 2-AMCHA complex: 3(1)-helix in homologous domains",published,journal,Biochemistry,,38,,,,,,,,,,,,,,,,,,,,,,,15741,15755,1999, citations,entry_citation,4278,197073,1,,entry citation,,,,,"Laajoki, L. G., Milner, S. J., Francis, G. L., Carver, J. A., and Keniry, M. A., ""1H and 15N Assignments of Long-[L60]-IGF-I, an Insulin-Like Growth Factor I Analogue,"" J. Biomol. NMR, submitted (1999).","1H and 15N Assignments of Long-[L60]-IGF-I, an Insulin-Like Growth Factor I Analogue",submitted,journal,J. Biomol. NMR,,,,,,,,,,,,,,,,,,,,,,,,,,,1999, citations,citation_one,4278,197074,2,,reference citation,,,,,"Bartels,C., Xia,T-H., Billeter,M., Geuntert,P. and Wuthrich,K. J. Biomolecular NMR, 6, 1-10 (1995).",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_two,4278,197075,3,,reference citation,,,,,"Varian Associates, Palo Alto, CA",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_three,4278,197076,4,,reference citation,,,,,"Bartels,C., Xia,T-H., Billeter,M., Geuntert,P and Wuthrich,K. (1995) J.Biomolecular NMR, 6, 1-10.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4279,197100,1,,entry citation,,99119324,,,"Jablonsky, M. J., Jackson, P. L., Trent, J. O., Watt, D. D., and Krishna, N. R., ""Solution Structure of a beta-Neurotoxin from the New World Scorpion Centruroides sculpturatus Ewing"", Biochem. Biophys. Res. Commun., 254, 406-412(1999).","Solution Structure of a beta-Neurotoxin from the New World Scorpion Centruroides sculpturatus Ewing",published,journal,Biochem. Biophys. Res. Commun.,Biochemical and Biophysical Research Communications,254,,,,,,,,,,,,,,,,,,,,,,,406,412,1999, citations,entry_citation,428,197116,1,,entry citation,,,,,"Otter, Albin, Kotovych, George, Scott, Paul G., ""Solution Conformation of the Type I Collagen alpha-1 Chain N-Telopeptide Studied by 1H NMR Spectroscopy,"" Biochemistry 28, 8003-8010 (1989).","Solution Conformation of the Type I Collagen alpha-1 Chain N-Telopeptide Studied by 1H NMR Spectroscopy",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,8003,8010,1989, citations,entry_citation,4280,197130,1,,entry citation,,,,,"Wakefield R.I.D., Smith B.O., Nan X.S., Free A., Soteriou A., Uhrin D., Bird A.P., and Barlow P.N., ""The solution structure of the domain from MeCP2 that binds to methylated DNA"", J. Mol. Biol. 291, 1055-1065 (1999).",The solution structure of the domain from MeCP2 that binds to methylated DNA,published,journal,J. Mol. Biol.,,291,5,,,,,,,,,,,,,,,,,,,,,,1055,1065,1999, citations,entry_citation,4281,197143,1,,entry citation,,,,,,"Revised structure of the AbrB N-terminal domain unifies a diverse superfamily of putative DNA-binding proteins",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_one,4283,197205,2,,reference citation,,,9729785,,"Markley et al, J. Biomol. NMR, 12 (1998), 1-23.",Recommendations for the presentation of NMR structures of proteins and nucleic acids. IUPAC-IUBMB-IUPAB Inter-Union Task Group on the Standardization of Data Bases of Protein and Nucleic Acid Structures Determined by NMR Spectroscopy.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,12,1,,0925-2738,,,,,,,,,,,,,,,,,,,,1,23,1998,"The recommendations presented here are designed to support easier communication of NMR data and NMR structures of proteins and nucleic acids through unified nomenclature and reporting standards. Much of this document pertains to the reporting of data in journal articles; however, in the interest of the future development of structural biology, it is desirable that the bulk of the reported information be stored in computer-accessible form and be freely accessible to the scientific community in standardized formats for data exchange. These recommendations stem from an IUPAC-IUBMB-IUPAB inter-union venture with the direct involvement of ICSU and CODATA. The Task Group has reviewed previous formal recommendations and has extended them in the light of more recent developments in the field of biomolecular NMR spectroscopy. Drafts of the recommendations presented here have been examined critically by more than 50 specialists in the field and have gone through two rounds of extensive modification to incorporate suggestions and criticisms." citations,entry_citation,4284,197221,1,,entry citation,,99425120,,,"Elshorst, B., Hennig, M., Foersterling, H., Diener, A., Maurer, M., Schulte P., Schwalbe, H., Griesinger, C., Krebs, J., Schmid, H., Vorherr, T., and Carafoli, E., ""NMR Solution Structure of a Complex of Calmodulin with a Binding Peptide of the Ca2+-Pump,"" Biochemistry 38, 12320-12332 (1999).","NMR Solution Structure of a Complex of Calmodulin with a Binding Peptide of the Ca2+-Pump",published,journal,Biochemistry,,38,,,,,,,,,,,,,,,,,,,,,,,12320,12332,1999, citations,entry_citation,4285,197256,1,,entry citation,,99311321,,,"Baldisseri, D. M., Rustandi, R. R., Zhong, Z., Tang, C., Bair, C. L., Landar, A., Landar, A., Zimmer, D. B., and Weber, D. J., ""1H, 13C and 15N NMR Sequence-Specific Resonance Assignments for Rat Apo-S100A1(aa),"" J. Biomol. NMR 14, 91-92 (1999).","1H, 13C and 15N NMR Sequence-Specific Resonance Assignments for Rat Apo-S100A1(aa).",published,journal,J. Biomol. NMR,,14,1,,,,,,,,,,,,,,,,,,,,,,91,92,1999, citations,entry_citation,4286,197272,1,,entry citation,,99140290,,,"Fiebig, K. M., Rice, L. M., Pollock, E., and Brunger, A. T., ""Folding Intermediates of SNARE Complex Assembly,"" Nat. Struct. Biol. 6, 117-123 (1999).",Folding Intermediates of SNARE Complex Assembly,published,journal,Nat. Struct. Biol.,Nature Structural Biology,6,2,,,,,,,,,,,,,,,,,,,,,,117,123,1999, citations,entry_citation,4287,197290,1,,entry citation,,99140290,,,"Fiebig, K. M., Rice, L. M., Pollock, E., and Brunger, A. T., ""Folding Intermediates of SNARE Complex Assembly,"" Nat. Struct. Biol. 6, 117-123 (1999).",Folding Intermediates of SNARE Complex Assembly,published,journal,Nat. Struct. Biol.,Nature Structural Biology,6,2,,,,,,,,,,,,,,,,,,,,,,117,123,1999, citations,entry_citation,4288,197308,1,,entry citation,,99311324,,,"Carotenuto, A., Tessari, M., Whitehead, B., Aelen, J.M.A., van Bergen en Henegouwen, P.M.P., Vuister, G.W., ""Sequence-specific 1H, 13C and 15N Assignment and Secondary Structure of the Apo EH2 Domain of Mouse Eps15,"" J. Biomol. NMR 14, 97-98 (1999).","Sequence-specific 1H, 13C and 15N Assignment and Secondary Structure of the Apo EH2 Domain of Mouse Eps15",published,journal,J. Biomol. NMR,,14,,,,,,,,,,,,,,,,,,,,,,,97,98,1999, citations,entry_citation,4289,197322,1,,entry citation,,,,,"Sun, Y., and Krishna, N. R., ""1H and 15N Chemical-Shift Assignments of a Carboxy-Terminal Functional Domain of the Bacteriophage P22 Scaffolding Protein,"" Magn. Reson. Chem., 37,602-604 (1999).","1H and 15N Chemical-Shift Assignments of a Carboxy-Terminal Functional Domain of the Bacteriophage P22 Scaffolding Protein",published,journal,Magn. Reson. Chem.,,37,,,,,,,,,,,,,,,,,,,,,,,602,604,1999, citations,entry_citation,429,197344,1,,entry citation,,,,,"Otter, Albin, Kotovych, George, Scott, Paul G., ""Solution Conformation of the Type I Collagen alpha-1 Chain N-Telopeptide Studied by 1H NMR Spectroscopy,"" Biochemistry 28, 8003-8010 (1989).","Solution Conformation of the Type I Collagen alpha-1 Chain N-Telopeptide Studied by 1H NMR Spectroscopy",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,8003,8010,1989, citations,entry_citation,4290,197358,1,,entry citation,,20309732,10770921,,,"Chitin-binding Proteins in Invertebrates and Plants Comprise a Common Chitin-binding Structural Motif",published,journal,J. Biol. Chem.,,275,24,,,,,,,,,,,,,,,,,,,,,,17929,17932,2000, citations,entry_citation,4291,197376,1,,entry citation,,98378464,,,"Messias, A. C., Kastrau, D. H.W., Costa, H. S., Legall, J., Turner, D. L., Santos, H., and Xavier, A. V., ""Solution Structure of Desulfovibrio Vulgaris (Hildenborough) Ferrocytochrome C3: Structural Basis for Functional Cooperativity,"" J. Mol. Biol. 281, 719-739 (1998).","Solution Structure of Desulfovibrio Vulgaris (Hildenborough) Ferrocytochrome C3: Structural Basis for Functional Cooperativity",published,journal,J. Mol. Biol.,,281,4,,,,,,,,,,,,,,,,,,,,,,719,739,1998, citations,entry_citation,4292,197395,1,,entry citation,,99143099,,,,Structure of the Insect Cytokine Peptide PSP1 from Pseudoplusia includens,published,journal,J. Biol. Chem.,Journal of Biological Chemistry,274,,,,,,,,,,,,,,,,,,,,,,,4493,4496,1999, citations,entry_citation,4293,197409,1,,entry citation,,,,,"Whittaker, S. B.-M., Boetzel, R., MacDonald, C. J., Lian, L-Y., James, R., Kleanthous, C., and Moore, G. R., ""Assignment of 1H, 13C and 15N Signals of the DNase Domain of Colicin E9,"" J. Biomol. NMR in preparation.","Assignment of 1H, 13C and 15N Signals of the DNase Domain of Colicin E9",in preparation,journal,J. Biomol. NMR,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref-1,4293,197410,2,,reference citation,,,8520220,,"Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J. and Bax, A. J. Biomol. NMR 6, 277-293 (1995)",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,entry_citation,4294,197440,1,,entry citation,,99455329,,,"Mishima, M., Ozaki, J., Ikegami, T., Kabe, Y., Goto, M., Ueda, H., Hirose, S., Handa, H., and Shirakawa, M., ""Resonance Assignments, Secondary Structure and 15N Relaxation data of the Human Transcriptional Coactivator hMBF1(57-148),"" J. Biomol. NMR 14, 373-376 (1999).","Resonance Assignments, Secondary Structure and 15N Relaxation data of the Human Transcriptional Coactivator hMBF1(57-148)",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,14,,,,,,,,,,,,,,,,,,,,,,,373,376,1999, citations,entry_citation,4295,197454,1,,entry citation,,98455511,,,"Muhle-Goll, C., Pastore, A., and Nilges, M., ""The 3D Structure of a Type I Module from Titin: a Prototype of Intracellular Fibronectin Type III Domains,"" Structure 6, 1291-1302 (1998).","The 3D Structure of a Type I Module from Titin: a Prototype of Intracellular Fibronectin Type III Domains",published,journal,Structure,,6,,,,,,,,,,,,,,,,,,,,,,,1291,1302,1998, citations,ref2,4295,197455,2,,reference citation,,,9081541,,"Muhle-Goll C., Nilges M., Pastore A., ""1H and 15N NMR Resonance Assignments and Secondary Structure of Titin Type I domains,"" J. Biomol. NMR 9, (1997)",1H and 15N NMR resonance assignments and secondary structure of titin type I domains.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,9,1,,0925-2738,,,,,,,,,,,,,,,,,,,,2,10,1997,"Titin/connectin is a giant muscle protein with a highly modular architecture consisting of multiple repeats of two sequence motifs, named type I and type II. Type I modules have been suggested to be intracellular members of the fibronectin type III (Fn3) domain family. Along the titin sequence they are exclusively present in the region of the molecule located in the sarcomere A-band. This region has been shown to interact with myosin and C-protein. One of the most noticeable features of type I modules is that they are particularly rich in semiconserved prolines, since these residues account for about 8% of their sequence. We have determined the secondary structure of a representative type I domain (A71) by 15N and 1H NMR. We show that the type I domains of titin have the Fn3 fold as proposed, consisting of a three- and a four-stranded beta-sheet. When the two sheets are placed on top of each other to form the beta-sandwich characteristic of the Fn3 fold, 8 out of 10 prolines are found on the same side of the molecule and form an exposed hydrophobic patch. This suggests that the semiconserved prolines might be relevant for the function of type I modules, providing a surface for binding to other A-band proteins. The secondary structure of A71 was structurally aligned to other extracellular Fn3 modules of known 3D structure. The alignment shows that titin type I modules have closest similarity to the first Fn3 domain of Drosophila neuroglian." citations,entry_citation,4296,197472,1,,entry citation,,98359762,,,"Feng, W., Tejero, R., Zimmerman, D. E., Inouye, M., and Montelione, G. T., ""Solution NMR Structure and Backbone Dynamics of the Major Cold-shock Protein (CspA) from Escherichia coli: Evidence for Conformational Dyanamics in the Single-stranded RNA-binding Site,"" Biochemistry 37, 10881-10896 (1998).","Solution NMR Structure and Backbone Dynamics of the Major Cold-shock Protein (CspA) from Escherichia coli: Evidence for Conformational Dyanamics in the Single-stranded RNA-binding Site",published,journal,Biochemistry,Biochemistry,37,,,,,,,,,,,,,,,,,,,,,,,10881,10896,1998, citations,ref_1,4296,197473,2,,reference citation,,,7515185,,"Newkirk K., Feng W., Jiang W., Tejero R., Emerson S. D., Inouye M., Montelione G. T., ""Solution NMR Structure of the Major Cold Shock Protein (CspA) from Escherichia coli: Identification of a Binding Epitope for DNA,"" Proc. Natl. Acad. Sci. USA 91, 5114-5118 (1994).",Solution NMR structure of the major cold shock protein (CspA) from Escherichia coli: identification of a binding epitope for DNA.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,91,11,,0027-8424,,,,,,,,,,,,,,,,,,,,5114,5118,1994,"Sequence-specific 1H and 15N resonance assignments have been determined for the major cold shock protein (CspA) from Escherichia coli with recently developed three-dimensional triple-resonance NMR experiments. By use of these assignments, five antiparallel beta-strands were identified from analysis of NMR data. Strands 1-4 have a classical 3-2-1-4 Greek key beta-sheet topology and there are two beta-bulges, at positions Lys10-Trp11 and Gly65-Asn66. Three-dimensional structures of CspA were generated from NMR data by using simulated annealing with molecular dynamics. The overall chain fold of CspA is a beta-barrel structure, with a tightly packed hydrophobic core. Two-dimensional isotope-edited pulsed-field gradient 15N-1H heteronuclear single-quantum coherence spectroscopy was used to characterize the 15N-1H fingerprint spectrum with and without a 24-base oligodeoxyribonucleotide, 5'-AACGGTTTGACGTACAGACCATTA-3'. Protein-DNA complex formation perturbs a subset of the amide resonances that are located mostly on one face of the CspA molecule. This portion of the CspA molecular surface includes two putative RNA-binding sequence motifs which contribute to an unusual cluster of eight surface aromatic side chains: Trp11, Phe12, Phe18, Phe20, Phe31, His33, Phe34, and Tyr42. These surface aromatic groups, and also residues Lys16, Ser44, and Lys60 located on this same face of CspA, are highly conserved in the family of CspA homologues. These isotope-edited pulsed-field gradient NMR data provide a low-resolution mapping of a DNA-binding epitope on CspA." citations,ref_2,4296,197474,3,,reference citation,,,9217263,,"Zimmerman et al. (1997) J. Mol. Biol. 269, 592 - 610",Automated analysis of protein NMR assignments using methods from artificial intelligence.,published,journal,J. Mol. Biol.,Journal of molecular biology,269,4,,0022-2836,,,,,,,,,,,,,,,,,,,,592,610,1997,"An expert system for determining resonance assignments from NMR spectra of proteins is described. Given the amino acid sequence, a two-dimensional 15N-1H heteronuclear correlation spectrum and seven to eight three-dimensional triple-resonance NMR spectra for seven proteins, AUTOASSIGN obtained an average of 98% of sequence-specific spin-system assignments with an error rate of less than 0.5%. Execution times on a Sparc 10 workstation varied from 16 seconds for smaller proteins with simple spectra to one to nine minutes for medium size proteins exhibiting numerous extra spin systems attributed to conformational isomerization. AUTOASSIGN combines symbolic constraint satisfaction methods with a domain-specific knowledge base to exploit the logical structure of the sequential assignment problem, the specific features of the various NMR experiments, and the expected chemical shift frequencies of different amino acids. The current implementation specializes in the analysis of data derived from the most sensitive of the currently available triple-resonance experiments. Potential extensions of the system for analysis of additional types of protein NMR data are also discussed." citations,entry_citation,4297,197508,1,,entry citation,,99332676,,,"Weigelt, J., Brown, S. E., Miles, C. S., Dixon, N. E., and Otting, G., ""NMR Structure of the N-terminal Domain of E. coli DnaB Helicase: Implications for Structure Rearrangements in the Helicase Hexamer and its Biological Function,"" Structure Fold Des. 7(6) 681-690 (1999).","NMR Structure of the N-terminal Domain of E. coli DnaB Helicase: Implications for Structure Rearrangements in the Helicase Hexamer and its Biological Function",published,journal,Structure Fold Des.,,7,6,,,,,,,,,,,,,,,,,,,,,,681,690,1999, citations,ref_1,4297,197509,2,,reference citation,,,8589602,,"Wishart D.S., Bigam C.G., Yao J., Abildgaard F., Dyson H.J., Oldfield E., Markley J.L., Sykes B.D., ""1H, 13C and 15N Chemical Shift Referencing in Biomolecular NMR,"" J. Biomol. NMR, 6, 135-40 (1995)","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,primary_citation,4298,197525,1,,entry citation,,96184885,,,"Vranken, W. F., Budesinsky, M., Martins, J. C., Fant, F., Boulez, K., Gras-Masse, H., and Borremans, F. A. M., ""Conformational Features of a Synthetic Cyclic Peptide Corresponding to the Complete V3 Loop of the RF HIV-1 Strain in Water and Water/Trifluoroethanol Solutions,"" Eur. J. Biochem. 236, 100-108 (1996).","Conformational Features of a Synthetic Cyclic Peptide Corresponding to the Complete V3 Loop of the RF HIV-1 Strain in Water and Water/Trifluoroethanol Solutions",published,journal,Eur. J. Biochem.,European Journal of Biochemistry,236,,,,,,,,,,,,,,,,,,,,,,,100,108,1996, citations,ref_1,4332,198202,2,,reference citation,,,,,"Live, D.H., Davis, D.G., Agosta, W.C. and Cowburn, D. J. (1984) J. Am. Chem. Soc. Vol 106, 1939-1941.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_one,4298,197526,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4299,197541,1,,entry citation,,99356754,,,"Shi, G., Gao, J., and Yan, H., ""1H, 13C and 15N Resonance Assignments of Escherichia coli 6-hydroxymethyl-7,8-dihydropterin Pyrophosphokinase and its Complex with MgAMPPCP,"" J. Biomol. NMR 14, 189-190 (1999).","1H, 13C and 15N Resonance Assignments of Escherichia coli 6-hydroxymethyl-7,8-dihydropterin Pyrophosphokinase and its Complex with MgAMPPCP",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,14,,,,,,,,,,,,,,,,,,,,,,,189,190,1999, citations,entry_citation,430,197555,1,,entry citation,,,,,"Otter, Albin, Kotovych, George, Scott, Paul G., ""Solution Conformation of the Type I Collagen alpha-1 Chain N-Telopeptide Studied by 1H NMR Spectroscopy,"" Biochemistry 28, 8003-8010 (1989).","Solution Conformation of the Type I Collagen alpha-1 Chain N-Telopeptide Studied by 1H NMR Spectroscopy",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,8003,8010,1989, citations,entry_citation,4300,197569,1,,entry citation,,99356754,,,"Shi, G., Gao, J., and Yan, H., ""1H, 13C and 15N Resonance Assignments of Escherichia coli 6-hydroxymethyl-7,8-dihydropterin Pyrophosphokinase and its Complex with MgAMPPCP,"" J. Biomol. NMR 14, 189-190 (1999).","1H, 13C and 15N Resonance Assignments of Escherichia coli 6-hydroxymethyl-7,8-dihydropterin Pyrophosphokinase and its Complex with MgAMPPCP",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,14,,,,,,,,,,,,,,,,,,,,,,,189,190,1999, citations,entry_citation,4301,197586,1,,entry citation,,97220236,,,"Fernandez, C., Szyperski, T., Bruyere, T., Ramage, P., Mosinger, E. and Wuthrich, K., ""NMR solution structure of the pathogenesis-related protein P14a"". J. Mol. Biol. 266, 576-593 (1997).",NMR solution structure of the pathogenesis-related protein P14a,published,journal,J. Mol. Biol.,,266,3,,,,,,,,,,,,,,,,,,,,,,576,593,1997, citations,entry_citation,4302,197603,1,,entry citation,,,,,"Dijkstra, K., Karvonen, P., Huovinen, A., Koivunen, P., Kivirikko, K. I., Darby, N. J., van Straaten, M., Scheek, R. M., and Kemmink, J., ""Assignment of 1H, 13C and 15N Resonances of the a' Domain of Protein Disulfide Isomerase,"" J. Biomol. NMR, in Preparation.","Assignment of 1H, 13C and 15N Resonances of the a' Domain of Protein Disulfide Isomerase",in preparation,journal,J. Biomol. NMR,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4303,197617,1,,entry citation,,,,,"Conroy, M. J., Westerhuis, W.H.J., Parkes-Loach, P. S., Loach, P. A., Hunter, C. N., and Williamson, M. P., ""The Solution Structure of Rhodobacter sphaeroides LH1beta Reveals Two Helical Domains Separated by a More Flexible Region: Structural Consequences for the LH1 Complex,"" J. Mol. Biol. 298, 83-94 (2000).","The Solution Structure of Rhodobacter sphaeroides LH1beta Reveals Two Helical Domains Separated by a More Flexible Region: Structural Consequences for the LH1 Complex",published,journal,J. Mol. Biol.,Journal of Molecular Biology,298,,,,,,,,,,,,,,,,,,,,,,,83,94,2000, citations,entry_citation,4304,197634,1,,entry citation,,99260733,,,"Tochio, H., Zhang, Q., Li, M., and Zhang, M., ""Solution Structure of the Extended Neuronal Nitric Oxide Synthase PDZ Domain Complexed with an Associated Peptide,"" Nat. Struct. Biol. 6, 417-421 (1999).","Solution Structure of the Extended Neuronal Nitric Oxide Synthase PDZ Domain Complexed with an Associated Peptide",published,journal,Nat. Struct. Biol.,Nature Structural Biology,6,,,,,,,,,,,,,,,,,,,,,,,417,421,1999, citations,entry_citation,4305,197650,1,,entry citation,,99023194,,,"Tochio, H., Ohki, S., Zhang, Q., Li, M., and Zhang, M., ""Solution Structure of a Protein Inhibitor of Neuronal Nitric Oxide Synthase,"" Nat. Struct. Biol. 5, 965-969 (1998).",Solution Structure of a Protein Inhibitor of Neuronal Nitric Oxide Synthase,published,journal,Nat. Struct. Biol.,Nature Structural Biology,5,,,,,,,,,,,,,,,,,,,,,,,965,969,1998, citations,entry_citation,4306,197664,1,,entry citation,,,,,,"Backbone NMR assignments of a cyanobacterial transcriptional factor, SmtB, that binds zinc ions",published,journal,J. Biomol. NMR,,14,2,,,,,,,,,,,,,,,,,,,,,,191,192,1999, citations,ref_1,4306,197665,2,,reference citation,,,,,"Morita HE, Kosada T, Yamazaki T, Kyogoku Y, Hayashi H, J. Biomol. NMR 1998; 12:453-4",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4307,197688,1,,entry citation,,99238311,10220323,,,Solution structure of Syrian hamster prion protein rPrP(90-231),published,journal,Biochemistry,Biochemistry,38,,,,,,,,,,,,,,,,,,,,,,,5362,5377,1999, citations,ref_1,4307,197689,2,,reference citation,,,9294167,,"Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform T. L. James, H. Liu, N. B. Ulyanov, S. Farr-Jones, H. Zhang, D. G. Donne, K. Kaneko, D. Groth, I. Mehlhorn, S. B. Prusiner, and F. E. Cohen Proc. Natl. Acad. Sci. USA 94 (1997) 10086-10091.",Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,94,19,,0027-8424,,,,,,,,,,,,,,,,,,,,10086,10091,1997,"The scrapie prion protein (PrPSc) is the major, and possibly the only, component of the infectious prion; it is generated from the cellular isoform (PrPC) by a conformational change. N-terminal truncation of PrPSc by limited proteolysis produces a protein of approximately 142 residues designated PrP 27-30, which retains infectivity. A recombinant protein (rPrP) corresponding to Syrian hamster PrP 27-30 was expressed in Escherichia coli and purified. After refolding rPrP into an alpha-helical form resembling PrPC, the structure was solved by multidimensional heteronuclear NMR, revealing many structural features of rPrP that were not found in two shorter PrP fragments studied previously. Extensive side-chain interactions for residues 113-125 characterize a hydrophobic cluster, which packs against an irregular beta-sheet, whereas residues 90-112 exhibit little defined structure. Although identifiable secondary structure is largely lacking in the N terminus of rPrP, paradoxically this N terminus increases the amount of secondary structure in the remainder of rPrP. The surface of a long helix (residues 200-227) and a structured loop (residues 165-171) form a discontinuous epitope for binding of a protein that facilitates PrPSc formation. Polymorphic residues within this epitope seem to modulate susceptibility of sheep and humans to prion disease. Conformational heterogeneity of rPrP at the N terminus may be key to the transformation of PrPC into PrPSc, whereas the discontinuous epitope near the C terminus controls this transition." citations,ref_2,4307,197690,3,,reference citation,,,10220323,,"Solution Structure of Syrian Hamster Prion Protein rPrP(90-231) H. Liu, S. Farr-Jones, N. B. Ulyanov, M. Llinas, S. Marqusee, D. Groth, F. E. Cohen, S. B. Prusiner, and T. L. James Biochemistry 1999 Apr 27;38(17):5362-77",Solution structure of Syrian hamster prion protein rPrP(90-231).,published,journal,Biochemistry,Biochemistry,38,17,,0006-2960,,,,,,,,,,,,,,,,,,,,5362,5377,1999,"NMR has been used to refine the structure of Syrian hamster (SHa) prion protein rPrP(90-231), which is commensurate with the infectious protease-resistant core of the scrapie prion protein PrPSc. The structure of rPrP(90-231), refolded to resemble the normal cellular isoform PrPC spectroscopically and immunologically, has been studied using multidimensional NMR; initial results were published [James et al. (1997) Proc. Natl. Acad. Sci. U.S.A. 94, 10086-10091]. We now report refinement with better definition revealing important structural and dynamic features which can be related to biological observations pertinent to prion diseases. Structure refinement was based on 2778 unambiguously assigned nuclear Overhauser effect (NOE) connectivities, 297 ambiguous NOE restraints, and 63 scalar coupling constants (3JHNHa). The structure is represented by an ensemble of 25 best-scoring structures from 100 structures calculated using ARIA/X-PLOR and further refined with restrained molecular dynamics using the AMBER 4.1 force field with an explicit shell of water molecules. The rPrP(90-231) structure features a core domain (residues 125-228), with a backbone atomic root-mean-square deviation (RMSD) of 0.67 A, consisting of three alpha-helices (residues 144-154, 172-193, and 200-227) and two short antiparallel beta-strands (residues 129-131 and 161-163). The N-terminus (residues 90-119) is largely unstructured despite some sparse and weak medium-range NOEs implying the existence of bends or turns. The transition region between the core domain and flexible N-terminus, i.e., residues 113-128, consists of hydrophobic residues or glycines and does not adopt any regular secondary structure in aqueous solution. There are about 30 medium- and long-range NOEs within this hydrophobic cluster, so it clearly manifests structure. Multiple discrete conformations are evident, implying the possible existence of one or more metastable states, which may feature in conversion of PrPC to PrPSc. To obtain a more comprehensive picture of rPrP(90-231), dynamics have been studied using amide hydrogen-deuterium exchange and 15N NMR relaxation times (T1 and T2) and 15N{1H} NOE measurements. Comparison of the structure with previous reports suggests sequence-dependent features that may be reflected in a species barrier to prion disease transmission." citations,entry_citation,4308,197707,1,,entry citation,,99410891,,,"Mulhern, T. D., Bagley, C. J., Gaunt, C., Lopez, A. F., Vadas, M.A., D'Andrea, R. J., and Booker, G. W., ""1H and 15N Chemical Shift Assignments for Domain 4 of the Common Beta-Chain of the IL-3, IL-5 and GM-CSF Receptors,"" J. Biomol. NMR 14, 281-282 (1999).","1H and 15N Chemical Shift Assignments for Domain 4 of the Common Beta-Chain of the IL-3, IL-5 and GM-CSF Receptors",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,14,,,,,,,,,,,,,,,,,,,,,,,281,282,1999, citations,entry_citation,4309,197730,1,,entry citation,,99356755,,,"Izadi-Pruneyre, N., Wolff, N., Castagne, C., Czisch, M., Wandersman, C., Delepierre, M., and Lecroisey, A., ""Backbone NMR Assignment and Secondary Structure of the 19 kDa Hemophore HasA,"" J. Biomol. NMR 14, 193-194 (1999).",Backbone NMR Assignment and Secondary Structure of the 19 kDa Hemophore HasA,published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,14,,,,,,,,,,,,,,,,,,,,,,,193,194,1999, citations,entry_citation,4310,197753,1,,entry citation,,21167469,11266605,,,"A Novel Target Recognition Revealed by Calmodulin in Complex with the Basic Helix-loop-helix Transcription Factor SEF2-1/E2-2",published,journal,Protein Sci.,,10,1,,,,,,,,,,,,,,,,,,,,,,169,186,2001,Calmodulin transcription regulation. citations,entry_citation,4311,197776,1,,entry citation,,99356758,,,"Khorasanizadeh, S., Campos-Olivas, R., Clark, C.A., and Summers, M. F., ""Sequence-Specific 1H, 13C and 15N Chemical Shift Assignment and Secondary Structure of the HTLV-I Capsid Protein,"" J. Biomol. NMR 14, 199-200 (1999).","Sequence-Specific 1H, 13C and 15N Chemical Shift Assignment and Secondary Structure of the HTLV-I Capsid Protein",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,14,,,,,,,,,,,,,,,,,,,,,,,199,200,1999, citations,entry_citation,4312,197791,1,,entry citation,,,,,"Dhalluin, C., Carlson, J., Zeng, L., He, C., Aggarwal, A. K., and Zhou, M-M., ""1H, 15N and 13C Resonance Assignments for the Bromodomain of the Histone Acetyltransferase hsP/CAF,"" J. Biomol. NMR, in preparation.","1H, 15N and 13C Resonance Assignments for the Bromodomain of the Histone Acetyltransferase hsP/CAF",in preparation,journal,J. Biomol. NMR,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_1,4312,197792,2,,reference citation,,,8520220,,"Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G. Pfeifer, J. and Bax, A (1995) J. Biomol. NMR 6, 277-293.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref_2,4312,197793,3,,reference citation,,,,,"Johnson, B. A. and Blevins, R. A. (1994) J. Biomol. NMR 4, 603-614.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_3,4312,197794,4,,reference citation,,,8684459,,"X.J.Yang,V.V.Ogryzko,J.I.Nishikawa,B.H.Howard,Y.Nakatani, Nature (1996) 382, 319.",A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A.,published,journal,Nature,Nature,382,6589,,0028-0836,,,,,,,,,,,,,,,,,,,,319,324,1996,"The adenoviral oncoprotein E1A induces progression through the cell cycle by binding to the products of the p300/CBP and retinoblastoma gene families. A new cellular p300/CBP-associated factor (P/CAF) having intrinsic histone acetylase activity has been identified that competes with E1A. Exogenous expression of P/CAF in HeLa cells inhibits cell-cycle progression and counteracts the mitogenic activity of E1A. E1A disturbs the normal cellular interaction between p300/CBP and its associated histone acetylase." citations,entry_citation,4313,197811,1,,entry citation,,,,,,,to be published,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,reference_1,4313,197812,2,,reference citation,,,12402029,,"Pochapsky, T. C., Pochapsky, S. S., Ju, T. Mo, H., Al-Mjeni, F. and Maroney, M. J., Modeling and experiment yields the structure of acireductone dioxygenase from Klebsiella pneumoniae, Nature Struct. Biol. 9, 966-972 (2002).","Modeling and experiment yields the structure of acireductone dioxygenase from Klebsiella pneumoniae",,journal,Nature Struct. Biol.,Nature Structural Biology,9,12,,,,,,,,,,,,,,,,,,,,,,966,972,2002, citations,entry_citation,4314,197837,1,,entry citation,,99255353,,,"Sticht, H., Escher, S. E., Schweimer, K., Forssmann, W-G., Roesch, P., and Adermann, K., ""Solution Structure of the Human CC chemokine 2:A Monomeric Representative of the CC chemokine Subtype,"" Biochemistry 38, 5995-6002 (1999).","Solution Structure of the Human CC chemokine 2:A Monomeric Representative of the CC chemokine Subtype",published,journal,Biochemistry,Biochemistry,38,19,,,,,,,,,,,,,,,,,,,,,,5995,6002,1999, citations,entry_citation,4315,197855,1,,entry citation,,,,,"Vathyam, S., Byrd, R. A., and Miller, A-F., ""Assignment of the Backbone of Oxidized Fe-superoxide Dismutase, a 42kDa Paramagnet-containing Enzyme,"" J. Biomol. NMR, in preparation.","Assignment of the Backbone of Oxidized Fe-superoxide Dismutase, a 42kDa Paramagnet- containing Enzyme",in preparation,journal,J. Biomol. NMR,Journal of Biomolecular NMR,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4316,197878,1,,entry citation,,99234020,,,"Matthey, U., Kaim, G., Braun, D., Wuthrich, K. and Dimroth, P., ""NMR Studies of Subunit C of the ATP Synthase from Propionigenium modestum in Dodecylsulfate Micelles,"" Eur. J. Biochem., 261, 459-467 (1999).","NMR Studies of Subunit C of the ATP Synthase from Propionigenium modestum in Dodecylsulfate Micelles",published,journal,Eur. J. Biochem.,European Journal of Biochemistry,261,2,,,,,,,,,,,,,,,,,,,,,,459,467,1999, citations,entry_citation,4317,197912,1,,entry citation,,,,,,A novel RNA-binding motif in influenza A virus non-structural protein 1,published,journal,Nat. Struct. Biol.,,4,,,,,,,,,,,,,,,,,,,,,,,891,,1997, citations,entry_citation,4318,197931,1,,entry citation,,99356757,,,"Xia, B., Chung, J., Vlamis-Gardikas, A., Holmgren, A., Wright, P. E., and Dyson, H. J., ""Assignment of 1H, 13C, and 15N Resonances of Reduced Escherichia coli Glutaredoxin 2,"" J. Biomol. NMR 14, 197-198 (1999).","Assignment of 1H, 13C, and 15N Resonances of Reduced Escherichia coli Glutaredoxin 2",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,14,2,,,,,,,,,,,,,,,,,,,,,,197,198,1999, citations,entry_citation,4319,197944,1,,entry citation,,,,,,"Redox-dependent magnetic alignment of Clostridium pasterianum rubredoxin: measurement of magnetic susceptibility anisotropy and prediction of pseudocontact shift contributions",published,journal,J. Am. Chem. Soc.,,121,,,,,,,,,,,,,,,,,,,,,,,4677,4688,1999, citations,citation_one,4319,197945,2,,reference citation,,,9169226,,"Tjandra, N. & Bax, A., J. Magn. Reson. 124, 512-515, 1997.",Measurement of dipolar contributions to 1JCH splittings from magnetic-field dependence of J modulation in two-dimensional NMR spectra.,published,journal,J. Magn. Reson.,"Journal of magnetic resonance (San Diego, Calif. : 1997)",124,2,,1090-7807,,,,,,,,,,,,,,,,,,,,512,515,1997, citations,citation_two,4319,197946,3,,reference citation,,,,,"Tjandra, N., Grzesiek, S. & Bax, A., J. Am. Chem. Soc., 118, 6264-6272, 1996.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,432,197970,1,,entry citation,,,,,"Redfield, Alfred G., Papastavros, Mary Z., ""NMR Study of the Phosphoryl Binding Loop in Purine Nucleotide Proteins: Evidence for a Strong Hydrogen Bonding in Human N-ras p21,"" Biochemistry 29, 3509-3514 (1990).","NMR Study of the Phosphoryl Binding Loop in Purine Nucleotide Proteins: Evidence for a Strong Hydrogen Bonding in Human N-ras p21",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,3509,3514,1990, citations,citation_1,5645,229362,2,,reference citation,,,12522297,,,Random Coil Proton Chemical Shifts of Deoxyribonucleic Acids,published,journal,J. Biomol. NMR,,24,4,,,,,,,,,,,,,,,,,,,,,,329,337,2002, citations,entry_citation,4320,197983,1,,entry citation,,,,,,"Redox-dependent magnetic alignment of Clostridium pasterianum rubredoxin: measurement of magnetic susceptibility anisotropy and prediction of pseudocontact shift contributions",published,journal,J. Am. Chem. Soc.,,121,,,,,,,,,,,,,,,,,,,,,,,4677,4688,1999, citations,citation_one,4320,197984,2,,reference citation,,,9169226,,"Tjandra, N. & Bax, A., J. Magn. Reson. 124, 512-515, 1997.",Measurement of dipolar contributions to 1JCH splittings from magnetic-field dependence of J modulation in two-dimensional NMR spectra.,published,journal,J. Magn. Reson.,"Journal of magnetic resonance (San Diego, Calif. : 1997)",124,2,,1090-7807,,,,,,,,,,,,,,,,,,,,512,515,1997, citations,citation_two,4320,197985,3,,reference citation,,,,,"Tjandra, N., Grzesiek, S. & Bax, A., J. Am. Chem. Soc., 118, 6264-6272, 1996.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4321,198009,1,,entry citation,,20142316,,,"Lin, Y., and Wagner, G., ""Efficient Side-chain and Backbone Assignment in Large Proteins: Application to tGCN5,"" J. Biomol. NMR 15, 227-239 (1999).","Efficient Side-chain and Backbone Assignment in Large Proteins: Application to tGCN5",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,15,,,,,,,,,,,,,,,,,,,,,,,227,239,1999, citations,entry_citation,4322,198024,1,,entry citation,,96049568,,,"Vranken, W. F., Budesinsky, M., Fant, F., Boulez, K., and Borremans, F. A. M., ""The Complete Consensus V3 Loop Peptide of the Envelope Protein gp120 of HIV-1 Shows Pronounced Helical Character in Solution,"" FEBS Lett. 374, 117-121 (1995).","The Complete Consensus V3 Loop Peptide of the Envelope Protein gp120 of HIV-1 Shows Pronounced Helical Character in Solution.",published,journal,FEBS Lett.,FEBS Letters,374,,,,,,,,,,,,,,,,,,,,,,,117,121,1995, citations,entry_citation,4323,198042,1,,entry citation,,99410892,,,"Huang, X., Link, K., Koide, A., Dunn, J.J., Luft, B.J., and Koide, S.,""1H, 13C, and 15N NMR Backbone Assignments of 37 kDa Surface Antigen OspC from Borrelia burgdorferi,"" J. Biomol. NMR 14, 283-284 (1999).","1H, 13C, 15N NMR backbone assignments of 37 kDa surface antigen OspC from Borrelia burgdorferi",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,14,3,,,,,,,,,,,,,,,,,,,,,,283,284,1999, citations,entry_citation,4324,198055,1,,entry citation,,,,,"Karimi, A., Matsumura, M., Wright, P. E., and Dyson, H. J., ""Characterization of Monomeric and Dimeric B-domain of Staphyococcal Protein A: Sources of Stabilization of a 3-helix Bundle Protein,"" J. Pept. Res., Submitted.","Characterization of Monomeric and Dimeric B-domain of Staphyococcal Protein A: Sources of Stabilization of a 3-helix Bundle Protein.",submitted,journal,J. Pept. Res.,Journal of Peptide Research,,na,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_1,4324,198056,2,,reference citation,,,8589602,,"Wishart et al., 1995 (J.Biomol.NMR 6, 135-140)""","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4325,198072,1,,entry citation,,20000040,,,"Karimi, A., Matsumura, M., Wright, P. E., and Dyson, H. J., ""Characterization of Monomeric and Dimeric B-domain of Staphylococcal Protein A,"" J. Pept. Res. 54, 344-352 (1999).",Characterization of Monomeric and Dimeric B-domain of Staphylococcal Protein A.,published,journal,J. Pept. Res.,Journal of Peptide Research,54,4,,,,,,,,,,,,,,,,,,,,,,344,352,1999, citations,entry_citation,4326,198089,1,,entry citation,,94347721,,,"Liu, D., DeRose, E. F., Prasad, R., Wilson, S. H., and Mullen, G. P., ""Assignments of 1H, 15N, and 13C Resonances for the Backbone and Side Chains of the N-Terminal Domain of DNA Polymerase B. Determination of the Secondary Structure and Tertiary Contacts.,"" Biochemistry 33, 9537-9545 (1994).","Assignments of 1H, 15N, and 13C Resonances for the Backbone and Side Chains of the N-Terminal Domain of DNA Polymerase B. Determination of the Secondary Structure and Tertiary Contacts",published,journal,Biochemistry,,33,32,,,,,,,,,,,,,,,,,,,,,,9537,9545,1994, citations,Reference_1,4326,198090,2,,reference citation,,94347721,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4327,198106,1,,entry citation,,99410895,,,"Wu, B., Arumugam, S., Huang, W., Brew, K., and Van Doren, S.R., ""1H, 13C and 15N Resonance Assignment and Secondary Structure of the N-terminal Inhibitory Domain of Human Tissue Inhibitor of Metalloproteinases-1,"" J. Biomol. NMR 14, 289-290 (1999).","1H, 13C and 15N Resonance Assignment and Secondary Structure of the N-terminal Inhibitory Domain of Human Tissue Inhibitor of Metalloproteinases-1",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,14,,,,,,,,,,,,,,,,,,,,,,,289,290,1999, citations,entry_citation,4328,198122,1,,entry citation,,99321989,,,"Aihara, H., Ito, Y., Kurumizaka, H., Yokoyama, S., and Shibata, T., ""The N-terminal Domain of the Human Rad51 Protein Binds DNA; Structure and a DNA Binding Surface as Revealed by NMR,"" J. Mol. Biol. 290, 495-504.","The N-terminal Domain of the Human Rad51 Protein Binds DNA; Structure and a DNA Binding Surface as Revealed by NMR",published,journal,J. Mol. Biol.,Journal of Molecular Biology,290,na,,,,,,,,,,,,,,,,,,,,,,495,504,1999, citations,entry_citation,4329,198138,1,,entry citation,,99410898,,,"Johansson, C., Bergkvist, A., Fjellstrom, O., Rydstrom, J., and Karlsson, G., ""Sequential Assignment and Secondary Structure Analysis of the NADP(H)-Binding Domain of Escherichia coli Transhydrogenase,"" J. Biomol. NMR, 14, 295-296 (1999).","Sequential Assignment and Secondary Structure Analysis of the NADP(H)-Binding Domain of Escherichia coli Transhydrogenase",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,14,,,,,,,,,,,,,,,,,,,,,,,295,296,1999, citations,entry_citation,433,198160,1,,entry citation,,,,,"Redfield, Alfred G., Papastavros, Mary Z., ""NMR Study of the Phosphoryl Binding Loop in Purine Nucleotide Proteins: Evidence for a Strong Hydrogen Bonding in Human N-ras p21,"" Biochemistry 29, 3509-3514 (1990).","NMR Study of the Phosphoryl Binding Loop in Purine Nucleotide Proteins: Evidence for a Strong Hydrogen Bonding in Human N-ras p21",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,3509,3514,1990, citations,entry_citation,4330,198173,1,,entry citation,,10360364,,,,"Structure, Specificity and CDR Mobility of a Class II Restricted T Cell Receptor.",published,journal,Nat. Struct. Biol.,,6,,,,,,,,,,,,,,,,,,,,,,,574,581,1999, citations,entry_citation,4331,198188,1,,entry citation,,,,,"Sasakawa, H., Tamura, A., Taguchi, S., Akasaka, K., Miyake, Y., Kainosho, M., ""Backbone 1H, 13C, and 15N Resonance Assignments of Streptomyces Subtilisin Inhibitor,"" J. Biomol. NMR, in preparation (1999).","Backbone 1H, 13C, and 15N Resonance Assignments of Streptomyces Subtilisin Inhibitor",in preparation,journal,J. Biomol. NMR,,,,,,,,,,,,,,,,,,,,,,,,,,,1999, citations,entry_citation,4332,198201,1,,entry citation,,,,,"Forge, V., Wijesinha, R. T., Balbach, J., Brew, K., Robinson, C. V., Redfield, C., and Dobson, C. M., ""Rapid Collapse and Slow Structural Reorganization During the Refolding of Bovine Alpha-Lactalbumin,"" J. Mol. Biol., in press (1999).","Rapid Collapse and Slow Structural Reorganization During the Refolding of Bovine Alpha-Lactalbumin",in press,journal,J. Mol. Biol.,,,,,,,,,,,,,,,,,,,,,,,,,,,1999, citations,entry_citation,4334,198234,1,,entry citation,,,,,"Iwahara, J. and Clubb, R., ""1H, 13C, 15N Resonance Assignments of ARID Domain of Dead-Ringer Protein,"" (1999).","1H, 13C, 15N Resonance Assignments of ARID Domain of Dead-Ringer Protein.",published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,1999, citations,entry_citation,4335,198249,1,,entry citation,,,,,,"NMR Assignments, Secondary Structure and Global Fold of Calerythrin, an EF-hand Calcium-binding Protein from Saccharopolyspora erythraea.",published,journal,Protein Sci.,,8,,,,,,,,,,,,,,,,,,,,,,,2580,2588,1999, citations,entry_citation,4336,198275,1,,entry citation,,,10605092,,"Guilhaudis, L., Simorre, J-P., Bouchayer, E.,Neuburger, M., Bourguignon, J., Douce, R., Marion, D., and Gans, P., ""Backbone and Sequence-Specific Assignment of Three Forms of the Lipoate Containing H-protein of the Glycine Decarboxylase Complex,"" J. Biomol. NMR, in preparation (1999).","Backbone and Sequence-Specific Assignment of Three Forms of the Lipoate Containing H-protein of the Glycine Decarboxylase Complex.",published,journal,J. Biomol. NMR,,15,2,,,,,,,,,,,,,,,,,,,,,,185,186,1999, citations,ref_1,4336,198276,2,,reference citation,,,8589602,,"""Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).""","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,ref_2,4336,198277,3,,reference citation,,90110145,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_3,4336,198278,4,,reference citation,,90303277,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_4,4336,198279,5,,reference citation,,92412042,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_5,4336,198280,6,,reference citation,,96184875,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4337,198299,1,,entry citation,,,10605092,,"Guilhaudis, L., Simorre, J-P., Bouchayer, E., Marion, D., and Gans, P., ""Backbone and Sequence-Specific Assignment of Three Forms of the Lipoate-Containing H-protein of the Glycine Decarboxylase Complex,"" J. Biomol. NMR, in preparation (1999).","Backbone and Sequence-Specific Assignment of Three Forms of the Lipoate-Containing H-protein of the Glycine Decarboxylase Complex.",published,journal,J. Biomol. NMR,,15,2,,,,,,,,,,,,,,,,,,,,,,185,186,1999, citations,ref_1,4337,198300,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR",published,journal,,,6,2,,,,,,,,,,,,,,,,,,,,,,135,140,1995, citations,ref_2,4337,198301,3,,reference citation,,90110145,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_3,4337,198302,4,,reference citation,,9030277,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_4,4337,198303,5,,reference citation,,92412042,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_5,4337,198304,6,,reference citation,,96184875,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4338,198320,1,,entry citation,,,10605092,,"Guilhaudis, L., Simorre, J-P., Bouchayer, E., Marion, D., and Gans, P., ""Backbone and Sequence-Specific Assignment of Three Forms of the Lipoate-Containing H-protein of the Glycine Decarboxylase Complex,"" J. Biomol. NMR, in preparation (1999).","Backbone and Sequence-Specific Assignment of Three Forms of the Lipoate-Containing H-protein of the Glycine Decarboxylase Complex.",published,journal,J. Biomol. NMR,,15,2,,,,,,,,,,,,,,,,,,,,,,185,186,1999, citations,ref_1,4338,198321,2,,reference citation,,,8589602,,"Whishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L. and Sykes, B. D. (1995) J. Biomol. NMR 6, 135-140.","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,ref_2,4338,198322,3,,reference citation,,90110145,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_3,4338,198323,4,,reference citation,,90303277,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_4,4338,198324,5,,reference citation,,92412042,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_5,4338,198325,6,,reference citation,,96184875,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4339,198343,1,,entry citation,,,,,"Mao, H. N. and Williamson, J. R., ""Local Folding Accompanied by RNA Binding in Yeast Ribosomal Protein L30,"" J. Mol. Biol., in preparation.",Local Folding Accompanied by RNA Binding in Yeast Ribosomal Protein L30,in preparation,journal,J. Mol. Biol.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,434,198362,1,,entry citation,,,,,"Driscoll, Paul C., Clore, G. Marius, Marion, Dominique, Wingfield, Paul, Gronenborn, Angela M., ""Complete Resonance Assignment for the Polypeptide Backbone of Interleukin 1beta Using Three-Dimensional Heteronuclear NMR Spectroscopy,"" Biochemistry 29, 3542-3556 (1990).","Complete Resonance Assignment for the Polypeptide Backbone of Interleukin 1beta Using Three-Dimensional Heteronuclear NMR Spectroscopy",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,3542,3556,1990, citations,entry_citation,4340,198375,1,,entry citation,,20073019,,,"Abbate, F., Franzoni, L., Loehr, F., Luecke, C., Ferrari, E., Sorbi, R. T., Rueterjans, H., and Spisni, A., ""Complete 1H, 15N and 13C Assignment of a Recombinant Mouse Major Urinary Protein,"" J. Biomol. NMR 15, 187-188 (1999).","Complete 1H, 15N and 13C Assignment of a Recombinant Mouse Major Urinary Protein",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,15,,,,,,,,,,,,,,,,,,,,,,,187,188,1999, citations,reference_1,4340,198376,2,,reference citation,,,9003809,,"Ferrari, E., Lodi, T., Sorbi, R.T., Tirindelli, R., C Avaggioni, A. and Spisni, A. (1997) FEBS Letters 401, 73-77","Expression of a lipocalin in Pichia pastoris: secretion, purification and binding activity of a recombinant mouse major urinary protein.",published,journal,FEBS Lett.,FEBS letters,401,1,,0014-5793,,,,,,,,,,,,,,,,,,,,73,77,1997,"The proteins of the mouse major urinary protein complex (MUP), members of the lipocalin family, bind volatile pheromones and interact with the vomeronasal neuroepithelium of the olfactory system. We report the expression of a MUP protein using its native signal sequence for secretion in the methylotrophic yeast, Pichia pastoris. Mature recombinant MUP (rMUP) is secreted at a concentration of 270 mg/l in minimal medium and it is isolated from the culture supernatant by one step ion-exchange chromatography in a nearly pure form. Binding activity, tested with an odorant molecule which displays high affinity for native MUP, indicates that rMUP has a behavior similar to the native one. This finding suggests that the protein, and in particular its hydrophobic binding pocket, is properly folded." citations,entry_citation,4341,198408,1,,entry citation,,99410897,,,"Vathyam, S., Byrd, R. A., and Miller, A-F., ""Assignment of the Backbone Resonances of Oxidized Fe-superoxide Dismutase, a 42 kDa Paramagnet-containing Enzyme,"" J. Biomol. NMR 14, 293-294 (1999).","Assignment of the Backbone Resonances of Oxidized Fe-superoxide Dismutase, a 42 kDa Paramagnet-containing Enzyme",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,14,,,,,,,,,,,,,,,,,,,,,,,293,294,1999, citations,entry_citation,4342,198434,1,,entry citation,,20016853,,,"Musco, G., de Tommasi, T., Stier, G., Kolmerer, B., Bottomle, M., Adinolfi, S., Musket, F., Gibson, T., Frenkiel, T., and Pastore, A., ""Assignment of the 1H, 15N, and 13C Resonances of the C-terminal Domain of Frataxin, the Protein Responsible for Friedreich Ataxia,"" J. Biomol. NMR 15, 87-88 (1999).","Assignment of the 1H, 15N, and 13C Resonances of the C-terminal Domain of Frataxin, the Protein Involved in Friedreich Ataxia.",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,15,,,,,,,,,,,,,,,,,,,,,,,87,88,1999, citations,entry_citation,4343,198458,1,,entry citation,,,,,,Letter to the Editor: Resonance assignment and topology of a 22 kDa C-terminal fragment of the polypyrimidine tract binding protein (PTB) containing two RNA binding domains,published,journal,J. Biomol. NMR,,14,4,,,,,,,,,,,,,,,,,,,,,,383,384,1999, citations,entry_citation,4344,198471,1,,entry citation,,,,,"Wimmer, R., Herrmann, T., Solioz, M., and Wuethrich, K., ""NMR Structure and Metal Interactions of the CopZ Copper Chaperone,"" J. Biol. Chem., In press.",NMR Structure and Metal Interactions of the CopZ Copper Chaperone,in press,journal,J. Biol. Chem.,Journal of Biological Chemistry,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4345,198496,1,,entry citation,,20051011,,,"Mao, H. N., White, S. A., and Williamson, J. R., ""A Novel Loop-loop Recognition Motif in the Yeast Ribosomal Protein L30 Autoregulatory RNA Complex,"" Nat. Struct. Biol. 6, 1139-1147 (1999).","A Novel Loop-loop Recognition Motif in the Yeast Ribosomal Protein L30 Autoregulatory RNA Complex",published,journal,Nat. Struct. Biol.,Nature Structural Biology,6,12,,,,,,,,,,,,,,,,,,,,,,1139,1147,1999, citations,entry_citation,4346,198517,1,,entry citation,,20051011,,,"Mao, H. N., White, S. A., and Williamson, J. R., ""A Novel Loop-loop Recognition Motif in the Yeast Ribosomal Protein L30 Autoregulatory RNA Complex,"" Nat. Struct. Biol. 6, 1139-1147 (1999).","A Novel Loop-loop Recognition Motif in the Yeast Ribosomal Protein L30 Autoregulatory RNA Complex",published,journal,Nat. Struct. Biol.,Nature Structural Biology,6,12,,,,,,,,,,,,,,,,,,,,,,1139,1147,1999, citations,entry_citation,4347,198534,1,,entry citation,,,,,"Hill, R. Blake and Degrado, William, F., ""Solution Structure of Alpha2D, a Nativelike de Novo Designed Protein,"" J. Am. Chem. Soc. 120, 1138-1145 (1998).","Solution Structure of Alpha2D, a Nativelike de Novo Designed Protein",published,journal,J. Am. Chem. Soc.,,120,6,,,,,,,,,,,,,,,,,,,,,,1138,1145,1998, citations,citation_1,4347,198535,2,,reference citation,,,,,"Kraulis, P.J. J. Magn. Res. 84:627-633(1989)",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4348,198553,1,,entry citation,,,,,"Pelton, J. G., Kustu, S., and Wemmer, D. E., ""Solution Structure of the DNA-binding Domain of NtrC with Three Alanine Substitutions,"" J. Mol. Biol., in preparation.","Solution Structure of the DNA-binding Domain of NtrC with Three Alanine Substitutions",in preparation,journal,J. Mol. Biol.,Journal of Molecular Biology,,na,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_1,4348,198554,2,,reference citation,,,7901122,,"Porter, S. C., North, A. K., Wedel, A. B., Kustu, S. (1993). Oligomerization of NtrC at the GlnA Enhancer Is Required for Transcriptional Activation. Genes Dev. 7, 2258-2273.",Oligomerization of NTRC at the glnA enhancer is required for transcriptional activation.,published,journal,Genes Dev.,Genes & development,7,11,,0890-9369,,,,,,,,,,,,,,,,,,,,2258,2273,1993,"To activate transcription of the glnA gene, the dimeric NTRC protein (nitrogen regulatory protein C) of enteric bacteria binds to an enhancer located approximately 100 bp upstream of the promoter. The enhancer is composed of two binding sites for NTRC that are three turns of the DNA helix apart. One role of the enhancer is to tether NTRC in high local concentration near the promoter to allow for its frequent interaction with sigma 54 holoenzyme by DNA looping. We have found that a second role of the enhancer is to ensure oligomerization of NTRC into a complex of at least two dimers that is required for transcriptional activation. Formation of this complex is greatly facilitated by a protein-protein interaction between NTRC dimers that is increased when the protein is phosphorylated." citations,entry_citation,4349,198574,1,,entry citation,,20016852,,,"Kroon, G. J. A., Martinez-Yamout, M. A., Krebs, J. F., Chung, J., Dyson, H. J., and Wright, P. E., ""Backbone Resonance Assignments for the Fv Fragment of the Catalytic Antibody NPN43C9 with Bound p-nitrophenol,"" J. Biomol. NMR 15, 83-84 (1999).","Backbone Resonance Assignments for the Fv Fragment of the Catalytic Antibody NPN43C9 with Bound p-nitrophenol",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,15,,,,,,,,,,,,,,,,,,,,,,,83,84,1999, citations,citation_1,4349,198575,2,,reference citation,,,8520220,,"Delaglio et al. J. Biomol. NMR, 6, 277 (1995)",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,citation_2,4349,198576,3,,reference citation,,,,,"Johson et al. J. Biomol. NMR, 4, 603 (1994)",NMR View: A computer program for the visualization and analysis of NMR data,,,J. Biomol. NMR,,4,5,,,,,,,,,,,,,,,,,,,,,,603,614,1994, citations,citation_3,4349,198577,4,,reference citation,,,8477186,,"Grezsiek et al. J. Biomol. NMR, 3, 185 (1993)",Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N-enriched proteins,,,J. Biomol. NMR,,3,2,,,,,,,,,,,,,,,,,,,,,,185,204,1993, citations,entry_citation,4362,198846,1,,entry citation,,,,,,"Structure determination by restrained molecular dynamics using NMR pseudocontact shifts as experimentally determined constraints",published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,121,,,,,,,,,,,,,,,,,,,,,,,9276,9285,1999, citations,entry_citation,435,198599,1,,entry citation,,,,,"Driscoll, Paul C., Clore, G. Marius, Marion, Dominique, Wingfield, Paul, Gronenborn, Angela M., ""Complete Resonance Assignment for the Polypeptide Backbone of Interleukin 1beta Using Three-Dimensional Heteronuclear NMR Spectroscopy,"" Biochemistry 29, 3542-3556 (1990).","Complete Resonance Assignment for the Polypeptide Backbone of Interleukin 1beta Using Three-Dimensional Heteronuclear NMR Spectroscopy",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,3542,3556,1990, citations,entry_citation,4350,198612,1,,entry citation,,,,,"Burlacu-Miron, S., Gilles, A.-M., Popescu, A, Barzu, O. and Craescu, C. T. ""Multinuclear Magnetic Resonance Studies of Escherichia coli Adenylate Kinase in Free and Bound Forms: Resonance Assignment, Secondary Structure and Ligand Binding"", in press.","NMR Studies on Escherichia coli Adenylate Kinase, Free and in Complex with AP5A",in press,journal,Eur. J. Biochem.,European Journal of Biochemistry,264,na,,,,,,,,,,,,,,,,,,,,,,765,774,1999, citations,entry_citation,4351,198632,1,,entry citation,,99351641,10424355,,,"A 30-residue Fragment of the Carp Granulin-1 Protein Folds into a Stack of two Beta-hairpins Similar to that found in the Native Protein",published,journal,J. Pept. Res.,,53,5,,,,,,,,,,,,,,,,,,,,,,590,597,1999, citations,entry_citation,4352,198649,1,,entry citation,,20252387,,,"Whittaker, S. B.-M., Czisch, M., Wechselberger, R., Kaptein, R., Hemmings, A. M., James, R., Kleanthous, C., and Moore, G. R., ""Slow Conformational Dynamics of an Endonuclease Persist in its Complex with its Natural Protein Inhibitor,"" Protein Sci. 9, 713-720 (2000).","Slow Conformational Dynamics of an Endonuclease Persist in its Complex with its Natural Protein Inhibitor",published,journal,Protein Sci.,Protein Science,9,,,,,,,,,,,,,,,,,,,,,,,713,720,2000, citations,citation_one,4352,198650,2,,reference citation,,,8520220,,"Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J. & Bax, A. (1995) J. Biomol. NMR 6, 277-293",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,citation_two,4352,198651,3,,reference citation,,,,,"Bartels, C., Xia, T.-H., Billeter, M., Guentert, P. & Wuethrich, K. (1995) J. Biomol. NMR 6, 1-10",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_three,4352,198652,4,,reference citation,,,2646600,,"Eaton, T. & James, R. (1989) Nucleic Acids Res. 17, 1761-1761",Complete nucleotide sequence of the colicin E9 (cei) gene.,published,journal,Nucleic Acids Res.,Nucleic acids research,17,4,,0305-1048,,,,,,,,,,,,,,,,,,,,1761,1761,1989, citations,citation_four,4352,198653,5,,reference citation,,,3312476,,"James, R., Jarvis, M. & Barker, D.F. (1987) J. Gen. Microbiol. 133, 1553-1562.",Nucleotide sequence of the immunity and lysis region of the ColE9-J plasmid.,published,journal,J. Gen. Microbiol.,Journal of general microbiology,133,6,,0022-1287,,,,,,,,,,,,,,,,,,,,1553,1562,1987,"We have determined the nucleotide sequence of a 1500 bp fragment of the ColE9-J plasmid which encodes colicin E9 immunity and colicin E5 immunity and contains two lys genes. Open reading frames corresponding to the four genes have been located and their position confirmed by transposon mutagenesis of sub-clones of the ColE9-J plasmid. The E9imm gene shows 69% homology at both the nucleotide and the amino acid level to the previously sequenced E2imm gene. The E5imm gene shows little homology to any other E colicin immunity gene which has been sequenced. The lys gene distal to the 3' end of the E5imm gene shows considerable sequence homology to all other previously sequenced E colicin lys genes. The lys gene distal to the 3' end of the E9imm gene is identical to the pColE2 and pColE3 lys genes for the first 59 nucleotides but encodes a much smaller gene product than any other lys gene which has been sequenced. The two lys genes sequenced here are exceptions to Shepherd's rule concerning the number of RNY codons in the three possible reading frames." citations,entry_citation,4353,198673,1,,entry citation,,,,,"Volk, D. E., Thiviyanathan, V., House, P. G., Lloyd, S., and Gorenstein, D. G., ""1H, 13C, and 15N Resonance Assignments of C-terminal Domain of MutY,"" J. Biomol. NMR, submitted.","1H, 13C, and 15N Resonance Assignments of C-terminal Domain of MutY",submitted,journal,J. Biomol. NMR,Journal of Biomolecular NMR,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_1,4353,198674,2,,reference citation,,,9287157,,"Manuel, R.C., & Lloyd, R.S., (1997) Biochemistry, 36, 11140-11152","Cloning, overexpression, and biochemical characterization of the catalytic domain of MutY.",published,journal,Biochemistry,Biochemistry,36,37,,0006-2960,,,,,,,,,,,,,,,,,,,,11140,11152,1997,"Proteolysis of MutY with trypsin indicated that this DNA mismatch repair enzyme could exist as two modules and that the N-terminal domain (Met1-Lys225), designated as p26, could serve as the catalytic domain [Manuel et al. (1996) J. Biol. Chem. 271, 16218-16226]. In this study, the p26 domain has been cloned, overproduced, and purified to homogeneity. Synthetic DNA duplexes containing mismatches, generated with regular bases and nucleotide analogs containing altered functional groups, have been used to characterize the substrate specificity and mismatch repair efficiency of p26. In general, p26 recognized and cleaved most of the substrates which were catalyzed by the intact protein. However, p26 displayed enhanced specificity for DNA containing an inosine. guanine mismatch, and the specificity constant (Kcat/Km) was 2-fold higher. The truncated MutY was able to cleave DNA containing an abasic site with equal efficiency. Dissociation constants (Kd) were obtained for p26 on noncleavable DNA substrates containing a tetrahydrofuran (abasic site analog) or a reduced abasic site. p26 bound these substrates with high specificity, and the Kd values were 3-fold higher when compared to the intact MutY. p26 contains both DNA glycosylase and AP lyase activities, and we provide evidence for a reaction mechanism that proceeds through an imino intermediate. Thus, we have shown for the first time that deletion of 125 amino acids at the C-terminus of MutY generates a stable catalytic domain which retains the functional identity of the intact protein." citations,entry_citation,5646,229375,1,,entry citation,,,14675814,,,Random coil carbon chemical shifts of deoxyribonucleic acids,published,journal,J. Magn. Reson.,,166,1,,,,,,,,,,,,,,,,,,,,,,11,18,2004, citations,entry_citation,4354,198687,1,,entry citation,,,,,"Gardner, K. H., Zhang, X., Gehring, K., and Kay, L. E., ""Solution NMR Studies of a 42kDa Escherichia coli Maltose Binding Protein/Beta-Cyclodextrin Complex: Chemical Shift Assignments and Analysis,"" J. Am. Chem. Soc. 120, 11738-11748 (1998).","Solution NMR Studies of a 42kDa Escherichia coli Maltose Binding Protein/ Beta-Cyclodextrin Complex: Chemical Shift Assignments and Analysis",published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,120,45,,,,,,,,,,,,,,,,,,,,,,11738,11748,1998, citations,reference_1,4354,198688,2,,reference citation,,,,,"Gardner, K.H., Zhang, X., Gehring, K. and Kay, L.E. ""Solution NMR Studies of a 42KDa Escherichia coli Maltose Binding Protein/Beta-Cyclodextrin Complex: Chemical Shift Assignments and Analysis."" J. Am. Chem. Soc. 120(1998): 11738-11748.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4355,198705,1,,entry citation,,99356013,10426954,,,"The Tetramerization Domain of the Mnt Repressor Consists of two Right-handed Coiled Coils",published,journal,Nat. Struct. Biol.,,6,8,,,,,,,,,,,,,,,,,,,,,,755,759,1999, citations,entry_citation,4357,198724,1,,entry citation,,99380399,,,"Jabet, C., Gitti, R., Summers, M.F., and Wolberger, C., ""NMR studies of the Pbx1 TALE Homeodomain Protein free in Solution and bound to DNA : Proposal for a Mechanism of HoxB1-Pbx1-DNA Complex Assembly"", J. Mol. Biol. 291, 521- 530 (1999).","NMR studies of the Pbx1 TALE Homeodomain Protein free in Solution and bound to DNA : Proposal for a Mechanism of HoxB1-Pbx1-DNA Complex Assembly",published,journal,J. Mol. Biol.,Journal of Molecular Biology,291,3,,,,,,,,,,,,,,,,,,,,,,521,530,1999, citations,entry_citation,4358,198745,1,,entry citation,,99380399,,,"Jabet, C., Gitti, R., Summers, M.F., and Wolberger, C., ""NMR studies of the Pbx1 TALE Homeodomain Protein free in Solution and bound to DNA : Proposal for a Mechanism of HoxB1-Pbx1-DNA Complex Assembly"", J. Mol. Biol. 291, 521- 530 (1999).","NMR studies of the Pbx1 TALE Homeodomain Protein free in Solution and bound to DNA : Proposal for a Mechanism of HoxB1-Pbx1-DNA Complex Assembly",published,journal,J. Mol. Biol.,Journal of Molecular Biology,291,3,,,,,,,,,,,,,,,,,,,,,,521,530,1999, citations,entry_citation,4359,198766,1,,entry citation,,99380399,,,"Jabet, C., Gitti, R., Summers, M.F., and Wolberger, C., ""NMR studies of the Pbx1 TALE Homeodomain Protein free in Solution and bound to DNA : Proposal for a Mechanism of HoxB1-Pbx1-DNA Complex Assembly"", J. Mol. Biol. 291, 521- 530 (1999).","NMR studies of the Pbx1 TALE Homeodomain Protein free in Solution and bound to DNA : Proposal for a Mechanism of HoxB1-Pbx1-DNA Complex Assembly",published,journal,J. Mol. Biol.,Journal of Molecular Biology,291,3,,,,,,,,,,,,,,,,,,,,,,521,530,1999, citations,entry_citation,436,198789,1,,entry citation,,,,,"Feng, Yiqing, Englander, S. Walter, ""Salt-Dependent Structure Change and Ion Binding in Cytochrome c Studied by Two-Dimensional Proton NMR,"" Biochemistry 29, 3505-3509 (1990).","Salt-Dependent Structure Change and Ion Binding in Cytochrome c Studied by Two-Dimensional Proton NMR",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,3505,3509,1990, citations,entry_citation,4360,198805,1,,entry citation,,,,,"Ubach, J., Garcia, J., Nittler, M.P., Sudhof, T., and Rizo, J., ""Structure of the Janus-faced C2B Domain of Rabphilin,"" Nature Cell Biol. 1, 106-112 (1999).",Structure of the Janus-faced C2B Domain of Rabphilin,published,journal,Nature Cell Biol.,Nature Cell Biology,1,,,,,,,,,,,,,,,,,,,,,,,106,112,1999, citations,entry_citation,4361,198822,1,,entry citation,,,,,,"Structure determination by restrained molecular dynamics using NMR pseudocontact shifts as experimentally determined constraints",published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,121,,,,,,,,,,,,,,,,,,,,,,,9276,9285,1999, citations,ref_1,4361,198823,2,,reference citation,,,9751997,,"Gochin M. Nuclear magnetic resonance characterization of a paramagnetic DNA-drug complex with high spin cobalt; assignment of the 1H and 31P NMR spectra, and determination of electronic, spectroscopic and molecular properties. J Biomol NMR. 1998 Aug;12(2):243-57","Nuclear magnetic resonance characterization of a paramagnetic DNA-drug complex with high spin cobalt; assignment of the 1H and 31P NMR spectra, and determination of electronic, spectroscopic and molecular properties.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,12,2,,0925-2738,,,,,,,,,,,,,,,,,,,,243,257,1998,"The proton NMR spectrum of the ternary complex between the octamer duplex d(TTGGCCAA)2, two molecules of the drug chromomycin-A3, and a divalent cobalt ion has been assigned. Assignment procedures used standard two-dimensional techniques and relied upon the expected NOE contacts observed in the equivalent diamagnetic complex containing zinc. The magnetic susceptibility tensor for the cobalt was determined and used to calculate shifts for all nuclei, aiding in the assignment process and verification. Relaxation, susceptibility, temperature and field dependence studies of the paramagnetic spectrum enabled determination of electronic properties of the octahedral cobalt complex. The electronic relaxation tau(s) was determined to be 2.5 +/- 1.5 ps; the effective isotropic g value was found to be 2.6 +/- 0.2, indicating strong spin-orbit coupling. The magnetic susceptibility tensor was determined to be chi(xx) = 8.9 x 10(-3) cm3/mol, chi(yy) = 9.5 x 10(-3) cm3/mol, chi(zz) = 12.8 * 10(-3) cm3/mol. A tentative rotational correlation time of 8 ns was obtained for the complex. Both macroscopic and microscopic susceptibility measurements revealed deviations from Curie behavior over the temperature range accessible in the study. Non-selective relaxation rates were found to be inaccurate for defining distances from the metal center. However, pseudocontact shifts could be calculated with high accuracy using the dipolar shift equation. Isotropic hyperfine shifts were factored into contact and dipolar terms, revealing that the dipolar shift predominates and that contact shifts are relatively small." citations,ref_2,4361,198824,3,,reference citation,,,10801486,,"Gochin M. Structure with Folding & Design., 2000 Apr 15, 8(4):441-52",A high-resolution structure of a DNA-chromomycin-Co(II) complex determined from pseudocontact shifts in nuclear magnetic resonance.,published,journal,Structure,"Structure (London, England : 1993)",8,4,,0969-2126,,,,,,,,,,,,,,,,,,,,441,452,2000,"BACKGROUND: The drug chromomycin-A(3) binds to the minor groove of DNA and requires a divalent metal ion for complex formation. (1)H, (31)P and (13)C pseudocontact shifts occurring in the presence of a tightly bound divalent cobalt ion in the complex between d(TTGGCCAA)(2) and chromomycin-A(3) have been used to determine the structure of the complex. The accuracy of the structure was verified by validation with nuclear Overhauser enhancements (NOEs) and J-coupling constants not used in the structure calculation. RESULTS: The final structure was determined to 0.7 A resolution. The structure was compared with a structure obtained in an earlier study using NOEs, in order to assess the accuracy of NOEs in giving global structural information for a DNA complex. Although some basic features of the structures agreed, they differed substantially in the fine structural details and in the DNA axis curvature generated by the drug. The distortion of base-pair planarity that was observed in the NOE structure was not seen in our structure. Differences in drug orientation and hydrogen bonding also occurred. The curvature and elongation of the DNA that was obtained previously was not found to occur in our study. CONCLUSIONS: The use of pseudocontact shifts has enabled us to obtain a high-precision global structure of the chromomycin-DNA complex, which provides an accurate template on which to consider targeting minor groove binding drugs. The effect of such binding is not propagated far along the helix but is restricted to a local kink in the axis that reverts to its original direction within four base pairs." citations,citation_1,5646,229376,2,,reference citation,,,12522297,,,Random Coil Proton Chemical Shifts of Deoxyribonucleic Acids,published,journal,J. Biomol. NMR,,24,4,,,,,,,,,,,,,,,,,,,,,,329,337,2002, citations,ref_1,4362,198847,2,,reference citation,,,9751997,,"Gochin M. Nuclear magnetic resonance characterization of a paramagnetic DNA-drug complex with high spin cobalt; assignment of the 1H and 31P NMR spectra, and determination of electronic, spectroscopic and molecular properties. J Biomol NMR. 1998 Aug;12(2):243-57","Nuclear magnetic resonance characterization of a paramagnetic DNA-drug complex with high spin cobalt; assignment of the 1H and 31P NMR spectra, and determination of electronic, spectroscopic and molecular properties.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,12,2,,0925-2738,,,,,,,,,,,,,,,,,,,,243,257,1998,"The proton NMR spectrum of the ternary complex between the octamer duplex d(TTGGCCAA)2, two molecules of the drug chromomycin-A3, and a divalent cobalt ion has been assigned. Assignment procedures used standard two-dimensional techniques and relied upon the expected NOE contacts observed in the equivalent diamagnetic complex containing zinc. The magnetic susceptibility tensor for the cobalt was determined and used to calculate shifts for all nuclei, aiding in the assignment process and verification. Relaxation, susceptibility, temperature and field dependence studies of the paramagnetic spectrum enabled determination of electronic properties of the octahedral cobalt complex. The electronic relaxation tau(s) was determined to be 2.5 +/- 1.5 ps; the effective isotropic g value was found to be 2.6 +/- 0.2, indicating strong spin-orbit coupling. The magnetic susceptibility tensor was determined to be chi(xx) = 8.9 x 10(-3) cm3/mol, chi(yy) = 9.5 x 10(-3) cm3/mol, chi(zz) = 12.8 * 10(-3) cm3/mol. A tentative rotational correlation time of 8 ns was obtained for the complex. Both macroscopic and microscopic susceptibility measurements revealed deviations from Curie behavior over the temperature range accessible in the study. Non-selective relaxation rates were found to be inaccurate for defining distances from the metal center. However, pseudocontact shifts could be calculated with high accuracy using the dipolar shift equation. Isotropic hyperfine shifts were factored into contact and dipolar terms, revealing that the dipolar shift predominates and that contact shifts are relatively small." citations,ref_2,4362,198848,3,,reference citation,,,10801486,,"Gochin M. Structure with Folding & Design., 2000 Apr 15, 8(4):441-52",A high-resolution structure of a DNA-chromomycin-Co(II) complex determined from pseudocontact shifts in nuclear magnetic resonance.,published,journal,Structure,"Structure (London, England : 1993)",8,4,,0969-2126,,,,,,,,,,,,,,,,,,,,441,452,2000,"BACKGROUND: The drug chromomycin-A(3) binds to the minor groove of DNA and requires a divalent metal ion for complex formation. (1)H, (31)P and (13)C pseudocontact shifts occurring in the presence of a tightly bound divalent cobalt ion in the complex between d(TTGGCCAA)(2) and chromomycin-A(3) have been used to determine the structure of the complex. The accuracy of the structure was verified by validation with nuclear Overhauser enhancements (NOEs) and J-coupling constants not used in the structure calculation. RESULTS: The final structure was determined to 0.7 A resolution. The structure was compared with a structure obtained in an earlier study using NOEs, in order to assess the accuracy of NOEs in giving global structural information for a DNA complex. Although some basic features of the structures agreed, they differed substantially in the fine structural details and in the DNA axis curvature generated by the drug. The distortion of base-pair planarity that was observed in the NOE structure was not seen in our structure. Differences in drug orientation and hydrogen bonding also occurred. The curvature and elongation of the DNA that was obtained previously was not found to occur in our study. CONCLUSIONS: The use of pseudocontact shifts has enabled us to obtain a high-precision global structure of the chromomycin-DNA complex, which provides an accurate template on which to consider targeting minor groove binding drugs. The effect of such binding is not propagated far along the helix but is restricted to a local kink in the axis that reverts to its original direction within four base pairs." citations,entry_citation,4363,198870,1,,entry citation,,99370086,,,"Riek, R., Precheur, B., Wang, Y., Mackay, E. A., Wider, G., Guntert, P., Liu, A., Kaegi, J. H. R.., and Wuthrich, K., ""NMR Structure of the Sea Urchin (Strongylocentrotus purpuratus) Metallothionein MTA,"" J. Mol. Biol., 291,417-428 (1999).","NMR Structure of the Sea Urchin (Strongylocentrotus purpuratus) Metallothionein MTA",published,journal,J. Mol. Biol.,,291,,,,,,,,,,,,,,,,,,,,,,,417,428,1999, citations,entry_citation,4364,198894,1,,entry citation,,10549133,,,,"Dynamics of Stromelysin/Inhibitor Interactions Studied by 15N NMR Relaxation Measurements: Comparison of Ligand Binding to the S1-S3 and S1-S3 Subsites",published,journal,J. Biomol. NMR,,15,,,,,,,,,,,,,,,,,,,,,,,55,64,1999, citations,entry_citation,4365,198913,1,,entry citation,,10549133,,,,"Dynamics of Stromelysin/Inhibitor Interactions Studied by 15N NMR Relaxation Measurements: Comparison of Ligand Binding to the S1-S3 and S1-S3 Subsites",published,journal,J. Biomol. NMR,,15,,,,,,,,,,,,,,,,,,,,,,,55,64,1999, citations,entry_citation,4366,198934,1,,entry citation,,10549133,,,,"Dynamics of Stromelysin/Inhibitor Interactions Studied by 15N NMR Relaxation Measurements: Comparison of Ligand Binding to the S1-S3 and S1-S3 Subsites",published,journal,J. Biomol. NMR,,15,,,,,,,,,,,,,,,,,,,,,,,55,64,1999, citations,entry_citation,4367,198955,1,,entry citation,,20129263,10667801,,,Design of single-layer beta-sheets without a hydrophobic core,published,journal,Nature,,403,,,,,,,,,,,,,,,,,,,,,,,456,460,2000, citations,citation_1,4367,198956,2,,reference citation,,,,,"Pham, T. N. & Koide, S. (1998) NMR studies of Borrelia burgdorferi OspA, a 28 kDa protein containing a single-layer b-sheet. J. Biomol. NMR 11, 407-414.",,published,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_2,4367,198957,3,,reference citation,,,9461076,,"Pham, T.-N., Koide, A. & Koide, S. (1998) A stable single-layer b-sheet without a hydrophobic core. Nat. Struct. Biol. 5, 115-119.",A stable single-layer beta-sheet without a hydrophobic core.,published,journal,Nat. Struct. Biol.,Nature structural biology,5,2,,1072-8368,,,,,,,,,,,,,,,,,,,,115,119,1998,"Outer surface protein A from the Lyme disease spirochete Borrelia burgdorferi contains a single-layer beta-sheet connecting the N- and C-terminal globular domains. The central beta-sheet consists largely of polar amino acids and is solvent-exposed on both faces, which so far appears to be unique among known protein structures. We show that the single-layer beta-sheet segment is surprisingly stable (deltaG for hydrogen exchange is approximately 8 kcal mol(-1) at 45 degrees C). Possible factors contributing to the stability of the single-layer beta-sheet are discussed based on an analysis of the crystal structure." citations,entry_citation,4371,199054,1,,entry citation,,20149605,,,"Gorbatyuk, V. Y., Chen, Y-C., Wu, Y-J., Youle, R.J., and Huang, T-H., ""Sequence-specific 1H, 13C and 15N Resonance Assignments of Recombinant Onconase/P-30 Protein,"" J. Biomol. NMR 15, 343-344 (1999).","Sequence-specific 1H, 13C and 15N Resonance Assignments of Recombinant Onconase/P-30 Protein",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,15,,,,,,,,,,,,,,,,,,,,,,,343,344,1999, citations,entry_citation,4372,199072,1,,entry citation,,20221595,10756199,,,"Structures of the potassium-saturated, 2:1, and intermediate, 1:1, forms of a quadruplex DNA.",published,journal,Nucleic Acids Res.,,28,9,,,,,,,,,,,,,,,,,,,,,,1969,1977,2000, citations,entry_citation,4373,199085,1,,entry citation,,20142321,,,"Blomberg, N., Sattler, M., and Nilges, M., ""1H, 15N, and 13C Resonance Assignment of the PH Domain from C. elegans UNC-89,"" J. Biomol. NMR 15, 269-270 (1999).","1H, 15N, and 13C Resonance Assignment of the PH Domain from C. elegans UNC-89",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,15,,,,,,,,,,,,,,,,,,,,,,,269,270,1999, citations,entry_citation,5647,229389,1,,entry citation,,,14675814,,,Random coil carbon chemical shifts of deoxyribonucleic acids,published,journal,J. Magn. Reson.,,166,1,,,,,,,,,,,,,,,,,,,,,,11,18,2004, citations,citation_3,4367,198958,4,,reference citation,,,10200164,,"Koide, S., Bu, Z., Risal,D., Pham, T.-N., Nakagawa, T., Tamura, A. & Engelman, D. M. (1999) Multi-step denaturation of Borrelia burgdorferi OspA, a protein containing a single-layer b-sheet. Biochemistry 38, 4757-4767","Multistep denaturation of Borrelia burgdorferi OspA, a protein containing a single-layer beta-sheet.",published,journal,Biochemistry,Biochemistry,38,15,,0006-2960,,,,,,,,,,,,,,,,,,,,4757,4767,1999,"Outer surface protein A (OspA) from the Lyme disease spirochete, Borrelia burgdorferi, is a dumbbell-shaped protein in which two globular domains are connected by a three-stranded beta-sheet segment that is solvent-exposed on both faces. Previous studies showed that the whole protein, including the single-layer beta-sheet, is highly rigid. To elucidate the folding mechanism and the role of the central beta-sheet in the formation of the rigid molecule, we investigated the equilibrium thermal denaturation reaction of OspA. We applied differential scanning calorimetry, heteronuclear NMR spectroscopy, and solution small-angle X-ray scattering (SAXS) to characterize the reaction in detail. All three techniques revealed that OspA denatures in two separable cooperative transitions. NMR measurements on OspA specifically 15N-labeled at Lys residues identified the locations of the two folding units and revealed that the C-terminal segment is less stable than the remaining N-terminal segment. The boundary between the two folding units is located within the central beta-sheet. The interconversion among the three folding states (fully folded, C-terminus unfolded, and fully denatured) is slow relative to chemical shift differences (<24 Hz), indicating that there are significant kinetic barriers in the denaturation reactions. SAXS measurements determined the radius of gyration of the native protein to be 25.0 +/- 0.3 A, which increases to 34.4 +/- 1.0 A in the first transition, and then to 56.1 +/- 1.6 A in the second transition. Thus, the intermediate state, in which the C-terminal folding unit is already denatured, is still compact. These results provide a basis for elucidating the folding mechanism of OspA." citations,entry_citation,4368,198969,1,,entry citation,,98301588,,,"Xiang, B., Weiler, S., Nirenberg, M., and Ferretti, J.A., ""Structural Basis of an Embryonically Lethal Single Ala --> Thr Mutation in the vnd/NK-2 Homeodomain,"" Proc. Natl. Acad. Sci. USA 95, 7412-7416 (1998).","Structural Basis of an Embryonically Lethal Single Ala --> Thr Mutation in the vnd/NK-2 Homeodomain",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,95,,,,,,,,,,,,,,,,,,,,,,,7412,7416,1998, citations,entry_citation,4369,198997,1,,entry citation,,,,,"Helgstrand, M., Rak, A. V., Allard, P., Davydova, N., Garber, M. B., and Hard, T., ""1H, 15N and 13C Assigned Chemical Shifts of S19 from Thermus thermophilus,"" personal communication (1999).","1H, 15N and 13C Assigned Chemical Shifts of S19 from Thermus thermophilus",published,personal communication,,,,,,,,,,,,,,,,,,,,,,,,,,,,1999, citations,ref-1,4369,198998,2,,reference citation,,,7830586,,"Kjaer, M., Andersen, K. V. & Poulsen, F. M. (1994). Automated and semiautomated analysis of homo- and heteronuclear multidimensional nuclear magnetic resonance spectra of proteins: the program Pronto. Methods Enzymol 239, 288-307.",Automated and semiautomated analysis of homo- and heteronuclear multidimensional nuclear magnetic resonance spectra of proteins: the program Pronto.,published,journal,Meth. Enzymol.,Methods in enzymology,239,,,0076-6879,,,,,,,,,,,,,,,,,,,,288,307,1994, citations,entry_citation,437,199015,1,,entry citation,,,,,"Feng, Yiqing, Englander, S. Walter, ""Salt-Dependent Structure Change and Ion Binding in Cytochrome c Studied by Two-Dimensional Proton NMR,"" Biochemistry 29, 3505-3509 (1990).","Salt-Dependent Structure Change and Ion Binding in Cytochrome c Studied by Two-Dimensional Proton NMR",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,3505,3509,1990, citations,entry_citation,4370,199031,1,,entry citation,,20142319,,,"El-Joubary, A., Bruix, M., Santoro, J., Cafaro, V., Scognamiglio, R., Di Donato, A., D'Alessio, G., Kover, K.E., Batta, G., Szilagyi, L, and Rico, M., ""1H and 15N Sequential Assignment and Solution Secondary Structure of 15N Labelled Human Pancreatic Ribonuclease,"" J. Biomol. NMR 15, 265-266 (1999).","1H and 15N Sequential Assignment and Solution Secondary Structure of 15N Labelled Human Pancreatic Ribonuclease",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,15,,,,,,,,,,,,,,,,,,,,,,,265,266,1999, citations,ref_1,4370,199032,2,,reference citation,,,6201087,,"Beintema, J.J., Wietzes, P. Weickmann, J.L. and Glitz, D.G. Anal. Biochem. (1984) 136, 48-64",The amino acid sequence of human pancreatic ribonuclease.,published,journal,Anal. Biochem.,Analytical biochemistry,136,1,,0003-2697,,,,,,,,,,,,,,,,,,,,48,64,1984,"The primary structure of human (Homo sapiens) pancreatic ribonuclease has been determined by automatic sequencing of the native protein and by analysis of peptides obtained by cleavage with proteolytic enzymes, cyanogen bromide, and hydroxylamine. The following sequence was deduced: (sequence in text). Human pancreatic ribonuclease differs at 37 positions from bovine pancreatic ribonuclease. In addition the human enzyme has three more residues at the C-terminus. About half of the enzyme molecules contain carbohydrate attached to the sequence Asn-Met-Thr (34-36). Two other Asn-X-Ser/Thr sequences are carbohydrate free. Human pancreatic ribonuclease contains many positively charged residues, especially near the N-terminus, while negatively charged residues are more concentrated near the C-terminus." citations,ref_2,4370,199033,3,,reference citation,,,7654266,,"Russo, N., de NIgris, M., Ciardello, A., Di Donato, A and D'Alessio, G. FEBS Lett. (1993) 333, 233-237. Anal. Biochem. (1984) 136, 48-64","Expression in mammalian cells, purification and characterization of recombinant human pancreatic ribonuclease.",published,journal,FEBS Lett.,FEBS letters,333,3,,0014-5793,,,,,,,,,,,,,,,,,,,,233,237,1993,"A synthetic cDNA coding for human pancreatic RNase, equipped with a secretion signal sequence, was cloned and stably expressed in Chinese hamster ovary cells. The recombinant RNase, secreted into the culture medium, was purified and characterized. It was found to be indistinguishable, by structural and catalytic parameters, from the enzyme isolated from human pancreas. Furthermore, the glycosylated forms were separated from the non-glycosylated form. Up until now, human RNases have been isolated only in small amounts from autopic specimens. This has hindered the exploitation of a human RNase for the construction of immunotolerated immunotoxins. On the other hand, the availability of an effective system for the expression of a human RNase may render feasible the transfer, by protein engineering, of the interesting pharmacological actions of non-human RNase [1993 Trends Cell Biol. 3, 106-109] to an immunotolerated, human RNase." citations,ref_3,4370,199034,4,,reference citation,,,10393896,,"Piccoli, R., Di Gaetano, S., De Lorenzo, C., Grauso, M., Monaco, C., Saplleti Cernia, D., Lacetti, P. Cinatl, J., Matousek, J. D'Alessio, G. Proc. Natl. Academ. Sci. USA (1999) in press",A dimeric mutant of human pancreatic ribonuclease with selective cytotoxicity toward malignant cells.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,96,14,,0027-8424,,,,,,,,,,,,,,,,,,,,7768,7773,1999,"Monomeric human pancreatic RNase, devoid of any biological activity other than its RNA degrading ability, was engineered into a dimeric protein with a cytotoxic action on mouse and human tumor cells, but lacking any appreciable toxicity on mouse and human normal cells. This dimeric variant of human pancreas RNase selectively sensitizes to apoptotic death cells derived from a human thyroid tumor. Because of its selectivity for tumor cells, and because of its human origin, this protein represents a potentially very attractive, novel tool for anticancer therapy." citations,ref_4,4370,199035,5,,reference citation,,,,,"Youle, R.J. and D'Alessio, G. Ribonucleases. Structure and Functions (D'Alessio, G. & Riordan, F.J. Eds) (1997) pp491-514, Academic Press, New York, NY.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_2,4373,199087,3,,reference citation,,,8520220,,"Delaglio, F., S. Greziek, G. Vuister, G. Zhu, J. Pfeifer, and A. Bax, `{NMRP}ipe: a multidimensional spectral processing program based on {UNIX} pipes.' J. Biomol., 6, 277-293 (1995).",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,entry_citation,4374,199104,1,,entry citation,,,,,,Mutational and structural analyses of the ribonucleotide reductase inhibitor sml1 define its rnr1 interaction domain whose inactivation allows suppression of mec1 and rad53 lethality,published,journal,Mol. Cell. Biol.,,20,23,,,,,,,,,,,,,,,,,,,,,,9076,9083,2000, citations,entry_citation,4375,199120,1,,entry citation,,21151318,11256811,,,"Chemical Shifts in Denatured Proteins: Resonance Assignments for Denatured Ubiquitin and Comparisons with other Denatured Proteins",published,journal,J. Biomol. NMR,,19,2,,,,,,,,,,,,,,,,,,,,,,153,165,2001, citations,entry_citation,4376,199133,1,,entry citation,,,,,"Coles, M., Diercks, T., Liermann, J., Groeger, A., Rockel, B., Baumeister, W., Koretke, K.K., Lupas, A., Peters, J., Kessler, H., ""The Solution Structure of VAT-N Reveals a 'Missing Link' in the Evolution of Complex Enzymes from a Simple babb Element."" Current Biology 1999, 9:1158-1168.","The Solution Strucutre of VAT-N Reveals a Missing Link in the Evolution of Complex Enzymes from a Simple bbab Element.",published,journal,Current Biology,,9,,,,,,,,,,,,,,,,,,,,,,,1158,1168,1999, citations,citation_1,4376,199134,2,,reference citation,,,10543442,,"Golbik, R., Lupas, A., Koretke, K.K., Peters, J., Baumeister, W. The Janus Face of the Archaeal Cdc48/p97 Homologue VAT: Protein Folding versus Unfolding. Biological Chemistry 1999, 380:1049-1062.",The Janus face of the archaeal Cdc48/p97 homologue VAT: protein folding versus unfolding.,published,journal,Biol. Chem.,Biological chemistry,380,9,,1431-6730,,,,,,,,,,,,,,,,,,,,1049,1062,1999,"Members of the AAA family of ATPases have been implicated in chaperone-like activities. We used the archaeal Cdc48/p97 homologue VAT as a model system to investigate the effect of an AAA protein on the folding and unfolding of two well-studied, heterologous substrates, cyclophilin and penicillinase. We found that, depending on the Mg2+ concentration, VAT assumes two states with maximum rates of ATP hydrolysis that differ by an order of magnitude. In the low-activity state, VAT accelerated the refolding of penicillinase, whereas in the high-activity state, it accelerated its unfolding. Both reactions were ATP-dependent. In its interaction with cyclophilin, VAT was ATP-independent and only promoted refolding. The N-terminal domain of VAT, which lacks ATPase activity, also accelerated the refolding of cyclophilin but showed no effect on penicillinase. VAT appears to be structurally equivalent over its entire length to Sec18/NSF, suggesting that these results apply more broadly to group II AAA proteins." citations,citation_2,4376,199135,3,,reference citation,,,9119075,,"Pamnani, V., Tamura T., Lupas, A., Peters, J.,Cejka, Z., Ashraf, W. & Baumeister, W. FEBS Lett. 404 263-268 (1997)","Cloning, sequencing and expression of VAT, a CDC48/p97 ATPase homologue from the archaeon Thermoplasma acidophilum.",published,journal,FEBS Lett.,FEBS letters,404,2-3,,0014-5793,,,,,,,,,,,,,,,,,,,,263,268,1997,"A member of the AAA family of Mg2(+)-ATPases from the archaeon Thermoplasma acidophilum has been cloned and expressed in Escherichia coli. The protein, VCP-like ATPase of Thermoplasma acidophilum (VAT), is a homologue of SAV from Sulfolobus acidocaldarius and CdcH of Halobacterium salinarium, and belongs to the CDC48/VCP/p97 subfamily. The deduced product of the vat gene is 745 residues long (Mr 83,000), which has an optimal Mg2(+)-ATPase activity at 70 degrees C. Electron microscopy shows the purified protein to form single and double homo-hexameric rings. Although the symmetry is different, the appearance of the complexes formed of two rings resembles the 20S proteasome and Hsp60/GroEL." citations,citation_3,4376,199136,4,,reference citation,,,8019132,,"Wishart, D.S. & Sykes, B.D. J. Biomol. NMR 4 171-180 (1994)",The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,4,2,,0925-2738,,,,,,,,,,,,,,,,,,,,171,180,1994,"A simple technique for identifying protein secondary structures through the analysis of backbone 13C chemical shifts is described. It is based on the Chemical-Shift Index [Wishart et al. (1992) Biochemistry, 31, 1647-1651] which was originally developed for the analysis of 1H(alpha) chemical shifts. By extending the Chemical-Shift Index to include 13C(alpha), 13C(beta) and carbonyl 13C chemical shifts, it is now possible to use four independent chemical-shift measurements to identify and locate protein secondary structures. It is shown that by combining both 1H and 13C chemical-shift indices to produce a 'consensus' estimate of secondary structure, it is possible to achieve a predictive accuracy in excess of 92%. This suggests that the secondary structure of peptides and proteins can be accurately obtained from 1H and 13C chemical shifts, without recourse to NOE measurements." citations,entry_citation,4377,199153,1,,entry citation,,20120586,10653641,,,"Solution structure of the CBM10 cellulose binding module from Pseudomonas Xylanase A",published,journal,Biochemistry,Biochemistry,39,,,,,,,,,,,,,,,,,,,,,,,978,984,2000, citations,entry_citation,4383,199288,1,,entry citation,,20138001,10672021,,,"The wide binding properties of a wheat nonspecific lipid transfer protein Solution structure of a complex with prostaglandin B2",published,journal,Eur. J. Biochem.,,267,,,,,,,,,,,,,,,,,,,,,,,1117,1124,2000, citations,entry_citation,4384,199303,1,,entry citation,,20142320,10677830,,,"1H, 13C, and 15N Chemical Shift Assignments of the Capsid Protein from Rous Sarcoma Virus",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,15,,,,,,,,,,,,,,,,,,,,,,,267,268,1999, citations,entry_citation,4453,200870,1,,entry citation,,,,,,"Letter to the Editor: Assignment of the 1H, 13C and 15N resonances of the C-terminal EF-hands of alpha-actinin in a 14 kDa complex with Z-repeat 7 of titin",published,journal,J. Biomol. NMR,,16,3,,,,,,,,,,,,,,,,,,,,,,277,278,2000, citations,reference_1,4453,200871,2,,reference citation,,92250531,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref._1,4377,199154,2,,reference citation,,,7717975,,"Ferreira, LMA, Durrant, AJ, Hall, J, Hazlewood, GP, Gilbert, HJ (1990) Biochem. J., 307, 191-195",A modular xylanase containing a novel non-catalytic xylan-specific binding domain.,published,journal,Biochem. J.,The Biochemical journal,307 ( Pt 1),,,0264-6021,,,,,,,,,,,,,,,,,,,,191,195,1995,"Xylanase D (XYLD) from Cellulomonas fimi contains a C-terminal cellulose-binding domain (CBD) and an internal domain that exhibits 65% sequence identity with the C-terminal CBD. Full-length XYLD binds to both cellulose and xylan. Deletion of the C-terminal CBD from XYLD abolishes the capacity of the enzyme to bind to cellulose, although the truncated xylanase retains its xylan-binding properties. A derivative of XYLD lacking both the C-terminal CBD and the internal CBD homologue did not bind to either cellulose or xylan. A fusion protein consisting of the XYLD internal CBD homologue linked to the C-terminus of glutathione S-transferase (GST) bound to xylan, but not to cellulose, while GST bound to neither of the polysaccharides. The Km and specific activity of full-length XYLD and truncated derivatives of the enzyme lacking the C-terminal CBD (XYLDcbd), and both the CBD and the internal CBD homologue (XYLDcd), were determined with soluble and insoluble xylan as the substrates. The data showed that the specific activities of the three enzymes were similar for both substrates, as were the Km values for soluble substrate. However, the Km values of XYLD and XYLDcbd for insoluble xylan were significantly lower than the Km of XYLDcd. Overall, these data indicate that the internal CBD homologue in XYLD constitutes a discrete xylan-binding domain which influences the affinity of the enzyme for insoluble xylan but does not directly affect the catalytic activity of the xylanase. The rationale for the evolution of this domain is discussed." citations,ref._2,4377,199155,3,,reference citation,,,2507868,,"Hall, J, Hazlewood, GP, Huskisson, NS, Durrant, AJ, Gilbert, HJ (1989) Mol. Microbiol., 3, 1211-1219",Conserved serine-rich sequences in xylanase and cellulase from Pseudomonas fluorescens subspecies cellulosa: internal signal sequence and unusual protein processing.,published,journal,Mol. Microbiol.,Molecular microbiology,3,9,,0950-382X,,,,,,,,,,,,,,,,,,,,1211,1219,1989,"The complete nucleotide sequence of the xynA gene coding for a xylanase (XYLA) expressed by Pseudomonas fluorescens subspecies cellulosa, has been determined. The structural gene consists of an open reading frame of 1833 bp followed by a TAA stop codon. Confirmation of the nucleotide sequence was obtained by comparing the predicted amino acid sequence with that derived by N-terminal analysis of purified forms of the xylanase. The signal peptide present at the N terminus of mature XYLA closely resembles signal peptides of other secreted proteins. Truncated forms of the xylanase gene, in which the sequence encoding the N-terminal signal peptide had been deleted, still expressed coli. XYLA contains domains which are homologous to an endoglucanase expressed by the same organism. These structures include serine-rich sequences. Bal31 deletions of xynA revealed the extent to which these conserved sequences, in XYLA, were essential for xylanase activity. Downstream of the TAA stop codon is a G + C-rich region of dyad symmetry (delta G = 24 kcal) characteristic of E. coli Rho-independent transcription terminators." citations,entry_citation,4378,199175,1,,entry citation,,,,,"Kragelund, B. B., Hauenschild, A., Carlstr?m, G., Pongs, O. and Finn B. E. ""Letter to the Editor: 1H, 13C, and 15N assignments of un-myristoylated Ca2+-frequenin, a synaptic efficacy modulator"" J. Biomol. NMR 16, 85-86 (2000).","Letter to the Editor: 1H, 13C, and 15N assignments of un-myristoylated Ca2+-frequenin, a synaptic efficacy modulator",published,journal,J. Biomol. NMR,,16,1,,,,,,,,,,,,,,,,,,,,,,85,86,2000, citations,ref_1,4378,199176,2,,reference citation,,,,,"Cavanagh, J., Fairbrother, W. J., Palmer, A. G., & Skelton, N. J. (1996) protein NMR spectroscopy, pp 175-176, Academic Press, New York",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4379,199195,1,,entry citation,,20087216,,,,NMR Solution Structure of the Human Prion Protein,published,journal,Proc. Natl. Acad. Sci. U. S. A.,,97,,,,,,,,,,,,,,,,,,,,,,,145,150,2000, citations,entry_citation,438,199220,1,,entry citation,,,,,"Feng, Yiqing, Englander, S. Walter, ""Salt-Dependent Structure Change and Ion Binding in Cytochrome c Studied by Two-Dimensional Proton NMR,"" Biochemistry 29, 3505-3509 (1990).","Salt-Dependent Structure Change and Ion Binding in Cytochrome c Studied by Two-Dimensional Proton NMR",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,3505,3509,1990, citations,entry_citation,4380,199235,1,,entry citation,,96271285,,,"Overduin, M., Tong, K. I., Kay, C. M., and Ikura, M., ""1H, 15N and 13C Resonance Assignments and Monomeric Structure of the Amino-Terminal Extracellular Domain of Epithelial Cadherin,"" J. Biomol. NMR 7, 173-189 (1996).","1H, 15N and 13C Resonance Assignments and Monomeric Structure of the Amino-Terminal Extracellular Domain of Epithelial Cadheri",published,journal,J. Biomol. NMR,,7,3,,,,,,,,,,,,,,,,,,,,,,173,189,1996, citations,entry_citation,4381,199251,1,,entry citation,,,,,,"Letter to the Editor: Sequence-specific 1H, 13C, and 15N assignments for the third EH domain of Eps15 (EH3)",published,journal,J. Biomol. NMR,,16,,,,,,,,,,,,,,,,,,,,,,,81,82,2000, citations,citation_1,4381,199252,2,,reference citation,,,8520220,,"Delaglio et al., J. Biomol NMR 6, 277-293 (1995)",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,citation_2,4381,199253,3,,reference citation,,,,,"Garret et al., J. Magn. Reson. 95, 214-220.(1995)",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4382,199270,1,,entry citation,,20427309,,,,"Solution Structure of a Zinc Substituted Eukaryotic Rubredoxin from the Cryptomonad Algal Guillardia theta",published,journal,Protein Sci.,Protein Science,9,8,,,,,,,,,,,,,,,,,,,,,,1474,1486,2000,"First NMR assignments of a eukaryotic rubredoxin" citations,ref-1,4382,199271,2,,reference citation,,,,,"Johnson, B.A. and Blevins, R.A. J. Biomol. NMR 4(1994), 603-614",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,reference_2,4453,200872,3,,reference citation,,97092327,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4385,199324,1,,entry citation,,20414184,,,"Kozlov, G., Ekiel, I., Beglova, N., Yee, A., Dharamsi, A., Engel, A., Siddiqui, N., Nong, A., and Gehring, K., ""Rapid Fold and Sructure Determination of the Archaeal Translation Elongation Factor 1beta from Methanobacterium thermoautotrophicum,"" J. Biomol. NMR 17, 187-194 (2000).","Rapid Fold and Sructure Determination of the Archaeal Translation Elongation Factor 1beta from Methanobacterium thermoautotrophicum",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,17,3,,,,,,,,,,,,,,,,,,,,,,187,194,2000, citations,entry_citation,4386,199348,1,,entry citation,,10852703,,,,"NMR Structure of Free RGS4 Reveals an Induced Conformational Change upon Binding G-alpha",published,journal,Biochemistry,Biochemistry,39,,,,,,,,,,,,,,,,,,,,,,,7063,7073,2000, citations,entry_citation,4387,199369,1,,entry citation,,98430981,,,"MANDARD, N., SODANO, P., LABBE, H., BONMATIN, J. M., BULET, P., HETRU, C., PTAK, M., and VOVELLE, F., ""Solution structure of thanatin, a potent bactericidal and fungicidal insect peptide, determined from 1H-2D NMR,"" Eur. J. Biochem. 256, 404-410 (1998).","Solution structure of thanatin, a potent bactericidal and fungicidal insect peptide, determined from 1H-2D NMR",published,journal,Eur. J. Biochem.,,256,,,,,,,,,,,,,,,,,,,,,,,404,410,1998, citations,entry_citation,4388,199385,1,,entry citation,,,,,,"Letter to the Editor: Backbone NMR assignments of a high molecular weight protein (47 kDa), cyclic AMP receptor protein (apo-CRP)",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,16,1,,,,,,,,,,,,,,,,,,,,,,79,80,2000, citations,ref-1,4388,199386,2,,reference citation,,,,,"Johnson, B. A. & Blevins, R. A. (1994) NMR View: A computer program for the visualization and analysis of NMR data. J. Biomol. NMR 4, 603-614.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref-2,4388,199387,3,,reference citation,,,8520220,,"Delaglio, F. Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J. & Bax, A. (1995) NMR Pipe: A multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,entry_citation,4389,199406,1,,entry citation,,20149604,,,"Kashimori, H., Yoshida, T., Kijima, H., Shimahara, H., Uchiyama, S., Ishino, T., Shuda, M., Nakano, H., Shibata, Y., Saihara, Y., Ohkubo, T., Yoshida, T., Kaji, A., and Kobayashi, Y., ""Backbone NMR Assignment and Secondary Structure of Ribosome Recycling Factor (RRF) from Pseudomonas aeruginosa,"" J. Biomol. NMR 15, 341-342 (1999).","Backbone NMR Assignment and Secondary Structure of Ribosome Recycling Factor (RRF) from Pseudomonas aeruginosa",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,15,,,,,,,,,,,,,,,,,,,,,,,341,342,1999, citations,ref_1,4389,199407,2,,reference citation,,96374905,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_2,4389,199408,3,,reference citation,,99138750,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_3,4389,199409,4,,reference citation,,,,,"Garrett, D.S., Powers, R., Gronenborn, A.M. and Clore, G.M. J. Magn. Reson., 95, 214-220 (1991).",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,439,199424,1,,entry citation,,,,,"Feng, Yiqing, Englander, S. Walter, ""Salt-Dependent Structure Change and Ion Binding in Cytochrome c Studied by Two-Dimensional Proton NMR,"" Biochemistry 29, 3505-3509 (1990).","Salt-Dependent Structure Change and Ion Binding in Cytochrome c Studied by Two-Dimensional Proton NMR",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,3505,3509,1990, citations,entry_citation,4390,199439,1,,entry citation,,,10605085,,,Backbone dynamics of the human CC-chemokine eotaxin,published,journal,J. Biomol. NMR,,15,2,,,,,,,,,,,,,,,,,,,,,,115,124,1999, citations,entry_citation,4391,199455,1,,entry citation,,,,,,"Isolation, purification, 1H NMR assignments and secondary structure characterization of a neurotoxin from Bungarus candidus",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,,in preparation citations,entry_citation,4392,199466,1,,entry citation,,99398329,,,"Yang, X-L., Kaenzig, C., Lee, M., and Wang, A. H.-J., ""Binding of AR-1-144, a tri-imidazole DNA minor groove binder, to CCGG sequence analyzed by NMR spectroscopy,"" Eur. J. Biochem. 263, 646-655 (1999).","Binding of AR-1-144, a tri-imidazole DNA minor groove binder, to CCGG sequence analyzed by NMR spectroscop",published,journal,Eur. J. Biochem.,European Journal of Biochemistry,263,3,,,,,,,,,,,,,,,,,,,,,,646,655,1999, citations,entry_citation,4393,199484,1,,entry citation,,20149606,10685345,,"Park, S., Liao, X., Johnson, M.E., and Fung, L.W., ""1H, 15N, and 13C NMR Backbone Assignments of the N-terminal Region of Human Erythrocyte alpha Spectrin Including one Structural Domain,"" J. Biomol. NMR 15, 345-346 (1999).","1H, 15N, and 13C NMR Backbone Assignments of the N-terminal Region of Human Erythrocyte alpha Spectrin Including one Structural Domain",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,15,,,,,,,,,,,,,,,,,,,,,,,345,346,1999, citations,entry_citation,4394,199498,1,,entry citation,,,,,"DE COCK, E., BLANQUET, S., LALLEMAND, J. -Y., and DARDEL, F., ""INTERACTION OF E. COLI TRANSLATION INITIATION FACTOR IF3 WITH THE RIBOSOME,"" in preparation.",INTERACTION OF E. COLI TRANSLATION INITIATION FACTOR IF3 WITH THE RIBOSOME,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_1,4394,199499,2,,reference citation,,7490747,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_2,4394,199500,3,,reference citation,,9054966,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4395,199515,1,,entry citation,,99016057,,,"Stoldt, M., Wohnert, J., Gorlach, M., and Brown, L. R., ""The NMR Structure of Escherichia coli Ribosomal Protein L25 shows Homology to General Stress Proteins and Glutaminyl-tRNA Synthetases,"" EMBO J. 17, 6377-6384 (1998).","The NMR Structure of Escherichia coli Ribosomal Protein L25 shows Homology to General Stress Proteins and Glutaminyl-tRNA Synthetases",published,journal,EMBO J.,,17,,,,,,,,,,,,,,,,,,,,,,,6377,6384,1998, citations,entry_citation,4396,199531,1,,entry citation,,99435967,10504384,,,"Inherent flexibility in a potent inhibitor of blood coagulation, recombinant nematode anticoagulant protein c2",published,journal,Eur. J. Biochem.,,265,,,,,,,,,,,,,,,,,,,,,,,539,548,1999, citations,ref_4,4396,199532,2,,reference citation,,,8700900,,"Stassens P, Bergum PW, Gansemans Y, Jespers L, Laroche Y, Huang S, Maki S, Messens J, Lauwereys M, Cappello M, Hotez PJ, Lasters I, Vlasuk GP. Anticoagulant repertoire of the hookworm Ancylostoma caninum. Proc Natl Acad Sci U S A. 1996 Mar 5;93(5):2149-54.",Anticoagulant repertoire of the hookworm Ancylostoma caninum.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,93,5,,0027-8424,,,,,,,,,,,,,,,,,,,,2149,2154,1996,"Hookworms are hematophagous nematodes that infect a wide range of mammalian hosts, including humans. There has been speculation for nearly a century as to the identity of the anticoagulant substances) used by these organisms to subvert host hemostasis. Using molecular cloning, we describe a family of potent small protein (75-84 amino acids) anticoagulants from the hookworm Ancylostoma caninum termed AcAP (A. caninum anticoagulant protein). Two recombinant AcAP members (AcAP5 and AcAP6) directly inhibited the catalytic activity of blood coagulation factor Xa (fXa), while a third form (AcAPc2) predominantly inhibited the catalytic activity of a complex composed of blood coagulation factor VIIa and tissue factor (fVIIa/TF). The inhibition of fVIIa/TF was by a unique mechanism that required the initial formation of a binary complex of the inhibitor with fXa at a site on the enzyme that is distinct from the catalytic center (exo-site). The sequence of AcAPc2 as well as the utilization of an exo-site on fXa distinguishes this inhibitor from the mammalian anticoagulant TFPI (tissue factor pathway inhibitor), which is functionally equivalent with respect to fXa-dependent inhibition of fIIa/TF. The relative sequence positions of the reactive site residues determined for AcAP5 with the homologous regions in AcAP6 and AcAPc2 as well as the pattern of 10 cysteine residues present in each of the inhibitors suggest that the AcAPs are distantly related to the family of small protein serine protease inhibitors found in the nonhematophagous nematode Ascaris lumbricoides var. suum." citations,ref_22,4396,199533,3,,reference citation,,,9367762,,"Guntert P, Mumenthaler C, Wuthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J Mol Biol. 1997 Oct 17;273(1):283-98.",Torsion angle dynamics for NMR structure calculation with the new program DYANA.,published,journal,J. Mol. Biol.,Journal of molecular biology,273,1,,0022-2836,,,,,,,,,,,,,,,,,,,,283,298,1997,"The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from distance constraints and torsion angle constraints collected by nuclear magnetic resonance (NMR) experiments performs simulated annealing by molecular dynamics in torsion angle space and uses a fast recursive algorithm to integrate the equations of motions. Torsion angle dynamics can be more efficient than molecular dynamics in Cartesian coordinate space because of the reduced number of degrees of freedom and the concomitant absence of high-frequency bond and angle vibrations, which allows for the use of longer time-steps and/or higher temperatures in the structure calculation. It also represents a significant advance over the variable target function method in torsion angle space with the REDAC strategy used by the predecessor program DIANA. DYANA computation times per accepted conformer in the ""bundle"" used to represent the NMR structure compare favorably with those of other presently available structure calculation algorithms, and are of the order of 160 seconds for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300 computer. Test calculations starting from conformers with random torsion angle values further showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures." citations,ref_24,4396,199534,4,,reference citation,,,1579569,,"Morris AL, MacArthur MW, Hutchinson EG, Thornton JM. Stereochemical quality of protein structure coordinates. Proteins. 1992 Apr;12(4):345-64.",Stereochemical quality of protein structure coordinates.,published,journal,Proteins,Proteins,12,4,,0887-3585,,,,,,,,,,,,,,,,,,,,345,364,1992,"Methods have been developed to assess the stereochemical quality of any protein structure both globally and locally using various criteria. Several parameters can be derived from the coordinates of a given structure. Global parameters include the distribution of phi, psi and chi 1 torsion angles, and hydrogen bond energies. There are clear correlations between these parameters and resolution; as the resolution improves, the distribution of the parameters becomes more clustered. These features show a broad distribution about ideal values derived from high-resolution structures. Some structures have tightly clustered distributions even at relatively low resolutions, while others show abnormal scatter though the data go to high resolution. Additional indicators of local irregularity include proline phi angles, peptide bond planarities, disulfide bond lengths, and their chi 3 torsion angles. These stereochemical parameters have been used to generate measures of stereochemical quality which provide a simple guide as to the reliability of a structure, in addition to the most important measures, resolution and R-factor. The parameters used in this evaluation are not novel, and are easily calculated from structure coordinates. A program suite is currently being developed which will quickly check a given structure, highlighting unusual stereochemistry and possible errors." citations,entry_citation,4397,199557,1,,entry citation,,99129937,,,"Mizoue, L. S., Bazan, J. F., Johnson, E. C., and Handel, T. M., ""Solution Structure and Dynamics of the CX3C Chemokine Domain of Fractalkine and Its Interaction with an N-Terminal Fragment of CX3CR1,"" Biochemistry 38, 1402-1414 (1999).","Solution Structure and Dynamics of the CX3C Chemokine Domain of Fractalkine and Its Interaction with an N-Terminal Fragment of CX3CR1",published,journal,Biochemistry,Biochemistry,38,5,,,,,,,,,,,,,,,,,,,,,,1402,1414,1999, citations,entry_citation,4398,199570,1,,entry citation,,20029622,,,"Barnham, K. J., Catalfamo, F., Pallaghy, P. K., Howlett, G. J., and Norton, R. S., ""Helical Structure and Self-association in a 13-residue Neuropeptide Y Y2 Receptor Agonist:Relationship to Biological Activity,"" Biochim. Biophys. Acta 1435, 127-137 (1999).","Helical Structure and Self-association in a 13-residue Neuropeptide Y Y2 Receptor Agonist:Relationship to Biological Activity",published,journal,Biochim. Biophys. Acta,Biochimica et Biophysica Acta,1435,,,,,,,,,,,,,,,,,,,,,,,127,137,1999, citations,entry_citation,4399,199586,1,,entry citation,,99324017,,,"Gehrmann, J., Daly, N. L., Alewood, P. F., and Craik, D. J., ""Solution Structure of Alpha-Conotoxin ImI by 1H Nuclear Magnetic Resonance,"" J. Med. Chem. 42, 2364-2372 (1999).",Solution Structure of Alpha-Conotoxin ImI by 1H Nuclear Magnetic Resonance,published,journal,J. Med. Chem.,Journal of Medical Chemistry,42,13,,,,,,,,,,,,,,,,,,,,,,2364,2372,1999, citations,entry_citation,44,199601,1,,entry citation,,,,,"Rhyu, Gyung Ihm, Markley, John L., ""Two-Dimensional NMR Studies of Kazal Proteinase Inhibitors. 2. Sequence-Specific Assignments and Secondary Structure of Reactive Site Modified Turkey Ovomucoid Third Domain,"" Biochemistry 27, 2529-2539 (1988).","Two-Dimensional NMR Studies of Kazal Proteinase Inhibitors. 2. Sequence-Specific Assignments and Secondary Structure of Reactive Site Modified Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,27,,,,,,,,,,,,,,,,,,,,,,,2529,2539,1988, citations,entry_citation,440,199614,1,,entry citation,,,,,"Nettesheim, David G., Edalji, Rohinton P., Mollison, Karl W., Greer, Jonathan, Zuiderweg, Erik R. P., ""Secondary structure of complement component C3a anaphylatoxin in solution as determined by NMR spectroscopy: Differences between crystal and solution conformations,"" Proc. Natl. Acad. Sci. U.S.A. 85, 5036-5040 (1988).","Secondary structure of complement component C3a anaphylatoxin in solution as determined by NMR spectroscopy: Differences between crystal and solution conformations",published,journal,Proc. Natl. Acad. Sci. U.S.A.,,85,,,,,,,,,,,,,,,,,,,,,,,5036,5040,1988, citations,entry_citation,4400,199627,1,,entry citation,,99396740,,,"van Dongen, M. J.P., Doreleijers, J. F., van der Marel, G. A., van Boom, J. H., Hilbers, C. W., and Wijmenga, S. S., ""Structure and Mechanism of Formation of the H-y5 isomer of an intramolecular DNA triple helix,"" Nat. Struct. Biol. 6, 854-859 (1999).","Structure and Mechanism of Formation of the H-y5 isomer of an intramolecular DNA triple helix",published,journal,Nat. Struct. Biol.,Nature Structural Biology,6,9,,,,,,,,,,,,,,,,,,,,,,854,859,1999, citations,entry_citation,4401,199643,1,,entry citation,,98400947,,,"McKay, R. T., Pearlstone, J. R., Corson, D. C., Gagne, S. M., Smillie, L. B., and Sykes, B. D., ""Structure and Interaction Site of the Regulatory Domain of Troponin-C when Complexed with the 96-148 Region of Troponin-I,"" Biochemistry 37, 12419-12430 (1998).","Structure and Interaction Site of the Regulatory Domain of Troponin-C when Complexed with the 96-148 Region of Troponin-I",published,journal,Biochemistry,,37,36,,,,,,,,,,,,,,,,,,,,,,12419,12430,1998, citations,ref-48,4401,199644,2,,reference citation,,,8520220,,"Delaglio, F, Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., and Bax, A. (1995) J. Biomol. NMR 6, 277-293",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref-49,4401,199645,3,,reference citation,,,,,"Garrett, D.S., Powers, R., Gronenborn, A.M., and Clore, G.M. (1991) J. Magn. Reson. 95, 214-220",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4402,199675,1,,entry citation,,20087216,,,,NMR Solution Structure of the Human Prion Protein.,published,journal,Proc. Natl. Acad. Sci. U. S. A.,,97,,,,,,,,,,,,,,,,,,,,,,,145,150,2000, citations,ref_1,4402,199676,2,,reference citation,,,9280297,,"Recombinant full-length murine prion protein, mPrP(23-231): purification and spectroscopic characterization. FEBS Lett. 1997 Aug 18;413(2):277-81.","Recombinant full-length murine prion protein, mPrP(23-231): purification and spectroscopic characterization.",published,journal,FEBS Lett.,FEBS letters,413,2,,0014-5793,,,,,,,,,,,,,,,,,,,,277,281,1997,"The cellular prion protein of the mouse, mPrP(C), consists of 208 amino acids (residues 23-231). It contains a carboxy-terminal domain, mPrP(121-231), which represents an autonomous folding unit with three alpha-helices and a two-stranded antiparallel beta-sheet. We expressed the complete amino acid sequence of the prion protein, mPrP(23-231), in the cytoplasm of Escherichia coli. mPrP(23-231) was solubilized from inclusion bodies by 8 M urea, oxidatively refolded and purified to homogeneity by conventional chromatographic techniques. Comparison of near-UV circular dichroism, fluorescence and one-dimensional 1H-NMR spectra of mPrP(23-231) and mPrP(121-231) shows that the amino-terminal segment 23-120, which includes the five characteristic octapeptide repeats, does not contribute measurably to the manifestation of three-dimensional structure as detected by these techniques, indicating that the residues 121-231 might be the only polypeptide segment of PrP(C) with a defined three-dimensional structure." citations,ref_2,4402,199677,3,,reference citation,,,8700211,,"NMR structure of the mouse prion protein domain PrP(121-321). Nature. 1996 Jul 11;382(6587):180-2.",NMR structure of the mouse prion protein domain PrP(121-321).,published,journal,Nature,Nature,382,6587,,0028-0836,,,,,,,,,,,,,,,,,,,,180,182,1996,"The 'protein only' hypothesis states that a modified form of normal prion protein triggers infectious neurodegenerative diseases, such as bovine spongiform encephalopathy (BSE), or Creutzfeldt-Jakob disease (CJD) in humans. Prion proteins are thought to exist in two different conformations: the 'benign' PrPcform, and the infectious 'scrapie form', PrPsc. Knowledge of the three-dimensional structure of PrPc is essential for understanding the transition to PrPsc. The nuclear magnetic resonance (NMR) structure of the autonomously folding PrP domain comprising residues 121-231 (ref. 6) contains a two-stranded antiparallel beta-sheet and three alpha-helices. This domain contains most of the point-mutation sites that have been linked, in human PrP, to the occurrence of familial prion diseases. The NMR structure shows that these mutations occur within, or directly adjacent to, regular secondary structures. The presence of a beta-sheet in PrP(121-231) is in contrast with model predictions of an all-helical structure of PrPc (ref. 8), and may be important for the initiation of the transition from PrPc to PrPsc." citations,entry_citation,4403,199698,1,,entry citation,,,,,"Berjanskii, M. V., Riley, M. I., Xie, A., Semenchenko, V., Folk, W. R., and Van Doren, S. R., ""NMR Structure of the N-terminal J Domain of Murine Polyomavirus T Antigens: Implications for DnaJ-like Domains and for Mutations of T Antigens"", J. Biol. Chem. 275, 36094-36103 (2000).","NMR Structure of the N-terminal J Domain of Murine Polyomavirus T Antigens: Implications for DnaJ-like Domains and for Mutations of T Antigens",published,journal,J. Biol. Chem.,,275,,,,,,,,,,,,,,,,,,,,,,,36094,36103,2000, citations,entry_citation,4404,199723,1,,entry citation,,99329063,,,"Lu, S., Deng, P., Liu, X., Luo, J., Han, R., Gu, X., Liang, S., Wang, X., Li, F., Lozanov, V., Patthy, A., and Pongor, S., ""Solution Structure of the Major alpha-amylase Inhibitor of the crop plant Amaranth,"" J. Biol. Chem. 274, 20473-20478 (1999).","Solution Structure of the Major alpha-amylase Inhibitor of the crop plant Amaranth",published,journal,J. Biol. Chem.,Journal of Biological Chemistry,274,29,,,,,,,,,,,,,,,,,,,,,,20473,20478,1999, citations,ref_1,4404,199724,2,,reference citation,,99329063,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_2,4404,199725,3,,reference citation,,97419323,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_3,4404,199726,4,,reference citation,,94375474,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4405,199746,1,,entry citation,,99299390,,,,"HIGH PRECISION SOLUTION STRUCTURE OF THE C-TERMINAL KH DOMAIN OF HNRNP K, A C-MYC TRANSCRIPTION FACTOR",published,journal,J. Mol. Biol.,,289,,,,,,,,,,,,,,,,,,,,,,,949,962,1999, citations,entry_citation,4426,200228,1,,entry citation,,99230195,,,,"Solution Structure of Apo- and Holo-biotinyl Domain from Acetyl Coenzyme A Carboxylase of Escherichia coli Determined by Triple-Resonance NMR Spectroscopy",published,journal,Biochemistry,,38,,,,,,,,,,,,,,,,,,,,,,,5045,5053,1999, citations,entry_citation,4406,199759,1,,entry citation,,99400497,,,"Pallaghy, P. K., Melnikova, A. P., Jimenez, E. C., Olivera, B. M., and Norton, R. S., ""Solution structure of contryphan-R, a naturally occurring disulfide-bridged octapeptide containing D-tryptophan: comparison with protein loops,"" Biochemistry 38, 11553-11559 (1999).","Solution structure of contryphan-R, a naturally occurring disulfide-bridged octapeptide containing D-tryptophan: comparison with protein loops",published,journal,Biochemistry,,38,,,,,,,,,,,,,,,,,,,,,,,11553,11559,1999, citations,entry_citation,4407,199777,1,,entry citation,,99384138,,,"de Alba, E., De Vries, L., Farquhar, M., and Tjandra, N., ""Solution structure of human GAIP (G alpha interacting protein). A regulator of G protein signaling,"" J. Mol. Biol. 291, 927-939 (1999).","Solution structure of human GAIP (G alpha interacting protein). A regulator of G protein signaling",published,journal,J. Mol. Biol.,Journal of Molecular Biology,291,4,,,,,,,,,,,,,,,,,,,,,,927,939,1999, citations,ref_1,4407,199778,2,,reference citation,,,10452897,,"J. Mol. Biol. 1999. 291,927-939",Solution structure of human GAIP (Galpha interacting protein): a regulator of G protein signaling.,published,journal,J. Mol. Biol.,Journal of molecular biology,291,4,,0022-2836,,,,,,,,,,,,,,,,,,,,927,939,1999,"The solution structure of the human protein GAIP (Galpha interacting protein), a regulator of G protein signaling, has been determined by NMR techniques. Dipolar couplings of the oriented protein in two different liquid crystal media have been used in the structure calculation. The solution structure of GAIP is compared to the crystal structure of an homologous protein from rat (RGS4) complexed to the alpha-subunit of a G protein. Some of RGS4 residues involved in the Galpha-RGS binding interface have similar orientations in GAIP (free form), indicating that upon binding these residues do not suffer conformational rearrangements, and therefore, their role does not seem to be restricted to Galpha interaction but also to RGS folding and stability. We suggest that other structural differences between the two proteins may be related to the process of binding as well as to a distinct efficiency in their respective GTPase activating function." citations,entry_citation,4408,199799,1,,entry citation,,99400497,,,"Pallaghy, P. K., Melnikova, A. P., Jimenez, E. C., Olivera, B. M., and Norton, R. S., ""Solution structure of contryphan-R, a naturally occurring disulfide-bridged octapeptide containing D-tryptophan: comparison with protein loops,"" Biochemistry 38, 11553-11559 (1999).","Solution structure of contryphan-R, a naturally occurring disulfide-bridged octapeptide containing D-tryptophan: comparison with protein loops",published,journal,Biochemistry,,38,,,,,,,,,,,,,,,,,,,,,,,11553,11559,1999, citations,entry_citation,4409,199817,1,,entry citation,,,10758155,,,"The Dewar Photoproduct of the Thymidylyl(3' to 5')-thymidine (Dewar Product) Exhibits Mutagenic Behavior in Accordance with the ""A rule""",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,97,9,,,,,,,,,,,,,,,,,,,,,,4591,4596,2000, citations,entry_citation,441,199836,1,,entry citation,,,,,"Hyde, Eva I., Ramesh, Vasudevan, Roberts, G.C.K., Arrowsmith, Cheryl H., Treat-Clemons, Lynda, Klaic, Branimir, Jardetzky, Oleg, ""NMR studies of the Escherichia coli trp aporepressor Sequence-specific assignment of the aromatic proton residues,"" Eur. J. Biochem. 183, 545-553 (1989).","NMR studies of the Escherichia coli trp aporepressor Sequence-specific assignment of the aromatic proton residues",published,journal,Eur. J. Biochem.,,183,,,,,,,,,,,,,,,,,,,,,,,545,553,1989, citations,entry_citation,4410,199849,1,,entry citation,,99452410,,,"Lu, S., Liang, S., and Gu, X., ""Three dimensional structure of Selenocosmia huwena Lectin-I (SHL-I) from the venom of the spider Selenocosmia huwena by 2D-NMR,"" J. Protein Chem. 18, 609-617 (1999).","Three dimensional structure of Selenocosmia huwena Lectin-I (SHL-I) from the venom of the spider Selenocosmia huwena by 2D-NMR",published,journal,J. Protein Chem.,,18,,,,,,,,,,,,,,,,,,,,,,,609,617,1999, citations,ref_1,4410,199850,2,,reference citation,,,8588212,,"Liang SP, Pan X, ""A lectin-like peptide isolated from the venom of the Chinese bird spider Selenocosmia huwena,"" Toxicon. 1995 Jul;33(7):875-82.",A lectin-like peptide isolated from the venom of the Chinese bird spider Selenocosmia huwena.,published,journal,Toxicon,Toxicon : official journal of the International Society on Toxinology,33,7,,0041-0101,,,,,,,,,,,,,,,,,,,,875,882,1995,"A peptide with haemagglutination activity was isolated from the venom of the Chinese bird spider Selenocosmia huwena by means of ion-exchange and reverse-phase high-performance liquid chromatography. This peptide, named SHLP-I, agglutinates human and mice erythrocytes at a minimum concentration of 125 micrograms/ml and 31 micrograms/ml, respectively. It consists of 32 amino acid residues including 3 Trp and 6 Cys residues, the latter of which form three disulfide bounds. The complete amino acid sequence was determined. The N-terminal and C-terminal residues were Gly and Trp, respectively. SHLP-I shows homology with a fragment of great nettle lectin and with huwentoxin-I from the venom of the same spider." citations,entry_citation,4411,199871,1,,entry citation,,,,,,"Letter to the Editor: Sequence-specific 1H and 15N assignment and secondary structure of transforming growth factor beta3",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,16,2,,,,,,,,,,,,,,,,,,,,,,179,180,2000, citations,ref-1,4411,199872,2,,reference citation,,,,,"Bartels C., Xia T.-H., Billeter M., Guntert P., Wuthrich K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J. Biomol. NMR (1995) 6, 1-10.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4412,199891,1,,entry citation,,20200612,,,"Lee, J-H., Choi, Y-J., and Choi, B-S., ""Solution Structure of the DNA Decamer Duplex Containing a 3'-T.T base pair of the cis-syn Cyclobutane Pyrimidine Dimer: Implication for the Mutagenic Property of the cis-syn Dimer,"" Nuc. Acids Res. 28, 1794-1801 (2000).","Solution Structure of the DNA Decamer Duplex Containing a 3'-T.T base pair of the cis-syn Cyclobutane Pyrimidine Dimer: Implication for the Mutagenic Property of the cis-syn Dimer",published,journal,Nucleic Acids Res.,Nucleic Acids Research,28,8,,,,,,,,,,,,,,,,,,,,,,1794,1801,2000, citations,entry_citation,4413,199908,1,,entry citation,,99380160,,,,"Solution structure of a conserved C-terminal domain of p73 with structural homology to the SAM domain",published,journal,EMBO J.,,18,16,,,,,,,,,,,,,,,,,,,,,,4438,4445,1999, citations,entry_citation,4427,200244,1,,entry citation,,20074524,,,"Delepierre, M., Prochnicka-Chalufour, A., Boisbouvier, J., and Possani, L.D., ""Pi7, an Orphan Peptide from the Scorpion Pandinus imperator: A 1H-NMR Analysis Using a Nano-NMR Probe,"" Biochemistry 38, 16756-16765 (1999).","Pi7, an Orphan Peptide from the Scorpion Pandinus imperator: A 1H-NMR Analysis Using a Nano-NMR Probe",published,journal,Biochemistry,Biochemistry,38,,,,,,,,,,,,,,,,,,,,,,,16756,16765,1999, citations,entry_citation,4428,200259,1,,entry citation,,,10600386,,,"NMR structure of an F-actin-binding ""headpiece"" motif from villin",published,journal,J. Mol. Biol.,,294,,,,,,,,,,,,,,,,,,,,,,,1299,1310,1999, citations,entry_citation,4429,200287,1,,entry citation,,96184584,,,"Bocharov, E. V., Gudkov, A. T., and Arseniev, A. S., ""Topology of the secondary structure elements of ribosomal protein L7/L12 from E.coli in solution,"" FEBS Lett. 379, 291-294 (1996).","Topology of the secondary structure elements of ribosomal protein L7/L12 from E.coli in solutio",published,journal,FEBS Lett.,,379,,,,,,,,,,,,,,,,,,,,,,,291,294,1996, citations,ref-1,4413,199909,2,,reference citation,,,7844833,,"Nilges, M. (1995) J.Mol.Biol., 245, 645-660",Calculation of protein structures with ambiguous distance restraints. Automated assignment of ambiguous NOE crosspeaks and disulphide connectivities.,published,journal,J. Mol. Biol.,Journal of molecular biology,245,5,,0022-2836,,,,,,,,,,,,,,,,,,,,645,660,1995,"The distances derived from nuclear Overhauser effect (NOE) spectra are usually converted into three-dimensional structures by computer algorithms loosely termed distance geometry. To a varying degree, these methods require that the distance data is unambiguously assigned to pairs of atoms. Typically, however, there are many NOE crosspeaks that cannot be assigned without some knowledge of the structure. These crosspeaks have to be assigned in an iterative manner, using preliminary structures calculated from the unambiguous crosspeaks. In this paper, I present an alternative to this iterative approach. The ambiguity of an NOE crosspeak is correctly described in terms of the distances between all pairs of protons that may be involved. A simple restraining term is defined in terms of ""ambiguous"" distance restraints that can allow all possible assignments. A new minimization procedure based on simulated annealing is described that is capable of using highly ambiguous data for ab initio structure calculations. In particular, it is feasible to specify the restraint list directly in terms of the proton chemical shift assignment and the NOE peak table, without having assigned NOE crosspeaks to proton pairs. While the primary aim of this paper is determining the global fold of proteins from NMR data, similar strategies can be used for other types of ambiguous distance data. The application to one example, disulphide bridges with unknown connectivity, is described. Model NOE data were generated from the X-ray crystal structure of a small protein with known chemical shift assignments. Varying degrees of ambiguity in the data were assumed. The method obtained the correct polypeptide fold even when all distance restraints were ambiguous. Thus, the new approach may facilitate structure calculations with data derived from very overlapped spectra. It is also a step towards automating the calculation of structures from NMR data. This could prove especially valuable for data derived from three- and four-dimensional experiments. The approach may also prove useful for model building studies and tertiary structure prediction." citations,entry_citation,4414,199943,1,,entry citation,,99230189,,,"Babu, C. R., Volkman, B. F., and Bullerjahn, G. S., ""NMR Solution Structure of Plastocyanin from the Photosynthetic Prokaryote, Prochlorothrix hollandica,"" Biochemistry 38, 4988-4995 (1999).","NMR Solution Structure of Plastocyanin from the Photosynthetic Prokaryote, Prochlorothrix hollandica",published,journal,Biochemistry,,38,16,,,,,,,,,,,,,,,,,,,,,,4988,4995,1999, citations,entry_citation,4415,199962,1,,entry citation,,98428625,,,"McAteer, K., Jing, Y., Kao, J., Taylor, J. -., and Kennedy, M. A., ""Solution-state Structure of a DNA Dodecamer Duplex Containing a Cis-Syn Thymine Cyclobutane Dimer, the Major UV photoproduct of DNA,"" Journal of Molecular Biology 282, 1013-1032 (1998).","Solution-state Structure of a DNA Dodecamer Duplex Containing a Cis-Syn Thmine Cyclobutane Dimer, the Major UV photoproduct of DNA",published,journal,J. Mol. Biol.,Journal of Molecular Biology,282,,,,,,,,,,,,,,,,,,,,,,,1013,1032,1998, citations,entry_citation,4416,199983,1,,entry citation,,98428625,,,,"Solution-state Structure of a DNA Dodecamer Duplex Containing a Cis-Syn Thymine Cyclobutane Dimer, the Major UV photoproduct of DNA.",published,journal,J. Mol. Biol.,Journal of Molecular Biology,282,,,,,,,,,,,,,,,,,,,,,,,1013,1032,1998, citations,entry_citation,4417,200003,1,,entry citation,,,,,,"NMR Spectroscopy Reveals Common Structural Features of the Birch Pollen Allergen Bet v 1 and the Cherry Allergen Pru a 1",published,journal,Appl. Magn. Reson.,Applied Magnetic Resonance,17,,,,,,,,,,,,,,,,,,,,,,,449,646,1999, citations,citation_one,4417,200004,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4418,200031,1,,entry citation,,99359382,,,"Dementieva, D. V., Bocharov, E. V., and Arseniev, A. S., ""Two forms of cytotoxin II (cardiotoxin) from Naja naja oxiana in aqueous solution. Spatial structures with tightly bound water molecules.,"" Eur. J. Biochem. 263, 152-162 (1999).","Two forms of cytotoxin II (cardiotoxin) from Naja naja oxiana in aqueous solution. Spatial structures with tightly bound water molecules",published,journal,Eur. J. Biochem.,,263,,,,,,,,,,,,,,,,,,,,,,,152,162,1999, citations,ref-1,4418,200032,2,,reference citation,,,,,"Bartels C., Xia T.-H., Billeter M., Guntert P. & Wuthrich K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules, J. Biomol. NMR (1995) 6, 1-10.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref-2,4418,200033,3,,reference citation,,,9367762,,"Guntert P., Mumenthaler C. & Wuthrich K. Torsion angle dynamics for NMR structure calculation with new program DYANA, J. Mol. Biol. (1997) 273, 283-298.",Torsion angle dynamics for NMR structure calculation with the new program DYANA.,published,journal,J. Mol. Biol.,Journal of molecular biology,273,1,,0022-2836,,,,,,,,,,,,,,,,,,,,283,298,1997,"The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from distance constraints and torsion angle constraints collected by nuclear magnetic resonance (NMR) experiments performs simulated annealing by molecular dynamics in torsion angle space and uses a fast recursive algorithm to integrate the equations of motions. Torsion angle dynamics can be more efficient than molecular dynamics in Cartesian coordinate space because of the reduced number of degrees of freedom and the concomitant absence of high-frequency bond and angle vibrations, which allows for the use of longer time-steps and/or higher temperatures in the structure calculation. It also represents a significant advance over the variable target function method in torsion angle space with the REDAC strategy used by the predecessor program DIANA. DYANA computation times per accepted conformer in the ""bundle"" used to represent the NMR structure compare favorably with those of other presently available structure calculation algorithms, and are of the order of 160 seconds for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300 computer. Test calculations starting from conformers with random torsion angle values further showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures." citations,ref-3,4418,200034,4,,reference citation,,,,,"Schaumann T., Braun W. & Wuthrich K. (1990) The program FANTOM for energy refinement of polypeptides and proteins using a Newton-Raphson minimizer in torsion angle space, Biopolymers 29, 679-694.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_1,4429,200288,2,,reference citation,,,,,"Bartels C., Xia T.-H., Billeter M., Guntert P. & Wuthrich K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules, J. Biomol. NMR (1995) 6, 1-10.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4454,200904,1,,entry citation,,,,,,The Binding of Alpha-actinin to Titin: Implications for Z-disk Assembly,submitted,journal,Biochemistry,,,na,,,,,,,,,,,,,,,,,,,,,,,,, citations,reference_1,4454,200905,2,,reference citation,,92250531,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,reference_2,4454,200906,3,,reference citation,,97092327,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref-4,4418,200035,5,,reference citation,,,8744573,,"Koradi R., Billiter M. & Wutrich, K (1996) MOLMOL: a program for display and analysis of macromolecular structures, J. Mol. Graphics 14, 51-55.",MOLMOL: a program for display and analysis of macromolecular structures.,published,journal,,Journal of molecular graphics,14,1,,0263-7855,,,,,,,,,,,,,,,,,,,,51,32,1996,"MOLMOL is a molecular graphics program for display, analysis, and manipulation of three-dimensional structures of biological macromolecules, with special emphasis on nuclear magnetic resonance (NMR) solution structures of proteins and nucleic acids. MOLMOL has a graphical user interface with menus, dialog boxes, and on-line help. The display possibilities include conventional presentation, as well as novel schematic drawings, with the option of combining different presentations in one view of a molecule. Covalent molecular structures can be modified by addition or removal of individual atoms and bonds, and three-dimensional structures can be manipulated by interactive rotation about individual bonds. Special efforts were made to allow for appropriate display and analysis of the sets of typically 20-40 conformers that are conventionally used to represent the result of an NMR structure determination, using functions for superimposing sets of conformers, calculation of root mean square distance (RMSD) values, identification of hydrogen bonds, checking and displaying violations of NMR constraints, and identification and listing of short distances between pairs of hydrogen atoms." citations,entry_citation,4419,200057,1,,entry citation,,99359382,,,"Dementieva, D. V., Bocharov, E. V., and Arseniev, A. S., ""Two forms of cytotoxin II (cardiotoxin) from Naja naja oxiana in aqueous solution. Spatial structures with tightly bound water molecules.,"" Eur. J. Biochem. 263, 152-162 (1999).","Two forms of cytotoxin II (cardiotoxin) from Naja naja oxiana in aqueous solution. Spatial structures with tightly bound water molecules",published,journal,Eur. J. Biochem.,,263,,,,,,,,,,,,,,,,,,,,,,,152,162,1999, citations,ref-1,4419,200058,2,,reference citation,,,,,"Bartels C., Xia T.-H., Billeter M., Guntert P. & Wuthrich K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules, J. Biomol. NMR (1995) 6, 1-10.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref-2,4419,200059,3,,reference citation,,,9367762,,"Guntert P., Mumenthaler C. & Wuthrich K. Torsion angle dynamics for NMR structure calculation with new program DYANA, J. Mol. Biol. (1997) 273, 283-298.",Torsion angle dynamics for NMR structure calculation with the new program DYANA.,published,journal,J. Mol. Biol.,Journal of molecular biology,273,1,,0022-2836,,,,,,,,,,,,,,,,,,,,283,298,1997,"The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from distance constraints and torsion angle constraints collected by nuclear magnetic resonance (NMR) experiments performs simulated annealing by molecular dynamics in torsion angle space and uses a fast recursive algorithm to integrate the equations of motions. Torsion angle dynamics can be more efficient than molecular dynamics in Cartesian coordinate space because of the reduced number of degrees of freedom and the concomitant absence of high-frequency bond and angle vibrations, which allows for the use of longer time-steps and/or higher temperatures in the structure calculation. It also represents a significant advance over the variable target function method in torsion angle space with the REDAC strategy used by the predecessor program DIANA. DYANA computation times per accepted conformer in the ""bundle"" used to represent the NMR structure compare favorably with those of other presently available structure calculation algorithms, and are of the order of 160 seconds for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300 computer. Test calculations starting from conformers with random torsion angle values further showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures." citations,ref-3,4419,200060,4,,reference citation,,,,,"Schaumann T., Braun W. & Wuthrich K. (1990) The program FANTOM for energy refinement of polypeptides and proteins using a Newton-Raphson minimizer in torsion angle space, Biopolymers 29, 679-694.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref-4,4419,200061,5,,reference citation,,,8744573,,"Koradi R., Billiter M. & Wutrich, K (1996) MOLMOL: a program for display and analysis of macromolecular structures, J. Mol. Graphics 14, 51-55.",MOLMOL: a program for display and analysis of macromolecular structures.,published,journal,,Journal of molecular graphics,14,1,,0263-7855,,,,,,,,,,,,,,,,,,,,51,32,1996,"MOLMOL is a molecular graphics program for display, analysis, and manipulation of three-dimensional structures of biological macromolecules, with special emphasis on nuclear magnetic resonance (NMR) solution structures of proteins and nucleic acids. MOLMOL has a graphical user interface with menus, dialog boxes, and on-line help. The display possibilities include conventional presentation, as well as novel schematic drawings, with the option of combining different presentations in one view of a molecule. Covalent molecular structures can be modified by addition or removal of individual atoms and bonds, and three-dimensional structures can be manipulated by interactive rotation about individual bonds. Special efforts were made to allow for appropriate display and analysis of the sets of typically 20-40 conformers that are conventionally used to represent the result of an NMR structure determination, using functions for superimposing sets of conformers, calculation of root mean square distance (RMSD) values, identification of hydrogen bonds, checking and displaying violations of NMR constraints, and identification and listing of short distances between pairs of hydrogen atoms." citations,entry_citation,442,200083,1,,entry citation,,,,,"Hyde, Eva I., Ramesh, Vasudevan, Roberts, G.C.K., Arrowsmith, Cheryl H., Treat-Clemons, Lynda, Klaic, Branimir, Jardetzky, Oleg, ""NMR studies of the Escherichia coli trp aporepressor Sequence-specific assignment of the aromatic proton residues,"" Eur. J. Biochem. 183, 545-553 (1989).","NMR studies of the Escherichia coli trp aporepressor Sequence-specific assignment of the aromatic proton residues",published,journal,Eur. J. Biochem.,,183,,,,,,,,,,,,,,,,,,,,,,,545,553,1989, citations,entry_citation,4420,200096,1,,entry citation,,,,,,"NMR SOLUTION STRUCTURE OF ALPHA-CONOTOXIN IMI AND COMPARISON TO OTHER CONOTOXINS SPECIFIC FOR NEURONAL NICOTINIC ACETYLCHOLINE RECEPTOR",published,journal,Biochemistry,,38,13,,,,,,,,,,,,,,,,,,,,,,3874,3882,1999, citations,entry_citation,4421,200112,1,,entry citation,,,,,,"13C, 15N and 1H Assigned Chemical Shifts for PhoB DNA-binding Domain.",published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4422,200125,1,,entry citation,,20306980,,,"Cierpicki, T., Bania, J., and Otlewski, J., ""NMR Solution Structure of Apis mellifera Chymotrypsin/Cathepsin G Inhibitor-1 (AMCI-1): Structural Similarity with Ascaris Protease Inhibitors,"" Protein Sci. 9, 976-984 (2000).","NMR Solution Structure of Apis mellifera Chymotrypsin/Cathepsin G Inhibitor-1 (AMCI-1): Structural Similarity with Ascaris Protease Inhibitors.",published,journal,Protein Sci.,Protein Science,9,,,,,,,,,,,,,,,,,,,,,,,976,984,2000, citations,entry_citation,4455,200931,1,,entry citation,,99286218,,,,"Functional Glycan-free Adhesion Domain of Human Cell Surface Receptor CD58: Design, Production, and NMR Studies",published,journal,EMBO J.,EMBO Journal,18,,,,,,,,,,,,,,,,,,,,,,,2941,2949,1999, citations,ref_1,4422,200126,2,,reference citation,,,8520220,,"Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A, ""NMRPipe: a multidimensional spectral processing system based on UNIX pipes,"" J Biomol NMR 1995 Nov;6(3):277-93",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref_2,4422,200127,3,,reference citation,,,9367762,,"Guntert P, Mumenthaler C, Wuthrich K, ""Torsion angle dynamics for NMR structure calculation with the new program DYANA,"" J Mol Biol 1997 Oct 17;273(1):283-98",Torsion angle dynamics for NMR structure calculation with the new program DYANA.,published,journal,J. Mol. Biol.,Journal of molecular biology,273,1,,0022-2836,,,,,,,,,,,,,,,,,,,,283,298,1997,"The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from distance constraints and torsion angle constraints collected by nuclear magnetic resonance (NMR) experiments performs simulated annealing by molecular dynamics in torsion angle space and uses a fast recursive algorithm to integrate the equations of motions. Torsion angle dynamics can be more efficient than molecular dynamics in Cartesian coordinate space because of the reduced number of degrees of freedom and the concomitant absence of high-frequency bond and angle vibrations, which allows for the use of longer time-steps and/or higher temperatures in the structure calculation. It also represents a significant advance over the variable target function method in torsion angle space with the REDAC strategy used by the predecessor program DIANA. DYANA computation times per accepted conformer in the ""bundle"" used to represent the NMR structure compare favorably with those of other presently available structure calculation algorithms, and are of the order of 160 seconds for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300 computer. Test calculations starting from conformers with random torsion angle values further showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures." citations,entry_citation,4423,200146,1,,entry citation,,99229455,10212985,,"Kowalski, K., Czolij, R., King, G. F., Crossley, M., and Mackay, J. P., ""The Solution Structure of the N-terminal Zinc Finger of GATA-1 Reveals a Specific Binding Face for the Transcriptional Co-factor FOG,"" J. Biomol. NMR 13, 249-262 (1999).","The Solution Structure of the N-terminal Zinc Finger of GATA-1 Reveals a Specific Binding Face for the Transcriptional Co-factor FO",published,journal,J. Biomol. NMR,,13,,,,,,,,,,,,,,,,,,,,,,,249,262,1999, citations,entry_citation,4424,200177,1,,entry citation,,99380410,,,,"NMR Structure of the N-terminal Domain of Saccharomyces cerevisiae RNase HI Reveals a Fold with a Strong Resemblance to the N-terminal Domain of Ribosomal Protein L",published,journal,J. Mol. Biol.,,291,3,,,,,,,,,,,,,,,,,,,,,,661,669,1999, citations,ref_1,4424,200178,2,,reference citation,,,7489497,,,The non-RNase H domain of Saccharomyces cerevisiae RNase H1 binds double-stranded RNA: magnesium modulates the switch between double-stranded RNA binding and RNase H activity.,published,journal,RNA,"RNA (New York, N.Y.)",1,3,,1355-8382,,,,,,,,,,,,,,,,,,,,246,259,1995,"Eukaryotic ribonucleases H of known sequence are composed of an RNase H domain similar in size and sequence to that of Escherichia coli RNase HI and additional domains of unknown function. The RNase H1 of Saccharomyces cerevisiae has such an RNase H domain at its C-terminus. Here we show that the N-terminal non-RNase H portion of the yeast RNase H1 binds tightly to double-stranded RNA (dsRNA) and RNA-DNA hybrids even in the absence of the RNase H domain. Two copies of a sequence with limited similarity to the dsRNA-binding motif are present in this N-terminus. When the first of these sequences is altered, the protein no longer binds tightly to dsRNA and exhibits an increase in RNase H activity. Unlike other dsRNA-binding proteins, increasing the Mg2+ concentration from 0.5 mM to 5 mM inhibits binding of RNase H1 to dsRNA; yet a protein missing the RNase H domain binds strongly to dsRNA even at the higher Mg2+ concentration. These results suggest that binding to dsRNA and RNase H activity are mutually exclusive, and the Mg2+ concentration is critical for switching between the activities. Changes in the Mg2+ concentration or proteolytic severing of the dsRNA-binding domain could alter the activity or location of the RNase H and may govern access of the enzyme to the substrate. Sequences similar to the dsRNA-binding motif are present in other eukaryotic RNases H and the transactivating protein of cauliflower mosaic virus, suggesting that these proteins may also bind to dsRNA." citations,ref_2,4424,200179,3,,reference citation,,,1650910,,,"Selective cloning of genes encoding RNase H from Salmonella typhimurium, Saccharomyces cerevisiae and Escherichia coli rnh mutant.",published,journal,Mol. Gen. Genet.,Molecular & general genetics : MGG,227,3,,0026-8925,,,,,,,,,,,,,,,,,,,,438,445,1991,"We have cloned genes encoding RNase H from Escherichia coli rnh mutants, Salmonella typhimurium and Saccharomyces cerevisiae. Selection was accomplished by suppression of the temperature-sensitive growth phenotype of Escherichia coli strains containing the rnh-339::cat and either recB270 (Ts) or recC271 (Ts) mutations. RNases H from E. coli and S. typhimurium contained 155 amino acid residues and differed at only 11 positions. The S. cerevisiae and E. coli RNases H were about 30% homologous. A comparison of the amino acid sequences of several RNases H from cellular and retroviral sources revealed some strongly conserved regions as well as variable regions; the carboxyl-terminus was particularly variable. The overlapping, divergent promoter gene organization found in E. coli was observed to be present in S. typhimurium." citations,entry_citation,4425,200202,1,,entry citation,,99230195,,,,"SOLUTION STRUCTURES OF APO- AND HOLO-BIOTINYL DOMAINS FROM ACETYL COENZYME A CARBOXYLASE OF ESCHERICHIA COLI DETERMINED BY TRIPLE-RESONANCE NMR SPECTROSCOP",published,journal,Biochemistry,,38,,,,,,,,,,,,,,,,,,,,,,,5045,5053,1999, citations,reference_3,4463,201104,4,,reference citation,,,,,"Neidig, K.-P., Geyer, M., Gorler, A., Antz, C., Saffrich, R., Beneicke, W. and Kalbitzer, H. R. (1995) J. Biomol. NMR, 6, 255-270.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_2,4429,200289,3,,reference citation,,,9367762,,"Guntert P., Mumenthaler C. & Wuthrich K. Torsion angle dynamics for NMR structure calculation with new program DYANA, J. Mol. Biol. (1997) 273, 283-298.",Torsion angle dynamics for NMR structure calculation with the new program DYANA.,published,journal,J. Mol. Biol.,Journal of molecular biology,273,1,,0022-2836,,,,,,,,,,,,,,,,,,,,283,298,1997,"The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from distance constraints and torsion angle constraints collected by nuclear magnetic resonance (NMR) experiments performs simulated annealing by molecular dynamics in torsion angle space and uses a fast recursive algorithm to integrate the equations of motions. Torsion angle dynamics can be more efficient than molecular dynamics in Cartesian coordinate space because of the reduced number of degrees of freedom and the concomitant absence of high-frequency bond and angle vibrations, which allows for the use of longer time-steps and/or higher temperatures in the structure calculation. It also represents a significant advance over the variable target function method in torsion angle space with the REDAC strategy used by the predecessor program DIANA. DYANA computation times per accepted conformer in the ""bundle"" used to represent the NMR structure compare favorably with those of other presently available structure calculation algorithms, and are of the order of 160 seconds for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300 computer. Test calculations starting from conformers with random torsion angle values further showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures." citations,ref_3,4429,200290,4,,reference citation,,,,,"Schaumann T., Braun W. & Wuthrich K. (1990) The program FANTOM for energy refinement of polypeptides and proteins using a Newton-Raphson minimizer in torsion angle space, Biopolymers 29, 679-694.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_4,4429,200291,5,,reference citation,,,,,"Koradi R., Billiter M. & Wutrich, K (1996) MOLMOL: a program for display and analysis of macromolecular structures, J. Mol. Graphics 14, 51-55.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,443,200315,1,,entry citation,,,,,"Rico, Manuel, Bruix, Marta, Santoro, Jorge, Gonzalez, Carlos, Neira, Jose Luis, Nieto, Jose Luis, Herranz, Jose, ""Sequential 1H-NMR assignment and solution structure of bovine pancreatic ribonuclease A,"" Eur. J. Biochem. 183, 623-638 (1989).","Sequential 1H-NMR assignment and solution structure of bovine pancreatic ribonuclease A",published,journal,Eur. J. Biochem.,,183,,,,,,,,,,,,,,,,,,,,,,,623,638,1989, citations,entry_citation,4430,200328,1,,entry citation,,99229454,10212984,,,"High resolution solution structure of apo calcyclin and structural variations in the S100 family of calcium-binding proteins",published,journal,J. Biomol. NMR,,13,,,,,,,,,,,,,,,,,,,,,,,233,247,1999, citations,ref_1,4430,200329,2,,reference citation,,,7552751,,"Potts BC, Smith J, Akke M, Macke TJ, Okazaki K, Hidaka H, Case DA, Chazin WJ.""The structure of calcyclin reveals a novel homodimeric fold for S100 Ca(2+)-binding proteins,"" Nat Struct Biol. 1995 Sep;2(9):790-6",The structure of calcyclin reveals a novel homodimeric fold for S100 Ca(2+)-binding proteins.,published,journal,Nat. Struct. Biol.,Nature structural biology,2,9,,1072-8368,,,,,,,,,,,,,,,,,,,,790,796,1995,"The S100 calcium-binding proteins are implicated as effectors in calcium-mediated signal transduction pathways. The three-dimensional structure of the S100 protein calcyclin has been determined in solution in the apo state by NMR spectroscopy and a computational strategy that incorporates a systematic docking protocol. This structure reveals a symmetric homodimeric fold that is unique among calcium-binding proteins. Dimerization is mediated by hydrophobic contacts from several highly conserved residues, which suggests that the dimer fold identified for calcyclin will serve as a structural paradigm for the S100 subfamily of calcium-binding proteins." citations,ref_2,4430,200330,3,,reference citation,,,8931135,,"Potts BC, Carlstrom G, Okazaki K, Hidaka H, Chazin WJ. ""1H NMR assignments of apo calcyclin and comparative structural analysis with calbindin D9k and S100 beta,"" Protein Sci. 1996 Nov;5(11):2162-74.",1H NMR assignments of apo calcyclin and comparative structural analysis with calbindin D9k and S100 beta.,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,5,11,,0961-8368,,,,,,,,,,,,,,,,,,,,2162,2174,1996,"The homodimeric S100 protein calcyclin has been studied in the apo state by two-dimensional 1H NMR spectroscopy. Using a combination of scalar correlation and NOE experiments, sequence-specific 1H NMR assignments were obtained for all but one backbone and > 90% of the side-chain resonances. To our knowledge, the 2 x 90 residue (20 kDa) calcyclin dimer is the largest protein system for which such complete assignments have been made by purely homonuclear methods. Sequential and medium-range NOEs and slowly exchanging backbone amide protons identified directly the four helices and the short antiparallel beta-type interaction between the two binding loops that comprise each subunit of the dimer. Further analysis of NOEs enabled the unambiguous assignment of 556 intrasubunit distance constraints, 24 intrasubunit hydrogen bonding constraints, and 2 x 26 intersubunit distance constraints. The conformation of the monomer subunit was refined by distance geometry and restrained molecular dynamics calculations using the intrasubunit constraints only. Calculation of the dimer structure starting from this conformational ensemble has been reported elsewhere. The extent of structural homology among the apo calcyclin subunit, the monomer subunit of apo S100 beta, and monomeric apo calbindin D9k has been examined in detail by comparing 1H NMR chemical shifts and secondary structures. This analysis was extended to a comprehensive comparison of the three-dimensional structures of the calcyclin monomer subunit and calbindin D9k, which revealed greater similarity in the packing of their hydrophobic cores than was anticipated previously. Together, these results support the hypothesis that all members of the S100 family have similar core structures and similar modes of dimerization. Analysis of the amphiphilicity of Helix IV is used to explain why calbindin D9k is monomeric, but full-length S100 proteins form homodimers." citations,entry_citation,4431,200348,1,,entry citation,,99324156,,,"Walters, K. J., Gassner, G. T., Lippard, S. J., and Wagner, G., ""Structure of the soluble methane monooxygenase regulatory protein B,"" Proc Natl Acad Sci U S A. 1999 96(14):7877-82.",Structure of the soluble methane monooxygenase regulatory protein B,published,journal,Proc. Natl. Acad. Sci. U. S. A.,"Proceedings of the National Academy of Sciences, U.S.A.",96,,,,,,,,,,,,,,,,,,,,,,,7877,7882,1999, citations,entry_citation,4442,200612,1,,entry citation,,,,,,"Interactions in two Prototypical [2Fe-2S] Proteins: Selective (Chiral) Deuteration and Analysis of 1H and 2H NMR Signals from the Alpha and Beta Hydrogens of Cysteinyl Residues that Ligate the Iron in the Active Sites of Human Ferredoxin and Anabaena 712",in press,journal,Arch. Biochem. Biophys.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4443,200627,1,,entry citation,,,,,,NMR Solution Structure of Butantoxin,published,journal,Arch. Biochem. Biophys.,,379,1,,,,,,,,,,,,,,,,,,,,,,18,27,2000, citations,entry_citation,4444,200647,1,,entry citation,,,,,,"Letter to the Editor: Sequence-specific 1H, 13C and 15N resonance assignments and secondary structure of [2Fe-2S] ferredoxin from Halobacterium salinarum",published,journal,J. Biomol. NMR,,16,,,,,,,,,,,,,,,,,,,,,,,347,348,2000, citations,entry_citation,4445,200667,1,,entry citation,,20113483,,,,"The 3D structure of the HRDC domain and implications for the Werner and Bloom syndrome proteins.",published,journal,Structure,Structure,7,,,,,,,,,,,,,,,,,,,,,,,1557,1566,1999, citations,entry_citation,4464,201134,1,,entry citation,,20496763,,,,"Structures of the Contryphan Family of Cyclic Peptides. Role of Electrostatic Interactions in Cis-trans Isomerism",published,journal,Biochemistry,Biochemistry,39,,,,,,,,,,,,,,,,,,,,,,,12845,12852,2000, citations,entry_citation,4432,200376,1,,reference citation,,,8520220,,,NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,Ref_1,4432,200377,2,,reference citation,,,8520220,,"Grenningloh, G., V. Schmieden, P. R. Schofield, P. H. Seeburg, T. Siddique, T. K. Mohandas, C. M. Becker, and H. Betz. 1990. ""Alpha subunit variants of the human glycine receptor: primary structures, functional expression and chromosomal localization of the corresponding genes."" Embo J. 9:771-776.""",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,Ref_2,4432,200378,3,,reference citation,,,8520220,,"Delaglio, F., S. Grzesiek, G. W. Vuister, G. Zhu, J. Pfeifer, and A. Bax. 1995. ""NMRPipe: a multidimensional spectral processing system based on UNIX pipes."" J. Biomol. NMR. 6:277-293.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,entry_citation,4433,200398,1,,entry citation,,22074772,12080117,,,"NMR structures of the Second Transmembrane domain of the human glycine receptor alpha(1) subunit: Model of pore architecture and channel gating.",published,journal,Biophys. J.,,83,1,,,,,,,,,,,,,,,,,,,,,,252,262,2002, citations,Ref_1,4433,200399,2,,reference citation,,,2155780,,"Grenningloh, G., V. Schmieden, P. R. Schofield, P. H. Seeburg, T. Siddique, T. K. Mohandas, C. M. Becker, and H. Betz. 1990. ""Alpha subunit variants of the human glycine receptor: primary structures, functional expression and chromosomal localization of the corresponding genes."" Embo J. 9:771-776.""","Alpha subunit variants of the human glycine receptor: primary structures, functional expression and chromosomal localization of the corresponding genes.",published,journal,EMBO J.,The EMBO journal,9,3,,0261-4189,,,,,,,,,,,,,,,,,,,,771,776,1990,"Two cDNAs encoding variants (alpha 1 and alpha 2) of the strychnine binding subunit of the inhibitory glycine receptor (GlyR) were isolated from a human fetal brain cDNA library. The predicted amino acid sequences exhibit approximately 99% and approximately 76% identity to the previously characterized rat 48 kd polypeptide. Heterologous expression of the human alpha 1 and alpha 2 subunits in Xenopus oocytes resulted in the formation of glycine-gated strychnine-sensitive chloride channels, indicating that both polypeptides can form functional GlyRs. Using a panel of rodent-human hybrid cell lines, the gene encoding alpha 2 was mapped to the short arm (Xp21.2-p22.1) of the human X chromosome. In contrast, the alpha 1 subunit gene is autosomally located. These data indicate molecular heterogeneity of the human GlyR at the level of alpha subunit genes." citations,ref1,4445,200668,2,,reference citation,,,,10.1016/S0079-6565(97)00025-3,"Nilges, M. and O' Donoghue, S. (1998) Prog. NMR Spectroscopy 32, 107-139.",Ambiguous NOEs and automated NOE assignment,published,journal,Prog. NMR Spectroscopy,Progress in Nuclear Magnetic Resonance Spectroscopy,32,2,,,,,,,,,,,,,,,,,,,,,,107,139,1998, citations,entry_citation,4469,201246,1,,entry citation,,,,,,,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4492,201554,1,,entry citation,,99315881,10383444,,,"Three-dimensional structure of guanylyl cyclase activating protein-2, a calcium-sensitive modulator of photoreceptor guanylyl cyclases",published,journal,J. Biol. Chem.,,274,,,,,,,,,,,,,,,,,,,,,,,19329,19337,1999, citations,Ref_2,4433,200400,3,,reference citation,,,8520220,,"Delaglio, F., S. Grzesiek, G. W. Vuister, G. Zhu, J. Pfeifer, and A. Bax. 1995. ""NMRPipe: a multidimensional spectral processing system based on UNIX pipes."" J. Biomol. NMR. 6:277-293.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,entry_citation,4434,200420,1,,entry citation,,,,,,NMR Solution Structure of the Human Prion Protein,published,journal,Proc. Natl. Acad. Sci. U. S. A.,,97,,,,,,,,,,,,,,,,,,,,,,,145,150,2000, citations,entry_citation,4435,200445,1,,entry citation,,20221436,,,"Brennan, L., Turner, D.L., Messias A.C., Teodoro, M.L., LeGall, J., Santos, H., and Xavier, A.V., ""Structural Basis for the Network of Functional Cooperativities in Cytochrome c(3) from Desulfovibrio gigas: Solution Structures of the Oxidised and Reduced states,"" J. Mol. Biol. 298, 61-82 (2000).","Structural Basis for the Network of Functional Cooperativities in Cytochrome c(3) from Desulfovibrio gigas: Solution Structures of the Oxidised and Reduced states",published,journal,J. Mol. Biol.,Journal of Molecular Biology,298,1,,,,,,,,,,,,,,,,,,,,,,61,82,2000, citations,entry_citation,4436,200468,1,,entry citation,,20221436,,,"Brennan, L., Turner, D.L., Messias A.C., Teodoro, M.L., LeGall, J., Santos, H., and Xavier, A.V., ""Structural Basis for the Network of Functional Cooperativities in Cytochrome c(3) from Desulfovibrio gigas: Solution Structures of the Oxidised and Reduced states,"" J. Mol. Biol. 298, 61-82 (2000).","Structural Basis for the Network of Functional Cooperativities in Cytochrome c(3) from Desulfovibrio gigas: Solution Structures of the Oxidised and Reduced states",published,journal,J. Mol. Biol.,Journal of Molecular Biology,298,1,,,,,,,,,,,,,,,,,,,,,,61,82,2000, citations,entry_citation,4437,200491,1,,entry citation,,99272559,,,,"Solution structure of an EGF module pair from the Plasmodium falciparum merozoite surface protein 1",published,journal,J. Mol. Biol.,JOURNAL OF MOLECULAR BIOLOGY,289,,,,,,,,,,,,,,,,,,,,,,,113,122,1999, citations,entry_citation,4438,200527,1,,entry citation,,20090956,10623549,,,"NMR structure of the sterol carrier protein-2; implications for the biological role",published,journal,J. Mol. Biol.,Journal of Molecular Biology,295,,,,,,,,,,,,,,,,,,,,,,,595,603,2000, citations,ref1,4438,200528,2,,reference citation,,,,,"Guntert, P., Dotsch, V., Wider, G., Wuthrich, K., Processing of multi-dimensional NMR data with the new software, J. Biomol. NMR 2, 619-629",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref2,4438,200529,3,,reference citation,,,,,"Bartels, C., Xia, T.H., Billeter, M., Buntert, P., Wuthrich, K., The program XEASY for computer-supported NMR spectral-analysis of biological macromolecules, J. Biomol. NMR 6, 1-10",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref3,4438,200530,4,,reference citation,,,9367762,,"Guntert, P., Mumenthaler, C., Wuthrich, K., Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. (1997) 273(1):283-98.",Torsion angle dynamics for NMR structure calculation with the new program DYANA.,published,journal,J. Mol. Biol.,Journal of molecular biology,273,1,,0022-2836,,,,,,,,,,,,,,,,,,,,283,298,1997,"The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from distance constraints and torsion angle constraints collected by nuclear magnetic resonance (NMR) experiments performs simulated annealing by molecular dynamics in torsion angle space and uses a fast recursive algorithm to integrate the equations of motions. Torsion angle dynamics can be more efficient than molecular dynamics in Cartesian coordinate space because of the reduced number of degrees of freedom and the concomitant absence of high-frequency bond and angle vibrations, which allows for the use of longer time-steps and/or higher temperatures in the structure calculation. It also represents a significant advance over the variable target function method in torsion angle space with the REDAC strategy used by the predecessor program DIANA. DYANA computation times per accepted conformer in the ""bundle"" used to represent the NMR structure compare favorably with those of other presently available structure calculation algorithms, and are of the order of 160 seconds for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300 computer. Test calculations starting from conformers with random torsion angle values further showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures." citations,entry_citation,4439,200554,1,,entry citation,,,,,,"Electron-Nuclear Interactions in two Prototypical [2Fe-2S] Proteins: Selective (Chiral) Deuteration and Analysis of 1H and 2H NMR Signals from the Alpha and Beta Hydrogens of Cysteinyl Residues that Ligate the Iron in the Active Sites of Human Ferredoxin and Anabaena 7120 Vegetative Ferredoxin",in press,journal,Arch. Biochem. Biophys.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,444,200569,1,,entry citation,,,,,"van Duynhoven, John P.M., Folkers, P.J.M., Stassen, A.P.M., Harmsen, B.J.M., Konings, R.N.H., Hilbers, C. W., ""Structure of the DNA binding wing of the gene-V encoded single-stranded DNA binding protein of the filamentous bacteriophage M13,"" FEBS Lett. 261, 1-4 (1990).","Structure of the DNA binding wing of the gene-V encoded single-stranded DNA binding protein of the filamentous bacteriophage M13",published,journal,FEBS Lett.,,261,,,,,,,,,,,,,,,,,,,,,,,1,4,1990, citations,entry_citation,4440,200582,1,,entry citation,,,,,,"Electron-Nuclear Interactions in two Prototypical [2Fe-2S] Proteins: Selective (Chiral) Deuteration and Analysis of 1H and 2H NMR Signals from the Alpha and Beta Hydrogens of Cysteinyl Residues that Ligate the Iron in the Active Sites of Human Ferredoxin and Anabaena 7120 Vegetative Ferredoxin",in press,journal,Arch. Biochem. Biophys.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4441,200597,1,,entry citation,,,,,,"Interactions in two Prototypical [2Fe-2S] Proteins: Selective (Chiral) Deuteration and Analysis of 1H and 2H NMR Signals from the Alpha and Beta Hydrogens of Cysteinyl Residues that Ligate the Iron in the Active Sites of Human Ferredoxin and Anabaena 7120",in press,journal,Arch. Biochem. Biophys.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref2,4445,200669,3,,reference citation,,,9757107,,"A. T. Brunger, P. D. Adams, G. M. Clore, W. L. Delano, P. Gros, R. W. Grosse-Kunstleve, J.-S. Jiang, J. Kuszewski, M. Nilges, N. S. Pannu, R. J. Read, L. M. Rice, T. Simonson, G. L. Warren",Crystallography & NMR system: A new software suite for macromolecular structure determination.,published,journal,Acta Crystallogr. D Biol. Crystallogr.,"Acta crystallographica. Section D, Biological crystallography",54,Pt 5,,0907-4449,,,,,,,,,,,,,,,,,,,,905,921,1998,"A new software suite, called Crystallography & NMR System (CNS), has been developed for macromolecular structure determination by X-ray crystallography or solution nuclear magnetic resonance (NMR) spectroscopy. In contrast to existing structure-determination programs, the architecture of CNS is highly flexible, allowing for extension to other structure-determination methods, such as electron microscopy and solid-state NMR spectroscopy. CNS has a hierarchical structure: a high-level hypertext markup language (HTML) user interface, task-oriented user input files, module files, a symbolic structure-determination language (CNS language), and low-level source code. Each layer is accessible to the user. The novice user may just use the HTML interface, while the more advanced user may use any of the other layers. The source code will be distributed, thus source-code modification is possible. The CNS language is sufficiently powerful and flexible that many new algorithms can be easily implemented in the CNS language without changes to the source code. The CNS language allows the user to perform operations on data structures, such as structure factors, electron-density maps, and atomic properties. The power of the CNS language has been demonstrated by the implementation of a comprehensive set of crystallographic procedures for phasing, density modification and refinement. User-friendly task-oriented input files are available for nearly all aspects of macromolecular structure determination by X-ray crystallography and solution NMR." citations,ref3,4445,200670,4,,reference citation,,,10718612,,"Refinement of the protein backbone angle y in NMR structure calculations. R Sprangers, MJ Bottomley, JP Linge, J Schultz, M Nilges and M Sattler. Journal of Biomolecular NMR (2000) 16, 47-58.",Refinement of the protein backbone angle psi in NMR structure calculations,published,journal,J. Biomol. NMR,,16,1,,,,,,,,,,,,,,,,,,,,,,47,58,2000, citations,ref4,4445,200671,5,,reference citation,,,10905826,10.1023/A:1008365802830,"Linge, J.P. and Nilges, M. (1999) Journal of Biomolecular NMR, 13, 51-59.",Influence of non-bonded parameters on the quality of NMR structures: a new force field for NMR structure calculation,published,journal,J. Biomol. NMR,,13,1,,0925-2738,,,,,,,,,,,,,,,,,,,,51,59,1999, citations,ref5,4445,200672,6,,reference citation,,,11462826,10.1016/S0076-6879(01)39310-2,"Assigning Ambiguous NOEs with ARIA. JP Linge, S O'Donoghue and M Nilges. Methods in Enzymology (2001)",Automated assignment of ambiguous nuclear overhauser effects with ARIA,published,journal,Methods Enzymol.,,339,,,,,,,,,,,,,,,,,,,,,,,71,90,2001, citations,entry_citation,4446,200712,1,,entry citation,,,,,,"NMR solution structure of a novel thioredoxin from Bacillus acidocaldarius: possible determinants of protein stability.",submitted,journal,Eur. J. Biochem.,European journal of Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_1,4446,200713,2,,reference citation,,,9359865,,"Bartolucci et al. (1997)Biochem. J. 328, 277-285","Thioredoxin from Bacillus acidocaldarius: characterization, high-level expression in Escherichia coli and molecular modelling.",published,journal,Biochem. J.,The Biochemical journal,328 ( Pt 1),,,0264-6021,,,,,,,,,,,,,,,,,,,,277,285,1997,"The thioredoxin (Trx) from Bacillus acidocaldarius (BacTrx) was purified to homogeneity by anion-exchange chromatography and gel-filtration chromatography, based on its ability to catalyse the dithiothreitol-dependent reduction of bovine insulin disulphides. The protein has a molecular mass of 11577 Da, determined by electrospray mass spectrometry, a pI of 4.2, and its primary structure was obtained by automated Edman degradation after cleavage with trypsin and cyanogen bromide. The sequences of known bacterial Trxs were aligned at the active site: BacTrx has an identity ranging from 45 to 53% with all sequences except that of the unusual Anabaena strain 7120 Trx (37% identity). The gene coding for BacTrx was isolated by a strategy based on PCR gene amplification and cloned in a plasmid downstream of a lac-derived promoter sequence; the recombinant clone was used as the expression vector for Escherichia coli. The expression was optimized by varying both the time of cell growth and the time of exposure to the inducer isopropyl beta-d-thiogalactoside; expressed BacTrx represents approx. 5% of the total cytosolic protein. CD spectra and differential scanning calorimetry measurements demonstrated that BacTrx is endowed with a higher conformational heat stability than the Trx from E. coli. Nanogravimetry experiments showed a lower content of bound water in BacTrx than in E. coli Trx, and a transition temperature approx. 10 degrees C higher for BacTrx. The three-dimensional model of the oxidized form of BacTrx was constructed by a comparative molecular modelling technique, using E. coli Trx and Anabaena strain 7120 Trx as reference proteins. Increased networks of ion-pairs and shorter loops emerged as major features of the BacTrx structure compared with those of the template proteins. The findings are discussed in the light of the current knowledge about molecular determinants of protein stability." citations,entry_citation,4447,200737,1,,entry citation,,,,,,"Letter to the Editor: Backbone assignment of the 19kDa translationally controlled tumor-associated protein p23 fyp from Schizosaccharomyces pombe",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,16,1,,,,,,,,,,,,,,,,,,,,,,83,84,2000, citations,entry_citation,4448,200758,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N backbone assignment and secondary structure of the 19 kDa diadenosine 5', 5'''-P1, P4-tetraphosphate hydrolase from Lupinus angustifolius L",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,16,3,,,,,,,,,,,,,,,,,,,,,,269,270,2000, citations,entry_citation,4449,200789,1,,entry citation,,,,,,"Letter to the Editor: Assignments of 1H, 13C, and 15N resonances of intramolecular dimer antifreeze protein RD3",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,16,3,,,,,,,,,,,,,,,,,,,,,,273,274,2000, citations,ref_1,4449,200790,2,,reference citation,,,10423534,,"MEDLINE_UI_code 99353969 J Biochem (Tokyo) 1999 Aug;126(2):387-94 Determination of the solution structure of the N-domain plus linker of antarctic eel pout antifreeze protein RD3. Miura K, Ohgiya S, Hoshino T, Nemoto N, Odaira M, Nitta K, Tsuda S",Determination of the solution structure of the N-domain plus linker of Antarctic eel pout antifreeze protein RD3.,published,journal,J. Biochem.,Journal of biochemistry,126,2,,0021-924X,,,,,,,,,,,,,,,,,,,,387,394,1999,"RD3, a new antifreeze protein (AFP) extracted from antarctic eel pout is a single polypeptide divided into homologous N-terminal (residues Asn(1)-Glu(64)) and C-terminal (residues Ser(74)-Glu(134)) domains, each of which has a high sequence identity with Type III AFP. A 9-residue linker (-D(65)GTTSPGLK(73)-) connects these two domains in tandem and is thought to play a significant role in defining the nature of the intact molecule. The present paper shows for the first time the solution structure and preliminary (15)N-NMR backbone dynamics data of the N-domain plus the linker of recombinant RD3 protein (RD3-Nl: residues 1-73) by employing homo- and heteronuclear multidimensional NMR spectroscopy. Forty converged structures of RD3-Nl were successfully calculated by using a total of 958 NMR-derived structural restraints. It was found that the N-domain of RD3-Nl has a globular form comprising six beta-strands, three type III turns, and several loops, which stabilize a flat, ice-binding site formed on one side of this domain. Further, the linker portion appears to have a definitive structure, which is independent of the globular N-domain. This definitive linker is roughly divided into two short strands, -D(65)GTTSP(70)- and -G(71)LK(73)-, which are bent around -T(67)TSPG(71)- at an angle of approximately 60 degrees. This bending motif of the linker may function to orient the two ice-binding sites of the N- and C-domains of RD3 in the same direction, leading to their simultaneous interactions with the ice crystal surface." citations,entry_citation,4451,200816,1,,entry citation,,20229876,,,,"Structure of the CAD Domain of Caspase-activated DNase and Interaction with the CAD Domain of its Inhibitor",published,journal,J. Mol. Biol.,Journal of Molecular Biology,297,5,,,,,,,,,,,,,,,,,,,,,,1121,1128,2000, citations,entry_citation,4452,200841,1,,entry citation,,98206886,,,,"The Solution Structure of Type II Antifreeze Protein Reveals a New Member of the Lectin Family",published,journal,Biochemistry,Biochemistry,37,,,,,,,,,,,,,,,,,,,,,,,4712,4721,1998, citations,ref1,4452,200842,2,,reference citation,,,17810339,,"Brunger, A.T., Kuriyan, J. and Karplus, M. (1987) Science, 235, 458-460",Crystallographic R Factor Refinement by Molecular Dynamics.,published,journal,Science,"Science (New York, N.Y.)",235,4787,,1095-9203,,,,,,,,,,,,,,,,,,,,458,460,1987,"Molecular dynamics was used to refine macromolecular structures by incorporating the difference between the observed crystallographic structure factor amplitude and that calculated from an assumed atomic model into the total energy of the system. The method has a radius of convergence that is larger than that of conventional restrained least-squares refinement. Test cases showed that the need for manual corrections during refinement of macromolecular crystal structures is reduced. In crambin, the dynamics calculation moved residues that were misplaced by more than 3 angstroms into the correct positions without human intervention." citations,ref2,4452,200843,3,,reference citation,,,,,"Varian, palo Alto, CA",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_1,4455,200932,2,,reference citation,,,10357807,,"Sun ZY, Dotsch V, Kim M, Li J, Reinherz EL, Wagner G Functional glycan-free adhesion domain of human cell surface receptor CD58: design, production and NMR studies. EMBO J. 1999 Jun 1;18(11):2941-9.","Functional glycan-free adhesion domain of human cell surface receptor CD58: design, production and NMR studies.",published,journal,EMBO J.,The EMBO journal,18,11,,0261-4189,,,,,,,,,,,,,,,,,,,,2941,2949,1999,"A general strategy is presented here for producing glycan-free forms of glycoproteins without loss of function by employing apolar-to-polar mutations of surface residues in functionally irrelevant epitopes. The success of this structure-based approach was demonstrated through the expression in Escherichia coli of a soluble 11 kDa adhesion domain extracted from the heavily glycosylated 55 kDa human CD58 ectodomain. The solution structure was subsequently determined and binding to its counter-receptor CD2 studied by NMR. This mutant adhesion domain is functional as determined by several experimental methods, and the size of its binding site has been probed by chemical shift perturbations in NMR titration experiments. The new structural information supports a 'hand-shake' model of CD2-CD58 interaction involving the GFCC'C"" faces of both CD2 and CD58 adhesion domains. The region responsible for binding specificity is most likely localized on the C, C' and C"" strands and the C-C' and C'-C"" loops on CD58." citations,ref_2,4455,200933,3,,reference citation,,,,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).",,published,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4456,200952,1,,entry citation,,20283154,,,"Hwang, P.M., and Vogel, H.J., ""Structures of the Platelet Calcium- and Integrin-binding Protein and the alphaIIb-integrin Cytoplasmic Domain Suggest a Mechanism for Calcium-regulated Recognition; Homology Modeling and NMR Studies,"" J. Mol. Recognit. 13, 83-92 (2000).","Structures of the Platelet Calcium- and Integrin-binding Protein and the alphaIIb-integrin Cytoplasmic Domain Suggest a Mechanism for Calcium-regulated Recognition; Homology Modeling and NMR Studies",published,journal,J. Mol. Recognit.,Journal of Molecular Recognition,13,,,,,,,,,,,,,,,,,,,,,,,83,92,2000, citations,entry_citation,4457,200969,1,,entry citation,,,,,,"Letter to the Editor: Sequence-specific resonance assignments and partial unfolding of extracellular domains II and III of E-cadherin",published,journal,J. Biomol. NMR,,16,,,,,,,,,,,,,,,,,,,,,,,181,182,2000, citations,entry_citation,4458,200994,1,,entry citation,,,15017142,,,Solution structures of reduced and oxidized bacteriophage T4 glutaredoxin.,published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,29,1,,,,,,,,,,,,,,,,,,,,,,85,90,2004, citations,entry_citation,4459,201009,1,,entry citation,,,15017142,,,Solution structures of reduced and oxidized bacteriophage T4 glutaredoxin.,published,journal,J. Biomol. NMR,,29,1,,,,,,,,,,,,,,,,,,,,,,85,90,2004, citations,entry_citation,4460,201024,1,,entry citation,,20377251,,,,"1H, 15N and 13C Resonance Assignments for the C-terminal Protein Interaction Region of the 32 kDa Subunit of Human Replication Protein A",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,17,2,,,,,,,,,,,,,,,,,,,,,,179,180,2000, citations,citation_1,4460,201025,2,,reference citation,,,2406247,,"Erdile, L.F., Wold, M.S., and Kelly, T.J. ""The primary structure of the 32-kDA subunit of human replication protein A"". J. Biol. Chem. (1990) 265:3177-3182.",The primary structure of the 32-kDa subunit of human replication protein A.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,265,6,,0021-9258,,,,,,,,,,,,,,,,,,,,3177,3182,1990,"Replication protein A (RP-A) is a complex of three polypeptides of molecular mass 70, 32, and 14 kDa, which is absolutely required for simian virus 40 DNA replication in vitro. We have isolated a cDNA coding for the 32-kDa subunit of RP-A. An oligonucleotide probe was constructed based upon a tryptic peptide sequence derived from whole RP-A, and clones were isolated from a lambda gt11 library containing HeLa cDNA inserts. The amino acid sequence predicted from the cDNA contains the peptide sequence obtained from whole RP-A along with two sequences obtained from tryptic peptides derived from sodium dodecyl sulfate-polyacrylamide gel-purified 32-kDa subunit. The coding sequence predicts a protein of 29,228 daltons, in good agreement with the electrophoretically determined molecular mass of the 32-kDa subunit. No significant homology was found with any of the sequences in the GenBank data base. The protein predicted from the cDNA has an N-terminal region rich in glycine and serine along with two acidic and two basic segments. Monoclonal antibodies have been raised against the 70- and 32-kDa subunits of RP-A. The cloned cDNA has been overexpressed in bacteria using an inducible T7 expression system. The protein made in bacteria is recognized by a monoclonal antibody that is specific for the 32-kDa subunit of RP-A. This monoclonal antibody against the 32-kDa subunit inhibits DNA replication in vitro." citations,entry_citation,4461,201063,1,,entry citation,,20069951,10600388,,,"Plant Cyclotides - a unique family of cyclic and knotted proteins that defines the cyclic cystine knot structural moti",published,journal,J. Mol. Biol.,,294,,,,,,,,,,,,,,,,,,,,,,,1327,1336,1999, citations,entry_citation,4462,201079,1,,entry citation,,20095839,10631978,,,"Three-dimensional solution structure of mouse [Cd7]-metallothionein-1 by homonuclear and heteronuclear NMR spectroscopy",published,journal,Protein Sci.,Protein Science,8,12,,,,,,,,,,,,,,,,,,,,,,2630,2638,1999, citations,entry_citation,4463,201101,1,,entry citation,,20285167,,,"Huber, F., Gronwald, W., Wohlgemuth, S., Herrmann, C., Geyer, M., Wittinghofer, A., and Kalbitzer, H.R., ""Letter to the Editor: Sequential NMR Assignment of the RAS-binding Domain of Byr2,"" J. Biomol. NMR 16, 355-356 (2000).","Letter to the Editor: Sequential NMR Assignment of the RAS-binding Domain of Byr2",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,16,4,,,,,,,,,,,,,,,,,,,,,,355,356,2000, citations,reference_1,4463,201102,2,,reference citation,,,2046669,,"Mol Cell Biol 1991 Jul;11(7):3554-63 byr2, a Schizosaccharomyces pombe gene encoding a protein kinase capable of partial suppression of the ras1 mutant phenotype. Wang Y, Xu HP, Riggs M, Rodgers L, Wigler M","byr2, a Schizosaccharomyces pombe gene encoding a protein kinase capable of partial suppression of the ras1 mutant phenotype.",published,journal,Mol. Cell. Biol.,Molecular and cellular biology,11,7,,0270-7306,,,,,,,,,,,,,,,,,,,,3554,3563,1991,"Schizosaccharomyces pombe contains a single gene, ras1, which is a homolog of the mammalian RAS genes. ras1 is required for conjugation, sporulation, and normal cell shape. ras1 has been previously identified as ste5. We report here a gene we call byr2 that can encode a predicted protein kinase and can partially suppress defects in ras1 mutants. ras1 mutant strains expressing high levels of byr2 can sporulate competently but are still defective in conjugation and abnormally round. byr2 mutants are viable and have normal shape but are absolutely defective in conjugation and sporulation. byr2 is probably identical to ste8. In many respects, byr2 resembles the byr1 gene, another suppressor of the ras1 mutation, which has been identified previously as ste1. Our data indicate that if ras1, byr2, and byr1 act along the same pathway, then the site of action for byr2 is between the sites for ras1 and byr1." citations,reference_2,4463,201103,3,,reference citation,,,,,"Bruker, Karlsruhe, Germany",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4465,201149,1,,entry citation,,,10835281,,"Jeuken, L.J., Ubbink, M., Bitter, J.H., van Vliet, P., Meyer-Klaucke, W., and Canters, G.W., ""The Structural role of the Copper-coordinating and Surface-exposed Histidine Residue in the Blue Copper Protein Azurin,"" J. Mol. Biol. 299, 737-755 (2000).","The Structural role of the Copper-coordinating and Surface-exposed Histidine Residue in the Blue Copper Protein Azurin",published,journal,J. Mol. Biol.,Journal of Molecular Biology,299,3,,,,,,,,,,,,,,,,,,,,,,737,755,2000,"Copper K-edge EXAFS spectroscopy and 15N NMR relaxation studies were performed on samples of a variant azurin in which the surface exposed histidine ligand of the copper (His117) had been replaced by a glycine" citations,Ref._1,4465,201150,2,,reference citation,,,,,"provided by Wayne Boucher and the Department of Biochemistry, University of Cambridge. The code may be obtained via anonymous ftp to www.bio.cam.ac.uk in the directory ~ftp/pub/azara",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,Ref._2,4465,201151,3,,reference citation,,,,,"Kraulis, P. J. (1989). ANSIG: A program for the assignment of protein 1H 2D NMR spectra by interactive graphics. J. Magn. Reson. 84, 627-633.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4466,201174,1,,entry citation,,,,,,"The Structure and Dynamics in Solution of Cu(I) Pseudoazurin from Paracoccus pantotrophus.",published,journal,Protein Sci.,Protein Science,9,,,,,,,,,,,,,,,,,,,,,,,846,858,2000, citations,live_cs_ref,4466,201175,2,,reference citation,,,,,"Protein NMR Spectroscopy, (Principles and Paractice) Cavanagh J., Fairbrother W. J., Palmer III A. G., & Skelton N. J. 1st Edn. Academic Press, 1996. page 175-176.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4467,201193,1,,entry citation,,20377249,,,,"Sequence-specific 1H, 13C, and 15N Assignments of the MAR-binding Domain of Chicken MeCP2/ARBP",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,17,2,,,,,,,,,,,,,,,,,,,,,,175,176,2000, citations,ref_1,4467,201194,2,,reference citation,,,10508514,,"Amir, R.E., Van den Veyver, I.B., Wan, M., Tran, C.Q., Francke, U. and Zoghbi, H.Y. (1999) Nature Genet. 23, 185-188.","Rett syndrome is caused by mutations in X-linked MECP2, encoding methyl-CpG-binding protein 2.",published,journal,Nat. Genet.,Nature genetics,23,2,,1061-4036,,,,,,,,,,,,,,,,,,,,185,188,1999,"Rett syndrome (RTT, MIM 312750) is a progressive neurodevelopmental disorder and one of the most common causes of mental retardation in females, with an incidence of 1 in 10,000-15,000 (ref. 2). Patients with classic RTT appear to develop normally until 6-18 months of age, then gradually lose speech and purposeful hand use, and develop microcephaly, seizures, autism, ataxia, intermittent hyperventilation and stereotypic hand movements. After initial regression, the condition stabilizes and patients usually survive into adulthood. As RTT occurs almost exclusively in females, it has been proposed that RTT is caused by an X-linked dominant mutation with lethality in hemizygous males. Previous exclusion mapping studies using RTT families mapped the locus to Xq28 (refs 6,9,10,11). Using a systematic gene screening approach, we have identified mutations in the gene (MECP2 ) encoding X-linked methyl-CpG-binding protein 2 (MeCP2) as the cause of some cases of RTT. MeCP2 selectively binds CpG dinucleotides in the mammalian genome and mediates transcriptional repression through interaction with histone deacetylase and the corepressor SIN3A (refs 12,13). In 5 of 21 sporadic patients, we found 3 de novo missense mutations in the region encoding the highly conserved methyl-binding domain (MBD) as well as a de novo frameshift and a de novo nonsense mutation, both of which disrupt the transcription repression domain (TRD). In two affected half-sisters of a RTT family, we found segregation of an additional missense mutation not detected in their obligate carrier mother. This suggests that the mother is a germline mosaic for this mutation. Our study reports the first disease-causing mutations in RTT and points to abnormal epigenetic regulation as the mechanism underlying the pathogenesis of RTT." citations,ref_2,4467,201195,3,,reference citation,,,9620779,,"Jones, P.L., Veenstra, G.J.C., Wade, P.A., Vermaak, D., Kass, S.U., Landsberger, N., Strouboulis, J. and Wolffe, A.P. (1998) Nature Genet. 19, 187-191.",Methylated DNA and MeCP2 recruit histone deacetylase to repress transcription.,published,journal,Nat. Genet.,Nature genetics,19,2,,1061-4036,,,,,,,,,,,,,,,,,,,,187,191,1998,"CpG methylation in vertebrates correlates with alterations in chromatin structure and gene silencing. Differences in DNA-methylation status are associated with imprinting phenomena and carcinogenesis. In Xenopus laevis oocytes, DNA methylation dominantly silences transcription through the assembly of a repressive nucleosomal array. Methylated DNA assembled into chromatin binds the transcriptional repressor MeCP2 which cofractionates with Sin3 and histone deacetylase. Silencing conferred by MeCP2 and methylated DNA can be relieved by inhibition of histone deacetylase, facilitating the remodelling of chromatin and transcriptional activation. These results establish a direct causal relationship between DNA methylation-dependent transcriptional silencing and the modification of chromatin." citations,ref_3,4467,201196,4,,reference citation,,,1606614,,"Lewis, J.D., Meehan, R.R., Henzel, W.J., Maurer-Fogy, I., Jeppesen, P., Klein, F. and Bird, A. (1992) Cell 69, 905-914.","Purification, sequence, and cellular localization of a novel chromosomal protein that binds to methylated DNA.",published,journal,Cell,Cell,69,6,,0092-8674,,,,,,,,,,,,,,,,,,,,905,914,1992,"Methylation of mammalian DNA can lead to repression of transcription and alteration of chromatin structure. Recent evidence suggests that both effects are the result of an interaction between the methylated sites and methyl-CpG-binding proteins (MeCPs). MeCP1 has previously been detected in crude nuclear extracts. Here we report the identification, purification, and cDNA cloning of a novel MeCP called MeCP2. Unlike MeCP1, the new protein is able to bind to DNA that contains a single methyl-CpG pair. By staining with an antibody, we show that the distribution of MeCP2 along the chromosomes parallels that of methyl-CpG. In mouse, for example, MeCP2 is concentrated in pericentromeric heterochromatin, which contains a large fraction (about 40%) of all genomic 5-methylcytosine." citations,ref_4,4467,201197,5,,reference citation,,,,,"Markley, J.L., Bax, A., Arata, Y., Hilbers, C.W., Kaptein, R., Sykes, B.D., Wright, P.E. and W?thrich, K. (1998) Pure & Appl. Chem. 70, 117-142.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_5,4467,201198,6,,reference citation,,,8177735,,"Nan, X., Meehan, R.R. and Bird, A. (1993) Nucleic Acids Res. 21, 4886-4892.",Dissection of the methyl-CpG binding domain from the chromosomal protein MeCP2.,published,journal,Nucleic Acids Res.,Nucleic acids research,21,21,,0305-1048,,,,,,,,,,,,,,,,,,,,4886,4892,1993,"MeCP2 is a chromosomal protein which binds to DNA that is methylated at CpG. In situ immunofluorescence in mouse cells has shown that the protein is most concentrated in pericentromeric heterochromatin, suggesting that MeCP2 may play a role in the formation of inert chromatin. Here we have isolated a minimal methyl-CpG binding domain (MBD) from MeCP2. MBD is 85 amino acids in length, and binds exclusively to DNA that contains one or more symmetrically methylated CpGs. MBD has negligable non-specific affinity for DNA, confirming that non-specific and methyl-CpG specific binding domains of MeCP2 are distinct. In vitro footprinting indicates that MBD binding can protect a 12 nucleotide region surrounding a methyl-CpG pair, with an approximate dissociation constant of 10(-9) M." citations,ref_6,4467,201199,7,,reference citation,,,9038338,,"Nan, X., Campoy, F.J. and Bird, A. (1997) Cell 88, 471-481.",MeCP2 is a transcriptional repressor with abundant binding sites in genomic chromatin.,published,journal,Cell,Cell,88,4,,0092-8674,,,,,,,,,,,,,,,,,,,,471,481,1997,"MeCP2 is an abundant mammalian protein that binds to methylated CpG. We have found that native and recombinant MeCP2 repress transcription in vitro from methylated promoters but do not repress nonmethylated promoters. Repression is nonlinearly dependent on the local density of methylation, becoming significant at the density found in bulk vertebrate genomic DNA. Transient transfection using fusions with the GAL4 DNA binding domain identified a region of MeCP2 that is capable of long-range repression in vivo. Moreover, MeCP2 is able to displace histone H1 from preassembled chromatin that contains methyl-CpG. These properties, together with the abundance of MeCP2 and the high frequency of its 2 bp binding site, suggest a role as a global transcriptional repressor in vertebrate genomes." citations,entry_citation,447,201260,1,,entry citation,,,,,"Oh, Byung-Ha, Markley, John L., ""Multinuclear Magnetic Resonance Studies of the 2Fe-2S, Ferredoxin from Anabaena Species Strain PCC 7120. 1. Sequence-Specific Hydrogen-1 Resonance Assignments and Secondary Structure in Solution of the Oxidized Form,"" Biochemistry 29, 3993-4004 (1990).","Multinuclear Magnetic Resonance Studies of the 2Fe-2S, Ferredoxin from Anabaena Species Strain PCC 7120. 1. Sequence-Specific Hydrogen-1 Resonance Assignments and Secondary Structure in Solution of the Oxidized Form",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,3993,4004,1990, citations,ref_7,4467,201200,8,,reference citation,,,9620804,,"Nan, X., Ng, H.-H., Johnson, C.A., Laherty, C.D., Turner, B.M., Eisenmann, R.N. and Bird, A. (1998) Nature 393, 386-389.",Transcriptional repression by the methyl-CpG-binding protein MeCP2 involves a histone deacetylase complex.,published,journal,Nature,Nature,393,6683,,0028-0836,,,,,,,,,,,,,,,,,,,,386,389,1998,"Cytosine residues in the sequence 5'CpG (cytosine-guanine) are often postsynthetically methylated in animal genomes. CpG methylation is involved in long-term silencing of certain genes during mammalian development and in repression of viral genomes. The methyl-CpG-binding proteins MeCP1 and MeCP2 interact specifically with methylated DNA and mediate transcriptional repression. Here we study the mechanism of repression by MeCP2, an abundant nuclear protein that is essential for mouse embryogenesis. MeCP2 binds tightly to chromosomes in a methylation-dependent manner. It contains a transcriptional-repression domain (TRD) that can function at a distance in vitro and in vivo. We show that a region of MeCP2 that localizes with the TRD associates with a corepressor complex containing the transcriptional repressor mSin3A and histone deacetylases. Transcriptional repression in vivo is relieved by the deacetylase inhibitor trichostatin A, indicating that deacetylation of histones (and/or of other proteins) is an essential component of this repression mechanism. The data suggest that two global mechanisms of gene regulation, DNA methylation and histone deacetylation, can be linked by MeCP2." citations,ref_8,4467,201201,9,,reference citation,,,1846084,,"von Kries, J.P., Buhrmester, H. and Str?tling, W.H. (1991) Cell 64, 123-135.","A matrix/scaffold attachment region binding protein: identification, purification, and mode of binding.",published,journal,Cell,Cell,64,1,,0092-8674,,,,,,,,,,,,,,,,,,,,123,135,1991,"Matrix/scaffold attachment regions (MARs/SARs) partition chromatin into functional loop domains. Here we have identified a chicken protein that selectively binds to MARs from the chicken lysozyme locus and to MARs from Drosophila, mouse, and human genes. This protein, named ARBP (for attachment region binding protein), was purified to homogeneity and shown to bind to MARs in a cooperative fashion. ARBP is an abundant nuclear protein and a component of the internal nuclear network. Deletion mutants indicate that multiple AT-rich sequences, if contained in a minimal approximately 350 bp MAR fragment, can lead to efficient binding of ARBP. Furthermore, dimerization mutants show that, to bind ARBP efficiently, MAR sequences can act synergistically over large distances, apparently with the intervening DNA looping out. The binding characteristics of ARBP to MARs reproduce those of unfractionated matrix preparations, suggesting that ARBP is an important nuclear element for the generation of functional chromatin loops." citations,ref_9,4467,201202,10,,reference citation,,,10518942,,"Wakefield, R.I.D., Smith, B.O., Nan, X., Free, A., Soteriou, A., Uhrin, D., Bird, A.P. and Barlow, P.N. (1999) J. Mol. Biol. 291, 1055-1065.",The solution structure of the domain from MeCP2 that binds to methylated DNA.,published,journal,J. Mol. Biol.,Journal of molecular biology,291,5,,0022-2836,,,,,,,,,,,,,,,,,,,,1055,1065,1999,"MeCP2 is an abundant mammalian protein that binds methylated CpG (mCpG) sequences within double-stranded DNA, represses transcription by recruiting histone deacetylases, and is essential for embryonic development. It is one of a family of proteins which mediate the biological consequences of DNA methylation. These proteins each possess a sequence motif of about 70 residues which, in MeCP2, form a domain necessary and sufficient for binding to mCpG. The solution structure of the mCpG-binding domain (MBD) from MeCP2 has been solved and the DNA-binding surface of the domain mapped using NMR spectroscopy. Residues 95-162 of MeCP2 adopt a novel fold forming a wedge-shaped structure. An N-terminal four-stranded antiparallel beta-sheet forms one face of the wedge, while the other face is formed mainly by a C-terminal helical region. The thin end of the wedge is extended by a long loop between beta-strands B and C containing many basic residues. The B-C loop together with residues in strands B, C and D, and at the N terminus of the alpha-helix, appears to form an interface with methylated DNA. Unstructured residues at the NH2 terminus of the domain are also involved in formation of the complex. The presence of numerous arginine and lysine side-chains on the DNA-binding surface of MBD is consistent with the requirement for the mCpG site to be flanked by non-specific sequences of base-pairs. The absence of symmetry in the domain implies that recognition does not exploit the symmetry of the binding site. A conserved hydrophobic pocket containing the side-chains of Tyr123 and Ile125 on the positively charged beta-sheet face is a candidate for the region of contact with the methyl-groups of the modified cytosine residues." citations,ref_10,4467,201203,11,,reference citation,,,9271441,,"Weitzel, J.M., Buhrmester, H. and Str?tling, W.H. (1997) Mol. Cell. Biol. 17, 5656-5666.",Chicken MAR-binding protein ARBP is homologous to rat methyl-CpG-binding protein MeCP2.,published,journal,Mol. Cell. Biol.,Molecular and cellular biology,17,9,,0270-7306,,,,,,,,,,,,,,,,,,,,5656,5666,1997,"Here, we describe the cloning and further characterization of chicken ARBP, an abundant nuclear protein with a high affinity for MAR/SARs. Surprisingly, ARBP was found to be homologous to the rat protein MeCP2, previously identified as a methyl-CpG-binding protein. A region spanning 125 amino acids in the N-terminal halves is 96.8% identical between chicken ARBP and rat MeCP2. A deletion mutation analysis using Southwestern and band shift assays identified this highly conserved region as the MAR DNA binding domain. Alignment of chicken ARBP with rat and human MeCP2 proteins revealed six trinucleotide amplifications generating up to 34-fold repetitions of a single amino acid. Because MeCP2 was previously localized to pericentromeric heterochromatin in mouse chromosomes, we analyzed the in vitro binding of ARBP to various repetitive sequences. In band shift experiments, ARBP binds to two chicken repetitive sequences as well as to mouse satellite DNA with high affinity similar to that of its binding to chicken lysozyme MAR fragments. In mouse satellite DNA, use of several footprinting techniques characterized two high-affinity binding sites, whose sequences are related to the ARBP binding site consensus in the chicken lysozyme MAR (5'-GGTGT-3'). Band shift experiments indicated that methylation increased in vitro binding of ARBP to mouse satellite DNA two- to fivefold. Our results suggest that ARBP/MeCP2 is a multifunctional protein with roles in loop domain organization of chromatin, the structure of pericentromeric heterochromatin, and DNA methylation." citations,ref_11,4467,201204,12,,reference citation,,,8019132,,"Wishart, D.S. and Sykes B.D. (1994) J. Biomol. NMR 4, 171-180.",The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,4,2,,0925-2738,,,,,,,,,,,,,,,,,,,,171,180,1994,"A simple technique for identifying protein secondary structures through the analysis of backbone 13C chemical shifts is described. It is based on the Chemical-Shift Index [Wishart et al. (1992) Biochemistry, 31, 1647-1651] which was originally developed for the analysis of 1H(alpha) chemical shifts. By extending the Chemical-Shift Index to include 13C(alpha), 13C(beta) and carbonyl 13C chemical shifts, it is now possible to use four independent chemical-shift measurements to identify and locate protein secondary structures. It is shown that by combining both 1H and 13C chemical-shift indices to produce a 'consensus' estimate of secondary structure, it is possible to achieve a predictive accuracy in excess of 92%. This suggests that the secondary structure of peptides and proteins can be accurately obtained from 1H and 13C chemical shifts, without recourse to NOE measurements." citations,entry_citation,4468,201230,1,,entry citation,,20496763,,,,"Structures of the Contryphan Family of Cyclic Peptides. Role of Electrostatic Interactions in Cis-trans Isomerism.",published,journal,Biochemistry,Biochemistry,39,,,,,,,,,,,,,,,,,,,,,,,12845,12852,2000, citations,entry_citation,4471,201294,1,,entry citation,,20285166,,,"Pristovsek, P., Luecke, C., Reincke, B., Lohr, F., Ludwig, B., and Rueterjans, H., ""Letter to the Editor: Complete 1H, 15N and 13C Assignment of the Functional Domain of Paracoccus denitrificans Cytochrome c552 in the Reduced state,"" J. Biomol. NMR 16, 353-354 (2000).","Letter to the Editor: Complete 1H, 15N and 13C Assignment of the Functional Domain of Paracoccus denitrificans Cytochrome c552 in the Reduced state",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,16,,,,,,,,,,,,,,,,,,,,,,,353,354,2000, citations,ref_1,4471,201295,2,,reference citation,,,10216157,,"Reincke, B., Thony-Meyer, L., Dannehl, C., Odenwald, A., Aidim, M., Witt, H., Ruterjans, H. & Ludwig, B. (1999) Heterologous expression of soluble fragments of cytochrome c552 acting as electron donor to the Paracoccus denitrificans cytochrome c oxidase. Biochim. Biophys. Acta, 1441, 114-120.",Heterologous expression of soluble fragments of cytochrome c552 acting as electron donor to the Paracoccus denitrificans cytochrome c oxidase.,published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1411,1,,0006-3002,,,,,,,,,,,,,,,,,,,,114,120,1999,"A membrane-bound c-type cytochrome, c552, acts as the electron mediator between the cytochrome bc1 complex and cytochrome c oxidase in the branched respiratory chain of the bacterium Paracoccus denitrificans. Unlike in mitochondria where a soluble cytochrome c interacts with both complexes, the bacterial c552, the product of the cycM gene, shows a tripartite structure, with an N-terminal membrane anchor separated from a typical class I cytochrome domain by a highly charged region. Two derivative fragments, lacking either only the membrane spanning region or both N-terminal domains, were constructed on the genetic level, and expressed in Escherichia coli cotransformed with the ccm gene cluster encoding host-specific cytochrome c maturation factors. High levels of cytochromes c were expressed and located in the periplasm as holo-proteins; both these purified c552 fragments are functional in electron transport to oxidase, as ascertained by kinetic measurements, and will prove useful for future structural studies of complex formation by NMR and X-ray diffraction." citations,ref_2,4471,201296,3,,reference citation,,,7628479,,"Turba, A., Jetzek, M. & Ludwig, B. (1995) Purification of Paracoccus denitrificans cytochrome c552 and sequence analysis of the gene. Eur. J. Biochem., 231, 259-265.",Purification of Paracoccus denitrificans cytochrome c552 and sequence analysis of the gene.,published,journal,Eur. J. Biochem.,European journal of biochemistry / FEBS,231,1,,0014-2956,,,,,,,,,,,,,,,,,,,,259,265,1995,"Unlike mitochondria, many bacteria use a large repertoire of c-type cytochromes in different branches of their electron transport system. Among the many cytochromes c present in the soil bacterium Paracoccus denitrificans, a membrane-bound cytochrome (c552) has been suggested to mediate the electron transport between the cytochrome bc1 complex and cytochrome-c oxidase [Berry, E. A. & Trumpower, B. L. (1985) J. Biol. Chem. 260, 2458-2467]. We have purified this cytochrome from cytoplasmic membranes, and cloned and sequenced its gene, cycM. Sequence analysis reveals that, while its C-terminal portion is highly similar to type-I cytochromes c, its N-terminal part contains a hydrophobic segment providing membrane attachment. In addition, we present immunological evidence for its functional role in respiration." citations,entry_citation,4472,201329,1,,entry citation,,20198307,,,"Cho, H.S., Lee, S-Y., Yan, D., Pan, X., Parkinson, J.S., Kustu, S., Wemmer, D.E., and Pelton, J.G., ""NMR Structure of Activated CheY,"" J. Mol. Biol. 297, 543-551 (2000).",NMR Structure of Activated CheY,published,journal,J. Mol. Biol.,Journal of Molecular Biology,297,,,,,,,,,,,,,,,,,,,,,,,543,551,2000, citations,entry_citation,4473,201353,1,,entry citation,,99173235,,,,The Molecular Basis for Protein Kinase A Anchoring Revealed by Solution NMR,published,journal,Nat. Struct. Biol.,Nature Structural Biology,6,,,,,,,,,,,,,,,,,,,,,,,222,227,1999, citations,entry_citation,4475,201373,1,,entry citation,,99253972,10318830,,,"NMR solution structure of complement-like repeat CR8 from the low density lipoprotein receptor-related protein",published,journal,J. Biol. Chem.,,274,,,,,,,,,,,,,,,,,,,,,,,14130,14136,1999, citations,entry_citation,4476,201390,1,,entry citation,,,9000078,,,"NMR structure of inactivation gates from mammalian voltage-dependent potassium channels",published,journal,Nature,,385,,,,,,,,,,,,,,,,,,,,,,,272,275,1997, citations,entry_citation,4477,201405,1,,entry citation,,,9000078,,,"NMR structure of inactivation gates from mammalian voltage-dependent potassium channels",published,journal,Nature,,385,,,,,,,,,,,,,,,,,,,,,,,272,275,1997, citations,entry_citation,4478,201421,1,,entry citation,,99107746,,,,"The Structure of a PKD Domain from Polycystin-1: Implications for Polycystic Kidney Diseas",published,journal,EMBO J.,,18,,,,,,,,,,,,,,,,,,,,,,,297,305,1999, citations,entry_citation,448,201434,1,,entry citation,,,,,"Bruch, Martha D., McKnight, C. James, Gierasch, Lila M., ""Helix Formation and Stability in a Signal Sequence,"" Biochemistry 28, 8554-8561 (1989).",Helix Formation and Stability in a Signal Sequence,published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,8554,8561,1989, citations,entry_citation,4483,201447,1,,entry citation,,99282203,,,,"Local interactions drive the formation of nonnative structure in the denatured state of human alpha-lactalbumin: a high resolution structural characterization of a peptide model in aqueous solution.",published,journal,Biochemistry,Biochemistry,38,,,,,,,,,,,,,,,,,,,,,,,7380,7387,1999, citations,entry_citation,4486,201463,1,,entry citation,,992499790,,,,"SOLUTION STRUCTURE OF COMPONENT B FROM METHANE MONOOXYGENASE DERIVED THROUGH HETERONUCLEAR NMR AND MOLECULAR MODELING""",published,journal,Biochemistry,Biochemistry,38,,,,,,,,,,,,,,,,,,,,,,,5799,5812,1999, citations,entry_citation,4487,201477,1,,entry citation,,99354413,,,,"Structure of a putative ancestral protein encoded by a single sequence repeat from a multidomain proteinase inhibitor gene fro Nicotiana alata",published,journal,Struc. Fold. Des.,Structure and Folding Design,7,,,,,,,,,,,,,,,,,,,,,,,793,802,1999, citations,entry_citation,4488,201495,1,,entry citation,,99289522,10359763,,,"Solution structure of a DNA decamer duplex containing the stable 3' T.G base pair of the pyrimidine(6-4)pyrimidone photoproduct [(6-4) adduct]: implications for the highly specific 3' T --> C transition of the (6-4) adduct",published,journal,Proc. Natl. Acad. Sci. USA,"Proceedings of the National Academy of Science, USA",96,,,,,,,,,,,,,,,,,,,,,,,6632,6636,1999, citations,entry_citation,449,201512,1,,entry citation,,,,,"Weaver, Arthur J., Kemple, Marvin D., Prendergast, Franklyn G., ""Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy,"" Biochemistry 28, 8614-8623 (1989).","Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,8614,8623,1989, citations,entry_citation,4490,201526,1,,entry citation,,99329063,,,,"Solution structure of the major alpha-amylase inhibitor of the crop plant Amaranth",published,journal,J. Biol. Chem.,Journal of Biological Chemistry,274,,,,,,,,,,,,,,,,,,,,,,,20473,20478,1999, citations,entry_citation,4491,201539,1,,entry citation,,99052122,9835057,,,"Sequence-specific 1H, 13C and 15N assignment of the EH1 domain of mouse Eps15",published,journal,J. Biomol. NMR,,12,,,,,,,,,,,,,,,,,,,,,,,465,466,1998, citations,entry_citation,4494,201599,1,,entry citation,,20209364,,,,"Solution Structure and Backbone Dynamics of Human Long-[Arg3]-Insulin Like Growth factor-1",published,journal,J. Biol. Chem.,Journal of Biological Chemistry,275,,,,,,,,,,,,,,,,,,,,,,,10009,10015,2000, citations,entry_citation,4496,201612,1,,entry citation,,20185067,10721992,,,"Structure Basis of Presequence Recognition by the Mitochondrial Protein Import Receptor Tom20",published,journal,Cell,Cell,100,,,,,,,,,,,,,,,,,,,,,,,551,560,2000, citations,entry_citation,4497,201641,1,,entry citation,,99303702,10373374,,,"High-resolution solution structure of the 18 kDa substrate-binding domain of the mammalian chaperone protein Hsc70",published,journal,J. Mol. Biol.,,289,,,,,,,,,,,,,,,,,,,,,,,1387,1403,1999, citations,entry_citation,4498,201670,1,,entry citation,,99043695,,,,"Solution Structure and Backbone Dynamics of Mason-Pfizer Monkey Virus (MPMV) Nucleocapsid Protein",published,journal,Protein Sci.,,7,,,,,,,,,,,,,,,,,,,,,,,2265,2280,1998, citations,entry_citation,45,201686,1,,entry citation,,,,,"Wagner, Gerhard, Wuthrich, Kurt, ""Sequential Resonance Assignments in Protein 1H Nuclear Magnetic Resonance Spectra (Basic Pancreatic Trypsin Inhibitor),"" J. Mol. Biol. 155, 347-366 (1982).","Sequential Resonance Assignments in Protein 1H Nuclear Magnetic Resonance Spectra (Basic Pancreatic Trypsin Inhibitor)",published,journal,J. Mol. Biol.,,155,,,,,,,,,,,,,,,,,,,,,,,347,366,1982, citations,entry_citation,450,201699,1,,entry citation,,,,,"Weaver, Arthur J., Kemple, Marvin D., Prendergast, Franklyn G., ""Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy,"" Biochemistry 28, 8614-8623 (1989).","Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,8614,8623,1989, citations,entry_citation,4500,201713,1,,entry citation,,99303703,10373375,,,"Structure-Activity relationships of w-conotoxins MVIIA, MVIIC and 14 loop splice hybrids at N- and P/Q-type calcium channel",published,journal,J. Mol. Biol.,Journal of Molecular Biology,289,,,,,,,,,,,,,,,,,,,,,,,1405,1421,1999, citations,entry_citation,4503,201733,1,,entry citation,,20374965,,,,Solution Structure of Alpha-conotoxin SI,published,journal,FEBS Lett.,FEBS Letters,476,,,,,,,,,,,,,,,,,,,,,,,287,295,2000, citations,citation_1,4503,201734,2,,reference citation,,,8520220,,"Delaglio, F. and Grzesiek, S. and Vuister, G. and Zhu, G. and Pfeifer, J. and Bax, A. NMRpipe - a multidimensional spectral processing system based on unix pipes. Journal of Biomolecular NMR (1995),6,277-293",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,citation_2,4503,201735,3,,reference citation,,,,,"Bartels, C. and Xia, T. H. and Billeter, M. and Guntert, P. and Wuthrich, K. The program XEasy for computer-supported NMR spectral-analysis of biological macromolecules. Journal of Biomolecular NMR (1995),6,1-10",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_3,4503,201736,4,,reference citation,,,8589602,,"Wishart, D. S. and Bigam, C. G. and Yao, J. and Abildgaard, F. and Dyson, H. J. and Oldfield, E. and Markley, J. L. and Sykes, B. D. 1H, 13C and 15N Chemical Shift Referencing in Biomolecular NMR. Journal of Biomolecular NMR (1995), 6, 135-140","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4506,201764,1,,entry citation,,20039867,10569926,,,"Solution structure of carnobacteriocin B2 and implications for structure-activity relationships among type IIa bacteriocins from lactic acid bacteria",published,journal,Biochemistry,,47,,,,,,,,,,,,,,,,,,,,,,,15438,15447,1999, citations,entry_citation,4507,201782,1,,entry citation,,,10572140,,,"Solution Structure of Carnobacteriocin B2 and Implications for Structure- Activity Relationships Among Type IIa Bacteriocins from Lactic Acid Bacteria",published,journal,Biochemistry,,38,,,,,,,,,,,,,,,,,,,,,,,15438,15447,1999, citations,entry_citation,4509,201797,1,,entry citation,,99106048,9887292,,,"Automated 2D NOESY assignment and structure calculation of Crambin(S22/I25) with the self-correcting distance geometry based NOAH/DIAMOD programs",published,journal,J. Magn. Reson.,,136,,,,,,,,,,,,,,,,,,,,,,,76,85,1999, citations,entry_citation,451,201816,1,,entry citation,,,,,"Weaver, Arthur J., Kemple, Marvin D., Prendergast, Franklyn G., ""Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy,"" Biochemistry 28, 8614-8623 (1989).","Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,8614,8623,1989, citations,entry_citation,4510,201830,1,,entry citation,,20015374,,,,"The second type II module from human matrix metalloproteinase 2: structure, function and dynamics",published,journal,Structure,,7,,,,,,,,,,,,,,,,,,,,,,,1235,1245,1999, citations,entry_citation,4514,201862,1,,entry citation,,,10652313,,,"NMR solution structure of complement-like repeat CR3 from the low density lipoprotein receptor-related protein (LRP). Evidence for specific binding to the receptor binding domain of human alpha-2 macroglobulin",published,journal,J. Biol. Chem.,,275,,,,,,,,,,,,,,,,,,,,,,,3264,3269,2000, citations,entry_citation,4572,202740,1,,entry citation,,20393887,,,,"Conformational changes in the PBX Homeodomain and C-terminal Extension upon Binding DNA and HOX-derived YPWM Peptides",published,journal,Biochemistry,Biochemistry,39,,,,,,,,,,,,,,,,,,,,,,,9943,9950,2000, citations,entry_citation,4516,201887,1,,entry citation,,20170882,,,,"Solution Structure of the PDZ2 Domain from Human Phosphatase hPTP1E and its Interactions with C-terminal Peptides from the Fas Receptor",published,journal,Biochemistry,Biochemistry,39,,,,,,,,,,,,,,,,,,,,,,,2572,2580,2000, citations,entry_citation,4519,201912,1,,entry citation,,20142663,10678173,,,"The eIF1A solution structure reveals a large RNA-binding surface important for scanning function",published,journal,Mol Cell,,5,,,,,,,,,,,,,,,,,,,,,,,109,119,2000, citations,entry_citation,452,201936,1,,entry citation,,,,,"Weaver, Arthur J., Kemple, Marvin D., Prendergast, Franklyn G., ""Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy,"" Biochemistry 28, 8614-8623 (1989).","Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,8614,8623,1989, citations,entry_citation,4522,201950,1,,entry citation,,20035963,,,,"Solution Structure of Anti-HIV-1 and Anti-Tumor Protein Map30: Structural Insights Into its Multiple Functions",published,journal,Cell,,99,,,,,,,,,,,,,,,,,,,,,,,433,442,1999, citations,entry_citation,4524,201969,1,,entry citation,,,11273698,,,"Solution Structure of a Type I Dockerin Domain, a Novel Prokaryotic, Extracellular Calcium-binding Domain",published,journal,J. Mol. Biol.,,307,,,,,,,,,,,,,,,,,,,,,,,745,753,2001, citations,ref-1,4524,201970,2,,reference citation,,98035057,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref-2,4524,201971,3,,reference citation,,96088118,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref-3,4524,201972,4,,reference citation,,,,,"Bartels, C., Xia, T., Billeter, M., Guentert, P. and Wuethrich, K. J. Biomol. NMR 6, 1-10 (1995).",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4526,201998,1,,entry citation,,20348894,10892805,,,"Tumor suppressor INK4: refinement of p16INK4A structure and determination of p15INK4B structure by comparative modeling and NMR data",published,journal,Protein Sci.,,9,,,,,,,,,,,,,,,,,,,,,,,1120,1128,2000, citations,entry_citation,4527,202022,1,,entry citation,,20085967,,,,"Structure of a Transiently Phosphorylated ""Switch"" in Bacterial Signal Transduction",published,journal,Nature,Nature,402,,,,,,,,,,,,,,,,,,,,,,,894,898,1999, citations,ref_1,4527,202023,2,,reference citation,,,7827089,,,Three-dimensional solution structure of the N-terminal receiver domain of NTRC.,published,journal,Biochemistry,Biochemistry,34,4,,0006-2960,,,,,,,,,,,,,,,,,,,,1413,1424,1995,"NTRC is a transcriptional enhancer binding protein whose N-terminal domain is a member of the family of receiver domains of two-component regulatory systems. Using 3D and 4D NMR spectroscopy, we have completed the 1H, 15N, and 13C assignments and determined the solution structure of the N-terminal receiver domain of the NTRC protein. Determination of the three-dimensional structure was carried out with the program X-PLOR (Brunger, 1992) using a total of 915 NMR-derived distance and dihedral angle restraints. The resultant family of structures has an average root mean square deviation of 0.81 A from the average structure for the backbone atoms involved in well-defined secondary structure. The structure is comprised of five alpha-helices and a five-stranded parallel beta-sheet, in a (beta/alpha)5 topology. Comparison of the solution structure of the NTRC receiver domain with the crystal structures of the homologous protein CheY in both the Mg(2+)-free and Mg(2+)-bound forms [Stock, A.M., Mottonen, J. M., Stock, J. B., & Schutt, C. E. (1989) Nature 337, 745-749; Volz, K., & Matsumura, P. (1991) J. Biol. Chem. 296, 15511-15519; Stock, A. M., Martinez-Hackert, E., Rasmussen, B. F., West, A. H., Stock, J. B., Ringe, D., & Petsko, G. A. (1993) Biochemistry 32, 13375-13380; Bellsolell, L., Prieto, J., Serrano, L., & Coll, M. (1994) J. Mol. Biol. 238, 489-495] reveals a very similar fold, with the only significant difference occurring in the positioning of helix 4 relative to the rest of the protein. Examination of the conformation of consensus residues of the receiver domain superfamily [Volz, K. (1993) Biochemistry 32, 11741-11753] in the structures of the NTRC receiver domain and CheY establishes the structural importance of residues whose side chains are involved in hydrogen bonding or hydrophobic core interactions. The importance of some nonconsensus residues which may be conserved for their ability to fulfill helix capping roles is also discussed." citations,entry_citation,4528,202041,1,,entry citation,,20085967,,,,"Structure of a Transiently Phosphorylated ""Switch"" in Bacterial Signal Transduction",published,journal,Nature,Nature,402,,,,,,,,,,,,,,,,,,,,,,,894,898,1999, citations,ref_1,4528,202042,2,,reference citation,,,7827089,,,Three-dimensional solution structure of the N-terminal receiver domain of NTRC.,published,journal,Biochemistry,Biochemistry,34,4,,0006-2960,,,,,,,,,,,,,,,,,,,,1413,1424,1995,"NTRC is a transcriptional enhancer binding protein whose N-terminal domain is a member of the family of receiver domains of two-component regulatory systems. Using 3D and 4D NMR spectroscopy, we have completed the 1H, 15N, and 13C assignments and determined the solution structure of the N-terminal receiver domain of the NTRC protein. Determination of the three-dimensional structure was carried out with the program X-PLOR (Briinger, 1992) using a total of 915 NMR-derived distance and dihedral angle restraints. The resultant family of structures has an average root mean square deviation of 0.81 A from the average structure for the backbone atoms involved in well-defined secondary structure. The structure is comprised of five alpha-helices and a five-stranded parallel beta-sheet, in a (beta/alpha)5 topology. Comparison of the solution structure of the NTRC receiver domain with the crystal structures of the homologous protein CheY in both the Mg(2+)-free and Mg(2+)-bound forms [Stock, A.M., Mottonen, J. M., Stock, J. B., & Schutt, C. E. (1989) Nature 337, 745-749; Volz, K., & Matsumura, P. (1991) J. Biol. Chem. 296, 15511-15519; Stock, A. M., Martinez-Hackert, E., Rasmussen, B. F., West, A. H., Stock, J. B., Ringe, D., & Petsko, G. A. (1993) Biochemistry 32, 13375-13380; Bellsolell, L., Prieto, J., Serrano, L., & Coll, M. (1994) J. Mol. Biol. 238, 489-495] reveals a very similar fold, with the only significant difference occurring in the positioning of helix 4 relative to the rest of the protein. Examination of the conformation of consensus residues of the receiver domain superfamily [Volz, K. (1993) Biochemistry 32, 11741-11753] in the structures of the NTRC receiver domain and CheY establishes the structural importance of residues whose side chains are involved in hydrogen bonding or hydrophobic core interactions. The importance of some nonconsensus residues which may be conserved for their ability to fulfill helix capping roles is also discussed." citations,entry_citation,453,202065,1,,entry citation,,,,,"Weaver, Arthur J., Kemple, Marvin D., Prendergast, Franklyn G., ""Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy,"" Biochemistry 28, 8614-8623 (1989).","Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,8614,8623,1989, citations,entry_citation,4536,202080,1,,entry citation,,10756190,,,,Structural basis for uracil DNA glycosylase interaction with uracil: NMR study,published,journal,Nucleic Acids Res.,,28,,,,,,,,,,,,,,,,,,,,,,,1906,1912,2000, citations,entry_citation,454,202102,1,,entry citation,,,,,"Weaver, Arthur J., Kemple, Marvin D., Prendergast, Franklyn G., ""Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy,"" Biochemistry 28, 8614-8623 (1989).","Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,8614,8623,1989, citations,entry_citation,4540,202116,1,,entry citation,,99212145,10195898,,,Evolution of a protein fold in vitro,published,journal,Science,,284,,,,,,,,,,,,,,,,,,,,,,,325,328,1999, citations,entry_citation,4642,203963,1,,entry citation,,,11300761,,,"The NMR Structure of Human Beta-Defensin-2 Reveals a Novel Alpha-Helical Segment",published,journal,Biochemistry,,40,,,,,,,,,,,,,,,,,,,,,,,3810,3816,2001, citations,entry_citation,4541,202129,1,,entry citation,,20095844,,,,"Structural and functional consequences of the presence of a fourth disulfide bridge in the scorpion short toxins: Solution structure of the potassium channel inhibitor HsTX1",published,journal,Protein Sci.,,8,,,,,,,,,,,,,,,,,,,,,,,2672,2685,1999, citations,entry_citation,4542,202147,1,,entry citation,,99412438,10481034,,,"Structural Characterization of a Uracil Containing Hairpin DNA by NMR and Molecular Dynamics",published,journal,Nucleic Acids Res.,,27,19,,,,,,,,,,,,,,,,,,,,,,3938,3944,1999, citations,entry_citation,4547,202169,1,,entry citation,,20039868,10569927,,,"Solution structure of a DNA.RNA hybrid containing an alpha-anomeric thymidine and polarity reversals: d(ATGG-3'-3'-(alpha-T)-5'-5'-GCTC).r(gagcaccau)",published,journal,Biochemistry,,38,47,,,,,,,,,,,,,,,,,,,,,,15448,15458,1999, citations,entry_citation,455,202198,1,,entry citation,,,,,"Weaver, Arthur J., Kemple, Marvin D., Prendergast, Franklyn G., ""Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy,"" Biochemistry 28, 8614-8623 (1989).","Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,8614,8623,1989, citations,entry_citation,4550,202212,1,,entry citation,,,,,,NMR Structure of the Palindromic DNA Decamer d(GCGTTAACGC)2,published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4551,202234,1,,entry citation,,,9454593,,,"Structure and stability of the N-terminal domain of the ribosomal protein L9: evidence for rapid two-state folding.",published,journal,Biochemistry,Biochemistry,37,4,,,,,,,,,,,,,,,,,,,,,,1025,1032,1998, citations,entry_citation,4552,202248,1,,entry citation,,20573569,11123901,,,"Structure of the Bovine Antimicrobial Peptide Indolicidin bound to Dodecylphosphocholine and Sodium Dodecyl Sulfate Micelles",published,journal,Biochemistry,,39,51,,,,,,,,,,,,,,,,,,,,,,15765,15774,2000, citations,entry_citation,4553,202266,1,,entry citation,,20262885,,,"Kriwacki, R.W., Legge, G.B., Hommel, U., Ramage, P., Chung, J., Tennant, L.L., Wright, P.E., and Dyson, H.J., ""Assignment of 1H, 13C and 15N Resonances of the I-domain of Human Leukocyte Function Associated Antigen-1,"" J. Biomol. NMR 16, 271-272 (2000).","Assignment of 1H, 13C and 15N Resonances of the I-domain of Human Leukocyte Function Associated Antigen-1",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,16,3,,,,,,,,,,,,,,,,,,,,,,271,272,2000, citations,ref_1,4553,202267,2,,reference citation,,,,,"Assignment of the 1H, 13C and 15N Resonances of the I-domain of Human Leukocyte Function Associated Antigen-1 In preparation. J. Biomol. NMR",,published,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_2,4553,202268,3,,reference citation,,,10653701,,"NMR solution structure of the inserted domain of human Leukocyte Function Associated Antigen-1 J. Mol. Biol. (In press) Glen B. Legge, Richard W. Kriwacki, John Chung, Ulrich Hommel|, Paul Ramage|, H. Jane Dyson and Peter E. Wright",NMR solution structure of the inserted domain of human leukocyte function associated antigen-1.,published,journal,J. Mol. Biol.,Journal of molecular biology,295,5,,0022-2836,,,,,,,,,,,,,,,,,,,,1251,1264,2000,"The interaction between the leukocyte function-associated antigen-1 (LFA-1) and the intercellular adhesion molecule is thought to be mediated primarily via the inserted domain (I-domain) in the alpha-subunit. The activation of LFA-1 is an early step in triggering the adhesion of leukocytes to target cells decorated with intercellular adhesion molecules. There is some disagreement in the literature over the respective roles of conformational changes in the I-domain and of divalent cations (Mg(2+), Mn(2+)) in the activation of LFA-1 for intercellular adhesion molecule binding. X-ray crystallographic structures of the I-domains of LFA-1 and Mac-1 in the presence and absence of cations show structural differences in the C-terminal alpha-helix; this change was proposed to represent the active and inactive conformations of the I-domain. However, more recent X-ray results have called this proposal into question. The solution structure of the Mg(2+) complex of the I-domain of LFA-1 has been determined by NMR methods, using a model-based approach to nuclear Overhauser enhancement spectroscopy peak assignment. The protein adopts the same structure in solution as that of the published I-domain X-ray structures, but the C-terminal region, where the X-ray structures are most different from each other, is different again in the solution structures. The secondary structure of this helix is well formed, but NMR relaxation data indicate that there is considerable flexibility present, probably consisting of breathing or segmental motion of the helix. The conformational diversity seen in the various X-ray structures could be explained as a result of the inherent flexibility of this C-terminal region and as a result of crystal contacts. Our NMR data are consistent with a model where the C-terminal helix has the potential flexibility to take up alternative conformations, for example, in the presence and absence of the intercellular adhesion molecule ligand. The role of divalent cations appears from our results not to be as a direct mediator of a conformational change that alters affinity for the ligand. Rather, the presence of the cation appears to be involved in some other way in ligand binding, perhaps by acting as a bridge to the ligand and by modulation of the charge of the binding surface." citations,ref_3,4553,202269,4,,reference citation,,,10493852,,"Structural Basis for LFA-1 Inhibition upon Lovastatin Binding to the CD11a I-Domain J. Kallen, K. Welzenbach, P. Ramage, D. Geyl, R. Kriwacki, G. Legge, S. Cottens,G. Weitz-Schmidt, U. Hommel Journal of Molecular Biology, Vol. 292, No. 1, Sep 1999, pp. 1-9 (doi:10.1006/jmbi.1999.3047)",Structural basis for LFA-1 inhibition upon lovastatin binding to the CD11a I-domain.,published,journal,J. Mol. Biol.,Journal of molecular biology,292,1,,0022-2836,,,,,,,,,,,,,,,,,,,,1,9,1999,"The lymphocyte function-associated antigen (LFA-1) belongs to the family of beta2-integrins and plays an important role in T-cell activation and leukocyte migration to sites of inflammation. We report here that lovastatin, a drug clinically used for lowering cholesterol levels, inhibits the interaction of human LFA-1 with its counter-receptor intercellular adhesion molecule-1. Using nuclear magnetic resonance spectroscopy and X-ray crystallography we show that the inhibitor binds to a highly conserved domain of the LFA-1 alpha-chain called the I-domain. The first three-dimensional structure of an integrin inhibitor bound to its receptor reveals atomic details for a hitherto unknown mode of LFA-1 inhibition. It also sheds light into possible mechanisms of LFA-1 mediated signalling and will support the design of novel anti-adhesive and immunosuppressive drugs." citations,entry_citation,4554,202289,1,,entry citation,,,,,,"Letter to the Editor: Backbone HN, N, Ca, C' and Cb assignments of the 19 kDa DHFR/NADPH complex at 9C and pH 7.6",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,16,,,,,,,,,,,,,,,,,,,,,,,349,350,2000, citations,ref_1,4554,202290,2,,reference citation,,,,,"Hsu, M.C., Ho, Y., Huang, F.Y.(1998) Journal of the Chinese Chemical Society, 45, 115-121.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4567,202642,1,,entry citation,,20285165,,,"Hamilton, K.S., Ellison, M.J., and Shaw, G.S., ""Letter to the Editor: 1H, 15N and 13C Resonance Assignments for the Catalytic Domain of the Yeast E2, UBC1,"" J. Biomol. NMR 16, 351-352 (2000).","Letter to the Editor: 1H, 15N and 13C Resonance Assignments for the Catalytic Domain of the Yeast E2, UBC1",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,16,,,,,,,,,,,,,,,,,,,,,,,351,352,2000, citations,entry_citation,4568,202666,1,,entry citation,,,,,,"Native and non-native secondary structure and dynamics in the pH 4 intermediate of apomyoglobin",submitted,journal,Biochemistry,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_1,4568,202667,2,,reference citation,,98120979,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_2,4568,202668,3,,reference citation,,98055460,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_3,4568,202669,4,,reference citation,,96026357,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4643,203977,1,,entry citation,,21930705,11856344,,,SMAP-29 has two LPS-binding sites and a central hinge,published,journal,Eur. J. Biochem.,,269,4,,,,,,,,,,,,,,,,,,,,,,1181,1189,2002, citations,ref_2,4554,202291,3,,reference citation,,,3307916,,"Fierke, C.A., Johnson, K.A., Benkovic, S.J.(1987) Biochemistry, 26, 4085-4092.",Construction and evaluation of the kinetic scheme associated with dihydrofolate reductase from Escherichia coli.,published,journal,Biochemistry,Biochemistry,26,13,,0006-2960,,,,,,,,,,,,,,,,,,,,4085,4092,1987,"A kinetic scheme is presented for Escherichia coli dihydrofolate reductase that predicts steady-state kinetic parameters and full time course kinetics under a variety of substrate concentrations and pHs. This scheme was derived from measuring association and dissociation rate constants and pre-steady-state transients by using stopped-flow fluorescence and absorbance spectroscopy. The binding kinetics suggest that during steady-state turnover product dissociation follows a specific, preferred pathway in which tetrahydrofolate (H4F) dissociation occurs after NADPH replaces NADP+ in the ternary complex. This step, H4F dissociation from the E X NADPH X H4F ternary complex, is proposed to be the rate-limiting step for steady-state turnover at low pH because koff = VM. The rate constant for hydride transfer from NADPH to dihydrofolate (H2F), measured by pre-steady-state transients, has a deuterium isotope effect of 3 and is rapid, khyd = 950 s-1, essentially irreversible, Keq = 1700, and pH dependent, pKa = 6.5, reflecting ionization of a single group in the active site. This scheme accounts for the apparent pKa = 8.4 observed in the steady state as due to a change in the rate-determining step from product release at low pH to hydride transfer above pH 8.4. This kinetic scheme is a necessary background to analyze the effects of single amino acid substitutions on individual rate constants." citations,ref_3,4554,202292,4,,reference citation,,,9012674,,"Sawaya, M.R., Kraut, J.(1997) Biochemistry, 36, 586-603.",Loop and subdomain movements in the mechanism of Escherichia coli dihydrofolate reductase: crystallographic evidence.,published,journal,Biochemistry,Biochemistry,36,3,,0006-2960,,,,,,,,,,,,,,,,,,,,586,603,1997,"The reaction catalyzed by Escherichia coli dihydrofolate reductase (ecDHFR) cycles through five detectable kinetic intermediates: holoenzyme, Michaelis complex, ternary product complex, tetrahydrofolate (THF) binary complex, and THF.NADPH complex. Isomorphous crystal structures analogous to these five intermediates and to the transition state (as represented by the methotrexate-NADPH complex) have been used to assemble a 2.1 A resolution movie depicting loop and subdomain movements during the catalytic cycle (see Supporting Information). The structures suggest that the M20 loop is predominantly closed over the reactants in the holoenzyme, Michaelis, and transition state complexes. But, during the remainder of the cycle, when nicotinamide is not bound, the loop occludes (protrudes into) the nicotinamide-ribose binding pocket. Upon changing from the closed to the occluded conformation, the central portion of the loop rearranges from beta-sheet to 3(10) helix. The change may occur by way of an irregularly structured open loop conformation, which could transiently admit a water molecule into position to protonate N5 of dihydrofolate. From the Michaelis to the transition state analogue complex, rotation between two halves of ecDHFR, the adenosine binding subdomain and loop subdomain, closes the (p-aminobenzoyl)glutamate (pABG) binding crevice by approximately 0.5 A. Resulting enhancement of contacts with the pABG moiety may stabilize puckering at C6 of the pteridine ring in the transition state. The subdomain rotation is further adjusted by cofactor-induced movements (approximately 0.5 A) of helices B and C, producing a larger pABG cleft in the THF.NADPH analogue complex than in the THF analogue complex. Such movements may explain how THF release is assisted by NADPH binding. Subdomain rotation is not observed in vertebrate DHFR structures, but an analogous loop movement (residues 59-70) appears to similarly adjust the pABG cleft width, suggesting that these movements are important for catalysis. Loop movement, also unobserved in vertebrate DHFR structures, may preferentially weaken NADP+ vs NADPH binding in ecDHFR, an evolutionary adaptation to reduce product inhibition in the NADP+ rich environment of prokaryotes." citations,ref_4,4554,202293,5,,reference citation,,,,,"Oppenheimer, N.J.(1982) in The Pyridine Nucleotide Coenzymes (Everse, J., Anderson, B., You, K., Eds), 51-89, Academic Press, New York 36, 586-603.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_5,4554,202294,6,,reference citation,,,,,"Rafter, G.W. and Colowick, S.P. (1957) in Methods in Enzymology, 3, 887-890.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_6,4554,202295,7,,reference citation,,,8477186,,"Grzesiek, S. and Bax, A. (1993) J. Biomol. NMR, 3, 185-204.",Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N-enriched proteins.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,3,2,,0925-2738,,,,,,,,,,,,,,,,,,,,185,204,1993,"Experiments and procedures are described that greatly alleviate the sequential assignment process of uniformly 13C/15N-enriched proteins by determining the type of amino acid from experiments that correlate side chain with backbone amide resonances. A recently proposed 3D NMR experiment, CBCA(CO)NH, correlates C alpha and C beta resonances to the backbone amide 1H and 15N resonances of the next residue (Grzesiek, S. and Bax, A. (1992) J. Am. Chem. Soc., 114, 6291-6293). An extension of this experiment is described which correlates the proton H beta and H alpha resonances to the amide 1H and 15N resonances of the next amino acid, and a detailed product operator description is given. A simple 2D-edited constant-time HSQC experiment is described which rapidly identifies H beta and C beta resonances of aromatic or Asn/Asp residues. The extent to which combined knowledge of the C alpha and C beta chemical shift values determines the amino acid type is investigated, and it is demonstrated that the combined C alpha and C beta chemical shifts of three or four adjacent residues usually are sufficient for defining a unique position in the protein sequence." citations,ref_7,4554,202296,8,,reference citation,,,,,"Yamazaki, T., Lee, W., Arrowsmith, C.H., Muhandiram, D.R. and Kay, L.E. (1994) Journal of the American Chemical Society, 116, 11655-11666.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_8,4554,202297,9,,reference citation,,,7669761,,"Epstein, D.M., Benkovic, S.J. and Wright, P.E. (1995) Biochemistry, 34, 11037-11048.",Dynamics of the dihydrofolate reductase-folate complex: catalytic sites and regions known to undergo conformational change exhibit diverse dynamical features.,published,journal,Biochemistry,Biochemistry,34,35,,0006-2960,,,,,,,,,,,,,,,,,,,,11037,11048,1995,"Backbone and tryptophan side-chain dynamics of uniformly 15N-labeled Escherichia coli dihydrofolate reductase were determined for the binary folate complex. The 15N T1 and T2 relaxation times and [1H]-15N heteronuclear NOEs were measured for 118 protonated backbone nitrogen atoms. The generalized order parameter (S2), the effective correlation time for internal motions (tau e), and the contribution to spin-spin relaxation through 15N exchange broadening (Rex) were determined for each residue by model-free analysis. Back-calculation of the relaxation rates for each resonance showed that the calculated dynamical parameters accurately predict the experimental data. Diverse dynamical features were evident in the DHFR backbone. Six sites exhibited order parameters significantly below the weighted mean S2 value (for the complex) of 0.81 +/- 0.002: residues G67 and D69 of the adenosine binding domain, and ""hinge"" residues K38 and V88, exhibited low S2 (0.29 < or = S2 < or = 0.6) and high tau e values (700 ps < or = tau e < or = 2 ns), as did sites within the beta A-alpha B loop and the beta F-beta G loop. Thus, large amplitude backbone motions, on the picosecond and nanosecond time scales, occurred at regions implicated in transition-state stabilization and in ligand-dependent conformational change. Significant Rex values (> or = 1 s-1) were determined for 45% of assigned resonances, many of which arise from residues surrounding the folate binding site. The mean S2 values of the occupied folate binding site and the unoccupied NADPH binding site were similar, indicating the backbone of the latter is at least as conformationally restricted as that of the occupied folate site. We conclude that the observed time-dependent structural fluctuations of the binary complex are in fact associated with catalytic properties of the molecule." citations,entry_citation,4571,202721,1,,entry citation,,20300898,,,"Mackereth, C.D., Arrowsmith, C.H., Edwards, A.M., and McIntosh, L.P., ""Zinc-bundle Structure of the Essential RNA Polymerase Subunit RPB10 from Methanobacterium thermoautotrophicum,"" Proc. Natl. Acad. Sci. U.S.A. 97, 6316-6321 (2000).","Zinc-bundle Structure of the Essential RNA Polymerase Subunit RPB10 from Methanobacteriumthermoautotrophicum",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,97,,,,,,,,,,,,,,,,,,,,,,,6316,6321,2000, citations,ref_9,4554,202298,10,,reference citation,,,8019142,,"Falzone, C.J., Cavanagh, J., Cowart, M., Palmer III, A.G., Matthews, C.R., Benkovic, S.J. and Wright, P.E. (1994) Journal of Biomolecular NMR, 4, 349-366.","1H, 15N and 13C resonance assignments, secondary structure, and the conformation of substrate in the binary folate complex of Escherichia coli dihydrofolate reductase.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,4,3,,0925-2738,,,,,,,,,,,,,,,,,,,,349,366,1994,"By using fully 15N- and 15N/13C-labeled Escherichia coli dihydrofolate reductase, the sequence-specific 1H and 15N NMR assignments were achieved for 95% of the backbone resonances and for 90% of the 13C alpha resonances in the binary folate complex. These assignments were made through a variety of three-dimensional proton-detected 15N and 13C experiments. A smaller but significant subset of side-chain 1H and 13C assignments were also determined. In this complex, only one 15N or 13C resonance was detected per 15N or 13C protein nucleus, which indicated a single conformation. Proton-detected 13C experiments were also performed with unlabeled DHFR, complexed with 13C-7/13C-9 folate to probe for multiple conformations of the substrate in its binary complex. As was found for the protein resonances, only a single bound resonance corresponding to a productive conformation could be detected for C-7. These results are consistent with an earlier report based on 1H NMR data [Falzone, C.J. et al. (1990) Biochemistry, 29, 9667-9677] and suggest that the E. coli enzyme is not involved in any catalytically unproductive binding modes in the binary complex. This feature of the E. coli enzyme seems to be unique among the bacterial forms of DHFR that have been studied to date." citations,entry_citation,4555,202332,1,,entry citation,,,,,"Castagne C., Murphy, E.C., Gronenborn A.M., and Delepierre, M., ""31P NMR Analysis of the DNA Conformation Induced by Protein Binding SRY/DNA Complexes,"" Eur. J. Biochem. 267, 1223-1229 (2000).","31P NMR Analysis of the DNA Conformation Induced by Protein Binding SRY/DNA Complexes",published,journal,Eur. J. Biochem.,European Journal of Biochemistry,267,,,,,,,,,,,,,,,,,,,,,,,1223,1229,2000, citations,entry_citation,4556,202353,1,,entry citation,,,,,,"31P NMR analysis of the DNA conformation induced by protein binding:SRY-DNA complexes",submitted,journal,Eur. J. Biochem.,European Journal of Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4557,202374,1,,entry citation,,10521276,,,,"The structure of the active domain of the herpes simplex virus protein ICP47 in water/sodium dodecyl sulfate solution determined by nuclear magnetic resonance spectroscop",published,journal,Biochemistry,,38,41,,,,,,,,,,,,,,,,,,,,,,13692,13698,1999, citations,entry_citation,4558,202395,1,,entry citation,,21544931,11693571,,,"Letter to the editor: 1H, 15N and 13C Assignments of the N-terminal Domain of Yersinia outer Protein H in its apo form and in Complex with a Phosphotyrosine Peptide",published,journal,J. Biomol. NMR,,21,1,,,,,,,,,,,,,,,,,,,,,,69,70,2001, citations,entry_citation,4559,202418,1,,entry citation,,20143476,10677209,,,"The NMR structure of the nucleocapsid protein from the mouse mammary tumor virus reveals unusual folding of the C-terminal zinc knuckle",published,journal,Biochemistry,,39,,,,,,,,,,,,,,,,,,,,,,,1604,1612,2000, citations,entry_citation,456,202445,1,,entry citation,,,,,"Weaver, Arthur J., Kemple, Marvin D., Prendergast, Franklyn G., ""Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy,"" Biochemistry 28, 8614-8623 (1989).","Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,8614,8623,1989, citations,entry_citation,4560,202459,1,,entry citation,,,,,,"Letter to the Editor: Assignment of 1H, 13C and 15N signals of a recombinant effector protein (T4MOD) in Toluene-4-monooxygenase complex",published,journal,J. Biomol. NMR,,16,,,,,,,,,,,,,,,,,,,,,,,359,360,2000, citations,entry_citation,4561,202491,1,,entry citation,,,,,,"Solution Structure of Imperatoxin A (IpTxa) from the scorpion P. imperator Determined by 1H-NMR Spectroscopy",in preparation,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4562,202515,1,,entry citation,,20365224,,,,"Letter to the Editor: Complete 1H and Non-carbonylic 13C Assignments of Native Hen Egg-white Lysozyme",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,17,,,,,,,,,,,,,,,,,,,,,,,83,84,2000, citations,entry_citation,4563,202535,1,,entry citation,,,,,,NMR Structure of the Bovine Prion Protein,in preparation,journal,Proc. Natl. Acad. Sci. U.S.A.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4564,202560,1,,entry citation,,,,,,NMR Structure of the Bovine Prion Protein,in preparation,journal,Proc. Natl. Acad. Sci. U.S.A.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4565,202587,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N resonance assignments for a truncated and inhibited catalytic domain of matrix metalloproteinase-2",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,17,1,,,,,,,,,,,,,,,,,,,,,,85,86,2000, citations,entry_citation,4566,202602,1,,entry citation,,,,,,"Letter to the Editor: Assignment of 1H, 13C and 15N signals of bovine adrenodoxin",published,journal,J. Biomol. NMR,,17,4,,,,,,,,,,,,,,,,,,,,,,355,356,2000, citations,ref_1,4566,202603,2,,reference citation,,,14317399,,"Kimura, T. and Suzuki (1965), Biochem. Biophys. Res. Comm. 19, S. 340-345",AN IRON PROTEIN AS A COMPONENT OF STEROID 11-BETA-HYDROXYLASE COMPLEX.,published,journal,Biochem. Biophys. Res. Commun.,Biochemical and biophysical research communications,19,,,0006-291X,,,,,,,,,,,,,,,,,,,,340,345,1965, citations,ref_4,4566,202604,3,,reference citation,,,438190,,"Stormer, F.C., Pedersen, J.I. and Oftebro, H. (1979), JBC 254, S. 4331-4334",The presence of an adrenodoxin-like ferredoxin and cytochrome P-450 in brain mitochondria.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,254,11,,0021-9258,,,,,,,,,,,,,,,,,,,,4331,4334,1979,"An iron-sulfur protein has been isolated from bovine brain mitochondria and purified 200-fold. The optical spectrum (peaks at 412 and 455 nm which disappear upon reduction) and the EPR spectrum (g values at 1.94 and 2.02) were typical for a ferredoxin. In reconstitution experiments, the protein could replace adrenodoxin in the cholesterol side chain cleavage reaction. The additional detection of cytochrome P-450 in brain mitochondria indicates that the isolated ferredoxin is part of a cytochrome P-450-dependent hydroxylation system." citations,entry_citation,457,202690,1,,entry citation,,,,,"Weaver, Arthur J., Kemple, Marvin D., Prendergast, Franklyn G., ""Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy,"" Biochemistry 28, 8614-8623 (1989).","Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,8614,8623,1989, citations,entry_citation,4570,202704,1,,entry citation,,99435745,,,,"A Single-Point Mutation in the Extreme Heat- and Pressure-Resistant Sso7d From Sulfolobus Solfataricus Leads to a Major Rearrangement of the Hydrophobic Core",published,journal,Biochemistry,Biochemistry,38,39,,,,,,,,,,,,,,,,,,,,,,12709,12717,1999, citations,ref_5,4566,202605,4,,reference citation,,,6274987,,"Saarem, K., Bjorkhem, I., Pedersen, J.I. and Oftebro, H. (1981), J.Lipid. Res. 22, S. 1254-1264",Side chain hydroxylation of C27-steroids and vitamin D3 by a cytochrome P-450 enzyme system isolated from human liver mitochondria.,published,journal,J. Lipid Res.,Journal of lipid research,22,8,,0022-2275,,,,,,,,,,,,,,,,,,,,1254,1264,1981,"The present study was undertaken to obtain information on the involvement of cytochrome P-450 in the 26-hydroxylation on bile acid intermediates and in the 25-hydroxylation of vitamin D3 in human liver mitochondria. Cytochrome P-450 was solubilized from human liver mitochondria and purified two times to a specific content of 0.125 nmol per mg protein. Furthermore, a ferredoxin was isolated from the mitochondria and partly purified. This iron-sulfur protein had properties similar to bovine adrenal ferredoxin. A mitochondrial NADPH-ferredoxin reductase was also isolated and purified to homogeneity. This enzyme was a flavoprotein with properties very similar to the bovine adrenal NADPH-ferredoxin reductase. The cytochrome P-450 preparation catalyzed 26-hydroxylation of C27-steroids and 25-hydroxylation of vitamin D3 when reconstructed with NADPH, the ferredoxin and the ferredoxin reductase. With different substrates the following turnover numbers (nmol product X nmol P-450(-1) X min-1) were found: cholesterol, 8; 5-cholestene-3 beta, 7 alpha-diol, 10; 7 alpha-hydroxy-4-cholesten-3-one, 23; 7 alpha, 12 alpha-dihydroxy-4-cholesten-3-one, 27; 5 beta-cholestane-3 alpha, 7 alpha-diol, 28; 5 beta-cholestane-3 alpha, 7 alpha, 12 alpha-triol, 41; and vitamin D3, 0.16. The hydroxylation reactions were inhibited by CO and metyrapone. The human liver mitochondrial ferredoxin and ferredoxin reductase could be replaced by adrenal ferredoxin and adrenal ferredoxin reductase without reduction of activity, but they could not be replaced by microsomal NADPH-cytochrome P-450 reductase. It is concluded that human liver mitochondria contain cytochrome P-450 involved in the oxidation of the side chain of C27-steroids and vitamin D3." citations,ref_6,4566,202606,5,,reference citation,,,207706,,"Okuda, K. and Atsuta, Y. (1978), JBC 253, S. 4653-4658","Isolation of rat liver mitochondrial ferredoxin and its reductase active in the 5beta-cholestane-3alpha, 7alpha, 12alpha-triol 26-hydroxylase.",published,journal,J. Biol. Chem.,The Journal of biological chemistry,253,13,,0021-9258,,,,,,,,,,,,,,,,,,,,4653,4658,1978, citations,ref_7,4566,202607,6,,reference citation,,,3080335,,"Hiwatashi, A., Ichikawa, Y. and Waki, N. (1986), FEBS Lett. 195, S. 87-91",Purification and biochemical characterization of hepatic ferredoxin (hepatoredoxin) from bovine liver mitochondria.,published,journal,FEBS Lett.,FEBS letters,195,1-2,,0014-5793,,,,,,,,,,,,,,,,,,,,87,91,1986,"Hepatic ferredoxin (hepatoredoxin) was purified from bovine liver mitochondria. The monomeric molecular mass of the hepatoredoxin was larger than that of adrenocortical ferredoxin (adrenodoxin) from bovine adrenocortical mitochondria at 14 kDa. We studied the amino acid residues and NH2-terminal sequence of this protein. The hepatoredoxin was organ-specific protein. The optical absorption spectrum of oxidized hepatoredoxin had two peaks, at 414 and 455 nm in the visible region. Hepatoredoxin formed an immunoprecipitin line against anti-adrenodoxin immunoglobulin in Ouchterlony double diffusion, and an immunochemical staining band in Western blotting." citations,ref_3,4566,202608,7,,reference citation,,,,,"Kimura, T. (1968), Struct. Bonding 5, S. 1-40",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_2,4566,202609,8,,reference citation,,,3401007,,"Cupp, J.R., Vickery, L.E. and Coghlan, V.M. (1988), Arch.Biochem.Biophys. 264, S. 376-382",Purification and characterization of human placental ferredoxin.,published,journal,Arch. Biochem. Biophys.,Archives of biochemistry and biophysics,264,2,,0003-9861,,,,,,,,,,,,,,,,,,,,376,382,1988,"A ferredoxin-type iron-sulfur protein was isolated from human placenta mitochondria. The properties of the purified protein were very similar to those of adrenal ferredoxin (adrenodoxin), and immunological cross-reactivity with polyclonal antibodies to bovine adrenodoxin was observed. The N-terminal amino acid sequence and the visible absorption spectrum were identical to bovine adrenodoxin. The molecular mass as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (Mr approximately 13,500), however, is slightly smaller than that of adrenodoxin, and the C-terminal sequence is different. Human placental ferredoxin can substitute for bovine adrenodoxin in reactions reconstituted with bovine adrenal enzymes which catalyze the side chain cleavage of cholesterol to pregnenolone and the 11 beta-hydroxylation of deoxycorticosterone to corticosterone." citations,ref_8,4566,202610,9,,reference citation,,,1332711,,"Uhlmann, H., Beckert, V., Schwarz, D. and Bernhardt, R. (1992), Biochem. Biophys. Res. Commun. 188, S. 1131-1138",Expression of bovine adrenodoxin in E. coli and site-directed mutagenesis of /2 Fe-2S/ cluster ligands.,published,journal,Biochem. Biophys. Res. Commun.,Biochemical and biophysical research communications,188,3,,0006-291X,,,,,,,,,,,,,,,,,,,,1131,1138,1992,"Expression systems for adrenodoxin into the periplasm and the cytoplasm of E. coli have been developed as a prerequisite for site-directed mutagenesis studies. In both systems the /2Fe-2S/ cluster of the protein was correctly assembled, the cytoplasmic one gives, however, a tenfold higher expression level. To determine which of the five cysteines at positions 46, 52, 55, 92, and 95 coordinate the /2Fe-2S/ center, they have been individually mutated into serines. From these mutants, only C95S forms a functionally active holoprotein. Thus, residues 46, 52, 55, and 92 are the cysteines that coordinate the /2Fe-2S/ cluster in adrenodoxin." citations,ref_9,4566,202611,10,,reference citation,,,9551550,,"Muller, A., Muller, J.J., Muller, Y.A., Uhlmann, H., Bernhardt, R. and Heinemann, U. (1998), Structure 6, S. 269-280","New aspects of electron transfer revealed by the crystal structure of a truncated bovine adrenodoxin, Adx(4-108).",published,journal,Structure,"Structure (London, England : 1993)",6,3,,0969-2126,,,,,,,,,,,,,,,,,,,,269,280,1998,"BACKGROUND: Adrenodoxin (Adx) is a [2Fe-2S] ferredoxin involved in steroid hormone biosynthesis in the adrenal gland mitochondrial matrix of mammals. Adx is a small soluble protein that transfers electrons from adrenodoxin reductase (AR) to different cytochrome P450 isoforms where they are consumed in hydroxylation reactions. A crystallographic study of Adx is expected to reveal the structural basis for an important electron transfer reaction mediated by a vertebrate [2Fe-2S] ferredoxin. RESULTS: The crystal structure of a truncated bovine adrenodoxin, Adx(4-108), was determined at 1.85 A resolution and refined to a crystallographic R value of 0.195. The structure was determined using multiple wavelength anomalous dispersion phasing techniques, making use of the iron atoms in the [2Fe-2S] cluster of the protein. The protein displays the compact (alpha + beta) fold typical for [2Fe-2S] ferredoxins. The polypeptide chain is organized into a large core domain and a smaller interaction domain which comprises 35 residues, including all those previously determined to be involved in binding to AR and cytochrome P450. A small interdomain motion is observed as a structural difference between the two independent molecules in the asymmetric unit of the crystal. Charged residues of Adx(4-108) are clustered to yield a strikingly asymmetric electric potential of the protein molecule. CONCLUSIONS: The crystal structure of Adx(4-108) provides the first detailed description of a vertebrate [2Fe-2S] ferredoxin and serves to explain a large body of biochemical studies in terms of a three-dimensional structure. The structure suggests how a change in the redox state of the [2Fe-2S] cluster may be coupled to a domain motion of the protein. It seems likely that the clearly asymmetric charge distribution on the surface of Adx(4-108) and the resulting strong molecular dipole are involved in electrostatic steering of the interactions with AR and cytochrome P450." citations,ref_10,4566,202612,11,,reference citation,,,8589602,,"Wishart,David S., Bigam,Colin G., Yo,Jian, Abildgaard,Frits ,H. Dyson, H. Jane , Eric Oldfield, Markley,John L., and Sykes,Brian D. (1995), J. of. Biomolecular NMR 6, 135-140","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,citation_1,5647,229390,2,,reference citation,,,12522297,,,Random Coil Proton Chemical Shifts of Deoxyribonucleic Acids,published,journal,J. Biomol. NMR,,24,4,,,,,,,,,,,,,,,,,,,,,,329,337,2002, citations,entry_citation,4573,202763,1,,entry citation,,,,,,"NMR Assignment and Secondary Structure Determination of an Octameric 110 kDa Protein Using TROSY in Triple Resonance Experiments",published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,122,,,,,,,,,,,,,,,,,,,,,,,7543,7548,2000, citations,ref1,4573,202764,2,,reference citation,,,8019132,,"Wishart DS, Sykes BD. The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data. J Biomol NMR. 1994 Mar;4(2):171-80.",The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,4,2,,0925-2738,,,,,,,,,,,,,,,,,,,,171,180,1994,"A simple technique for identifying protein secondary structures through the analysis of backbone 13C chemical shifts is described. It is based on the Chemical-Shift Index [Wishart et al. (1992) Biochemistry, 31, 1647-1651] which was originally developed for the analysis of 1H(alpha) chemical shifts. By extending the Chemical-Shift Index to include 13C(alpha), 13C(beta) and carbonyl 13C chemical shifts, it is now possible to use four independent chemical-shift measurements to identify and locate protein secondary structures. It is shown that by combining both 1H and 13C chemical-shift indices to produce a 'consensus' estimate of secondary structure, it is possible to achieve a predictive accuracy in excess of 92%. This suggests that the secondary structure of peptides and proteins can be accurately obtained from 1H and 13C chemical shifts, without recourse to NOE measurements." citations,entry_citation,4574,202778,1,,entry citation,,20084446,,,"Lugovskoy, A.A., Zhou, P., Chou, J.J., McCarty, J.S., Li, P., and Wagner, G., ""Solution Structure of the CIDE-N Domain of CIDE-B and a Model for CIDE-N/CIDE-N Interactions in the DNA Fragmentation Pathway of Apoptosis,"" Cell 99, 747-755 (1999).","Solution Structure of the CIDE-N Domain of CIDE-B and a Model for CIDE-N/CIDE-N Interactions in the DNA Fragmenttion Pathway of Apoptosis",published,journal,Cell,Cell,99,7,,,,,,,,,,,,,,,,,,,,,,747,755,1999, citations,entry_citation,4575,202796,1,,entry citation,,20285168,,,"Klaus, W., Ross, A., Gsell, B., and Senn, H., ""Letter to the Editor: Backbone Resonance Assignment of the N-terminal 24 kDa Fragment of the Gyrase B Subunit from S. aureus Complexed with Novobiocin,"" J. Biomol. NMR 16, 357-358 (2000).","Letter to the Editor: Backbone Resonance Assignment of the N-terminal 24 kDa Fragment of the Gyrase B Subunit from S. aureus Complexed with Novobiocin",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,16,,,,,,,,,,,,,,,,,,,,,,,357,358,2000, citations,entry_citation,4576,202819,1,,entry citation,,,,,,Hydration of [d(CGC)r(aaa)d(TTTGCG)]2,in press,journal,J. Mol. Biol.,Journal of Molecular Biology,,na,,,,,,,,,,,,,,,,,,,,,,,,2000, citations,entry_citation,4577,202838,1,,entry citation,,98372722,,,,"The solution structure of ribosomal protein S4 delta41 reveals two subdomains and a positively charged surface that may interact with RNA.",published,journal,EMBO J.,,17,,,,,,,,,,,,,,,,,,,,,,,4559,4571,1998, citations,refined_structure,4577,202839,2,,reference citation,,,10493882,,Journal of Molecular Biology (1999) 292: 375-387,Refining the overall structure and subdomain orientation of ribosomal protein S4 delta41 with dipolar couplings measured by NMR in uniaxial liquid crystalline phases.,published,journal,J. Mol. Biol.,Journal of molecular biology,292,2,,0022-2836,,,,,,,,,,,,,,,,,,,,375,387,1999,"Prokaryotic protein S4 initiates assembly of the small ribosomal subunit by binding to 16 S rRNA. Residues 43-200 of S4 from Bacillus stearothermophilus (S4 Delta41) bind to both 16 S rRNA and to a mRNA pseudoknot. In order to obtain structure-based insights regarding RNA binding, we previously determined the solution structure of S4 Delta41 using NOE, hydrogen bond, and torsion angle restraints. S4 Delta41 is elongated, with two distinct subdomains, one all helical, the other including a beta-sheet. In contrast to the high resolution structures obtained for each individual subdomain, their relative orientation was not precisely defined because only 17 intersubdomain NOE restraints were determined. Compared to the 1.7 A crystal structure, when the sheet-containing subdomains are superimposed, the helical subdomain is twisted by almost 45 degrees about the long axis of the molecule in the solution structure. Because variations in subdomain orientation may explain how the protein recognizes multiple RNA targets, our current goal is to determine the orientation of the subdomains in solution with high precision. To this end, NOE assignments were re-examined. NOESY experiments on a specifically labeled sample revealed that one of the intersubdomain restraints had been misassigned. However, the revised set of NOE restraints produces solution structures that still have imprecisely defined subdomain orientations and that lie between the original NMR structure and the crystal structure. In contrast, augmenting the NOE restraints with N-H dipolar couplings, measured in uniaxial liquid crystalline phases, clearly establishes the relative orientation of the subdomains. Data obtained from two independent liquid crystalline milieux, DMPC/DHPC bicelles and the filamentous bacteriophage Pf1, show that the relative orientation of the subdomains in solution is quite similar to the subdomain orientation in the crystal structure. The solution structure, refined with dipolar data, is presented and its implications for S4's RNA binding activity are discussed." citations,entry_citation,4578,202880,1,,entry citation,,,10918067,,,"Selected Mutations in a Mesophilic Cytochrome c Confer the Stability of a Thermophilic Counterpart",published,journal,J. Biol. Chem.,,275,,,,,,,,,,,,,,,,,,,,,,,37824,37828,2000, citations,entry_citation,4579,202909,1,,entry citation,,,,,,"Letter to the Editor: Sequence-specific 1H, 15N and 13C resonance assignments of the EEA1 FYVE domain",published,journal,J. Biomol. NMR,,17,1,,,,,,,,,,,,,,,,,,,,,,89,90,2000, citations,entry_citation,458,202943,1,,entry citation,,,,,"Weaver, Arthur J., Kemple, Marvin D., Prendergast, Franklyn G., ""Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy,"" Biochemistry 28, 8614-8623 (1989).","Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,8614,8623,1989, citations,entry_citation,4580,202957,1,,entry citation,,,,,,"Letter to the Editor: Backbone 1H, 13C, and 15N resonance assignments of the anti-dansyl antibody Fv fragment",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,17,4,,,,,,,,,,,,,,,,,,,,,,357,358,2000, citations,entry_citation,4581,202980,1,,entry citation,,20165185,,,,Site-site Communication in the EF-hand Ca2+ Binding Protein Calbindin D9k,published,journal,Nat. Struct. Biol.,Nature Structural Biology,7,,,,,,,,,,,,,,,,,,,,,,,245,250,2000, citations,entry_citation,4598,203287,1,,entry citation,,99303984,10360942,,,"Cystic Fibrosis Transmembrane Conductance Regulator: Solution Structures of Peptides Based on the Phe508 Region, the Most Common Site of Disease-Causing DeltaF508 Mutation",published,journal,Biochemistry,,38,,,,,,,,,,,,,,,,,,,,,,,7453,7461,1999, citations,entry_citation,4599,203305,1,,entry citation,,99303702,,,,"High-Resolution Solution Structure of the 18 kDa Substrate-Binding Domain of the Mammalian Chaperone Protein Hsc70",published,journal,J. Mol. Biol.,,289,,,,,,,,,,,,,,,,,,,,,,,1387,1403,1999, citations,entry_citation,46,203337,1,,entry citation,,,,,"Wagner, Gerhard, Bruhwiler, Daniel, ""Toward the Complete Assignment of the Carbon Nuclear Magnetic Resonance Spectrum of the Basic Pancreatic Trypsin Inhibitor,"" Biochemistry 25 (20), 5839-5843 (1986).","Toward the Complete Assignment of the Carbon Nuclear Magnetic Resonance Spectrum of the Basic Pancreatic Trypsin Inhibitor",published,journal,Biochemistry,,25,20,,,,,,,,,,,,,,,,,,,,,,5839,5843,1986, citations,entry_citation,4760,206275,1,,entry citation,,20178341,,,,"Structural and Functional Differences of Two Toxins from the Scorpion Pandinus Imperator",published,journal,"Proteins: Struct., Funct., Genet.",,38,,,,,,,,,,,,,,,,,,,,,,,441,449,2000, citations,ref_1,4581,202981,2,,reference citation,,,7549869,,"Wimberly, B.; Thulin, E. and Chazin W.J. Protein Science (1995) 4 1045-1055",Characterization of the N-terminal half-saturated state of calbindin D9k: NMR studies of the N56A mutant.,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,4,6,,0961-8368,,,,,,,,,,,,,,,,,,,,1045,1055,1995,"Calbindin D9k is a small EF-hand protein that binds two calcium ions with positive cooperativity. The molecular basis of cooperativity for the binding pathway where the first ion binds in the N-terminal site (1) is investigated by NMR experiments on the half-saturated state of the N56A mutant, which exhibits sequential yet cooperative binding (Linse S, Chazin WJ, 1995, Protein Sci 4:1038-1044). Analysis of calcium-induced changes in chemical shifts, amide proton exchange rates, and NOEs indicates that ion binding to the N-terminal binding loop causes significant changes in conformation and/or dynamics throughout the protein. In particular, all three parameters indicate that the hydrophobic core undergoes a change in packing to a conformation very similar to the calcium-loaded state. These results are similar to those observed for the (Cd2+)1 state of the wild-type protein, a model for the complementary half-saturated state with an ion bound in the C-terminal site (II). Thus, with respect to cooperativity in either of the binding pathways, binding of the first ion drives the conformation and dynamics of the protein far toward the (Ca2+)2 state, thereby facilitating binding of the second ion. Comparison with the half-saturated state of the analogous E65Q mutant confirms that mutation of this critical bidentate calcium ligand at position 12 of the consensus EF-hand binding loop causes very significant structural perturbations. This result has important implications regarding numerous studies that have utilized mutation of this critical residue for site deactivation." citations,entry_citation,4583,203003,1,,entry citation,,20283639,10821859,,,"The structure and the characteristic DNA binding property of the C-terminal domain of the RNA polymerase alpha subunit from Thermus thermophilus",published,journal,J. Biol. Chem.,,275,21,,,,,,,,,,,,,,,,,,,,,,16057,16063,2000, citations,entry_citation,4584,203019,1,,entry citation,,21159140,11258958,,,Solution Structure of the DNA-binding Domain of TraM,published,journal,Biochemistry,Biochemistry,40,,,,,,,,,,,,,,,,,,,,,,,3370,3377,2001, citations,ref_XPLOR_upto_v3.8,4584,203020,2,,reference citation,,,,,,"X-PLOR, version 3.1: A system for X-ray crystallography and NMR",published,book,,,,,,,,"X-PLOR, version 3.1: A system for X-ray crystallography and NMR",,,,Yale University Press,New Haven,0300054025,,,,,,,,,,,,,,1992, citations,ref_NMRPipe,4584,203021,3,,reference citation,,96088118,,,"Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR. 1995 Nov;6(3):277-93.",,published,journal,J. Biomol. NMR,,6,3,,,,,,,,,,,,,,,,,,,,,,277,293,1995, citations,ref_MOLMOL,4584,203022,4,,reference citation,,96305672,,,"Koradi R, Billeter M, Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph. 1996 Feb;14(1):51-5, 29-32.",,published,journal,J Mol Graph.,,14,1,,,,,,,,,,,,,,,,,,,,,,51,55,1996, citations,ref_ANSIG,4584,203023,5,,reference citation,,94190870,,,"Kraulis PJ, Domaille PJ, Campbell-Burk SL, Van Aken T, Laue ED. Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy. Biochemistry. 1994 Mar 29;33(12):3515-31.",,published,journal,Biochemistry,,33,12,,,,,,,,,,,,,,,,,,,,,,3515,3531,1994, citations,entry_citation,4585,203048,1,,entry citation,,,,,,"Solution Structure of BmP02, a new Potassium channel Blocker from the Venom of the Chinese Scorpion Buthus martensi Karsch",published,journal,Biochemistry,Biochemistry,39,,,,,,,,,,,,,,,,,,,,,,,13669,13675,2000, citations,ref_CNS,4585,203049,2,,reference citation,,98437621,,,,"Crystallography & NMR system: A new software suite for macromolecular structure determination.",,,Acta Crystallogr D Biol Crystallogr.,,54,,,,,,,,,,,,,,,,,,,,,,,905,921,1998, citations,entry_citation,4587,203067,1,,entry citation,,,10947973,,,NMR structural determination of viscotoxin A3 from Viscum album L,published,journal,Biochem. J.,,350,,,,,,,,,,,,,,,,,,,,,,,569,577,2000, citations,entry_citation,4588,203085,1,,entry citation,,20250925,10788483,,,"Solution structure of the chitin-binding domain of Bacillus circulans WL-12 chitinase A1",published,journal,J. Biol. Chem.,,275,18,,,,,,,,,,,,,,,,,,,,,,13654,13661,2000, citations,entry_citation,4589,203113,1,,entry citation,,20534886,,,,"NMR Solution Structure of the Last Unknown Module of the Cellulosomal Scaffoldin Protein CIPC of Clostridum cellulolyticum",published,journal,J. Mol. Biol.,,304,,,,,,,,,,,,,,,,,,,,,,,201,217,2000, citations,entry_citation,459,203137,1,,entry citation,,,,,"Weaver, Arthur J., Kemple, Marvin D., Prendergast, Franklyn G., ""Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy,"" Biochemistry 28, 8614-8623 (1989).","Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,8614,8623,1989, citations,entry_citation,4590,203151,1,,entry citation,,20374512,,,,"NMR Solution Structure and Receptor Peptide Binding of the CC-CHemokine Eotaxin-2",published,journal,Biochemistry,,39,,,,,,,,,,,,,,,,,,,,,,,8382,8395,2000, citations,entry_citation,4591,203171,1,,entry citation,,98250752,,,,"Solution Structure of a Syndecan-4 Cytoplasmic Domain and Its Interaction with Phosphatidylinositol 4,5-Bisphosphate",published,journal,J. Biol. Chem.,Journal of Biological Chemistry,273,,,,,,,,,,,,,,,,,,,,,,,13022,13029,1998, citations,entry_citation,4592,203190,1,,entry citation,,98250752,,,,"Solution Structure of a Syndecan-4 Cytoplasmic Domain and Its Interaction with Phosphatidylinositol 4,5-Bisphosphate",published,journal,J. Biol. Chem.,Journal of Biological Chemistry,273,,,,,,,,,,,,,,,,,,,,,,,13022,13029,1998, citations,entry_citation,4593,203211,1,,entry citation,,20335023,,,,Structure and Self-association of the Rous Sarcoma Virus Capsid Protein,published,journal,Structure Fold Des.,,8,,,,,,,,,,,,,,,,,,,,,,,617,628,2000, citations,entry_citation,4595,203233,1,,entry citation,,99303984,10360942,,,"Cystic fibrosis transmembrane conductance regulator: solution structures of peptides based on the Phe508 region, the most common site of disease-causing DeltaF508 mutation",published,journal,Biochemistry,,38,,,,,,,,,,,,,,,,,,,,,,,7453,7461,1999, citations,entry_citation,4596,203251,1,,entry citation,,99303984,10360942,,,"Cystic fibrosis transmembrane conductance regulator: solution structures of peptides based on the Phe508 region, the most common site of disease-causing DeltaF508 mutation -- P26",published,journal,Biochemistry,,38,,,,,,,,,,,,,,,,,,,,,,,7453,7461,1999, citations,entry_citation,4597,203269,1,,entry citation,,99303984,10360942,,,"Cystic Fibrosis Transmembrane Conductance Regulator: Solution Structures of Peptides Based on the Phe508 Region, the Most Common Site of Disease-Causing DeltaF508 Mutation",published,journal,Biochemistry,,38,,,,,,,,,,,,,,,,,,,,,,,7453,7461,1999, citations,entry_citation,4610,203508,1,,entry citation,,99412426,,,,"NMR studies on truncated sequences of human telomeric DNA: observation of a novel A-tetrad",published,journal,Nucleic Acids Res.,,27,,,,,,,,,,,,,,,,,,,,,,,3836,3843,1999, citations,entry_citation,460,203350,1,,entry citation,,,,,"Weaver, Arthur J., Kemple, Marvin D., Prendergast, Franklyn G., ""Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy,"" Biochemistry 28, 8614-8623 (1989).","Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,8614,8623,1989, citations,entry_citation,4600,203364,1,,entry citation,,99043695,9827993,,,"Solution Structure and Backbone Dynamics of Mason-Pfizer Monkey Virus (MPMV) Nucleocapsid Protein",published,journal,Protein Sci.,,7,,,,,,,,,,,,,,,,,,,,,,,2265,2280,1998, citations,entry_citation,4601,203380,1,,entry citation,,20145059,,,,NMR Structure of the Channel-Former Zervamicin IIB in Isotropic Solvents,published,journal,,,,,,,,,,,,,,,,,,,,,,,,,,333,336,2000, citations,entry_citation,4602,203402,1,,entry citation,,20117684,10651812,,,"Solution structure of oxidized microsomal rabbit cytochrome b5. Factors determining the heterogeneous binding of the heme",published,journal,Eur. J. Biochem.,,267,,,,,,,,,,,,,,,,,,,,,,,755,766,2000, citations,ref_1,4602,203403,2,,reference citation,,,9367762,,"Guntert P, Mumenthaler C, Wuthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J Mol Biol. 1997 Oct 17;273(1):283-98.",Torsion angle dynamics for NMR structure calculation with the new program DYANA.,published,journal,J. Mol. Biol.,Journal of molecular biology,273,1,,0022-2836,,,,,,,,,,,,,,,,,,,,283,298,1997,"The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from distance constraints and torsion angle constraints collected by nuclear magnetic resonance (NMR) experiments performs simulated annealing by molecular dynamics in torsion angle space and uses a fast recursive algorithm to integrate the equations of motions. Torsion angle dynamics can be more efficient than molecular dynamics in Cartesian coordinate space because of the reduced number of degrees of freedom and the concomitant absence of high-frequency bond and angle vibrations, which allows for the use of longer time-steps and/or higher temperatures in the structure calculation. It also represents a significant advance over the variable target function method in torsion angle space with the REDAC strategy used by the predecessor program DIANA. DYANA computation times per accepted conformer in the ""bundle"" used to represent the NMR structure compare favorably with those of other presently available structure calculation algorithms, and are of the order of 160 seconds for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300 computer. Test calculations starting from conformers with random torsion angle values further showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures." citations,entry_citation,4603,203420,1,,entry citation,,,,,,"Biosynthesis of D-alanyl-lipoteichoic acid: the tertiary structure of apo-D-alanyl carrier protein",published,journal,Biochemistry,Biochemistry,40,,,,,,,,,,,,,,,,,,,,,,,7964,7972,2001, citations,entry_citation,4604,203439,1,,entry citation,,20177705,10712611,,,"The NMR solution structure of the ion channel peptaibol chrysospermin C bound to dodecylphosphocholine micelles",published,journal,Eur. J. Biochem.,,267,6,,,,,,,,,,,,,,,,,,,,,,1784,1794,2000, citations,ref_1,4604,203440,2,,reference citation,,,9367762,,"Guntert, P., Mumenthaler, C. and Wuthrich, K. (1997) J.Mol.Biol., 273: 283-298.",Torsion angle dynamics for NMR structure calculation with the new program DYANA.,published,journal,J. Mol. Biol.,Journal of molecular biology,273,1,,0022-2836,,,,,,,,,,,,,,,,,,,,283,298,1997,"The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from distance constraints and torsion angle constraints collected by nuclear magnetic resonance (NMR) experiments performs simulated annealing by molecular dynamics in torsion angle space and uses a fast recursive algorithm to integrate the equations of motions. Torsion angle dynamics can be more efficient than molecular dynamics in Cartesian coordinate space because of the reduced number of degrees of freedom and the concomitant absence of high-frequency bond and angle vibrations, which allows for the use of longer time-steps and/or higher temperatures in the structure calculation. It also represents a significant advance over the variable target function method in torsion angle space with the REDAC strategy used by the predecessor program DIANA. DYANA computation times per accepted conformer in the ""bundle"" used to represent the NMR structure compare favorably with those of other presently available structure calculation algorithms, and are of the order of 160 seconds for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300 computer. Test calculations starting from conformers with random torsion angle values further showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures." citations,ref_2,4604,203441,3,,reference citation,,,8914272,,"Luginbuhl, P., Guntert, P., Billeter, M. and Wuthrich, K. (1996) J. Biomol. NMR 8: 136-146.",The new program OPAL for molecular dynamics simulations and energy refinements of biological macromolecules.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,8,2,,0925-2738,,,,,,,,,,,,,,,,,,,,136,146,1996,"A new program for molecular dynamics (MD) simulation and energy refinement of biological macromolecules, OPAL, is introduced. Combined with the supporting program TRAJEC for the analysis of MD trajectories, OPAL affords high efficiency and flexibility for work with different force fields, and offers a user-friendly interface and extensive trajectory analysis capabilities. Salient features are computational speeds of up to 1.5 GFlops on vector supercomputers such as the NEC SX-3, ellipsoidal boundaries to reduce the system size for studies in explicit solvents, and natural treatment of the hydrostatic pressure. Practical applications of OPAL are illustrated with MD simulations of pure water, energy minimization of the NMR structure of the mixed disulfide of a mutant E. coli glutaredoxin with glutathione in different solvent models, and MD simulations of a small protein, pheromone Er-2, using either instantaneous or time-averaged NMR restraints, or no restraints." citations,entry_citation,4607,203462,1,,entry citation,,,,,,"Solution Structure Determination and Mutational Analysis of the Papillomavirus E6-interacting Peptide of E6AP",published,journal,Biochemistry,Biochemistry,40,,,,,,,,,,,,,,,,,,,,,,,1293,,2001, citations,entry_citation,4609,203476,1,,entry citation,,99289488,,,,"NMR observation of T-tetrads in a parallel stranded DNA quadruplex formed by Saccharomyces cerevisiae telomere sequence",published,journal,Nucleic Acids Res.,,27,,,,,,,,,,,,,,,,,,,,,,,2457,2464,1999, citations,entry_citation,461,203494,1,,entry citation,,,,,"Weaver, Arthur J., Kemple, Marvin D., Prendergast, Franklyn G., ""Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy,"" Biochemistry 28, 8614-8623 (1989).","Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,8614,8623,1989, citations,entry_citation,4612,203527,1,,entry citation,,20237111,,,,"NMR Observation of a Novel C-Tetrad in the Structure of the SV40 Repeat Sequence GGGCGG",published,journal,Biochem. Biophys. Res. Commun.,Biochemical and Biophysical Research Communications,270,,,,,,,,,,,,,,,,,,,,,,,967,971,2000, citations,entry_citation,4614,203545,1,,entry citation,,10995243,,,,"The NMR structures of r(GCAGGCGUGC)2 and determinants of stability for single guanosine-guanosine base pairs",published,journal,Biochemistry,,39,,,,,,,,,,,,,,,,,,,,,,,11748,11762,2000, citations,entry_citation,4615,203562,1,,entry citation,,21435646,11551192,,,"Solution Structure of PAFP-S: A new Knottin-type Antifungal Peptide from the seeds of Phytolacca americana",published,journal,Biochemistry,,40,37,,,,,,,,,,,,,,,,,,,,,,10973,10978,2001, citations,entry_citation,4616,203578,1,,entry citation,,20221437,,,,"The solution structure of Rhodobacter sphaeroides LH1beta reveals two helical domains separated by a more flexible region: structural consequences for the LH1 complex.",published,journal,J. Mol. Biol.,,298,,,,,,,,,,,,,,,,,,,,,,,83,94,2000, citations,entry_citation,4617,203591,1,,entry citation,,20183601,10716920,,,"Inhibitor binding induces active site stabilization of the HCV NS3 protein serine protease domain",published,journal,EMBO J.,,19,,,,,,,,,,,,,,,,,,,,,,,1195,1206,2000, citations,entry_citation,4618,203610,1,,entry citation,,20120850,10653692,,,Hydration of [d(CGC)r(aaa)d(TTTGCG)]2,published,journal,J. Mol. Biol.,,295,5,,,,,,,,,,,,,,,,,,,,,,1129,1137,2000, citations,entry_citation,4619,203623,1,,entry citation,,98035191,,,,"Solution structure of the N-terminal HHCC domain of HIV-2 integrase: a three-helix bundle stabilized by zinc",published,journal,Curr. Biol.,,7,,,,,,,,,,,,,,,,,,,,,,,739,746,1997, citations,entry_citation,462,203643,1,,entry citation,,,,,"Weaver, Arthur J., Kemple, Marvin D., Prendergast, Franklyn G., ""Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy,"" Biochemistry 28, 8614-8623 (1989).","Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,8614,8623,1989, citations,entry_citation,4620,203657,1,,entry citation,,20359708,,,,NMR structures of three single-residue variants of the human prion protein,published,journal,Proc. Natl. Acad. Sci. U. S. 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Weiskirchen R, Bister K",Suppression in transformed avian fibroblasts of a gene (crp) encoding a cysteine-rich protein containing LIM domains.,published,journal,Oncogene,Oncogene,8,9,,0950-9232,,,,,,,,,,,,,,,,,,,,2317,2324,1993,"Using cDNA subtraction and differential hybridization techniques, a cDNA library derived from normal quail embryo fibroblasts was screened for clones corresponding to genes whose expression was suppressed in v-myc-transformed, as compared with normal, quail embryo fibroblasts. One of the isolated cDNA clones corresponded to a 0.9-kb mRNA that was present in normal quail and chicken embryo fibroblasts, but was virtually absent from all transformed avian cells tested: quail embryo fibroblasts transformed by the v-myc, v-myc/v-mil or v-src oncogenes, cells derived from a methylcholanthrene-induced quail fibrosarcoma or v-myc-transformed chicken macrophages. Nucleotide sequence analysis of the original and supplementary cDNA clones indicated that the corresponding gene encodes a 194 amino acid cysteine-rich protein (M(r) 20,911). A database search revealed that the gene is the avian homolog of a human primary response gene (crp) of unknown function. Both the quail and human CRP proteins contain two copies of a cysteine-rich amino acid sequence motif (LIM) with putative zinc-binding activity that was previously identified in several proteins with presumed regulatory functions essential for cell growth or differentiation." citations,entry_citation,4683,204595,1,,entry citation,,20211393,,,"Zwahlen, C., Li, S-C., Kay, L.E., Pawson, T., and Forman-Kay, J.D., ""Multiple Modes of Peptide Recognition by the PTB Domain of the cell fate Determinant Numb,"" EMBO J. 19, 1505-1515 (2000).","Multiple Modes of Peptide Recognition by the PTB Domain of the cell fate Determinant Numb",published,journal,EMBO J.,EMBO Journal,19,7,,,,,,,,,,,,,,,,,,,,,,1505,1515,2000,"1H, 13C and 15N assigned chemical shift for the PTB domain of Numb complexed to NAK" citations,entry_citation,4773,206515,1,,entry citation,,21226873,,,,"Formation of the Single-layer Beta-sheet of Borrelia burgdorferi OspA in the Absence of the C-terminal Capping Globular Domain",published,journal,J. 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In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref-3,4664,204282,4,,reference citation,,,,,"Kraulis, P.J., J. Magn. Reson. 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Biomol. NMR,Journal of Biomolecular NMR,17,3,,,,,,,,,,,,,,,,,,,,,,271,272,2000, citations,entry_citation,4671,204387,1,,entry citation,,20513409,,,,"Sequence-specific 1H, 13C and 15N Resonance Assignments of the Major Cherry Allergen Pru a 1",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,18,1,,,,,,,,,,,,,,,,,,,,,,71,72,2000, citations,ref_1,4671,204388,2,,reference citation,,,,,"K. Schweimer, H. Sticht, J. Nerkamp, M. Boehm, M. Breitenbach, S. Vieths and P. Roesch. NMR Spectroscopy Reveals Common Structural Features of the Birch Pollen Allergen Bet v 1 and the Cherry Allergen Pru a 1 Appl. Magn. Reson. 17, 449-464 (1999).",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4673,204407,1,,entry citation,,10806391,,,,Solution structure of Ileal Lipid Binding Protein in complex with glycocholate,published,journal,Eur. J. Biochem.,European Journal of Biochemistry,267,,,,,,,,,,,,,,,,,,,,,,,2929,2938,2000, citations,ref1,4673,204408,2,,reference citation,,89008259,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4674,204428,1,,entry citation,,20473232,11017201,,,Structural Proteomics of an archaeon,published,journal,Nat. Struct. Biol.,,7,10,,,,,,,,,,,,,,,,,,,,,,903,909,2000, citations,entry_citation,4675,204442,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N resonance assignments of the DNA binding domain of the human forkhead transcription factor AFX",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,17,2,,,,,,,,,,,,,,,,,,,,,,181,182,2000, citations,ref_1,4675,204443,2,,reference citation,,,8589602,,"Wishart D.S., Bigam C.G., Yao J., Abildgaard F., Dyson H.J., Oldfield E., Markley J.L., Sykes B.D., ""1H, 13C and 15N Chemical Shift Referencing in Biomolecular NMR,"" J. Biomol. NMR, 6, 135-40 (1995)","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4676,204456,1,,entry citation,,21194686,11297422,,,"NMR Structural and Dynamic Characterization of the Acid-unfolded State of Apomyoglobin Provides Insights into the Early Events in Protein Folding",published,journal,Biochemistry,Biochemistry,40,12,,,,,,,,,,,,,,,,,,,,,,3561,3571,2001, citations,entry_citation,4677,204470,1,,entry citation,,20351465,,,,"Solution Structure of the Cysteine-rich Domain of the Escherichia coli Chaperone Protein DnaJ",published,journal,J. Mol. Biol.,Journal of Molecular Biology,300,,,,,,,,,,,,,,,,,,,,,,,805,818,2000, citations,entry_citation,4712,205143,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N chemical shift assignments of the acidic fibroblast growth factor from Notopthalmus viridescens",published,journal,J. Biomol. NMR,,17,3,,,,,,,,,,,,,,,,,,,,,,279,280,2000, citations,entry_citation,4761,206294,1,,entry citation,,,,,,"Magnetic Susceptibility Tensor and Heme Contact Shifts Determinations in the Rhodobacter capsulatus Ferricytochrome c': NMR and Magnetic Susceptibility Studies",published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,123,10,,,,,,,,,,,,,,,,,,,,,,2231,2242,2001, citations,ref_1,4677,204471,2,,reference citation,,,8520220,,Delaglio et al J. Biomol. NMR 6 277 (1995),NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref_2,4677,204472,3,,reference citation,,,,,"Johnson and Blevins J. Chem. Phys. 29, 1012 (1994)",NMRView: A computer program for the visualization and analysis of NMR data.,,,J. Chem. Phys.,,29,,,,,,,,,,,,,,,,,,,,,,,1012,1014,1994, citations,entry_citation,4678,204492,1,,entry citation,,20300897,,,"Yee, A., Booth, V., Dharamsi, A., Engel, A., Edwards, A.M., Arrowsmith, C.H., ""Solution Structure of the RNA Polymerase Subunit RPB5 from Methanobacterium thermoautotrophicum,"" Proc. Natl. Acad. Sci. U.S.A. 97, 6311-6315 (2000).","Solution Structure of the RNA Polymerase Subunit RPB5 from Methanobacterium thermoautotrophicum",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,97,,,,,,,,,,,,,,,,,,,,,,,6311,6315,2000, citations,entry_citation,4679,204507,1,,entry citation,,20414192,,,,"Letter to the Editor: 1H, 15N, 13C, and 13CO Assignments and Secondary Structure Determination of Collagenase-3 (MMP-13) Complexed with a Hydroxamic acid Inhibitor",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,17,3,,,,,,,,,,,,,,,,,,,,,,269,270,2000, citations,entry_citation,468,204523,1,,entry citation,,,,,"Weaver, Arthur J., Kemple, Marvin D., Prendergast, Franklyn G., ""Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy,"" Biochemistry 28, 8614-8623 (1989).","Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,8614,8623,1989, citations,entry_citation,4680,204537,1,,entry citation,,20304905,,,"Bateman, A., Bycroft, M., ""The Structure of a LysM Domain from E.coli Membrane- bound Lytic Murein Transglycosylase D (MltD),"" J. Mol. Biol. 299, 1113-1119 (2000).","The Structure of a LysM Domain from E.coli Membrane-bound Lytic Murein Transglycosylase D (MltD)",published,journal,J. Mol. Biol.,Journal of Molecular Biology,299,,,,,,,,,,,,,,,,,,,,,,,1113,1119,2000, citations,entry_citation,4681,204550,1,,entry citation,,99158819,10047490,,,"The structure and dynamics of rat apo-cellular retinol-binding protein II in solution: comparison with the X-ray structure",published,journal,J. Mol. Biol.,,286,,,,,,,,,,,,,,,,,,,,,,,1179,1195,1999, citations,ref_1,4681,204551,2,,reference citation,,1004749,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_2,4681,204552,3,,reference citation,,,8487303,,,Crystal structures of holo and apo-cellular retinol-binding protein II.,published,journal,J. Mol. Biol.,Journal of molecular biology,230,4,,0022-2836,,,,,,,,,,,,,,,,,,,,1247,1259,1993,"Apo and holo-cellular retinol-binding protein II have been crystallized, and their crystal structures have been determined to 2.1 A and 1.9 A respectively. The apo and holo-crystals have different but related triclinic space groups. The X-ray phases for both structures were determined using the molecular replacement method. The crystal co-ordinates were refined to an R-factor of 0.200 for apo, and 0.173 for holo-cellular retinol-binding protein II. The holo and apo-models have nearly the same tertiary structures. Cellular retinol-binding protein II consists of a ten-stranded anti-parallel beta-barrel with the ligand binding cavity within the barrel. Two alpha-helices cover the open end of the beta-barrel making it almost solvent inaccessible. A single portal large enough to admit a water molecule was observed opening into the binding cavity. Exogenously added retinol was found within the cavity of each holo-cellular retinol-binding protein II molecule. Each retinol was surrounded by both polar and non-polar residues. The hydroxyl group of the bound retinol hydrogen bonds to the amide group of glutamine 108. The overall conformation of the bound retinol was derived from the four different molecules of holo-cellular retinol-binding protein II present in the triclinic form. The four copies of bound retinol had essentially the same conformation as found in crystalline retinaldehyde." citations,entry_citation,4682,204572,1,,entry citation,,20344924,10884357,,,"Binding of retinol induces changes in rat cellular retinol-binding protein II conformation and backbone dynamics",published,journal,J. Mol. Biol.,,300,,,,,,,,,,,,,,,,,,,,,,,619,632,2000, citations,ref_1,4682,204573,2,,reference citation,,1004749,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_2,4682,204574,3,,reference citation,,,8487303,,,Crystal structures of holo and apo-cellular retinol-binding protein II.,published,journal,J. Mol. Biol.,Journal of molecular biology,230,4,,0022-2836,,,,,,,,,,,,,,,,,,,,1247,1259,1993,"Apo and holo-cellular retinol-binding protein II have been crystallized, and their crystal structures have been determined to 2.1 A and 1.9 A respectively. The apo and holo-crystals have different but related triclinic space groups. The X-ray phases for both structures were determined using the molecular replacement method. The crystal co-ordinates were refined to an R-factor of 0.200 for apo, and 0.173 for holo-cellular retinol-binding protein II. The holo and apo-models have nearly the same tertiary structures. Cellular retinol-binding protein II consists of a ten-stranded anti-parallel beta-barrel with the ligand binding cavity within the barrel. Two alpha-helices cover the open end of the beta-barrel making it almost solvent inaccessible. A single portal large enough to admit a water molecule was observed opening into the binding cavity. Exogenously added retinol was found within the cavity of each holo-cellular retinol-binding protein II molecule. Each retinol was surrounded by both polar and non-polar residues. The hydroxyl group of the bound retinol hydrogen bonds to the amide group of glutamine 108. The overall conformation of the bound retinol was derived from the four different molecules of holo-cellular retinol-binding protein II present in the triclinic form. The four copies of bound retinol had essentially the same conformation as found in crystalline retinaldehyde." citations,entry_citation,4737,205656,1,,entry citation,,,,,,The Structure of the Transcriptional Antiterminator NusB from Escherichia Coli,published,journal,Nat. Struct. Biol.,,7,6,,,,,,,,,,,,,,,,,,,,,,470,474,2000, citations,ref_1,4683,204596,2,,reference citation,,,8520220,,"F. Delaglio, S. Grzesiek, G.W. Vuister, G. Zhu, J. Pfeifer, A. Bax J. Biolmol. NMR, 6, 277-293 (1995)",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref_2,4683,204597,3,,reference citation,,9846878,,,"B. A. Johnson, R.A. Blevins, J. Biolmol. NMR, 4, 603-614 (1994)",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4684,204615,1,,entry citation,,22744254,12859185,,,"Structural Consequences of Metallothionein Dimerization: Solution Structure of the Isolated Cd4-alpha Domain and Comparison with the Holoprotein Dimer",published,journal,Biochemistry,Biochemistry,42,28,,,,,,,,,,,,,,,,,,,,,,8403,8410,2003, citations,entry_citation,4685,204633,1,,entry citation,,,,,,"Discovery and characterization of a family of insecticidal neurotoxins with a rare vicinal disulfide bridge",submitted,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4686,204648,1,,entry citation,,20281327,10821677,,,"Human CC Chemokine I-309, Structural Consequences of the Additional Disulfide Bond.",published,journal,Biochemistry,,39,20,,,,,,,,,,,,,,,,,,,,,,6053,6059,2000, citations,entry_citation,4687,204663,1,,entry citation,,,,,,"NMR structure of two cyclic oligonucleotides. A monomer-dimer equlilibrium between dumbbell and quadruplex structures.",published,journal,J. Am. Chem. Soc.,,120,9,,,,,,,,,,,,,,,,,,,,,,2176,2177,1998, citations,entry_citation,4688,204681,1,,entry citation,,,,,,"Letter to the Editor: Assignment and secondary structure identification of the ribosomal protein L18 from Thermus thermophilus",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,17,3,,,,,,,,,,,,,,,,,,,,,,273,274,2000, citations,entry_citation,4689,204697,1,,entry citation,,22050830,12054815,,,"NMR Studies of the Backbone Flexibility and Structure of Human Growth Hormone: A Comparison of high and low pH Conformations",published,journal,J. Mol. Biol.,,318,3,,,,,,,,,,,,,,,,,,,,,,679,695,2002, citations,entry_citation,469,204726,1,,entry citation,,,,,"Weaver, Arthur J., Kemple, Marvin D., Prendergast, Franklyn G., ""Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy,"" Biochemistry 28, 8614-8623 (1989).","Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,8614,8623,1989, citations,entry_citation,4692,204740,1,,entry citation,,20328604,10860727,,,"The solution structure and internal motions of a fragment of the cytidine-rich strand of the human telomere",published,journal,J. Mol. Biol.,,299,,,,,,,,,,,,,,,,,,,,,,,123,144,2000, citations,entry_citation,4694,204759,1,,entry citation,,,,,,"NMR structure of two cyclic oligonucleotides. A monomer-dimer equlilibrium between dumbbell and quadruplex structures.",published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,120,9,,,,,,,,,,,,,,,,,,,,,,2176,2177,1998, citations,entry_citation,4695,204777,1,,entry citation,,,10985768,,,"Changes in the apomyoglobin folding pathway caused by mutation of the distal histidine residue",published,journal,Biochemistry,Biochemistry,39,37,,,,,,,,,,,,,,,,,,,,,,11227,11237,2000, citations,entry_citation,4696,204794,1,,entry citation,,,,,,"A NEW FOLD IN THE SCORPION TOXIN FAMILY, ASSOCIATED WITH AN ACTIVITY ON RYANODINE-SENSITIVE CALCIUM CHANNEL",in press,journal,Proteins,Proteins,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4697,204807,1,,entry citation,,20237627,,,,"Structure of the fMet-tRNA(fMet)-binding domain of B. stearothermophilus initiation factor IF2",published,journal,EMBO J.,,19,8,,,,,,,,,,,,,,,,,,,,,,1918,1926,2000, citations,entry_citation,4698,204824,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C, and 15N backbone assignments of the ligand binding domain of TGFb type II receptor",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,17,4,,,,,,,,,,,,,,,,,,,,,,349,350,2000, citations,reference_1,4698,204825,2,,reference citation,,94220749,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,reference_2,4698,204826,3,,reference citation,,93044345,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4699,204844,1,,entry citation,,,,,,"The transmembrane domains of hepatitis C virus envelope glycoproteins E1 and E2 play a major role in heterodimerisation",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,470,204858,1,,entry citation,,,,,"Weaver, Arthur J., Kemple, Marvin D., Prendergast, Franklyn G., ""Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy,"" Biochemistry 28, 8614-8623 (1989).","Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,8614,8623,1989, citations,entry_citation,4700,204872,1,,entry citation,,20264518,,,"Morreale, A., Venkatesan, M., Mott, H.R., Owen, D., Nietlispach, D., Lowe, P.N., and Laue, E.D., ""Structure of Cdc42 bound to the GTPase Binding Domain of PAK,"" Nat. Struct. Biol. 7, 384-388 (2000).",Structure of Cdc42 bound to the GTPase Binding Domain of PAK,published,journal,Nat. Struct. Biol.,Nature Structural Biology,7,,,,,,,,,,,,,,,,,,,,,,,384,388,2000, citations,entry_citation,4701,204893,1,,entry citation,,,,,,"Tumor suppressor INK4: refinement of p16/INK4A structure and determination of p15/INK4B structure by comparative modeling and NMR data",in press,journal,Protein Sci.,Protein Science,,,,,,,,,,,,,,,,,,,,,,,,,,2000, citations,entry_citation,4702,204915,1,,entry citation,,20336897,,,,Structure of the Negative Regulatory Domain of p53 bound to S100B,published,journal,Nat. Struct. Biol.,Nature Structural Biology,7,,,,,,,,,,,,,,,,,,,,,,,570,574,2000, citations,entry_citation,4703,204939,1,,entry citation,,21359412,11373289,,,"NMR Solution Structure of Murine CCL20/MIP-3alpha, a Chemokine that Specifically Chemoattracts Immature Dendritic cells and Lymphocytes through its highly Specific Interaction with the Beta-chemokine Receptor CCR6",published,journal,J. Biol. Chem.,,276,30,,,,,,,,,,,,,,,,,,,,,,28372,28379,2001, citations,ref_1,4703,204940,2,,reference citation,,,9862452,,"FEBS Lett. (1998) 440, 188-194","Molecular cloning, functional characterization and mRNA expression analysis of the murine chemokine receptor CCR6 and its specific ligand MIP-3alpha.",published,journal,FEBS Lett.,FEBS letters,440,1-2,,0014-5793,,,,,,,,,,,,,,,,,,,,188,194,1998,"We have cloned the murine CCR6 receptor and its ligand, the beta-chemokine mMIP-3alpha. Calcium mobilization assays performed with mCCR6 transfectants showed significant responses upon addition of mMIP-3alpha. Murine MIP-3alpha RNA is expressed in thymus, small intestine and colon, whereas mCCR6 RNA is expressed in spleen and lymph nodes. RT-PCR analysis of FACS-sorted lymphoid and antigen presenting cell subsets showed mCCR6 expression mainly in B cells, CD8- splenic dendritic cells and CD4+ T cells. The cloning and functional characterization of the mCCR6 and mMIP-3alpha will allow the study of the role of these proteins in mouse models of inflammation and immunity." citations,ref_2,4703,204941,3,,reference citation,,,10577517,,"J. Leukoc. Biol. (1999) 66, 837-844",Down-regulation of the beta-chemokine receptor CCR6 in dendritic cells mediated by TNF-alpha and IL-4.,published,journal,J. Leukoc. Biol.,Journal of leukocyte biology,66,5,,0741-5400,,,,,,,,,,,,,,,,,,,,837,844,1999,"Chemokines are involved in the control of dendritic cell (DC) trafficking, which is critical for the immune response. We have generated DC from human umbilical cord blood CD34+ progenitors cultured with granulocyte-macrophage colony-stimulating factor, tumor necrosis factor alpha (TNF-alpha), and stem cell factor. Using an anti-CCR6 monoclonal antibody, we observed that these cells showed maximum expression of this beta-chemokine receptor when they were immature, as determined by their relatively low expression of several DC maturation markers such as CD1a, CD11c, CD14, CD40, CD80, and CD83. Immature DC responded strongly to macrophage inflammatory protein-3alpha (MIP-3alpha), the CCR6 ligand, in migration and calcium mobilization assays. CCR6 expression decreased in parallel with the DC maturation induced by prolonged TNF-alphaq treatments. Interleukin-4 was also able to decrease CCR6 protein levels. Our findings suggest that the MIP-3alpha/CCR6 interaction plays an important role in the trafficking of immature DC to chemokine production sites such as injured or inflamed peripheral tissues, where DC undergo maturation on contact with antigens." citations,entry_citation,4704,204958,1,,entry citation,,,,,,"Analysis of the dynamic properties of Bacillus circulans xylanase upon formation of a covalent glycosyl-enzyme intermediate",published,journal,Protein Sci.,Protein Science,9,,,,,,,,,,,,,,,,,,,,,,,512,524,2000, citations,ref_1,4704,204959,2,,reference citation,,,8762143,,,Secondary structure and NMR assignments of Bacillus circulans xylanase.,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,5,6,,0961-8368,,,,,,,,,,,,,,,,,,,,1118,1135,1996,"Bacillus circulans xylanase (BCX) is a member of the family of low molecular weight endo-beta-(1,4)-xylanases. The main-chain 1H, 13C, and 15N resonances of this 20.4-kDa enzyme were assigned using heteronuclear NMR experiments recorded on a combination of selectively and uniformly labeled protein samples. Using chemical shift, NOE, J coupling, and amide hydrogen exchange information, 14 beta-strands, arranged in a network of three beta-sheets, and a single alpha-helix were identified in BCX. The NMR-derived secondary structure and beta-sheet topology agree closely with that observed in the crystal structure of this protein. The HN of Ile 118 has a strongly upfield-shifted resonance at 4.03 ppm, indicative of a potential amide-aromatic hydrogen bond to the indole ring of Trp 71. This interaction, which is conserved in all low molecular weight xylanases of known structure, may play an important role in establishing the active site conformation of these enzymes. Following hen egg white and bacteriophage T4 lysozymes, B. circulans xylanase represents the third family of beta-glycanases for which extensive NMR assignments have been reported. These assignments provide the background for detailed studies of the mechanism of carbohydrate recognition and hydrolysis by this bacterial xylanase." citations,entry_citation,4706,204975,1,,entry citation,,20170870,,,,"Structure and Binding Specificity of the Second N-Terminal Cellulose-Binding Domain from Cellulomonas fimi Endoglucanase C",published,journal,Biochemistry,Biochemistry,39,10,,,,,,,,,,,,,,,,,,,,,,2445,2458,2000, citations,entry_citation,4707,204999,1,,entry citation,,,,,,"Alternative Splicing of Wilms' Tumor Suppressor Protein Modulates DNA Binding Activity Through Isoform-Specific DNA-Induced Conformational Changes",in press,journal,Biochemistry,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,2000,"amide 1H and 15N, and backbone 13Ca chemical shifts of free and DNA-bound WT1 of two alternative splice forms are compared""" citations,wt1_ref_1,4707,205000,2,,reference citation,,90304885,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,wt1_ref_2,4707,205001,3,,reference citation,,90158822,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4708,205026,1,,entry citation,,,,,,"Alternative Splicing of Wilms' Tumor Suppressor Protein Modulates DNA Binding Activity Through Isoform-Specific DNA-Induced Conformational Changes",in press,journal,Biochemistry,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,2000,"amide 1H and 15N, and backbone 13Ca chemical shifts of free and DNA-bound WT1 of two alternative splice forms are compared""" citations,wt1_ref_1,4708,205027,2,,reference citation,,90304885,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,wt1_ref_2,4708,205028,3,,reference citation,,90158822,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4709,205055,1,,entry citation,,,,,,"Alternative Splicing of Wilms' Tumor Suppressor Protein Modulates DNA Binding Activity Through Isoform-Specific DNA-Induced Conformational Changes",in press,journal,Biochemistry,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,2000,"amide 1H and 15N, and backbone 13Ca chemical shifts of free and DNA-bound WT1 of two alternative splice forms are compared""" citations,wt1_ref_1,4709,205056,2,,reference citation,,90304885,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,wt1_ref_2,4709,205057,3,,reference citation,,90158822,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,471,205082,1,,entry citation,,,,,"Weaver, Arthur J., Kemple, Marvin D., Prendergast, Franklyn G., ""Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy,"" Biochemistry 28, 8614-8623 (1989).","Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,8614,8623,1989, citations,entry_citation,4710,205096,1,,entry citation,,,,,,"Alternative Splicing of Wilms' Tumor Suppressor Protein Modulates DNA Binding Activity Through Isoform-Specific DNA-Induced Conformational Changes",in press,journal,Biochemistry,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,2000,"amide 1H and 15N, and backbone 13Ca chemical shifts of free and DNA-bound WT1 of two alternative splice forms are compared""" citations,wt1_ref_1,4710,205097,2,,reference citation,,90304885,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,wt1_ref_2,4710,205098,3,,reference citation,,90158822,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4711,205125,1,,entry citation,,,,,,"Letter to the Editor: NMR backbone assignments of the cold-regulated RNA-binding protein, RbpA1, in the cyanobacterium, Anabaena variabilis M3",published,journal,J. Biomol. NMR,,17,4,,,,,,,,,,,,,,,,,,,,,,351,352,2000, citations,Ref_2,4712,205144,2,,reference citation,,,9086327,,"Growth Factors 1997;14(1):39-57 Amphibian FGF-1 is structurally and functionally similar to but antigenically distinguishable from its mammalian counterpart. Patrie K, Botelho MJ, Ray SK, Mehta VB, Chiu IM",Amphibian FGF-1 is structurally and functionally similar to but antigenically distinguishable from its mammalian counterpart.,published,journal,Growth Factors,"Growth factors (Chur, Switzerland)",14,1,,0897-7194,,,,,,,,,,,,,,,,,,,,39,57,1997,"Recent studies have shown that fibroblast growth factors (FGF) play an important role in the diverse cellular mechanisms involved with vertebrate development. One system which has received a great deal of attention is the developing limb in part because of the extensive epithelial-mesenchymal interactions that take place during this process. Because it closely parallels the developmental process of the limb and is a model for wound repair, the phenomenon of amphibian limb regeneration has been used to investigate the role of FGF in these processes. We have recently reported on the cloning and functional characterization of an FGF receptor (FGFR) isolated from amphibian regenerative tissue. In this report, we describe the isolation and characterization of an FGF-1 molecule from the newt, Notophthalmus viridescens. Amino acid sequence comparisons indicate that the newt FGF-1 exhibits between 79 to 83% identity with FGF-1 from mammalian and avian species. The full length cDNA of the newt FGF-1 was cloned into a prokaryotic expression vector and purified from E. coli. Although the newt FGF-1 shares a high degree of primary amino acid sequence similarity with other FGF-1 molecules, the recombinant protein was not detected in a Western blot analysis using a polyclonal antibody directed against mammalian FGF-1. Despite the antigenic divergence, the newt FGF-1 was capable of binding to NIH/3T3 and Chinese hamster ovary cells overexpressing mammalian and amphibian FGFRs with dissociation constants comparable to those reported for mammalian FGF-1. Newt FGF-1 could also be cross-linked to receptors on the surface of NIH/3T3 cells. In addition, it elicits a mitogenic response in NIH/3T3 cells indistinguishable from human recombinant FGF-1." citations,entry_citation,4713,205160,1,,entry citation,,20264516,,,,Structural analysis of WW domains and design of a WW prototype,published,journal,Nat. Struct. Biol.,Nature Structural Biology,7,5,,,,,,,,,,,,,,,,,,,,,,375,379,2000, citations,entry_citation,4714,205178,1,,entry citation,,20264516,,,,Structural analysis of WW domains and design of a WW prototype,published,journal,Nat. Struct. Biol.,Nature Structural Biology,7,5,,,,,,,,,,,,,,,,,,,,,,375,379,2000, citations,entry_citation,4715,205196,1,,entry citation,,20264516,,,,Structural analysis of WW domains and design of a WW prototype,published,journal,Nat. Struct. Biol.,Nature Structural Biology,7,5,,,,,,,,,,,,,,,,,,,,,,375,379,2000, citations,entry_citation,4716,205214,1,,entry citation,,,,,,"Letter to the Editor: 1H, 15N, and 13C NMR backbone assignments and secondary structure of the C-terminal recombinant fragment of auxilin including the J-domain",published,journal,J. Biomol. NMR,,17,3,,,,,,,,,,,,,,,,,,,,,,281,282,2000, citations,entry_citation,4717,205232,1,,entry citation,,,,,,"Letter to the Editor: 1H, 15N, 13C, and 13CO assignments and secondary structure determination of ZipA*",published,journal,J. Biomol. NMR,,17,3,,,,,,,,,,,,,,,,,,,,,,275,276,2000, citations,entry_citation,4718,205246,1,,entry citation,,21127481,11224562,,,"Structure of the RTP-DNA Complex and the Mechanism of Polar Replication Fork Arrest",published,journal,Nat. Struct. Biol.,Nature Structural Biology,8,3,,,,,,,,,,,,,,,,,,,,,,206,210,2001, citations,entry_citation,4719,205267,1,,entry citation,,20513410,,,,Sequence-specific Resonance Assignment of the Ras-binding Domain of AF6,published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,18,1,,,,,,,,,,,,,,,,,,,,,,73,74,2000, citations,ref1,4719,205268,2,,reference citation,,,8703846,,"Genes Chromosomes Cancer 1996 Apr;15(4):206-16 Analysis of the t(6;11)(q27;q23) in leukemia shows a consistent breakpoint in Tanabe S, Zeleznik-Le NJ, Kobayashi H, Vignon C, Espinosa R 3rd, LeBeau MM, Thirman MJ, Rowley JD AF6 in three patients and in the ML-2 cell line.",Analysis of the t(6;11)(q27;q23) in leukemia shows a consistent breakpoint in AF6 in three patients and in the ML-2 cell line.,published,journal,Genes Chromosomes Cancer,"Genes, chromosomes & cancer",15,4,,1045-2257,,,,,,,,,,,,,,,,,,,,206,216,1996,"The t(6;11)(q27;23) is one of the most common translocations observed in patients with acute myeloid leukemia (AML). The translocation breakpoint involves the MLL gene, which is the human homolog of the Drosophila trithorax gene, at 11q23 and the AF6 gene at 6q27. Reverse transcriptase-polymerase chain reaction (RT-PCR) using an MLL sense primer and an AF6 antisense primer detected the MLL/AF6 fusion cDNA from three leukemia patients with the t(6;11) [two AML and one T-acute lymphoblastic leukemia (ALL)] and one cell line. The fusion point in the AF6 cDNA from these cases is identical, regardless of the leukemia phenotype. The ML-2 cell line, which was established from a patient with AML that developed after complete remission of T-cell lymphoma, has retained an 11q23-24 deletion from the lymphoma stage and has acquired the t(6;11) with development of AML. The ML-2 cells have no normal MLL gene on Southern blot analysis, which indicates that an intact MLL gene is not necessary for survival of leukemic cells." citations,ref2,4719,205269,3,,reference citation,,,9349501,,"Oncogene 1997 Oct 2;15(14):1681-7 Chimeric MLL products with a Ras binding cytoplasmic protein AF6 involved in t(6;11) (q27;q23) leukemia localize in the nucleus. Joh T, Yamamoto K, Kagami Y, Kakuda H, Sato T, Yamamoto T, Takahashi T, Ueda R, Kaibuchi K, Seto M",Chimeric MLL products with a Ras binding cytoplasmic protein AF6 involved in t(6;11) (q27;q23) leukemia localize in the nucleus.,published,journal,Oncogene,Oncogene,15,14,,0950-9232,,,,,,,,,,,,,,,,,,,,1681,1687,1997,"In infantile leukemias and therapy-related leukemias, the MLL gene is frequently found to be disrupted and fused to various translocation partner genes, such as AF4/FEL, LTG9/AF9 and LTG19/ENL as a result of 11q23 translocations. We previously showed that the N-terminal portion common to various chimeric MLL products, as well as to MLL-LTG9 and MLL-LTG19, localizes in the nuclei, and therefore suggested that it might play an important role in leukemogenesis. In the present study, MLL-AF6 chimeric products found in the t(6;11)(q27;q23) translocation were analysed since AF6, a Ras-binding protein, exhibits a different subcellular localization from that of LTG9/AF9 and LTG19/ENL. Immunofluorescence staining data and cell fractionation analyses demonstrated that MLL-AF6 chimeric products localize in the nuclei despite the fact that AF6 itself localizes in the cytoplasm, confirming the importance of the nuclear localization of chimeric MLL products. The region in the N-terminal portion of MLL responsible for this nuclear localization was examined and found to be a region containing AT-hook motifs." citations,ref3,4719,205270,4,,reference citation,,,10224125,,"J Biol Chem 1999 May 7;274(19):13556-62 Thermodynamic and kinetic characterization of the interaction between the Ras binding domain of AF6 and members of the Ras subfamily. Linnemann T, Geyer M, Jaitner BK, Block C, Kalbitzer HR, Wittinghofer A, Herrmann C",Thermodynamic and kinetic characterization of the interaction between the Ras binding domain of AF6 and members of the Ras subfamily.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,274,19,,0021-9258,,,,,,,,,,,,,,,,,,,,13556,13562,1999,"Cellular signaling downstream of Ras is highly diversified and may involve many different effector molecules. A potential candidate is AF6 which was originally identified as a fusion to ALL-1 in acute myeloid leukemia. In the present work the interaction between Ras and AF6 is characterized and compared with other effectors. The binding characteristics are quite similar to Raf and RalGEF, i.e. nucleotide dissociation as well as GTPase-activating protein activity are inhibited, whereas the intrinsic GTPase activity of Ras is unperturbed by AF6 binding. Particularly, the dynamics of interaction are similar to Raf and RalGEF with a lifetime of the Ras. AF6 complex in the millisecond range. As probed by 31P NMR spectroscopy one of two major conformational states of Ras is stabilized by the interaction with AF6. Looking at the affinities of AF6 to a number of Ras mutants in the effector region, a specificity profile emerges distinct from that of other effector molecules. This finding may be useful in defining the biological function of AF6 by selectively switching off other pathways downstream of Ras using the appropriate effector mutant. Notably, among the Ras-related proteins AF6 binds most tightly to Rap1A which could imply a role of Rap1A in AF6 regulation." citations,entry_citation,4754,206156,1,,entry citation,,22191392,12203008,,,"Structure of the 113Cd3 Beta Domains from Homarus americanus Metallothionein-1: Hydrogen bonding and Solvent Accessibility of Sulfur Atoms",published,journal,J. Biol. Inorg. Chem.,,7,7-8,,,,,,,,,,,,,,,,,,,,,,713,724,2002, citations,ref4,4719,205271,5,,reference citation,,,8557659,,"J Biol Chem 1996 Jan 12;271(2):607-10 Identification of AF-6 and canoe as putative targets for Ras. Kuriyama M, Harada N, Kuroda S, Yamamoto T, Nakafuku M, Iwamatsu A, Yamamoto D, Prasad R, Croce C, Canaani E, Kaibuchi K",Identification of AF-6 and canoe as putative targets for Ras.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,271,2,,0021-9258,,,,,,,,,,,,,,,,,,,,607,610,1996,"Ras (Ha-Ras, Ki-Ras, N-Ras) is implicated in the regulation of various cell functions such as gene expression and cell proliferation downstream from specific extracellular signals. Here, we partially purified a Ras-interacting protein with molecular mass of about 180 kDa (p180) from bovine brain membrane extract by glutathione S-transferase (GST)-Ha-Ras affinity column chromatography. This protein bound to the GTP gamma S (guanosine 5'-(3-O-thio)triphosphate, a nonhydrolyzable GTP analog).GST-Ha-Ras affinity column but not to those containing GDP.GST-Ha-Ras or GTP gamma S.GST-Ha-Ras with a mutation in the effector domain (Ha-RasA38). The amino acid sequences of the peptides derived from p180 were almost identical to those of human AF-6 that is identified as the fusion partner of the ALL-1 protein. The ALL-1/AF-6 chimeric protein is the critical product of the t (6:11) abnormality associated with some human leukemia. AF-6 has a GLGF/Dlg homology repeat (DHR) motif and shows a high degree of sequence similarity with Drosophila Canoe, which is assumed to function downstream from Notch in a common developmental pathway. The recombinant N-terminal domain of AF-6 and Canoe specifically interacted with GTP gamma S.GST-Ha-Ras. The known Ras target c-Raf-1 inhibited the interaction of AF-6 with GTP gamma S.GST-Ha-Ras. These results indicate that AF-6 and Canoe are putative targets for Ras." citations,entry_citation,472,205298,1,,entry citation,,,,,"Weaver, Arthur J., Kemple, Marvin D., Prendergast, Franklyn G., ""Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy,"" Biochemistry 28, 8614-8623 (1989).","Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,8614,8623,1989, citations,entry_citation,4720,205312,1,,entry citation,,20466532,,,,"Backbone 1H, 15N, and 13C Resonance Assignments of Inhibitor-2-- a Protein Inhibitor of Protein Phosphatase-1",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,17,4,,,,,,,,,,,,,,,,,,,,,,359,360,2000, citations,entry_citation,4721,205325,1,,entry citation,,20183615,,,"Okuda, M., Watanabe, Y., Okamura, H., Hanaoka, F., Ohkuma, Y., and Nishimura, Y., ""Structure of the Central Core Domain of TFIIEbeta with a Novel Double-stranded DNA-binding Surface,"" EMBO J. 19, 1346-1356 (2000).","Structure of the Central Core Domain of TFIIEbeta with a Novel Double-stranded DNA-binding Surface",published,journal,EMBO J.,EMBO Journal,19,,,,,,,,,,,,,,,,,,,,,,,1346,1356,2000, citations,entry_citation,4722,205348,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N resonance assignments of Aquifex aeolicus shikimate kinase in complex with the substrate shikimate",published,journal,J. Biomol. NMR,,17,3,,,,,,,,,,,,,,,,,,,,,,277,278,2000, citations,ref_1,4722,205349,2,,reference citation,,,10427747,,"J Biomol NMR 1999 Jun;14(2):189-90 1H, 13C and 15N resonance assignments of Escherichia coli 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase and its complex with MgAMPPCP. Shi G, Gao J, Yan H","1H, 13C and 15N resonance assignments of Escherichia coli 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase and its complex with MgAMPPCP.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,14,2,,0925-2738,,,,,,,,,,,,,,,,,,,,189,190,1999, citations,entry_citation,4723,205365,1,,entry citation,,,,,,"Involvement of Electrostatic Interactions in the Mechanism of Peptide Folding Induced by Sodium Dodecyl Sulfate Binding",submitted,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,,2000, citations,entry_citation,4724,205386,1,,entry citation,,,,,,"Involvement of Electrostatic Interactions in the Mechanism of Peptide Folding Induced by Sodium Dodecyl Sulfate Binding",submitted,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,,2000, citations,entry_citation,4725,205409,1,,entry citation,,22191392,12203008,,,"Structure of the 113Cd3 Beta Domains from Homarus americanus Metallothionein-1: Hydrogen bonding and Solvent Accessibility of Sulfur Atoms",published,journal,J. Biol. Inorg. Chem.,,7,7-8,,,,,,,,,,,,,,,,,,,,,,713,724,2002, citations,entry_citation,4726,205435,1,,entry citation,,20469488,,,"Booth, V., Koth, C.M., Edwards, A.M., and Arrowsmith, C.H., ""Structure of a Conserved Domain Common to the Transcription Factors TFIIS, elongin A, and CRSP70,"" J. Biol. Chem. 275, 31266-31268 (2000).","Structure of a Conserved Domain Common to the Transcription Factors TFIIS, elongin A, and CRSP70",published,journal,J. Biol. Chem.,Journal of Biological Chemistry,275,,,,,,,,,,,,,,,,,,,,,,,31266,31268,2000, citations,entry_citation,4727,205448,1,,entry citation,,20450712,,,,"Another piece of the Ribosome: Solution Structure of S16 and its Location in the 30S Subunit",published,journal,Structure Fold. Des.,Structure with Folding and Design,8,8,,,,,,,,,,,,,,,,,,,,,,875,882,2000, citations,entry_citation,4728,205481,1,,entry citation,,,,,,"1H, 15N and 13C assignments and secondary structure of the EGF-like module pair 3-4 from vitamin K-dependent protein S",in preparation,journal,FEBS Lett.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4729,205496,1,,entry citation,,,,,,"1H, 15N and 13C assignments and secondary structure of the EGF-like module pair 3-4 from vitamin K-dependent protein S",in preparation,journal,FEBS Lett.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,473,205525,1,,entry citation,,,,,"Weaver, Arthur J., Kemple, Marvin D., Prendergast, Franklyn G., ""Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy,"" Biochemistry 28, 8614-8623 (1989).","Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,8614,8623,1989, citations,entry_citation,4731,205539,1,,entry citation,,20365226,,,,"Letter to the Editor: Sequence-specific 1H, 13C, and 15N Assignment of the Human Melanoma Inhibitory Activity (MIA) Protein",published,journal,J. Biomol. NMR,,17,1,,,,,,,,,,,,,,,,,,,,,,87,88,2000, citations,entry_citation,4732,205552,1,,entry citation,,,,,,HMG-D complexed to a bulge DNA: an NMR study,in preparation,journal,Protein Sci.,,,,,,,,,,,,,,,,,,,,,,,,,,,2000, citations,entry_citation,4733,205572,1,,entry citation,,,,,,HMG-D complexed to a bulge DNA: an NMR study,in preparation,journal,Protein Sci.,,,,,,,,,,,,,,,,,,,,,,,,,,,2000, citations,entry_citation,4734,205594,1,,entry citation,,,,,,HMG-D complexed to a bulge DNA: an NMR study,in preparation,journal,Protein Sci.,,,,,,,,,,,,,,,,,,,,,,,,,,,2000, citations,entry_citation,4735,205618,1,,entry citation,,,,,,"Letter to the Editor: Sequence-specific NMR resonance assignments of the backbone atoms for the olfactory marker protein, OMP",published,journal,J. Biomol. NMR,,17,4,,,,,,,,,,,,,,,,,,,,,,353,354,2000, citations,entry_citation,4736,205643,1,,entry citation,,,,,,NMR structures of three single-residue variants of the human prion protein,submitted,journal,Proc. Natl. Acad. Sci. U.S.A.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,cit_1,4737,205657,2,,reference citation,,,9351000,,"Reference: A.S. Altieri et. al., FEBS Lett., 415,221-226 (1997)",Sequential assignments and secondary structure of the RNA-binding transcriptional regulator NusB.,published,journal,FEBS Lett.,FEBS letters,415,2,,0014-5793,,,,,,,,,,,,,,,,,,,,221,226,1997,"The NusB protein is involved in transcriptional regulation in bacteriophage lambda. NusB binds to the RNA form of the nut site and along with N, NusA, NusE and NusG, stabilizes the RNA polymerase transcription complex and allows stable, persistent antitermination. NusB contains a 10 residue Arg-rich RNA-binding motif (ARM) at the N-terminus but is not sequentially homologous to any other proteins. In contrast to other known ARM-containing proteins, NusB forms a stable structure in solution in the absence of RNA. NMR spectroscopy was used to determine that NusB contains six alpha-helices: R10-Q21, 127-F34, V45-L65, Q79-S93, Y100-F114 and D118-L127. The structure of NusB makes it a member of a newly emerging class of alpha-helical RNA-binding proteins." citations,cit_2,4737,205658,3,,reference citation,,,,,"Kraulis, P.J., J. Magn. Reson. 84, 627-633 (1989)",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,cit_3,4737,205659,4,,reference citation,,,8520220,,"""Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J. and Bax, A., J. Biomol. NMR, 6, 277-293 (1995)""",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,cit_4,4737,205660,5,,reference citation,,,8142349,,,Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy.,published,journal,Biochemistry,Biochemistry,33,12,,0006-2960,,,,,,,,,,,,,,,,,,,,3515,3531,1994,"A high-resolution solution structure of the GDP form of a truncated version of the ras p21 protein (residues 1-166) has been determined using NMR spectroscopy. Ras p21 is the product of the human ras protooncogene and a member of a ubiquitous eukaryotic gene family which is highly conserved in evolution. A virtually complete assignment (13C, 15N, and 1H), including stereospecific assignments of 54 C beta methylene protons and 10 C gamma methyl protons of valine residues, was obtained by analysis of three- and four-dimensional (3D and 4D) heteronuclear NMR spectra using a newly developed 3D/4D version of the ANSIG software. A total of 40 converged structures were computed from 3369 experimental restraints consisting of 3,167 nuclear Overhauser effect (NOE) derived distances, 14 phi and 54 chi 1 torsion angle restraints, 109 hydrogen bond distance restraints, and an additional 25 restraints derived from literature data defining interactions between the GDP ligand, the magnesium ion, and the protein. The structure in the region of residues 58-66 (loop L4), and to a lesser degree residues 30-38 (loop L2), is ill-defined. Analysis of the dynamics of the backbone 15N nuclei in the protein showed that residues within the regions 58-66, 107-109, and, to a lesser degree, 30-38 are dynamically mobile on the nanosecond time scale. The root mean square (rms) deviations between the 40 solution structures and the mean atomic coordinates are 0.78 A for the backbone heavy atoms and 1.29 A for all non-hydrogen atoms if all residues (1-166) are included in the analysis. If residues 30-38 and residues 58-66 are excluded from the analysis, the rms deviations are reduced to 0.55 and 1.00 A, respectively. The structure was compared to the most highly refined X-ray crystal structure of ras p21.GDP (1-189) [Milburn, M. V., Tong, L., de Vos, A. M., Brunger, A. T., Yamaizumi, Z., Nishimura, S., & Kim, S.-H. (1990) Science 24, 939-945]. The structures are very similar except in the regions found to be mobile by NMR spectroscopy. In addition, the second alpha-helix (helix-2) has a slightly different orientation. The rms deviation between the average of the solution structures and the X-ray crystal structure is 0.94 A for the backbone heavy atoms if residues 31-37 and residues 59-73 are excluded from the analysis." citations,entry_citation,4738,205690,1,,entry citation,,,,,,"Determination by High Field NMR Spectroscopy of the Longitudinal Electron Relaxation Rate in Cu(II)Plastocyanin from Anabaena variablis.",published,journal,J. Am. Chem. Soc.,,122,,,,,,,,,,,,,,,,,,,,,,,7823,7824,2000, citations,entry_citation,4739,205710,1,,entry citation,,20351256,,,"Theret, I., Baladi, S., Cox, J.A., Sakamoto, H., and Craescu, C.T., ""Sequential Calcium Binding to the Regulatory Domain of Calcium Vector Protein Reveals Functional Asymmetry and a Novel Mode of Structural Rearrangement,"" Biochemistry 39, 7920-7926 (2000).","Sequential Calcium Binding to the Regulatory Domain of Calcium Vector Protein Reveals Functional Asymmetry and a Novel Mode of Structural Rearrangement",published,journal,Biochemistry,Biochemistry,39,27,,,,,,,,,,,,,,,,,,,,,,7920,7926,2000, citations,entry_citation,474,205734,1,,entry citation,,,,,"Weaver, Arthur J., Kemple, Marvin D., Prendergast, Franklyn G., ""Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy,"" Biochemistry 28, 8614-8623 (1989).","Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,8614,8623,1989, citations,entry_citation,4740,205748,1,,entry citation,,,11017201,,,Structural proteomics of an archaeon,published,journal,Nat. Struct. Biol.,,7,10,,,,,,,,,,,,,,,,,,,,,,903,909,2000, citations,entry_citation,4741,205774,1,,entry citation,,,,,,Structure and folding of Glucagon-like Peptide 1-7-(7-36)-amide in aqueous trifluoroethanol studied by NMR,published,journal,Magn. Reson. Chem.,,39,,,,,,,,,,,,,,,,,,,,,,,477,483,2001, citations,entry_citation,4755,206180,1,,entry citation,,21025439,,,,"Solution Structure of hpTX2, a Toxin from Heteropoda venatoria Spider that blocks Kv4.2 Potassium Channel",published,journal,Protein Sci.,Protein Science,9,,,,,,,,,,,,,,,,,,,,,,,2059,2067,2000, citations,entry_citation,4757,206193,1,,entry citation,,20541363,,,,"Biochemical and Structural Analysis of the Interaction Between the UBA(2) Domain of the DNA Repair Protein HHR23A and HIV-1 Vpr",published,journal,Biochemistry,Biochemistry,39,,,,,,,,,,,,,,,,,,,,,,,14103,14112,2000, citations,cit_1,4757,206194,2,,reference citation,,,,,"Bartels, C. et al. (1995) J. Biomol. NMR 6, 1-10",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4758,206224,1,,entry citation,,20566721,11114251,,,"NMR Structure of Streptomyces Killer Toxin-like Protein, SKLP: Further Evidence for the Wide Distribution of Single-domain Betagamma-crystallin Superfamily Proteins",published,journal,J. Mol. Biol.,Journal of Molecular Biology,305,1,,,,,,,,,,,,,,,,,,,,,,109,120,2001, citations,entry_citation,4759,206239,1,,entry citation,,,,,,"Backbone 1H, 15N and 13Calpha assigned chemical shifts for reduced Escherichia coli cytochrome b56",in preparation,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,2000, citations,re_1,4741,205775,2,,reference citation,,,11943215,,"Xiaoqing Chang, Danielle Keller, Se?n I.O'Donoghue and Jens J. Led. ""NMR studies of the aggregation of glucagon-like peptide-1: formation of a symmetric helical dimer."" FEBS Letters 515, 165-170 (2002).",NMR studies of the aggregation of glucagon-like peptide-1: formation of a symmetric helical dimer.,published,journal,FEBS Lett.,FEBS letters,515,1-3,,0014-5793,,,,,,,,,,,,,,,,,,,,165,170,2002,"Nuclear magnetic resonance (NMR) spectroscopy reveals that higher-order aggregates of glucagon-like peptide-1-(7-36)-amide (GLP-1) in pure water at pH 2.5 are disrupted by 35% 2,2,2-trifluoroethanol (TFE), and form a stable and highly symmetric helical self-aggregate. NMR spectra show that the helical structure is identical to that formed by monomeric GLP-1 under the same experimental conditions [Chang et al., Magn. Reson. Chem. 37 (2001) 477-483; Protein Data Bank at RCSB code: 1D0R], while amide proton exchange rates reveal a dramatic increase of the stability of the helices of the self-aggregate. Pulsed-field gradient NMR diffusion experiments show that the TFE-induced helical self-aggregate is a dimer. The experimental data and model calculations indicate that the dimer is a parallel coiled coil, with a few hydrophobic residues on the surface that may cause aggregation in pure water. The results suggest that the coiled coil dimer is an intermediate state towards the formation of higher aggregates, e.g. fibrils." citations,entry_citation,4742,205809,1,,entry citation,,20250925,,,,"Solution Structure of the Chitin-Binding Domain of Bacillus circulans WL-12 Chitinase A1",published,journal,J. Biol. Chem.,,275,18,,,,,,,,,,,,,,,,,,,,,,13654,13661,2000, citations,ref_1,4742,205810,2,,reference citation,,,10788483,,,Solution structure of the chitin-binding domain of Bacillus circulans WL-12 chitinase A1.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,275,18,,0021-9258,,,,,,,,,,,,,,,,,,,,13654,13661,2000,"The three-dimensional structure of the chitin-binding domain (ChBD) of chitinase A1 (ChiA1) from a Gram-positive bacterium, Bacillus circulans WL-12, was determined by means of multidimensional heteronuclear NMR methods. ChiA1 is a glycosidase that hydrolyzes chitin and is composed of an N-terminal catalytic domain, two fibronectin type III-like domains, and C-terminal ChBD(ChiA1) (45 residues, Ala(655)-Gln(699)), which binds specifically to insoluble chitin. ChBD(ChiA1) has a compact and globular structure with the topology of a twisted beta-sandwich. This domain contains two antiparallel beta-sheets, one composed of three strands and the other of two strands. The core region formed by the hydrophobic and aromatic residues makes the overall structure rigid and compact. The overall topology of ChBD(ChiA1) is similar to that of the cellulose-binding domain (CBD) of Erwinia chrysanthemi endoglucanase Z (CBD(EGZ)). However, ChBD(ChiA1) lacks the three aromatic residues aligned linearly and exposed to the solvent, which probably interact with cellulose in CBDs. Therefore, the binding mechanism of a group of ChBDs including ChBD(ChiA1) may be different from that proposed for CBDs." citations,entry_citation,4743,205838,1,,entry citation,,10561607,,,,"A proton-NMR investigation of the fully reduced cytochrome c7 from Desulfuromonas acetoxidans. Comparison between the reduced and the oxidized forms.",published,journal,Eur. J. Biochem.,,266,,,,,,,,,,,,,,,,,,,,,,,634,643,1999, citations,ref_1,4743,205839,2,,reference citation,,,10561607,,,A proton-NMR investigation of the fully reduced cytochrome c7 from Desulfuromonas acetoxidans. Comparison between the reduced and the oxidized forms.,published,journal,Eur. J. Biochem.,European journal of biochemistry / FEBS,266,2,,0014-2956,,,,,,,,,,,,,,,,,,,,634,643,1999,"The solution structure via 1H NMR of the fully reduced form of cytochrome c7 has been obtained. The protein sample was kept reduced by addition of catalytic amounts of Desulfovibrio gigas iron hydrogenase in H2 atmosphere after it had been checked that the presence of the hydrogenase did not affect the NMR spectrum. A final family of 35 conformers with rmsd values with respect to the mean structure of 8.7 +/- 1.5 nm and 12.4 +/- 1.3 nm for the backbone and heavy atoms, respectively, was obtained. A highly disordered loop involving residues 54-61 is present. If this loop is ignored, the rmsd values are 6.2 +/- 1.1 nm and 10.2 +/- 1.0 nm for the backbone and heavy atoms, respectively, which represent a reasonable resolution. The structure was analyzed and compared with the already available structure of the fully oxidized protein. Within the indetermination of the two solution structures, the result for the two redox forms is quite similar, confirming the special structural features of the three-heme cluster. A useful comparison can be made with the available crystal structures of cytochromes c3, which appear to be highly homologous except for the presence of a further heme. Finally, an analysis of the factors affecting the reduction potentials of the heme irons was performed, revealing the importance of net charges in differentiating the reduction potential when the other parameters are kept constant." citations,entry_citation,4744,205867,1,,entry citation,,98430963,9760163,,,"800 MHz 1H NMR solution structure refinement of oxidized cytochrome c7 from Desulfuromonas acetoxidans",published,journal,Eur. J. Biochem.,,256,,,,,,,,,,,,,,,,,,,,,,,261,270,1998, citations,ref_1,4744,205868,2,,reference citation,,,9760163,,,800 MHz 1H NMR solution structure refinement of oxidized cytochrome c7 from Desulfuromonas acetoxidans.,published,journal,Eur. J. Biochem.,European journal of biochemistry / FEBS,256,2,,0014-2956,,,,,,,,,,,,,,,,,,,,261,270,1998,"The solution structure of Desulfuromonas acetoxidans cytochrome c7 has been refined by using 1H-NMR spectra recorded at 800 MHz and by using pseudocontact shifts in the final energy minimization procedure. The protein, composed of 68 amino acids, contains three paramagnetic heme moieties, each with one unpaired electron. The largely distributed paramagnetism broadens the lines in several protein parts. The structure is now relatively well resolved all over the backbone by the use of 1315 meaningful NOEs and 90 pseudocontact shifts. The statistical analysis of the structure indicates its satisfactory quality. The protein-fold is quite similar to that of the analogous four-heme cytochromes c3 for those parts which can be considered homologous. The solvent accessibility and the electrostatic potential surfaces surrounding the three hemes have been analyzed in terms of their reduction potentials. The resulting magnetic susceptibility anisotropy data obtained from pseudocontact shifts are analyzed in terms of structural data." citations,entry_citation,4745,205888,1,,entry citation,,20366237,,,,"Solution Conformation of a Bulged Adenosine in an RNA Duplex by Relaxation Matrix Refinement",published,journal,J. Mol. Biol.,Journal of Molecular Biology,300,,,,,,,,,,,,,,,,,,,,,,,1143,1154,2000, citations,entry_citation,4746,205904,1,,entry citation,,20264310,10801486,,,"A high-resolution structure of a DNA-chromomycin-Co(II) complex determined from pseudocontact shifts in nuclear magnetic resonance",published,journal,Structure Fold. Des.,,8,4,,,,,,,,,,,,,,,,,,,,,,441,452,2000, citations,entry_citation,476,206262,1,,entry citation,,,,,"Mayo, Kevin H., Burke, Carl, Lindon, J.N., Kloczewiak, Marek A., ""1H NMR Sequential Assignments and Secondary Structure Analysis of Human Fibrinogen gamma-Chain C-Terminal Residues 385-411,"" Biochemistry 29, 3277-3286 (1990).","1H NMR Sequential Assignments and Secondary Structure Analysis of Human Fibrinogen gamma-Chain C-Terminal Residues 385-411",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,3277,3286,1990, citations,ref_1,4746,205905,2,,reference citation,,,17917690,,"Tu, K. and Gochin, M., J. AM. CHEM. SOC. 1999, v121, 9276-85",Structure determination by restrained molecular dynamics using NMR pseudocontact shifts as experimentally determined constraints.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,121,40,,0002-7863,,,,,,,,,,,,,,,,,,,,9276,9285,1999,"The structure of a DNA octamer d(TTGGCCAA)(2) complexed to chromomycin-A(3) and a single divalent cobalt ion has been solved by using the pseudocontact shifts due to the unpaired electrons on the cobalt. A protocol was developed and critically evaluated for using the pseudocontact shifts in structure determination. The pseudocontact shifts were input as experimental restraints in molecular dynamics simulations with or without NOE constraints. Both the magnitude and orientation of the susceptibility anisotropy tensor required for the shift calculations were determined during the simulations by iterative refinement. The pseudocontact shifts could be used to define the structure to a very high precision and accuracy compared with a corresponding NOE-determined structure. Convergence was obtained from different starting structures and tensors. A structure determination using both NOE's and pseudocontact shifts revealed a general agreement between the two data sets. However, some evidence for a discrepancy between NOE's and pseudocontact shifts was observed in the backbone and terminal base pairs of the DNA. Violations in shift or NOE restraints remaining in the final structures were examined and may be a reflection of motional averaging of the constraints and evidence for flexibility. This work demonstrates that pseudocontact shifts are a powerful tool for NMR structure determination." citations,entry_citation,4747,205933,1,,entry citation,,20513405,11061227,,,"Random coil chemical shifts in acidic 8 M urea: implementation of random coil shift data in NMRView",published,journal,J. Biomol. NMR,,18,,,,,,,,,,,,,,,,,,,,,,,43,48,2000, citations,entry_citation,4748,205990,1,,entry citation,,,,,,"Three-Dimensional Solution Structure of Oryzacystatin-I, a Cysteine Proteinase Inhibitor of the Rice, Oryza sativa L. japonica",published,journal,Biochemistry,Biochemistry,39,,,,,,,,,,,,,,,,,,,,,,,14753,14760,2000, citations,entry_citation,4749,206022,1,,entry citation,,99410888,,,,"Hybrid-Hybrid matrix structural refinement of a DNA three-way junction from 3D NOESY-NOES",published,journal,J. Biomol. NMR,,14,,,,,,,,,,,,,,,,,,,,,,,209,221,1999, citations,ref1,4749,206023,2,,reference citation,,,10481274,,"J. Biomolecular NMR, (1999), 14: 209-221",Hybrid-hybrid matrix structural refinement of a DNA three-way junction from 3D NOESY-NOESY.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,14,3,,0925-2738,,,,,,,,,,,,,,,,,,,,209,221,1999,"Homonuclear 3D NOESY-NOESY has shown great promise for the structural refinement of large biomolecules. A computationally efficient hybrid-hybrid relaxation matrix refinement methodology, using 3D NOESY-NOESY data, was used to refine the structure of a DNA three-way junction having two unpaired bases at the branch point of the junction. The NMR data and the relaxation matrix refinement confirm that the DNA three-way junction exists in a folded conformation with two of the helical stems stacked upon each other. The third unstacked stem extends away from the junction, forming an acute angle (approximately 60 degrees) with the stacked stems. The two unpaired bases are stacked upon each other and are exposed to the solvent. Helical parameters for the bases in all three strands show slight deviations from typical values expected for right-handed B-form DNA. Inter-nucleotide imino-imino NOEs between the bases at the branch point of the junction show that the junction region is well defined. The helical stems show mobility (+/- 20 degrees) indicating dynamic processes around the junction region. The unstacked helical stem adjacent to the unpaired bases shows greater mobility compared to the other two stems. The results from this study indicate that the 3D hybrid-hybrid matrix MORASS refinement methodology, by combining the spectral dispersion of 3D NOESY-NOESY and the computational efficiency of 2D refinement programs, provides an accurate and robust means for structure determination of large biomolecules. Our results also indicate that the 3D MORASS method gives higher quality structures compared to the 2D complete relaxation matrix refinement method." citations,entry_citation,475,206043,1,,entry citation,,,,,"Weaver, Arthur J., Kemple, Marvin D., Prendergast, Franklyn G., ""Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy,"" Biochemistry 28, 8614-8623 (1989).","Characterization of Selectively 13C-Labeled Synthetic Melittin and Melittin Analogues in Isotropic Solvents by Circular Dichroism, Fluorescence, and NMR Spectroscopy",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,8614,8623,1989, citations,entry_citation,4750,206057,1,,entry citation,,99332051,,,,Structure of the Most Conserved internal loop in Srp RNA,published,journal,Nat. Struct. Biol.,,6,,,,,,,,,,,,,,,,,,,,,,,634,638,1999, citations,entry_citation,4751,206076,1,,entry citation,,,,,,"Letter to the Editor: Assignment of 1H and 15N resonances of mouse lysozyme M",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,18,4,,,,,,,,,,,,,,,,,,,,,,361,362,2000, citations,entry_citation,4752,206091,1,,entry citation,,,,,,"Letter to the Editor: Assignment of the 1H, 13C, and 15N resonances of the DNA binding domain of gpNu1, a genome packaging protein from bacteriophage l",published,journal,J. Biomol. NMR,,18,1,,,,,,,,,,,,,,,,,,,,,,69,70,2000, citations,entry_citation,4753,206127,1,,entry citation,,20264310,10801486,,,"A High Resolution Structure of a DNA-chromomycin-Co (II) Complex Determined from Pseudocontact Shifts in Nuclear Magnetic Resonance",published,journal,Structure Fold. Des.,,8,4,,,,,,,,,,,,,,,,,,,,,,441,452,2000, citations,ref_1,4753,206128,2,,reference citation,,,17917690,,"Tu, K. and Gochin, M., J. AM. CHEM. SOC. 1999, v121, 9276-85",Structure determination by restrained molecular dynamics using NMR pseudocontact shifts as experimentally determined constraints.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,121,40,,0002-7863,,,,,,,,,,,,,,,,,,,,9276,9285,1999,"The structure of a DNA octamer d(TTGGCCAA)(2) complexed to chromomycin-A(3) and a single divalent cobalt ion has been solved by using the pseudocontact shifts due to the unpaired electrons on the cobalt. A protocol was developed and critically evaluated for using the pseudocontact shifts in structure determination. The pseudocontact shifts were input as experimental restraints in molecular dynamics simulations with or without NOE constraints. Both the magnitude and orientation of the susceptibility anisotropy tensor required for the shift calculations were determined during the simulations by iterative refinement. The pseudocontact shifts could be used to define the structure to a very high precision and accuracy compared with a corresponding NOE-determined structure. Convergence was obtained from different starting structures and tensors. A structure determination using both NOE's and pseudocontact shifts revealed a general agreement between the two data sets. However, some evidence for a discrepancy between NOE's and pseudocontact shifts was observed in the backbone and terminal base pairs of the DNA. Violations in shift or NOE restraints remaining in the final structures were examined and may be a reflection of motional averaging of the constraints and evidence for flexibility. This work demonstrates that pseudocontact shifts are a powerful tool for NMR structure determination." citations,ref_1,4762,206310,2,,reference citation,,,7827089,,"Volkman BF, Nohaile MJ, Amy NK, Kustu S, Wemmer DE. Three-dimensional solution structure of the N-terminal receiver domain of NTRC. Biochemistry. 1995 Jan 31;34(4):1413-24.",Three-dimensional solution structure of the N-terminal receiver domain of NTRC.,published,journal,Biochemistry,Biochemistry,34,4,,0006-2960,,,,,,,,,,,,,,,,,,,,1413,1424,1995,"NTRC is a transcriptional enhancer binding protein whose N-terminal domain is a member of the family of receiver domains of two-component regulatory systems. Using 3D and 4D NMR spectroscopy, we have completed the 1H, 15N, and 13C assignments and determined the solution structure of the N-terminal receiver domain of the NTRC protein. Determination of the three-dimensional structure was carried out with the program X-PLOR (Brunger, 1992) using a total of 915 NMR-derived distance and dihedral angle restraints. The resultant family of structures has an average root mean square deviation of 0.81 A from the average structure for the backbone atoms involved in well-defined secondary structure. The structure is comprised of five alpha-helices and a five-stranded parallel beta-sheet, in a (beta/alpha)5 topology. Comparison of the solution structure of the NTRC receiver domain with the crystal structures of the homologous protein CheY in both the Mg(2+)-free and Mg(2+)-bound forms [Stock, A.M., Mottonen, J. M., Stock, J. B., & Schutt, C. E. (1989) Nature 337, 745-749; Volz, K., & Matsumura, P. (1991) J. Biol. Chem. 296, 15511-15519; Stock, A. M., Martinez-Hackert, E., Rasmussen, B. F., West, A. H., Stock, J. B., Ringe, D., & Petsko, G. A. (1993) Biochemistry 32, 13375-13380; Bellsolell, L., Prieto, J., Serrano, L., & Coll, M. (1994) J. Mol. Biol. 238, 489-495] reveals a very similar fold, with the only significant difference occurring in the positioning of helix 4 relative to the rest of the protein. Examination of the conformation of consensus residues of the receiver domain superfamily [Volz, K. (1993) Biochemistry 32, 11741-11753] in the structures of the NTRC receiver domain and CheY establishes the structural importance of residues whose side chains are involved in hydrogen bonding or hydrophobic core interactions. The importance of some nonconsensus residues which may be conserved for their ability to fulfill helix capping roles is also discussed." citations,entry_citation,4763,206330,1,,entry citation,,,,,,Two-state allosteric behavior in a single domain signaling protein,published,journal,Science,,291,,,,,,,,,,,,,,,,,,,,,,,2429,2433,2001, citations,ref_1,4763,206331,2,,reference citation,,,7827089,,"Volkman BF, Nohaile MJ, Amy NK, Kustu S, Wemmer DE. Three-dimensional solution structure of the N-terminal receiver domain of NTRC. Biochemistry. 1995 Jan 31;34(4):1413-24.",Three-dimensional solution structure of the N-terminal receiver domain of NTRC.,published,journal,Biochemistry,Biochemistry,34,4,,0006-2960,,,,,,,,,,,,,,,,,,,,1413,1424,1995,"NTRC is a transcriptional enhancer binding protein whose N-terminal domain is a member of the family of receiver domains of two-component regulatory systems. Using 3D and 4D NMR spectroscopy, we have completed the 1H, 15N, and 13C assignments and determined the solution structure of the N-terminal receiver domain of the NTRC protein. Determination of the three-dimensional structure was carried out with the program X-PLOR (Brunger, 1992) using a total of 915 NMR-derived distance and dihedral angle restraints. The resultant family of structures has an average root mean square deviation of 0.81 A from the average structure for the backbone atoms involved in well-defined secondary structure. The structure is comprised of five alpha-helices and a five-stranded parallel beta-sheet, in a (beta/alpha)5 topology. Comparison of the solution structure of the NTRC receiver domain with the crystal structures of the homologous protein CheY in both the Mg(2+)-free and Mg(2+)-bound forms [Stock, A.M., Mottonen, J. M., Stock, J. B., & Schutt, C. E. (1989) Nature 337, 745-749; Volz, K., & Matsumura, P. (1991) J. Biol. Chem. 296, 15511-15519; Stock, A. M., Martinez-Hackert, E., Rasmussen, B. F., West, A. H., Stock, J. B., Ringe, D., & Petsko, G. A. (1993) Biochemistry 32, 13375-13380; Bellsolell, L., Prieto, J., Serrano, L., & Coll, M. (1994) J. Mol. Biol. 238, 489-495] reveals a very similar fold, with the only significant difference occurring in the positioning of helix 4 relative to the rest of the protein. Examination of the conformation of consensus residues of the receiver domain superfamily [Volz, K. (1993) Biochemistry 32, 11741-11753] in the structures of the NTRC receiver domain and CheY establishes the structural importance of residues whose side chains are involved in hydrogen bonding or hydrophobic core interactions. The importance of some nonconsensus residues which may be conserved for their ability to fulfill helix capping roles is also discussed." citations,entry_citation,4765,206351,1,,entry citation,,,,,,"Letter to the Editor: Backbone 1H, 13C, and 15N resonance assignments of an 18.2 kDa protein, E. coli peptidyl-prolyl cis-trans isomerase b (EPPIb)",published,journal,J. Biomol. NMR,,18,1,,,,,,,,,,,,,,,,,,,,,,75,76,2000, citations,entry_citation,4766,206370,1,,entry citation,,,,,,"Letter to the Editor: Assignments of the 1H, 13C, and 15N resonances of the 21 kDa Vesl/Homer family protein, Vesl-1S",published,journal,J. Biomol. NMR,,18,2,,,,,,,,,,,,,,,,,,,,,,181,182,2000, citations,entry_citation,4767,206394,1,,entry citation,,21966000,11969411,,,"The C terminus of apocytochrome b562 undergoes fast motions and slow exchange among ordered conformations resembling the folded state",published,journal,Biochemistry,,41,17,,,,,,,,,,,,,,,,,,,,,,5505,5514,2002, citations,entry_citation,4768,206413,1,,entry citation,,20425097,,,,"NMR Solution Structure of hPar14 Reveals Similarity to the Peptidyl Prolyl cis/tans Isomerase Domain of the Mitotic Regulator hPin1 but Indicates a Different Functionality of the Protein",published,journal,J. Mol. Biol.,Journal of Molecular Biology,301,4,,,,,,,,,,,,,,,,,,,,,,1003,1017,2000, citations,entry_citation,4769,206429,1,,entry citation,,21040563,11200526,,,"Identification of the Ubiquitin Interfacial Residues in a Ubiquitin-E2 Covalent Complex",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,18,4,,,,,,,,,,,,,,,,,,,,,,319,327,2000, citations,entry_citation,477,206446,1,,entry citation,,,,,"Mayo, Kevin H., Burke, Carl, Lindon, J.N., Kloczewiak, Marek A., ""1H NMR Sequential Assignments and Secondary Structure Analysis of Human Fibrinogen gamma-Chain C-Terminal Residues 385-411,"" Biochemistry 29, 3277-3286 (1990).","1H NMR Sequential Assignments and Secondary Structure Analysis of Human Fibrinogen gamma-Chain C-Terminal Residues 385-411",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,3277,3286,1990, citations,entry_citation,4770,206459,1,,entry citation,,,,,,"Efficient expression of isotopically labeled peptides for high resolution NMR studies: Application to the Cdc42/Rac binding domains of virulent kinases in Candida albicans",published,journal,J. Biomol. NMR,,26,4,,,,,,,,,,,,,,,,,,,,,,317,326,2003, citations,entry_citation,4771,206478,1,,entry citation,,,,,,"Letter to the Editor: Assignment of the 1H, 15N and 13C resonances of the C-terminal domain of the TolA protein of Escherichia coli, involved in cell envelope integrity",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,18,2,,,,,,,,,,,,,,,,,,,,,,179,180,2000, citations,entry_citation,4772,206493,1,,entry citation,,,,,,"Letter to the Editor: Resonance assignments for the N-terminal domain from human RNA-binding protein with multiple splicing (RBP-MS)",published,journal,J. Biomol. NMR,,19,3,,,,,,,,,,,,,,,,,,,,,,285,286,2001, citations,cit_1,4772,206494,2,,reference citation,,,,,"Zimmerman et al, (1997) J. Mol. Biol., 269:592-610",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_1,4772,206495,3,,reference citation,,,,,"Shimamoto A, Kitao S, Ichikawa K, Suzuki N, Yamabe Y, Imamura O, Tokutake Y, Satoh M, Matsumoto T, Kuromitsu J, Kataoka H, Sugawara K, Sugawara M, Sugimoto M, Goto M, Furuichi Y., A unique human gene that spans over 230 kb in the human chromosome 8p11-12 and codes multiple family proteins sharing RNA-binding motifs. Proc Natl Acad Sci U S A. 1996 Oct 1,93(20):10913-7. PMID: 8855282, UI: 97008106",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_2,4772,206496,4,,reference citation,,,,,"Sahasrabudhe PV, Tejero R, Kitao S, Furuichi Y, Montelione GT. ,Homology modeling of an RNP domain from a human RNA-binding protein: Homology-constrained energy optimization provides a criterion for distinguishing potential sequence alignments. Proteins. 1998 Dec 1,33(4):558-66. PMID: 9849939, UI: 99065191",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4774,206532,1,,entry citation,,21099332,11168402,,,"Three-dimensional Structure of the Histidine-containing Phosphocarrier Protein (Hpr) from Enterococcus faecalis in Solution",published,journal,Eur. J. Biochem.,European Journal of Biochemistry,268,3,,,,,,,,,,,,,,,,,,,,,,635,644,2001, citations,ref_2,4774,206533,2,,reference citation,,,8421502,,"Jia Z, Vandonselaar M, Quail JW, Delbaere LT., Active-centre torsion-angle strain revealed in 1.6 A-resolution structure of histidine-containing phosphocarrier protein. Nature. 1993 Jan 7;361(6407):94-7. PMID: 8421502; UI: 93133294",Active-centre torsion-angle strain revealed in 1.6 A-resolution structure of histidine-containing phosphocarrier protein.,published,journal,Nature,Nature,361,6407,,0028-0836,,,,,,,,,,,,,,,,,,,,94,97,1993,"The histidine-containing phosphocarrier protein (HPr) is a central component of the phosphoenolpyruvate: sugar phosphotransferase system that transports carbohydrates across the cell membrane of bacteria. A typical phosphotransfer sequence is phosphoenolpyruvate-->enzyme I-->HPr-->enzyme II/IIIsugar-->sugar. This is thermodynamically favourable owing to the participation of the high-energy phosphoenolpyruvate. We report here the structure of HPr from Streptococcus faecalis determined at 1.6 A resolution. Remarkable disallowed Ramachandran torsion angles at the active centre, revealed by the X-ray structure, demonstrate a unique example of torsion-angle strain that is probably directly involved in protein function. During phosphorylation, the active-centre torsion-angle strain should facilitate the phosphotransfer reaction by lowering the activation-energy barrier. A recently reported Bacillus subtilis HPr structure, which represents the phosphorylated state of HPr with no torsion-angle strain, provides direct evidence supporting our hypothesis that torsion-angle strain plays a direct part in the function of HPr. An HPr phosphotransfer cycling mechanism is proposed, based primarily on the structures of HPr and other phosphotransferase system proteins." citations,ref_3,4774,206534,3,,reference citation,,,9523711,,"Hahmann M, Maurer T, Lorenz M, Hengstenberg W, Glaser S, Kalbitzer HR., Structural studies of histidine-containing phosphocarrier protein from Enterococcus faecalis. Eur J Biochem. 1998 Feb 15;252(1):51-8. PMID: 9523711; UI: 98181885",Structural studies of histidine-containing phosphocarrier protein from Enterococcus faecalis.,published,journal,Eur. J. Biochem.,European journal of biochemistry / FEBS,252,1,,0014-2956,,,,,,,,,,,,,,,,,,,,51,58,1998,"Based on the complete sequential assignment of the 1H-NMR spectrum by multidimensional NMR techniques the secondary structure and the local geometry of the active site of histidine-containing phosphocarrier protein (HPr) from Enterococcus faecalis were elucidated. We present a comparative analysis of the active site in the seven known structures of HPr from different organisms determined by NMR or X-ray crystallography. In catalysis, HPr is phosphorylated at the ring N61 of His15. No general agreement exists in literature regarding the structure of the active-centre loop. In the crystal structure of HPr from E. faecalis, a torsion strain of the backbone at position 16 was observed, which was assumed to be important to the catalytic mechanism. Coupling constants were determined in order to calculate phi angles to establish whether there are strained torsion angles in HPr from E. faecalis in the solution state. The evaluation of data obtained indicate a stable and well-defined structure of HPr from E. faecalis, with an overall fold similar to that found in HPr from other bacteria. We find that in the active-site region there are relatively large variations in local geometry between the evaluated structures. In HPr from E. faecalis, a particularly detailed view of the phosphate-binding His15 and residues in close spatial proximity was obtained by determination of coupling constants obtained from the double-quantum-filtered COSY spectrum. Our data indicate that in aqueous solution, in the dominant conformational state there is no torsion strain of the backbone at position 16, as observed in the crystal state. The maximum population of a strained conformation in solution can be estimated to be smaller than 23%. The analysis of the data suggests that the active-centre loop is able to adopt different conformations in solution. A similar observation was made for HPr from E. faecalis phosphorylated at its regulatory site (Ser46). 31P-NMR shows that phosphorylated HPr exists in two conformational substates with nearly equal populations." citations,ref_4,4774,206535,4,,reference citation,,,8126724,,"Jia Z, Vandonselaar M, Hengstenberg W, Quail JW, Delbaere LT., The 1.6 A structure of histidine-containing phosphotransfer protein HPr from Streptococcus faecalis. J Mol Biol. 1994 Mar 11;236(5):1341-55. PMID: 8126724; UI: 94172632",The 1.6 A structure of histidine-containing phosphotransfer protein HPr from Streptococcus faecalis.,published,journal,J. Mol. Biol.,Journal of molecular biology,236,5,,0022-2836,,,,,,,,,,,,,,,,,,,,1341,1355,1994,"The histidine-containing phosphocarrier protein (HPr) is a central component of the phosphoenolpyruvate: sugar phosphotransferase system (PTS) that transports carbohydrates across the cell membrane of bacteria. The three-dimensional structure of Gram-positive Streptococcus faecalis HPr has been determined using the method of multiple isomorphous replacement. The R factor for all data is 0.156 for S. faecalis HPr at 1.6 A resolution with very good geometry. The overall folding topology of HPr is a classical open-faced beta-sandwich, consisting of four antiparallel beta-strands and three alpha-helices. Remarkable disallowed Ramachandran torsion angles of Ala16 at the active center, revealed by the X-ray structure of S. faecalis HPr, demonstrate a unique example of torsion-angle strain that is likely involved directly in protein function. A brief report concerning the torsion-angle strain has been presented recently. A newly-determined pH 7.0 structure is shown to have the same open conformation of the active center and the same torsion-angle strain at Ala16, suggesting that pH is not responsible for the structural observations. The current structure suggests a role for residues 12 and 51 in HPr's function, since they are involved in the active center through direct and indirect hydrogen-bonding interactions with the imidazole ring of His15. It is found that Ser46, the regulatory site in HPr from Gram-positive bacteria, N-caps the minor alpha-B helix and is also involved in the Asn43-Ser46 beta-turn. This finding, in conjunction with the proposed routes of communication between the regulatory site Ser46 and the active center in S. faecalis HPr, provides new insight into the understanding of how Ser46 might function. The putative involvement of the C-terminal alpha-carboxyl group and the related Gly67-Glu70 reverse beta-turn with respect to the function of HPr are described." citations,ref_5,4774,206536,5,,reference citation,,,9367762,,"GUNTERT, P., MUMENTHALER, C. & WUTHRICH, K. (1997). Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273, 283-298.",Torsion angle dynamics for NMR structure calculation with the new program DYANA.,published,journal,J. Mol. Biol.,Journal of molecular biology,273,1,,0022-2836,,,,,,,,,,,,,,,,,,,,283,298,1997,"The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from distance constraints and torsion angle constraints collected by nuclear magnetic resonance (NMR) experiments performs simulated annealing by molecular dynamics in torsion angle space and uses a fast recursive algorithm to integrate the equations of motions. Torsion angle dynamics can be more efficient than molecular dynamics in Cartesian coordinate space because of the reduced number of degrees of freedom and the concomitant absence of high-frequency bond and angle vibrations, which allows for the use of longer time-steps and/or higher temperatures in the structure calculation. It also represents a significant advance over the variable target function method in torsion angle space with the REDAC strategy used by the predecessor program DIANA. DYANA computation times per accepted conformer in the ""bundle"" used to represent the NMR structure compare favorably with those of other presently available structure calculation algorithms, and are of the order of 160 seconds for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300 computer. Test calculations starting from conformers with random torsion angle values further showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures." citations,entry_citation,4775,206556,1,,entry citation,,20165182,10700282,,,"Structure of the Mad2 spindle assembly checkpoint protein and its interaction with Cdc20",published,journal,Nat. Struct. Biol.,,7,3,,,,,,,,,,,,,,,,,,,,,,224,229,2000, citations,entry_citation,4777,206581,1,,entry citation,,21040570,,,,"Complete 1H, 15N and 13C Assignment of the Functional Domain of Paracoccus denitrificans Cytochrome c552 in the Oxidized state",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,18,4,,,,,,,,,,,,,,,,,,,,,,365,366,2000, citations,ref_1,4777,206582,2,,reference citation,,,10826890,,"Pristovsek, P., Luecke, C., Reincke, B., Loehr, F., Ludwig, B. & Rueterjans, H. (2000). Complete 1H, 15N and 13C assignment of the functional domain of Paracoccus denitrificans cytochrome c552 in the reduced state. J. Biomol. NMR 16, 353-354","Complete 1H, 15N and 13C assignment of the functional domain of paracoccus denitrificans cytochrome c552 in the reduced state.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,16,4,,0925-2738,,,,,,,,,,,,,,,,,,,,353,354,2000, citations,ref_2,4777,206583,3,,reference citation,,,10216157,,"Reincke, B., Thoeny-Meyer, L., Dannehl, C., Odenwald, A., Aidim, M., Witt, H., Rueterjans, H. & Ludwig, B. (1999) Heterologous expression of soluble fragments of cytochrome c552 acting as electron donor to the Paracoccus denitrificans cytochrome c oxidase. Biochim. Biophys. Acta, 1441, 114-120",Heterologous expression of soluble fragments of cytochrome c552 acting as electron donor to the Paracoccus denitrificans cytochrome c oxidase.,published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1411,1,,0006-3002,,,,,,,,,,,,,,,,,,,,114,120,1999,"A membrane-bound c-type cytochrome, c552, acts as the electron mediator between the cytochrome bc1 complex and cytochrome c oxidase in the branched respiratory chain of the bacterium Paracoccus denitrificans. Unlike in mitochondria where a soluble cytochrome c interacts with both complexes, the bacterial c552, the product of the cycM gene, shows a tripartite structure, with an N-terminal membrane anchor separated from a typical class I cytochrome domain by a highly charged region. Two derivative fragments, lacking either only the membrane spanning region or both N-terminal domains, were constructed on the genetic level, and expressed in Escherichia coli cotransformed with the ccm gene cluster encoding host-specific cytochrome c maturation factors. High levels of cytochromes c were expressed and located in the periplasm as holo-proteins; both these purified c552 fragments are functional in electron transport to oxidase, as ascertained by kinetic measurements, and will prove useful for future structural studies of complex formation by NMR and X-ray diffraction." citations,ref_3,4777,206584,4,,reference citation,,,7628479,,"Turba, A., Jetzek, M. & Ludwig, B. (1995) Purification of Paracoccus denitrificans cytochrome c552 and sequence analysis of the gene. Eur. J. Biochem., 231, 259-265",Purification of Paracoccus denitrificans cytochrome c552 and sequence analysis of the gene.,published,journal,Eur. J. Biochem.,European journal of biochemistry / FEBS,231,1,,0014-2956,,,,,,,,,,,,,,,,,,,,259,265,1995,"Unlike mitochondria, many bacteria use a large repertoire of c-type cytochromes in different branches of their electron transport system. Among the many cytochromes c present in the soil bacterium Paracoccus denitrificans, a membrane-bound cytochrome (c552) has been suggested to mediate the electron transport between the cytochrome bc1 complex and cytochrome-c oxidase [Berry, E. A. & Trumpower, B. L. (1985) J. Biol. Chem. 260, 2458-2467]. We have purified this cytochrome from cytoplasmic membranes, and cloned and sequenced its gene, cycM. Sequence analysis reveals that, while its C-terminal portion is highly similar to type-I cytochromes c, its N-terminal part contains a hydrophobic segment providing membrane attachment. In addition, we present immunological evidence for its functional role in respiration." citations,entry_citation,4778,206618,1,,entry citation,,,12815258,,,"Efficient expression of isotopically labeled peptides for high resolution NMR studies: application to the Cdc42/Rac binding domains of virulent kinases in Candida albicans",published,journal,J. Biomol. NMR,,26,4,,,,,,,,,,,,,,,,,,,,,,317,326,2003, citations,entry_citation,4779,206636,1,,entry citation,,,,,,"Letter to the Editor: Sequential resonance assignments of the extracellular ligand binding domain of the human TGF-b type II receptor",published,journal,J. Biomol. NMR,,18,4,,,,,,,,,,,,,,,,,,,,,,369,370,2000, citations,entry_citation,478,206659,1,,entry citation,,,,,"Campbell-Burk, Sharon, ""Structural and Dynamic Differences between Normal and Transforming N-ras Gene Products: A 31P and Isotope-Edited 1H NMR Study,"" Biochemistry 28, 9478-9484 (1989).","Structural and Dynamic Differences between Normal and Transforming N-ras Gene Products: A 31P and Isotope-Edited 1H NMR Study",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,9478,9484,1989, citations,entry_citation,4780,206672,1,,entry citation,,20328605,10860728,,,"NMR Structure of Stem-loop SL2 of the HIV-1 Psi RNA Packaging Signal Reveals a Novel A-U-A Base-triple Platform",published,journal,J. Mol. Biol.,Journal of Molecular Biology,299,,,,,,,,,,,,,,,,,,,,,,,145,156,2000,"SL2 RNA stem loop is the major 5' splice donor site. Located in the Psi-RNA packaging signal, SL2 is also involved in nucleocapsid protein mediated RNA packaging." citations,entry_citation,4781,206700,1,,entry citation,,20328605,10860728,,,"NMR Structure of Stem-loop SL2 of the HIV-1 Psi RNA Packaging Signal Reveals a Novel A-U-A Base-triple Platform",published,journal,J. Mol. Biol.,Journal of Molecular Biology,299,,,,,,,,,,,,,,,,,,,,,,,145,156,2000,"SL2 RNA stem loop is the major 5' splice donor site. Located in the Psi-RNA packaging signal, SL2 is also involved in nucleocapsid protein mediated RNA packaging." citations,entry_citation,4782,206724,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N NMR assignments of the C-type lectin TC14",published,journal,J. Biomol. NMR,,18,3,,,,,,,,,,,,,,,,,,,,,,283,284,2000, citations,ref_1,4782,206725,2,,reference citation,,,10398588,,"Poget SF, Legge GB, Proctor MR, Butler PJ, Bycroft M, Williams RL. Protein Structure, The structure of a tunicate C-type lectin from Polyandrocarpa misakiensis complexed with D -galactose. J Mol Biol. 1999 Jul 23;290(4):867-79. PMID: 10398588; UI: 99329135",The structure of a tunicate C-type lectin from Polyandrocarpa misakiensis complexed with D -galactose.,published,journal,J. Mol. Biol.,Journal of molecular biology,290,4,,0022-2836,,,,,,,,,,,,,,,,,,,,867,879,1999,"C-type lectins are calcium-dependent carbohydrate-recognising proteins. Isothermal titration calorimetry of the C-type Polyandrocarpa lectin (TC14) from the tunicate Polyandrocarpa misakiensis revealed the presence of a single calcium atom per monomer with a dissociation constant of 2.6 microM, and confirmed the specificity of TC14 for D -galactose and related monosaccharides. We have determined the 2.2 A X-ray crystal structure of Polyandrocarpa lectin complexed with D -galactose. Analytical ultracentrifugation revealed that TC14 behaves as a dimer in solution. This is reflected by the presence of two molecules in the asymmetric unit with the dimeric interface formed by antiparallel pairing of the two N-terminal beta-strands and hydrophobic interactions. TC14 adopts a typical C-type lectin fold with differences in structure from other C-type lectins mainly in the diverse loop regions and in the second alpha-helix, which is involved in the formation of the dimeric interface. The D -galactose is bound through coordination of the 3 and 4-hydroxyl oxygen atoms with a bound calcium atom. Additional hydrogen bonds are formed directly between serine, aspartate and glutamate side-chains of the protein and the sugar 3 and 4-hydroxyl groups. Comparison of the galactose binding by TC14 with the mannose binding by rat mannose-binding protein reveals how monosaccharide specificity is achieved in this lectin. A tryptophan side-chain close to the binding site and the distribution of hydrogen-bond acceptors and donors around the 3 and 4-hydroxyl groups of the sugar are essential determinants of specificity. These elements are, however, arranged in a very different way than in an engineered galactose-specific mutant of MBPA. Possible biological functions can more easily be understood from the fact that TC14 is a dimer under physiological conditions." citations,entry_citation,4784,206753,1,,entry citation,,21243163,,,,"Solution Structure of the DNA-binding Domain of the TyrR Protein of Haemophilus influenzae",published,journal,Protein Sci.,Protein Science,10,,,,,,,,,,,,,,,,,,,,,,,592,598,2001, citations,entry_citation,4785,206768,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C, and 15N assignment of a bleomycin resistance protein in its native form and in a complex with Zn2+ ligated bleomycin",published,journal,J. Biomol. NMR,,18,2,,,,,,,,,,,,,,,,,,,,,,177,178,2000, citations,entry_citation,4786,206784,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C, and 15N assignment of a bleomycin resistance protein in its native form and in a complex with Zn2+ ligated bleomycin",published,journal,J. Biomol. NMR,,18,2,,,,,,,,,,,,,,,,,,,,,,177,178,2000, citations,entry_citation,4787,206804,1,,entry citation,,,,,,"Letter to the Editor: Assignment of 1H, 13C and 15N resonances of domain III of the ectodomain of apical membrane antigen 1 from Plasmodium falciparum",published,journal,J. Biomol. NMR,,19,1,,,,,,,,,,,,,,,,,,,,,,85,86,2001, citations,ref_1,4787,206805,2,,reference citation,,,8910611,,"Hodder AN, Crewther PE, Matthew ML, Reid GE, Moritz RL, Simpson RJ, Anders RF. The disulfide bond structure of Plasmodium apical membrane antigen-1. J Biol Chem. 1996 Nov 15;271(46):29446-52. PMID: 8910611; UI: 97067209",The disulfide bond structure of Plasmodium apical membrane antigen-1.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,271,46,,0021-9258,,,,,,,,,,,,,,,,,,,,29446,29452,1996,"Apical membrane antigen-1 (AMA-1) of Plasmodium falciparum is one of the leading asexual blood stage antigens being considered for inclusion in a malaria vaccine. The ability of this molecule to induce a protective immune response has been shown to be dependent upon a conformation stabilized by disulfide bonds. In this study we have utilized the reversed-phase high performance liquid chromatography of dithiothreitol-reduced and nonreduced tryptic digests of Plasmodium chabaudi AMA-1 secreted from baculovirus-infected insect cells, in conjunction with N-terminal sequencing and electrospray-ionization mass spectrometry, to identify and assign disulfide-linked peptides. All 16 cysteine residues that are conserved in all known sequences of AMA-1 are incorporated into intramolecular disulfide bonds. Six of the eight bonds have been assigned unequivocally, whereas the two unassigned disulfide bonds connect two Cys-Xaa-Cys sequences separated by 14 residues. The eight disulfide bonds fall into three nonoverlapping groups that define three possible subdomains within the AMA-1 ectodomain. Although the pattern of disulfide bonds within subdomain III has not been fully elucidated, one of only two possible linkage patterns closely resembles the cystine knot motif found in growth factors. Sites of amino acid substitutions in AMA-1 that are well separated in the primary sequence are clustered by the disulfide bonds in subdomains II and III. These findings are consistent with the conclusion that these amino acid substitutions are defining conformational disulfide bond-dependent epitopes that are recognized by protective immune responses." citations,ref_2,4787,206806,3,,reference citation,,,8589602,,"Wishart DS, Bigam CG, Yao J, Abildgaard F, Dyson HJ, Oldfield E, Markley JL, Sykes BD. 1H, 13C and 15N chemical shift referencing in biomolecular NMR. J Biomol NMR. 1995 Sep;6(2):135-40. PMID: 8589602; UI: 96173087","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,ref_3,4787,206807,4,,reference citation,,,,,"Bartels, C., Xia ,T., Billeter, M., Guntert, P. and Wuthrich, K. (1995) J. Biomol. NMR, 6, 1-10.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4788,206835,1,,entry citation,,,,,,"Letter to the Editor: 1H, 15N, and 13C NMR resonance assignments for the Eps15 homology domain of Reps1",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,18,4,,,,,,,,,,,,,,,,,,,,,,367,368,2000, citations,ref_1,4788,206836,2,,reference citation,,,9395447,,"Yamaguchi A, Urano T, Goi T, Feig LA. An Eps homology (EH) domain protein that binds to the Ral-GTPase target, RalBP1. J Biol Chem. 1997 Dec 12;272(50):31230-4.","An Eps homology (EH) domain protein that binds to the Ral-GTPase target, RalBP1.",published,journal,J. Biol. Chem.,The Journal of biological chemistry,272,50,,0021-9258,,,,,,,,,,,,,,,,,,,,31230,31234,1997,"Ral proteins constitute a family of small GTPases that can be activated by Ras in cells. In the GTP-bound state, Ral proteins bind to RalBP1, a GTPase-activating protein for CDC42 and Rac GTPases. We have used the two-hybrid system in yeast to clone a cDNA for a novel approximately 85-kDa protein that can bind to an additional site on RalBP1. This newly identified protein contains an Eps homology (EH) domain, which was first detected in the epidermal growth factor (EGF) receptor substrate Eps15. Recently, the EH domain of Eps15 has been shown to bind to proteins containing an asparagine-proline-phenylalanine motif. Moreover, EH domains have been found in proteins involved in endocytosis and/or actin cytoskeleton regulation. The RalBP1 associated Eps-homology domain protein, Reps1, is tyrosine-phosphorylated in response to EGF stimulation of cells. In addition, Reps1 has the capacity to form a complex with the SH3 domains of the adapter proteins Crk and Grb2, which may link Reps1 to an EGF-responsive tyrosine kinase. Thus, Reps1 may coordinate the cellular actions of activated EGF receptors and Ral-GTPases." citations,entry_citation,4789,206866,1,,entry citation,,20481412,,,,"Solution Structure of the TAZ2(CH3) Domain of the Transcriptional Adaptor Protein CBP",published,journal,J. Mol. Biol.,,303,2,,,,,,,,,,,,,,,,,,,,,,243,253,2000, citations,ref_1,4789,206867,2,,reference citation,,,,,"B. A.Johnson and R. A. Blevins, J. Biomol. NMR. 4, 603 (1994)",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_2,4789,206868,3,,reference citation,,,8520220,,"F. Delaglio, et al., J. Biomol. NMR 6, 277 (1995)",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,entry_citation,4813,207460,1,,entry citation,,,,,,"The Solution Structure of Lac Repressor Headpiece 62 Complexed to a Symmetrical Lac Operator",published,journal,Structure,,7,,,,,,,,,,,,,,,,,,,,,,,1483,1492,1999, citations,entry_citation,479,206901,1,,entry citation,,,,,"Campbell-Burk, Sharon, ""Structural and Dynamic Differences between Normal and Transforming N-ras Gene Products: A 31P and Isotope-Edited 1H NMR Study,"" Biochemistry 28, 9478-9484 (1989).","Structural and Dynamic Differences between Normal and Transforming N-ras Gene Products: A 31P and Isotope-Edited 1H NMR Study",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,9478,9484,1989, citations,entry_citation,4790,206914,1,,entry citation,,21040573,11200536,,,"1H, 13C and 15N Resonance Assignments of the SNT PTB Domain in Complex with FGFR1 Peptide",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,18,4,,,,,,,,,,,,,,,,,,,,,,371,372,2000, citations,entry_citation,4791,206930,1,,entry citation,,21022127,,,,"Letter to the Editor: Sequence-specific 1H, 15N and 13C Resonance Assignments for an Engineered Arginine-rich Domain of the Hepatitis C Virus NS3 RNA Helicase",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,18,3,,,,,,,,,,,,,,,,,,,,,,279,280,2000, citations,entry_citation,4792,206954,1,,entry citation,,21609805,11743881,,,"The Anti-toxin ParD of Plasmid RK2 Consists of two Structurally Distinct Moieties and Belongs to the Ribbon-helix-helix Family of DNA-binding Proteins",published,journal,Biochem. J.,,361,Pt 1,,,,,,,,,,,,,,,,,,,,,,41,47,2002, citations,ref_1,4792,206955,2,,reference citation,,,,,"Ch. Bartels, T.-H. Xia, M. Billeter, P. G?ntert and K. W?thrich (1995) The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J. Biomolecular NMR 5, 1-10",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4793,206980,1,,entry citation,,20422734,,,,"Structure-based Functional Classification of Hypothetical Protein MTH538 from Methanobacterium thermoautotrophicum",published,journal,J. Mol. Biol.,Journal of Molecular Biology,302,1,,,,,,,,,,,,,,,,,,,,,,189,203,2000, citations,entry_citation,4794,207009,1,,entry citation,,,,,,"Elucidating the Mechanism of Familial Amyloidosis--Finnish Type: NMR Studies of Human Gelsolin Domain 2",published,journal,Proc. Natl. Acad. Sci. U.S.A.,,97,,,,,,,,,,,,,,,,,,,,,,,10706,10711,2000, citations,entry_citation,4795,207028,1,,entry citation,,,,,,"Elucidating the Mechanism of Familial Amyloidosis--Finnish Type: NMR Studies of Human Gelsolin Domain 2",published,journal,Proc. Natl. Acad. Sci. U.S.A.,,97,,,,,,,,,,,,,,,,,,,,,,,10706,10711,2000, citations,entry_citation,4796,207047,1,,entry citation,,,,,,"NMR Structure Determination and Structure-Based Functional Classification of Conserved Hypothetical Protein MTH1175 from Methanobacterium thermoautotrophicum",published,journal,J. Struct. Funct. Gen.,,1,,,,,,,,,,,,,,,,,,,,,,,15,25,2000, citations,entry_citation,4797,207078,1,,entry citation,,,,,,"Letter to the Editor: Sequence-specific resonance assignments of the potent cytolysin equinatoxin II",published,journal,J. Biomol. NMR,,18,3,,,,,,,,,,,,,,,,,,,,,,281,282,2000, citations,entry_citation,4798,207094,1,,entry citation,,20471909,,,,"Structure and Calcium-binding Properties of frq1, a Novel Calcium Sensor in the Yeast Saccharomyces cerevisiae",published,journal,Biochemistry,Biochemistry,39,40,,,,,,,,,,,,,,,,,,,,,,12149,12161,2000, citations,entry_citation,4799,207114,1,,entry citation,,,,,,"Solution Structure of Human Immunodeficiency Virus Type 1 Vpr (13-33) Peptide in Micells",submitted,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,48,207131,1,,entry citation,,,,,"Wagner, Gerhard, Braun, Werner, Havel, Timothy F., Schaumann, Thomas, Go, Nobuhiro, Wuthrich, Kurt, ""Protein Structures in Solution by Nuclear Magnetic Resonance and Distance Geometry (The Polypeptide Fold of the Basic Pancreatic Trypsin Inhibitor Determined using Two Different Algorithms, DISGEO and DISMAN),"" J. Mol. Biol. 196, 611-639 (1987).","Protein Structures in Solution by Nuclear Magnetic Resonance and Distance Geometry (The Polypeptide Fold of the Basic Pancreatic Trypsin Inhibitor Determined using Two Different Algorithms, DISGEO and DISMAN)",published,journal,J. Mol. Biol.,,196,,,,,,,,,,,,,,,,,,,,,,,611,639,1987, citations,entry_citation,480,207144,1,,entry citation,,,,,"Driscoll, Paul C., Clore, G. Marius, Beress, Lazlo, Gronenborn, Angela M., ""A Proton Nuclear Magnetic Resonance Study of the Antihypertensive and Antiviral Protein BDS-I from the Sea Anemone Anemonia sulcata: Sequential and Stereospecific Resonance Assignment and Secondary Structure,"" Biochemistry 28, 2178-2187 (1989).","A Proton Nuclear Magnetic Resonance Study of the Antihypertensive and Antiviral Protein BDS-I from the Sea Anemone Anemonia sulcata: Sequential and Stereospecific Resonance Assignment and Secondary Structure",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,2178,2187,1989, citations,entry_citation,4800,207157,1,,entry citation,,,,,,"Heme Ligation and Conformational Plasticity in the Isolated c Domain of Cytochrome cd1 Nitrite Reductase",published,journal,J. Biol. Chem.,Journal of Biological Chemistry,276,,,,,,,,,,,,,,,,,,,,,,,5846,5855,2001, citations,entry_citation,4801,207182,1,,entry citation,,,,,,"Heme Ligation and Conformational Plasticity in the Isolated c Domain of Cytochrome cd1 Nitrite Reductase",published,journal,J. Biol. Chem.,Journal of Biological Chemistry,276,,,,,,,,,,,,,,,,,,,,,,,5846,5855,2001, citations,entry_citation,4802,207205,1,,entry citation,,,,,,"Structural Insight to the Oligomerisation of the Bacterial Chromatin-Structuring Protein H-N",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_1,4802,207206,2,,reference citation,,,10844682,,"Smyth, C. P., Lundback, T., Renzoni, D., Siligardi, G., Beavil, R., Layton, M., Sidebotham, J. M., Hinton, J. C., Driscoll, P. C., Higgins, C. F. and Ladbury, J. E. (2000) Oligomerisation of the chromatin-structuring protein H-NS. Mol. Microbiol. 36, 962-972.",Oligomerization of the chromatin-structuring protein H-NS.,published,journal,Mol. Microbiol.,Molecular microbiology,36,4,,0950-382X,,,,,,,,,,,,,,,,,,,,962,972,2000,"H-NS is a major component of the bacterial nucleoid, involved in condensing and packaging DNA and modulating gene expression. The mechanism by which this is achieved remains unclear. Genetic data show that the biological properties of H-NS are influenced by its oligomerization properties. We have applied a variety of biophysical techniques to study the structural basis of oligomerization of the H-NS protein from Salmonella typhimurium. The N-terminal 89 amino acids are responsible for oligomerization. The first 64 residues form a trimer dominated by an alpha-helix, likely to be in coiled-coil conformation. Extending this polypeptide to 89 amino acids generated higher order, heterodisperse oligomers. Similarly, in the full-length protein no single, defined oligomeric state is adopted. The C-terminal 48 residues do not participate in oligomerization and form a monomeric, DNA-binding domain. These N- and C-terminal domains are joined via a flexible linker which enables them to function independently within the context of the full-length protein. This novel mode of oligomerization may account for the unusual binding properties of H-NS." citations,entry_citation,4814,207479,1,,entry citation,,,,,,"Letter to the Editor: Complete 1H, 15N, and 13C assignments of an exchangeable apolipoprotein, Locusta migratoria apolipophorin III",published,journal,J. Biomol. NMR,,19,1,,,,,,,,,,,,,,,,,,,,,,83,84,2001, citations,entry_citation,4868,208532,1,,entry citation,,92071964,,,,"Two-dimensional 1H nuclear magnetic resonance study of the (5-55) single-disulphide folding intermediate of bovine pancreatic trypsin inhibitor",published,journal,J. Mol. Biol.,,222,,,,,,,,,,,,,,,,,,,,,,,373,390,1991, citations,ref_2,4802,207207,3,,reference citation,,,8520220,,"Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. Related Articles NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR. 1995 Nov;6(3):277-93.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref_3,4802,207208,4,,reference citation,,,,,"Boucher, W. (1996) AZARA v2.0, Department of Biochemistry, University of Cambridge, UK.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_4,4802,207209,5,,reference citation,,,,,"Kraulis, P. (1989) ANSIG: A program for the assignment of protein 1H 2D NMR spectra by interactive graphics. J. Magn. Reson. 24, 627-633.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4803,207227,1,,entry citation,,,,,,NMR Studies of the Association of Cytochrome b5 with Cytochrome c,in press,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_1,4803,207228,2,,reference citation,,,,,"Day, M. (1990) Striker, NMR Processing Program, unpublished, Copyright University of California, San Francisco",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_2,4803,207229,3,,reference citation,,,8520220,,"Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Peifer, J. and Bax, A. (1995) J. Biomol. NMR 6, 277-293",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref_3,4803,207230,4,,reference citation,,,,,"Goddard, T. and James, T.L. (1997) Sparky, NMR Display and Analysis Program, Version 3.3.2 Copyright University of California, San Francisco",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4804,207249,1,,entry citation,,,,,,NMR Studies of the Association of Cytochrome b5 with Cytochrome c,in press,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_1,4804,207250,2,,reference citation,,,,,"Day, M. (1990) Striker, NMR Processing Program, unpublished, Copyright University of California, San Francisco",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_2,4804,207251,3,,reference citation,,,8520220,,"Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Peifer, J. and Bax, A. (1995) J. Biomol. NMR 6, 277-293",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref_3,4804,207252,4,,reference citation,,,,,"Goddard, T. and James, T.L. (1997) Sparky, NMR Display and Analysis Program, Version 3.3.2 Copyright University of California, San Francisco",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4805,207271,1,,entry citation,,,,,,NMR Studies of the Association of Cytochrome b5 with Cytochrome c,in press,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_1,4805,207272,2,,reference citation,,,,,"Day, M. (1990) Striker, NMR Processing Program, unpublished, Copyright University of California, San Francisco",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4850,208174,1,,entry citation,,,11031118,,,NMR Structure of Oxidized Glutaredoxin 3 from Escherichia coli,published,journal,J. Mol. Biol.,Journal of Molecular Biology,303,,,,,,,,,,,,,,,,,,,,,,,423,432,2000, citations,entry_citation,4851,208192,1,,entry citation,,,,,,"Structure of Cdc4p, a contractile ring protein essential for cytokinesis in Schizosaccharomyces pombe",published,journal,J. Biol. Chem.,,276,,,,,,,,,,,,,,,,,,,,,,,5943,5951,2001, citations,entry_citation,4852,208219,1,,entry citation,,,,,,"Accessibility of selenomethionine proteins by total synthesis: structural studies of human herpesvirus-8 MIP-II",published,journal,FEBS Lett.,,441,1,,,,,,,,,,,,,,,,,,,,,,77,82,1998, citations,ref_2,4805,207273,3,,reference citation,,,8520220,,"Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Peifer, J. and Bax, A. (1995) J. Biomol. NMR 6, 277-293",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref_3,4805,207274,4,,reference citation,,,,,"Goddard, T. and James, T.L. (1997) Sparky, NMR Display and Analysis Program, Version 3.3.2 Copyright University of California, San Francisco",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4806,207296,1,,entry citation,,,,,,NMR Studies of the Association of Cytochrome b5 with Cytochrome c,in press,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_1,4806,207297,2,,reference citation,,,,,"Day, M. (1990) Striker, NMR Processing Program, unpublished, Copyright University of California, San Francisco",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_2,4806,207298,3,,reference citation,,,8520220,,"Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Peifer, J. and Bax, A. (1995) J. Biomol. NMR 6, 277-293",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref_3,4806,207299,4,,reference citation,,,,,"Goddard, T. and James, T.L. (1997) Sparky, NMR Display and Analysis Program, Version 3.3.2 Copyright University of California, San Francisco",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4807,207318,1,,entry citation,,,,,,NMR Studies of the Association of Cytochrome b5 with Cytochrome c,in press,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_1,4807,207319,2,,reference citation,,,,,"Day, M. (1990) Striker, NMR Processing Program, unpublished, Copyright University of California, San Francisco",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_2,4807,207320,3,,reference citation,,,8520220,,"Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Peifer, J. and Bax, A. (1995) J. Biomol. NMR 6, 277-293",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref_3,4807,207321,4,,reference citation,,,,,"Goddard, T. and James, T.L. (1997) Sparky, NMR Display and Analysis Program, Version 3.3.2 Copyright University of California, San Francisco",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4808,207340,1,,entry citation,,,,,,NMR Studies of the Association of Cytochrome b5 with Cytochrome c,in press,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_1,4808,207341,2,,reference citation,,,,,"Day, M. (1990) Striker, NMR Processing Program, unpublished, Copyright University of California, San Francisco",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4853,208239,1,,entry citation,,,,,,"A Cis-trans Isomerism of a Non-prolyl Peptide Bond in Lqh III Alpha-like Scorpion Toxin Revealed by Solution NMR",submitted,journal,J. Mol. Biol.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_1,4853,208240,2,,reference citation,,,,,"Pons, J.L., Malliavin, T.E. and Delsuc, M.A., 1996. Gifa V4 : a complete package for NMR data-set processing. J. Biomol. NMR, 8, 445-452.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50024,212021,1,,entry citation,,,31628949,,,The WW1 Domain Enhances Autoinhibition in Smurf Ubiquitin Ligases,published,journal,J. Mol. Biol.,Journal of molecular biology,431,24,,1089-8638,,,,,,,,,,,,,,,,,,,,4834,4847,2019, citations,citations_1,50025,212034,1,,entry citation,,,32030620,,,Backbone assignment of ribose-5-phosphate isomerase of Mycobacterium tuberculosis (MtRpiB),published,journal,Biomol. NMR Assignments,,14,1,,1874-270X,,,,,,,,,,,,,,,,,,,,119,122,2020, citations,ref_2,4808,207342,3,,reference citation,,,8520220,,"Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Peifer, J. and Bax, A. (1995) J. Biomol. NMR 6, 277-293",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref_3,4808,207343,4,,reference citation,,,,,"Goddard, T. and James, T.L. (1997) Sparky, NMR Display and Analysis Program, Version 3.3.2 Copyright University of California, San Francisco",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4809,207365,1,,entry citation,,,,,,NMR Studies of the Association of Cytochrome b5 with Cytochrome c,in press,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_1,4809,207366,2,,reference citation,,,,,"Day, M. (1990) Striker, NMR Processing Program, unpublished, Copyright University of California, San Francisco",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_2,4809,207367,3,,reference citation,,,8520220,,"Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Peifer, J. and Bax, A. (1995) J. Biomol. NMR 6, 277-293",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref_3,4809,207368,4,,reference citation,,,,,"Goddard, T. and James, T.L. (1997) Sparky, NMR Display and Analysis Program, Version 3.3.2 Copyright University of California, San Francisco",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,481,207390,1,,entry citation,,,,,"Driscoll, Paul C., Clore, G. Marius, Beress, Lazlo, Gronenborn, Angela M., ""A Proton Nuclear Magnetic Resonance Study of the Antihypertensive and Antiviral Protein BDS-I from the Sea Anemone Anemonia sulcata: Sequential and Stereospecific Resonance Assignment and Secondary Structure,"" Biochemistry 28, 2178-2187 (1989).","A Proton Nuclear Magnetic Resonance Study of the Antihypertensive and Antiviral Protein BDS-I from the Sea Anemone Anemonia sulcata: Sequential and Stereospecific Resonance Assignment and Secondary Structure",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,2178,2187,1989, citations,entry_citation,4810,207403,1,,entry citation,,,,,,NMR Studies of the Association of Cytochrome b5 with Cytochrome c,in press,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_1,4810,207404,2,,reference citation,,,,,"Day, M. (1990) Striker, NMR Processing Program, unpublished, Copyright University of California, San Francisco",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_2,4810,207405,3,,reference citation,,,8520220,,"Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Peifer, J. and Bax, A. (1995) J. Biomol. NMR 6, 277-293",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref_3,4810,207406,4,,reference citation,,,,,"Goddard, T. and James, T.L. (1997) Sparky, NMR Display and Analysis Program, Version 3.3.2 Copyright University of California, San Francisco",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4811,207428,1,,entry citation,,21172998,11273708,,,"Comparison of the Structural and Dynamical Properties of Holo and Apo bovine Alpha-lactalbumin by NMR Spectroscopy",published,journal,J. Mol. Biol.,,307,3,,,,,,,,,,,,,,,,,,,,,,885,898,2001, citations,ref_1,4811,207429,2,,reference citation,,,,,"Live, D.H., Davis, D.G., Agosta, W.C. and Cowburn, D. J. (1984) J.Am. Chem. Soc. Vol 106, 1939-1941.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4812,207443,1,,entry citation,,,,,,"Structure and Conformational Heterogeneity of a Weak Toxin from Naja kaouthia venom",submitted,journal,Boorg. Khim.,Russian Journal of Bioorganic Chemistry,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_1,4814,207480,2,,reference citation,,,8520220,,"Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J. and Bax, A. (1995) NMRpipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,entry_citation,4815,207495,1,,entry citation,,,11114253,,,Membrane Binding Motif of the P-type Cardiotoxin,published,journal,J. Mol. Biol.,,305,,,,,,,,,,,,,,,,,,,,,,,137,149,2001, citations,ref-1,4815,207496,2,,reference citation,,,,,"Bartels C., Xia T.-H., Billeter M., Guentert P. & Wuethrich K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules, J. Biomol. NMR (1995) 6, 1-10.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref-2,4815,207497,3,,reference citation,,,9367762,,"Guentert P., Mumenthaler C. & Wuethrich K. Torsion angle dynamics for NMR structure calculation with new program DYANA, J. Mol. Biol. (1997) 273, 283-298.",Torsion angle dynamics for NMR structure calculation with the new program DYANA.,published,journal,J. Mol. Biol.,Journal of molecular biology,273,1,,0022-2836,,,,,,,,,,,,,,,,,,,,283,298,1997,"The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from distance constraints and torsion angle constraints collected by nuclear magnetic resonance (NMR) experiments performs simulated annealing by molecular dynamics in torsion angle space and uses a fast recursive algorithm to integrate the equations of motions. Torsion angle dynamics can be more efficient than molecular dynamics in Cartesian coordinate space because of the reduced number of degrees of freedom and the concomitant absence of high-frequency bond and angle vibrations, which allows for the use of longer time-steps and/or higher temperatures in the structure calculation. It also represents a significant advance over the variable target function method in torsion angle space with the REDAC strategy used by the predecessor program DIANA. DYANA computation times per accepted conformer in the ""bundle"" used to represent the NMR structure compare favorably with those of other presently available structure calculation algorithms, and are of the order of 160 seconds for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300 computer. Test calculations starting from conformers with random torsion angle values further showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures." citations,entry_citation,4816,207515,1,,entry citation,,21438036,11553808,,,"Structural Features of an Influenza Virus Promoter and Their Implications for Viral RNA Synthesis",published,journal,Proc. Natl. Acad. Sci. U.S.A.,,98,19,,,,,,,,,,,,,,,,,,,,,,10602,10607,2001, citations,entry_citation,4817,207540,1,,entry citation,,21167488,11266624,,,"Solution Nuclear Magnetic Resonance Structure of a Protein Disulfide Oxidoreductase from Methanococcus jannaschii",published,journal,Protein Sci.,,10,2,,,,,,,,,,,,,,,,,,,,,,384,396,2001, citations,entry_citation,4818,207566,1,,entry citation,,21151325,11256818,,,"1H, 13C and 15N Resonance Assignments of the ERK2 Binding Domain of the MAPK Phosphatase MKP-3",published,journal,J. Biomol. NMR,,19,2,,,,,,,,,,,,,,,,,,,,,,195,196,2001, citations,entry_citation,4819,207580,1,,entry citation,,20534887,11080457,,,"High precision NMR structure of YhhP, a novel escherichia coli protein implicated in cell division",published,journal,J. Mol. Biol.,,304,,,,,,,,,,,,,,,,,,,,,,,219,229,2000, citations,entry_citation,4820,207593,1,,entry citation,,,,,,"Letter to the Editor: NMR structure of the pheromone Er-22 from Euplotes raikovi",published,journal,J. Biomol. NMR,,19,1,,,,,,,,,,,,,,,,,,,,,,75,78,2001, citations,ref1,4820,207594,2,,reference citation,,,,,"Guntert, Dotsch, Wider, Wuthrich (1992) J Biomol NMR 2, 619-629",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref2,4820,207595,3,,reference citation,,,,,"Bartels, Xia, Billeter, Guntert, Wuthrich (1995) J Biomol NMR 5, 1-10",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref3,4820,207596,4,,reference citation,,,1847217,,"Guntert, Braun, Wuthrich (1991) J Mol Biol 217, 517-530","Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA.",published,journal,J. Mol. Biol.,Journal of molecular biology,217,3,,0022-2836,,,,,,,,,,,,,,,,,,,,517,530,1991,"A novel procedure for efficient computation of three-dimensional protein structures from nuclear magnetic resonance (n.m.r.) data in solution is described, which is based on using the program DIANA in combination with the supporting programs CALIBA, HABAS and GLOMSA. The first part of this paper describes the new programs DIANA. CALIBA and GLOMSA. DIANA is a new, fully vectorized implementation of the variable target function algorithm for the computation of protein structures from n.m.r. data. Its main advantages, when compared to previously available programs using the variable target function algorithm, are a significant reduction of the computation time, and a novel treatment of experimental distance constraints involving diastereotopic groups of hydrogen atoms that were not individually assigned. CALIBA converts the measured nuclear Overhauser effects into upper distance limits and thus prepares the input for the previously described program HABAS and for DIANA. GLOMSA is used for obtaining individual assignments for pairs of diastereotopic substituents by comparison of the experimental constraints with preliminary results of the structure calculations. With its general outlay, the presently used combination of the four programs is particularly user-friendly. In the second part of the paper, initial results are presented on the influence of the novel DIANA treatment of diastereotopic protons on the quality of the structures obtained, and a systematic study of the central processing unit times needed for the same protein structure calculation on a range of different, commonly available computers is described." citations,entry_citation,4860,208399,1,,entry citation,,,,,,"Letter to the Editor: Sequence-specific 1H, 13C and 15N resonance assignments of lymphocyte specific kinase unique and SH3 domains",published,journal,J. Biomol. NMR,,19,2,,,,,,,,,,,,,,,,,,,,,,193,194,2001, citations,entry_citation,4862,208422,1,,entry citation,,,,,,"The First Selective Agonist at the Neuropeptide Y Y5-Receptor Increases Food Intake in Rats",in press,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,2000, citations,citations_1,50174,213369,1,Rab1b and Cdc42,entry citation,,,32123090,,,Conformational Control of Small GTPases by AMPylation,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,117,11,,1091-6490,,,,,,,,,,,,,,,,,,,,5772,5781,2020, citations,ref4,4820,207597,5,,reference citation,,,8914272,,"Luginbuhl, Guntert, Billeter, Wuthrich (1996) J Biomol NMR 8, 136-146",The new program OPAL for molecular dynamics simulations and energy refinements of biological macromolecules.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,8,2,,0925-2738,,,,,,,,,,,,,,,,,,,,136,146,1996,"A new program for molecular dynamics (MD) simulation and energy refinement of biological macromolecules, OPAL, is introduced. Combined with the supporting program TRAJEC for the analysis of MD trajectories, OPAL affords high efficiency and flexibility for work with different force fields, and offers a user-friendly interface and extensive trajectory analysis capabilities. Salient features are computational speeds of up to 1.5 GFlops on vector supercomputers such as the NEC SX-3, ellipsoidal boundaries to reduce the system size for studies in explicit solvents, and natural treatment of the hydrostatic pressure. Practical applications of OPAL are illustrated with MD simulations of pure water, energy minimization of the NMR structure of the mixed disulfide of a mutant E. coli glutaredoxin with glutathione in different solvent models, and MD simulations of a small protein, pheromone Er-2, using either instantaneous or time-averaged NMR restraints, or no restraints." citations,entry_citation,4821,207616,1,,entry citation,,,,,,"Letter to the Editor: Assignment of 1H, 13C, and 15N resonances to the sensory domain of membraneous two-component fumarate sensor (histidine protein kinase) DcuS of Escherichia coli",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,19,1,,,,,,,,,,,,,,,,,,,,,,91,92,2001, citations,entry_citation,4822,207641,1,,entry citation,,20507572,,,,"Conformations of the Regulatory Domain of Cardiac Troponin C Examined by Residual Dipolar Couplings",published,journal,Eur. J. Biochem.,European Journal of Biochemistry,267,,,,,,,,,,,,,,,,,,,,,,,6665,6672,2000, citations,entry_citation,4823,207653,1,,entry citation,,20507572,,,,"Conformations of the Regulatory Domain of Cardiac Troponin C Examined by Residual Dipolar Couplings",published,journal,Eur. J. Biochem.,European Journal of Biochemistry,267,,,,,,,,,,,,,,,,,,,,,,,6665,6672,2000, citations,entry_citation,4824,207667,1,,entry citation,,20507572,,,,"Conformations of the Regulatory Domain of Cardiac Troponin C Examined by Residual Dipolar Couplings",published,journal,Eur. J. Biochem.,European Journal of Biochemistry,267,,,,,,,,,,,,,,,,,,,,,,,6665,6672,2000, citations,entry_citation,4825,207680,1,,entry citation,,21140948,,,,"1H, 15N and 13C resonance assignments and secondary structure determination of the RC-RNase 2 from oocytes of bullfrog Rana catesbeiana",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,19,1,,,,,,,,,,,,,,,,,,,,,,87,88,2001, citations,entry_citation,4827,207706,1,,entry citation,,,,,,"Structural comparison between WT and P25S human cystatin A by NMR spectroscopy. Does this mutation affect the alpha-helix conformation?",published,journal,J. Struct. Func. Genomics.,,1,,,,,,,,,,,,,,,,,,,,,,,26,42,2001,"The effect of the substitution of Pro25 with Ser, located in the alpha-helical region, on the cystatin A structure has been studied." citations,entry_citation,4828,207724,1,,entry citation,,,,,,"Structural comparison between WT and P25S human cystatin A by NMR spectroscopy. Does this mutation affect the alpha-helix conformation?",published,journal,J. Struct. Func. Genomics.,,1,,,,,,,,,,,,,,,,,,,,,,,26,42,2001,"The effect of the substitution of Pro25 with Ser, located in the alpha-helical region, on the cystatin A structure has been studied." citations,entry_citation,4829,207742,1,,entry citation,,,12402362,,,"Solution structure of the DNA-binding domain of interleukin enhancer binding factor 1 (FOXK1a)",published,journal,"Proteins: Struct., Funct., Genet.",,49,4,,,,,,,,,,,,,,,,,,,,,,543,553,2002, citations,entry_citation,4830,207770,1,,entry citation,,21181811,11285216,,,"The Hairpin Structure of the (6)F1(1)F2(2)F2 Fragment from Human Fibronectin Enhances Gelatin Binding",published,journal,EMBO J.,,20,7,,,,,,,,,,,,,,,,,,,,,,1519,1529,2001, citations,entry_citation,4831,207785,1,,entry citation,,,11274458,,,"A Refined Solution Structure of Hen Lysozyme Determined Using Residual Dipolar Coupling Data",published,journal,Protein Sci.,Protein Science,10,,,,,,,,,,,,,,,,,,,,,,,677,688,2001, citations,entry_citation,4832,207807,1,,entry citation,,97084804,,,,Solution Structure of a Mini IGF-1,published,journal,Protein Sci.,,5,,,,,,,,,,,,,,,,,,,,,,,2193,2202,1996, citations,entry_citation,4833,207823,1,,entry citation,,21248995,11350173,,,"Solution Structure, Backbone Dynamics and Chitin Binding of the Anti-fungal Protein from Streptomyces tendae Tu901",published,journal,J. Mol. Biol.,,308,4,,,,,,,,,,,,,,,,,,,,,,765,782,2001, citations,ref1,4833,207824,2,,reference citation,,,10601197,,"Bormann C, Baier D, Horr I, Raps C, Berger J, Jung G, Schwarz H. Characterization of a novel, antifungal, chitin-binding protein from Streptomyces tendae Tu901 that interferes with growth polarity. J Bacteriol. 1999 Dec; 181(24):7421-9.","Characterization of a novel, antifungal, chitin-binding protein from Streptomyces tendae Tu901 that interferes with growth polarity.",published,journal,J. Bacteriol.,Journal of bacteriology,181,24,,0021-9193,,,,,,,,,,,,,,,,,,,,7421,7429,1999,"The afp1 gene, which encodes the antifungal protein AFP1, was cloned from nikkomycin-producing Streptomyces tendae Tu901, using a nikkomycin-negative mutant as a host and screening transformants for antifungal activity against Paecilomyces variotii in agar diffusion assays. The 384-bp afp1 gene has a low G+C content (63%) and a transcription termination structure with a poly(T) region, unusual attributes for Streptomyces genes. AFP1 was purified from culture filtrate of S. tendae carrying the afp1 gene on the multicopy plasmid pIJ699. The purified protein had a molecular mass of 9,862 Da and lacked a 42-residue N-terminal peptide deduced from the nucleotide sequence. AFP1 was stable at extreme pH values and high temperatures and toward commercial proteinases. AFP1 had limited similarity to cellulose-binding domains of microbial plant cell wall hydrolases and bound to crab shell chitin, chitosan, and cell walls of P. variotii but showed no enzyme activity. The biological activity of AFP1, which represents the first chitin-binding protein from bacteria exhibiting antifungal activity, was directed against specific ascomycetes, and synergistic interaction with the chitin synthetase inhibitor nikkomycin inhibited growth of Aspergillus species. Microscopy studies revealed that fluorescein-labeled AFP1 strongly bound to the surface of germinated conidia and to tips of growing hyphae, causing severe alterations in cell morphogenesis that gave rise to large spherical conidia and/or swollen hyphae and to atypical branching." citations,entry_citation,4834,207855,1,,entry citation,,,,,,"Letter to the Editor: Backbone (1H, 15N, 13C) resonance assignments of a 21 kDa construct of S. aureus peptide deformylase",published,journal,J. Biomol. NMR,,19,1,,,,,,,,,,,,,,,,,,,,,,81,82,2001, citations,entry_citation,4835,207880,1,,entry citation,,,,,,DNA structure by 1H NMR methods: Studies of d(GCGTTAACGC)2,published,thesis,,,,,,,,,,,,,,,,,,,,,,The Scripps Research Institute,"La Jolla, CA",USA,,,,1999, citations,entry_citation,4836,207897,1,,entry citation,,,,,,"Letter to the Editor: Complete 1H, 13C and 15N backbone assignments for the hepatitis A virus 3C protease",published,journal,J. Biomol. NMR,,19,2,,,,,,,,,,,,,,,,,,,,,,187,188,2001, citations,entry_citation,4837,207923,1,,entry citation,,21226872,11327772,,,"Solution Structure of Methylophilus methylotrophus Cytochrome C'': Insights into the Structural Basis of Heme-ligand Detachment",published,journal,J. Mol. Biol.,,308,2,,,,,,,,,,,,,,,,,,,,,,353,365,2001, citations,entry_citation,4838,207945,1,,entry citation,,21229533,11331011,,,"NMR Mapping and Secondary Structure Determination of the Major Acetylcholine Receptor alpha-Subunit Determinant Interacting with alpha-Bungarotoxin",published,journal,Biochemistry,,40,18,,,,,,,,,,,,,,,,,,,,,,5464,5473,2001, citations,entry_citation,4839,207963,1,,entry citation,,,,,,"Letter to the editor: 1H, 15N and 13C assignments of a monomeric N-terminal deletion mutant of the Rous sarcoma virus protease",published,journal,J. Biomol. NMR,,19,3,,,,,,,,,,,,,,,,,,,,,,279,280,2001, citations,entry_citation,4840,207994,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N resonance assignment and secondary structure of Mycobacterium tuberculosis adenylate kinase",published,journal,J. Biomol. NMR,,19,1,,,,,,,,,,,,,,,,,,,,,,89,90,2001, citations,entry_citation,4841,208010,1,,entry citation,,21262923,11370785,,,"Letter to the Editor: Sequence-specific Assignment of the PAH2 Domain of Sin3B free and bound to Mad1",published,journal,J. Biomol. NMR,,19,4,,,,,,,,,,,,,,,,,,,,,,377,378,2001, citations,entry_citation,4863,208441,1,,entry citation,,20481411,11023788,,,"Solution Strcuture of the two N-terminal RNA-binding Domains of Nucleolin and NMR Study of the Interaction with its RNA Target",published,journal,J. Mol. Biol.,,303,2,,,,,,,,,,,,,,,,,,,,,,227,241,2000, citations,ref_1,4841,208011,2,,reference citation,,,8520220,,"Delaglio, F. et al. J. Biomol. NMR 6, 277-293 (1995)",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref_2,4841,208012,3,,reference citation,,,,,"Ch. Bartels, et al. J. Biomol. NMR 5, 1-10 (1995)",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_3,4841,208013,4,,reference citation,,,9757107,,"Brunger, A.T. et al. Acta Cryst. D54, 905-921 (1998)",Crystallography & NMR system: A new software suite for macromolecular structure determination.,published,journal,Acta Crystallogr. D Biol. Crystallogr.,"Acta crystallographica. Section D, Biological crystallography",54,Pt 5,,0907-4449,,,,,,,,,,,,,,,,,,,,905,921,1998,"A new software suite, called Crystallography & NMR System (CNS), has been developed for macromolecular structure determination by X-ray crystallography or solution nuclear magnetic resonance (NMR) spectroscopy. In contrast to existing structure-determination programs, the architecture of CNS is highly flexible, allowing for extension to other structure-determination methods, such as electron microscopy and solid-state NMR spectroscopy. CNS has a hierarchical structure: a high-level hypertext markup language (HTML) user interface, task-oriented user input files, module files, a symbolic structure-determination language (CNS language), and low-level source code. Each layer is accessible to the user. The novice user may just use the HTML interface, while the more advanced user may use any of the other layers. The source code will be distributed, thus source-code modification is possible. The CNS language is sufficiently powerful and flexible that many new algorithms can be easily implemented in the CNS language without changes to the source code. The CNS language allows the user to perform operations on data structures, such as structure factors, electron-density maps, and atomic properties. The power of the CNS language has been demonstrated by the implementation of a comprehensive set of crystallographic procedures for phasing, density modification and refinement. User-friendly task-oriented input files are available for nearly all aspects of macromolecular structure determination by X-ray crystallography and solution NMR." citations,ref_4,4841,208014,5,,reference citation,,,9199409,,"Nilges, M. et al. J. Mol. Biol. 269, 408-422 (1997)",Automated NOESY interpretation with ambiguous distance restraints: the refined NMR solution structure of the pleckstrin homology domain from beta-spectrin.,published,journal,J. Mol. Biol.,Journal of molecular biology,269,3,,0022-2836,,,,,,,,,,,,,,,,,,,,408,422,1997,"We have used a novel, largely automated, calculation method to refine the NMR solution structure of the pleckstrin homology domain of beta-spectrin. The method is called ARIA for Ambiguous Restraints for Iterative Assignment. The starting point for ARIA is an almost complete assignment of the proton chemical shifts, and a list of partially assigned NOEs, mostly sequential and secondary structure NOEs. The restraint list is then augmented by automatically interpreting peak lists generated by automated peak-picking. The central task of ARIA is the assignment of ambiguous NOEs during the structure calculation using a combination of ambiguous distance restraints and an iterative assignment strategy. In addition, ARIA calibrates ambiguous NOEs to derive distance restraints, merges overlapping data sets to remove duplicate information, and uses empirical rules to identify erroneous peaks. While the distance restraints for the structure calculations were exclusively extracted from homonuclear 2D experiments, ARIA is especially suited for the analysis of multidimensional spectra. Applied to the pleckstrin homology domain, ARIA generated structures of good quality, and of sufficiently high accuracy to solve the X-ray crystal structure of the same domain by molecular replacement. The comparison of the free NMR solution structure to the X-ray structure, which is complexed to D-myo-inositol-1,4,5-triphosphate, shows that the ligand primarily induces a disorder-order transition in the binding loops, which are disordered in the NMR ensemble but well ordered in the crystal. The structural core of the protein is unaffected, as evidenced by a backbone root-mean-square difference between the average NMR coordinates and the X-ray crystal structure for the secondary structure elements of less than 0.6 A." citations,entry_citation,4842,208035,1,,entry citation,,20393886,,,,"Solution structure of monomeric peptide YY supports the functional significance of the PP-fold",published,journal,Biochemistry,,39,32,,,,,,,,,,,,,,,,,,,,,,9935,9942,2000, citations,entry_citation,4843,208052,1,,entry citation,,,,,,"Letter to the Editor: Secondary Structure and Backbone Resonance Assignments for Human Interleukin-13",published,journal,J. Biomol. NMR,,19,1,,,,,,,,,,,,,,,,,,,,,,93,94,2000, citations,entry_citation,4844,208066,1,,entry citation,,,,,,"Letter to the Editor: Backbone HN, N, Ca, C? and Cb assignment of the 25 kDa peptide methionine sulfoxide reductase from Erwinia chrysanthemi",published,journal,J. Biomol. NMR,,20,1,,,,,,,,,,,,,,,,,,,,,,97,98,2001, citations,entry_citation,4845,208087,1,,entry citation,,,,,,"Structure-activity Relationships in a Peptidic Alpha7 Nicotinic Acetylcholine Receptor Antagonist",published,journal,J. Mol. Biol.,Journal of Molecular Biology,304,,,,,,,,,,,,,,,,,,,,,,,911,926,2000, citations,entry_citation,4846,208103,1,,entry citation,,,,,,"Structure-activity Relationships in a Peptidic Alpha7 Nicotinic Acetylcholine Receptor Antagonist",published,journal,J. Mol. Biol.,Journal of Molecular Biology,304,,,,,,,,,,,,,,,,,,,,,,,911,926,2000, citations,entry_citation,4847,208118,1,,entry citation,,,,,,"Structure-activity Relationships in a Peptidic Alpha7 Nicotinic Acetylcholine Receptor Antagonist",published,journal,J. Mol. Biol.,Journal of Molecular Biology,304,,,,,,,,,,,,,,,,,,,,,,,911,926,2000, citations,entry_citation,4848,208133,1,,entry citation,,21447269,11563562,,,"Letter to the Editor: Sequential Assignments of the Isolated N-terminal Domain of 5-Enolpyruvylshikimate-3-phosphate Synthase",published,journal,J. Biomol. NMR,,20,4,,,,,,,,,,,,,,,,,,,,,,387,388,2001, citations,entry_citation,4849,208148,1,,entry citation,,21140944,,,,NMR Assignment of the A form of the Pheromone-binding Protein of Bombyx mori,published,journal,J. Biomol. NMR,,19,1,,,,,,,,,,,,,,,,,,,,,,79,80,2001, citations,entry_citation,485,208161,1,,entry citation,,,,,"Glushka, John, Lee, Maria, Coffin, Scott, Cowburn, David, ""15N Chemical Shifts of Backbone Amides in Bovine Pancreatic Trypsin Inhibitor and Apamin [Additions and Corrections to J. Am. Chem. Soc. 1989 111,7716-7722],"" J. Am. Chem. Soc. 112 (7), 2843-2843 (1990).","15N Chemical Shifts of Backbone Amides in Bovine Pancreatic Trypsin Inhibitor and Apamin [Additions and Corrections to J. Am. Chem. Soc. 1989 111,7716-7722]",published,journal,J. Am. Chem. Soc.,,112,7,,,,,,,,,,,,,,,,,,,,,,2843,2843,1990, citations,ref_2,4853,208241,3,,reference citation,,,9917409,,"Krimm, I. et al (1999) NMR Structures and Activity of a Novel Alpha-Like Toxin from the Scorpion Leiurus quinquestriatus hebraeus. J. Mol. Biol., 285: 1749-1763.",NMR structures and activity of a novel alpha-like toxin from the scorpion Leiurus quinquestriatus hebraeus.,published,journal,J. Mol. Biol.,Journal of molecular biology,285,4,,0022-2836,,,,,,,,,,,,,,,,,,,,1749,1763,1999,"NMR structures of a new toxin from the scorpion Leiurus quinquestriatus hebraeus (Lqh III) have been investigated in conjunction with its pharmacological properties. This toxin is proposed to belong to a new group of scorpion toxins, the alpha-like toxins that target voltage-gated sodium channels with specific properties compared with the classical alpha-scorpion toxins. Electrophysiological analysis showed that Lqh III inhibits a sodium current inactivation in the cockroach axon, but induces in addition a resting depolarization due to a slowly decaying tail current atypical to other alpha-toxin action. Binding studies indicated that radiolabeled Lqh III binds with a high degree of affinity (Ki=2.2 nM) on cockroach sodium channels and that the alpha-toxin from L quinquestriatus hebraeus highly active on insects (LqhalphaIT) and alpha-like toxins compete at low concentration for its receptor binding site, suggesting that the alpha-like toxin receptor site is partially overlapping with the receptor site 3. Conversely, in rat brain, Lqh III competes for binding of the most potent anti-mammal alpha-toxin from Androctonus australis Hector venom (AaH II) only at very high concentration.The NMR structures were used for the scrutiny of the similarities and differences with representative scorpion alpha-toxins targeting the voltage-gated sodium channels of either mammals or insects. Three turn regions involved in the functional binding site of the anti-insect LqhalphaIT toxin reveal significant differences in the Lqh III structure. The electrostatic charge distribution in the Lqh III toxin is also surprisingly different when compared with the anti-mammal alpha-toxin AaH II. Similarities in the electrostatic charge distribution are, however, recognized between alpha-toxins highly active on insects and the alpha-like toxin Lqh III. This affords additional important elements to the definition of the new alpha-like group of scorpion toxins and the mammal versus insect scorpion toxin selectivities." citations,entry_citation,4854,208260,1,,entry citation,,21447269,11563562,,,"Letter to the Editor: Sequential Assignments of the Isolated N-terminal Domain of 5-Enolpyruvylshikimate-3-phosphate Synthase",published,journal,J. Biomol. NMR,,20,4,,,,,,,,,,,,,,,,,,,,,,387,388,2001, citations,entry_citation,4855,208282,1,,entry citation,,92071963,,,,"(14-38, 30-51) Double-disulphide intermediate in folding of Bovine Pancreatic Trypsin Inhibitor: A two-dimensional 1H nuclear magnetic resonance study",published,journal,J. Mol. Biol.,,222,,,,,,,,,,,,,,,,,,,,,,,353,371,1991, citations,ref_1,4855,208283,2,,reference citation,,,1960731,,"van Mierlo CP, Darby NJ, Neuhaus D, Creighton TE. (14-38, 30-51) double-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor: a two-dimensional 1H nuclear magnetic resonance study. J Mol Biol. 1991 Nov 20;222(2):353-71.","(14-38, 30-51) double-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor: a two-dimensional 1H nuclear magnetic resonance study.",published,journal,J. Mol. Biol.,Journal of molecular biology,222,2,,0022-2836,,,,,,,,,,,,,,,,,,,,353,371,1991,"An analogue of the BPTI folding intermediate that contains only the disulphide bonds between Cys14 and Cys38 and between Cys30 and Cys51 has been prepared in Escherichia coli by protein engineering methods. The other two Cys residues of native BPTI (at positions 5 and 55) have been replaced by Ser. Essentially complete proton resonance assignments of the analogue were obtained by employing two-dimensional 1H nuclear magnetic resonance techniques. The intermediate has a more extended conformation in the N-terminal (residues 1 to 7) region and there are other differences in the C-terminal (residues 55 to 58) region. The remainder of the protein is substantially identical to native BPTI. The conformational properties of the analogue can explain several aspects of the kinetic role that the normal (14-38, 30-51) intermediate plays in the folding of BPTI." citations,ref_2,4855,208284,3,,reference citation,,,1960732,,"van Mierlo CP, Darby NJ, Neuhaus D, Creighton TE. Two-dimensional 1H nuclear magnetic resonance study of the (5-55) single-disulphide folding intermediate of bovine pancreatic trypsin inhibitor. J Mol Biol. 1991 Nov 20;222(2):373-90.",Two-dimensional 1H nuclear magnetic resonance study of the (5-55) single-disulphide folding intermediate of bovine pancreatic trypsin inhibitor.,published,journal,J. Mol. Biol.,Journal of molecular biology,222,2,,0022-2836,,,,,,,,,,,,,,,,,,,,373,390,1991,"An analogue of the bovine pancreatic trypsin inhibitor (BPTI) folding intermediate that contains only the disulphide bond between Cys5 and Cys55 has been prepared in Escherichia coli by protein engineering methods, with the other four Cys residues replaced by Ser. Two-dimensional 1H nuclear magnetic resonance studies of the analogue have resulted in essentially complete resonance assignments of the folded form of the protein. The folded protein has a compact conformation that is structurally very similar to that of native BPTI, although there are subtle differences and the folded conformation is not very stable. Approximately half of the protein molecules are unfolded at 3 degrees C, and this proportion increases at higher temperatures. The folded and unfolded conformations are in slow exchange. The conformational properties of the analogue can explain many aspects of the kinetic role that the normal (5-55) intermediate plays in the folding of BPTI." citations,ref_3,4855,208285,4,,reference citation,,,1373775,,"Darby NJ, van Mierlo CP, Scott GH, Neuhaus D, Creighton TE. Kinetic roles and conformational properties of the non-native two-disulphide intermediates in the refolding of bovine pancreatic trypsin inhibitor. J Mol Biol. 1992 Apr 20;224(4):905-11.",Kinetic roles and conformational properties of the non-native two-disulphide intermediates in the refolding of bovine pancreatic trypsin inhibitor.,published,journal,J. Mol. Biol.,Journal of molecular biology,224,4,,0022-2836,,,,,,,,,,,,,,,,,,,,905,911,1992,"The most productive folding pathway of reduced bovine pancreatic trypsin inhibitor (BPTI) proceeds through the disulphide intermediates (30-51), (30-51, 5-14), and (30-51, 5-38); these are important kinetic intermediates in folding, even though the latter pair contain non-native disulphide bonds. Analogues of these intermediates have been prepared by protein engineering methods and their conformational properties examined by circular dichroism and 1H-nuclear magnetic resonance. The (30-51), (30-51, 5-14) and (30-51, 5-38) analogues exhibit comparable degrees of stable structure, which cannot include those portions of the polypeptide chain involving Cys5, Cys14 and Cys38. These properties are consistent with the roles of (30-51, 5-14) and (30-51, 5-38) in the folding pathway of BPTI, which demand that they exhibit a considerable degree of conformational flexibility in part of the molecule." citations,entry_citation,4864,208460,1,,entry citation,,,,,,"NMR Chemical shift mapping of the binding site of a protein proteinase inhibitor: changes in the 1H, 13C and 15N NMR chemical shifts of turkey ovomucoid third domain upon binding to bovine chymotrypsin Aa",published,journal,J. Mol. Recognit.,,14,,,,,,,,,,,,,,,,,,,,,,,166,171,2001, citations,entry_citation,4865,208473,1,,entry citation,,,,,,"NMR Chemical shift mapping of the binding site of a protein proteinase inhibitor: changes in the 1H, 13C and 15N NMR chemical shifts of turkey ovomucoid third domain upon binding to bovine chymotrypsin Aa",published,journal,J. Mol. Recognit.,,14,,,,,,,,,,,,,,,,,,,,,,,166,171,2001, citations,entry_citation,4866,208490,1,,entry citation,,,,,,"Letter to the Editor: Backbone resonance assignment of human UBC4",published,journal,J. Biomol. NMR,,18,4,,,,,,,,,,,,,,,,,,,,,,363,364,2000, citations,entry_citation,4867,208510,1,,entry citation,,,11118222,,,"Molecular Basis of Sequence-specific Recognition of Pre-ribosomal RNA by Nucleolin",published,journal,EMBO Journal,,19,24,,,,,,,,,,,,,,,,,,,,,,6870,6881,2000, citations,ref_4,4855,208286,5,,reference citation,,,1379719,,"van Mierlo CP, Darby NJ, Creighton TE. The partially folded conformation of the Cys-30 Cys-51 intermediate in the disulfide folding pathway of bovine pancreatic trypsin inhibitor. Proc Natl Acad Sci U S A. 1992 Aug 1;89(15):6775-9.",The partially folded conformation of the Cys-30 Cys-51 intermediate in the disulfide folding pathway of bovine pancreatic trypsin inhibitor.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,89,15,,0027-8424,,,,,,,,,,,,,,,,,,,,6775,6779,1992,"The best-characterized protein folding pathway is that of bovine pancreatic trypsin inhibitor, which folds from the reduced form through a series of disulfide bond intermediates. The crucial one-disulfide intermediate of bovine pancreatic trypsin inhibitor with the disulfide bond between Cys-30 and Cys-51 is shown here to have a partially folded conformation in which the major elements of secondary structure interact via a core of apolar side chains, which resembles part of the native conformation. The stability of this structure can account for the predominance of this one-disulfide intermediate during folding. Much of the remaining one-third of the polypeptide chain, in particular the N-terminal 14 residues, is largely disordered; this accounts for the ability of this intermediate to form readily any of the three possible second disulfide bonds involving Cys-5, -14, and -38. The partially folded conformation of this intermediate provides direct evidence for the importance of native-like interactions between elements of secondary structure in directing protein folding, which is assumed in many studies." citations,ref_5,4855,208287,6,,reference citation,,,7680380,,"van Mierlo CP, Darby NJ, Keeler J, Neuhaus D, Creighton TE. Partially folded conformation of the (30-51) intermediate in the disulphide folding pathway of bovine pancreatic trypsin inhibitor. 1H and 15N resonance assignments and determination of backbone dynamics from 15N relaxation measurements. J Mol Biol. 1993 Feb 20;229(4):1125-46.",Partially folded conformation of the (30-51) intermediate in the disulphide folding pathway of bovine pancreatic trypsin inhibitor. 1H and 15N resonance assignments and determination of backbone dynamics from 15N relaxation measurements.,published,journal,J. Mol. Biol.,Journal of molecular biology,229,4,,0022-2836,,,,,,,,,,,,,,,,,,,,1125,1146,1993,"An analogue of the important folding intermediate of BPTI with only the disulphide bond between Cys30 and Cys51 has been characterized by 1H and 15N NMR techniques. In particular, the dynamics of the polypeptide backbone were characterized using (1H)-15N NOE and 15N T1 and T2 relaxation data. The intermediate is partially folded, with part of the polypeptide chain stably folded and the remainder flexible or unfolded. The folded portion consists of the major elements of native-like secondary structure interacting through the hydrophobic core of the molecule. The 15N relaxation data show that the N-terminal 15 residues are very flexible, and the (1H, 1H) NOESY data show that these residues have no NOE interactions with the remainder of the molecule. The segment of residues 37 to 41 is also flexible. These observations explain why during folding this intermediate most readily forms any of the possible disulphide bonds between Cys5, Cys14 and Cys38, including the non-native 5-14 and 5-38 bonds. The native-like folded portion of the molecule limits the possible disulphide bonds that can be formed to those in the remainder of the polypeptide chain. Also, forming the non-native disulphide bonds need not involve any disruption of that folded structure, as the Cys residues involved are in flexible regions of the molecule." citations,ref_6,4855,208288,7,,reference citation,,,7507172,,"van Mierlo CP, Kemmink J, Neuhaus D, Darby NJ, Creighton TE. 1H NMR analysis of the partly-folded non-native two-disulphide intermediates (30-51,5-14) and (30-51,5-38) in the folding pathway of bovine pancreatic trypsin inhibitor. J Mol Biol. 1994 Jan 21;235(3):1044-61.","1H NMR analysis of the partly-folded non-native two-disulphide intermediates (30-51,5-14) and (30-51,5-38) in the folding pathway of bovine pancreatic trypsin inhibitor.",published,journal,J. Mol. Biol.,Journal of molecular biology,235,3,,0022-2836,,,,,,,,,,,,,,,,,,,,1044,1061,1994,"The conformational properties of analogues of the (30-51,5-14) and (30-51,5-38) disulphide intermediates in refolding of reduced BPTI, with non-native second disulphide bonds, have been characterized in detail by 1H NMR analysis. They are shown to have partly-folded conformations, very similar to that of the (30-51) one-disulphide intermediate from which they arise during folding. The non-native disulphide bonds are formed in flexible or unfolded parts of the polypeptide chain; they do not disrupt the folded portion nor do they introduce substantial non-native conformation. The conformational properties of these intermediates explain their important roles in the folding pathway." citations,entry_citation,4856,208309,1,,entry citation,,21518228,11606065,,,Structural Insight into Human Zn(2+)-bound S100A2 from NMR and Homology Modeling,published,journal,Biochem. Biophys. Res. Commun.,,288,2,,,,,,,,,,,,,,,,,,,,,,462,467,2001, citations,ref_1,4856,208310,2,,reference citation,,,2928325,,"Proline isomerism leads to multiple folded conformations of calbindin D9k: direct evidence from two-dimensional 1H NMR specrtoscopy. Proc Natl Acad Sci USA. 1989 Apr;86(7):2195-8",Proline isomerism leads to multiple folded conformations of calbindin D9k: direct evidence from two-dimensional 1H NMR spectroscopy.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,86,7,,0027-8424,,,,,,,,,,,,,,,,,,,,2195,2198,1989,"A complete analysis of calbindin D9k by two-dimensional 1H nuclear magnetic resonance spectroscopy has established the existence of two conformations for the folded protein in solution. Well-resolved major and minor resonances in a ratio of 3:1 are observed throughout the 1H NMR spectrum. Two-dimensional exchange experiments show that the major and minor species are related by an equilibrium process. Analysis of short proton-proton distances along the peptide backbone, identified by two-dimensional nuclear Overhauser effect spectroscopy, provides unambiguous evidence that the two forms of the folded protein differ only in the isomerization state of the peptide bond between Gly-42 and Pro-43. Cis-trans isomerism of Pro-43 is thereby directly identified as the cause of multiple conformations for the folded protein in solution. In addition, when Pro-43 is mutated to a glycine residue there is no indication of multiple conformations. These results provide evidence for the possibility of conformational heterogeneity in the native state of globular proteins." citations,entry_citation,4857,208329,1,,entry citation,,,,,,"Solution structure and dynamic character of the histidine-containing phosphotransfer domain of anaerobic sensor kinase ArcB from Escherichia coli",in press,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4858,208346,1,,entry citation,,20481411,11023788,,,"Solution Strcuture of the two N-terminal RNA-binding Domains of Nucleolin and NMR Study of the Interaction with its RNA Target",published,journal,J. Mol. Biol.,,303,2,,,,,,,,,,,,,,,,,,,,,,227,241,2000, citations,entry_citation,4859,208364,1,,entry citation,,20137989,10672009,,,High Resolution Solution Structure of the Protein Part of Cu7 Metallothionein,published,journal,Eur. J. Biochem.,,267,,,,,,,,,,,,,,,,,,,,,,,1008,1018,2000, citations,entry_citation,486,208386,1,,entry citation,,,,,"Neri, Dario, Otting, Gottfried, Wuthrich, Kurt, ""1H and 13C NMR Chemical Shifts of the Diastereotopic Methyl Groups of Valyl and Leucyl Residues in Peptides and Proteins,"" Tetrahedron 46 (9), 3287-3296 (1990).","1H and 13C NMR Chemical Shifts of the Diastereotopic Methyl Groups of Valyl and Leucyl Residues in Peptides and Proteins",published,journal,Tetrahedron,,46,9,,,,,,,,,,,,,,,,,,,,,,3287,3296,1990, citations,ref_1,4868,208533,2,,reference citation,,,1960732,,"van Mierlo CP, Darby NJ, Neuhaus D, Creighton TE. Two-dimensional 1H nuclear magnetic resonance study of the (5-55) single-disulphide folding intermediate of bovine pancreatic trypsin inhibitor. J Mol Biol. 1991 Nov 20;222(2):373-90.",Two-dimensional 1H nuclear magnetic resonance study of the (5-55) single-disulphide folding intermediate of bovine pancreatic trypsin inhibitor.,published,journal,J. Mol. Biol.,Journal of molecular biology,222,2,,0022-2836,,,,,,,,,,,,,,,,,,,,373,390,1991,"An analogue of the bovine pancreatic trypsin inhibitor (BPTI) folding intermediate that contains only the disulphide bond between Cys5 and Cys55 has been prepared in Escherichia coli by protein engineering methods, with the other four Cys residues replaced by Ser. Two-dimensional 1H nuclear magnetic resonance studies of the analogue have resulted in essentially complete resonance assignments of the folded form of the protein. The folded protein has a compact conformation that is structurally very similar to that of native BPTI, although there are subtle differences and the folded conformation is not very stable. Approximately half of the protein molecules are unfolded at 3 degrees C, and this proportion increases at higher temperatures. The folded and unfolded conformations are in slow exchange. The conformational properties of the analogue can explain many aspects of the kinetic role that the normal (5-55) intermediate plays in the folding of BPTI." citations,ref_2,4868,208534,3,,reference citation,,,1704858,,"Darby NJ, van Mierlo CP, Creighton TE. The 5-55 single-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor. FEBS Lett. 1991 Feb 11;279(1):61-4.",The 5-55 single-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor.,published,journal,FEBS Lett.,FEBS letters,279,1,,0014-5793,,,,,,,,,,,,,,,,,,,,61,64,1991,"An analogue of the BPT1 folding intermediate that contains only the disulphide bond between Cys-5 and Cys-55 has been prepared by mutation of the other four Cys residues to Ser. On the basis of its circular dichroism and 1H-nuclear magnetic resonance spectra and its electrophoretic mobility, this intermediate is shown to be at least partially folded at low temperatures. This probably accounts for several of the unique properties of this intermediate observed during folding." citations,ref_3,4868,208535,4,,reference citation,,,1960731,,"van Mierlo CP, Darby NJ, Neuhaus D, Creighton TE. (14-38, 30-51) double-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor: a two-dimensional 1H nuclear magnetic resonance study. J Mol Biol. 1991 Nov 20;222(2):353-71.","(14-38, 30-51) double-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor: a two-dimensional 1H nuclear magnetic resonance study.",published,journal,J. Mol. Biol.,Journal of molecular biology,222,2,,0022-2836,,,,,,,,,,,,,,,,,,,,353,371,1991,"An analogue of the BPTI folding intermediate that contains only the disulphide bonds between Cys14 and Cys38 and between Cys30 and Cys51 has been prepared in Escherichia coli by protein engineering methods. The other two Cys residues of native BPTI (at positions 5 and 55) have been replaced by Ser. Essentially complete proton resonance assignments of the analogue were obtained by employing two-dimensional 1H nuclear magnetic resonance techniques. The intermediate has a more extended conformation in the N-terminal (residues 1 to 7) region and there are other differences in the C-terminal (residues 55 to 58) region. The remainder of the protein is substantially identical to native BPTI. The conformational properties of the analogue can explain several aspects of the kinetic role that the normal (14-38, 30-51) intermediate plays in the folding of BPTI." citations,ref_4,4868,208536,5,,reference citation,,,1373775,,"Darby NJ, van Mierlo CP, Scott GH, Neuhaus D, Creighton TE. Kinetic roles and conformational properties of the non-native two-disulphide intermediates in the refolding of bovine pancreatic trypsin inhibitor. J Mol Biol. 1992 Apr 20;224(4):905-11.",Kinetic roles and conformational properties of the non-native two-disulphide intermediates in the refolding of bovine pancreatic trypsin inhibitor.,published,journal,J. Mol. Biol.,Journal of molecular biology,224,4,,0022-2836,,,,,,,,,,,,,,,,,,,,905,911,1992,"The most productive folding pathway of reduced bovine pancreatic trypsin inhibitor (BPTI) proceeds through the disulphide intermediates (30-51), (30-51, 5-14), and (30-51, 5-38); these are important kinetic intermediates in folding, even though the latter pair contain non-native disulphide bonds. Analogues of these intermediates have been prepared by protein engineering methods and their conformational properties examined by circular dichroism and 1H-nuclear magnetic resonance. The (30-51), (30-51, 5-14) and (30-51, 5-38) analogues exhibit comparable degrees of stable structure, which cannot include those portions of the polypeptide chain involving Cys5, Cys14 and Cys38. These properties are consistent with the roles of (30-51, 5-14) and (30-51, 5-38) in the folding pathway of BPTI, which demand that they exhibit a considerable degree of conformational flexibility in part of the molecule." citations,ref_5,4868,208537,6,,reference citation,,,1379719,,"van Mierlo CP, Darby NJ, Creighton TE. The partially folded conformation of the Cys-30 Cys-51 intermediate in the disulfide folding pathway of bovine pancreatic trypsin inhibitor. Proc Natl Acad Sci U S A. 1992 Aug 1;89(15):6775-9.",The partially folded conformation of the Cys-30 Cys-51 intermediate in the disulfide folding pathway of bovine pancreatic trypsin inhibitor.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,89,15,,0027-8424,,,,,,,,,,,,,,,,,,,,6775,6779,1992,"The best-characterized protein folding pathway is that of bovine pancreatic trypsin inhibitor, which folds from the reduced form through a series of disulfide bond intermediates. The crucial one-disulfide intermediate of bovine pancreatic trypsin inhibitor with the disulfide bond between Cys-30 and Cys-51 is shown here to have a partially folded conformation in which the major elements of secondary structure interact via a core of apolar side chains, which resembles part of the native conformation. The stability of this structure can account for the predominance of this one-disulfide intermediate during folding. Much of the remaining one-third of the polypeptide chain, in particular the N-terminal 14 residues, is largely disordered; this accounts for the ability of this intermediate to form readily any of the three possible second disulfide bonds involving Cys-5, -14, and -38. The partially folded conformation of this intermediate provides direct evidence for the importance of native-like interactions between elements of secondary structure in directing protein folding, which is assumed in many studies." citations,ref_2,4873,208660,3,,reference citation,,,1704858,,"Darby NJ, van Mierlo CP, Creighton TE. The 5-55 single-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor. FEBS Lett. 1991 Feb 11;279(1):61-4.",The 5-55 single-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor.,published,journal,FEBS Lett.,FEBS letters,279,1,,0014-5793,,,,,,,,,,,,,,,,,,,,61,64,1991,"An analogue of the BPT1 folding intermediate that contains only the disulphide bond between Cys-5 and Cys-55 has been prepared by mutation of the other four Cys residues to Ser. On the basis of its circular dichroism and 1H-nuclear magnetic resonance spectra and its electrophoretic mobility, this intermediate is shown to be at least partially folded at low temperatures. This probably accounts for several of the unique properties of this intermediate observed during folding." citations,ref_6,4868,208538,7,,reference citation,,,7680380,,"van Mierlo CP, Darby NJ, Keeler J, Neuhaus D, Creighton TE. Partially folded conformation of the (30-51) intermediate in the disulphide folding pathway of bovine pancreatic trypsin inhibitor. 1H and 15N resonance assignments and determination of backbone dynamics from 15N relaxation measurements. J Mol Biol. 1993 Feb 20;229(4):1125-46.",Partially folded conformation of the (30-51) intermediate in the disulphide folding pathway of bovine pancreatic trypsin inhibitor. 1H and 15N resonance assignments and determination of backbone dynamics from 15N relaxation measurements.,published,journal,J. Mol. Biol.,Journal of molecular biology,229,4,,0022-2836,,,,,,,,,,,,,,,,,,,,1125,1146,1993,"An analogue of the important folding intermediate of BPTI with only the disulphide bond between Cys30 and Cys51 has been characterized by 1H and 15N NMR techniques. In particular, the dynamics of the polypeptide backbone were characterized using (1H)-15N NOE and 15N T1 and T2 relaxation data. The intermediate is partially folded, with part of the polypeptide chain stably folded and the remainder flexible or unfolded. The folded portion consists of the major elements of native-like secondary structure interacting through the hydrophobic core of the molecule. The 15N relaxation data show that the N-terminal 15 residues are very flexible, and the (1H, 1H) NOESY data show that these residues have no NOE interactions with the remainder of the molecule. The segment of residues 37 to 41 is also flexible. These observations explain why during folding this intermediate most readily forms any of the possible disulphide bonds between Cys5, Cys14 and Cys38, including the non-native 5-14 and 5-38 bonds. The native-like folded portion of the molecule limits the possible disulphide bonds that can be formed to those in the remainder of the polypeptide chain. Also, forming the non-native disulphide bonds need not involve any disruption of that folded structure, as the Cys residues involved are in flexible regions of the molecule." citations,ref_7,4868,208539,8,,reference citation,,,7507172,,"van Mierlo CP, Kemmink J, Neuhaus D, Darby NJ, Creighton TE. 1H NMR analysis of the partly-folded non-native two-disulphide intermediates (30-51,5-14) and (30-51,5-38) in the folding pathway of bovine pancreatic trypsin inhibitor. J Mol Biol. 1994 Jan 21;235(3):1044-61.","1H NMR analysis of the partly-folded non-native two-disulphide intermediates (30-51,5-14) and (30-51,5-38) in the folding pathway of bovine pancreatic trypsin inhibitor.",published,journal,J. Mol. Biol.,Journal of molecular biology,235,3,,0022-2836,,,,,,,,,,,,,,,,,,,,1044,1061,1994,"The conformational properties of analogues of the (30-51,5-14) and (30-51,5-38) disulphide intermediates in refolding of reduced BPTI, with non-native second disulphide bonds, have been characterized in detail by 1H NMR analysis. They are shown to have partly-folded conformations, very similar to that of the (30-51) one-disulphide intermediate from which they arise during folding. The non-native disulphide bonds are formed in flexible or unfolded parts of the polypeptide chain; they do not disrupt the folded portion nor do they introduce substantial non-native conformation. The conformational properties of these intermediates explain their important roles in the folding pathway." citations,entry_citation,4869,208555,1,,entry citation,,99246280,10228169,,,"Solution Structure of the Hmg Protein Nhp6A and its Interaction with DNA Reveals the Structural Determinants for Non-sequence-specific Binding",published,journal,EMBO J.,,18,9,,,,,,,,,,,,,,,,,,,,,,2563,2579,1999, citations,entry_citation,4870,208579,1,,entry citation,,,,,,"Letter to the Editor: Sequence-specific 1H, 15N, and 13C resonance assignments for the whole region 4 of Escherichia coli RNA polymerase sigma70 subunit",published,journal,J. Biomol. NMR,,20,2,,,,,,,,,,,,,,,,,,,,,,181,182,2001, citations,ref_1,4870,208580,2,,reference citation,,82014879,,,"Burton Z, Burgess RR, Lin J, Moore D, Holder S, Gross CA. The nucleotide sequence of the cloned rpoD gene for the RNA polymerase sigma subunit from E coli K12. Nucleic Acids Res. 1981 Jun 25;9(12):2889-903.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_2,4870,208581,3,,reference citation,,96088118,,,"Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR. 1995 Nov;6(3):277-93.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_3,4870,208582,4,,reference citation,,,,,"Bartels,CH; Xia,T-H; Billeter,M; Guntert,P; Wuthrich,K. (1995) The program XEASY for computer-supported NMR specreal analysis pf biological macromolecules. J. Biomol. NMR 5,1-10",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_4,4870,208583,5,,reference citation,,96173087,,,"Wishart DS, Bigam CG, Yao J, Abildgaard F, Dyson HJ, Oldfield E, Markley JL, Sykes BD. 1H, 13C and 15N chemical shift referencing in biomolecular NMR. J Biomol NMR. 1995 Sep;6(2):135-40.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4871,208615,1,,entry citation,,21151323,11256816,,,"1H, 13C and 15N Resonance Assignments and Secondary Structure of the c-Myc Binding Domain (MBD) and the SH3 Domain of the Tumor Suppressor Bin1",published,journal,J. Biomol. NMR,,19,2,,,,,,,,,,,,,,,,,,,,,,191,192,2001, citations,entry_citation,4872,208637,1,,entry citation,,11041845,,,,"Interhelical Ion Pairing in Coiled Coils: Solution Structure of a Heterodimeric Leucine Zipper and Determination of pKa Values of Glu Side Chains",published,journal,Biochemistry,,39,,,,,,,,,,,,,,,,,,,,,,,12804,12818,2000, citations,entry_citation,4873,208658,1,,entry citation,,93188004,,,,"Partially folded conformation of the (30-51) intermediate in the disulphide folding pathway of bovine pancreatic trypsin inhibitor. 1H and 15N resonance assignments and determination of backbone dynamics from 15N relaxation measurements.",published,journal,J. Mol. Biol.,,229,,,,,,,,,,,,,,,,,,,,,,,1125,1146,1993, citations,ref_1,4873,208659,2,,reference citation,,,1960732,,"van Mierlo CP, Darby NJ, Neuhaus D, Creighton TE. Two-dimensional 1H nuclear magnetic resonance study of the (5-55) single-disulphide folding intermediate of bovine pancreatic trypsin inhibitor. J Mol Biol. 1991 Nov 20;222(2):373-90",Two-dimensional 1H nuclear magnetic resonance study of the (5-55) single-disulphide folding intermediate of bovine pancreatic trypsin inhibitor.,published,journal,J. Mol. Biol.,Journal of molecular biology,222,2,,0022-2836,,,,,,,,,,,,,,,,,,,,373,390,1991,"An analogue of the bovine pancreatic trypsin inhibitor (BPTI) folding intermediate that contains only the disulphide bond between Cys5 and Cys55 has been prepared in Escherichia coli by protein engineering methods, with the other four Cys residues replaced by Ser. Two-dimensional 1H nuclear magnetic resonance studies of the analogue have resulted in essentially complete resonance assignments of the folded form of the protein. The folded protein has a compact conformation that is structurally very similar to that of native BPTI, although there are subtle differences and the folded conformation is not very stable. Approximately half of the protein molecules are unfolded at 3 degrees C, and this proportion increases at higher temperatures. The folded and unfolded conformations are in slow exchange. The conformational properties of the analogue can explain many aspects of the kinetic role that the normal (5-55) intermediate plays in the folding of BPTI." citations,ref_1,4880,208834,2,,reference citation,,,8589602,,"J. Biomol. NMR (1995) 6, 135-140 Wishart, D.S., Bigam, C.G., Yao, J., Abildgaard, F., Dyson, H.J., Oldfield, E., Markley, J.L. and Sykes, B.D.","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,ref_3,4873,208661,4,,reference citation,,,1960731,,"van Mierlo CP, Darby NJ, Neuhaus D, Creighton TE. (14-38, 30-51) double-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor: a two-dimensional 1H nuclear magnetic resonance study. J Mol Biol. 1991 Nov 20;222(2):353-71.","(14-38, 30-51) double-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor: a two-dimensional 1H nuclear magnetic resonance study.",published,journal,J. Mol. Biol.,Journal of molecular biology,222,2,,0022-2836,,,,,,,,,,,,,,,,,,,,353,371,1991,"An analogue of the BPTI folding intermediate that contains only the disulphide bonds between Cys14 and Cys38 and between Cys30 and Cys51 has been prepared in Escherichia coli by protein engineering methods. The other two Cys residues of native BPTI (at positions 5 and 55) have been replaced by Ser. Essentially complete proton resonance assignments of the analogue were obtained by employing two-dimensional 1H nuclear magnetic resonance techniques. The intermediate has a more extended conformation in the N-terminal (residues 1 to 7) region and there are other differences in the C-terminal (residues 55 to 58) region. The remainder of the protein is substantially identical to native BPTI. The conformational properties of the analogue can explain several aspects of the kinetic role that the normal (14-38, 30-51) intermediate plays in the folding of BPTI." citations,ref_4,4873,208662,5,,reference citation,,,1373775,,"Darby NJ, van Mierlo CP, Scott GH, Neuhaus D, Creighton TE. Kinetic roles and conformational properties of the non-native two-disulphide intermediates in the refolding of bovine pancreatic trypsin inhibitor. J Mol Biol. 1992 Apr 20;224(4):905-11.",Kinetic roles and conformational properties of the non-native two-disulphide intermediates in the refolding of bovine pancreatic trypsin inhibitor.,published,journal,J. Mol. Biol.,Journal of molecular biology,224,4,,0022-2836,,,,,,,,,,,,,,,,,,,,905,911,1992,"The most productive folding pathway of reduced bovine pancreatic trypsin inhibitor (BPTI) proceeds through the disulphide intermediates (30-51), (30-51, 5-14), and (30-51, 5-38); these are important kinetic intermediates in folding, even though the latter pair contain non-native disulphide bonds. Analogues of these intermediates have been prepared by protein engineering methods and their conformational properties examined by circular dichroism and 1H-nuclear magnetic resonance. The (30-51), (30-51, 5-14) and (30-51, 5-38) analogues exhibit comparable degrees of stable structure, which cannot include those portions of the polypeptide chain involving Cys5, Cys14 and Cys38. These properties are consistent with the roles of (30-51, 5-14) and (30-51, 5-38) in the folding pathway of BPTI, which demand that they exhibit a considerable degree of conformational flexibility in part of the molecule." citations,ref_5,4873,208663,6,,reference citation,,,1379719,,"van Mierlo CP, Darby NJ, Creighton TE. The partially folded conformation of the Cys-30 Cys-51 intermediate in the disulfide folding pathway of bovine pancreatic trypsin inhibitor. Proc Natl Acad Sci U S A. 1992 Aug 1;89(15):6775-9.",The partially folded conformation of the Cys-30 Cys-51 intermediate in the disulfide folding pathway of bovine pancreatic trypsin inhibitor.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,89,15,,0027-8424,,,,,,,,,,,,,,,,,,,,6775,6779,1992,"The best-characterized protein folding pathway is that of bovine pancreatic trypsin inhibitor, which folds from the reduced form through a series of disulfide bond intermediates. The crucial one-disulfide intermediate of bovine pancreatic trypsin inhibitor with the disulfide bond between Cys-30 and Cys-51 is shown here to have a partially folded conformation in which the major elements of secondary structure interact via a core of apolar side chains, which resembles part of the native conformation. The stability of this structure can account for the predominance of this one-disulfide intermediate during folding. Much of the remaining one-third of the polypeptide chain, in particular the N-terminal 14 residues, is largely disordered; this accounts for the ability of this intermediate to form readily any of the three possible second disulfide bonds involving Cys-5, -14, and -38. The partially folded conformation of this intermediate provides direct evidence for the importance of native-like interactions between elements of secondary structure in directing protein folding, which is assumed in many studies." citations,ref_6,4873,208664,7,,reference citation,,,7680380,,"van Mierlo CP, Darby NJ, Keeler J, Neuhaus D, Creighton TE. Partially folded conformation of the (30-51) intermediate in the disulphide folding pathway of bovine pancreatic trypsin inhibitor. 1H and 15N resonance assignments and determination of backbone dynamics from 15N relaxation measurements. J Mol Biol. 1993 Feb 20;229(4):1125-46.",Partially folded conformation of the (30-51) intermediate in the disulphide folding pathway of bovine pancreatic trypsin inhibitor. 1H and 15N resonance assignments and determination of backbone dynamics from 15N relaxation measurements.,published,journal,J. Mol. Biol.,Journal of molecular biology,229,4,,0022-2836,,,,,,,,,,,,,,,,,,,,1125,1146,1993,"An analogue of the important folding intermediate of BPTI with only the disulphide bond between Cys30 and Cys51 has been characterized by 1H and 15N NMR techniques. In particular, the dynamics of the polypeptide backbone were characterized using (1H)-15N NOE and 15N T1 and T2 relaxation data. The intermediate is partially folded, with part of the polypeptide chain stably folded and the remainder flexible or unfolded. The folded portion consists of the major elements of native-like secondary structure interacting through the hydrophobic core of the molecule. The 15N relaxation data show that the N-terminal 15 residues are very flexible, and the (1H, 1H) NOESY data show that these residues have no NOE interactions with the remainder of the molecule. The segment of residues 37 to 41 is also flexible. These observations explain why during folding this intermediate most readily forms any of the possible disulphide bonds between Cys5, Cys14 and Cys38, including the non-native 5-14 and 5-38 bonds. The native-like folded portion of the molecule limits the possible disulphide bonds that can be formed to those in the remainder of the polypeptide chain. Also, forming the non-native disulphide bonds need not involve any disruption of that folded structure, as the Cys residues involved are in flexible regions of the molecule." citations,ref_7,4873,208665,8,,reference citation,,,7507172,,"van Mierlo CP, Kemmink J, Neuhaus D, Darby NJ, Creighton TE. 1H NMR analysis of the partly-folded non-native two-disulphide intermediates (30-51,5-14) and (30-51,5-38) in the folding pathway of bovine pancreatic trypsin inhibitor. J Mol Biol. 1994 Jan 21;235(3):1044-61.","1H NMR analysis of the partly-folded non-native two-disulphide intermediates (30-51,5-14) and (30-51,5-38) in the folding pathway of bovine pancreatic trypsin inhibitor.",published,journal,J. Mol. Biol.,Journal of molecular biology,235,3,,0022-2836,,,,,,,,,,,,,,,,,,,,1044,1061,1994,"The conformational properties of analogues of the (30-51,5-14) and (30-51,5-38) disulphide intermediates in refolding of reduced BPTI, with non-native second disulphide bonds, have been characterized in detail by 1H NMR analysis. They are shown to have partly-folded conformations, very similar to that of the (30-51) one-disulphide intermediate from which they arise during folding. The non-native disulphide bonds are formed in flexible or unfolded parts of the polypeptide chain; they do not disrupt the folded portion nor do they introduce substantial non-native conformation. The conformational properties of these intermediates explain their important roles in the folding pathway." citations,entry_citation,4874,208692,1,,entry citation,,,,,,"Letter to the editor: Sequence-specific assignment of the PAH2 domain of Sin3B free and bound to Mad1",published,journal,J. Biomol. NMR,,19,4,,,,,,,,,,,,,,,,,,,,,,377,378,2001, citations,citation_1,4874,208693,2,,reference citation,,,8520220,,"Delaglio, F. et al. J. Biomol. NMR 6, 277-293 (1995)",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,citation_2,4874,208694,3,,reference citation,,,,,"Ch. Bartels, et al. J. Biomol. NMR 6, 1-10 (1995).",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4875,208709,1,,entry citation,,94118338,,,,"1H NMR Analysis of the partly-folded non-native two-disulphide intermediates (30-51, 5-14) and (30-51, 5-38) in the folding pathway of bovine pancreatic trypsin inhibitor",published,journal,J. Mol. Biol.,,235,,,,,,,,,,,,,,,,,,,,,,,1044,1061,1994, citations,ref_1,4875,208710,2,,reference citation,,,1960732,,"van Mierlo CP, Darby NJ, Neuhaus D, Creighton TE. Two-dimensional 1H nuclear magnetic resonance study of the (5-55) single-disulphide folding intermediate of bovine pancreatic trypsin inhibitor. J Mol Biol. 1991 Nov 20;222(2):373-90.",Two-dimensional 1H nuclear magnetic resonance study of the (5-55) single-disulphide folding intermediate of bovine pancreatic trypsin inhibitor.,published,journal,J. Mol. Biol.,Journal of molecular biology,222,2,,0022-2836,,,,,,,,,,,,,,,,,,,,373,390,1991,"An analogue of the bovine pancreatic trypsin inhibitor (BPTI) folding intermediate that contains only the disulphide bond between Cys5 and Cys55 has been prepared in Escherichia coli by protein engineering methods, with the other four Cys residues replaced by Ser. Two-dimensional 1H nuclear magnetic resonance studies of the analogue have resulted in essentially complete resonance assignments of the folded form of the protein. The folded protein has a compact conformation that is structurally very similar to that of native BPTI, although there are subtle differences and the folded conformation is not very stable. Approximately half of the protein molecules are unfolded at 3 degrees C, and this proportion increases at higher temperatures. The folded and unfolded conformations are in slow exchange. The conformational properties of the analogue can explain many aspects of the kinetic role that the normal (5-55) intermediate plays in the folding of BPTI." citations,ref_2,4875,208711,3,,reference citation,,,1704858,,"Darby NJ, van Mierlo CP, Creighton TE. The 5-55 single-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor. FEBS Lett. 1991 Feb 11;279(1):61-4.",The 5-55 single-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor.,published,journal,FEBS Lett.,FEBS letters,279,1,,0014-5793,,,,,,,,,,,,,,,,,,,,61,64,1991,"An analogue of the BPT1 folding intermediate that contains only the disulphide bond between Cys-5 and Cys-55 has been prepared by mutation of the other four Cys residues to Ser. On the basis of its circular dichroism and 1H-nuclear magnetic resonance spectra and its electrophoretic mobility, this intermediate is shown to be at least partially folded at low temperatures. This probably accounts for several of the unique properties of this intermediate observed during folding." citations,ref_3,4875,208712,4,,reference citation,,,1960731,,"van Mierlo CP, Darby NJ, Neuhaus D, Creighton TE (14-38, 30-51) double-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor: a two-dimensional 1H nuclear magnetic resonance study. J Mol Biol. 1991 Nov 20;222(2):353-71.","(14-38, 30-51) double-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor: a two-dimensional 1H nuclear magnetic resonance study.",published,journal,J. Mol. Biol.,Journal of molecular biology,222,2,,0022-2836,,,,,,,,,,,,,,,,,,,,353,371,1991,"An analogue of the BPTI folding intermediate that contains only the disulphide bonds between Cys14 and Cys38 and between Cys30 and Cys51 has been prepared in Escherichia coli by protein engineering methods. The other two Cys residues of native BPTI (at positions 5 and 55) have been replaced by Ser. Essentially complete proton resonance assignments of the analogue were obtained by employing two-dimensional 1H nuclear magnetic resonance techniques. The intermediate has a more extended conformation in the N-terminal (residues 1 to 7) region and there are other differences in the C-terminal (residues 55 to 58) region. The remainder of the protein is substantially identical to native BPTI. The conformational properties of the analogue can explain several aspects of the kinetic role that the normal (14-38, 30-51) intermediate plays in the folding of BPTI." citations,ref_4,4875,208713,5,,reference citation,,,1373775,,"Darby NJ, van Mierlo CP, Scott GH, Neuhaus D, Creighton TE. Kinetic roles and conformational properties of the non-native two-disulphide intermediates in the refolding of bovine pancreatic trypsin inhibitor. J Mol Biol. 1992 Apr 20;224(4):905-11.",Kinetic roles and conformational properties of the non-native two-disulphide intermediates in the refolding of bovine pancreatic trypsin inhibitor.,published,journal,J. Mol. Biol.,Journal of molecular biology,224,4,,0022-2836,,,,,,,,,,,,,,,,,,,,905,911,1992,"The most productive folding pathway of reduced bovine pancreatic trypsin inhibitor (BPTI) proceeds through the disulphide intermediates (30-51), (30-51, 5-14), and (30-51, 5-38); these are important kinetic intermediates in folding, even though the latter pair contain non-native disulphide bonds. Analogues of these intermediates have been prepared by protein engineering methods and their conformational properties examined by circular dichroism and 1H-nuclear magnetic resonance. The (30-51), (30-51, 5-14) and (30-51, 5-38) analogues exhibit comparable degrees of stable structure, which cannot include those portions of the polypeptide chain involving Cys5, Cys14 and Cys38. These properties are consistent with the roles of (30-51, 5-14) and (30-51, 5-38) in the folding pathway of BPTI, which demand that they exhibit a considerable degree of conformational flexibility in part of the molecule." citations,entry_citation,4881,208859,1,,entry citation,,9521106,,,,"Apparent stability of the secondary structure of Azotobacter vinelandii holoflavodoxin II as probed by hydrogen exchange: implications for redox potential regulation and flavodoxin folding",published,journal,Protein Sci.,,7,,,,,,,,,,,,,,,,,,,,,,,306,317,1998, citations,ref_5,4875,208714,6,,reference citation,,,1379719,,"van Mierlo CP, Darby NJ, Creighton TE. The partially folded conformation of the Cys-30 Cys-51 intermediate in the disulfide folding pathway of bovine pancreatic trypsin inhibitor. Proc Natl Acad Sci U S A. 1992 Aug 1;89(15):6775-9.",The partially folded conformation of the Cys-30 Cys-51 intermediate in the disulfide folding pathway of bovine pancreatic trypsin inhibitor.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,89,15,,0027-8424,,,,,,,,,,,,,,,,,,,,6775,6779,1992,"The best-characterized protein folding pathway is that of bovine pancreatic trypsin inhibitor, which folds from the reduced form through a series of disulfide bond intermediates. The crucial one-disulfide intermediate of bovine pancreatic trypsin inhibitor with the disulfide bond between Cys-30 and Cys-51 is shown here to have a partially folded conformation in which the major elements of secondary structure interact via a core of apolar side chains, which resembles part of the native conformation. The stability of this structure can account for the predominance of this one-disulfide intermediate during folding. Much of the remaining one-third of the polypeptide chain, in particular the N-terminal 14 residues, is largely disordered; this accounts for the ability of this intermediate to form readily any of the three possible second disulfide bonds involving Cys-5, -14, and -38. The partially folded conformation of this intermediate provides direct evidence for the importance of native-like interactions between elements of secondary structure in directing protein folding, which is assumed in many studies." citations,ref_6,4875,208715,7,,reference citation,,,7680380,,"van Mierlo CP, Darby NJ, Keeler J, Neuhaus D, Creighton TE. Partially folded conformation of the (30-51) intermediate in the disulphide folding pathway of bovine pancreatic trypsin inhibitor. 1H and 15N resonance assignments and determination of backbone dynamics from 15N relaxation measurements. J Mol Biol. 1993 Feb 20;229(4):1125-46.",Partially folded conformation of the (30-51) intermediate in the disulphide folding pathway of bovine pancreatic trypsin inhibitor. 1H and 15N resonance assignments and determination of backbone dynamics from 15N relaxation measurements.,published,journal,J. Mol. Biol.,Journal of molecular biology,229,4,,0022-2836,,,,,,,,,,,,,,,,,,,,1125,1146,1993,"An analogue of the important folding intermediate of BPTI with only the disulphide bond between Cys30 and Cys51 has been characterized by 1H and 15N NMR techniques. In particular, the dynamics of the polypeptide backbone were characterized using (1H)-15N NOE and 15N T1 and T2 relaxation data. The intermediate is partially folded, with part of the polypeptide chain stably folded and the remainder flexible or unfolded. The folded portion consists of the major elements of native-like secondary structure interacting through the hydrophobic core of the molecule. The 15N relaxation data show that the N-terminal 15 residues are very flexible, and the (1H, 1H) NOESY data show that these residues have no NOE interactions with the remainder of the molecule. The segment of residues 37 to 41 is also flexible. These observations explain why during folding this intermediate most readily forms any of the possible disulphide bonds between Cys5, Cys14 and Cys38, including the non-native 5-14 and 5-38 bonds. The native-like folded portion of the molecule limits the possible disulphide bonds that can be formed to those in the remainder of the polypeptide chain. Also, forming the non-native disulphide bonds need not involve any disruption of that folded structure, as the Cys residues involved are in flexible regions of the molecule." citations,ref_7,4875,208716,8,,reference citation,,,7507172,,"van Mierlo CP, Kemmink J, Neuhaus D, Darby NJ, Creighton TE. 1H NMR analysis of the partly-folded non-native two-disulphide intermediates (30-51,5-14) and (30-51,5-38) in the folding pathway of bovine pancreatic trypsin inhibitor. J Mol Biol. 1994 Jan 21;235(3):1044-61.","1H NMR analysis of the partly-folded non-native two-disulphide intermediates (30-51,5-14) and (30-51,5-38) in the folding pathway of bovine pancreatic trypsin inhibitor.",published,journal,J. Mol. Biol.,Journal of molecular biology,235,3,,0022-2836,,,,,,,,,,,,,,,,,,,,1044,1061,1994,"The conformational properties of analogues of the (30-51,5-14) and (30-51,5-38) disulphide intermediates in refolding of reduced BPTI, with non-native second disulphide bonds, have been characterized in detail by 1H NMR analysis. They are shown to have partly-folded conformations, very similar to that of the (30-51) one-disulphide intermediate from which they arise during folding. The non-native disulphide bonds are formed in flexible or unfolded parts of the polypeptide chain; they do not disrupt the folded portion nor do they introduce substantial non-native conformation. The conformational properties of these intermediates explain their important roles in the folding pathway." citations,entry_citation,4876,208731,1,,entry citation,,,,,,"Letter to the Editor: Assignment of 1H, 13C, and 15N Resonances of Canine Milk Lysozyme",published,journal,J. Biomol. NMR,,19,4,,,,,,,,,,,,,,,,,,,,,,387,388,2001, citations,entry_citation,4877,208746,1,,entry citation,,1960732,,,,"1H NMR Analysis of the partly-folded non-native two-disulphide intermediates (30-51, 5-14) and (30-51, 5-38) in the folding pathway of bovine pancreatic trypsin inhibitor",published,journal,J. Mol. Biol.,,235,,,,,,,,,,,,,,,,,,,,,,,1044,1061,1994, citations,ref_1,4877,208747,2,,reference citation,,,1704858,,"Darby NJ, van Mierlo CP, Creighton TE. The 5-55 single-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor. FEBS Lett. 1991 Feb 11;279(1):61-4.",The 5-55 single-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor.,published,journal,FEBS Lett.,FEBS letters,279,1,,0014-5793,,,,,,,,,,,,,,,,,,,,61,64,1991,"An analogue of the BPT1 folding intermediate that contains only the disulphide bond between Cys-5 and Cys-55 has been prepared by mutation of the other four Cys residues to Ser. On the basis of its circular dichroism and 1H-nuclear magnetic resonance spectra and its electrophoretic mobility, this intermediate is shown to be at least partially folded at low temperatures. This probably accounts for several of the unique properties of this intermediate observed during folding." citations,ref_2,4877,208748,3,,reference citation,,,1960731,,"van Mierlo CP, Darby NJ, Neuhaus D, Creighton TE. (14-38, 30-51) double-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor: a two-dimensional 1H nuclear magnetic resonance study. J Mol Biol. 1991 Nov 20;222(2):353-71.","(14-38, 30-51) double-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor: a two-dimensional 1H nuclear magnetic resonance study.",published,journal,J. Mol. Biol.,Journal of molecular biology,222,2,,0022-2836,,,,,,,,,,,,,,,,,,,,353,371,1991,"An analogue of the BPTI folding intermediate that contains only the disulphide bonds between Cys14 and Cys38 and between Cys30 and Cys51 has been prepared in Escherichia coli by protein engineering methods. The other two Cys residues of native BPTI (at positions 5 and 55) have been replaced by Ser. Essentially complete proton resonance assignments of the analogue were obtained by employing two-dimensional 1H nuclear magnetic resonance techniques. The intermediate has a more extended conformation in the N-terminal (residues 1 to 7) region and there are other differences in the C-terminal (residues 55 to 58) region. The remainder of the protein is substantially identical to native BPTI. The conformational properties of the analogue can explain several aspects of the kinetic role that the normal (14-38, 30-51) intermediate plays in the folding of BPTI." citations,entry_citation,4900,209302,1,,entry citation,,21226234,11327868,,,"Evidence for Synergy Between Family 2b Carbohydrate Binding Modules in Cellulomonas fimi xylanase 11A",published,journal,Biochemistry,,40,8,,,,,,,,,,,,,,,,,,,,,,2468,2477,2001, citations,ref_3,4877,208749,4,,reference citation,,,1373775,,"Darby NJ, van Mierlo CP, Scott GH, Neuhaus D, Creighton TE. Kinetic roles and conformational properties of the non-native two-disulphide intermediates in the refolding of bovine pancreatic trypsin inhibitor. J Mol Biol. 1992 Apr 20;224(4):905-11.",Kinetic roles and conformational properties of the non-native two-disulphide intermediates in the refolding of bovine pancreatic trypsin inhibitor.,published,journal,J. Mol. Biol.,Journal of molecular biology,224,4,,0022-2836,,,,,,,,,,,,,,,,,,,,905,911,1992,"The most productive folding pathway of reduced bovine pancreatic trypsin inhibitor (BPTI) proceeds through the disulphide intermediates (30-51), (30-51, 5-14), and (30-51, 5-38); these are important kinetic intermediates in folding, even though the latter pair contain non-native disulphide bonds. Analogues of these intermediates have been prepared by protein engineering methods and their conformational properties examined by circular dichroism and 1H-nuclear magnetic resonance. The (30-51), (30-51, 5-14) and (30-51, 5-38) analogues exhibit comparable degrees of stable structure, which cannot include those portions of the polypeptide chain involving Cys5, Cys14 and Cys38. These properties are consistent with the roles of (30-51, 5-14) and (30-51, 5-38) in the folding pathway of BPTI, which demand that they exhibit a considerable degree of conformational flexibility in part of the molecule." citations,ref_4,4877,208750,5,,reference citation,,,1379719,,"van Mierlo CP, Darby NJ, Creighton TE. The partially folded conformation of the Cys-30 Cys-51 intermediate in the disulfide folding pathway of bovine pancreatic trypsin inhibitor. Proc Natl Acad Sci U S A. 1992 Aug 1;89(15):6775-9.",The partially folded conformation of the Cys-30 Cys-51 intermediate in the disulfide folding pathway of bovine pancreatic trypsin inhibitor.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,89,15,,0027-8424,,,,,,,,,,,,,,,,,,,,6775,6779,1992,"The best-characterized protein folding pathway is that of bovine pancreatic trypsin inhibitor, which folds from the reduced form through a series of disulfide bond intermediates. The crucial one-disulfide intermediate of bovine pancreatic trypsin inhibitor with the disulfide bond between Cys-30 and Cys-51 is shown here to have a partially folded conformation in which the major elements of secondary structure interact via a core of apolar side chains, which resembles part of the native conformation. The stability of this structure can account for the predominance of this one-disulfide intermediate during folding. Much of the remaining one-third of the polypeptide chain, in particular the N-terminal 14 residues, is largely disordered; this accounts for the ability of this intermediate to form readily any of the three possible second disulfide bonds involving Cys-5, -14, and -38. The partially folded conformation of this intermediate provides direct evidence for the importance of native-like interactions between elements of secondary structure in directing protein folding, which is assumed in many studies." citations,ref_5,4877,208751,6,,reference citation,,,7680380,,"van Mierlo CP, Darby NJ, Keeler J, Neuhaus D, Creighton TE. Partially folded conformation of the (30-51) intermediate in the disulphide folding pathway of bovine pancreatic trypsin inhibitor. 1H and 15N resonance assignments and determination of backbone dynamics from 15N relaxation measurements. J Mol Biol. 1993 Feb 20;229(4):1125-46.",Partially folded conformation of the (30-51) intermediate in the disulphide folding pathway of bovine pancreatic trypsin inhibitor. 1H and 15N resonance assignments and determination of backbone dynamics from 15N relaxation measurements.,published,journal,J. Mol. Biol.,Journal of molecular biology,229,4,,0022-2836,,,,,,,,,,,,,,,,,,,,1125,1146,1993,"An analogue of the important folding intermediate of BPTI with only the disulphide bond between Cys30 and Cys51 has been characterized by 1H and 15N NMR techniques. In particular, the dynamics of the polypeptide backbone were characterized using (1H)-15N NOE and 15N T1 and T2 relaxation data. The intermediate is partially folded, with part of the polypeptide chain stably folded and the remainder flexible or unfolded. The folded portion consists of the major elements of native-like secondary structure interacting through the hydrophobic core of the molecule. The 15N relaxation data show that the N-terminal 15 residues are very flexible, and the (1H, 1H) NOESY data show that these residues have no NOE interactions with the remainder of the molecule. The segment of residues 37 to 41 is also flexible. These observations explain why during folding this intermediate most readily forms any of the possible disulphide bonds between Cys5, Cys14 and Cys38, including the non-native 5-14 and 5-38 bonds. The native-like folded portion of the molecule limits the possible disulphide bonds that can be formed to those in the remainder of the polypeptide chain. Also, forming the non-native disulphide bonds need not involve any disruption of that folded structure, as the Cys residues involved are in flexible regions of the molecule." citations,ref_6,4877,208752,7,,reference citation,,,7507172,,"van Mierlo CP, Kemmink J, Neuhaus D, Darby NJ, Creighton TE. 1H NMR analysis of the partly-folded non-native two-disulphide intermediates (30-51,5-14) and (30-51,5-38) in the folding pathway of bovine pancreatic trypsin inhibitor. J Mol Biol. 1994 Jan 21;235(3):1044-61.","1H NMR analysis of the partly-folded non-native two-disulphide intermediates (30-51,5-14) and (30-51,5-38) in the folding pathway of bovine pancreatic trypsin inhibitor.",published,journal,J. Mol. Biol.,Journal of molecular biology,235,3,,0022-2836,,,,,,,,,,,,,,,,,,,,1044,1061,1994,"The conformational properties of analogues of the (30-51,5-14) and (30-51,5-38) disulphide intermediates in refolding of reduced BPTI, with non-native second disulphide bonds, have been characterized in detail by 1H NMR analysis. They are shown to have partly-folded conformations, very similar to that of the (30-51) one-disulphide intermediate from which they arise during folding. The non-native disulphide bonds are formed in flexible or unfolded parts of the polypeptide chain; they do not disrupt the folded portion nor do they introduce substantial non-native conformation. The conformational properties of these intermediates explain their important roles in the folding pathway." citations,entry_citation,4878,208767,1,,entry citation,,,11163798,,,"Three-dimensional Structure Topology of the Calreticulin P-domain based on NMR Assignment",published,journal,FEBS Lett.,,488,1-2,,,,,,,,,,,,,,,,,,,,,,69,73,2000, citations,entry_citation,4879,208789,1,,entry citation,,,,,,"Letter to the Editor: Assignment of the 1H, 13C and 15N Signals of Sortase",published,journal,J. Biomol. NMR,,19,4,,,,,,,,,,,,,,,,,,,,,,379,380,2001, citations,entry_citation,488,208820,1,,entry citation,,,,,"Gould, Alison R., Mabbutt, Bridget C., Norton, Raymond S., ""Structure-function relationships in the polypeptide cardiac stimulant, anthopleurin-A (Effects of limited proteolysis by trypsin),"" Eur. J. Biochem. 189, 145-153 (1990).","Structure-function relationships in the polypeptide cardiac stimulant, anthopleurin-A (Effects of limited proteolysis by trypsin)",published,journal,Eur. J. Biochem.,,189,,,,,,,,,,,,,,,,,,,,,,,145,153,1990, citations,entry_citation,4880,208833,1,,entry citation,,,,,,"Letter to the Editor: 1H, 15N and 13C resonance assignments of the N-terminal region of calponin",published,journal,J. Biomol. NMR,,19,2,,,,,,,,,,,,,,,,,,,,,,189,190,2001, citations,entry_citation,4901,209318,1,,entry citation,,,,,,"Letter to the Editor: 1H, 15N, 13C resonances of the N-terminal domain of the human TFIIH p62 subunit",published,journal,J. Biomol. NMR,,19,3,,,,,,,,,,,,,,,,,,,,,,281,282,2001, citations,citations_1,50026,212049,1,,entry citation,,,31895552,,,Side Chain Hydrogen-Bonding Interactions within Amyloid-like Fibrils Formed by the Low-Complexity Domain of FUS: Evidence from Solid State Nuclear Magnetic Resonance Spectroscopy,published,journal,Biochemistry,,59,4,,,,,,,,,,,,,,,,,,,,,,364,378,2020, citations,ref_1,4881,208860,2,,reference citation,,,9521106,,"Steensma E, Nijman MJ, Bollen YJ, de Jager PA, van den Berg WA, van Dongen WM, van Mierlo CP. Apparent local stability of the secondary structure of Azotobacter vinelandii holoflavodoxin II as probed by hydrogen exchange: implications for redox potential regulation and flavodoxin folding. Protein Sci. 1998 Feb;7(2):306-17.",Apparent local stability of the secondary structure of Azotobacter vinelandii holoflavodoxin II as probed by hydrogen exchange: implications for redox potential regulation and flavodoxin folding.,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,7,2,,0961-8368,,,,,,,,,,,,,,,,,,,,306,317,1998,"As a first step to determine the folding pathway of a protein with an alpha/beta doubly wound topology, the 1H, 13C, and 15N backbone chemical shifts of Azotobacter vinelandii holoflavodoxin II (179 residues) have been determined using multidimensional NMR spectroscopy. Its secondary structure is shown to contain a five-stranded parallel beta-sheet (beta2-beta1-beta3-beta4-beta5) and five alpha-helices. Exchange rates for the individual amide protons of holoflavodoxin were determined using the hydrogen exchange method. The amide protons of 65 residues distributed throughout the structure of holoflavodoxin exchange slowly at pH* 6.2 [kex < 10(-5) s(-1)] and can be used as probes in future folding studies. Measured exchange rates relate to apparent local free energies for transient opening. We propose that the amide protons in the core of holoflavodoxin only exchange by global unfolding of the apo state of the protein. The results obtained are discussed with respect to their implications for flavodoxin folding and for modulation of the flavin redox potential by the apoprotein. We do not find any evidence that A. vinelandii holoflavodoxin II is divided into two subdomains based on its amide proton exchange rates, as opposed to what is found for the structurally but not sequentially homologous alpha/beta doubly wound protein Che Y." citations,ref_2,4881,208861,3,,reference citation,,,9737928,,"Steensma E, van Mierlo CP. Structural characterisation of apoflavodoxin shows that the location of the stable nucleus differs among proteins with a flavodoxin-like topology. J Mol Biol. 1998 Sep 25;282(3):653-66.",Structural characterisation of apoflavodoxin shows that the location of the stable nucleus differs among proteins with a flavodoxin-like topology.,published,journal,J. Mol. Biol.,Journal of molecular biology,282,3,,0022-2836,,,,,,,,,,,,,,,,,,,,653,666,1998,"The structural characteristics of Azotobacter vinelandii apoflavodoxin II have been determined using multidimensional NMR spectroscopy. Apoflavodoxin has a stable, well-ordered core but its flavin binding region is flexible. The local stability of apoflavodoxin was probed using hydrogen/deuterium exchange measurements. The existence of an apoflavodoxin equilibrium folding intermediate is inferred from the non-coincidence of CD and fluorescence unfolding curves obtained for the guanidinium hydrochloride induced unfolding of apoflavodoxin. We suggest that the structured part of the putative intermediate is composed of the elements of secondary structure which have the slowest exchanging amide protons in the native protein. These elements are strands beta1, beta3, beta4 and beta5a and helices alpha4 and alpha5. We propose that it is a general feature of flavodoxins that the stable nucleus resides in the C-terminal part of these proteins. The results on flavodoxin are compared with those on two sequentially unrelated proteins sharing the flavodoxin-like fold: Che Y and cutinase. It is shown that the stable nucleus is found in different parts of the flavodoxin-like topology." citations,ref_3,4881,208862,4,,reference citation,,,9827999,,"van Mierlo CP, van Dongen WM, Vergeldt F, van Berkel WJ, Steensma E. The equilibrium unfolding of Azotobacter vinelandii apoflavodoxin II occurs via a relatively stable folding intermediate. Protein Sci. 1998 Nov;7(11):2331-44.",The equilibrium unfolding of Azotobacter vinelandii apoflavodoxin II occurs via a relatively stable folding intermediate.,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,7,11,,0961-8368,,,,,,,,,,,,,,,,,,,,2331,2344,1998,"A flavodoxin from Azotobacter vinelandii is chosen as a model system to study the folding of alpha/beta doubly wound proteins. The guanidinium hydrochloride induced unfolding of apoflavodoxin is demonstrated to be reversible. Apoflavodoxin thus can fold in the absence of the FMN cofactor. The unfolding curves obtained for wild-type, C69A and C69S apoflavodoxin as monitored by circular dichroism and fluorescence spectroscopy do not coincide. Apoflavodoxin unfolding occurs therefore not via a simple two-state mechanism. The experimental data can be described by a three-state mechanism of apoflavodoxin equilibrium unfolding in which a relatively stable intermediate is involved. The intermediate species lacks the characteristic tertiary structure of native apoflavodoxin as deduced from fluorescence spectroscopy, but has significant secondary structure as inferred from circular dichroism spectroscopy. Both spectroscopic techniques show that thermally-induced unfolding of apoflavodoxin also proceeds through formation of a similar molten globule-like species. Thermal unfolding of apoflavodoxin is accompanied by anomalous circular dichroism characteristics: the negative ellipticity at 222 nM increases in the transition zone of unfolding. This effect is most likely attributable to changes in tertiary interactions of aromatic side chains upon protein unfolding. From the presented results and hydrogen/deuterium exchange data, a model for the equilibrium unfolding of apoflavodoxin is presented." citations,ref_4,4881,208863,5,,reference citation,,,8631324,,"Steensma E, Heering HA, Hagen WR, Van Mierlo CP. Redox properties of wild-type, Cys69Ala, and Cys69Ser Azotobacter vinelandii flavodoxin II as measured by cyclic voltammetry and EPR spectroscopy,. Eur J Biochem. 1996 Jan 15;235(1-2):167-72.","Redox properties of wild-type, Cys69Ala, and Cys69Ser Azotobacter vinelandii flavodoxin II as measured by cyclic voltammetry and EPR spectroscopy,.",published,journal,Eur. J. Biochem.,European journal of biochemistry / FEBS,235,1-2,,0014-2956,,,,,,,,,,,,,,,,,,,,167,172,1996,"This study deals with the detailed electrochemistry and complete EPR-monitored titrations of flavodoxin II of Azotobacter vinelandii (ATCC 478). Since wild-type flavodoxin dimerises via intermolecular disulphide bond formation between Cys69 residues, Cys69 has been replaced by both an alanine and a serine residue. Redox properties of the C69A and C69S flavodoxin mutants were compared to those of wild-type flavodoxin. In the presence of the promotor neomycin, C69A and C69S flavodoxin showed a reversible response of the semiquinone/hydroquinone couple at the glassy carbon electrode. However, the addition of dithiothreitol proved to be necessary for the stabilisation of the wild-type flavodoxin response. EPR-monitored redox titrations of wild-type and C69A flavodoxin at high and low pH confirmed the redox potentials measured using cyclic voltammetry. The pH dependence of the semiquinone/hydroquinone redox potentials cannot be described using a model assuming one redox-linked pK. Instead, the presence of at least two redox-linked protonation sites is suggested: pKred.1 = 5.39 +/- 0.08, pKox = 7.29 +/- 0.14, and pKred.2 = 7.84 +/- 0.14 with Em.7 = -459 +/- 4 mV, and a constant redox potential at high pH of -485 +/- 4 mV. The dependence of the semiquinone/hydroquinone redox potential on temperature is -0.5 +/- 0.1 mV . K(-1), yielding delta H degrees = 28.6 +/- 1.5 kJ . mol(1) and delta S degrees = -50.0 +/- 6.2 J . mol(-1) . K(-1). No significant differences in redox properties of wild-type, C69A, and C69S flavodoxin were observed. The electrochemical data suggest that replacement of Cys69 in the vicinity of the FMN by either an alanine or a serine residue does not alter the dielectric properties and structure of A. vinelandii flavodoxin II." citations,ref_5,4881,208864,6,,reference citation,,,,,"van Mierlo, C.P.M. and Steensma, E. Journal of Molecular Catalysis B: Enzymatic 7 (1999) 147-156. Stabilisation centres differ between structurally homologous proteins as shown by NMR spectroscopy.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_6,4881,208865,7,,reference citation,,,10867188,,"van Mierlo CP, Steensma E. Protein folding and stability investigated by fluorescence, circular dichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy: the flavodoxin story. J Biotechnol. 2000 May 26;79(3):281-98.","Protein folding and stability investigated by fluorescence, circular dichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy: the flavodoxin story.",published,journal,J. Biotechnol.,Journal of biotechnology,79,3,,0168-1656,,,,,,,,,,,,,,,,,,,,281,298,2000,"In this review, the experimental results obtained on the folding and stability of Azotobacter vinelandii flavodoxin are summarised. By doing so, three main spectroscopic techniques used to investigate protein folding and stability are briefly introduced. These techniques are: circular dichroism (CD) spectroscopy, fluorescence emission spectroscopy, and nuclear magnetic resonance (NMR) spectroscopy in combination with the hydrogen exchange methodology. Results on the denaturant-induced and thermal equilibrium unfolding of apoflavodoxin from A. vinelandii, i.e. flavodoxin in the absence of the riboflavin-5'-monophosphate (FMN) cofactor, are discussed. A scheme for the equilibrium unfolding of apoflavodoxin is presented which involves a relatively stable molten globule-like intermediate. Denaturant-induced apoflavodoxin (un)folding as followed at the residue-level by NMR shows that the transition of native A. vinelandii apoflavodoxin to its molten globule state is highly co-operative. However, the unfolding of the molten globule to the unfolded state of the protein is non-co-operative. A comparison of the folding of A. vinelandii flavodoxin with the folding of flavodoxin from Anaboena PCC 7119 is made. The local stabilities of apo- and holoflavodoxin from A. vinelandii as measured by NMR spectroscopy are compared. Both Che Y and cutinase, which have no sequence homology with apoflavodoxin but which share the flavodoxin-like topology, have stabilisation centres different from that of apoflavodoxin from A. vinelandii. The stable centres of structurally similar proteins can thus reside in different parts of the same protein topology. Insight in the variations in (local) unfolding processes of structurally similar proteins can be used to stabilise proteins with a flavodoxin-like fold. Finally, the importance of some recent experimental and theoretical developments for the study of flavodoxin folding is briefly discussed." citations,ref_7,4881,208866,8,,reference citation,,,10739257,,"van Mierlo CP, van den Oever JM, Steensma E. Apoflavodoxin (un)folding followed at the residue level by NMR. Protein Sci. 2000 Jan;9(1):145-57.",Apoflavodoxin (un)folding followed at the residue level by NMR.,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,9,1,,0961-8368,,,,,,,,,,,,,,,,,,,,145,157,2000,"The denaturant-induced (un)folding of apoflavodoxin from Azotobacter vinelandii has been followed at the residue level by NMR spectroscopy. NH groups of 21 residues of the protein could be followed in a series of 1H-15N heteronuclear single-quantum coherence spectra recorded at increasing concentrations of guanidinium hydrochloride despite the formation of protein aggregate. These NH groups are distributed throughout the whole apoflavodoxin structure. The midpoints of unfolding determined by NMR coincide with the one obtained by fluorescence emission spectroscopy. Both techniques give rise to unfolding curves with transition zones at significantly lower denaturant concentrations than the one obtained by circular dichroism spectroscopy. The NMR (un)folding data support a mechanism for apoflavodoxin folding in which a relatively stable intermediate is involved. Native apoflavodoxin is shown to cooperatively unfold to a molten globule-like state with extremely broadened NMR resonances. This initial unfolding step is slow on the NMR chemical shift timescale. The subsequent unfolding of the molten globule is faster on the NMR chemical shift timescale and the limited appearance of 1H-15N HSQC cross peaks of unfolded apoflavodoxin in the denaturant range studied indicates that it is noncooperative." citations,ref_8,4881,208867,9,,reference citation,,,889809,,"Tanaka M, Haniu M, Yasunobu KT, Yoch DC. Complete amino acid sequence of azotoflavin, a flavodoxin from Azotobacter vinelandii. Biochemistry. 1977 Aug 9;16(16):3525-37. No abstract available.","Complete amino acid sequence of azotoflavin, a flavodoxin from Azotobacter vinelandii.",published,journal,Biochemistry,Biochemistry,16,16,,0006-2960,,,,,,,,,,,,,,,,,,,,3525,3537,1977, citations,entry_citation,4882,208888,1,,entry citation,,21326075,11313338,,,1H NMR Study on the Binding of Pin1 Trp-trp domain with Phosphothreonine Peptides,published,journal,J. Biol. Chem.,,276,27,,,,,,,,,,,,,,,,,,,,,,25150,25156,2001, citations,entry_citation,4883,208903,1,,entry citation,,,,,,"Letter to the Editor: Assignment of 1H, 13C, and 15N Resonances of Canine Milk Lysozyme",published,journal,J. Biomol. NMR,,19,4,,,,,,,,,,,,,,,,,,,,,,387,388,2001, citations,entry_citation,4884,208916,1,,entry citation,,,11078733,,,"Solution Structure of Focal Adhesion Adaptor PINCH LIM1 Domain and Characterization of Its Interaction with Integrin Linked Kinase Ankyrin Repeat Domain",published,journal,J. Biol. Chem.,,276,7,,,,,,,,,,,,,,,,,,,,,,4932,4939,2001, citations,entry_citation,4885,208945,1,,entry citation,,21228260,11330818,,,"Backbone 1H, 15N and 13C Resonance Assignments of the NTPase Subdomain of the Hepatitis C Virus NS3 RNA Helicase",published,journal,J. Biomol. NMR,,19,3,,,,,,,,,,,,,,,,,,,,,,283,284,2001, citations,entry_citation,4886,208967,1,,entry citation,,98411455,9737928,,,"Structural characterisation of apoflavodoxin shows that the location of the stable nucleus differs among proteins with a flavodoxin-like topology",published,journal,J. Mol. Biol.,Journal of Molecular Biology,282,,,,,,,,,,,,,,,,,,,,,,,653,666,1998, citations,ref_1,4886,208968,2,,reference citation,,,9737928,,"Steensma E, van Mierlo CP. Structural characterisation of apoflavodoxin shows that the location of the stable nucleus differs among proteins with a flavodoxin-like topology.",Structural characterisation of apoflavodoxin shows that the location of the stable nucleus differs among proteins with a flavodoxin-like topology.,published,journal,J. Mol. Biol.,Journal of molecular biology,282,3,,0022-2836,,,,,,,,,,,,,,,,,,,,653,666,1998,"The structural characteristics of Azotobacter vinelandii apoflavodoxin II have been determined using multidimensional NMR spectroscopy. Apoflavodoxin has a stable, well-ordered core but its flavin binding region is flexible. The local stability of apoflavodoxin was probed using hydrogen/deuterium exchange measurements. The existence of an apoflavodoxin equilibrium folding intermediate is inferred from the non-coincidence of CD and fluorescence unfolding curves obtained for the guanidinium hydrochloride induced unfolding of apoflavodoxin. We suggest that the structured part of the putative intermediate is composed of the elements of secondary structure which have the slowest exchanging amide protons in the native protein. These elements are strands beta1, beta3, beta4 and beta5a and helices alpha4 and alpha5. We propose that it is a general feature of flavodoxins that the stable nucleus resides in the C-terminal part of these proteins. The results on flavodoxin are compared with those on two sequentially unrelated proteins sharing the flavodoxin-like fold: Che Y and cutinase. It is shown that the stable nucleus is found in different parts of the flavodoxin-like topology." citations,ref_2,4886,208969,3,,reference citation,,,9521106,,"Steensma E, Nijman MJ, Bollen YJ, de Jager PA, van den Berg WA, van Dongen WM, van Mierlo CP. Apparent local stability of the secondary structure of Azotobacter vinelandii holoflavodoxin II as probed by hydrogen exchange: implications for redox potential regulation and flavodoxin folding.",Apparent local stability of the secondary structure of Azotobacter vinelandii holoflavodoxin II as probed by hydrogen exchange: implications for redox potential regulation and flavodoxin folding.,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,7,2,,0961-8368,,,,,,,,,,,,,,,,,,,,306,317,1998,"As a first step to determine the folding pathway of a protein with an alpha/beta doubly wound topology, the 1H, 13C, and 15N backbone chemical shifts of Azotobacter vinelandii holoflavodoxin II (179 residues) have been determined using multidimensional NMR spectroscopy. Its secondary structure is shown to contain a five-stranded parallel beta-sheet (beta2-beta1-beta3-beta4-beta5) and five alpha-helices. Exchange rates for the individual amide protons of holoflavodoxin were determined using the hydrogen exchange method. The amide protons of 65 residues distributed throughout the structure of holoflavodoxin exchange slowly at pH* 6.2 [kex < 10(-5) s(-1)] and can be used as probes in future folding studies. Measured exchange rates relate to apparent local free energies for transient opening. We propose that the amide protons in the core of holoflavodoxin only exchange by global unfolding of the apo state of the protein. The results obtained are discussed with respect to their implications for flavodoxin folding and for modulation of the flavin redox potential by the apoprotein. We do not find any evidence that A. vinelandii holoflavodoxin II is divided into two subdomains based on its amide proton exchange rates, as opposed to what is found for the structurally but not sequentially homologous alpha/beta doubly wound protein Che Y." citations,ref_3,4886,208970,4,,reference citation,,,9827999,,"van Mierlo CP, van Dongen WM, Vergeldt F, van Berkel WJ, Steensma E. The equilibrium unfolding of Azotobacter vinelandii apoflavodoxin II occurs via a relatively stable folding intermediate.",The equilibrium unfolding of Azotobacter vinelandii apoflavodoxin II occurs via a relatively stable folding intermediate.,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,7,11,,0961-8368,,,,,,,,,,,,,,,,,,,,2331,2344,1998,"A flavodoxin from Azotobacter vinelandii is chosen as a model system to study the folding of alpha/beta doubly wound proteins. The guanidinium hydrochloride induced unfolding of apoflavodoxin is demonstrated to be reversible. Apoflavodoxin thus can fold in the absence of the FMN cofactor. The unfolding curves obtained for wild-type, C69A and C69S apoflavodoxin as monitored by circular dichroism and fluorescence spectroscopy do not coincide. Apoflavodoxin unfolding occurs therefore not via a simple two-state mechanism. The experimental data can be described by a three-state mechanism of apoflavodoxin equilibrium unfolding in which a relatively stable intermediate is involved. The intermediate species lacks the characteristic tertiary structure of native apoflavodoxin as deduced from fluorescence spectroscopy, but has significant secondary structure as inferred from circular dichroism spectroscopy. Both spectroscopic techniques show that thermally-induced unfolding of apoflavodoxin also proceeds through formation of a similar molten globule-like species. Thermal unfolding of apoflavodoxin is accompanied by anomalous circular dichroism characteristics: the negative ellipticity at 222 nM increases in the transition zone of unfolding. This effect is most likely attributable to changes in tertiary interactions of aromatic side chains upon protein unfolding. From the presented results and hydrogen/deuterium exchange data, a model for the equilibrium unfolding of apoflavodoxin is presented." citations,citations_1,50027,212063,1,,entry citation,,,32719135,,,The unusual structure of Ruminococcin C1 antimicrobial peptide confers activity against clinical pathogens,published,journal,Proc. Natl. Acad. Sci. U. S. A.,,,,,,,,,,,,,,,,,,,,,,,,,,,2020, citations,entry_citation,5648,229403,1,,entry citation,,,14675814,,,Random coil carbon chemical shifts of deoxyribonucleic acids,published,journal,J. Magn. Reson.,,166,1,,,,,,,,,,,,,,,,,,,,,,11,18,2004, citations,ref_4,4886,208971,5,,reference citation,,,8631324,,"Steensma E, Heering HA, Hagen WR, Van Mierlo CP. Redox properties of wild-type, Cys69Ala, and Cys69Ser Azotobacter vinelandii flavodoxin II as measured by cyclic voltammetry and EPR spectroscopy,.","Redox properties of wild-type, Cys69Ala, and Cys69Ser Azotobacter vinelandii flavodoxin II as measured by cyclic voltammetry and EPR spectroscopy,.",published,journal,Eur. J. Biochem.,European journal of biochemistry / FEBS,235,1-2,,0014-2956,,,,,,,,,,,,,,,,,,,,167,172,1996,"This study deals with the detailed electrochemistry and complete EPR-monitored titrations of flavodoxin II of Azotobacter vinelandii (ATCC 478). Since wild-type flavodoxin dimerises via intermolecular disulphide bond formation between Cys69 residues, Cys69 has been replaced by both an alanine and a serine residue. Redox properties of the C69A and C69S flavodoxin mutants were compared to those of wild-type flavodoxin. In the presence of the promotor neomycin, C69A and C69S flavodoxin showed a reversible response of the semiquinone/hydroquinone couple at the glassy carbon electrode. However, the addition of dithiothreitol proved to be necessary for the stabilisation of the wild-type flavodoxin response. EPR-monitored redox titrations of wild-type and C69A flavodoxin at high and low pH confirmed the redox potentials measured using cyclic voltammetry. The pH dependence of the semiquinone/hydroquinone redox potentials cannot be described using a model assuming one redox-linked pK. Instead, the presence of at least two redox-linked protonation sites is suggested: pKred.1 = 5.39 +/- 0.08, pKox = 7.29 +/- 0.14, and pKred.2 = 7.84 +/- 0.14 with Em.7 = -459 +/- 4 mV, and a constant redox potential at high pH of -485 +/- 4 mV. The dependence of the semiquinone/hydroquinone redox potential on temperature is -0.5 +/- 0.1 mV . K(-1), yielding delta H degrees = 28.6 +/- 1.5 kJ . mol(1) and delta S degrees = -50.0 +/- 6.2 J . mol(-1) . K(-1). No significant differences in redox properties of wild-type, C69A, and C69S flavodoxin were observed. The electrochemical data suggest that replacement of Cys69 in the vicinity of the FMN by either an alanine or a serine residue does not alter the dielectric properties and structure of A. vinelandii flavodoxin II." citations,ref_5,4886,208972,6,,reference citation,,,,,"van Mierlo, C.P.M. and Steensma, E.; Journal of Molecular Catalysis B: Enzymatic 7 (1999) 147-156. Stabilisation centres differ between structurally homologous proteins as shown by NMR spectroscopy",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_6,4886,208973,7,,reference citation,,,10867188,,"van Mierlo CP, Steensma E. Protein folding and stability investigated by fluorescence, circular dichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy: the flavodoxin story.","Protein folding and stability investigated by fluorescence, circular dichroism (CD), and nuclear magnetic resonance (NMR) spectroscopy: the flavodoxin story.",published,journal,J. Biotechnol.,Journal of biotechnology,79,3,,0168-1656,,,,,,,,,,,,,,,,,,,,281,298,2000,"In this review, the experimental results obtained on the folding and stability of Azotobacter vinelandii flavodoxin are summarised. By doing so, three main spectroscopic techniques used to investigate protein folding and stability are briefly introduced. These techniques are: circular dichroism (CD) spectroscopy, fluorescence emission spectroscopy, and nuclear magnetic resonance (NMR) spectroscopy in combination with the hydrogen exchange methodology. Results on the denaturant-induced and thermal equilibrium unfolding of apoflavodoxin from A. vinelandii, i.e. flavodoxin in the absence of the riboflavin-5'-monophosphate (FMN) cofactor, are discussed. A scheme for the equilibrium unfolding of apoflavodoxin is presented which involves a relatively stable molten globule-like intermediate. Denaturant-induced apoflavodoxin (un)folding as followed at the residue-level by NMR shows that the transition of native A. vinelandii apoflavodoxin to its molten globule state is highly co-operative. However, the unfolding of the molten globule to the unfolded state of the protein is non-co-operative. A comparison of the folding of A. vinelandii flavodoxin with the folding of flavodoxin from Anaboena PCC 7119 is made. The local stabilities of apo- and holoflavodoxin from A. vinelandii as measured by NMR spectroscopy are compared. Both Che Y and cutinase, which have no sequence homology with apoflavodoxin but which share the flavodoxin-like topology, have stabilisation centres different from that of apoflavodoxin from A. vinelandii. The stable centres of structurally similar proteins can thus reside in different parts of the same protein topology. Insight in the variations in (local) unfolding processes of structurally similar proteins can be used to stabilise proteins with a flavodoxin-like fold. Finally, the importance of some recent experimental and theoretical developments for the study of flavodoxin folding is briefly discussed." citations,ref_7,4886,208974,8,,reference citation,,,10739257,,"van Mierlo CP, van den Oever JM, Steensma E. Apoflavodoxin (un)folding followed at the residue level by NMR.",Apoflavodoxin (un)folding followed at the residue level by NMR.,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,9,1,,0961-8368,,,,,,,,,,,,,,,,,,,,145,157,2000,"The denaturant-induced (un)folding of apoflavodoxin from Azotobacter vinelandii has been followed at the residue level by NMR spectroscopy. NH groups of 21 residues of the protein could be followed in a series of 1H-15N heteronuclear single-quantum coherence spectra recorded at increasing concentrations of guanidinium hydrochloride despite the formation of protein aggregate. These NH groups are distributed throughout the whole apoflavodoxin structure. The midpoints of unfolding determined by NMR coincide with the one obtained by fluorescence emission spectroscopy. Both techniques give rise to unfolding curves with transition zones at significantly lower denaturant concentrations than the one obtained by circular dichroism spectroscopy. The NMR (un)folding data support a mechanism for apoflavodoxin folding in which a relatively stable intermediate is involved. Native apoflavodoxin is shown to cooperatively unfold to a molten globule-like state with extremely broadened NMR resonances. This initial unfolding step is slow on the NMR chemical shift timescale. The subsequent unfolding of the molten globule is faster on the NMR chemical shift timescale and the limited appearance of 1H-15N HSQC cross peaks of unfolded apoflavodoxin in the denaturant range studied indicates that it is noncooperative." citations,ref_8,4886,208975,9,,reference citation,,,889809,,"Tanaka M, Haniu M, Yasunobu KT, Yoch DC. Complete amino acid sequence of azotoflavin, a flavodoxin from Azotobacter vinelandii.","Complete amino acid sequence of azotoflavin, a flavodoxin from Azotobacter vinelandii.",published,journal,Biochemistry,Biochemistry,16,16,,0006-2960,,,,,,,,,,,,,,,,,,,,3525,3537,1977, citations,entry_citation,4887,208991,1,,entry citation,,,,,,"Letter to the Editor: Assignment of 1H, 13C, and 15N Resonances of Canine Milk Lysozyme",published,journal,J. Biomol. NMR,,19,4,,,,,,,,,,,,,,,,,,,,,,387,388,2001, citations,entry_citation,4888,209006,1,,entry citation,,21555253,11697910,,,The Role of Backbone Motions in Ligand Binding to the c-Src SH3 Domain,published,journal,J. Mol. Biol.,,313,4,,,,,,,,,,,,,,,,,,,,,,873,887,2001, citations,entry_citation,4889,209020,1,,entry citation,,21555253,11697910,,,The Role of Backbone Motions in Ligand Binding to the c-Src SH3 Domain,published,journal,J. Mol. Biol.,,313,4,,,,,,,,,,,,,,,,,,,,,,873,887,2001, citations,entry_citation,489,209038,1,,entry citation,,,,,"Gould, Alison R., Mabbutt, Bridget C., Norton, Raymond S., ""Structure-function relationships in the polypeptide cardiac stimulant, anthopleurin-A (Effects of limited proteolysis by trypsin),"" Eur. J. Biochem. 189, 145-153 (1990).","Structure-function relationships in the polypeptide cardiac stimulant, anthopleurin-A (Effects of limited proteolysis by trypsin)",published,journal,Eur. J. Biochem.,,189,,,,,,,,,,,,,,,,,,,,,,,145,153,1990, citations,entry_citation,4890,209051,1,,entry citation,,,,,,"Solution Structure of the N-terminal Domain of the Human TFIIH MAT1 Subunit: New Insights into the RING Finger Family",in press,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50028,212076,1,,entry citation,,,31624123,,,Topological analysis of the gp41 MPER on lipid bilayers relevant to the metastable HIV-1 envelope prefusion state,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,116,45,,1091-6490,,,,,,,,,,,,,,,,,,,,22556,22566,2019, citations,entry_citation,5003,212091,1,,entry citation,,21882793,11885986,,,"Letter to the Editor: Backbone Sequential Resonance Assignments of Yeast iso-2 Cytochrome c, Reduced and Oxidized forms",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,22,1,,,,,,,,,,,,,,,,,,,,,,93,94,2002, citations,ref_1,4890,209052,2,,reference citation,,,8521393,,"Yee A, Nichols MA, Wu L, Hall FL, Kobayashi R, Xiong Y. Molecular cloning of CDK7-associated human MAT1, a cyclin-dependent kinase-activating kinase (CAK) assembly factor. Cancer Res. 1995 Dec 15;55(24):6058-62.","Molecular cloning of CDK7-associated human MAT1, a cyclin-dependent kinase-activating kinase (CAK) assembly factor.",published,journal,Cancer Res.,Cancer research,55,24,,0008-5472,,,,,,,,,,,,,,,,,,,,6058,6062,1995,"Mammalian CDK7 is a protein kinase identified as the catalytic subunit of cyclin-dependent kinase (CDK)-activating kinase and as an essential component of the transcription factor TFIIH that is involved in transcription initiation and DNA repair. We have identified in human cells a number of CDK7-associated cellular proteins that appear to fall into two classes based on their relative [35S] metabolic labeling intensity. One class of proteins present in CDK7 immunocomplexes as a minor fraction contains components of the TFIIH transcription complex such as p62 and p89ERCC3, whereas the other fraction contains four polypeptides (p35, p37Cyclin H, p75, and p95) that are stoichiometrically associated with CDK7. Whereas the levels of association of p35, p37Cyclin H, and p75 with CDK7 remain unchanged between density-arrested and proliferating Ewing sarcoma EW-1 cells, the association of p95 with CDK7 was significantly decreased as cells reached confluency. Through a large-scale immunopurification of CDK7 complexes and protein microsequencing, we have isolated a cDNA that encodes p35 and have shown that it is the human homologue of Mat1 that is involved in the assembly of CAK. MAT1 contains a highly conserved C3HC4 motif at its NH2 terminus, a characteristic feature shared among RING finger proteins. The human MAT1 gene expresses a single 1.6-kb transcript, the steady-state level of which, like CDK7 and cyclin H, varies significantly in different cell lines and in different terminally differentiated tissues." citations,ref_2,4890,209053,3,,reference citation,,,,,,"X-PLOR, version 3.1: A system for X-ray crystallography and NMR",,book,,,,,,,,"X-PLOR, version 3.1: A system for X-ray crystallography and NMR",,,,Yale University Press,New Haven,0300054025,,,,,,,,,,,,,,1992, citations,ref_3,4890,209054,4,,reference citation,,,,,,"The program XEASY for computer-supported NMR spectral analysis of biological macromolecules.",,journal,J. Biomol. NMR,,6,,,,,,,,,,,,,,,,,,,,,,,1,10,1995, citations,entry_citation,4891,209072,1,,entry citation,,,,,,1H Assigned Chemical Shifts for Neurotoxin B (ntb),published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,2000, citations,ref_1,4891,209073,2,,reference citation,,,8443154,,"Yu C, Bhaskaran R, Chuang LC, Yang CC. Solution conformation of cobrotoxin: a nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing study. Biochemistry. 1993 Mar 9;32(9):2131-6.",Solution conformation of cobrotoxin: a nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing study.,published,journal,Biochemistry,Biochemistry,32,9,,0006-2960,,,,,,,,,,,,,,,,,,,,2131,2136,1993,"The solution conformation of cobrotoxin has been determined by using proton nuclear magnetic resonance spectroscopy. With the combination of various two-dimensional NMR techniques, the 1H-NMR spectrum of cobrotoxin was completely assigned (Yu et al., 1990). A set of 435 approximate interproton distance restraints was derived from nuclear Overhauser enhancement (NOE) measurements. These NOE constraints, in addition to the 29 dihedral angle constraints (from coupling constant measurements) and 26 hydrogen bonding restraints (from the pattern of short-range NOEs), form the basis of 3-D structure determination by the hybrid distance geometry-dynamical simulated annealing method. The 23 structures that were obtained satisfy the experimental restraints, display small deviation from idealized covalent geometry, and possess good nonbonded contacts. Analysis of converged structures indicated that there are two antiparallel beta sheets (double and triple stranded), duly confirming our earlier observations. These are well defined in terms of both atomic root mean square (RMS) differences and backbone torsional angles. The average backbone RMS deviation between the calculated structures and the mean structure, for the beta-sheet regions, is 0.92 A. The mean solution structure was compared with the X-ray crystal structure of erabutoxin b, the homologous protein. This yielded information that both structures resemble each other except at the exposed loop/surface regions, where the solution structure seems to possess more flexibility." citations,entry_citation,4892,209089,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N NMR sequence-specific resonance assignments for human apo-Mts1 (S100A4)",published,journal,J. Biomol. NMR,,19,4,,,,,,,,,,,,,,,,,,,,,,381,382,2001, citations,entry_citation,4893,209113,1,,entry citation,,21323471,11430762,,,"Letter to the Editor: 1H, 13C and 15N Resonance Assignments and Secondary Structure of the Cytotoxic Protein RNase 4 from Bullfrog Rana catesbeiana Oocytes",published,journal,J. Biomol. NMR,,20,1,,,,,,,,,,,,,,,,,,,,,,93,94,2001, citations,entry_citation,4894,209128,1,,entry citation,,20164467,,,,RNA recognition by a staufen double-stranded RNA-binding domain,published,journal,EMBO J.,,19,,,,,,,,,,,,,,,,,,,,,,,997,1009,2000, citations,entry_citation,4895,209143,1,,entry citation,,21223006,11322871,,,"Solution NMR Structure of the Cold-shock Protein from the Hyperthermophilic Bacterium Thermotoga maritima",published,journal,Eur. J. Biochem.,European Journal of Biochemistry,268,9,,,,,,,,,,,,,,,,,,,,,,2527,2539,2001, citations,entry_citation,4896,209163,1,,entry citation,,21228262,11330820,,,"Letter to the Editor: Sequential Assignment and Secondary Structure of the 14 kDa Chemotactic Protein CheY2 from Sinorhizobium meliloti",published,journal,J. Biomol. NMR,,19,3,,,,,,,,,,,,,,,,,,,,,,287,288,2001, citations,entry_citation,4897,209192,1,,entry citation,,,,,,"Letter to the Editor: Sequential assignment and secondary structure of the triple-labelled carbohydrate-binding domain of papG from uropathogenic E. coli",published,journal,J. Biomol. NMR,,19,2,,,,,,,,,,,,,,,,,,,,,,197,198,2001, citations,ref_AURELIA,4897,209193,2,,reference citation,,,,,"""AURELIA, A Program for computer-aided analysis of multidimensional NMR-spectra,"" K.-P. Neidig, M. Geyer, A. Gorler, C. Antz, R. Saffrich, W. Beneicke, H. R. Kalbitzer, J. Biomol. NMR 6 255 (1995)",,published,journal,J. Biomol. NMR,,6,3,,,,,,,,,,,,,,,,,,,,,,255,270,1995, citations,entry_citation,4898,209215,1,,entry citation,,,14578346,,,Multivalent mechanism of membrane insertion by the FYVE domain,published,journal,J. Biol. Chem.,,279,4,,,,,,,,,,,,,,,,,,,,,,3050,3057,2004, citations,ref_1,4898,209216,2,,reference citation,,96088118,,,,NMRPipe: a multidimensional spectral processing system based on UNIX pipes,,journal,J. Biomol. NMR,,6,3,,,,,,,,,,,,,,,,,,,,,,277,293,1995, citations,ref_2,4898,209217,3,,reference citation,,,,,,"A Common Sense Approach to Peak Picking in Two-, Three-, and Four-Dimensional Spectra Uning Automatic Computer Analysis of Contour Diagrams",,journal,J. Magn. Reson.,,95,,,,,,,,,,,,,,,,,,,,,,,214,220,1991, citations,entry_citation,4899,209252,1,,entry citation,,20577270,11135666,,,SMN Tudor Domain Structure and its Interaction with the Sm Proteins,published,journal,Nat. Struct. Biol.,,8,1,,,,,,,,,,,,,,,,,,,,,,27,31,2001, citations,ref_1,4899,209253,2,,reference citation,,96088118,,,,NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,,,J Biomol NMR.,,6,3,,,,,,,,,,,,,,,,,,,,,,277,293,1995, citations,ref_2,4899,209254,3,,reference citation,,,,,,"The program XEASY for computer-supported NMR spectral analysis of biological macromolecules.",,journal,J. Biomol. NMR,,6,,,,,,,,,,,,,,,,,,,,,,,1,10,1995, citations,ref_3,4899,209255,4,,reference citation,,98437621,,,,"Crystallography & NMR system: A new software suite for macromolecular structure determination.",,,"Acta Crystallogr., Sect. D: Biol. Crystallogr.",,54,,,,,,,,,,,,,,,,,,,,,,,905,921,1998, citations,entry_citation,49,209276,1,,entry citation,,,,,"Chazin, Walter J., Goldenberg, David P., Creighton, Thomas E., Wuthrich, Kurt, ""Comparative studies of conformation and internal mobility in native and circular basic pancreatic trypsin inhibitor by 1H nuclear magnetic resonance in solution,"" Eur. J. Biochem. 152, 429-437 (1985).","Comparative studies of conformation and internal mobility in native and circular basic pancreatic trypsin inhibitor by 1H nuclear magnetic resonance in solution",published,journal,Eur. J. Biochem.,,152,,,,,,,,,,,,,,,,,,,,,,,429,437,1985, citations,entry_citation,490,209289,1,,entry citation,,,,,"Ni, Feng, Konishi, Yasuo, Scheraga, H.A., ""Thrombin-Bound Conformation of the C-Terminal Fragments of Hirudin Determined by Transferred Nuclear Overhauser Effects,"" Biochemistry 29, 4479-4489 (1990).","Thrombin-Bound Conformation of the C-Terminal Fragments of Hirudin Determined by Transferred Nuclear Overhauser Effects",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,4479,4489,1990, citations,reference_1,4901,209319,2,,reference citation,,,1529339,,"Fischer L, Gerard M, Chalut C, Lutz Y, Humbert S, Kanno M, Chambon P, Egly JM. Cloning of the 62-kilodalton component of basic transcription factor BTF2. Science. 1992 Sep 4;257(5075):1392-5.",Cloning of the 62-kilodalton component of basic transcription factor BTF2.,published,journal,Science,"Science (New York, N.Y.)",257,5075,,0036-8075,,,,,,,,,,,,,,,,,,,,1392,1395,1992,"Cloning of the mammalian basic transcription factors serves as a major step in understanding the mechanism of transcription initiation. The 62-kilodalton component (p62) of one of these transcription factors, BTF2 was cloned and overexpressed. A monoclonal antibody to this polypeptide inhibited transcription in vitro. Immunoaffinity experiments demonstrated that the 62-kilodalton component is closely associated with the other polypeptides present in the BTF2 factor. Sequence similarity suggests that BTF2 may be the human counterpart of RNA polymerase II initiation factor b from yeast." citations,reference_2,4901,209320,3,,reference citation,,,,,,"The program XEASY for computer-supported NMR spectral analysis of biological macromolecules.",published,journal,J. Biomol. NMR,,6,,,,,,,,,,,,,,,,,,,,,,,1,10,1995, citations,entry_citation,4902,209350,1,,entry citation,,,,,,"Letter to the Editor: Complete sequence-specific 1H, 13C and 15N resonance assignments of the human PTK6 SH2 domain",published,journal,J. Biomol. NMR,,19,3,,,,,,,,,,,,,,,,,,,,,,291,292,2001, citations,entry_citation,4905,209380,1,,entry citation,,21140180,11243822,,,"Self-association Reaction of Denatured Staphylococcal Nuclease Fragments Characterized by Heteronuclear NMR",published,journal,J. Mol. Biol.,Journal of Molecular Biology,307,1,,,,,,,,,,,,,,,,,,,,,,309,322,2001, citations,entry_citation,4906,209404,1,,entry citation,,,,,,"Solution Structure of a C-terminal Coiled-coil Domain from Bovine IF1: The Inhibitor Protein of F1 ATPase",published,journal,J. Mol. Biol.,,308,2,,,,,,,,,,,,,,,,,,,,,,325,339,2001, citations,ref-1,4906,209405,2,,reference citation,,,,,,"X-PLOR, version 3.1: A system for X-ray crystallography and NMR",published,book,,,,,,,,"X-PLOR, version 3.1: A system for X-ray crystallography and NMR",,,,Yale University Press,New Haven,0300054025,,,,,,,,,,,,,,1992, citations,entry_citation,4907,209436,1,,entry citation,,,,,,NMR Solution Structure of Phospholamban,published,journal,Helv. Chim. Acta,,83,,,,,,,,,,,,,,,,,,,,,,,2141,2152,2000, citations,entry_citation,4908,209454,1,,entry citation,,21447268,11563561,,,"Letter to the Editor: Assignment of 1H, 13C and 15N Resonances of the a'-domain of ERp57",published,journal,J. Biomol. NMR,,20,4,,,,,,,,,,,,,,,,,,,,,,385,386,2001, citations,entry_citation,4909,209481,1,,entry citation,,,,,,"Letter to the Editor: Assignment of 1H, 15N and 13C resonances of the carbohydrate recognition domain of human galectin-3",published,journal,J. Biomol. NMR,,20,1,,,,,,,,,,,,,,,,,,,,,,91,92,2001, citations,entry_citation,491,209502,1,,entry citation,,,,,"Sodano, Patrick, Chary, Kandala V. R., Bjornberg, Olof, Holmgren, Arne, Kren, Betsy, Fuchs, James A., Wuthrich, Kurt, ""Nuclear magnetic resonance studies of recombinant Escherichia coli glutaredoxin (Sequence-specific assignments and secondary structure determination of the oxidized form),"" Eur. J. Biochem. 200, 369-377 (1991).","Nuclear magnetic resonance studies of recombinant Escherichia coli glutaredoxin (Sequence-specific assignments and secondary structure determination of the oxidized form)",published,journal,Eur. J. Biochem.,,200,,,,,,,,,,,,,,,,,,,,,,,369,377,1991, citations,entry_citation,4910,209515,1,,entry citation,,,12684009,,,"Homologous proteins with different folds: the three-dimensional structures of domains 1 and 6 of the multiple Kazal-type inhibitor LEKTI",published,journal,J. Mol. Biol.,,328,1,,,,,,,,,,,,,,,,,,,,,,205,219,2003, citations,ref-1,4910,209516,2,,reference citation,,,,,,NMRView: A computer program for the visualization and analysis of NMR data,published,journal,J. Biomol. NMR,,4,,,,,,,,,,,,,,,,,,,,,,,603,614,1994, citations,entry_citation,4911,209534,1,,entry citation,,21103709,11178896,,,"Structural Basis of Diverse Sequence-dependent Target Recognition by the 8kDa Dynein light chain",published,journal,J. Mol. Biol.,Journal of Molecular Biology,306,1,,,,,,,,,,,,,,,,,,,,,,97,108,2001, citations,entry_citation,4912,209561,1,,entry citation,,21103709,11178896,,,"Structural Basis of Diverse Sequence-dependent Target Recognition by the 8kDa Dynein light chain",published,journal,J. Mol. Biol.,Journal of Molecular Biology,306,1,,,,,,,,,,,,,,,,,,,,,,97,108,2001, citations,entry_citation,4913,209584,1,,entry citation,,21262926,11370788,,,"Backbone 1H, 15N, and 13C Resonance Assignments of ARPP-19",published,journal,J. Biomol. NMR,,19,4,,,,,,,,,,,,,,,,,,,,,,383,384,2001, citations,entry_citation,4914,209597,1,,entry citation,,21099872,11165244,,,"Structure/Function of Human Herpesvirus-8 MIP-II (1-71) and the Antagonist N-terminal Segment (1-10)",published,journal,FEBS Lett.,,489,2-3,,,,,,,,,,,,,,,,,,,,,,171,175,2001, citations,entry_citation,4915,209616,1,,entry citation,,21192642,11287632,,,"Structure and Function of the C-terminal PABC Domain of Human Poly(A)-binding Protein",published,journal,Proc. Natl. Acad. Sci. U.S.A.,,98,8,,,,,,,,,,,,,,,,,,,,,,4409,4413,2001, citations,entry_citation,4916,209638,1,,entry citation,,21109798,11175907,,,Conformation of a Peptide Ligand bound to its G-protein Coupled Receptor,published,journal,Nat. Struct. Biol.,,8,2,,,,,,,,,,,,,,,,,,,,,,161,165,2001,Receptor-bound conformation of a peptide hormone using TRNOE method citations,ref_1,4916,209639,2,,reference citation,,,,,,"X-PLOR, version 3.1: A system for X-ray crystallography and NMR",published,book,,,,,,,,"X-PLOR, version 3.1: A system for X-ray crystallography and NMR",,,,Yale University Press,New Haven,0300054025,,,,,,,,,,,,,,1992, citations,ref_2,4916,209640,3,,reference citation,,,,,"Boelens, R., Koning, T.M.G., Van der Marel, G.A., Van Boom, J.H. & Kaptein, R. Iterative procedure for structure determination from Proton-proton NOEs using a full relaxation matrix approach. Application to a DNA octamer. J.Magn.Reson. 82, 290-308(1989)""",,published,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4917,209659,1,,entry citation,,99192814,10092854,,,"Solution structure of a lipid transfer protein extracted from rice seeds. Comparison with homologous proteins",published,journal,Eur. J. Biochem.,,259,,,,,,,,,,,,,,,,,,,,,,,692,708,1999, citations,ref_3,4944,210263,4,,reference citation,,,10681053,,"Messens J, Hayburn G, Brosens E, Laus G, Wyns L. Development of a downstream process for the isolation of Staphylococcus aureus arsenate reductase overproduced in Escherichia coli. J Chromatogr B Biomed Sci Appl. 2000 Jan 14;737(1-2):167-78.",Development of a downstream process for the isolation of Staphylococcus aureus arsenate reductase overproduced in Escherichia coli.,published,journal,J. Chromatogr. B Biomed. Sci. Appl.,"Journal of chromatography. B, Biomedical sciences and applications",737,1-2,,1387-2273,,,,,,,,,,,,,,,,,,,,167,178,2000,"Arsenate reductase (ArsC) encoded by Staphylococcus aureus arsenic-resistance plasmid pI258 reduces intracellular As(V) (arsenate) to the more toxic As(III) (arsenite). In order to study the structure of ArsC and to unravel biochemical and physical properties of this redox enzyme, wild type enzyme and a number of cysteine mutants were overproduced soluble in Escherichia coli. In this paper we describe a novel purification method to obtain high production levels of highly pure enzyme. A reversed-phase method was developed to separate and analyze the many different forms of ArsC. The oxidation state and the methionine oxidized forms were determined by mass spectroscopy." citations,ref_1,4917,209660,2,,reference citation,,,2458699,,"Yu YG, Chung CH, Fowler A, Suh SW. Amino acid sequence of a probable amylase/protease inhibitor from rice seeds. Arch Biochem Biophys. 1988 Sep;265(2):466-75.",Amino acid sequence of a probable amylase/protease inhibitor from rice seeds.,published,journal,Arch. Biochem. Biophys.,Archives of biochemistry and biophysics,265,2,,0003-9861,,,,,,,,,,,,,,,,,,,,466,475,1988,"The primary structure of a 9-kDa basic protein from rice seeds was determined by gas-phase sequencing of the intact protein and peptides derived from it by digestion with trypsin, chymotrypsin, and endopeptidase Lys-K. The protein consists of a single polypeptide chain of 91 amino acid residues with a calculated molecular mass of 8909 Da. It is rich in alanine, serine, glycine, and cysteine. The eight cysteines form four disulfide bonds. There is no methionine, histidine, phenylalanine, or tryptophan. The sequence is highly homologous with an alpha-amylase inhibitor, I-2, from seeds of Indian finger millet [F. A. P. Campos and M. Richardson (1984) FEBS Lett. 167, 221-225] and a 10-kDa barley seed protein, also called a probable amylase/protease inhibitor [B. Svensson et al. (1986) Carlsberg Res. Commun. 51, 493-500; J. Mundy and J. C. Rogers (1986) Planta 169, 51-63]. In analogy with the barley protein, the purified protein is tentatively called a rice probable amylase/protease inhibitor (PAPI). The rice PAPI does not show inhibitory activities against proteases and amylases tested. The amino acid sequence is as follows: Ile-Thr-Cys-Gly-Gln-Val-Asn-Ser-Ala-Val(10)-Gly-Pro-Cys-Leu-Thr-Tyr- Ala-Arg-Gly-Gly(20)-Ala-Gly-Pro-Ser-Ala-Ala-Cys-Cys-Ser-Gly(30)-Val-Arg- Ser-Leu-Lys-Ala-Ala-Ala-Ser-Thr(40)-Thr-Ala-Asp-Arg-Arg-Thr-Ala-Cys- Asn-Cys(50)-Leu-Lys-Asn-Ala-Ala-Arg-Gly-Ile-Lys-Gly(60)-Leu-Asn-Ala-Gly- Asn-Ala-Ala-Ser-Ile-Pro(70)-Ser-Lys-Cys-Gly-Val-Ser-Val-Pro-Tyr-Thr(80)- Ile-Ser-Ala-Ser-Ile-Asp-Cys-Ser-Arg-Val-Ser(91)." citations,ref_2,4917,209661,3,,reference citation,,,,,,"The program XEASY for computer-supported NMR spectral analysis of biological macromolecules.",published,journal,J. Biomol. NMR,,6,,,,,,,,,,,,,,,,,,,,,,,1,10,1995, citations,ref_3,4917,209662,4,,reference citation,,,1847217,,"Guntert P, Braun W, Wuthrich K. Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA. J Mol Biol. 1991 Feb 5;217(3):517-30.","Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA.",published,journal,J. Mol. Biol.,Journal of molecular biology,217,3,,0022-2836,,,,,,,,,,,,,,,,,,,,517,530,1991,"A novel procedure for efficient computation of three-dimensional protein structures from nuclear magnetic resonance (n.m.r.) data in solution is described, which is based on using the program DIANA in combination with the supporting programs CALIBA, HABAS and GLOMSA. The first part of this paper describes the new programs DIANA. CALIBA and GLOMSA. DIANA is a new, fully vectorized implementation of the variable target function algorithm for the computation of protein structures from n.m.r. data. Its main advantages, when compared to previously available programs using the variable target function algorithm, are a significant reduction of the computation time, and a novel treatment of experimental distance constraints involving diastereotopic groups of hydrogen atoms that were not individually assigned. CALIBA converts the measured nuclear Overhauser effects into upper distance limits and thus prepares the input for the previously described program HABAS and for DIANA. GLOMSA is used for obtaining individual assignments for pairs of diastereotopic substituents by comparison of the experimental constraints with preliminary results of the structure calculations. With its general outlay, the presently used combination of the four programs is particularly user-friendly. In the second part of the paper, initial results are presented on the influence of the novel DIANA treatment of diastereotopic protons on the quality of the structures obtained, and a systematic study of the central processing unit times needed for the same protein structure calculation on a range of different, commonly available computers is described." citations,ref_4,4917,209663,5,,reference citation,,,,,,"X-PLOR, version 3.1: A system for X-ray crystallography and NMR",published,book,,,,,,,,"X-PLOR, version 3.1: A system for X-ray crystallography and NMR",,,,Yale University Press,New Haven,0300054025,,,,,,,,,,,,,,1992, citations,entry_citation,4918,209683,1,,entry citation,,,,,,"Letter to the Editor: Assignments of 1H and 15N resonances of the Pseudomonas aeruginosa K122-4 pilin monomer",published,journal,J. Biomol. NMR,,19,4,,,,,,,,,,,,,,,,,,,,,,385,386,2001, citations,entry_citation,4919,209709,1,,entry citation,,21345414,11435111,,,"Thioredoxin fold as a Homodimerization Module in the Putative Chaperone ERp29. NMR Structures of the Domains and Experimental Model of the 51 kDa Dimer",published,journal,Structure,,9,6,,,,,,,,,,,,,,,,,,,,,,457,471,2001, citations,entry_citation,4920,209732,1,,entry citation,,21345414,11435111,,,"Thioredoxin fold as a Homodimerization Module in the Putative Chaperone ERp29: NMR Structures of the Domains and Experimental Model of the 51 kDa Dimer",published,journal,Structure,,9,6,,,,,,,,,,,,,,,,,,,,,,457,471,2001, citations,entry_citation,4921,209755,1,,entry citation,,,15153103,,,"Poneratoxin, a neurotoxin from ant venom. Structure and expression in insect cells and construction of a bio-insecticide",published,journal,Eur. J. Biochem.,,271,11,,,,,,,,,,,,,,,,,,,,,,2127,2136,2004, citations,ref1,4921,209756,2,,reference citation,,,,,"Poneratoxin, neurotoxic pentacosapeptide from ant venom: synthetic, biological and conformational studies.; (In) Schneider C.H., Eberles A.N. (eds.); Peptides 1992, pp.759-760, Escom Science Publishers, Leiden (1993).",,published,book,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref2,4921,209757,3,,reference citation,,,8520220,,"Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR. 1995 Nov;6(3):277-93.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref3,4921,209758,4,,reference citation,,,,,"Bartels,CH; Xia,T-H; Billeter,M; Guntert,P; Wuthrich,K. (1995) The program XEASY for computer-supported NMR specreal analysis of biological macromolecules. J. Biomol. NMR 5,1-10",,published,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_NMRPipe,5003,212092,2,,reference citation,,96088118,,,,NMRPipe: a multidimensional spectral processing system based on UNIX pipes,,journal,J. Biomol. NMR,,6,3,,,,,,,,,,,,,,,,,,,,,,277,293,1995, citations,ref4,4921,209759,5,,reference citation,,,9367762,,"Guntert P, Mumenthaler C, Wuthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J Mol Biol. 1997 Oct 17;273(1):283-98.",Torsion angle dynamics for NMR structure calculation with the new program DYANA.,published,journal,J. Mol. Biol.,Journal of molecular biology,273,1,,0022-2836,,,,,,,,,,,,,,,,,,,,283,298,1997,"The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from distance constraints and torsion angle constraints collected by nuclear magnetic resonance (NMR) experiments performs simulated annealing by molecular dynamics in torsion angle space and uses a fast recursive algorithm to integrate the equations of motions. Torsion angle dynamics can be more efficient than molecular dynamics in Cartesian coordinate space because of the reduced number of degrees of freedom and the concomitant absence of high-frequency bond and angle vibrations, which allows for the use of longer time-steps and/or higher temperatures in the structure calculation. It also represents a significant advance over the variable target function method in torsion angle space with the REDAC strategy used by the predecessor program DIANA. DYANA computation times per accepted conformer in the ""bundle"" used to represent the NMR structure compare favorably with those of other presently available structure calculation algorithms, and are of the order of 160 seconds for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300 computer. Test calculations starting from conformers with random torsion angle values further showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures." citations,ref5,4921,209760,6,,reference citation,,,,,"Brunger, AT (1992) X-PLOR version 3.1. A systef mr X-ray crystallography and NMR, Yale University Press, New Haven",book,published,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4922,209785,1,,entry citation,,21216433,11316886,,,"Structural and Dynamic Characterization of an Unfolded State of Poplar Apo-plastocyanin Formed under Non-denaturing Conditions",published,journal,Protein Sci.,Protein Science,10,5,,,,,,,,,,,,,,,,,,,,,,1056,1066,2001, citations,entry_citation,4923,209810,1,,entry citation,,21523957,11522785,,,"Discovery and structure of a potent and highly specific blocker of insect calcium channels.",published,journal,J. Biol. Chem.,,276,43,,,,,,,,,,,,,,,,,,,,,,40306,40312,2001, citations,entry_citation,4924,209824,1,,entry citation,,,,,,Interactions of a toxin from the scorpion Tityus serrulatus with a cloned K+ channel from squid (SqKv1A).,published,journal,Biochemistry,,40,20,,,,,,,,,,,,,,,,,,,,,,5942,5953,2001, citations,entry_citation,4925,209838,1,,entry citation,,21181598,11284682,,,Structural Basis for the Functional switch of the E. Coli Ada Protein,published,journal,Biochemistry,Biochemistry,40,14,,,,,,,,,,,,,,,,,,,,,,4261,4271,2001, citations,entry_citation,4926,209860,1,,entry citation,,,,,,"Solution studies of chymotrypsin inhibitor-2 glutamine insertion mutants show no interglutamine interactions",published,journal,Biochem. Biophys. Res. Commun.,,280,,,,,,,,,,,,,,,,,,,,,,,855,860,2001, citations,entry_citation,4927,209875,1,,entry citation,,21228263,,,,"Letter to the editor: 1H, 13C, 15N Resonance Assignments and Fold Verification of a Circular Permuted Variant of the Potent HIV-inactivating Protein Cyanovirin-N",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,19,,,,,,,,,,,,,,,,,,,,,,,289,290,2001, citations,entry_citation,4928,209903,1,,entry citation,,,,,,"Structure of the PHD Zinc finger from human Williams-Beuren syndrome transcription factor",published,journal,J. Mol. Biol.,,304,5,,,,,,,,,,,,,,,,,,,,,,723,729,2000, citations,entry_citation,4929,209928,1,,entry citation,,,,,,"Letter to the Editor: 1H, 15N and 13C resonance assignments for the Tctex1 dynein light chain from Chlamydomonas flagella",published,journal,J. Biomol. NMR,,20,20,,,,,,,,,,,,,,,,,,,,,,89,90,2001, citations,entry_citation,4930,209957,1,,entry citation,,21184346,11286998,,,"The Solution Structure of the Disulphide-linked Homodimer of the Human Trefoil Protein TFF1",published,journal,FEBS Lett.,,493,2-3,,,,,,,,,,,,,,,,,,,,,,70,74,2001,"Assignments are based on those derived earlier from a monomeric variant of the protein Polshakov et al. (1995 & 1997) see references ref_1 and ref_2." citations,ref_1,4930,209958,2,,reference citation,,,9096235,,"Polshakov VI, Williams MA, Gargaro AR, Frenkiel TA, Westley BR, Chadwick MP, May FE, Feeney J. High-resolution solution structure of human pNR-2/pS2: a single trefoil motif protein. J Mol Biol. 1997 Mar 28;267(2):418-32.",High-resolution solution structure of human pNR-2/pS2: a single trefoil motif protein.,published,journal,J. Mol. Biol.,Journal of molecular biology,267,2,,0022-2836,,,,,,,,,,,,,,,,,,,,418,432,1997,"pNR-2/pS2 is a 60 residue extracellular protein, which was originally discovered in human breast cancer cells, and subsequently found in other tumours and normal gastric epithelial cells. We have determined the three-dimensional solution structure of a C58S mutant of human pNR-2/pS2 using 639 distance and 137 torsion angle constraints obtained from analysis of multidimensional NMR spectra. A series of simulated annealing calculations resulted in the unambiguous determination of the protein's disulphide bonding pattern and produced a family of 19 structures consistent with the constraints. The peptide contains a single ""trefoil"" sequence motif, a region of about 40 residues with a characteristic sequence pattern, which has been found, either singly or as a repeat, in about a dozen extracellular proteins. The trefoil domain contains three disulphide bonds, whose 1-5, 2-4 and 3-6 cysteine pairings form the structure into three closely packed loops with only a small amount of secondary structure, which consists of a short alpha-helix packed against a two-stranded antiparallel beta-sheet. The structure of the domain is very similar to those of the two trefoil domains that occur in porcine spasmolytic polypeptide (PSP), the only member of the trefoil family whose three-dimensional structure has been previously determined. Outside the trefoil domain, which forms the compact ""head"" of the molecule, the N and C-terminal strands are closely associated, forming an extended ""tail"", which has some beta-sheet character for part of its length and which becomes more disordered towards the termini as indicated by (15)N{(1)H} NOEs. We have considered the structural implications of the possible formation of a native C58-C58 disulphide-bonded homodimer. Comparison of the surface features of pNR-2/pS2 and PSP, and consideration of the sequences of the other human trefoil domains in the light of these structures, illuminates the possible role of specific residues in ligand/receptor binding." citations,entry_citation,496,210596,1,,entry citation,,,,,"Wang, Jinfeng, Hinck, Andrew P., Loh, Stewart N., Markley, John L., ""Two-Dimensional NMR Studies of Staphylococcal Nuclease. 2. Sequence-Specific Assignments of Carbon-13 and Nitrogen-15 Signals from the Nuclease H124L-Thymidine 3',5'-Bisphosphate-Ca2+ Ternary Complex,"" Biochemistry 29, 102-113 (1990).","Two-Dimensional NMR Studies of Staphylococcal Nuclease. 2. Sequence-Specific Assignments of Carbon-13 and Nitrogen-15 Signals from the Nuclease H124L-Thymidine 3',5'-Bisphosphate-Ca2+ Ternary Complex",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,102,113,1990, citations,entry_citation,4960,210609,1,,entry citation,,,,,,"Solution Conformation of the Met 61 to His 61 Mutant of Pseudomonas stutzeri ZoBell Foerrocytochrome c-551",submitted,journal,Biophys. J.,,80,,,,,,,,,,,,,,,,,,,,,,,,,2001, citations,entry_citation,4961,210629,1,,entry citation,,,,,,"Letter to the Editor: 1H, 15N and 13C assignments of the N-terminal domain of Yersinia outer protein H in its apo form and in complex with a phosphotyrosine peptide",published,journal,J. Biomol. NMR,,21,1,,,,,,,,,,,,,,,,,,,,,,69,70,2001, citations,entry_citation,4963,210658,1,,entry citation,,,,,,"Chemical Shift Assignments and Coupling Constants for the rat Nedd4 WWIII domain - rat ENaC bP2 Peptide Complex",published,journal,Nat. Struct. Biol.,,8,5,,,,,,,,,,,,,,,,,,,,,,407,412,2001, citations,ref_2,4930,209959,3,,reference citation,,,8521850,,"Polshakov VI, Frenkiel TA, Westley B, Chadwick M, May F, Carr MD, Feeney J. NMR-based structural studies of the pNR-2/pS2 single domain trefoil peptide. Similarities to porcine spasmolytic peptide and evidence for a monomeric structure. Eur J Biochem. 1995 Nov 1;233(3):847-55.",NMR-based structural studies of the pNR-2/pS2 single domain trefoil peptide. Similarities to porcine spasmolytic peptide and evidence for a monomeric structure.,published,journal,Eur. J. Biochem.,European journal of biochemistry / FEBS,233,3,,0014-2956,,,,,,,,,,,,,,,,,,,,847,855,1995,"NMR spectroscopy measurements have been used to obtain structural information about the pNR-2/pS2 single-domain trefoil peptide. NMR data from 2D (two dimensional) double-quantum-filtered correlation spectroscopy (DQF-COSY), total correlation spectroscopy (TOCSY), NOE spectroscopy (NOESY), rotating frame NOE spectroscopy (ROESY) and 2D 13C-1H heteronuclear single-quantum coherence (HSQC) and 13C-1H HSQC-TOCSY spectra have been analysed to provide essentially complete 1H and 13C sequence-specific assignments for the pNR-2/pS2 protein. From a consideration of the NOE intensities, 3J(NH-alpha CH) coupling constants, 1H and 13C chemical shifts of backbone atoms and amide-proton exchange rates, the pNR-2/pS2 was found to contain two short antiparallel beta-strands (32-35 and 43-46), a short helix (25-30) and a type I beta-turn (11-15). These elements of secondary structure are very similar to those found in the two trefoil domains of pSP for which detailed structural information is already available. Similar 1H chemical shifts were noted for several conserved residues in pNR-2/pS2 and pSP and a characteristic Phe residue with a slowly flipping ring was found in the pNR-2/pS2 variant and in both domains of pSP. The tertiary structures of the domains therefore appear to be very similar in the two proteins and it is likely that the pNR-2/pS2 has the same pattern of disulphide bonds (1-5, 2-4, 3-6) as pSP. Correlation time measurements derived from 1H-1H NOE measurements indicate that the Cys58-->Ser form of the pNR-2/pS2 protein used in this study is monomeric in solution at approximately 2 mM." citations,entry_citation,4931,209974,1,,entry citation,,21103709,11178896,,,"Structural Basis of Diverse Sequence-dependent Target Recognition by the 8 kDa Dynein Light Chain",published,journal,J. Mol. Biol.,,306,1,,,,,,,,,,,,,,,,,,,,,,97,108,2001, citations,entry_citation,4932,209995,1,,entry citation,,,,,,1H Assigned Chemical Shifts for Wheat ns-LTP.,published,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,,"A NMR study of wheat ns-LTP has been published previously (Gincel E., Simorre J.P., Caille A., Ptak M., Vovelle F., Eur.J.Biochem. 1994, 226, 413-422)" citations,entry_citation,4933,210013,1,,entry citation,,96085149,,,,NMR-based structural Studies of the pNR-2/pS2 single domain trefoil peptide,published,journal,Eur. J. Biochem.,,233,,,,,,,,,,,,,,,,,,,,,,,847,855,1995,"Some supplementary and corrected assignments from Polshakov et al. (1997) see reference ref_1." citations,ref_1,4933,210014,2,,reference citation,,97250379,,,"Polshakov VI, Williams MA, Gargaro AR, Frenkiel TA, Westley BR, Chadwick MP, May FE, Feeney J. High-resolution solution structure of human pNR-2/pS2: a single trefoil motif protein. J Mol Biol. 1997 Mar 28;267(2):418-32.",,published,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4934,210038,1,,entry citation,,,,,,Structure and functionality of a designed p53 dimer,in press,journal,J. Mol. Biol.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4935,210062,1,,entry citation,,,,,,"Letter to the Editor: Sequence-specific 1H, 13C, and 15N signal assignments and secondary structure of Archaeoglobus fulgidus SRP19",published,journal,J. Biomol. NMR,,20,2,,,,,,,,,,,,,,,,,,,,,,187,188,2001, citations,citation_1,4935,210063,2,,reference citation,,,8520220,,"NMRPipe: a multidimensional spectral processing system based on UNIX Pipes F. Delaglio, S. Grzesiek, G. Vuister, G. Zhu, J. Pfeifer, and A. Bax J. Biomol. NMR, 6 (1995) 277-293.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,citation_2,4935,210064,3,,reference citation,,,,,"Garrett, Gronenborn, Clore (1991) J. Magn. Res., 95, 214-220.",,published,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_3,4935,210065,4,,reference citation,,,,,"Ch. Bartels, T.-H. Xia, M. Billeter, P. Guntert and K. Wuthrich (1995) The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J. Biomolecular NMR 5, 1-10",,published,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4936,210091,1,,entry citation,,,11226244,,,"Transverse relaxation-optimized NMR spectroscopy with the outer membrane protein OmpX in dihexanoyl phosphatidylcholine micelles.",published,journal,Proc. Natl. Acad. Sci. U. S. A.,Proceedings of the National Academy of Science of the USA,98,5,,,,,,,,,,,,,,,,,,,,,,2358,2363,2001,"The data reported here represent the 1H, 13C and 15N chemical shifts of 2H/13C/15N labeled OmpX in DHPC micelles obtained using TROSY-type triple resonance experiments. The size of the OmpX/DHPC particles is of about 60 kDa." citations,ref_1,4936,210092,2,,reference citation,,,,,,"The program XEASY for computer-supported NMR spectral analysis of biological macromolecules.",published,journal,J. Biomol. NMR,,6,,,,,,,,,,,,,,,,,,,,,,,1,10,1995, citations,entry_citation,4937,210110,1,,entry citation,,,,,,"Functional significance of the beta-hairpin in the insecticidal neurotoxin omega-atracotoxin-Hv1a",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,,"For related publications, see references in saveframes ref_1 and ref_2." citations,entry_citation,4964,210708,1,,entry citation,,,,,,"1H, 13C and 15N resonance assignment for barnase",published,journal,Appl. Magn. Reson.,,21,,,,,,,,,,,,,,,,,,,,,,,195,201,2001, citations,ref-1,4964,210709,2,,reference citation,,,,,"Bartels C., Xia T.-H., Billeter M., Guntert P. & Wuthrich K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules, J. Biomol. NMR (1995) 6, 1-10.",,published,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4965,210737,1,,entry citation,,21410523,11519754,,,"Letter to the Editor: 1H, 15N, and 13C Assignments and Secondary Structure Identification for Full-length Ribosomal Protein L11 from Thermus thermophilus",published,journal,J. Biomol. NMR,,20,3,,,,,,,,,,,,,,,,,,,,,,293,294,2001, citations,citations_1,50030,212096,1,,entry citation,,,31738549,,,Combining free energy simulations and NMR chemical-shift perturbation to identify transient cation-pi contacts in proteins,published,journal,J. Chem. Inf. Model.,Journal of chemical information and modeling,60,2,,1549-960X,,,,,,,,,,,,,,,,,,,,890,897,2020, citations,Ref_1,4937,210111,2,,reference citation,,,9228949,,"Fletcher JI, Smith R, O'Donoghue SI, Nilges M, Connor M, Howden ME, Christie MJ, King GF. The structure of a novel insecticidal neurotoxin, omega-atracotoxin-HV1, from the venom of an Australian funnel web spider. Nat Struct Biol. 1997 Jul;4(7):559-66.","The structure of a novel insecticidal neurotoxin, omega-atracotoxin-HV1, from the venom of an Australian funnel web spider.",published,journal,Nat. Struct. Biol.,Nature structural biology,4,7,,1072-8368,,,,,,,,,,,,,,,,,,,,559,566,1997,"A family of potent insecticidal toxins has recently been isolated from the venom of Australian funnel web spiders. Among these is the 37-residue peptide omega-atracotoxin-HV1 (omega-ACTX-HV1) from Hadronyche versuta. We have chemically synthesized and folded omega-ACTX-HV1, shown that it is neurotoxic, ascertained its disulphide bonding pattern, and determined its three-dimensional solution structure using NMR spectroscopy. The structure consists of a solvent-accessible beta-hairpin protruding from a disulphide-bonded globular core comprising four beta-turns. The three intramolecular disulphide bonds from a cystine knot motif similar to that seen in several other neurotoxic peptides. Despite limited sequence identity, omega-ACTX-HV1 displays significant structural homology with the omega-agatoxins and omega-conotoxins, both of which are vertebrate calcium channel antagonists; however, in contrast with these toxins, we show that omega-ACTX-HV1 inhibits insect, but not mammalian, voltage-gated calcium channel currents." citations,Ref_2,4937,210112,3,,reference citation,,,10491095,,"Wang X, Smith R, Fletcher JI, Wilson H, Wood CJ, Howden ME, King GF. Structure-function studies of omega-atracotoxin, a potent antagonist of insect voltage-gated calcium channels. Eur J Biochem. 1999 Sep;264(2):488-94.","Structure-function studies of omega-atracotoxin, a potent antagonist of insect voltage-gated calcium channels.",published,journal,Eur. J. Biochem.,European journal of biochemistry / FEBS,264,2,,0014-2956,,,,,,,,,,,,,,,,,,,,488,494,1999,"The omega-atracotoxins are a family of 36 to 37-residue peptide neurotoxins that block insect but not mammalian voltage-gated calcium channels. The high phylogenetic specificity of these toxins recommends them as lead compounds for targeting insects that have developed resistance to chemical pesticides. We have begun to examine structure-function relationships in the omega-atracotoxins in order to explore the molecular basis of their activity and phylogenetic specificity. By probing the venom of the Blue Mountains funnel-web spider, Hadronyche versuta, for insecticidal toxins with masses close to that of omega-atracotoxin-Hv1a (omega-ACTX-Hv1a), we have isolated and sequenced five additional omega-atracotoxins. Five of the six omega-atracotoxins isolated from the venom of H. versuta (omega-ACTX-Hv1a to -Hv1e) differ from one another by only 1-3 residues and have similar insecticidal potencies. In contrast, omega-ACTX-Hv1f differs from the other toxins by up to 10 residues and it has markedly reduced insecticidal potency, thus providing information on key functional residues. The new atracotoxin sequences have revealed that the three N-terminal residues are highly conserved. Despite the fact that these residues are structurally disordered in solution we show here, by a series of N-terminal truncations, that they contribute significantly to insecticidal potency. However, loss of activity does not correlate with deletion of highly conserved residues, which leads us to propose that the disposition of the N-terminal charge, rather than the chemical properties of the N-terminal residues themselves, may be critical for the activity of omega-atracotoxin on insect calcium channels." citations,entry_citation,4938,210127,1,,entry citation,,21126888,11226243,,,"Two Different Neurodegenerative Diseases Caused by Proteins with Similiar Structures",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,98,5,,,,,,,,,,,,,,,,,,,,,,2352,2357,2001, citations,entry_citation,4939,210141,1,,entry citation,,,,,,"Solution Structures of Two CCHC Zinc Fingers from the FOG Family Protein U-shaped that Mediate Protein-Protein Interactions",published,journal,Structure,,8,,,,,,,,,,,,,,,,,,,,,,,1157,1166,2000, citations,ref_1,4939,210142,2,,reference citation,,,11080638,,"Liew, C.K., Kowalski, K., Fox, A.H., Newton, A., Sharpe, B.K., Crossley, M., and Mackay, J.P. Solution Structures of Two CCHC Zinc Fingers from the FOG Family Protein U-shaped that Mediate Protein-Protein Interactions. Structure, 8, 1157-1166 (2000).",Solution structures of two CCHC zinc fingers from the FOG family protein U-shaped that mediate protein-protein interactions.,published,journal,Structure,"Structure (London, England : 1993)",8,11,,0969-2126,,,,,,,,,,,,,,,,,,,,1157,1166,2000,"BACKGROUND: Zinc finger domains have traditionally been regarded as sequence-specific DNA binding motifs. However, recent evidence indicates that many zinc fingers mediate specific protein-protein interactions. For instance, several zinc fingers from FOG family proteins have been shown to interact with the N-terminal zinc finger of GATA-1. RESULTS: We have used NMR spectroscopy to determine the first structures of two FOG family zinc fingers that are involved in protein-protein interactions: fingers 1 and 9 from U-shaped. These fingers resemble classical TFIIIA-like zinc fingers, with the exception of an unusual extended portion of the polypeptide backbone prior to the fourth zinc ligand. [15N,(1)H]-HSQC titrations have been used to define the GATA binding surface of USH-F1, and comparison with other FOG family proteins indicates that the recognition mechanism is conserved across species. The surface of FOG-type fingers that interacts with GATA-1 overlaps substantially with the surface through which classical fingers typically recognize DNA. This suggests that these fingers could not contact both GATA and DNA simultaneously. In addition, results from NMR, gel filtration, and sedimentation equilibrium experiments suggest that the interactions are of moderate affinity. CONCLUSIONS: Our results demonstrate unequivocally that zinc fingers comprising the classical betabetaalpha fold are capable of mediating specific contacts between proteins. The existence of this alternative function has implications for the prediction of protein function from sequence data and for the evolution of protein function." citations,entry_citation,494,210166,1,,entry citation,,,,,"Wang, Jinfeng, LeMaster, David M., Markley, John L., ""Two-Dimensional NMR Studies of Staphylococcal Nuclease. 1. Sequence-Specific Assignments of Hydrogen-1 Signals and Solution Structure of the Nuclease H124L-Thymidine 3',5'-Bisphosphate-Ca2+ Ternary Complex,"" Biochemistry 29, 88-101 (1990).","Two-Dimensional NMR Studies of Staphylococcal Nuclease. 1. Sequence-Specific Assignments of Hydrogen-1 Signals and Solution Structure of the Nuclease H124L-Thymidine 3',5'-Bisphosphate-Ca2+ Ternary Complex",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,88,101,1990, citations,entry_citation,4940,210179,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N chemical shift assignment of the honeybee pheromone carrier protein ASP1",published,journal,J. Biomol. NMR,,20,2,,,,,,,,,,,,,,,,,,,,,,183,184,2001, citations,entry_citation,4941,210197,1,,entry citation,,21474285,11457852,,,"The Three-dimensional Structure of the C-terminal DNA-binding Domain of Human Ku70",published,journal,J. Biol. Chem.,Journal of Biological Chemistry,276,41,,,,,,,,,,,,,,,,,,,,,,38231,38236,2001, citations,entry_citation,4942,210223,1,,entry citation,,21386226,,,,"Letter to the Editor: 1H, 15N and 13C Resonance Assignments and Secondary Structure of the Liver Ribonuclease from Bullfrog Rana catesbeiana",published,journal,J. Biomol. NMR,,20,2,,,,,,,,,,,,,,,,,,,,,,189,190,2001, citations,entry_citation,4943,210238,1,,entry citation,,,,,,"Comparison of Two Different Lysozyme Types Under Native and Crystallization Conditions using Two-Dimensional NMR and Dynamic Light Scattering",submitted,journal,Biophys. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,2002,See reference in the saveframe ref_1. citations,entry_citation,4966,210772,1,,entry citation,,21526408,11669614,,,"Dynamic Characterization of the Water binding loop in the P-type Cardiotoxin: Implication for the role of the bound Water Molecule",published,journal,Biochemistry,,40,43,,,,,,,,,,,,,,,,,,,,,,12782,12794,2001,"This paper describes a comprehensive NMR analysis of the structure and dynamics of P-type cardiotoxin and its bound water by using triple-quantum 17O NMR, NOE/ROE 2D NMR, and 13C T1 relaxation." citations,citations_1,50175,213384,1,Rab1b and Cdc42,entry citation,,,32123090,,,Conformational Control of Small GTPases by AMPylation,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,117,11,,1091-6490,,,,,,,,,,,,,,,,,,,,5772,5781,2020, citations,ref_1,4943,210239,2,,reference citation,,,3349024,,"Redfield C, Dobson CM. Sequential 1H NMR assignments and secondary structure of hen egg white lysozyme in solution. Biochemistry. 1988 Jan 12;27(1):122-36.",Sequential 1H NMR assignments and secondary structure of hen egg white lysozyme in solution.,published,journal,Biochemistry,Biochemistry,27,1,,0006-2960,,,,,,,,,,,,,,,,,,,,122,136,1988,"Assignments for 1H NMR resonances of 121 of the 129 residues of hen egg white lysozyme have been obtained by sequence-specific methods. Spin systems were identified with phase-sensitive two-dimensional (2-D) correlated spectroscopy and single and double relayed coherence transfer spectroscopy. For key types of amino acid residues, particularly alanine, threonine, valine, and glycine, complete spin systems were identified. For other residues a less complete definition of the spin system was found to be adequate for the purpose of sequential assignment. Sequence-specific assignments were achieved by phase-sensitive 2-D nuclear Overhauser enhancement spectroscopy (NOESY). Exploitation of the wide range of hydrogen exchange rates found in lysozyme was a useful approach to overcoming the problem of spectral overlap. The sequential assignment was built up from 21 peptide segments ranging in length from 2 to 13 residues. The NOESY spectra were also used to provide information about the secondary structure of the protein in solution. Three helical regions and two regions of beta-sheet were identified from the NOESY data; these regions are identical with those found in the X-ray structure of hen lysozyme. Slowly exchanging amides are generally correlated with hydrogen bonding identified in the X-ray structure; a number of exceptions to this general trend were, however, found. The results presented in this paper indicate that highly detailed information can be obtained from 2-D NMR spectra of a protein that is significantly larger than those studied previously." citations,ref_2,4943,210240,3,,reference citation,,,8520220,,"Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR. 1995 Nov;6(3):277-93.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref_3,4943,210241,4,,reference citation,,,,,"Bartels,CH; Xia,T-H; Billeter,M; Guntert,P; Wuthrich,K. The program XEASY for computer-supported NMR specreal analysis of biological macromolecules. J. Biomol. NMR 5,1-10(1995)",,published,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4944,210260,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N backbone resonance assignment of the arsenate reductase from Staphylococcus aureus in its reduced state",published,journal,J. Biomol. NMR,,20,1,,,,,,,,,,,,,,,,,,,,,,95,96,2001,"See references in saveframes ref_1, ref_2, ref-3, and ref_4." citations,ref_1,4944,210261,2,,reference citation,,,1409657,,"Ji G, Silver S. Reduction of arsenate to arsenite by the ArsC protein of the arsenic resistance operon of Staphylococcus aureus plasmid pI258. Proc Natl Acad Sci U S A. 1992 Oct 15;89(20):9474-8.",Reduction of arsenate to arsenite by the ArsC protein of the arsenic resistance operon of Staphylococcus aureus plasmid pI258.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,89,20,,0027-8424,,,,,,,,,,,,,,,,,,,,9474,9478,1992,"The arsenic resistance operon of Staphylococcus aureus plasmid pI258 consists of three genes, arsR (encoding the repressor regulatory protein), arsB (the determinant of the membrane efflux protein that confers resistance by pumping arsenic from the cells), and arsC (the small gene whose protein product is required for arsenate resistance only, not for arsenite resistance). ArsC has now been shown to be an arsenate reductase, converting intracellular arsenate [As(V)] to arsenite [As(III)], which is then exported from the cells by an energy-dependent efflux process. The arsenate reductase activity was found in the soluble cytoplasmic fraction in Escherichia coli (and not associated with the periplasmic fraction or the sedimentable cell envelope). Purified ArsC protein coupled in vitro with thioredoxin plus dithiothreitol (but not 2-mercaptoethanol or reduced glutathione) to reduce arsenate to arsenite." citations,ref_2,4944,210262,3,,reference citation,,,8003493,,"Ji G, Garber EA, Armes LG, Chen CM, Fuchs JA, Silver S. Arsenate reductase of Staphylococcus aureus plasmid pI258. Biochemistry. 1994 Jun 14;33(23):7294-9.",Arsenate reductase of Staphylococcus aureus plasmid pI258.,published,journal,Biochemistry,Biochemistry,33,23,,0006-2960,,,,,,,,,,,,,,,,,,,,7294,7299,1994,"Arsenate reductase encoded by Staphylococcus aureus arsenic-resistance plasmid pI258 was overproduced in Escherichia coli and purified. The purified enzyme reduced radioactive arsenate to arsenite when coupled to thioredoxin, thioredoxin reductase, and NADPH. NADPH oxidation coupled to arsenate reduction also required thioredoxin and thioredoxin reductase. Glutaredoxin and reduced glutathione did not stimulate arsenate reduction. NADPH oxidation showed Michaelis-Menten kinetics with a Km of 1 microM AsO4(3-) and an apparent Vmax of 200 nmol/min per mg of protein. At high substrate concentration (above 1 mM AsO4(3-), a secondary rise in the reaction rate was observed, with a Km of 2 mM and an apparent Vmax of 450 nmol/min per mg of protein. This secondary rise also occurred upon addition of phosphate or nitrate (which were not substrates for the enzyme). Arsenite (the product of the enzyme), tellurite, and antimonite [Sb(III)] were inhibitors. Selenate (but not selenite or sulfate) was a substrate for reductase-dependent NADPH oxidation, with an apparent Km of 13 mM SeO4(2-). Arsenate reductase was purified as a monomer of 14.5 kDa, consistent with the DNA sequence. Electrospray mass spectrometry showed two molecular masses of 14,810.5 and 14,436.0 Da, suggesting that 70% of the purified protein lacked the N-terminal three amino acids; HPLC coupled to electrospray mass spectroscopy of protease digest products confirmed this conclusion and verified the entire amino acid sequence." citations,ref_2,4980,211165,3,,reference citation,,,,,"Johnson, B.A., Blevins, R.A. NMR View: a computer program for the visualization and analysis of NMR data. J. Biomol. NMR (1994) 4, 603-614",,published,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_4,4944,210264,5,,reference citation,,,10606519,,"Messens J, Hayburn G, Desmyter A, Laus G, Wyns L. The essential catalytic redox couple in arsenate reductase from Staphylococcus aureus. Biochemistry. 1999 Dec 21;38(51):16857-65.",The essential catalytic redox couple in arsenate reductase from Staphylococcus aureus.,published,journal,Biochemistry,Biochemistry,38,51,,0006-2960,,,,,,,,,,,,,,,,,,,,16857,16865,1999,"Arsenate reductase (ArsC) encoded by Staphylococcus aureus arsenic-resistance plasmid pI258 reduces intracellular As(V) (arsenate) to the more toxic As(III) (arsenite), which is subsequently extruded from the cell. ArsC couples to thioredoxin, thioredoxin reductase, and NADPH to be enzymatically active. A novel purification method leads to high production levels of highly pure enzyme. A reverse phase method was introduced to systematically analyze and control the oxidation status of the enzyme. The essential cysteinyl residues and redox couple in arsenate reductase were identified by a combination of site-specific mutagenesis and endoprotease-digest mass spectroscopy analysis. The secondary structures, as determined with CD, of wild-type ArsC and its Cys mutants showed a relatively high helical content, independent of the redox status. Mutation of Cys 10, 82, and 89 led to redox-inactive enzymes. ArsC was oxidized in a single catalytic cycle and subsequently digested with endoproteinases ArgC, AspN, and GluC. From the peptide-mass profiles, cysteines 82 and 89 were identified as the redox couple of ArsC necessary to reduce arsenate to arsenite." citations,entry_citation,4945,210290,1,,entry citation,,21127492,11224573,,,Vam3p Structure Reveals Conserved and Divergent Properties of Syntaxins,published,journal,Nat. Struct. Biol.,Nature Structural Biology,8,3,,,,,,,,,,,,,,,,,,,,,,258,264,2001, citations,entry_citation,4946,210313,1,,entry citation,,21383385,11491295,,,"Solution Structures of C-1027 Apoprotein and Its Complex with the Aromatized Chromophore",published,journal,J. Mol. Biol.,,309,1,,,,,,,,,,,,,,,,,,,,,,267,283,2001, citations,entry_citation,4947,210329,1,,entry citation,,21383385,11491295,,,"Solution Structures of C-1027 Apoprotein and its Complex with the Aromatized Chromophore",published,journal,J. Mol. Biol.,,309,1,,,,,,,,,,,,,,,,,,,,,,267,283,2001, citations,entry_citation,4948,210347,1,,entry citation,,21673332,11814338,,,"NMR Structure of Alpha-bungarotoxin free and bound to a Mimotope of the Nicotinic Acetylcholine Receptor.",published,journal,Biochemistry,Biochemistry,41,5,,,,,,,,,,,,,,,,,,,,,,1457,1463,2002, citations,entry_citation,495,210367,1,,entry citation,,,,,"Wang, Jinfeng, LeMaster, David M., Markley, John L., ""Two-Dimensional NMR Studies of Staphylococcal Nuclease. 1. Sequence-Specific Assignments of Hydrogen-1 Signals and Solution Structure of the Nuclease H124L-Thymidine 3',5'-Bisphosphate-Ca2+ Ternary Complex,"" Biochemistry 29, 88-101 (1990).","Two-Dimensional NMR Studies of Staphylococcal Nuclease. 1. Sequence-Specific Assignments of Hydrogen-1 Signals and Solution Structure of the Nuclease H124L-Thymidine 3',5'-Bisphosphate-Ca2+ Ternary Complex",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,88,101,1990, citations,entry_citation,4950,210380,1,,entry citation,,99272560,,,,"Structure of the Anchor-Domain of Myristoylated and Non-myristoylated HIV-1 Nef Protein",published,journal,J. Mol. Biol.,,289,1,,,,,,,,,,,,,,,,,,,,,,123,138,1999, citations,ref_1,4950,210381,2,,reference citation,,,,,"Neidig KP, Geyer M, Gorler A, Antz C, Saffrich R, Beneicke W, Kalbitzer HR. AURELIA, A program for computer-aided analysis of multidimensional NMR spectra. Journal of Biomolecular NMR, 6:255-270, 1995.",,published,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4951,210401,1,,entry citation,,99272560,,,,"Structure of the Anchor-Domain of Myristoylated and Non-myristoylated HIV-1 Nef Protein",published,journal,J. Mol. Biol.,,289,1,,,,,,,,,,,,,,,,,,,,,,123,138,1999, citations,ref_1,4951,210402,2,,reference citation,,,,,"Neidig KP, Geyer M, Gorler A, Antz C, Saffrich R, Beneicke W, Kalbitzer HR. AURELIA, A program for computer-aided analysis of multidimensional NMR spectra. Journal of Biomolecular NMR, 6:255-270, 1995.",,published,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4952,210424,1,,entry citation,,,,,,The UBX Domain: A Widespread Ubquitin-like Module,in press,journal,J. Mol. Biol.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4953,210437,1,,entry citation,,,,,,"Letter to the Editor: Assignment of 1H, 13C and 15N resonances of the PPIase domain of the trigger factor from Mycoplasma genitalium",published,journal,J. Biomol. NMR,,20,2,,,,,,,,,,,,,,,,,,,,,,193,194,2001, citations,ref-1,4953,210438,2,,reference citation,,,,,"Ch. Bartels, T.-H. Xia, M. Billeter, P. G?ntert and K. W?thrich (1995) The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J. Biomolecular NMR 6, 1-10",,published,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4954,210470,1,,entry citation,,21293198,,,,The Solution Strucutre of the N-terminal Domain of Riboflavin Synthase,published,journal,J. Mol. Biol.,,309,4,,,,,,,,,,,,,,,,,,,,,,949,960,2001, citations,ref-1,4954,210471,2,,reference citation,,,9615996,,"Leutner M, Gschwind RM, Liermann J, Schwarz C, Gemmecker G, Kessler H. Automated backbone assignment of labeled proteins using the threshold accepting algorithm. J Biomol NMR. 1998 Jan;11(1):31-43.",Automated backbone assignment of labeled proteins using the threshold accepting algorithm.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,11,1,,0925-2738,,,,,,,,,,,,,,,,,,,,31,43,1998,"The sequential assignment of backbone resonances is the first step in the structure determination of proteins by heteronuclear NMR. For larger proteins, an assignment strategy based on proton side-chain information is no longer suitable for the use in an automated procedure. Our program PASTA (Protein ASsignment by Threshold Accepting) is therefore designed to partially or fully automate the sequential assignment of proteins, based on the analysis of NMR backbone resonances plus C beta information. In order to overcome the problems caused by peak overlap and missing signals in an automated assignment process, PASTA uses threshold accepting, a combinatorial optimization strategy, which is superior to simulated annealing due to generally faster convergence and better solutions. The reliability of this algorithm is shown by reproducing the complete sequential backbone assignment of several proteins from published NMR data. The robustness of the algorithm against misassigned signals, noise, spectral overlap and missing peaks is shown by repeating the assignment with reduced sequential information and increased chemical shift tolerances. The performance of the program on real data is finally demonstrated with automatically picked peak lists of human nonpancreatic synovial phospholipase A2, a protein with 124 residues." citations,entry_citation,4955,210489,1,,entry citation,,21251097,11352587,,,"NMR Structure of Cysteinyl-phosphorylated Enzyme IIB of the N,N'-diacetylchitobiose-specific Phosphoenolpyruvate-dependent Phosphotransferase System of Escherichia coli",published,journal,J. Mol. Biol.,,308,5,,,,,,,,,,,,,,,,,,,,,,993,1009,2001, citations,citations_1,50008,211823,1,,entry citation,,,31772021,,,Probing transient excited states of the bacterial cell division regulator MinE by relaxation dispersion NMR spectroscopy,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,116,51,,1091-6490,,,,,,,,,,,,,,,,,,,,25446,25455,2019, citations,citation_one,4955,210490,2,,reference citation,,,8003964,,"Eiso AB and Gea K. Schuurman-Wolters and Saier, Jr., Milton H. and Jonathan Reizer and Michel Jacuinod and Peter Roepstorff. Enzyme IIB-cellobiose of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli: backbone assignment and secondary structure determined by three-dimensional NMR spectroscopy Protein Sci. 1994. 3(2):282-290",Enzyme IIBcellobiose of the phosphoenol-pyruvate-dependent phosphotransferase system of Escherichia coli: backbone assignment and secondary structure determined by three-dimensional NMR spectroscopy.,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,3,2,,0961-8368,,,,,,,,,,,,,,,,,,,,282,290,1994,"The assignment of backbone resonances and the secondary structure determination of the Cys 10 Ser mutant of enzyme IIBcellobiose of the Escherichia coli cellobiose-specific phosphoenol-pyruvate-dependent phosphotransferase system are presented. The backbone resonances were assigned using 4 triple resonance experiments, the HNCA and HN(CO)CA experiments, correlating backbone 1H, 15N, and 13C alpha resonances, and the HN(CA)CO and HNCO experiments, correlating backbone 1H,15N and 13CO resonances. Heteronuclear 1H-NOE 1H-15N single quantum coherence (15N-NOESY-HSQC) spectroscopy and heteronuclear 1H total correlation 1H-15N single quantum coherence (15N-TOCSY-HSQC) spectroscopy were used to resolve ambiguities arising from overlapping 13C alpha and 13CO frequencies and to check the assignments from the triple resonance experiments. This procedure, together with a 3-dimensional 1H alpha-13C alpha-13CO experiment (COCAH), yielded the assignment for all observed backbone resonances. The secondary structure was determined using information both from the deviation of observed 1H alpha and 13C alpha chemical shifts from their random coil values and 1H-NOE information from the 15N-NOESY-HSQC. These data show that enzyme IIBcellobiose consists of a 4-stranded parallel beta-sheet and 5 alpha-helices. In the wild-type enzyme IIBcellobiose, the catalytic residue appears to be located at the end of a beta-strand." citations,citation_two,4955,210491,3,,reference citation,,,9041631,,"Eiso AB and Gea K. Schuurman-Wolters and Jonathan Reizer and Saier, Jr., Milton H. and Klaas Dijkstra and Ruud M. Scheek and George T. Robillard. The NMR side-chain assignments and solution structure of enzyme IIBcellobiose of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli. Protein Sci. 1997. 6(2):304-314",The NMR side-chain assignments and solution structure of enzyme IIBcellobiose of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli.,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,6,2,,0961-8368,,,,,,,,,,,,,,,,,,,,304,314,1997,"The assignment of the side-chain NMR resonances and the determination of the three-dimensional solution structure of the C10S mutant of enzyme IIBcellobiose (IIBcel) of the phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli are presented. The side-chain resonances were assigned nearly completely using a variety of mostly heteronuclear NMR experiments, including HCCH-TOCSY, HCCH-COSY, and COCCH-TOCSY experiments as well as CBCACOHA, CBCA(CO)NH, and HBHA(CBCA)(CO)NH experiments. In order to obtain the three-dimensional structure, NOE data were collected from 15N-NOESY-HSQC, 13C-HSQC-NOESY, and 2D NOE experiments. The distance restraints derived from these NOE data were used in distance geometry calculations followed by molecular dynamics and simulated annealing protocols. In an iterative procedure, additional NOE assignments were derived from the calculated structures and new structures were calculated. The final set of structures, calculated with approximately 2000 unambiguous and ambiguous distance restraints, has an rms deviation of 1.1 A on C alpha atoms. IIBcel consists of a four stranded parallel beta-sheet, in the order 2134. The sheet is flanked with two and three alpha-helices on either side. Residue 10, a cysteine in the wild-type enzyme, which is phosphorylated during the catalytic cycle, is located at the end of the first beta-strand. A loop that is proposed to be involved in the binding of the phosphoryl-group follows the cysteine. The loop appears to be disordered in the unphosphorylated state." citations,entry_citation,4956,210505,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N resonance assignment of YajQ, a protein of unknown structure and function from Escherichia coli",published,journal,J. Biomol. NMR,,20,3,,,,,,,,,,,,,,,,,,,,,,287,288,2001, citations,entry_citation,4957,210520,1,,entry citation,,21181601,11284685,,,"Solution Structure of the Transcriptional Activation Domain of the Bacteriophage T4 Protein, MotA",published,journal,Biochemistry,,40,14,,,,,,,,,,,,,,,,,,,,,,4293,4302,2001, citations,entry_citation,4958,210535,1,,entry citation,,21386227,,,,"Letter to the Editor: 1H, 13C and 15N Sequence-specific Resonance Assignment of the PSCD4 Domain of Diatom cell wall Protein Pleuralin-1",published,journal,J. Biomol. NMR,,20,2,,,,,,,,,,,,,,,,,,,,,,191,192,2001, citations,reference_1,4958,210536,2,,reference citation,,,2744488,,"Horton, R.M., Hunt, H.D., Ho, S.N. and Pease, L.R. (1989) Gene 77, 61-68.""",Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension.,published,journal,Gene,Gene,77,1,,0378-1119,,,,,,,,,,,,,,,,,,,,61,68,1989,"Gene splicing by overlap extension is a new approach for recombining DNA molecules at precise junctions irrespective of nucleotide sequences at the recombination site and without the use of restriction endonucleases or ligase. Fragments from the genes that are to be recombined are generated in separate polymerase chain reactions (PCRs). The primers are designed so that the ends of the products contain complementary sequences. When these PCR products are mixed, denatured, and reannealed, the strands having the matching sequences at their 3' ends overlap and act as primers for each other. Extension of this overlap by DNA polymerase produces a molecule in which the original sequences are 'spliced' together. This technique is used to construct a gene encoding a mosaic fusion protein comprised of parts of two different class-I major histocompatibility genes. This simple and widely applicable approach has significant advantages over standard recombinant DNA techniques." citations,reference_2,4958,210537,3,,reference citation,,,9431996,,"Kroger, N., Lehmann, G., Rachel, R. and Sumper, M. (1997) Eur. J. Biochem., 250, 99-105.""",Characterization of a 200-kDa diatom protein that is specifically associated with a silica-based substructure of the cell wall.,published,journal,Eur. J. Biochem.,European journal of biochemistry / FEBS,250,1,,0014-2956,,,,,,,,,,,,,,,,,,,,99,105,1997,"The cell wall of a diatom is made up of a silica-based scaffold and organic macromolecules. Proteins located in the cell wall are believed to control morphogenesis of the species-specific silica structures of the scaffold. However, data that correlate distinct silica elements and specific proteins within the diatom cell wall have not been reported. Here, the cell wall protein HEP200 (200-kDa HF-extractable protein) from the diatom Cylinidrotheca fusiformis is identified and characterized. HEP200 is tightly associated with a substructure of the silica scaffold. It is a member of a new protein family, of which two more members are identified. Each member displays the same bipartite structure. The N-terminal part consists of a variable number of a repeated sequence motif (PSCD domain), whereas the C-terminal part is unique. Immunolocalization experiments revealed the arrangement of different proteins within the cell wall. Frustulins, a previously described group of glycoproteins, constitute the outer coat of the cell wall and exhibit a ubiquitous distribution. In contrast, HEP200 is specifically located at a subset of about six silica strips in intact cell walls, shielded by frustulins. This study therefore identifies a diatom cell wall protein (HEP200) that is associated with a distinct substructure of the silica scaffold." citations,entry_citation,4959,210561,1,,entry citation,,,,,,Solution structure of the epsin N-terminal homology (ENTH) domain of human epsin,published,journal,J. Struct. Func. Genomics,Journal of Structural and Functional Genomics,2,,,,,,,,,,,,,,,,,,,,,,,1,8,2001, citations,citations_1,50009,211836,1,,entry citation,,,31754899,,,Backbone and methyl assignment of bacteriorhodopsin incorporated into nanodiscs,published,journal,J. Biomol. NMR.,,74,1,,,,,,,,,,,,,,,,,,,,,,45,60,2020, citations,ref_1,4966,210773,2,,reference citation,,,8308891,,"Bhaskaran R, Huang CC, Chang DK, Yu C. Cardiotoxin III from the Taiwan cobra (Naja naja atra). Determination of structure in solution and comparison with short neurotoxins. J Mol Biol. 1994 Jan 28;235(4):1291-301.",Cardiotoxin III from the Taiwan cobra (Naja naja atra). Determination of structure in solution and comparison with short neurotoxins.,published,journal,J. Mol. Biol.,Journal of molecular biology,235,4,,0022-2836,,,,,,,,,,,,,,,,,,,,1291,1301,1994,"The structure in solution of cardiotoxin III, a membrane toxin purified from the venom of the Taiwan cobra, Naja naja atra, is reported. Sequence-specific assignment of 1H-NMR lines was completed and the NMR data show the presence of a triple and a double-stranded antiparallel beta-sheet. Many NOE cross peaks identified in NOESY spectra were applied as distance constraints based on a hybrid distance geometry/dynamical simulated annealing technique; 20 structures were found within a single family. The average value of atomic RMS differences between the 20 structures and their geometric mean is 0.087 nm for the backbone atoms and 0.152 nm for all heavy atoms; they are 0.055 nm and 0.12 nm, respectively for the segments of secondary structure. In these selected structures the backbone of the polypeptide chain folds such that five strands emerge from a globular head. Three major loops link these strands to form a double and a triple-stranded antiparallel beta-sheet. Comparison of the structures of the toxin in solution with the X-ray crystal structure of its homologous protein, cardiotoxin V4II from Naja mossambica mossambica, showed good agreement between the structures except at segments of the turns. As the functions of short neurotoxins and cardiotoxins are distinct, despite their similar secondary structural patterns and tertiary folding, a comparative analysis has been carried out between cardiotoxin III and short neurotoxins of known structures. We discuss their structural features in order to clarify relationships between their structure and function." citations,ref_2,4966,210774,3,,reference citation,,,8703923,,"Chiang CM, Chang SL, Lin HJ, Wu WG. The role of acidic amino acid residues in the structural stability of snake cardiotoxins. Biochemistry. 1996 Jul 16;35(28):9177-86.",The role of acidic amino acid residues in the structural stability of snake cardiotoxins.,published,journal,Biochemistry,Biochemistry,35,28,,0006-2960,,,,,,,,,,,,,,,,,,,,9177,9186,1996,"We have recently shown that membrane-related activities of cardiotoxin V from Naja naja atra (CTX A5) are diminished at acidic pH although the overall beta-sheet structure of the molecule is maintained. In order to understand more about the mechanism of inactivation of CTX at acidic pH, we studied the effect of pH and denaturing reagents on the structural stability of CTX. We found, first, pH-induced structural transitions occurred in CTX A5 at two pH values as judged by the CD ellipticity around 195 nm: an increase in the beta-sheet content occurred around pH 4 and followed by a decrease, therein, around pH 2. The pKa of three acidic amino acid residues in CTX A5, i.e., Glu-17, Asp-42, and Asp-59, were determined to be 4.0, 3.2, and below 2.3, respectively, by NMR spectroscopy. The low pKa value of Asp-59 implies salt bridge formation between Lys-2 and Asp-59. Thus, electrostatic interaction may stabilize the three loop structure in addition to the hydrogen bonds between N- and C-termini of CTX molecule. Second, 2,2,2-trifluoroethanol (TFE) and guanidinium chloride (GdmHCI) were found to induce alpha-helical and random coil formation, respectively, in CTX A5 and eight other beta-sheet CTXs. Comparison of the relative potencies of TFE and GdmHCI to induce structural changes suggests that the amino acid residue located at position 17 plays a role in the structural stability. Specifically, CTXs containing negatively charged Glu-17 are least stable. It is suggested that Glu-17 may perturb the interaction between Lys-2 and Asp-59, and thus the overall stability of beta-sheet, in the presence of denaturing reagent. In conclusion, the perturbed structural stability of CTXs may partially explain the lower activity CTX exhibits at acidic pH. A structural model to account for the unfolding and refolding of CTX molecules without the breaking of disulfide bonds is also proposed." citations,entry_citation,4967,210789,1,,entry citation,,,,,,"Letter to the Editor: Backbone resonance assignment of Mason-Pfizer Monkey Virus Protease",published,journal,J. Biomol. NMR,,20,3,,,,,,,,,,,,,,,,,,,,,,291,292,2001, citations,entry_citation,4968,210808,1,,entry citation,,,,,,"Rapid Data Collection and Analysis of Protein Resonance Assignments Using AutoProc, AutoPeak, and AutoAssign Software",submitted,journal,J. Struct. Funct. Genomics,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4969,210822,1,,entry citation,,22088138,12093273,,,"Solution Structure of a Llama Single-domain Antibody with Hydrophobic Residues typical of the VH/VL Interface",published,journal,Biochemistry,Biochemistry,41,27,,,,,,,,,,,,,,,,,,,,,,8570,8579,2002, citations,entry_citation,497,210837,1,,entry citation,,,,,"Wang, Jinfeng, Hinck, Andrew P., Loh, Stewart N., Markley, John L., ""Two-Dimensional NMR Studies of Staphylococcal Nuclease. 2. Sequence-Specific Assignments of Carbon-13 and Nitrogen-15 Signals from the Nuclease H124L-Thymidine 3',5'-Bisphosphate-Ca2+ Ternary Complex,"" Biochemistry 29, 102-113 (1990).","Two-Dimensional NMR Studies of Staphylococcal Nuclease. 2. Sequence-Specific Assignments of Carbon-13 and Nitrogen-15 Signals from the Nuclease H124L-Thymidine 3',5'-Bisphosphate-Ca2+ Ternary Complex",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,102,113,1990, citations,primary_citation,4970,210850,1,,entry citation,,,11373686,,,"NMR Relaxation data for Protein Calmodulin in complex with the smooth muscle myosin light chain kinase calmodulin binding domain",published,journal,Nature,,411,,,,,,,,,,,,,,,,,,,,,,,501,504,2001, citations,entry_citation,4971,210947,1,,entry citation,,,11870861,,,"Solution structures of a 30 residue amino-terminal domain of the carp granulin-1 protein and its amino-terminally truncated 3-30 subfragment: implications for the conformational stability of the stack of two beta-hairpins.",published,journal,Proteins,,47,1,,,,,,,,,,,,,,,,,,,,,,14,24,2002, citations,entry_citation,4972,210964,1,,entry citation,,21914565,11916384,,,"Solution structure and dynamics of Crh, the Bacillus subtilis catabolite repression HPr",published,journal,J. Mol. Biol.,,317,1,,,,,,,,,,,,,,,,,,,,,,131,144,2002, citations,entry_citation,4973,210988,1,,entry citation,,21544935,11693575,,,"Letter to the editor: Sequential Assignment and Secondary Structure of Saratin, an Inhibitor of von Willebrand factor-dependent Platelet Adhesion to Collagen",published,journal,J. Biomol. NMR,,21,1,,,,,,,,,,,,,,,,,,,,,,77,78,2001, citations,ref_1,4973,210989,2,,reference citation,,,,,"Neidig, K.P., Geyer, M., Gorler, A., Antz, C., Saffrich, R., Beneicke, W. and Kalbitzer, H.R. (1995) J. Biomol. NMR, 6, 255-270.",,published,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4974,211010,1,,entry citation,,21631514,11775739,,,"Rapid Protein fold Determination using Secondary Chemical Shifts and Cross- hydrogen bond 15N-13C' Scalar Couplings (3hbJNC')",published,journal,J. Biomol. NMR,,21,3,,,,,,,,,,,,,,,,,,,,,,221,233,2001, citations,entry_citation,4975,211024,1,,entry citation,,,,,,"Letter to the Editor: Assignment of selectively 13C-labeled cellopentaose synthesized using an engineered glycosynthase",published,journal,J. Biomol. NMR,,21,1,,,,,,,,,,,,,,,,,,,,,,67,68,2001, citations,ref_1,4975,211025,2,,reference citation,,,,,"L.F. MacKenzie, Q. Wang, R.A.J. Warren, S.G. Withers, ""Glycosynthases: Mutant Glycosidases for Oligosaccharide Synthesis"" J.A.C.S. 120, 5583-5584 (1998)",,published,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4976,211043,1,,entry citation,,21464431,,,,"Solution Structures of the Antifungal Heliomicin and a Selected Variant with both Antibacterial and Antifungal Activities",published,journal,Biochemistry,,40,,,,,,,,,,,,,,,,,,,,,,,11995,12003,2001, citations,citations_1,50010,211854,1,,entry citation,,,31733726,,,NMR Reveals Light-Induced Changes in the Dynamics of a Photoswitchable Fluorescent Protein,published,journal,Biophys. J.,,117,11,,1542-0086,,,,,,,,,,,,,,,,,,,,2087,2100,2019,rsFolder on state citations,citations_1,50011,211870,1,,entry citation,,,31733726,,,NMR Reveals Light-Induced Changes in the Dynamics of a Photoswitchable Fluorescent Protein,published,journal,Biophys. J.,,117,11,,1542-0086,,,,,,,,,,,,,,,,,,,,2087,2100,2019,rsFolder off state citations,ref_1,4976,211044,2,,reference citation,,,10092609,,"Lamberty et al. (1999) J. Biol. Chem. 274, 9320",Insect immunity. Isolation from the lepidopteran Heliothis virescens of a novel insect defensin with potent antifungal activity.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,274,14,,0021-9258,,,,,,,,,,,,,,,,,,,,9320,9326,1999,"Lepidoptera have been reported to produce several antibacterial peptides in response to septic injury. However, in marked contrast to other insect groups, no inducible antifungal molecules had been described so far in this insect order. Surprisingly, also cysteine-rich antimicrobial peptides, which predominate in the antimicrobial defense of other insects, had not been discovered in Lepidoptera. Here we report the isolation from the hemolymph of immune induced larvae of the lepidopteran Heliothis virescens of a cysteine-rich molecule with exclusive antifungal activity. We have fully characterized this antifungal molecule, which has significant homology with the insect defensins, a large family of antibacterial peptides directed against Gram-positive strains. Interestingly, the novel peptide shows also similarities with the antifungal peptide drosomycin from Drosophila. Thus, Lepidoptera appear to have built their humoral immune response against bacteria on cecropins and attacins. In addition, we report that Lepidoptera have conferred antifungal properties to the well conserved structure of antibacterial insect defensins through amino acid replacements." citations,entry_citation,4977,211066,1,,entry citation,,,,,,1H and 15N NMR assignments of the 7kd wheat lipid transfer protein,published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_1,4977,211067,2,,reference citation,,,,,"J.L.Pons, T.E.Malliavin and M.A.Delsuc, J. Biomol. NMR 8, 445-452 (1996)",,published,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_2,4977,211068,3,,reference citation,,,9730928,,"T.E.Malliavin, J.L.Pons and M.A.Delsuc, Bioinformatics 14-7, 624-631 (1998)",An NMR assignment module implemented in the Gifa NMR processing program.,published,journal,Bioinformatics,"Bioinformatics (Oxford, England)",14,7,,1367-4803,,,,,,,,,,,,,,,,,,,,624,631,1998,"MOTIVATION: Peptide and protein structures are determined daily using NMR spectroscopy. Assignment of the NMR spectra is an important step within the procedure and is usually the limiting one. Computer-aided assignment tools should be user friendly with open architecture to communicate with other programs involved in the structure determination. RESULTS: Here we present an interactive NMR assignment module which provides numerous graphic tools for the user. The module is composed of a database management system-handling peaks, spins and spin-systems. The assignment information is maintained as a set of interrelated associative arrays, which serve as generic high-level data structures. The module is developed in the macro language embedded in the Gifa NMR processing program (Pons et al. , J. Biomol. NMR, 8 , 445-452, 1996). This provides the user with a consistent interface, a set of sophisticated tools, and an easily extendible and customizable environment. AVAILABILITY: The program is available on request from the authors. The Gifa package can be accessed at: ((http://www.cbs. univ-montp1.fr/GIFA)) CONTACT: Marc-Andre.Delsuc@cbs.univ-montp1.fr" citations,entry_citation,4978,211088,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N backbone assignments for the C-terminal globular domain of agrin",published,journal,J. Biomol. NMR,,20,3,,,,,,,,,,,,,,,,,,,,,,295,296,2001, citations,ref_1,4978,211089,2,,reference citation,,,10202544,,"Sanes, J.R. & Lichtman, J.W. (1999) Development of the vertebrate neuromuscular junction. Annu. Rev. Neurosci 22: 389-442.",Development of the vertebrate neuromuscular junction.,published,journal,Annu. Rev. Neurosci.,Annual review of neuroscience,22,,,0147-006X,,,,,,,,,,,,,,,,,,,,389,442,1999,"We describe the formation, maturation, elimination, maintenance, and regeneration of vertebrate neuromuscular junctions (NMJs), the best studied of all synapses. The NMJ forms in a series of steps that involve the exchange of signals among its three cellular components--nerve terminal, muscle fiber, and Schwann cell. Although essentially any motor axon can form NMJs with any muscle fiber, an additional set of cues biases synapse formation in favor of appropriate partners. The NMJ is functional at birth but undergoes numerous alterations postnatally. One step in maturation is the elimination of excess inputs, a competitive process in which the muscle is an intermediary. Once elimination is complete, the NMJ is maintained stably in a dynamic equilibrium that can be perturbed to initiate remodeling. NMJs regenerate following damage to nerve or muscle, but this process differs in fundamental ways from embryonic synaptogenesis. Finally, we consider the extent to which the NMJ is a suitable model for development of neuron-neuron synapses." citations,ref_2,4978,211090,3,,reference citation,,,1333640,,"Marx, J. (1992) Getting it together at the synapse. Science 258: 1304-1306.",Getting it together at the synapse.,published,journal,Science,"Science (New York, N.Y.)",258,5086,,0036-8075,,,,,,,,,,,,,,,,,,,,1304,1306,1992, citations,ref_3,4978,211091,4,,reference citation,,,10491152,,"Hoch, W. (1999) Formation of the neuromuscular junction: agrin and its unusual receptors. Eur. J. Biochem. 265: 1-10.",Formation of the neuromuscular junction. Agrin and its unusual receptors.,published,journal,Eur. J. Biochem.,European journal of biochemistry / FEBS,265,1,,0014-2956,,,,,,,,,,,,,,,,,,,,1,10,1999,"Synapses are essential relay stations for the transmission of information between neurones and other cells. An ordered and tightly regulated formation of these structures is crucial for the functioning of the nervous system. The induction of the intensively studied synapse between nerve and muscle is initiated by the binding of neurone-specific isoforms of the basal membrane protein agrin to receptors on the surface of myotubes. Agrin activates a receptor complex that includes the muscle-specific kinase and most likely additional, yet to be identified, components. Receptor activation leads to the aggregation of acetylcholine receptors (AChR) and other proteins of the postsynaptic apparatus. This activation process has unique features which distinguish it from other receptor tyrosine kinases. In particular, the autophosphorylation of the kinase domain, which usually induces the recruitment of adaptor and signalling molecules, is not sufficient for AChR aggregation. Apparently, interactions of the extracellular domain with unknown components are also required for this process. Agrin binds to a second protein complex on the muscle surface known as the dystrophin-associated glycoprotein complex. This binding forms one end of a molecular link between the extracellular matrix and the cytoskeleton. While many components of the machinery triggering postsynaptic differentiation have now been identified, our picture of the molecular pathway causing the redistribution of synaptic proteins is still incomplete." citations,citations_1,50012,211885,1,,entry citation,,,,,,Structure and molecular recognition mechanism of IMP-13 beta-lactamase,submitted,journal,Antimicrobial Agents and Chemotherapy,Antimicrobial Agents and Chemotherapy,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50013,211899,1,,entry citation,,,,,,Structure and molecular recognition mechanism of IMP-13 beta-lactamase,in preparation,journal,Antimicrobial Agents and Chemotherapy,Antimicrobial Agents and Chemotherapy,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50126,212882,1,,entry citation,,,32236802,,,"1H, 13C, and 15N chemical shift assignment of human PACSIN1/syndapin I SH3 domain in solution",published,journal,Biomol. NMR Assignments,,14,2,,1874-270X,,,,,,,,,,,,,,,,,,,,175,178,2020, citations,ref_4,4978,211092,5,,reference citation,,,1329871,,"McMahan, U.J.Horton, S.E., Werle, M.J., Honig, L.S., Kroger, S., Ruegg, M.A. & Escher, G. (1992) Agrin isoforms and their roles in synaptogenesis. Curr. Opin. Cell Biol. 4: 869-874.",Agrin isoforms and their role in synaptogenesis.,published,journal,Curr. Opin. Cell Biol.,Current opinion in cell biology,4,5,,0955-0674,,,,,,,,,,,,,,,,,,,,869,874,1992,"Agrin is thought to mediate the motor neuron-induced aggregation of synaptic proteins on the surface of muscle fibers at neuromuscular junctions. Recent experiments provide direct evidence in support of this hypothesis, reveal the nature of agrin immunoreactivity at sites other than neuromuscular junctions, and have resulted in findings that are consistent with the possibility that agrin plays a role in synaptogenesis throughout the nervous system." citations,ref_5,4978,211093,6,,reference citation,,,8653788,,"Gautam, M., Noakes, P.G., Moscoso, L., Rupp, F., Scheller, R.H., & Hall, Z. (1996) Defective neuromuscular synaptogenesis in agrin-deficient mutant mice. Cell 85: 525-535.",Defective neuromuscular synaptogenesis in agrin-deficient mutant mice.,published,journal,Cell,Cell,85,4,,0092-8674,,,,,,,,,,,,,,,,,,,,525,535,1996,"During neuromuscular synapse formation, motor axons induce clustering of acetylcholine receptors (AChRs) in the muscle fiber membrane. The protein agrin, originally isolated from the basal lamina of the synaptic cleft, is synthesized and secreted by motoneurons and triggers formation of AChR clusters on cultured myotubes. We show here postsynaptic AChR aggregates are markedly reduced in number, size, and density in muscles of agrin-deficient mutant mice. These results support the hypothesis that agrin is a critical organizer of postsynaptic differentiation does occur in the mutant, suggesting the existence of a second-nerve-derived synaptic organizing signal. In addition, we show that intramuscular nerve branching and presynaptic differentiation are abnormal in the mutant, phenotypes which may reflect either a distinct effect of agrin or impaired retrograde signaling from a defective postsynaptic apparatus." citations,ref_6,4978,211094,7,,reference citation,,,9425009,,"Megeath, L.J. & Fallon, J.R. (1998) Intracellular calcium regulates agrin-induced acetylcholine receptor clustering. J. Neurosci. 18: 672-678.",Intracellular calcium regulates agrin-induced acetylcholine receptor clustering.,published,journal,J. Neurosci.,The Journal of neuroscience : the official journal of the Society for Neuroscience,18,2,,0270-6474,,,,,,,,,,,,,,,,,,,,672,678,1998,"Agrin is an extracellular matrix protein that directs neuromuscular junction formation. Early signal transduction events in agrin-mediated postsynaptic differentiation include activation of a receptor tyrosine kinase and phosphorylation of acetylcholine receptors (AChRs), but later steps in this pathway are unknown. Here, we have investigated the role of intracellular calcium in agrin-induced AChR clustering on cultured myotubes. Clamping intracellular calcium levels by loading with the fast chelator BAPTA inhibited agrin-induced AChR aggregation. In addition, preexisting AChR aggregates dispersed under these conditions, indicating that the maintenance of AChR clusters is similarly dependent on intracellular calcium fluxes. The decrease in AChR clusters in BAPTA-loaded cells was dose-dependent and reversible, and no change in the number or mobility of AChRs was observed. Clamping intracellular calcium did not block agrin-induced tyrosine phosphorylation of the AChR beta-subunit, indicating that intracellular calcium fluxes are likely to act downstream from or parallel to AChR phosphorylation. Finally, the targets of the intracellular calcium are likely to be close to the calcium source, since agrin-induced AChR clustering was unaffected in cells loaded with EGTA, a slower-binding calcium chelator. These findings distinguish a novel step in the signal transduction mechanism of agrin and raise the possibility that the pathways mediating agrin- and activity-driven changes in synaptic architecture could intersect at the level of intracellular calcium fluxes." citations,ref_7,4978,211095,8,,reference citation,,,10339611,,"Donahue, J.E., Berzin, T.M., Rafii, M.S., Glass, D.J., Yancopoulos, G.D., Fallon, J.R., & Stopa, E.G. (1999) Agrin in alzheimer's disease: altered solubility and abnormal distribution within microvasculature and brain parenchyma. Proc. Natl. Acad. Sci. USA 96: 6468-6472.",Agrin in Alzheimer's disease: altered solubility and abnormal distribution within microvasculature and brain parenchyma.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,96,11,,0027-8424,,,,,,,,,,,,,,,,,,,,6468,6472,1999,"Agrin is a heparan sulfate proteoglycan that is widely expressed in neurons and microvascular basal lamina in the rodent and avian central nervous system. Agrin induces the differentiation of nerve-muscle synapses, but its function in either normal or diseased brains is not known. Alzheimer's disease (AD) is characterized by loss of synapses, changes in microvascular architecture, and formation of neurofibrillary tangles and senile plaques. Here we have asked whether AD causes changes in the distribution and biochemical properties of agrin. Immunostaining of normal, aged human central nervous system revealed that agrin is expressed in neurons in multiple brain areas. Robust agrin immunoreactivity was observed uniformly in the microvascular basal lamina. In AD brains, agrin is highly concentrated in both diffuse and neuritic plaques as well as neurofibrillary tangles; neuronal expression of agrin also was observed. Furthermore, patients with AD had microvascular alterations characterized by thinning and fragmentation of the basal lamina. Detergent extraction and Western blotting showed that virtually all the agrin in normal brain is soluble in 1% SDS. In contrast, a large fraction of the agrin in AD brains is insoluble under these conditions, suggesting that it is tightly associated with beta-amyloid. Together, these data indicate that the agrin abnormalities observed in AD are closely linked to beta-amyloid deposition. These observations suggest that altered agrin expression in the microvasculature and the brain parenchyma contribute to the pathogenesis of AD." citations,ref_8,4978,211096,9,,reference citation,,,10673326,,"Cotman, S.L., Halfter, W., & Cole G.J. (2000) Agrin binds to b-amyloid (Ab), accelerates Ab fibril formation, and is localized to Ab deposits in Alzheimer's disease brain . Molec. Cell. Neurosci. 15: 183-198.","Agrin binds to beta-amyloid (Abeta), accelerates abeta fibril formation, and is localized to Abeta deposits in Alzheimer's disease brain.",published,journal,Mol. Cell. Neurosci.,Molecular and cellular neurosciences,15,2,,1044-7431,,,,,,,,,,,,,,,,,,,,183,198,2000,"Agrin is an extracellular matrix heparan sulfate proteoglycan (HSPG) well known for its role in modulation of the neuromuscular junction during development. Although agrin is one of the major HSPGs of the brain, its function there remains elusive. Here we provide evidence suggesting a possible function for agrin in Alzheimer's disease brain. Agrin protein binds the amyloidogenic peptide Abeta (1-40) in its fibrillar state via a mechanism that involves the heparan sulfate glycosaminoglycan chains of agrin. Furthermore, agrin is able to accelerate Abeta fibril formation and protect Abeta (1-40) from proteolysis, in vitro. Supporting a biological significance for these in vitro data, immunocytochemical studies demonstrate agrin's presence within senile plaques and cerebrovascular amyloid deposits, and agrin immunostained capillaries exhibit pathological alterations in AD brain. These data therefore suggest that agrin may be an important factor in the progression of Abeta peptide aggregation and/or its persistence in Alzheimer's disease brain." citations,citations_1,50014,211915,1,,entry citation,,,31974312,,,Structural analysis of the intrinsically disordered splicing factor Spp2 and its binding to the DEAH-box ATPase Prp2,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,117,6,,1091-6490,,,,,,,,,,,,,,,,,,,,2948,2956,2020, citations,citations_1,50017,211934,1,,entry citation,,,32029630,,,Valence and Patterning of Aromatic Residues Determine the Phase Behavior of Prion-Like Domains,published,journal,Science,"Science (New York, N.Y.)",367,6478,,1095-9203,,,,,,,,,,,,,,,,,,,,694,699,2020, citations,citations_1,50019,211947,1,,entry citation,,,32077246,,,Pro-Islet Amyloid Polypeptide in Micelles Contains a Helical Prohormone Segment,published,journal,FEBS J.,,287,20,,,,,,,,,,,,,,,,,,,,,,4440,4457,2020, citations,ref_9,4978,211097,10,,reference citation,,,9480764,,"Beckmann,G., Hanke, J., Bork, P. & Reich, J.G. (1998). Merging extracellular domains: fold prediction for laminin G-like and amino-terminal thrombospondin-like modules based on homology to pentraxins. J. Mol. Biol. 275: 725-730.",Merging extracellular domains: fold prediction for laminin G-like and amino-terminal thrombospondin-like modules based on homology to pentraxins.,published,journal,J. Mol. Biol.,Journal of molecular biology,275,5,,0022-2836,,,,,,,,,,,,,,,,,,,,725,730,1998,"Using a new method for construction and database searches of sequence consensus strings, we have identified a new superfamily of protein modules comprising laminin G, thrombospondin N and the pentraxin families. The conserved patterns correspond mainly to hydrophobic core residues located in central beta strands of the known three-dimensional structures of two pentraxins, the human C-reactive protein and the serum amyloid P-component. Thus, we predict a similar jellyroll fold for all members of this superfamily. In addition, the conservation of two exposed aspartate residues in the majority of superfamily members suggests hitherto unrecognised functional sites." citations,ref_10,4978,211098,11,,reference citation,,,9430625,,"Denzer, A.J., Schulthess, T., Fauser, C., Schumacher, B., Kammerer, R.A., Engel, J. & Ruegg, M.A. (1998) Electron microscopic structure of agrin and mapping of its binding site in laminin-1. EMBO J 17: 335-343.",Electron microscopic structure of agrin and mapping of its binding site in laminin-1.,published,journal,EMBO J.,The EMBO journal,17,2,,0261-4189,,,,,,,,,,,,,,,,,,,,335,343,1998,"Agrin is a large, multidomain heparan sulfate proteoglycan that is associated with basement membranes of several tissues. Particular splice variants of agrin are essential for the formation of synaptic structures at the neuromuscular junction. The binding of agrin to laminin appears to be required for its localization to synaptic basal lamina and other basement membranes. Here, electron microscopy was used to determine the structure of agrin and to localize its binding site in laminin-1. Agrin appears as an approximately 95 nm long particle that consists of a globular, N-terminal laminin-binding domain, a central rod predominantly formed by the follistatin-like domains and three globular, C-terminal laminin G-like domains. In a few cases, heparan sulfate glycosaminoglycan chains were seen emerging from the central portion of the core protein. Moreover, we show that agrin binds to the central region of the three-stranded, coiled-coil oligomerization domain in the long arm of laminin-1, which mediates subunit assembly of the native laminin molecule. In summary, our data show for the first time a protein-protein interaction of the extracellular matrix that involves a coiled-coil domain, and they assign a novel role to this domain of laminin-1. Based on this, we propose that agrin associates with basal lamina in a polarized way." citations,ref_11,4978,211099,12,,reference citation,,,8654359,,"Meier, T., Gessemann, M., Cavalli, V., Ruegg, M.A. & Wallace, B.G. (1996) AChR phophorylation and aggregation induced by an agrin fragment that lacks the binding domain for a-dystroglycan. J. Cell Sci. 112: 1213-1223.",AChR phosphorylation and aggregation induced by an agrin fragment that lacks the binding domain for alpha-dystroglycan.,published,journal,EMBO J.,The EMBO journal,15,11,,0261-4189,,,,,,,,,,,,,,,,,,,,2625,2631,1996,"Agrin induces both phosphorylation and aggregation of nicotinic acetylcholine receptors (AChRs) when added to myotubes in culture, apparently by binding to a specific receptor on the myotube surface. One such agrin receptor is alpha-dystroglycan, although binding to alpha-dystroglycan appears not to mediate AChR aggregation. To determine whether agrin-induced AChR phosphorylation is mediated by alpha-dystroglycan or by a different agrin receptor, fragments of recombinant agrin that differ in affinity for alpha-dystroglycan were examined for their ability to induce AChR phosphorylation and aggregation in mouse C2 myotubes. The carboxy-terminal 95 kDa agrin fragment agrin-c95(A0B0), which binds to alpha-dystroglycan with high affinity, failed to induce AChR phosphorylation and aggregation. In contrast, agrin-c95(A4B8) which binds less strongly to alpha-dystroglycan, induced both phosphorylation and aggregation, as did a small 21 kDa fragment of agrin, agrin-c21(B8), that completely lacks the binding domain for alpha-dystroglycan. We conclude that agrin-induced AChR phosphorylation and aggregation are triggered by an agrin receptor that is distinct from alpha-dystroglycan." citations,ref_12,4978,211100,13,,reference citation,,,10619025,,"Hohenester, E., Tisi, D., Talts, J.F., & Timpl, R. (1999) The crystal structure of a laminin G-like module reveals the molecular basis of a-dystroglycan binding to laminins, perlecan, and agrin. Molecular Cell 4: 783-792.","The crystal structure of a laminin G-like module reveals the molecular basis of alpha-dystroglycan binding to laminins, perlecan, and agrin.",published,journal,Mol. Cell,Molecular cell,4,5,,1097-2765,,,,,,,,,,,,,,,,,,,,783,792,1999,"Laminin G-like (LG) modules in the extracellular matrix glycoproteins laminin, perlecan, and agrin mediate the binding to heparin and the cell surface receptor alpha-dystroglycan (alpha-DG). These interactions are crucial to basement membrane assembly, as well as muscle and nerve cell function. The crystal structure of the laminin alpha 2 chain LG5 module reveals a 14-stranded beta sandwich. A calcium ion is bound to one edge of the sandwich by conserved acidic residues and is surrounded by residues implicated in heparin and alpha-DG binding. A calcium-coordinated sulfate ion is suggested to mimic the binding of anionic oligosaccharides. The structure demonstrates a conserved function of the LG module in calcium-dependent lectin-like alpha-DG binding." citations,ref_13,4978,211101,14,,reference citation,,,2839519,,"Wallace, B.G. (1988) Regulation of agrin-induced acetylcholine receptor aggregation by Ca++ and phorbol ester, J. Cell Biol. 107: 267-278.",Regulation of agrin-induced acetylcholine receptor aggregation by Ca++ and phorbol ester.,published,journal,J. Cell Biol.,The Journal of cell biology,107,1,,0021-9525,,,,,,,,,,,,,,,,,,,,267,278,1988,"Agrin, a protein extracted from the electric organ of Torpedo californica, induces the formation of specializations on cultured chick myotubes that resemble the postsynaptic apparatus at the neuromuscular junction. The aim of the studies reported here was to characterize the effects of agrin on the distribution of acetylcholine receptors (AChRs) and cholinesterase as a step toward determining agrin's mechanism of action. When agrin was added to the medium bathing chick myotubes small (less than 4 micron 2) aggregates of AChRs began to appear within 2 h and increased rapidly in number until 4 h. Over the next 12-20 h the number of aggregates per myotube decreased as the mean size of each aggregate increased to approximately 15 micron 2. The accumulation of AChRs into agrin-induced aggregates occurred primarily by lateral migration of AChRs already in the myotube plasma membrane at the time agrin was added to the cultures. Aggregates of AChRs and cholinesterase remained as long as agrin was present in the medium; if agrin was removed the number of aggregates declined slowly. The formation and maintenance of agrin-induced AChR aggregates required Ca++, Co++ and Mn++ inhibited agrin-induced AChR aggregation and increased the rate of aggregate dispersal. Mg++ and Sr++ could not substitute for Ca++. Agrin-induced receptor aggregation also was inhibited by phorbol 12-myristate 13-acetate, an activator of protein kinase C, and by inhibitors of energy metabolism. The similarities between agrin's effects on cultured myotubes and events that occur during formation of neuromuscular junctions support the hypothesis that axon terminals release molecules similar to agrin that induce the differentiation of the postsynaptic apparatus." citations,citations_1,50020,211963,1,,entry citation,,,32031736,10.1002/2211-5463.12807,,Structural and biophysical characterization of the type VII collagen vWFA2 subdomain leads to identification of two binding sites,published,journal,FEBS Open Bio.,,10,4,,,,,,,,,,,,,,,,,,,,,,580,592,2020, citations,ref_14,4978,211102,15,,reference citation,,,8587694,,"Deyst, K.A., Ma, J. & Fallon, J.R. (1995) Agrin: toward a molecular understanding of synapse regeneration. Neurosurgery 37: 71-77.",Agrin: toward a molecular understanding of synapse regeneration.,published,journal,Neurosurgery,Neurosurgery,37,1,,0148-396X,,,,,,,,,,,,,,,,,,,,71,77,1995,"One of the foremost challenges to repairing damage after stroke, trauma, or disease is the regeneration of synaptic connections between neurons. Here, we consider recent strides in our understanding of the molecular basis of synapse formation and regeneration. We will focus on the protein agrin, a key player in synaptogenesis at neuromuscular junctions and perhaps at central nervous system synapses as well. Insights into agrin and its receptor could guide the development of rational therapies to combat neuronal degeneration. We will also consider recent surprising and provocative data linking the mechanisms of synapse formation and the cellular pathology in Duchenne muscular dystrophy." citations,entry_citation,4979,211126,1,,entry citation,,,11700049,,,"Communication: NMR structure of the Euplotes raikovi pheromone Er-23 and identification of its five disulfide bonds",published,journal,J. Mol. Biol.,,313,5,,,,,,,,,,,,,,,,,,,,,,923,931,2001, citations,reference_1,4979,211127,2,,reference citation,,,11246857,,"Liu A, Luginbuhl P, Zerbe O, Ortenzi C, Luporini P, Wuthrich K. NMR structure of the pheromone Er-22 from Euplotes raikovi. J Biomol NMR. 2001 Jan;19(1):75-8.",NMR structure of the pheromone Er-22 from Euplotes raikovi.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,19,1,,0925-2738,,,,,,,,,,,,,,,,,,,,75,78,2001, citations,reference_2,4979,211128,3,,reference citation,,,,,"Bartels C., Xia T., Billeter M., Guntert P., Wuthrich K. J. Biomol. NMR, Vol.5, p1-10 (1995).",,published,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,reference_3,4979,211129,4,,reference citation,,,9367762,,"Guntert P, Mumenthaler C, Wuthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA J Mol Biol. 1997 Oct 17;273(1):283-98.",Torsion angle dynamics for NMR structure calculation with the new program DYANA.,published,journal,J. Mol. Biol.,Journal of molecular biology,273,1,,0022-2836,,,,,,,,,,,,,,,,,,,,283,298,1997,"The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from distance constraints and torsion angle constraints collected by nuclear magnetic resonance (NMR) experiments performs simulated annealing by molecular dynamics in torsion angle space and uses a fast recursive algorithm to integrate the equations of motions. Torsion angle dynamics can be more efficient than molecular dynamics in Cartesian coordinate space because of the reduced number of degrees of freedom and the concomitant absence of high-frequency bond and angle vibrations, which allows for the use of longer time-steps and/or higher temperatures in the structure calculation. It also represents a significant advance over the variable target function method in torsion angle space with the REDAC strategy used by the predecessor program DIANA. DYANA computation times per accepted conformer in the ""bundle"" used to represent the NMR structure compare favorably with those of other presently available structure calculation algorithms, and are of the order of 160 seconds for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300 computer. Test calculations starting from conformers with random torsion angle values further showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures." citations,reference_4,4979,211130,5,,reference citation,,,8914272,,"Luginbuhl P, Guntert P, Billeter M, Wuthrich K. The new program OPAL for molecular dynamics simulations and energy refinements of biological macromolecules. J Biomol NMR. 1996 Sep;8(2):136-46.",The new program OPAL for molecular dynamics simulations and energy refinements of biological macromolecules.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,8,2,,0925-2738,,,,,,,,,,,,,,,,,,,,136,146,1996,"A new program for molecular dynamics (MD) simulation and energy refinement of biological macromolecules, OPAL, is introduced. Combined with the supporting program TRAJEC for the analysis of MD trajectories, OPAL affords high efficiency and flexibility for work with different force fields, and offers a user-friendly interface and extensive trajectory analysis capabilities. Salient features are computational speeds of up to 1.5 GFlops on vector supercomputers such as the NEC SX-3, ellipsoidal boundaries to reduce the system size for studies in explicit solvents, and natural treatment of the hydrostatic pressure. Practical applications of OPAL are illustrated with MD simulations of pure water, energy minimization of the NMR structure of the mixed disulfide of a mutant E. coli glutaredoxin with glutathione in different solvent models, and MD simulations of a small protein, pheromone Er-2, using either instantaneous or time-averaged NMR restraints, or no restraints." citations,entry_citation,498,211148,1,,entry citation,,,,,"Yu, Liping P., Smith, Gary M., ""Characterization of pH-Dependent Conformational Heterogeneity in Rhodospirillum rubrum Cytochrome c2 Using 15N and 1H NMR,"" Biochemistry 29, 2920-2925 (1990).","Characterization of pH-Dependent Conformational Heterogeneity in Rhodospirillum rubrum Cytochrome c2 Using 15N and 1H NMR",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,2920,2925,1990, citations,entry_citation,4980,211163,1,,entry citation,,,,,,"Letter to the Editor: 1H and 15N sequential assignment and secondary structure of the monomeric N67D mutant of bovine seminal ribonuclease",published,journal,J. Biomol. NMR,,20,3,,,,,,,,,,,,,,,,,,,,,,289,290,2001, citations,ref_1,4980,211164,2,,reference citation,,,8520220,,"Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., Bax, A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR (1995) 6, 277-93",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,citation_1,5648,229404,2,,reference citation,,,12522297,,,Random Coil Proton Chemical Shifts of Deoxyribonucleic Acids,published,journal,J. Biomol. NMR,,24,4,,,,,,,,,,,,,,,,,,,,,,329,337,2002, citations,ref_3,4980,211166,4,,reference citation,,,9367762,,"Guntert, P., Mumenthaler, C., Wuthrich, K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. (1997) 273, 283-98",Torsion angle dynamics for NMR structure calculation with the new program DYANA.,published,journal,J. Mol. Biol.,Journal of molecular biology,273,1,,0022-2836,,,,,,,,,,,,,,,,,,,,283,298,1997,"The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from distance constraints and torsion angle constraints collected by nuclear magnetic resonance (NMR) experiments performs simulated annealing by molecular dynamics in torsion angle space and uses a fast recursive algorithm to integrate the equations of motions. Torsion angle dynamics can be more efficient than molecular dynamics in Cartesian coordinate space because of the reduced number of degrees of freedom and the concomitant absence of high-frequency bond and angle vibrations, which allows for the use of longer time-steps and/or higher temperatures in the structure calculation. It also represents a significant advance over the variable target function method in torsion angle space with the REDAC strategy used by the predecessor program DIANA. DYANA computation times per accepted conformer in the ""bundle"" used to represent the NMR structure compare favorably with those of other presently available structure calculation algorithms, and are of the order of 160 seconds for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300 computer. Test calculations starting from conformers with random torsion angle values further showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures." citations,ref_4,4980,211167,5,,reference citation,,,,,"Pearlman, D.A., Case, D.A., Caldwell, J.W., Ross, W.S., Cheatham III, T.E., DeBolt, S., Ferguson, D., Seibel, G & Kollman, P.A. AMBER, a computer program for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to elucidate the structures and energies of molecules. Comp. Phys. Commun. (1995) 91, 1-41",,published,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4981,211187,1,,entry citation,,,11124037,,,"Identification of the phospholipid binding site of human beta2-glycoprotein I domain V by heteronuclear magnetic resonance",published,journal,J. Mol. Biol.,,304,5,,,,,,,,,,,,,,,,,,,,,,927,940,2000, citations,ref_1,4981,211188,2,,reference citation,,,8520220,,"Delaglio, F., Grzesiek, S., Vuister, G., Zhu, G., Pfeifer, J. & Bax, A. (1995). NMRPipe: a multidimensional spectral processing system based on UNIX Pipes. J. Biomol. NMR, 6, 277-293.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref_2,4981,211189,3,,reference citation,,,,,"Garrett, D.S., Powers, R., Gronenborn, A.M. & Clore, G.M. (1991). A common sense approach to peak picking in two-, three-, and four-dimensional spectra using automatic computer analysis of contour diagrams. J. Magn. Reson. 95, 214-220.",,published,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4982,211213,1,,entry citation,,,18088104,,,"Structural and motional changes induced in apo-S100A1 protein by the disulfide formation between its Cys 85 residue and beta-mercaptoethanol",published,journal,Biochemistry,,47,2,,,,,,,,,,,,,,,,,,,,,,640,650,2008, citations,ref_1,4982,211214,2,,reference citation,,,8520220,,"NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR. 1995 Nov;6(3):277-93.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref_2,4982,211215,3,,reference citation,,,,,"Bartels C., Xia T., Billeter M., Guntert P., and Wuthrich K. (1995) The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J. Biomol. NMR, 6, 1-10",,published,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50021,211982,1,,entry citation,,,31628949,,,The WW1 Domain Enhances Autoinhibition in Smurf Ubiquitin Ligases,published,journal,J. Mol. Biol.,Journal of molecular biology,431,24,,1089-8638,,,,,,,,,,,,,,,,,,,,4834,4847,2019, citations,citations_1,50022,211995,1,,entry citation,,,31628949,,,The WW1 Domain Enhances Autoinhibition in Smurf Ubiquitin Ligases,published,journal,J. Mol. Biol.,Journal of molecular biology,431,24,,1089-8638,,,,,,,,,,,,,,,,,,,,4834,4847,2019, citations,citations_1,50023,212008,1,,entry citation,,,31628949,,,The WW1 Domain Enhances Autoinhibition in Smurf Ubiquitin Ligases,published,journal,J. Mol. Biol.,Journal of molecular biology,431,24,,1089-8638,,,,,,,,,,,,,,,,,,,,4834,4847,2019, citations,ref_3,4982,211216,4,,reference citation,,,10212987,,"Cornilescu G, Delaglio F, Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J Biomol NMR. 1999 Mar;13(3):289-302.",Protein backbone angle restraints from searching a database for chemical shift and sequence homology.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,13,3,,0925-2738,,,,,,,,,,,,,,,,,,,,289,302,1999,"Chemical shifts of backbone atoms in proteins are exquisitely sensitive to local conformation, and homologous proteins show quite similar patterns of secondary chemical shifts. The inverse of this relation is used to search a database for triplets of adjacent residues with secondary chemical shifts and sequence similarity which provide the best match to the query triplet of interest. The database contains 13C alpha, 13C beta, 13C', 1H alpha and 15N chemical shifts for 20 proteins for which a high resolution X-ray structure is available. The computer program TALOS was developed to search this database for strings of residues with chemical shift and residue type homology. The relative importance of the weighting factors attached to the secondary chemical shifts of the five types of resonances relative to that of sequence similarity was optimized empirically. TALOS yields the 10 triplets which have the closest similarity in secondary chemical shift and amino acid sequence to those of the query sequence. If the central residues in these 10 triplets exhibit similar phi and psi backbone angles, their averages can reliably be used as angular restraints for the protein whose structure is being studied. Tests carried out for proteins of known structure indicate that the root-mean-square difference (rmsd) between the output of TALOS and the X-ray derived backbone angles is about 15 degrees. Approximately 3% of the predictions made by TALOS are found to be in error." citations,ref_4,4982,211217,5,,reference citation,,,,,"Hoffman R.E., and Davies D.B. (1988) Temperature dependence of NMR secondary references for D2O and (CD3)2SO solutions. Magn. Reson. in Chemistry, 26, 523-525",,published,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_5,4982,211218,6,,reference citation,,,8589602,,"Wishart DS, Bigam CG, Yao J, Abildgaard F, Dyson HJ, Oldfield E, Markley JL, Sykes BD. 1H, 13C and 15N chemical shift referencing in biomolecular NMR. J Biomol NMR. 1995 Sep;6(2):135-40.","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,4983,211248,1,,entry citation,,,,,,"Backbone 1H,13C,15N and side chain 13C assignment of YUH1-Ub in a 35 kDa covalent complex",in preparation,journal,J. Biomol. NMR,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4984,211274,1,,entry citation,,21671747,,,,The Solution Structure and Interactions of CheW from Thermotoga maritima,published,journal,Nat. Struct. Biol.,Nature Structural Biology,9,,,,,,,,,,,,,,,,,,,,,,,121,125,2002, citations,entry_citation,4985,211289,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C, and 15N assignment of the flavodoxin-like domain of the Escherichia coli sulfite reductase",published,journal,J. Biomol. NMR,,21,1,,,,,,,,,,,,,,,,,,,,,,71,72,2001, citations,entry_citation,4986,211321,1,,entry citation,,21293199,11399072,,,"Ligand-induced Structural changes to Maltodextrin-binding Protein as Studied by Solution NMR Spectroscopy",published,journal,J. Mol. Biol.,Journal of Molecular Biology,309,4,,,,,,,,,,,,,,,,,,,,,,961,974,2001, citations,entry_citation,4987,211341,1,,entry citation,,21293199,11399072,,,"Ligand-induced Structural changes to Maltodextrin-binding Protein as Studied by Solution NMR Spectroscopy",published,journal,J. Mol. Biol.,Journal of Molecular Biology,309,4,,,,,,,,,,,,,,,,,,,,,,961,974,2001, citations,entry_citation,4988,211376,1,,entry citation,,,,,,Three-dimensional Solution Structure Determination of Huwentoxin-II by 2D 1H-NMR,submitted,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_1,4988,211377,2,,reference citation,,,12053191,,"Q. SHU, S.Y. LU, X.C. GU, S.P. LIANG. Sequence-specific assignment of 1H-NMR resonance and determination of the secondary structure of HWTX-II. Acta Biochim. et Biophys. Sinica 2001,33: 65",Sequence-specific Assignment of (1)H-NMR Resonance and Determination of the Secondary Structure of HWTX-II.,published,journal,Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao,Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica,33,1,,0582-9879,,,,,,,,,,,,,,,,,,,,65,70,2001,"Huwentoxin-II (HWTX-II)is an insecticidal peptide purified from the venom of spider Selenocosmia huwena. The structure of this toxin in solution was investigated using 2D-NMR. The complete sequence-specific assignments of proton resonance in the (1)H-NMR spectra of HWTX-II were obtained by analyzing a series of 2D spectrum, including COSY, DQF-COSY, TOCSY and NOESY. All the backbone protons and side chain protons, except epsilonNH(2) protons of Lys residues, were identified by d(alphaN), d(alpha&dgr);, d(NN) and d(betaN) connectivities. The results provide a basis for further determination of the solution conformation of HWTX-II. Furthermore the secondary structure of HWTX-II was determined from NMR data. It contained mainly extended conformation, especially a double-stranded anti-parallel beta-sheet with Trp27--Cys29 and Cys34--Lys36 at the C terminal, and it lacked helix. These characters of the secondary structure of HWTX-II were similar to those spider toxins which structure in solution had been reported." citations,ref_2,4988,211378,3,,reference citation,,,11298747,,"Q.SHU,R.H.HUANG,S.P.LIANG Assignment of disulfide bonds of huwentoxin-ii by Edman degradation sequencing and stepwise thiol modification. Eur. J. Biochem. 2001, 268(8):2301-2307",Assignment of the disulfide bonds of huwentoxin-II by Edman degradation sequencing and stepwise thiol modification.,published,journal,Eur. J. Biochem.,European journal of biochemistry / FEBS,268,8,,0014-2956,,,,,,,,,,,,,,,,,,,,2301,2307,2001,"A novel strategy combining Edman degradation and thiol modification was developed to assign the three disulfides of huwentoxin-II (HWTX-II), an insecticidal peptide purified from the venom of the spider Selenocosmia huwena. Phenylthiohydantoin (Pth) derivatives of Cys and the elimination product, dehydroalanine (DeltaSer), can be observed in the Cys cycles during Edman degradation of native HWTX-II. The appearance of two products indicates that the disulfides of HWTX-II were split and that the free thiol group of the second half cystine has been generated. Information about the nature of the disulfide bridges of HWTX-II could be obtained from the sequencing signal if the nascent thiols were modified stepwise by 4-vinylpyridine. Using this method the disulfide bridges of HWTX-II were assigned as Cys4-Cys18, Cys8-Cys29 and Cys23-Cys34, which is different from that seen in HWTX-I, a neurotoxic peptide from the same spider. Using this strategy, one can assign the disulfide bonds of small proteins by sequencing and modification n - 1 times, where n is the number of disulfide bonds in the protein. The above assignment of the disulfide bonds of HWTX-II was confirmed by MALDI-TOF MS of tryptic fragments of HWTX-II. Some disulfide interchanging during proteolysis was observed by monitoring the kinetics of proteolysis of HWTX-II by MALDI-TOF MS." citations,ref_3,4988,211379,4,,reference citation,,,10424342,,"Purification and characterization of huwentoxin-II, a neurotoxic peptide from the venom of the Chinese bird spider Selenocosmia huwena. J. Pept. Res. 1999 May;53(5):486-491","Purification and characterization of huwentoxin-II, a neurotoxic peptide from the venom of the Chinese bird spider Selenocosmia huwena.",published,journal,J. Pept. Res.,The journal of peptide research : official journal of the American Peptide Society,53,5,,1397-002X,,,,,,,,,,,,,,,,,,,,486,491,1999,"A neurotoxic peptide, huwentoxin-II (HWTX-II), was purified from the venom of the Chinese bird spider Selenocosmia huwena by ion exchange chromatography and reversed phase HPLC. The toxin can reversibly paralyse cockroaches for several hours, with an ED50 of 127 +/- 54 microg/g. HWTX-II blocks neuromuscular transmission in an isolated mouse phrenic nerve diaphragm preparation and acts cooperatively to potentiate the activity of huwentoxin-I. The complete amino sequence of HWTX-II was determined and found to consist of 37 amino acid residues, including six Cys residues. There is microheterogeneity (Ile/Gln) in position 10, and mass spectrometry indicated that the two isoproteins have a tendency to dimerize. It was determined by mass spectrometry that the six Cys residues are involved in three disulphide bonds. The sequence of HWTX-II is highly homologous with ESTX, a toxin from the tarantula Eurypefina californicum." citations,entry_citation,4989,211395,1,,entry citation,,21416009,,,,Solution Structure of B.subtilis Acyl Carrier Protein,published,journal,Structure,,9,,,,,,,,,,,,,,,,,,,,,,,277,287,2001, citations,entry_citation,499,211412,1,,entry citation,,,,,"Satterlee, James D., Moench, Susan J., ""Proton hyperfine resonance assignments using the nuclear Overhauser effect for ferric forms of horse and tuna cytochrome c,"" Biophys. J. 52, 101-107 (1987).","Proton hyperfine resonance assignments using the nuclear Overhauser effect for ferric forms of horse and tuna cytochrome c",published,journal,Biophys. J.,,52,,,,,,,,,,,,,,,,,,,,,,,101,107,1987, citations,entry_citation,4990,211428,1,,entry citation,,22069898,12074582,,,"Solution structure of betacellulin, a new member of EGF-family ligands.",published,journal,Biochem. Biophys. Res. Commun.,,294,5,,,,,,,,,,,,,,,,,,,,,,1040,1046,2002, citations,entry_citation,4991,211443,1,,entry citation,,21937742,11939770,,,"Identification of a Novel Archaebacterial Thioredoxin: Determination of Function through Structure",published,journal,Biochemistry,,41,15,,,,,,,,,,,,,,,,,,,,,,4760,4770,2002, citations,entry_citation,4992,211457,1,,entry citation,,,,,,"Letter to the Editor: Assignment of 1H, 13C and 15N NMR signals from toluene 4-monooxygenase Rieske ferredoxin in its oxidized state",published,journal,J. Biomol. NMR,,21,1,,,,,,,,,,,,,,,,,,,,,,73,74,2001, citations,entry_citation,4993,211485,1,,entry citation,,21665736,,,,Spatial Structure of Zervamicin IIB bound to DPC Micelles: Implications for Voltage-gating,published,journal,Biophys. J.,,82,2,,,,,,,,,,,,,,,,,,,,,,762,771,2002, citations,entry_citation,4994,211509,1,,entry citation,,21326095,11320096,,,"Structure of the C-domain of Human Cardiac Troponin C in Complex with the Ca2+ Sensitizing drug EMD 57033",published,journal,J. Biol. Chem.,,276,27,,,,,,,,,,,,,,,,,,,,,,25456,25466,2001, citations,entry_citation,4995,211539,1,,entry citation,,21460866,11575936,,,"Solution NMR Structure and Folding Dynamics of the N-terminus of a rat Non-muscle Alpha-tropomyosin in an Engineered Chimeric Protein",published,journal,J. Mol. Biol.,,312,4,,,,,,,,,,,,,,,,,,,,,,833,847,2001, citations,entry_citation,4996,211581,1,,entry citation,,,,,,"Letter to the Editor: NMR-Based Structure of the Conserved Protein MTH865 from the Archaeon Methanobacterium thermoautotrophicum",published,journal,J. Biomol. NMR,,21,1,,,,,,,,,,,,,,,,,,,,,,63,66,2001, citations,entry_citation,4997,211599,1,,entry citation,,21415430,11524020,,,"Flexibility and Bioactivity of Insulin: an NMR Investigation of the Solution Structure and Folding of an Unusually Flexible Human Insulin Mutant with Increased Biological Activity",published,journal,Biochemistry,,40,35,,,,,,,,,,,,,,,,,,,,,,10732,10740,2001, citations,entry_citation,4998,211622,1,,entry citation,,,,,,"1H, 13C and 15N Chemical Shift Assignments for the HPV-18 E2 DNA-binding Domain",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,4999,211643,1,,entry citation,,,,,,"Letter to the Editor: Assignment of the 1H, 15N and 13C resonances of the nucleocapsid-binding domain of the Sendai virus Phosphoprotein",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,21,1,,,,,,,,,,,,,,,,,,,,,,75,76,2001, citations,entry_citation,5,211668,1,,entry citation,,,,,"Gooley, Paul R., Norton, Raymond S., ""Specific assignment of resonances in the 1H nuclear magnetic resonance spectrum of the polypeptide cardiac stimulant anthopleurin-A,"" Eur. J. Biochem. 153, 529-539 (1985).","Specific assignment of resonances in the 1H nuclear magnetic resonance spectrum of the polypeptide cardiac stimulant anthopleurin-A",published,journal,Eur. J. Biochem.,,153,,,,,,,,,,,,,,,,,,,,,,,529,539,1985, citations,entry_citation,50,211679,1,,entry citation,,,,,"Lecomte, Juliette T.J., Kaplan, David, Llinas, M., Thunberg, Eva, Samuelsson, Gunnar, ""Proton magnetic resonance characterization of phoratoxins and homologous proteins related to crambin,"" Biochemistry 26, 1187-1194 (1987).","Proton magnetic resonance characterization of phoratoxins and homologous proteins related to crambin",published,journal,Biochemistry,,26,,,,,,,,,,,,,,,,,,,,,,,1187,1194,1987, citations,entry_citation,500,211692,1,,entry citation,,,,,"Satterlee, James D., Moench, Susan J., ""Proton hyperfine resonance assignments using the nuclear Overhauser effect for ferric forms of horse and tuna cytochrome c,"" Biophys. J. 52, 101-107 (1987).","Proton hyperfine resonance assignments using the nuclear Overhauser effect for ferric forms of horse and tuna cytochrome c",published,journal,Biophys. J.,,52,,,,,,,,,,,,,,,,,,,,,,,101,107,1987, citations,entry_citation,5000,211708,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N Resonance Assignments of the Catalytic Domain of the MAPK Phosphatase, PAC-1",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,25,1,,,,,,,,,,,,,,,,,,,,,,79,80,2003, citations,citations_1,50000,211730,1,,entry citation,,,32075969,,,A molecular switch regulating transcriptional repression and activation of PPARgamma,published,journal,Nat. Commun.,Nature communications,11,1,,2041-1723,,,,,,,,,,,,,,,,,,,,956,956,2020, citations,citations_1,50001,211748,1,,entry citation,,,32611811,,,Intercepting second-messenger signaling by rationally designed peptides sequestering c-di-GMP,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,117,29,,1091-6490,,,,,,,,,,,,,,,,,,,,17211,17220,2020, citations,citations_1,50003,211778,1,,entry citation,,,32421702,,,NMR Resonance Assignment and Structure Prediction of the C-terminal Domain of the Microtubule End-Binding Protein 3,published,journal,PLOS ONE,,15,5,,1932-6203,,,,,,,,,,,,,,,,,,,,e0232338,e0232338,2020, citations,citations_1,50004,211792,1,,entry citation,,,32081588,,,The Pierced Lasso Topology Leptin has a Bolt on Dynamic Domain Composed by the Disordered Loops I and III,published,journal,J. Mol. Biol.,Journal of molecular biology,432,9,,1089-8638,,,,,,,,,,,,,,,,,,,,3050,3063,2020, citations,citations_1,50007,211805,1,,entry citation,,,32077246,,,Pro-Islet Amyloid Polypeptide in Micelles Contains a Helical Prohormone Segment,published,journal,FEBS J.,,287,20,,,,,,,,,,,,,,,,,,,,,,4440,4457,2020, citations,citations_1,50031,212109,1,,entry citation,,,31738549,,,Combining free energy simulations and NMR chemical-shift perturbation to identify transient cation-pi contacts in proteins,published,journal,J. Chem. Inf. Model.,Journal of chemical information and modeling,60,2,,1549-960X,,,,,,,,,,,,,,,,,,,,890,897,2020, citations,citations_1,50032,212122,1,,entry citation,,,31738549,,,Combining free energy simulations and NMR chemical-shift perturbation to identify transient cation-pi contacts in proteins,published,journal,J. Chem. Inf. Model.,Journal of chemical information and modeling,60,2,,1549-960X,,,,,,,,,,,,,,,,,,,,890,897,2020, citations,citations_1,50033,212135,1,,entry citation,,,31738549,,,Combining free energy simulations and NMR chemical-shift perturbation to identify transient cation-pi contacts in proteins,published,journal,J. Chem. Inf. Model.,Journal of chemical information and modeling,60,2,,1549-960X,,,,,,,,,,,,,,,,,,,,890,897,2020, citations,entry_citation,5004,212148,1,,entry citation,,21313626,11419948,,,Solution Structure of Human IL-13 and Implication for Receptor Binding,published,journal,J. Mol. Biol.,,310,1,,,,,,,,,,,,,,,,,,,,,,219,230,2001, citations,entry_citation,5005,212162,1,,entry citation,,21882793,11885986,,,"Letter to the Editor: Backbone Sequential Resonance Assignments of Yeast iso-2 Cytochrome c, Reduced and Oxidized forms",published,journal,J. Biomol. NMR,,22,1,,,,,,,,,,,,,,,,,,,,,,93,94,2002, citations,ref_NMRPipe,5005,212163,2,,reference citation,,96088118,,,,NMRPipe: a multidimensional spectral processing system based on UNIX pipes,,journal,J. Biomol. NMR,,6,3,,,,,,,,,,,,,,,,,,,,,,277,293,1995, citations,entry_citation,5006,212185,1,,entry citation,,21673332,11814338,,,"NMR Structure of Alpha-bungarotoxin free and bound to a Mimotope of the Nicotinic Acetylcholine Receptor",published,journal,Biochemistry,,41,5,,,,,,,,,,,,,,,,,,,,,,1457,1463,2002, citations,entry_citation,5007,212200,1,,entry citation,,,11350168,,,"A pH Controlled Conformational Switch In the Cleavage Site of the VS Ribozyme Substrate RNA",published,journal,J. Mol. Biol.,Journal of Molecular Biology,308,4,,,,,,,,,,,,,,,,,,,,,,665,679,2001, citations,citations_1,50074,212226,1,,entry citation,,,31975054,,,"1H, 13C, and 15N resonance assignment and secondary structure of the pheromone-binding protein2 from the agricultural pest Ostrinia furnacalis (OfurPBP2)",published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,14,1,,1874-270X,,,,,,,,,,,,,,,,,,,,115,118,2020, citations,citations_1,50075,212239,1,,entry citation,,,,,,Membrane-bound human PD-L1 cytoplasmic domain,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50077,212259,1,,entry citation,,,31900740,,,"1H, 13C and 15N backbone resonance assignment of the human BRCA2 N-terminal region",published,journal,Biomol. NMR Assignments,,14,1,,,,,,,,,,,,,,,,,,,,,,79,85,2020, citations,citations_1,50078,212272,1,,entry citation,,,31900740,,,"1H, 13C and 15N backbone resonance assignment of the human BRCA2 N-terminal region",published,journal,Biomol. NMR Assignments,,14,1,,,,,,,,,,,,,,,,,,,,,,79,85,2020, citations,citations_1,50079,212285,1,,entry citation,,,31900740,,,"1H, 13C and 15N backbone resonance assignment of the human BRCA2 N-terminal region",published,journal,Biomol. NMR Assignments,,14,1,,,,,,,,,,,,,,,,,,,,,,79,85,2020, citations,entry_citation,5008,212298,1,,entry citation,,,,,,"Letter to the Editor: Assignment of the 1H, 13C and 15N resonances and secondary structure of the monomeric p13suc1 protein of Saccharomyces pombe",published,journal,J. Biomol. NMR,,23,2,,,,,,,,,,,,,,,,,,,,,,155,156,2002, citations,citations_1,50084,212318,1,,entry citation,,,32639967,,,An Angelman Syndrome Substitution in the HECT E3 Ubiquitin Ligase C-terminal Lobe of E6AP Affects Protein Stability and Activity,published,journal,PLoS ONE,PloS one,15,7,,1932-6203,,,,,,,,,,,,,,,,,,,,e0235925,e0235925,2020, citations,citations_1,50085,212331,1,,entry citation,,,31925324,,,Collective exchange processes reveal an active site proton cage in bacteriorhodopsin,published,journal,Commun. Biol.,,3,1,,2399-3642,,,,,,,,,,,,,,,,,,,,4,4,2020, citations,citations_1,50088,212344,1,,entry citation,,,32220302,,,Structure and Function of the Bacterial Protein Toxin Phenomycin,published,journal,Structure,"Structure (London, England : 1993)",28,5,,1878-4186,,,,,,,,,,,,,,,,,,,,528,539,2020, citations,entry_citation,5009,212360,1,,entry citation,,,,,,"Letter to the Editor: Assignment of the 1H, 13C and 15N resonances and secondary structure of the monomeric p13suc1 protein of Saccharomyces pombe",published,journal,J. Biomol. NMR,,23,2,,,,,,,,,,,,,,,,,,,,,,155,156,2002, citations,citations_1,50090,212384,1,,entry citation,,,32132204,,,TDP-43 alpha-helical structure tunes liquid-liquid phase separation and function,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,117,11,,1091-6490,,,,,,,,,,,,,,,,,,,,5883,5894,2020, citations,citations_1,50093,212399,1,,entry citation,,,31785178,,,On the mechanism of calcium-dependent activation of NADPH oxidase 5 (NOX5),published,journal,FEBS J.,,287,12,,,,,,,,,,,,,,,,,,,,,,2486,2503,2020, citations,citations_1,50095,212417,1,,entry citation,,,32239363,,,"1H, 15N chemical shift assignments of the imino groups of yeast tRNA Phe: influence of the post-transcriptional modifications",published,journal,Biomol. NMR Assignments,,14,2,,,,,,,,,,,,,,,,,,,,,,169,174,2020, citations,citations_1,50096,212433,1,,entry citation,,,32239363,,,"1H, 15N chemical shift assignments of the imino groups of yeast tRNA Phe: influence of the post-transcriptional modifications",published,journal,Biomol. NMR Assignments,,14,2,,,,,,,,,,,,,,,,,,,,,,169,174,2020, citations,citations_1,50097,212449,1,,entry citation,,,32239363,,,"1H, 15N chemical shift assignments of the imino groups of yeast tRNA Phe: influence of the post-transcriptional modifications",published,journal,Biomol. NMR Assignments,,14,2,,,,,,,,,,,,,,,,,,,,,,169,174,2020, citations,citations_1,50098,212464,1,,entry citation,,,32348724,,,Structural Description of the Nipah Virus Phosphoprotein and Its Interaction With STAT1,published,journal,Biophys. J.,Biophysical journal,118,10,,1542-0086,,,,,,,,,,,,,,,,,,,,2470,2488,2020, citations,citations_1,50099,212477,1,,entry citation,,,32348724,,,Structural Description of the Nipah Virus Phosphoprotein and Its Interaction With STAT1,published,journal,Biophys. J.,Biophysical journal,118,10,,1542-0086,,,,,,,,,,,,,,,,,,,,2470,2488,2020, citations,entry_citation,5010,212490,1,,entry citation,,21584503,,,,"Letter to the Editor: 1H, 15N, and 13C Resonance Assignments for a 20 kDa DNA Polymerase from African Swine Fever Virus",published,journal,J. Biomol. NMR,Journal of Biomolecular NMR,21,2,,,,,,,,,,,,,,,,,,,,,,177,178,2001, citations,ref_NMRPipe,5010,212491,2,,reference citation,,96088118,,,,NMRPipe: a multidimensional spectral processing system based on UNIX pipes,,journal,J. Biomol. NMR,,6,3,,,,,,,,,,,,,,,,,,,,,,277,293,1995, citations,ref_XEASY,5010,212492,3,,reference citation,,,,,,"The program XEASY for computer-supported NMR spectral analysis of biological macromolecules.",,journal,J. Biomol. NMR,,6,,,,,,,,,,,,,,,,,,,,,,,1,10,1995, citations,citations_1,50127,212898,1,,entry citation,,,32157574,,,pH-dependent Secondary Structure Propensity of the Influenza A Virus M2 Cytoplasmic Tail,published,journal,Biomol. NMR Assignments,,14,1,,1874-270X,,,,,,,,,,,,,,,,,,,,157,161,2020, citations,citations_1,50128,212912,1,,entry citation,,,,,,Dietary flavonoid fisetin binds human SUMO1 and blocks sumoylation of p53,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,Reference_3,5010,212493,4,,reference citation,,,11831707,,"Yanez, R.J., Rodriguez, J.M., Nogal, M.L., Yuste, L., Enriquez, C., Rodriguez, J.F., and Vinuela, E. (1995) Virology 208, 249-278",Analysis of the complete nucleotide sequence of African swine fever virus.,published,journal,Virology,Virology,208,1,,0042-6822,,,,,,,,,,,,,,,,,,,,249,278,1995,"We present an analysis of the complete genome of African swine fever virus (ASFV) strain BA71V, including 80 kbp of novel sequence and 90 kbp previously reported by several authors. The viral DNA is 170,101 nucleotides long and contains 151 open reading frames. Structural and/or functional information is available on 113 viral proteins. ASFV encodes five multigene families, putative membrane and secreted proteins, and enzymes involved in nucleotide and nucleic acid metabolism (including DNA repair) and protein modification. Database comparisons have provided clues about genes that may modulate the virus-host interaction, thus, possibly controlling ASFV virulence and persistence. The virus possesses genes similar to CD2, IkappaB, C-type lectins, MyD116/gadd34/gamma, 34.5, bcl-2/bax, iap, NifS, and ERV1, which may allow a viral regulation of cell adhesion, apoptosis, and redox metabolism, as well as of the host immune response against ASFV infection. The proteins encoded by different ASFV isolates are highly similar, the most variable ones being those belonging to multigene families, some membrane proteins, and those containing tandem repeats. DNA sequence data confirm the intermediate characteristics of ASFV between poxviruses and iridoviruses, supporting the notion that ASFV belongs to an independent virus family." citations,citations_1,50100,212528,1,,entry citation,,,32348724,,,Structural Description of the Nipah Virus Phosphoprotein and Its Interaction With STAT1,published,journal,Biophys. J.,Biophysical journal,118,10,,1542-0086,,,,,,,,,,,,,,,,,,,,2470,2488,2020, citations,citations_1,50101,212541,1,,entry citation,,,32348724,,,Structural Description of the Nipah Virus Phosphoprotein and Its Interaction With STAT1,published,journal,Biophys. J.,Biophysical journal,118,10,,1542-0086,,,,,,,,,,,,,,,,,,,,2470,2488,2020, citations,citations_1,50102,212554,1,,entry citation,,,32348724,,,Structural Description of the Nipah Virus Phosphoprotein and Its Interaction With STAT1,published,journal,Biophys. 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Biol.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5022,213968,1,,entry citation,,21376075,11483531,,,"Converting a DNA Damage Checkpoint Effector (UmuD2C) into a Lesion Bypass Polymerase (UmuD'2C)",published,journal,EMBO J.,,20,15,,,,,,,,,,,,,,,,,,,,,,4287,4298,2001, citations,citations_1,50220,213991,1,,entry citation,,,32999060,,,Fusidic acid resistance through changes in the dynamics of the drug target,published,journal,Proc. Natl. Acad. Sci. U. S. A.,,,,,,,,,,,,,,,,,,,,,,,,,,,2020, citations,citations_1,50221,214009,1,,entry citation,,,32999060,,,Fusidic acid resistance through changes in the dynamics of the drug target,published,journal,Proc. Natl. Acad. Sci. U. S. A.,,,,,,,,,,,,,,,,,,,,,,,,,,,,Manuscript to be submitted shortly. Full details of the citation to follow after acceptance citations,citations_1,50228,214024,1,,entry citation,,,32696260,,,"1 H, 13 C and 15 N resonance assignments for the microtubule-binding domain of the kinetoplastid kinetochore protein KKT4 from Trypanosoma brucei",published,journal,Biomol. NMR Assignments,,,,,,,,,,,,,,,,,,,,,,,,,,,2020, citations,citations_1,50229,214042,1,,entry citation,,,32696260,,,"1 H, 13 C and 15 N resonance assignments for the microtubule-binding domain of the kinetoplastid kinetochore protein KKT4 from Trypanosoma brucei",published,journal,Biomol. NMR Assignments,,,,,,,,,,,,,,,,,,,,,,,,,,,2020, citations,entry_citation,5023,214059,1,,entry citation,,,11273704,,,"Structural and thermodynamic studies on mutant RNA motifs that impair the specificity between a viral replicase and its promoter",published,journal,J. Mol. Biol.,,307,,,,,,,,,,,,,,,,,,,,,,,827,839,2001, citations,citations_1,50231,214076,1,,entry citation,,,32583165,,,"1H, 13C and 15N backbone resonance assignment of BRCA1 fragment 219-504",published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,14,2,,1874-270X,,,,,,,,,,,,,,,,,,,,289,293,2020, citations,citations_1,50238,214090,1,entry citation,entry citation,,,32338601,,,Multi-state recognition pathway of the intrinsically disordered protein kinase inhibitor by protein kinase A,published,journal,eLIFE,,9,,,,,,,,,,,,,,,,,,,,,,,e55607,e55607,2020, citations,entry_citation,5024,214116,1,,entry citation,,,11312275,,,"The Solution Structure of the Complex Formed between alpha-Bungarotoxin and an 18mer Cognate Peptide Derived from the alpha1 Subunit of the Nicotinic Acetylcholine Receptor from Torpedo californica",published,journal,J. Biol. Chem.,,276,25,,,,,,,,,,,,,,,,,,,,,,22930,22940,2001, citations,citations_1,50241,214133,1,,entry citation,,,32699145,,,Calcium and hydroxyapatite binding site of human vitronectin provides new insights to abnormal deposit formation,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,117,31,,1091-6490,,,,,,,,,,,,,,,,,,,,18504,18510,2020, citations,citations_1,50242,214150,1,,entry citation,,,,,,"The origin of the high stability of 3'-terminal uridine tetrads. The contributions of hydrogen bonding, stacking interactions and steric factors evaluated using modified oligonucleotide analogs.",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50243,214165,1,entry citation,entry citation,,,32338601,,,Multi-state recognition pathway of the intrinsically disordered protein kinase inhibitor by protein kinase A,published,journal,eLIFE,,9,,,,,,,,,,,,,,,,,,,,,,,e55607,e55607,2020, citations,citations_1,50244,214193,1,,entry citation,,,,,,"The origin of the high stability of 3'-terminal uridine tetrads. The contributions of hydrogen bonding, stacking interactions and steric factors evaluated using modified oligonucleotide analogs.",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50245,214207,1,,entry citation,,,,,,"The origin of the high stability of 3'-terminal uridine tetrads. The contributions of hydrogen bonding, stacking interactions and steric factors evaluated using modified oligonucleotide analogs.",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50246,214221,1,,entry citation,,,,,,"The origin of the high stability of 3'-terminal uridine tetrads. The contributions of hydrogen bonding, stacking interactions and steric factors evaluated using modified oligonucleotide analogs.",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50247,214236,1,,entry citation,,,,,,"The origin of the high stability of 3'-terminal uridine tetrads. The contributions of hydrogen bonding, stacking interactions and steric factors evaluated using modified oligonucleotide analogs.",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50248,214251,1,,entry citation,,,,,,"The origin of the high stability of 3'-terminal uridine tetrads. The contributions of hydrogen bonding, stacking interactions and steric factors evaluated using modified oligonucleotide analogs.",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50249,214265,1,,entry citation,,,,,,"The origin of the high stability of 3'-terminal uridine tetrads. The contributions of hydrogen bonding, stacking interactions and steric factors evaluated using modified oligonucleotide analogs.",in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5025,214279,1,,entry citation,,,11312275,,,"The Solution Structure of the Complex Formed between alpha-Bungarotoxin and an 18mer Cognate Peptide Derived from the alpha1 Subunit of the Nicotinic Acetylcholine Receptor from Torpedo californica",published,journal,J. Biol. Chem.,,276,25,,,,,,,,,,,,,,,,,,,,,,22930,22940,2001, citations,citations_1,50250,214305,1,,entry citation,,,32519295,,,"1H, 13C, and 15N backbone chemical shift assignments of m7GTP cap-bound Leishmania initiation factor 4E-1",published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,14,2,,1874-270X,,,,,,,,,,,,,,,,,,,,259,263,2020, citations,citations_1,50253,214335,1,,entry citation,,,32561718,,,Non-cooperative 4E-BP2 folding with exchange between eIF4E-binding and binding-incompatible states tunes cap-dependent translation inhibition,published,journal,Nat. Commun.,Nature Communications,11,1,,2041-1723,,,,,,,,,,,,,,,,,,,,3146,3146,2020, citations,citations_1,50254,214353,1,,entry citation,,,32870271,,,Weak binding to the A2RE RNA rigidifies hnRNPA2 RRMs and reduces liquid-liquid phase separation and aggregation,published,journal,Nucleic Acids Res,Nucleic acids research,48,18,,1362-4962,,,,,,,,,,,,,,,,,,,,10542,10554,2020, citations,citations_1,50255,214367,1,,entry citation,,,32870271,,,Weak binding to the A2RE RNA rigidifies hnRNPA2 RRMs and reduces liquid-liquid phase separation and aggregation,published,journal,Nucleic Acids Res,Nucleic acids research,48,18,,1362-4962,,,,,,,,,,,,,,,,,,,,10542,10554,2020, citations,citations_1,50257,214381,1,,entry citation,,,32870271,,,Weak binding to the A2RE RNA rigidifies hnRNPA2 RRMs and reduces liquid-liquid phase separation and aggregation,published,journal,Nucleic Acids Res,Nucleic acids research,48,18,,1362-4962,,,,,,,,,,,,,,,,,,,,10542,10554,2020, citations,entry_citation,5026,214396,1,,entry citation,,21938260,11941512,,,"Solution Structure of Cyanoferricytochrome C: Ligand-controlled Conformational Flexibility and Electronic Structure of the Heme Moiety",published,journal,J. Biol. Inorg. Chem.,,7,4-5,,,,,,,,,,,,,,,,,,,,,,539,547,2002, citations,citations_1,50260,214418,1,,entry citation,,,32707235,,,"In-depth NMR characterization of Rab4a structure, nucleotide exchange and hydrolysis kinetics reveals an atypical GTPase profile",published,journal,J. Struct. Biol.,Journal of structural biology,212,1,,1095-8657,,,,,,,,,,,,,,,,,,,,107582,107582,2020, citations,citations_1,50261,214436,1,,entry citation,,,32699145,,,Calcium and hydroxyapatite binding site of human vitronectin provides new insights to abnormal deposit formation,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,117,31,,1091-6490,,,,,,,,,,,,,,,,,,,,18504,18510,2020, citations,citations_1,50262,214451,1,,entry citation,,,32855413,,,Feline coronavirus drug inhibits the main protease of SARS-CoV-2 and blocks virus replication,published,journal,Nat. Commun.,Nature communications,11,1,,2041-1723,,,,,,,,,,,,,,,,,,,,4282,4282,2020, citations,citations_1,50263,214467,1,,entry citation,,,32830336,10.15252/embj.2019104247,,gamma-Secretase cleavage of the Alzheimer risk factor TREM2 is determined by its intrinsic structural dynamics,published,journal,EMBO J.,,39,,,,,,,,,,,,,,,,,,,,,,,e104247,e104247,2020, citations,citations_1,50264,214481,1,,entry citation,,,32830336,10.15252/embj.2019104247,,gamma-Secretase cleavage of the Alzheimer risk factor TREM2 is determined by its intrinsic structural dynamics,published,journal,EMBO J.,,39,,,,,,,,,,,,,,,,,,,,,,,e104247,e104247,2020, citations,citations_1,50265,214495,1,,entry citation,,,32830336,10.15252/embj.2019104247,,gamma-Secretase cleavage of the Alzheimer risk factor TREM2 is determined by its intrinsic structural dynamics,published,journal,EMBO J.,,39,,,,,,,,,,,,,,,,,,,,,,,e104247,e104247,2020, citations,citations_1,50267,214510,1,,entry citation,,,32707235,,,"In-depth NMR characterization of Rab4a structure, nucleotide exchange and hydrolysis kinetics revealed an atypical GTPase profile.",published,journal,J. Struct. Biol.,Journal of structural biology,212,1,,1095-8657,,,,,,,,,,,,,,,,,,,,107582,107582,2020, citations,citations_1,50268,214529,1,,entry citation,,,32963221,,,IRES-targeting small molecule inhibits enterovirus 71 replication via allosteric stabilization of a ternary complex,published,journal,Nat. Commun.,Nature communications,11,1,,2041-1723,,,,,,,,,,,,,,,,,,,,4775,4775,2020, citations,entry_citation,5027,214553,1,,entry citation,,21631520,11775745,,,NMR Structure of Human Fibronectin EDA,published,journal,J. Biomol. NMR,,21,3,,,,,,,,,,,,,,,,,,,,,,281,284,2001, citations,citations_1,50273,214584,1,,entry citation,,,32601205,,,Maturation of the functional mouse CRES amyloid from globular form,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,117,28,,1091-6490,,,,,,,,,,,,,,,,,,,,16363,16372,2020, citations,citations_1,50274,214601,1,,entry citation,,,,,,pH Changes Trigger Structural Transitions in Drosophila Orb2A PLD Relevant for Functional Aggregation in Memory Consolidation,in preparation,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50275,214619,1,,entry citation,,,32601205,,,Maturation of the functional mouse CRES amyloid from globular form,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,117,28,,1091-6490,,,,,,,,,,,,,,,,,,,,16363,16372,2020, citations,citations_1,50276,214634,1,,entry citation,,,32888404,,,Conformational States of the Cytoprotective Protein Bcl-xL,published,journal,Biophys. J.,,,,,1542-0086,,,,,,,,,,,,,,,,,,,,,,2020, citations,citations_1,50277,214648,1,,entry citation,,,32535836,,,Backbone resonance assignments of the catalytic and regulatory domains of Ca 2+/calmodulin-dependent protein kinase 1D,published,journal,Biomol. NMR Assignments,,,,,,,,,,,,,,,,,,,,,,,,,,,2020, citations,citations_1,50278,214664,1,,entry citation,,,,,,Impact of 5-Formylcytosine on the Melting Kineticsof DNA by 1H NMR Chemical Exchange,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5028,214683,1,,entry citation,,,,,,"Circular Proteins in Plants: Solution Structure of a Novel Macrocyclic Trypsin Inhibitor from Momordica cochinchinensis",in press,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,2001, citations,reference_1,5028,214684,2,,reference citation,,,10801322,,"Hernandez JF, Gagnon J, Chiche L, Nguyen TM, Andrieu JP, Heitz A, Trinh Hong T, Pham TT, Le Nguyen D. Squash trypsin inhibitors from Momordica cochinchinensis exhibit an atypical macrocyclic structure. Biochemistry. 2000 May 16;39(19):5722-30.",Squash trypsin inhibitors from Momordica cochinchinensis exhibit an atypical macrocyclic structure.,published,journal,Biochemistry,Biochemistry,39,19,,0006-2960,,,,,,,,,,,,,,,,,,,,5722,5730,2000,"Three trypsin inhibitors (TIs), from the seeds of the squash Momordica cochinchinensis (MCo), have been isolated and purified using gel filtration, ion exchange chromatography, and reverse-phase HPLC. Their sequences could be determined only after proteolytic cleavages. In the case of MCoTI-I and -II, it was shown that their polypeptide backbones are cyclic, a structure that has never been described in squash TIs. They contain 34 amino acid residues with 3 disulfide bridges and measured molecular masses of 3453.0 and 3480.7, respectively. They are the largest known macrocyclic peptides containing disulfide bridges. Their sequences show strong homology to other squash TIs, suggesting a similar three-dimensional structure and an analogous mechanism of action. A model of MCoTI-II was constructed by analogy to the crystal structure of the complex between bovine trypsin and CMTI-I, indicating that the linker connecting the two termini is flexible and does not impose significant geometrical constraints. This flexibility allows an Asp-Gly peptide bond rearrangement to occur in this region, giving rise to two isoforms of MCoTI-II. Although the importance of cyclization is not clear, it might confer increased stability and resistance to proteolysis. A minor species, MCoTI-III, was also characterized as containing 30 amino acid residues with a molecular mass of 3379.6. This component possesses a linear backbone with a blocked N-terminus. MCoTIs represent interesting candidates for drug design, either by changing their specificity of inhibition or by using their structure as natural scaffolds bearing new binding activities." citations,entry_citation,5029,214701,1,,entry citation,,21338260,11444973,,,"Solution Structure of an Insect-specific Neurotoxin from the New World Scorpion Centruroides sculpturatus Ewing(,)",published,journal,Biochemistry,,40,28,,,,,,,,,,,,,,,,,,,,,,8273,8282,2001, citations,citations_1,50297,214715,1,,entry citation,,,32538627,,,Different solvent and conformational entropy contributions to the allosteric activation and inhibition mechanisms of yeast chorismate mutase,published,journal,Biochemistry,Biochemistry,59,27,,1520-4995,,,,,,,,,,,,,,,,,,,,2528,2540,2020, citations,citations_1,50298,214733,1,,entry citation,,,,,,"Double phosphorylation of BAF by VRK1 strongly impacts its conformational dynamics,but does not affect emerin and lamin A/C binding",in preparation,journal,J. Mol. Biol.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50299,214749,1,,entry citation,,,,,,Identification of Phenothiazine Derivatives as UHM-Binding Inhibitors of Early Spliceosome Assembly,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5030,214766,1,,entry citation,,21584505,11727984,,,"Letter to the Editor: 1H, 13C and 15N Chemical Shift Assignment of the Honeybee Odorant-binding Protein ASP2",published,journal,J. Biomol. NMR,,21,2,,,,,,,,,,,,,,,,,,,,,,181,182,2001, citations,ref_1,5030,214767,2,,reference citation,,,11168415,,"Briand L, Nespoulous C, Huet JC, Takahashi M, Pernollet JC. Ligand binding and physico-chemical properties of ASP2, a recombinant odorant-binding protein from honeybee (Apis mellifera L.). Eur J Biochem. 2001 Feb;268(3):752-60.","Ligand binding and physico-chemical properties of ASP2, a recombinant odorant-binding protein from honeybee (Apis mellifera L.).",published,journal,Eur. J. Biochem.,European journal of biochemistry / FEBS,268,3,,0014-2956,,,,,,,,,,,,,,,,,,,,752,760,2001,"In insects, the transport of airborne, hydrophobic odorants and pheromones through the sensillum lymph is generally thought to be accomplished by odorant-binding proteins (OBPs). We report the structural and functional properties of a honeybee OBP called ASP2, heterologously expressed by the yeast Pichia pastoris. ASP2 disulfide bonds were assigned after classic trypsinolysis followed by ion-spray mass spectrometry combined with microsequencing. The pairing [Cys(I)-Cys(III), Cys(II)-Cys(V), Cys(IV)-Cys(VI)] was found to be identical to that of Bombyx mori OBP, suggesting that this pattern occurs commonly throughout the highly divergent insect OBPs. CD measurements revealed that ASP2 is mainly constituted of alpha helices, like other insect OBPs, but different from lipocalin-like vertebrate OBPs. Gel filtration analysis showed that ASP2 is homodimeric at neutral pH, but monomerizes upon acidification or addition of a chaotropic agent. A general volatile-odorant binding assay allowed us to examine the uptake of some odorants and pheromones by ASP2. Recombinant ASP2 bound all tested molecules, except beta-ionone, which could not interact with it at all. The affinity constants of ASP2 for these ligands, determined at neutral pH by isothermal titration calorimetry, are in the micromolar range, as observed for vertebrate OBP. These results suggest that odorants occupy three binding sites per dimer, probably one in the core of each monomer and another whose location and biological role are questionable. At acidic pH, no binding was observed, in correlation with monomerization and a local conformational change supported by CD experiments." citations,entry_citation,5033,215039,1,,entry citation,,21464431,11580275,,,"Solution Structures of the Antifungal Heliomicin and a Selected Variant with both Antibacterial and Antifungal Activities",published,journal,Biochemistry,,40,40,,,,,,,,,,,,,,,,,,,,,,11995,12003,2001, citations,ref_2,5030,214768,3,,reference citation,,,10092496,,"Briand L, Perez V, Huet JC, Danty E, Masson C, Pernollet JC. Optimization of the production of a honeybee odorant-binding protein by Pichia pastoris. Protein Expr Purif. 1999 Apr;15(3):362-9.",Optimization of the production of a honeybee odorant-binding protein by Pichia pastoris.,published,journal,Protein Expr. Purif.,Protein expression and purification,15,3,,1046-5928,,,,,,,,,,,,,,,,,,,,362,369,1999,"A honeybee putative general odorant-binding protein ASP2 has been expressed in the methylotrophic yeast Pichia pastoris. It was secreted into the buffered minimal medium using either the alpha-factor preprosequence with and without the Glu-Ala-Glu-Ala spacer peptide of Saccharomyces cerevisiae or its native signal peptide. Whereas ASP2 secreted using the alpha-factor preprosequence with the spacer peptide showed N-terminal heterogeneity, the recombinant protein using the two other secretion peptides was correctly processed. Mass spectrometry showed that the protein secreted using the natural peptide sequence had a mass of 13,695.1 Da, in perfect agreement with the measured molecular mass of the native protein. These data showed a native-like processing and the three disulfide bridges formation confirmed by sulfhydryl titration analysis. After dialysis, the recombinant protein was purified by one-step anion-exchange chromatography in a highly pure form. The final expression yield after 7-day fermentation was approximately 150 mg/liter. To our knowledge, this is the first report of the use of a natural insect leader sequence for secretion with correct processing in P. pastoris. The overproduction of recombinant ASP2 should allow ligand binding and mutational analysis to understand the relationships between structure and biological function of the protein." citations,ref_3,5030,214769,4,,reference citation,,,10460253,,"Danty E, Briand L, Michard-Vanhee C, Perez V, Arnold G, Gaudemer O, Huet D, Huet JC, Ouali C, Masson C, Pernollet JC. Cloning and expression of a queen pheromone-binding protein in the honeybee: an olfactory-specific, developmentally regulated protein. J Neurosci. 1999 Sep 1;19(17):7468-75.","Cloning and expression of a queen pheromone-binding protein in the honeybee: an olfactory-specific, developmentally regulated protein.",published,journal,J. Neurosci.,The Journal of neuroscience : the official journal of the Society for Neuroscience,19,17,,1529-2401,,,,,,,,,,,,,,,,,,,,7468,7475,1999,"Odorant-binding proteins (OBPs) are small abundant extracellular proteins thought to participate in perireceptor events of odor-pheromone detection by carrying, deactivating, and/or selecting odor stimuli. The honeybee queen pheromone is known to play a crucial role in colony organization, in addition to drone sex attraction. We identified, for the first time in a social insect, a binding protein called antennal-specific protein 1 (ASP1), which binds at least one of the major queen pheromone components. ASP1 was characterized by cDNA cloning, expression in Pichia pastoris, and pheromone binding. In situ hybridization showed that it is specifically expressed in the auxiliary cell layer of the antennal olfactory sensilla. The ASP1 sequence revealed it as a divergent member of the insect OBP family. The recombinant protein presented the exact characteristics of the native protein, as shown by mass spectrometry, and N-terminal sequencing and exclusion-diffusion chromatography showed that recombinant ASP1 is dimeric. ASP1 interacts with queen pheromone major components, opposite to another putative honeybee OBP, called ASP2. ASP1 biosynthetic accumulation, followed by nondenaturing electrophoresis during development, starts at day 1 before emergence, in concomitance with the functional maturation of olfactory neurons. The isobar ASP1b isoform appears simultaneously to ASP1a in workers, but only at approximately 2 weeks after emergence in drones. Comparison of in vivo and heterologous expressions suggests that the difference between ASP1 isoforms might be because of dimerization, which might play a physiological role in relation with mate attraction." citations,citations_1,50300,214787,1,,entry citation,,,,,,Identification of compounds that bind the centriolar protein SAS-6 and inhibit its oligomerisation,accepted,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50301,214803,1,,entry citation,,,32737158,,,Energetics and kinetics of substrate analog-coupled staphylococcal nuclease folding revealed by a statistical mechanical approach,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,117,33,,1091-6490,,,,,,,,,,,,,,,,,,,,19953,19962,2020, citations,citations_1,50302,214816,1,,entry citation,,,,,,The role of the IT-state in D76N b2-microglobulin aggregation,in preparation,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50308,214832,1,,entry citation,,,,,,Identification of compounds that bind the centriolar protein SAS-6 and inhibit its oligomerisation,accepted,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50309,214848,1,,entry citation,,,,,,Backbone chemical shift assignments of the Methylcrotonyl-CoA carboxylase's Biotin carboxyl carrier protein domain of Leishmania major,in preparation,journal,Biomol. NMR Assignments,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5031,214861,1,,entry citation,,,,,,"Letter to the Editor: Sequence-specific 1H, 13C and 15N resonance assignments of the N-terminal, 135-residue domain of KaiA, a clock protein from Synechococcus elongatus",published,journal,J. Biomol. NMR,,21,2,,,,,,,,,,,,,,,,,,,,,,179,180,2001, citations,citations_1,50315,214885,1,,entry citation,,,32647013,,,Structure-activity analysis of truncated albumin-binding domains suggests new lead constructs for potential therapeutic delivery,published,journal,J. Biol. Chem.,The Journal of biological chemistry,295,34,,1083-351X,,,,,,,,,,,,,,,,,,,,12143,12152,2020, citations,citations_1,50316,214898,1,,entry citation,,,32647013,,,Structure-activity analysis of truncated albumin-binding domains suggests new lead constructs for potential therapeutic delivery,published,journal,J. Biol. Chem.,The Journal of biological chemistry,295,34,,1083-351X,,,,,,,,,,,,,,,,,,,,12143,12152,2020, citations,citations_1,50317,214911,1,,entry citation,,,32647013,,,Structure-activity analysis of truncated albumin-binding domains suggests new lead constructs for potential therapeutic delivery,published,journal,J. Biol. Chem.,The Journal of biological chemistry,295,34,,1083-351X,,,,,,,,,,,,,,,,,,,,12143,12152,2020, citations,citations_1,50318,214924,1,,entry citation,,,32647013,,,Structure-activity analysis of truncated albumin-binding domains suggests new lead constructs for potential therapeutic delivery,published,journal,J. Biol. Chem.,The Journal of biological chemistry,295,34,,1083-351X,,,,,,,,,,,,,,,,,,,,12143,12152,2020, citations,citations_1,50319,214937,1,,entry citation,,,32647013,,,Structure-activity analysis of truncated albumin-binding domains suggests new lead constructs for potential therapeutic delivery,published,journal,J. Biol. Chem.,The Journal of biological chemistry,295,34,,1083-351X,,,,,,,,,,,,,,,,,,,,12143,12152,2020, citations,entry_citation,5032,214950,1,,entry citation,,20377252,10921784,,,"Letter to the Editor: 1H, 13C and 15N Resonance Assignments of the DNA Binding Domain of the Human Forkhead Transcription Factor AFX",published,journal,J. Biomol. NMR,,17,2,,,,,,,,,,,,,,,,,,,,,,181,182,2000, citations,citations_1,50320,214971,1,,entry citation,,,32647013,,,Structure-activity analysis of truncated albumin-binding domains suggests new lead constructs for potential therapeutic delivery,published,journal,J. Biol. Chem.,The Journal of biological chemistry,295,34,,1083-351X,,,,,,,,,,,,,,,,,,,,12143,12152,2020, citations,citations_1,50321,214984,1,,entry citation,,,32647013,,,Structure-activity analysis of truncated albumin-binding domains suggests new lead constructs for potential therapeutic delivery,published,journal,J. Biol. Chem.,The Journal of biological chemistry,295,34,,1083-351X,,,,,,,,,,,,,,,,,,,,12143,12152,2020, citations,citations_1,50322,214997,1,,entry citation,,,32647013,,,Structure-activity analysis of truncated albumin-binding domains suggests new lead constructs for potential therapeutic delivery,published,journal,J. Biol. Chem.,The Journal of biological chemistry,295,34,,1083-351X,,,,,,,,,,,,,,,,,,,,12143,12152,2020, citations,citations_1,50323,215010,1,,entry citation,,,32647013,,,Structure-activity analysis of truncated albumin-binding domains suggests new lead constructs for potential therapeutic delivery,published,journal,J. Biol. Chem.,The Journal of biological chemistry,295,34,,1083-351X,,,,,,,,,,,,,,,,,,,,12143,12152,2020, citations,citations_1,50329,215023,1,,entry citation,,,32722282,,,"Structural Analysis of the SANT/Myb Domain of FLASH and YARP Proteins and Their Complex with the C-Terminal Fragment of NPAT by NMR Spectroscopy and Computer Simulations",published,journal,Int. J. Mol. Sci.,International journal of molecular sciences,21,15,,1422-0067,,,,,,,,,,,,,,,,,,,,5268,5268,2020, citations,entry_citation,5051,216148,1,,entry citation,,21843898,11854485,,,An NMR Approach to Stuctural Proteomics,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,99,4,,,,,,,,,,,,,,,,,,,,,,1825,1830,2002, citations,citations_1,50332,215057,1,,entry citation,,,32795535,,,The pneumococcal iron uptake protein A (PiuA) specifically recognizes tetradentate FeIII bis- and mono-catechol complexes,published,journal,J. Mol. Biol.,,,,,,,,,,,,,,,,,,,,,,,,,,,2020, citations,citations_1,50333,215073,1,,entry citation,,,32795535,,,The pneumococcal iron uptake protein A (PiuA) specifically recognizes tetradentate FeIII bis- and mono-catechol complexes,published,journal,J. Mol. Biol.,,,,,,,,,,,,,,,,,,,,,,,,,,,2020, citations,citations_1,50334,215093,1,,entry citation,,,32770392,,,"1H, 13C, and 15N backbone chemical shift assignments of the nucleic acid-binding domain of SARS-CoV-2 non-structural protein 3e",published,journal,Biomol. NMR Assign.,Biomolecular NMR assignments,14,2,,1874-270X,,,,,,,,,,,,,,,,,,,,329,333,2020, citations,citations_1,50335,215111,1,,entry citation,,,32722282,,,"Structural Analysis of the SANT/Myb Domain of FLASH and YARP Proteins and Their Complex with the C-Terminal Fragment of NPAT by NMR Spectroscopy and Computer Simulations",published,journal,Int. J. Mol. Sci.,International journal of molecular sciences,21,15,,1422-0067,,,,,,,,,,,,,,,,,,,,5268,5268,2020, citations,citations_1,50336,215128,1,,entry citation,,,32722282,,,"Structural Analysis of the SANT/Myb Domain of FLASH and YARP Proteins and Their Complex with the C-Terminal Fragment of NPAT by NMR Spectroscopy and Computer Simulations",published,journal,Int. J. Mol. Sci.,International journal of molecular sciences,21,15,,1422-0067,,,,,,,,,,,,,,,,,,,,5268,5268,2020, citations,citations_1,50339,215144,1,citations 1,entry citation,,,,,,Secondary structure determination of conserved SARS-CoV-2 RNA elements by NMR spectroscopy and DMS footprinting analysis,in preparation,journal,Nucleic Acids Res.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5034,215160,1,,entry citation,,21930705,11932493,,,"Impact of single-residue mutations on the structure and function of ovispirin/novispirin antimicrobial peptides",submitted,journal,Protein Eng.,,15,3,,,,,,,,,,,,,,,,,,,,,,225,232,2002, citations,citations_1,50340,215178,1,citations 1,entry citation,,,,,,Secondary structure determination of conserved SARS-CoV-2 RNA elements by NMR spectroscopy and DMS footprinting analysis,in preparation,journal,Nucleic Acids Res.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50341,215195,1,citations 1,entry citation,,,,,,Secondary structure determination of conserved SARS-CoV-2 RNA elements by NMR spectroscopy and DMS footprinting analysis,in preparation,journal,Nucleic Acids Res.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50342,215210,1,citations 1,entry citation,,,,,,Secondary structure determination of conserved SARS-CoV-2 RNA elements by NMR spectroscopy and DMS footprinting analysis,in preparation,journal,Nucleic Acids Res.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50343,215231,1,citations 1,entry citation,,,,,,Secondary structure determination of conserved SARS-CoV-2 RNA elements by NMR spectroscopy and DMS footprinting analysis,in preparation,journal,Nucleic Acids Res.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50344,215251,1,citations 1,entry citation,,,,,,Secondary structure determination of conserved SARS-CoV-2 RNA elements by NMR spectroscopy and DMS footprinting analysis,in preparation,journal,Nucleic Acids Res.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50346,215266,1,citations 1,entry citation,,,,,,Secondary structure determination of conserved SARS-CoV-2 RNA elements by NMR spectroscopy and DMS footprinting analysis,in preparation,journal,Nucleic Acids Res.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50347,215281,1,citations 1,entry citation,,,,,,Secondary structure determination of conserved SARS-CoV-2 RNA elements by NMR spectroscopy and DMS footprinting analysis,in preparation,journal,Nucleic Acids Res.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50348,215299,1,citations 1,entry citation,,,,,,Secondary structure determination of conserved SARS-CoV-2 RNA elements by NMR spectroscopy and DMS footprinting analysis,in preparation,journal,Nucleic Acids Res.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50349,215318,1,citations 1,entry citation,,,,,,Secondary structure determination of conserved SARS-CoV-2 RNA elements by NMR spectroscopy and DMS footprinting analysis,in preparation,journal,Nucleic Acids Res.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50350,215339,1,citations 1,entry citation,,,,,,Secondary structure determination of conserved SARS-CoV-2 RNA elements by NMR spectroscopy and DMS footprinting analysis,in preparation,journal,Nucleic Acids Res.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50351,215354,1,citations 1,entry citation,,,,,,Secondary structure determination of conserved SARS-CoV-2 RNA elements by NMR spectroscopy and DMS footprinting analysis,in preparation,journal,Nucleic Acids Res.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50352,215373,1,citations 1,entry citation,,,,,,Secondary structure determination of conserved SARS-CoV-2 RNA elements by NMR spectroscopy and DMS footprinting analysis,in preparation,journal,Nucleic Acids Res.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50353,215389,1,,entry citation,,,32767002,,,"Nearly complete 1H, 13C and 15N chemical shift assignment of monomeric form of N-terminal domain of Nephila clavipes major ampullate spidroin 2",published,journal,Biomol. NMR Assignments,,,,,,,,,,,,,,,,,,,,,,,,,,,2020, citations,entry_citation,5036,215404,1,,entry citation,,,11266597,,,"Solution Structure and Backbone Dynamics of the DNA-Binding Domain of Mouse Sox-5",published,journal,Protein Sci.,,10,,,,,,,,,,,,,,,,,,,,,,,83,98,2001, citations,citations_1,50369,215427,1,,entry citation,,,32822537,,,Structural basis for GTP versus ATP selectivity in the NMP kinase AK3,published,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5037,215445,1,,entry citation,,21930705,11932493,,,"Impact of single-residue mutations on the structure and function of ovispirin/novispirin antimicrobial peptides",submitted,journal,Protein Eng.,,15,3,,,,,,,,,,,,,,,,,,,,,,225,232,2002, citations,citations_1,50371,215463,1,,reference citation,,,,,,Crystal structure and main chain dynamics of the N-terminal fragment of Lon protease of Mycobacterium tuberculosis complex,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_2,50371,215464,2,,entry citation,,,,,,Backbone assignments of the Lon protease from Mycobacterium tuberculosis complex,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5038,215477,1,,entry citation,,21882792,11885984,,,The NMR Structure of the Class I Human Ubiquitin-conjugating Enzyme 2b,published,journal,J. Biomol. NMR,,22,1,,,,,,,,,,,,,,,,,,,,,,89,92,2002, citations,entry_citation,5052,216176,1,,entry citation,,,,,,1H Assigned Chemical Shifts for Neurotoxin II,published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5053,216190,1,,entry citation,,22063288,,,,"Solution Structure of the Orphan PABC Domain from Saccharomyces cerevisiae Poly(A)-binding Protein",published,journal,J. Biol. Chem.,,277,25,,,,,,,,,,,,,,,,,,,,,,22822,22828,2002, citations,entry_citation,5054,216217,1,,entry citation,,21829591,11839306,,,"The Structure of Ap(4)A Hydrolase Complexed with ATP-MgF(x) Reveals the Basis of Substrate Binding",published,journal,Structure,,10,2,,,,,,,,,,,,,,,,,,,,,,205,213,2002, citations,entry_citation,5055,216251,1,,entry citation,,,11551193,,,"Solution Structure of HI0257, a Bacterial Ribosome Binding Protein",published,journal,Biochemistry,,40,,,,,,,,,,,,,,,,,,,,,,,10979,10986,2001, citations,ref_1,5038,215478,2,,reference citation,,,10388568,,"Miura T, Klaus W, Gsell B, Miyamoto C, Senn H. Characterization of the binding interface between ubiquitin and class I human ubiquitin-conjugating enzyme 2b by multidimensional heteronuclear NMR spectroscopy in solution. J Mol Biol. 1999 Jul 2;290(1):213-28.",Characterization of the binding interface between ubiquitin and class I human ubiquitin-conjugating enzyme 2b by multidimensional heteronuclear NMR spectroscopy in solution.,published,journal,J. Mol. Biol.,Journal of molecular biology,290,1,,0022-2836,,,,,,,,,,,,,,,,,,,,213,228,1999,"Ubiquitin-conjugating enzymes (Ubc) are involved in ubiquitination of proteins in the protein degradation pathway of eukaryotic cells. Ubc transfers the ubiquitin (Ub) molecules to target proteins by forming a thioester bond between their active site cysteine residue and the C-terminal glycine residue of ubiquitin. Here, we report on the NMR assignment and secondary structure of class I human ubiquitin-conjugating enzyme 2b (HsUbc2b). Chemical shift perturbation studies allowed us to map the contact area and binding interface between ubiquitin and HsUbc2b by1H-15N HSQC NMR spectroscopy. The serine mutant of the active site Cys88 of HsUbc2b was employed to obtain a relatively stable covalent ubiquitin complex of HsUbc2b(C88S). Changes in chemical shifts of amide protons and nitrogen atoms induced by the formation of the covalent complex were measured by preparing two segmentally labeled complexes with either ubiquitin or HsUbc2b(C88S)15N-labeled. In ubiquitin, the interaction is primarily sensed by the C-terminal segment Val70 - Gly76, and residues Lys48 and Gln49. The surface area on ubiquitin, as defined by these residues, overlaps partially with the presumed binding site with ubiquitin-activating enzyme (E1). In HsUbc2b, most of the affected residues cluster in the vicinity of the active site, namely, around the active site Cys88 itself, the second alpha-helix, and the flexible loop which connects helices alpha2 and alpha3 and which is adjacent to the active site. An additional site on HsUbc2b for a weak interaction with ubiquitin could be detected in a titration study where the two proteins were not covalently linked. This site is located on the backside of HsUbc2b opposite to the active site and is part of the beta-sheet. The covalent and non-covalent interaction sites are clearly separated on the HsUbc2b surface, while no such clear-cut segregation of the interaction area was observed on ubiquitin." citations,citations_1,50385,215492,1,,entry citation,,,,,,Protein side-chain-DNA contacts probed by fast Magic-Angle Spinning NMR,in preparation,journal,J. Biomol. NMR,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50386,215507,1,,entry citation,,,,,,Phosphorylation and single-point mutation effects on the conformational dynamics of EIN,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50387,215526,1,citations 1,entry citation,,,32803496,,,"1H, 13C, and 15N backbone chemical shift assignments of the apo and the ADP-ribose bound forms of the macrodomain of SARS-CoV-2 non-structural protein 3b",published,journal,Biomol. NMR Assignments,,,,,,,,,,,,,,,,,,,,,,,,,,,2020, citations,citations_1,50388,215541,1,citations 1,entry citation,,,32803496,,,"1H, 13C, and 15N backbone chemical shift assignments of the apo and the ADP-ribose bound forms of the macrodomain of SARS-CoV-2 non-structural protein 3b",published,journal,Biomol. NMR Assignments,,,,,,,,,,,,,,,,,,,,,,,,,,,2020, citations,citations_1,50389,215558,1,,entry citation,,,32935194,,,"1H, 13C, 15N backbone resonance assignment of the recognition lobe subdomain 3 (Rec3) from Streptococcus pyogenes CRISPR-Cas9",published,journal,Biomol. NMR Assignments,,,,,,,,,,,,,,,,,,,,,,,,,,,2020, citations,entry_citation,5039,215572,1,,entry citation,,21526409,,,,"Solution Structure of Ptu1, a Toxin from the Assassin bug Peirates turpis that blocks the Voltage-sensitive Calcium Channel N-type",published,journal,Biochemistry,,40,43,,,,,,,,,,,,,,,,,,,,,,12795,12800,2001, citations,citations_1,50392,215585,1,citations 1,entry citation,,,,,,Secondary structure determination of conserved SARS-CoV-2 RNA elements by NMR spectroscopy and DMS footprinting analysis,in preparation,journal,Nucleic Acids Res.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5040,215607,1,,entry citation,,21631522,11775747,,,"Letter to the Editor: Backbone 1H, 15N, and 13C Resonance Assignments of Inhibitor-1--a Protein Inhibitor of Protein Phosphatase-1",published,journal,J. Biomol. NMR,,21,3,,,,,,,,,,,,,,,,,,,,,,287,288,2001, citations,citations_1,50405,215628,1,entry citation,entry citation,,,10820004,10.1021/bi9926678,,Alternative splicing of Wilms' tumor suppressor protein modulates DNA binding activity through isoform-specific DNA-induced conformational changes.,published,journal,Biochemistry,Biochemistry,39,18,,0006-2960,,,,,,,,,,,,,,,,,,,,5341,5348,2000, citations,citations_2,50405,215629,2,wt1 ref 1,reference citation,,,,,,RNA Binding by the KTS Splice Variants of the Wilms' Tumor Suppressor Protein WT1,submitted,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,,,recently submitted citations,citations_1,50407,215649,1,,entry citation,,,,,,Quantifying the relationship between Conformational Dynamics and Enzymatic Activity in Ribonuclease HI Homologues,submitted,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50408,215664,1,,entry citation,,,,,,Quantifying the relationship between Conformational Dynamics and Enzymatic Activity in Ribonuclease HI Homologues,submitted,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50409,215678,1,,entry citation,,,,,,Quantifying the relationship between Conformational Dynamics and Enzymatic Activity in Ribonuclease HI Homologues,submitted,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5041,215692,1,,entry citation,,,11683624,,,"Solution Structure and Backbone Dynamics of the Human DNA Ligase IIIalpha BRCT Domain",published,journal,Biochemistry,,40,44,,,,,,,,,,,,,,,,,,,,,,13158,13166,2001, citations,citations_1,50412,215714,1,,entry citation,,,,,,Backbone and side-chain chemical shift assignments of p50 subunit of NF-kB transcription factor,in preparation,journal,Biomol. NMR Assign.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50414,215736,1,,entry citation,,,25223348,10.1186/s12934-014-0140-1,,Bacterial cytoplasm as an effective cell compartment for producing functional VHH-based affinity reagents and Camelidae IgG-like recombinant antibodies.,published,journal,Microb. Cell Fact.,Microbial cell factories,13,,,1475-2859,,,,,,,,,,,,,,,,,,,,140,140,2014, citations,entry_citation,5042,215752,1,,entry citation,,,11601972,,,Monomeric Solution Structure of Prototypical 'C' Chemokine Lymphotactin,published,journal,Biochemistry,,40,42,,,,,,,,,,,,,,,,,,,,,,12486,12496,2001, citations,entry_citation,5043,215766,1,,entry citation,,,,,,"Structural Characterization of the LEM Motif Common to Three Human Inner Nuclear Membrane Proteins",published,journal,Structure,,9,,,,,,,,,,,,,,,,,,,,,,,503,511,2001, citations,entry_citation,5044,215784,1,,entry citation,,21363704,11469865,,,"Solution Structure of the Third Immunoglobulin Domain of the Neural Cell Adhesion Molecule N-CAM: Can Solution Studies Define the Mechanism of Homophilic Binding?",published,journal,J. Mol. Biol.,Journal of Molecular Biology,311,1,,,,,,,,,,,,,,,,,,,,,,161,172,2001, citations,entry_citation,5056,216279,1,,entry citation,,22257244,12369816,,,"NMR Solution Structure of ATTp, an Arabidopsis thaliana Trypsin Inhibitor",published,journal,Biochemistry,,41,41,,,,,,,,,,,,,,,,,,,,,,12284,12296,2002, citations,entry_citation,5057,216297,1,,entry citation,,21579731,11722581,,,"NMR Studies in Aqueous Solution Fail to Identify Significant Conformational Differences between the Monomeric Forms of Two Alzheimer Peptides with Widely Different Plaque-competence, A beta(1-40)(ox) and A beta(1-42)(ox)",published,journal,Eur. J. Biochem.,,268,22,,,,,,,,,,,,,,,,,,,,,,5930,5936,2001, citations,15Nlabel_citation,5272,220960,2,,reference citation,,,15035609,,,"Same fold with different mobility: backbone dynamics of small protease inhibitors from the desert locust, Schistocerca gregaria",published,journal,Biochemistry,,43,12,,,,,,,,,,,,,,,,,,,,,,3376,3384,2004, citations,ref_DYANA,5044,215785,2,,reference citation,,,9367762,,,Torsion angle dynamics for NMR structure calculation with the new program DYANA.,published,journal,J. Mol. Biol.,Journal of molecular biology,273,1,,0022-2836,,,,,,,,,,,,,,,,,,,,283,298,1997,"The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from distance constraints and torsion angle constraints collected by nuclear magnetic resonance (NMR) experiments performs simulated annealing by molecular dynamics in torsion angle space and uses a fast recursive algorithm to integrate the equations of motions. Torsion angle dynamics can be more efficient than molecular dynamics in Cartesian coordinate space because of the reduced number of degrees of freedom and the concomitant absence of high-frequency bond and angle vibrations, which allows for the use of longer time-steps and/or higher temperatures in the structure calculation. It also represents a significant advance over the variable target function method in torsion angle space with the REDAC strategy used by the predecessor program DIANA. DYANA computation times per accepted conformer in the ""bundle"" used to represent the NMR structure compare favorably with those of other presently available structure calculation algorithms, and are of the order of 160 seconds for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300 computer. Test calculations starting from conformers with random torsion angle values further showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures." citations,ref_SANE,5044,215786,3,,reference citation,,,11370778,,,SANE (Structure Assisted NOE Evaluation): an automated model-based approach for NOE assignment.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,19,4,,0925-2738,,,,,,,,,,,,,,,,,,,,321,329,2001,"A reliable automated approach for assignment of NOESY spectra would allow more rapid determination of protein structures by NMR. In this paper we describe a semi-automated procedure for complete NOESY assignment (SANE, Structure Assisted NOE Evaluation), coupled to an iterative procedure for NMR structure determination where the user is directly involved. Our method is similar to ARIA [Nilges et al. (1997) J. Mol. Biol., 269, 408-422], but is compatible with the molecular dynamics suites AMBER and DYANA. The method is ideal for systems where an initial model or crystal structure is available, but has also been used successfully for ab initio structure determination. Use of this semi-automated iterative approach assists in the identification of errors in the NOE assignments to short-cut the path to an NMR solution structure." citations,ref_AMBER,5044,215787,4,,reference citation,,11183777,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_NMRView,5044,215788,5,,reference citation,,,,,,NMRView: A computer program for the visualization and analysis of NMR data,,journal,J. Biomol. NMR,,4,,,,,,,,,,,,,,,,,,,,,,,603,614,1994, citations,ref_NMRPipe,5044,215789,6,,reference citation,,96088118,,,,NMRPipe: a multidimensional spectral processing system based on UNIX pipes,,journal,J. Biomol. NMR,,6,3,,,,,,,,,,,,,,,,,,,,,,277,293,1995, citations,citations_1,50454,215812,1,,entry citation,,,,10.1101/2020.09.04.283309,,Dynamics of the HD regulatory subdomain of PARP-1; substrate access and allostery in PARP activation and inhibition,published,journal,BioRxiv,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50455,215841,1,,entry citation,,,,10.1101/2020.09.04.283309,,Dynamics of the HD regulatory subdomain of PARP-1; substrate access and allostery in PARP activation and inhibition,published,journal,BioRxiv,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50456,215863,1,,entry citation,,,,10.1101/2020.09.04.283309,,Dynamics of the HD regulatory subdomain of PARP-1; substrate access and allostery in PARP activation and inhibition,published,journal,BioRxiv,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50457,215885,1,,entry citation,,,,10.1101/2020.09.04.283309,,Dynamics of the HD regulatory subdomain of PARP-1; substrate access and allostery in PARP activation and inhibition,published,journal,BioRxiv,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50458,215907,1,,entry citation,,,,10.1101/2020.09.04.283309,,Dynamics of the HD regulatory subdomain of PARP-1; substrate access and allostery in PARP activation and inhibition,published,journal,BioRxiv,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50459,215929,1,,entry citation,,,,10.1101/2020.09.04.283309,,Dynamics of the HD regulatory subdomain of PARP-1; substrate access and allostery in PARP activation and inhibition,published,journal,BioRxiv,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5046,215950,1,,entry citation,,,15476802,,,"Mutational and structural analysis of stem-loop IIIC of the hepatitis C virus and GB virus B internal ribosome entry sites",published,journal,J. Mol. Biol.,,343,4,,,,,,,,,,,,,,,,,,,,,,805,817,2004, citations,citations_1,50460,215972,1,,entry citation,,,,10.1101/2020.09.04.283309,,Dynamics of the HD regulatory subdomain of PARP-1; substrate access and allostery in PARP activation and inhibition,published,journal,BioRxiv,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50461,215992,1,,entry citation,,,,10.1101/2020.09.04.283309,,Dynamics of the HD regulatory subdomain of PARP-1; substrate access and allostery in PARP activation and inhibition,published,journal,BioRxiv,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations_1,50463,216012,1,,entry citation,,,23565145,10.1371/journal.pone.0059255,,Conformational and functional effects induced by D- and L-amino acid epimerization on a single gene encoded peptide from the skin secretion of Hypsiboas punctatus,published,journal,PLoS ONE,PloS one,8,4,,1932-6203,,,,,,,,,,,,,,,,,,,,e59255,e59255,2013, citations,entry_citation,5047,216030,1,,entry citation,,,11574466,,,NMR structure of the LCCL Domain and its Implications for DFNA9 Deafness Disorder,published,journal,EMBO J.,EMBO Journal,20,19,,,,,,,,,,,,,,,,,,,,,,5347,5353,2001, citations,citations_1,50478,216049,1,,entry citation,,,25846210,10.1042/BJ20141243,,Intrinsically disordered cytoplasmic domains of two cytokine receptors mediate conserved interactions with membranes.,published,journal,Biochem. J.,The Biochemical journal,468,3,,1470-8728,,,,,,,,,,,,,,,,,,,,495,506,2015, citations,entry_citation,5048,216064,1,,entry citation,,,11934897,,,"Structure and backbone dynamics of apo- and holo-cellular retinol-binding protein in solution",published,journal,J. Biol. Chem.,,277,24,,,,,,,,,,,,,,,,,,,,,,21983,21997,2002, citations,entry_citation,5049,216087,1,,entry citation,,21885813,11888273,,,"The Human Interferon Receptor: NMR-based Modeling, Mapping of the IFN-alpha2 Binding Site, and Observed Ligand-Induced Tightening",published,journal,Biochemistry,,41,11,,,,,,,,,,,,,,,,,,,,,,3575,3585,2002, citations,entry_citation,505,216102,1,,entry citation,,,,,"Banci, Lucia, Bertini, Ivano, Luchinat, Claudio, Piccioli, Mario, Scozzafava, Andrea, Turano, Paola, ""1H NOE Studies on Dicopper(II) Dicobalt(II)Superoxide Dismutase,"" Inorg. Chem. 28, 4650-4656 (1989).",1H NOE Studies on Dicopper(II) Dicobalt(II)Superoxide Dismutase,published,journal,Inorg. Chem.,,28,,,,,,,,,,,,,,,,,,,,,,,4650,4656,1989, citations,entry_citation,5050,216116,1,,entry citation,,21576162,11562364,,,"Solution Structure of a Kunitz-type Chymotrypsin Inhibitor Isolated from the Elapid Snake Bungarus fasciatus",published,journal,J. Biol. Chem.,,276,48,,,,,,,,,,,,,,,,,,,,,,45079,45087,2001, citations,citations_1,50509,216133,1,,entry citation,,,,,,"1H, 13C, 15N chemical shift assignments for RRM1 domain of human RBM6",in preparation,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_1,5057,216298,2,,reference citation,,,9636276,,"Dobeli H, Draeger N, Huber G, Jakob P, Schmidt D, Seilheimer B, Stuber D, Wipf B, Zulauf M. A biotechnological method provides access to aggregation competent monomeric Alzheimer's 1-42 residue amyloid peptide. Biotechnology (N Y). 1995 Sep;13(9):988-93.",A biotechnological method provides access to aggregation competent monomeric Alzheimer's 1-42 residue amyloid peptide.,published,journal,Biotechnology (N.Y.),Bio/technology (Nature Publishing Company),13,9,,0733-222X,,,,,,,,,,,,,,,,,,,,988,993,1995,"Senile plaques, a neuropathological hallmark of Alzheimer's disease, consist primarily of insoluble aggregates of beta-amyloid peptide (A beta). A 42-residue peptide (A beta 1-42) appears to be the predominant form. In contrast to A beta 1-40, A beta 1-42 is characterized by its extreme tendency to aggregate into fibers or precipitate. A tailored biotechnological method prevents aggregation of A beta 1-42 monomers during its production. The method is based on a protein tail fused to the amino terminus of A beta. This tail leads to a high expression in E. coli, and a histidine affinity tag facilitates purification. Selective cleavage of the fusion tail is performed with cyanogen bromide by immobilizing the fusion protein on a reversed phase chromatography column. Cleavage then occurs only at the methionine positioned at the designed site but not at the methionine contained in the membrane anchor sequence of A beta. Furthermore, immobilization prevents aggregation of cleaved A beta. Elution from the HPLC column and all succeeding purification steps are optimized to preserve A beta 1-42 as a monomer. Solutions of monomeric A beta 1-42 spontaneously aggregate into fibers within hours. This permits the investigation of the transition of monomers into fibers and the correlation of physico-chemical properties with biological activities. Mutations of A beta 1-42 at position 35 influence the aggregation properties. Wild-type A beta 1-42 with methionine at position 35 has similar properties as A beta with a methionine sulfoxide residue. The fiber formation tendency, however, is reduced when position 35 is occupied by a glutamine, serine, leucine, or a glutamic acid residue." citations,entry_citation,5058,216312,1,,entry citation,,,,,,"Letter to the Editor: Sequence specific 1H, 13C and 15N resonance assignments of human GABA receptor associated protein",published,journal,J. Biomol. NMR,,21,2,,,,,,,,,,,,,,,,,,,,,,183,184,2001, citations,entry_citation,5059,216336,1,,entry citation,,21843898,11854485,,,An NMR Approach to Stuctural Proteomics,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,99,4,,,,,,,,,,,,,,,,,,,,,,1825,1830,2002, citations,ref_1,5059,216337,2,,reference citation,,,9097040,,"Itoh T, Aiba H, Baba T, Hayashi K, Inada T, Isono K, Kasai H, Kimura S, Kitakawa M, Kitagawa M, Makino K, Miki T, Mizobuchi K, Mori H, Mori T, Motomura K, Nakade S, Nakamura Y, Nashimoto H, Nishio Y, Oshima T, Saito N, Sampei G, Seki Y, Horiuchi T, et al. A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map. DNA Res. 1996 Dec 31;3(6):379-92.",A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 40.1-50.0 min region on the linkage map.,published,journal,DNA Res.,DNA research : an international journal for rapid publication of reports on genes and genomes,3,6,,1340-2838,,,,,,,,,,,,,,,,,,,,379,392,1996,"The 465,813 base pair sequence corresponding to the 40.1-50.0 min region on the genetic map of Escherichia coli K-12 (W3110) was determined. Analysis of the sequence revealed that this region contained at least 466 potential open reading frames, of which 187 (40%) were previously reported, 105 (23%) were homologous to other known genes, 103 (22%) were identical or similar to hypothetical genes registered in databases, and the remaining 71 (15%) did not show a significant similarity to any other gene. At the 45.2-46.0 min region, we found a very large cluster of about 30 genes, whose functions are involved in the biosynthesis of polysaccharides as the components of outer membranes. In addition, we identified a new asn-tRNA gene, designated asnW, between the asnT and asnU genes and a new lysogenic phage attachment site as the cis-element." citations,entry_citation,506,216361,1,,entry citation,,,,,"Banci, Lucia, Bertini, Ivano, Luchinat, Claudio, Piccioli, Mario, Scozzafava, Andrea, Turano, Paola, ""1H NOE Studies on Dicopper(II) Dicobalt(II)Superoxide Dismutase,"" Inorg. Chem. 28, 4650-4656 (1989).",1H NOE Studies on Dicopper(II) Dicobalt(II)Superoxide Dismutase,published,journal,Inorg. Chem.,,28,,,,,,,,,,,,,,,,,,,,,,,4650,4656,1989, citations,entry_citation,5060,216375,1,,entry citation,,,,,,An NMR approach to structural proteomics,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,99,4,,,,,,,,,,,,,,,,,,,,,,1825,1830,2002, citations,entry_citation,5061,216405,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N resonance assignments and secondary structure of ADR6 DNA-binding domain",published,journal,J. Biomol. NMR,,21,2,,,,,,,,,,,,,,,,,,,,,,187,188,2001, citations,entry_citation,5062,216418,1,,entry citation,,21617172,11741592,,,"NMR Identification of local Structural Preferences in HIV-I Protease Tethered Heterodimer in 6 M Guanidine Hydrochloride",published,journal,FEBS Lett.,,509,2,,,,,,,,,,,,,,,,,,,,,,218,224,2001, citations,entry_citation,5064,216448,1,,entry citation,,,,,,"Letter to the Editor: Backbone 1H, 13C, and 15N resonance assignments for a 14 kD protein, GABAA receptor associated protein (GABARAP)",published,journal,J. Biomol. NMR,,21,2,,,,,,,,,,,,,,,,,,,,,,185,186,2001, citations,entry_citation,5065,216473,1,,entry citation,,21466850,11583159,,,"Application of Cross-correlated NMR Spin Relaxation to the Zinc-finger Protein CRP2(LIM2): Evidence for Collective Motions in LIM Domains",published,journal,Biochemistry,,40,32,,,,,,,,,,,,,,,,,,,,,,9596,9604,2001, citations,ref_1,5065,216474,2,,reference citation,,,9115265,,"Konrat R, Weiskirchen R, Krautler B, Bister K. Solution structure of the carboxyl-terminal LIM domain from quail cysteine-rich protein CRP2. J Biol Chem. 1997 May 2;272(18):12001-7.",Solution structure of the carboxyl-terminal LIM domain from quail cysteine-rich protein CRP2.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,272,18,,0021-9258,,,,,,,,,,,,,,,,,,,,12001,12007,1997,"Proteins of the cysteine-rich protein (CRP) family (CRP1, CRP2, and CRP3) are implicated in diverse processes linked to cellular differentiation and growth control. CRP proteins contain two LIM domains, each formed by two zinc-binding modules of the CCHC and CCCC type, respectively. The solution structure of the carboxyl-terminal LIM domain (LIM2) from recombinant quail CRP2 was determined by multidimensional homo- and heteronuclear magnetic resonance spectroscopy. The folding topology retains both independent zinc binding modules (CCHC and CCCC). Each module consists of two orthogonally arranged antiparallel beta-sheets, and the carboxyl-terminal CCCC module is terminated by an alpha-helix. 15N magnetic relaxation data indicate that the modules differ in terms of conformational flexibility. They pack together via a hydrophobic core region. In addition, Arg122 in the CCHC module and Glu155 in the CCCC module are linked by an intermodular hydrogen bond and/or salt bridge. These residues are absolutely conserved in the CRP family of LIM proteins, and their interaction might contribute to the relative orientation of the two zinc-binding modules in CRP LIM2 domains. The global fold of quail CRP2 LIM2 is very similar to that of the carboxyl-terminal LIM domain of the related but functionally distinct CRP family member CRP1, analyzed recently. The carboxyl-terminal CCCC module is structurally related to the DNA-binding domain of the erythroid transcription factor GATA-1. In the two zinc-binding modules of quail CRP2 LIM2, flexible loop regions made up of conserved amino acid residues are located on the same side of the LIM2 domain and may cooperate in macromolecular recognition." citations,entry_citation,5078,216796,1,,entry citation,,21975169,11839747,,,"Solution Structure and Dynamics of the Lipoic Acid-bearing Domain of Human Mitochondrial Branched-chain Alpha-Keto Acid Dehydrogenase",published,journal,J. Biol. Chem.,,277,18,,,,,,,,,,,,,,,,,,,,,,15865,15873,2002, citations,entry_citation,5079,216817,1,,entry citation,,,11591150,,,"Solution Structure and Dynamics of the Functional Domain of Paracoccus denitrificans Cytochrome c552 in both Redox States",published,journal,Biochemistry,,40,,,,,,,,,,,,,,,,,,,,,,,12312,12320,2001, citations,ref_2,5065,216475,3,,reference citation,,,9722554,,"Konrat R, Krautler B, Weiskirchen R, Bister K. Structure of cysteine- and glycine-rich protein CRP2. Backbone dynamics reveal motional freedom and independent spatial orientation of the lim domains. J Biol Chem. 1998 Sep 4;273(36):23233-40.",Structure of cysteine- and glycine-rich protein CRP2. Backbone dynamics reveal motional freedom and independent spatial orientation of the lim domains.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,273,36,,0021-9258,,,,,,,,,,,,,,,,,,,,23233,23240,1998,"Members of the cysteine- and glycine-rich protein family (CRP1, CRP2, and CRP3) contain two zinc-binding LIM domains, LIM1 (amino-terminal) and LIM2 (carboxyl-terminal), and are implicated in diverse cellular processes linked to differentiation, growth control, and pathogenesis. Here we report the solution structure of full-length recombinant quail CRP2 as determined by multi-dimensional triple-resonance NMR spectroscopy. The structural analysis revealed that the global fold of the two LIM domains in the context of the full-length protein is identical to the recently determined solution structures of the isolated individual LIM domains of quail CRP2. There is no preference in relative spatial orientation of the two domains. This supports the view that the two LIM domains are independent structural and presumably functional modules of CRP proteins. This is also reflected by the dynamic properties of CRP2 probed by 15N relaxation values (T1, T2, and nuclear Overhauser effect). A model-free analysis revealed local variations in mobility along the backbone of the two LIM domains in the native protein, similar to those observed for the isolated domains. Interestingly, fast and slow motions observed in the 58-amino acid linker region between the two LIM domains endow extensive motional freedom to CRP2. The dynamic analysis indicates independent backbone mobility of the two LIM domains and rules out correlated LIM domain motion in full-length CRP2. The finding that the LIM domains in a protein encompassing multiple LIM motifs are structurally and dynamically independent from each other supports the notion that these proteins may function as adaptor molecules arranging two or more protein constituents into a macromolecular complex." citations,entry_citation,5066,216506,1,,entry citation,,,11560491,,,"Three-dimensional Structure and Dynamics of a Brain Specific Growth Inhibitory Factor: Metallothionein-3",published,journal,Biochemistry,,40,,,,,,,,,,,,,,,,,,,,,,,11433,11441,2001, citations,ref_1,5066,216507,2,,reference citation,,,8589602,,"Wishart DS, Bigam CG, Yao J, Abildgaard F, Dyson HJ, Oldfield E, Markley JL, Sykes BD. 1H, 13C and 15N chemical shift referencing in biomolecular NMR. J Biomol NMR. 1995 Sep;6(2):135-40.","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,5067,216528,1,,entry citation,,21443460,11559360,,,"Solution Structure of the Lipoyl Domain of the Chimeric Dihydrolipoyl Dehydrogenase P64K from Neisseria meningitidis",published,journal,Eur. J. Biochem.,,268,18,,,,,,,,,,,,,,,,,,,,,,4908,4917,2001, citations,entry_citation,5068,216547,1,,entry citation,,21830315,11841203,,,"NMR Structural Study of Two-disulfide Variant of hen Lysozyme: 2SS[6-127, 30-115]--A Disulfide Intermediate with a Partly Unfolded Structure",published,journal,Biochemistry,,41,7,,,,,,,,,,,,,,,,,,,,,,2130,2139,2002, citations,entry_citation,5069,216567,1,,entry citation,,21830315,11841203,,,"NMR Structural Study of Two-disulfide Variant of hen Lysozyme : 2SS[6-127, 30-115]--A Disulfide Intermediate with a Partly Unfolded Structure",published,journal,Biochemistry,,41,7,,,,,,,,,,,,,,,,,,,,,,2130,2139,2002, citations,entry_citation,507,216587,1,,entry citation,,,,,"Robertson, Andrew D., Rhyu, Gyung Ihm, Westler, William M., Markley, John L., ""Assignment of the 13C-NMR Spectra of Virgin and Reactive-Site Modified Turkey Ovomucoid Third Domain,"" Biopolymers 29, 461-467 (1990).","Assignment of the 13C-NMR Spectra of Virgin and Reactive-Site Modified Turkey Ovomucoid Third Domain",published,journal,Biopolymers,,29,,,,,,,,,,,,,,,,,,,,,,,461,467,1990, citations,entry_citation,5070,216600,1,,entry citation,,,,,,"Structure and dynamics of the anticodon-arm binding domain of Bacillus stearothermophilus tyrosyl-tRNA synthetase",published,journal,Structure,,10,,,,,,,,,,,,,,,,,,,,,,,311,317,2002, citations,entry_citation,5071,216627,1,,entry citation,,21404978,11513585,,,"Structure, Dynamics, and Thermodynamics of the Structural Domain of Troponin C in Complex with the Regulatory Peptide 1-40 of Troponin I",published,journal,Biochemistry,,40,34,,,,,,,,,,,,,,,,,,,,,,10063,10077,2001, citations,entry_citation,5072,216657,1,,entry citation,,,11439187,,,"Mechanisms Contributing to T Cell Receptor Signaling and Assembly Revealed by the Solution Structure of an Ectodomain Fragment of the CD3eg Heterodimer",published,journal,Cell,,105,,,,,,,,,,,,,,,,,,,,,,,913,923,2001, citations,entry_citation,5073,216680,1,,entry citation,,21426425,11535053,,,"Structural Comparison of Monomeric Variants of the Chemokine MIP-1beta having Differing Ability to bind the Receptor CCR5",published,journal,Biochemistry,,40,36,,,,,,,,,,,,,,,,,,,,,,10782,10791,2001, citations,entry_citation,5074,216695,1,,entry citation,,21363388,11470279,,,"Structural Analysis of Emerin, an inner Nuclear Membrane Protein Mutated in X-linked Emery-Dreifuss Muscular Dystrophy",published,journal,FEBS Lett.,,501,2-3,,,,,,,,,,,,,,,,,,,,,,171,176,2001, citations,entry_citation,5075,216712,1,,entry citation,,21639988,11781107,,,Solution Structure of Human Apolipoprotein(a) Kringle IV type 6,published,journal,Biochemistry,,41,2,,,,,,,,,,,,,,,,,,,,,,660,668,2002, citations,entry_citation,5076,216730,1,,entry citation,,99052121,9835056,,,"Resonance Assignment and Secondary Structure of the Cold Shock Domain of the Human YB-1 Protein",published,journal,J. Biomol. NMR,,12,3,,,,,,,,,,,,,,,,,,,,,,463,464,1998, citations,entry_citation,5077,216761,1,,entry citation,,,12367520,,,"Myxoma virus immunomodulatory protein M156R is a structural mimic of eukaryotic translation initiation factor eIF2a",published,journal,J. Mol. Biol.,,322,,,,,,,,,,,,,,,,,,,,,,,943,954,2002, citations,ref_1,5077,216762,2,,reference citation,,,11854485,,"Yee A, Chang X, Pineda-Lucena A, Wu B, Semesi A, Le B, Ramelot T, Lee GM, Bhattacharyya S, Gutierrez P, Denisov A, Lee CH, Cort JR, Kozlov G, Liao J, Finak G, Chen L, Wishart D, Lee W, McIntosh LP, Gehring K, Kennedy MA, Edwards AM, Arrowsmith CH. An NMR approach to structural proteomics. Proc Natl Acad Sci U S A. 2002 Feb 19;99(4):1825-30.",An NMR approach to structural proteomics.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,99,4,,0027-8424,,,,,,,,,,,,,,,,,,,,1825,1830,2002,"The influx of genomic sequence information has led to the concept of structural proteomics, the determination of protein structures on a genome-wide scale. Here we describe an approach to structural proteomics of small proteins using NMR spectroscopy. Over 500 small proteins from several organisms were cloned, expressed, purified, and evaluated by NMR. Although there was variability among proteomes, overall 20% of these proteins were found to be readily amenable to NMR structure determination. NMR sample preparation was centralized in one facility, and a distributive approach was used for NMR data collection and analysis. Twelve structures are reported here as part of this approach, which allowed us to infer putative functions for several conserved hypothetical proteins." citations,entry_citation,5649,229417,1,,entry citation,,,14675814,,,Random coil carbon chemical shifts of deoxyribonucleic acids,published,journal,J. Magn. Reson.,,166,1,,,,,,,,,,,,,,,,,,,,,,11,18,2004, citations,ref_1,5079,216818,2,,reference citation,,,10826890,,"Pristovsek, P., Luecke, C., Reincke, B., Loehr, F., Ludwig, B. & Rueterjans, H. (2000). Complete 1H, 15N and 13C assignment of the functional domain of Paracoccus denitrificans cytochrome c552 in the reduced state. J. Biomol. NMR, 16, 353-354.","Complete 1H, 15N and 13C assignment of the functional domain of paracoccus denitrificans cytochrome c552 in the reduced state.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,16,4,,0925-2738,,,,,,,,,,,,,,,,,,,,353,354,2000, citations,ref_2,5079,216819,3,,reference citation,,,10866825,,"Pristovsek, P., Luecke, C., Reincke, B., Ludwig, B. & Rueterjans, H. (2000) Solution structure of the functional domain of Paracoccus denitrificans cytochrome c552 in the reduced state. Eur. J. Biochem. 267, 4205-4212.",Solution structure of the functional domain of Paracoccus denitrificans cytochrome c552 in the reduced state.,published,journal,Eur. J. Biochem.,European journal of biochemistry / FEBS,267,13,,0014-2956,,,,,,,,,,,,,,,,,,,,4205,4212,2000,"In order to determine the solution structure of Paracoccus denitrificans cytochrome c552 by NMR, we cloned and isotopically labeled a 10.5-kDa soluble fragment (100 residues) containing the functional domain of the 18.2-kDa membrane-bound protein. Using uniformly 15N-enriched samples of cytochrome c552 in the reduced state, a variety of two-dimensional and three-dimensional heteronuclear double-resonance NMR experiments was employed to achieve complete 1H and 15N assignments. A total of 1893 distance restraints was derived from homonuclear 2D-NOESY and heteronuclear 3D-NOESY spectra; 1486 meaningful restraints were used in the structure calculations. After restrained energy minimization a family of 20 structures was obtained with rmsd values of 0.56 +/- 0. 10 A and 1.09 +/- 0.09 A for the backbone and heavy atoms, respectively. The overall topology is similar to that seen in previously reported models of this class of proteins. The global fold consists of two long helices at the N-terminus and C-terminus and three shorter helices surrounding the heme moiety; the helices are connected by well-defined loops. Comparison with the X-ray structure shows some minor differences in the positions of the Trp57 and Phe65 side-chain rings as well as the heme propionate groups." citations,ref_3,5079,216820,4,,reference citation,,,10216157,,"Reincke, B., Thoeny-Meyer, L., Dannehl, C., Odenwald, A., Aidim, M., Witt, H., Rueterjans, H. & Ludwig, B. (1999) Heterologous expression of soluble fragments of cytochrome c552 acting as electron donor to the Paracoccus denitrificans cytochrome c oxidase. Biochim. Biophys. Acta, 1441, 114-120.",Heterologous expression of soluble fragments of cytochrome c552 acting as electron donor to the Paracoccus denitrificans cytochrome c oxidase.,published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1411,1,,0006-3002,,,,,,,,,,,,,,,,,,,,114,120,1999,"A membrane-bound c-type cytochrome, c552, acts as the electron mediator between the cytochrome bc1 complex and cytochrome c oxidase in the branched respiratory chain of the bacterium Paracoccus denitrificans. Unlike in mitochondria where a soluble cytochrome c interacts with both complexes, the bacterial c552, the product of the cycM gene, shows a tripartite structure, with an N-terminal membrane anchor separated from a typical class I cytochrome domain by a highly charged region. Two derivative fragments, lacking either only the membrane spanning region or both N-terminal domains, were constructed on the genetic level, and expressed in Escherichia coli cotransformed with the ccm gene cluster encoding host-specific cytochrome c maturation factors. High levels of cytochromes c were expressed and located in the periplasm as holo-proteins; both these purified c552 fragments are functional in electron transport to oxidase, as ascertained by kinetic measurements, and will prove useful for future structural studies of complex formation by NMR and X-ray diffraction." citations,ref_4,5079,216821,5,,reference citation,,,7628479,,"Turba, A., Jetzek, M. & Ludwig, B. (1995) Purification of Paracoccus denitrificans cytochrome c552 and sequence analysis of the gene. Eur. J. Biochem., 231, 259-265.",Purification of Paracoccus denitrificans cytochrome c552 and sequence analysis of the gene.,published,journal,Eur. J. Biochem.,European journal of biochemistry / FEBS,231,1,,0014-2956,,,,,,,,,,,,,,,,,,,,259,265,1995,"Unlike mitochondria, many bacteria use a large repertoire of c-type cytochromes in different branches of their electron transport system. Among the many cytochromes c present in the soil bacterium Paracoccus denitrificans, a membrane-bound cytochrome (c552) has been suggested to mediate the electron transport between the cytochrome bc1 complex and cytochrome-c oxidase [Berry, E. A. & Trumpower, B. L. (1985) J. Biol. Chem. 260, 2458-2467]. We have purified this cytochrome from cytoplasmic membranes, and cloned and sequenced its gene, cycM. Sequence analysis reveals that, while its C-terminal portion is highly similar to type-I cytochromes c, its N-terminal part contains a hydrophobic segment providing membrane attachment. In addition, we present immunological evidence for its functional role in respiration." citations,entry_citation,508,216848,1,,entry citation,,,,,"Robertson, Andrew D., Rhyu, Gyung Ihm, Westler, William M., Markley, John L., ""Assignment of the 13C-NMR Spectra of Virgin and Reactive-Site Modified Turkey Ovomucoid Third Domain,"" Biopolymers 29, 461-467 (1990).","Assignment of the 13C-NMR Spectra of Virgin and Reactive-Site Modified Turkey Ovomucoid Third Domain",published,journal,Biopolymers,,29,,,,,,,,,,,,,,,,,,,,,,,461,467,1990, citations,entry_citation,5080,216861,1,,entry citation,,,11591150,,,"Solution Structure and Dynamics of the Functional Domain of Paracoccus denitrificans Cytochrome c552 in both Redox States",published,journal,Biochemistry,,40,,,,,,,,,,,,,,,,,,,,,,,12312,12320,2001, citations,ref_1,5080,216862,2,,reference citation,,,11200533,,"Luecke, C., Reincke, B., Loehr, F., Pristovsek, P., Ludwig, B. & Rueterjans, H. (2000). Complete 1H, 15N and 13C assignment of the functional domain of Paracoccus denitrificans cytochrome c552 in the oxidized state. J. Biomol. NMR, 18, 365-366.","Complete 1H, 15N and 13C assignment of the functional domain of Paracoccus denitrificans cytochrome c552 in the oxidized state.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,18,4,,0925-2738,,,,,,,,,,,,,,,,,,,,365,366,2000, citations,entry_citation,5092,217126,1,,entry citation,,21551163,11517232,,,"NMR Structure of the ""Ball-and-chain"" Domain of KCNMB2, the beta 2-subunit of large Conductance Ca2+ and Voltage-activated Potassium Channels",published,journal,J. Biol. Chem.,,276,45,,,,,,,,,,,,,,,,,,,,,,42116,41121,2001, citations,entry_citation,5093,217143,1,,entry citation,,,11824762,,,"Resonance assignments for cold-shock protein ribosome-binding factor A (RbfA) from Escherichia coli",published,journal,J. Biomol. NMR,,21,4,,,,,,,,,,,,,,,,,,,,,,389,390,2001, citations,entry_citation,5273,220988,1,,entry citation,,,,,,"Comparative structure analysis of proteinase inhibitors from the desert locust, Schistocerca gregaria",published,journal,Eur. J. Biochem.,,269,,,,,,,,,,,,,,,,,,,,,,,527,537,2002, citations,entry_citation,5274,221002,1,,entry citation,,,,,,"Comparative structure analysis of proteinase inhibitors from the desert locust, Schistocerca gregaria",published,journal,Eur. J. Biochem.,,269,,,,,,,,,,,,,,,,,,,,,,,527,537,2002, citations,entry_citation,5275,221017,1,,entry citation,,,11867517,,,"The rhesus rotavirus VP4 sialic acid binding domain has a galectin fold with a novel carbohydrate binding site",published,journal,EMBO J.,,21,,,,,,,,,,,,,,,,,,,,,,,885,897,2002, citations,ref_2,5080,216863,3,,reference citation,,,10216157,,"Reincke, B., Thoeny-Meyer, L., Dannehl, C., Odenwald, A., Aidim, M., Witt, H., Rueterjans, H. & Ludwig, B. (1999) Heterologous expression of soluble fragments of cytochrome c552 acting as electron donor to the Paracoccus denitrificans cytochrome c oxidase. Biochim. Biophys. Acta, 1441, 114-120.",Heterologous expression of soluble fragments of cytochrome c552 acting as electron donor to the Paracoccus denitrificans cytochrome c oxidase.,published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1411,1,,0006-3002,,,,,,,,,,,,,,,,,,,,114,120,1999,"A membrane-bound c-type cytochrome, c552, acts as the electron mediator between the cytochrome bc1 complex and cytochrome c oxidase in the branched respiratory chain of the bacterium Paracoccus denitrificans. Unlike in mitochondria where a soluble cytochrome c interacts with both complexes, the bacterial c552, the product of the cycM gene, shows a tripartite structure, with an N-terminal membrane anchor separated from a typical class I cytochrome domain by a highly charged region. Two derivative fragments, lacking either only the membrane spanning region or both N-terminal domains, were constructed on the genetic level, and expressed in Escherichia coli cotransformed with the ccm gene cluster encoding host-specific cytochrome c maturation factors. High levels of cytochromes c were expressed and located in the periplasm as holo-proteins; both these purified c552 fragments are functional in electron transport to oxidase, as ascertained by kinetic measurements, and will prove useful for future structural studies of complex formation by NMR and X-ray diffraction." citations,ref_3,5080,216864,4,,reference citation,,,7628479,,"Turba, A., Jetzek, M. & Ludwig, B. (1995) Purification of Paracoccus denitrificans cytochrome c552 and sequence analysis of the gene. Eur. J. Biochem., 231, 259-265.",Purification of Paracoccus denitrificans cytochrome c552 and sequence analysis of the gene.,published,journal,Eur. J. Biochem.,European journal of biochemistry / FEBS,231,1,,0014-2956,,,,,,,,,,,,,,,,,,,,259,265,1995,"Unlike mitochondria, many bacteria use a large repertoire of c-type cytochromes in different branches of their electron transport system. Among the many cytochromes c present in the soil bacterium Paracoccus denitrificans, a membrane-bound cytochrome (c552) has been suggested to mediate the electron transport between the cytochrome bc1 complex and cytochrome-c oxidase [Berry, E. A. & Trumpower, B. L. (1985) J. Biol. Chem. 260, 2458-2467]. We have purified this cytochrome from cytoplasmic membranes, and cloned and sequenced its gene, cycM. Sequence analysis reveals that, while its C-terminal portion is highly similar to type-I cytochromes c, its N-terminal part contains a hydrophobic segment providing membrane attachment. In addition, we present immunological evidence for its functional role in respiration." citations,entry_citation,5081,216891,1,,entry citation,,,,,,"Letter to the Editor: 1H, 15N and 13C resonance assignments for the Gallium protoporphyrin IX-HasAsm hemophore complex",published,journal,J. Biomol. NMR,,21,2,,,,,,,,,,,,,,,,,,,,,,189,190,2001, citations,ref_1,5081,216892,2,,reference citation,,,9571116,,"Ottiger M, Delaglio F, Bax A. Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra. J. Magn. Reson. 1998 Apr;131(2):373-8.",Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra.,published,journal,J. Magn. Reson.,"Journal of magnetic resonance (San Diego, Calif. : 1997)",131,2,,1090-7807,,,,,,,,,,,,,,,,,,,,373,378,1998,"Simple procedures are described for recording complementary in-phase and antiphase J-coupled NMR spectra. The sum and difference of these spectra contain only the upfield and the downfield components of a doublet, making it possible to measure the J splitting directly from these combinations without an increase in resonance overlap relative to the decoupled spectrum. The approach is demonstrated for measurement of 1JNH splittings and 2JHNC splittings in oriented and isotropic ubiquitin. Dipolar couplings obtained from differences in the splittings measured in the oriented and isotropic phases are in excellent agreement with dipolar couplings obtained from direct measurement of the splitting or from a conventional E. COSY-type measurement." citations,ref_2,5081,216893,3,,reference citation,,,,,"Bartels, C., Xia, T., Billeter, M., Guntert, P. and Wuthrich, K. J. Biomol. NMR, 5, 1-10 (1995).",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5082,216910,1,,entry citation,,21651072,11790849,,,Solution Structure of a K(+)-Channel Blocker from the Scorpion Tityus cambridgei,published,journal,Protein Sci.,,11,2,,,,,,,,,,,,,,,,,,,,,,390,400,2002, citations,entry_citation,5083,216925,1,,entry citation,,,12049637,,,"Solution Structure and Backbone Dynamics of Human Epidermal-Type Fatty Acid-Binding Protein (E-FABP)",published,journal,Biochem. J.,,364,Pt 3,,,,,,,,,,,,,,,,,,,,,,725,737,2002, citations,entry_citation,5084,216943,1,,entry citation,,,11287632,,,"Structure and function of the C-terminal PABC domain of human poly(A)-binding protein",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,98,8,,,,,,,,,,,,,,,,,,,,,,4409,4413,2001, citations,entry_citation,5085,216970,1,,entry citation,,,11287632,,,"Structure and function of the C-terminal PABC domain of human poly(A)-binding protein",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,98,8,,,,,,,,,,,,,,,,,,,,,,4409,4413,2001, citations,entry_citation,5086,217001,1,,entry citation,,21932593,11935350,,,"Characterization of Hydrogenobacter thermophilus Cytochromes c(552) Expressed in the Cytoplasm and Periplasm of Escherichia coli",published,journal,J. Biol. Inorg. Chem.,,7,3,,,,,,,,,,,,,,,,,,,,,,260,272,2002, citations,entry_citation,5087,217020,1,,entry citation,,21932593,11935350,,,"Characterization of Hydrogenobacter thermophilus Cytochromes c(552) Expressed in the Cytoplasm and Periplasm of Escherichia coli",published,journal,J. Biol. Inorg. Chem.,,7,3,,,,,,,,,,,,,,,,,,,,,,260,272,2002, citations,entry_citation,5088,217038,1,,entry citation,,21932593,11935350,,,"Characterization of Hydrogenobacter thermophilus Cytochromes c(552) Expressed in the Cytoplasm and Periplasm of Escherichia coli",published,journal,J. Biol. Inorg. Chem.,,7,3,,,,,,,,,,,,,,,,,,,,,,260,272,2002, citations,entry_citation,5089,217057,1,,entry citation,,21932593,11935350,,,"Characterization of Hydrogenobacter thermophilus Cytochromes c(552) Expressed in the Cytoplasm and Periplasm of Escherichia coli",published,journal,J. Biol. Inorg. Chem.,,7,3,,,,,,,,,,,,,,,,,,,,,,260,272,2002, citations,entry_citation,509,217075,1,,entry citation,,,,,"Reed, Jennifer, de Ropp, Jeffrey S., Trewhella, Jill, Glass, David B., Liddle, William K., Bradbury, E. Morton, Kinzel, Volker, Walsh, Donal A., ""Conformational analysis of PKI(5-22)amide, the active inhibitory fragment of the inhibitor protein of the cyclic AMP-dependent protein kinase,"" Biochem. J. 264, 371-380 (1989).","Conformational analysis of PKI(5-22)amide, the active inhibitory fragment of the inhibitor protein of the cyclic AMP-dependent protein kinase",published,journal,Biochem. J.,,264,,,,,,,,,,,,,,,,,,,,,,,371,380,1989, citations,entry_citation,5090,217089,1,,entry citation,,21986772,11991358,,,"Letter to the Editor: 1H(N), 15N, 13CO, 13C[agr], 13C[bgr] Assignment and Secondary Structure of a 20 kDa [agr]-L-fucosidase from Pea using TROSY",published,journal,J. Biomol. NMR,,22,3,,,,,,,,,,,,,,,,,,,,,,295,296,2002, citations,entry_citation,5091,217102,1,,entry citation,,,,,,"Mutagenic modulation of the entropy change on oxidation of cytochrome B5: an analysis of the contribution of conformational entropy",submitted,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref-1,5093,217144,2,,reference citation,,,9217263,,"Zimmerman, D. E., Kulikowski, C. A., Huang, Y., Feng, W., Tashiro, M., Shimotakahara, S., Chien, C. Y., Powers, R., and Montelione, G. T. J. Mol. Biol. 269, 592-610, (1997)",Automated analysis of protein NMR assignments using methods from artificial intelligence.,published,journal,J. Mol. Biol.,Journal of molecular biology,269,4,,0022-2836,,,,,,,,,,,,,,,,,,,,592,610,1997,"An expert system for determining resonance assignments from NMR spectra of proteins is described. Given the amino acid sequence, a two-dimensional 15N-1H heteronuclear correlation spectrum and seven to eight three-dimensional triple-resonance NMR spectra for seven proteins, AUTOASSIGN obtained an average of 98% of sequence-specific spin-system assignments with an error rate of less than 0.5%. Execution times on a Sparc 10 workstation varied from 16 seconds for smaller proteins with simple spectra to one to nine minutes for medium size proteins exhibiting numerous extra spin systems attributed to conformational isomerization. AUTOASSIGN combines symbolic constraint satisfaction methods with a domain-specific knowledge base to exploit the logical structure of the sequential assignment problem, the specific features of the various NMR experiments, and the expected chemical shift frequencies of different amino acids. The current implementation specializes in the analysis of data derived from the most sensitive of the currently available triple-resonance experiments. Potential extensions of the system for analysis of additional types of protein NMR data are also discussed." citations,entry_citation,5094,217174,1,,entry citation,,21423492,11532009,,,"Chemosensory Protein from Moth Mamestra brassicae. Expression and Secondary Structure from 1H and 15N NMR",published,journal,Eur. J. Biochem.,,268,17,,,,,,,,,,,,,,,,,,,,,,4731,4739,2001, citations,entry_citation,5096,217198,1,,entry citation,,22218026,12110675,,,"Characterization of the Conserved Interaction between GATA and FOG Family Proteins",published,journal,J. Biol. Chem.,,277,38,,,,,,,,,,,,,,,,,,,,,,35720,35729,2002, citations,entry_citation,5097,217224,1,,entry citation,,,,,,"NMR structure of bucandin, a neurotoxin from the venom of the Malayan krait (Bungarus candidus)",published,journal,Biochem. J.,,360,,,,,,,,,,,,,,,,,,,,,,,539,548,2001, citations,entry_citation,5098,217243,1,,entry citation,,22518519,,,,"A Possible Physiological Function and the Tertiary Structure of a 4-kDa Peptide in Legumes",published,journal,Eur. J. Biochem.,,270,6,,,,,,,,,,,,,,,,,,,,,,1269,1276,2003, citations,entry_citation,5099,217261,1,,entry citation,,,12634064,,,"Increased backbone mobility in Beta-barrel enhances entropy gain driving binding of N-TIMP-1 to MMP-3",published,journal,J. Mol. Biol.,,327,3,,,,,,,,,,,,,,,,,,,,,,719,734,2003, citations,entry_reference_1,5099,217262,2,,reference citation,,,,,,"Global Orientation of Bound MMP-3 and N-TIMP-1 in Solution via Residual Dipolar Couplings",,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,510,217292,1,,entry citation,,,,,"Reed, Jennifer, de Ropp, Jeffrey S., Trewhella, Jill, Glass, David B., Liddle, William K., Bradbury, E. Morton, Kinzel, Volker, Walsh, Donal A., ""Conformational analysis of PKI(5-22)amide, the active inhibitory fragment of the inhibitor protein of the cyclic AMP-dependent protein kinase,"" Biochem. J. 264, 371-380 (1989).","Conformational analysis of PKI(5-22)amide, the active inhibitory fragment of the inhibitor protein of the cyclic AMP-dependent protein kinase",published,journal,Biochem. J.,,264,,,,,,,,,,,,,,,,,,,,,,,371,380,1989, citations,entry_citation,5100,217306,1,,entry citation,,21682384,11824760,,,"1H, 15N and 13C Assignments of FLIN2, an Intramolecular LMO2:ldb1 Complex",published,journal,J. Biomol. NMR,,21,4,,,,,,,,,,,,,,,,,,,,,,385,386,2001, citations,reference_1,5100,217307,2,,reference citation,,,11522923,,"J.E. Deane, E. Sum, J.P. Mackay, G.J. Lindeman, J.E. Visvader & J.M. Matthews Protein Engineering, in press (2001).","Design, production and characterization of FLIN2 and FLIN4: the engineering of intramolecular ldb1:LMO complexes.",published,journal,Protein Eng.,Protein engineering,14,7,,0269-2139,,,,,,,,,,,,,,,,,,,,493,499,2001,"The nuclear LIM-only (LMO) transcription factors LMO2 and LMO4 play important roles in both normal and leukemic T-cell development. LIM domains are cysteine/histidine-rich domains that contain two structural zinc ions and that function as protein-protein adaptors; members of the LMO family each contain two closely spaced LIM domains. These LMO proteins all bind with high affinity to the nuclear protein LIM domain binding protein 1 (ldb1). The LMO-ldb1 interaction is mediated through the N-terminal LIM domain (LIM1) of LMO proteins and a 38-residue region towards the C-terminus of ldb1 [ldb1(LID)]. Unfortunately, recombinant forms of LMO2 and LMO4 have limited solubility and stability, effectively preventing structural analysis. Therefore, we have designed and constructed a fusion protein in which ldb1(LID) and LIM1 of LMO2 can form an intramolecular complex. The engineered protein, FLIN2 (fusion of the LIM interacting domain of ldb1 and the N-terminal LIM domain of LMO2) has been expressed and purified in milligram quantities. FLIN2 is monomeric, contains significant levels of secondary structure and yields a sharp and well-dispersed one-dimensional (1)H NMR spectrum. The analogous LMO4 protein, FLIN4, has almost identical properties. These data suggest that we will be able to obtain high-resolution structural information about the LMO-ldb1 interactions." citations,entry_citation,5101,217340,1,,entry citation,,21592562,117733996,,,Structure and Properties of a Dimeric N-terminal Fragment of Human Ubiquitin,published,journal,J. Mol. Biol.,,314,4,,,,,,,,,,,,,,,,,,,,,,773,787,2001, citations,entry_citation,5102,217363,1,,entry citation,,,,,,"A helical region in the C-terminus of small-conductance Ca2+-activated K+ channels controls assembly with apo-calmodulin",published,journal,J. Biol. Chem.,,277,,,,,,,,,,,,,,,,,,,,,,,4558,4564,2002, citations,entry_citation,5103,217388,1,,entry citation,,,15213440,,,NMR structure of the Apo-S100P protein,published,journal,J. Biomol. NMR,,29,3,,,,,,,,,,,,,,,,,,,,,,399,402,2004, citations,entry_citation,514,218172,1,,entry citation,,,,,"Reed, Jennifer, de Ropp, Jeffrey S., Trewhella, Jill, Glass, David B., Liddle, William K., Bradbury, E. Morton, Kinzel, Volker, Walsh, Donal A., ""Conformational analysis of PKI(5-22)amide, the active inhibitory fragment of the inhibitor protein of the cyclic AMP-dependent protein kinase,"" Biochem. J. 264, 371-380 (1989).","Conformational analysis of PKI(5-22)amide, the active inhibitory fragment of the inhibitor protein of the cyclic AMP-dependent protein kinase",published,journal,Biochem. J.,,264,,,,,,,,,,,,,,,,,,,,,,,371,380,1989, citations,entry_citation,5140,218186,1,,entry citation,,22269625,12381305,,,"Structural and Immunological Characterization of Heteroclitic Peptide Analogues Corresponding to the 600-612 Region of the HIV Envelope gp41 Glycoprotein",published,journal,J. Mol. Biol.,,323,3,,,,,,,,,,,,,,,,,,,,,,503,521,2002, citations,entry_citation,5141,218205,1,,entry citation,,,,,,"Letter to the Editor: Sequence-specific resonance assignments of the N-terminal, 105-residue KaiC-interacting domain of SasA, a protein necessary for a robust circadian rhythm in Synechococcus elongatus",published,journal,J. Biomol. NMR,,24,1,,,,,,,,,,,,,,,,,,,,,,77,78,2002, citations,entry_citation,5142,218229,1,,entry citation,,21880664,11883780,,,"Letter to the Editor: Assignments of 1H, 13C and 15N Resonances of Human Lysozyme at 4 degrees C",published,journal,J. Biomol. NMR,,22,2,,,,,,,,,,,,,,,,,,,,,,183,184,2002, citations,reference_1,5103,217389,2,,reference citation,,,9514277,,"Gribenko A, Lopez MM, Richardson JM 3rd, Makhatadze GI. Cloning, overexpression, purification, and spectroscopic characterization ofhuman S100P. Protein Sci. 1998 Jan;7(1):211-5.","Cloning, overexpression, purification, and spectroscopic characterization of human S100P.",published,journal,Protein Sci.,Protein science : a publication of the Protein Society,7,1,,0961-8368,,,,,,,,,,,,,,,,,,,,211,215,1998,"The calcium-binding protein S100P has been found to be associated with human prostate cancer. We have overexpressed S100P in Escherichia coli using a T7 expression system. A rapid two-step procedure for the isolation of overexpressed S100P leads to a preparation of >95% pure protein with a yield of approximately 150 mg per liter of culture. The structural integrity of recombinant S100P was analyzed using CD and fluorescence spectroscopic techniques. The far-UV CD shows that secondary structure of recombinant S100P consists predominantly of a-helical structure. Both near-UV CD and tyrosine fluorescence spectra show that aromatic residues are involved in the formation of a specific, well packed structure, indicating that the recombinant S100P protein adopts a compact folded conformation. Ca2+ has a profound effect on S100P structure. Near-UV CD and fluorescence intensity of both internal (tyrosine) and external (ANS) probes suggest significant structural rearrangements in the tertiary structure of the molecule. The similarity of far-UV CD spectrum of S100P in the presence and in the absence of Ca2+ suggests that Ca2+ binding has only minor effects on secondary structure." citations,ref_2,5103,217390,3,,reference citation,,,10639564,,"Guerreiro Da Silva ID, Hu YF, Russo IH, Ao X, Salicioni AM, Yang X, Russo J. S100P calcium-binding protein overexpression is associated with immortalization of human breast epithelial cells in vitro and early stages of breast cancer development in vivo. Int J Oncol. 2000 Feb;16(2):231-40.",S100P calcium-binding protein overexpression is associated with immortalization of human breast epithelial cells in vitro and early stages of breast cancer development in vivo.,published,journal,Int. J. Oncol.,International journal of oncology,16,2,,1019-6439,,,,,,,,,,,,,,,,,,,,231,240,2000,"The mechanism of cell immortalization of human breast epithelial cells leading to neoplastic transformation is not clear. The isolation and characterization of a spontaneously immortalized human breast epithelial cell line, MCF-10F, have provided a valuable tool to identify genes involved in this process. Using the technique of differential display, we have identified seven cDNA bands differentially displayed in the MCF-10F cells when compared with the mortal S130 cells from which MCF-10F was originated. One of these bands was isolated and cloned. Sequence analysis revealed 99% homology to the EF-hand calcium-binding protein S100P (Placental). The clone was overexpressed in the immortal cell line MCF-10F when compared to the mortal counterpart S130 or other primary cultures of human breast epithelial cells. In addition, it was highly expressed in chemically transformed breast epithelial cell lines (BP1E and D3. 1), breast cancer cell line T47D, as well as in three invasive ductal carcinomas when compared to their normal adjacent tissue. The S100P protein was localized by immunohistochemistry, using a monoclonal antibody against the same amino acid sequence of the gene cloned, in ductal hyperplasias, in situ and invasive ductal carcinoma, but not in the normal tissues. We concluded that S100P overexpression is an early event that might play an important role in the immortalization of human breast epithelial cells in vitro and tumor progression in vivo." citations,entry_citation,5104,217405,1,,entry citation,,21843898,11854485,,,An NMR Approach to Structural Proteomics,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,99,4,,,,,,,,,,,,,,,,,,,,,,1825,1830,2002, citations,entry_citation,5105,217419,1,,entry citation,,21843898,11854485,,,An NMR Approach to Structural Proteomics,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,99,4,,,,,,,,,,,,,,,,,,,,,,1825,1830,2002, citations,entry_citation,5106,217433,1,,entry citation,,21843898,11854485,,,An NMR Approach to Structural Proteomics,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,99,4,,,,,,,,,,,,,,,,,,,,,,1825,1830,2002, citations,entry_citation,5107,217456,1,,entry citation,,21682385,11824761,,,"Letter to the Editor: Assignments of the 1H, 13C, and 15N resonances of the substrate-binding SSD domain from Lon protease",published,journal,J. Biomol. NMR,,21,4,,,,,,,,,,,,,,,,,,,,,,387,388,2001, citations,entry_citation,5108,217482,1,,entry citation,,22269625,,,,"Structural and Immunological Characterization of Heteroclitic Peptide Analogues Corresponding to the 600-612 Region of the HIV Envelope gp41 Glycoprotein",published,journal,J. Mol. Biol.,,323,3,,,,,,,,,,,,,,,,,,,,,,503,521,2002, citations,entry_citation,5109,217501,1,,entry citation,,22269625,,,,"Structural and Immunological Characterization of Heteroclitic Peptide Analogues Corresponding to the 600-612 Region of the HIV Envelope gp41 Glycoprotein",published,journal,J. Mol. Biol.,,323,3,,,,,,,,,,,,,,,,,,,,,,503,521,2002, citations,entry_citation,511,217520,1,,entry citation,,,,,"Reed, Jennifer, de Ropp, Jeffrey S., Trewhella, Jill, Glass, David B., Liddle, William K., Bradbury, E. Morton, Kinzel, Volker, Walsh, Donal A., ""Conformational analysis of PKI(5-22)amide, the active inhibitory fragment of the inhibitor protein of the cyclic AMP-dependent protein kinase,"" Biochem. J. 264, 371-380 (1989).","Conformational analysis of PKI(5-22)amide, the active inhibitory fragment of the inhibitor protein of the cyclic AMP-dependent protein kinase",published,journal,Biochem. J.,,264,,,,,,,,,,,,,,,,,,,,,,,371,380,1989, citations,entry_citation,5110,217535,1,,entry citation,,22269625,,,,"Structural and Immunological Characterization of Heteroclitic Peptide Analogues Corresponding to the 600-612 Region of the HIV Envelope gp41 Glycoprotein",published,journal,J. Mol. Biol.,,323,3,,,,,,,,,,,,,,,,,,,,,,503,521,2002, citations,entry_citation,5111,217555,1,,entry citation,,22269625,,,,"Structural and Immunological Characterization of Heteroclitic Peptide Analogues Corresponding to the 600-612 Region of the HIV Envelope gp41 Glycoprotein",published,journal,J. Mol. Biol.,,323,3,,,,,,,,,,,,,,,,,,,,,,503,521,2002, citations,entry_citation,5112,217575,1,,entry citation,,22651999,12767215,,,An Improved Solution Structure for Psi-conotoxin Piiie,published,journal,Biochemistry,,42,21,,,,,,,,,,,,,,,,,,,,,,6347,6352,2003, citations,entry_citation,5113,217600,1,,entry citation,,22651999,12767215,,,An Improved Solution Structure for Psi-conotoxin Piiie,published,journal,Biochemistry,,42,21,,,,,,,,,,,,,,,,,,,,,,6347,6352,2003, citations,entry_citation,5114,217622,1,,entry citation,,21885728,11888199,,,Refined Structure and Metal Binding Site of the Kalata B1 Peptide,published,journal,Arch. Biochem. Biophys.,,399,2,,,,,,,,,,,,,,,,,,,,,,142,148,2002, citations,entry_citation,5115,217638,1,,entry citation,,21579721,11722571,,,"Solution structure of Pyrobaculum aerophilum DsrC, an archaeal homologue of the gamma subunit of dissimilatory sulfite reductase",published,journal,Eur. J. Biochem.,,268,22,,,,,,,,,,,,,,,,,,,,,,5842,5850,2001, citations,entry_citation,5116,217671,1,,entry citation,,,11722571,,,"Solution Structure of Pyrobaculum aerophilum DsrC, an archaeal homologue of the gamma subunit of dissimilatory sulfite reductase",published,journal,Eur. J. Biochem.,,268,22,,,,,,,,,,,,,,,,,,,,,,5842,5850,2001, citations,entry_citation,5117,217702,1,,entry citation,,,11340665,,,"Structural and Dynamic Differences of Rhodostomin, an RGD-containing Disintegrin, and its D51E mutant",published,journal,"Proteins: Struct., Funct., Genet.",,43,4,,,,,,,,,,,,,,,,,,,,,,499,508,2001, citations,entry_citation,5143,218242,1,,entry citation,,,11888275,,,"NMR Structure of the Second Intracellular Loop of the alpha2A adrenergic receptor: evidence for a Novel Cytoplasmic Helix",published,journal,Biochemistry,,41,11,,,,,,,,,,,,,,,,,,,,,,3596,3604,2002, citations,ref_1,5117,217703,2,,reference citation,,,11340665,,"Guo RT, Chou LJ, Chen YC, Chen CY, Pari K, Jen CJ, Lo SJ, Huang SL, Lee CY, Chang TW, Chaung WJ. Expression in Pichia pastoris and characterization by circular dichroism and NMR of rhodostomin. Proteins. 2001 Jun 1;43(4):499-508.",Expression in Pichia pastoris and characterization by circular dichroism and NMR of rhodostomin.,published,journal,Proteins,Proteins,43,4,,0887-3585,,,,,,,,,,,,,,,,,,,,499,508,2001,"Rhodostomin (Rho) is a snake venom protein isolated from Calloselasma rhodostoma. Rho is a disintegrin that inhibits platelet aggregation by blocking the binding of fibrinogen to the integrin alpha(IIb)beta3 of platelets. Rho produced in Escherichia coli inhibited platelet aggregation with a K(I) value of 263 nM. Although functional, Rho produced in E. coli is misfolded based on our 2D and 3D NMR studies. In order to correct the folding problem, Rho was expressed in Pichia pastoris. The recombinant Rho expressed in P. pastoris inhibited platelet aggregation with a resulting K(I) value of 70 nM. This is the same potency as that of native Rho. CD analysis showed that the secondary structures of Rho are pH-independent and contain 3.5-7.9% alpha-helix, 48.2-50.5% beta-structures, and 42.3-47% coil. The sequential assignment and structure analysis of Rho were obtained using 2D and 3D 15N-edited NMR spectra. These results provide the first direct evidence that highly disulfide-bonded disintegrin can be expressed in P. pastoris with the correct fold. This evidence may serve as the basis for exploring the structure and function relationships as well as the dynamics of disintegrin and its variants." citations,entry_citation,5119,217725,1,,entry citation,,21950387,11952796,,,"NMR Investigations of Subunit c of the ATP Synthase from Propionigenium modestum in Chloroform/methanol/water (4:4:1)",published,journal,Eur. J. Biochem.,,269,7,,,,,,,,,,,,,,,,,,,,,,1942,1946,2002, citations,ref_1,5119,217726,2,,reference citation,,,10215857,,"Matthey U, Kaim G, Braun D, Wuthrich K, Dimroth P. NMR studies of subunit c of the ATP synthase from Propionigenium modestum in dodecylsulphate micelles. Eur J Biochem. 1999 Apr;261(2):459-67.",NMR studies of subunit c of the ATP synthase from Propionigenium modestum in dodecylsulphate micelles.,published,journal,Eur. J. Biochem.,European journal of biochemistry / FEBS,261,2,,0014-2956,,,,,,,,,,,,,,,,,,,,459,467,1999,"The structure of the Na+, Li+ or H+-binding c subunit of the ATP synthase from Propionigenium modestum was studied by NMR. Subunit c in dodecylsulphate micelles consists of four alpha-helical segments, I-IV, that are connected by short linker peptides with non-regular secondary structures. We propose that helices I (V4-I26) and IV (I69-V85) are membrane-spanning structures, and that helices II and III and the intervening hydrophilic loop are located in the cytoplasm. The Na+-binding residues Q32, E65 and S66 are located in the I-->II and III-->IV helix connections, probably near the membrane surface on the cytoplasmic side." citations,ref_2,5119,217727,3,,reference citation,,,10580496,,"Rastogi VK, Girvin ME. Structural changes linked to proton translocation by subunit c of the ATP synthase. Nature. 1999 Nov 18;402(6759):263-8.",Structural changes linked to proton translocation by subunit c of the ATP synthase.,published,journal,Nature,Nature,402,6759,,0028-0836,,,,,,,,,,,,,,,,,,,,263,268,1999,"F1F0 ATP synthases use a transmembrane proton gradient to drive the synthesis of cellular ATP. The structure of the cytosolic F1 portion of the enzyme and the basic mechanism of ATP hydrolysis by F1 are now well established, but how proton translocation through the transmembrane F0 portion drives these catalytic changes is less clear. Here we describe the structural changes in the proton-translocating F0 subunit c that are induced by deprotonating the specific aspartic acid involved in proton transport. Conformational changes between the protonated and deprotonated forms of subunit c provide the structural basis for an explicit mechanism to explain coupling of proton translocation by F0 to the rotation of subunits within the core of F1. Rotation of these subunits within F1 causes the catalytic conformational changes in the active sites of F1 that result in ATP synthesis." citations,ref_3,5119,217728,4,,reference citation,,,9636021,,"Girvin ME, Rastogi VK, Abildgaard F, Markley JL, Fillingame RH. Solution structure of the transmembrane H+-transporting subunit c of the F1F0 ATP synthase. Biochemistry. 1998 Jun 23;37(25):8817-24.",Solution structure of the transmembrane H+-transporting subunit c of the F1F0 ATP synthase.,published,journal,Biochemistry,Biochemistry,37,25,,0006-2960,,,,,,,,,,,,,,,,,,,,8817,8824,1998,"Subunit c is the H+-translocating component of the F1F0 ATP synthase complex. H+ transport is coupled to conformational changes that ultimately lead to ATP synthesis by the enzyme. The properties of the monomeric subunit in a single-phase solution of chloroform-methanol-water (4:4:1) have been shown to mimic those of the protein in the native complex. Triple resonance NMR experiments were used to determine the complete structure of monomeric subunit c in this solvent mixture. The structure of the protein was defined by >2000 interproton distances, 64 (3)JN alpha, and 43 hydrogen-bonding NMR-derived restraints. The root mean squared deviation for the backbone atoms of the two transmembrane helices was 0.63 A. The protein folds as a hairpin of two antiparallel helical segments, connected by a short structured loop. The conserved Arg41-Gln42-Pro43 form the top of this loop. The essential H+-transporting Asp61 residue is located at a slight break in the middle of the C-terminal helix, just prior to Pro64. The C-terminal helix changes direction by 30 +/- 5 degrees at the conserved Pro64. In its protonated form, the Asp61 lies in a cavity created by the absence of side chains at Gly23 and Gly27 in the N-terminal helix. The shape and charge distribution of the molecular surface of the monomeric protein suggest a packing arrangement for the oligomeric protein in the F0 complex, with the front face of one monomer packing favorably against the back face of a second monomer. The packing suggests that the proton (cation) binding site lies between packed pairs of adjacent subunit c." citations,entry_citation,512,217754,1,,entry citation,,,,,"Reed, Jennifer, de Ropp, Jeffrey S., Trewhella, Jill, Glass, David B., Liddle, William K., Bradbury, E. Morton, Kinzel, Volker, Walsh, Donal A., ""Conformational analysis of PKI(5-22)amide, the active inhibitory fragment of the inhibitor protein of the cyclic AMP-dependent protein kinase,"" Biochem. J. 264, 371-380 (1989).","Conformational analysis of PKI(5-22)amide, the active inhibitory fragment of the inhibitor protein of the cyclic AMP-dependent protein kinase",published,journal,Biochem. J.,,264,,,,,,,,,,,,,,,,,,,,,,,371,380,1989, citations,entry_citation,5120,217768,1,,entry citation,,21590355,11733021,,,Solution Structure of the mEGF/TGFalpha44-50 Chimeric Growth Factor,published,journal,Eur. J. Biochem.,,268,23,,,,,,,,,,,,,,,,,,,,,,6247,6255,2001, citations,entry_citation,5144,218258,1,,entry citation,,,11888275,,,"NMR Structure of the Second Intracellular Loop of the alpha2A adrenergic receptor: evidence for a Novel Cytoplasmic Helix",published,journal,Biochemistry,,41,11,,,,,,,,,,,,,,,,,,,,,,3596,3604,2002, citations,entry_citation,5145,218274,1,,entry citation,,22483920,12595265,,,NMR Structure of the Human Doppel Protein,published,journal,J. Mol. Biol.,,326,5,,,,,,,,,,,,,,,,,,,,,,1549,1557,2003, citations,entry_citation,5277,221085,1,,entry citation,,22131024,12135384,,,NMR Structure of Lung Surfactant Peptide SP-B(11-25),published,journal,Biochemistry,,41,30,,,,,,,,,,,,,,,,,,,,,,9627,9636,2002, citations,entry_citation,5278,221102,1,,entry citation,,22213647,12225754,,,Solution Structure of a Luteoviral P1-P2 frameshifting mRNA Pseudoknot,published,journal,J. Mol. Biol.,,322,3,,,,,,,,,,,,,,,,,,,,,,621,633,2002, citations,entry_citation,5386,223481,1,,entry citation,,22172844,12060657,,,"Structure of the Regulatory N-domain of Human Cardiac Troponin C in Complex with Human Cardiac Troponin I147-163 and Bepridil",published,journal,J. Biol. Chem.,,277,34,,,,,,,,,,,,,,,,,,,,,,31124,31133,2002, citations,ref_1,5120,217769,2,,reference citation,,,8940002,,"Puddicombe SM, Wood L, Chamberlin SG, Davies DE. The interaction of an epidermal growth factor/transforming growth facotr alpha tail chimera with the human epidermal growth factor receptor reveals uncexpected complexities. The Journal of Biological Chemistry. 271, 30392-30397.",The interaction of an epidermal growth factor/transforming growth factor alpha tail chimera with the human epidermal growth factor receptor reveals unexpected complexities.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,271,48,,0021-9258,,,,,,,,,,,,,,,,,,,,30392,30397,1996,"It has been assumed that substitution of homologous regions of transforming growth factor alpha (TGF-alpha) into epidermal growth factor (EGF) can be used to probe ligand-receptor recognition without detrimental effects on ligand characteristics for the human EGF receptor (EGFR). We show that a chimera of murine (m) EGF in which the carboxyl-terminal tail is substituted for that of TGF-alpha (mEGF/TGF-alpha44-50) results in complex features that belie this initial simplistic assumption. Comparison of EGF and mEGF/TGF-alpha44-50 in equilibrium binding assays showed that although the relative binding affinity of the chimera was reduced 80-200-fold, it was more potent than EGF in mitogenesis assays using NR6/HER cells. This superagonist activity could not be attributed to differences in ligand processing or to binding to other members of the c-erbB family. It appeared to be due, in part, to choice of an EGFR-overexpressing target cell where high receptor number compensated for the low affinity of the ligand; it also appeared to be related to the ability of the chimera to activate the EGFR tyrosine kinase. Thus, when EGFR autophosphorylation was measured, mEGF/TGF-alpha44-50 was more potent than EGF, despite its low affinity. When tested using chicken embryo fibroblasts, substitution of the TGF-alpha carboxyl-terminal tail into mEGF failed to enhance its binding affinity for chicken EGFRs; however, the chimera was intermediate in potency between TGF-alpha and mEGF in mitogenesis assays. Our results suggest a contextual requirement for EGFR recognition which is ligand-specific. Further, the unpredictable responses to chimeric ligands underline the complex nature of the processes of ligand recognition, receptor activation, and the ensuing cellular response." citations,entry_citation,5121,217783,1,,entry citation,,21864163,11742000,,,"In vivo Protein Cyclization Promoted by a Circularly Permuted Synechocystis sp. PCC6803 DnaB Mini-intein",published,journal,J. Biol. Chem.,,277,10,,,,,,,,,,,,,,,,,,,,,,7790,7798,2002, citations,entry_citation,5122,217803,1,,entry citation,,21864163,11742000,,,"In vivo Protein Cyclization Promoted by a Circularly Permuted Synechocystis sp. PCC6803 DnaB Mini-intein",published,journal,J. Biol. Chem.,,277,10,,,,,,,,,,,,,,,,,,,,,,7790,7798,2002, citations,entry_citation,5123,217821,1,,entry citation,,21571990,11714920,,,"Characterization of the Structure and Dynamics of Amyloidogenic Variants of Human Lysozyme by NMR Spectroscopy",published,journal,Protein Sci.,,10,12,,,,,,,,,,,,,,,,,,,,,,2525,2530,2001, citations,entry_citation,5124,217837,1,,entry citation,,21571990,11714920,,,"Characterization of the Structure and Dynamics of Amyloidogenic Variants of Human Lysozyme by NMR Spectroscopy",published,journal,Protein Sci.,,10,12,,,,,,,,,,,,,,,,,,,,,,2525,2530,2001, citations,entry_citation,5125,217852,1,,entry citation,,21571990,11714920,,,"Characterization of the Structure and Dynamics of Amyloidogenic Variants of Human Lysozyme by NMR Spectroscopy",published,journal,Protein Sci.,,10,12,,,,,,,,,,,,,,,,,,,,,,2525,2530,2001, citations,entry_citation,5126,217868,1,,entry citation,,21882794,11885987,,,"Complete 1H, 15N and 13C Assignment of the Carboxyl Terminal Domain of the Ciliary Neurotrophic Factor Receptor (CNTFR)",published,journal,J. Biomol. NMR,,22,1,,,,,,,,,,,,,,,,,,,,,,95,96,2002, citations,entry_citation,5127,217893,1,,entry citation,,21880663,11883779,,,"Letter to the Editor: Chemical shift assignment and chemical shift indexing of murine apo-Mts1",published,journal,J. Biomol. NMR,,22,2,,,,,,,,,,,,,,,,,,,,,,181,182,2002, citations,entry_citation,5128,217906,1,,entry citation,,21882795,11885988,,,"1H, 13C and 15N Resonance Assignments of GABARAP, GABAA Receptor Associated Protein",published,journal,J. Biomol. NMR,,22,1,,,,,,,,,,,,,,,,,,,,,,97,98,2002, citations,entry_citation,5129,217932,1,,entry citation,,,,,,Solution structure of MTH1880 from Methanobacterium Thermoautotrophicum,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,513,217957,1,,entry citation,,,,,"Reed, Jennifer, de Ropp, Jeffrey S., Trewhella, Jill, Glass, David B., Liddle, William K., Bradbury, E. Morton, Kinzel, Volker, Walsh, Donal A., ""Conformational analysis of PKI(5-22)amide, the active inhibitory fragment of the inhibitor protein of the cyclic AMP-dependent protein kinase,"" Biochem. J. 264, 371-380 (1989).","Conformational analysis of PKI(5-22)amide, the active inhibitory fragment of the inhibitor protein of the cyclic AMP-dependent protein kinase",published,journal,Biochem. J.,,264,,,,,,,,,,,,,,,,,,,,,,,371,380,1989, citations,entry_citation,5130,217971,1,,entry citation,,,,,,"Assignment of 1H, 13C and 15N resonances of Human Lysozyme at 35 and 4 degree C",in preparation,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5131,217984,1,,entry citation,,21881810,11884147,,,"Structure, Dynamics and Binding Characteristics of the Second PDZ Domain of PTP-BL",published,journal,J. Mol. Biol.,,316,5,,,,,,,,,,,,,,,,,,,,,,1101,1110,2002, citations,entry_citation,5132,218020,1,,entry citation,,22257244,12369816,,,"NMR Solution Structure of ATTp, an Arabidopsis thaliana Trypsin Inhibitor",published,journal,Biochemistry,,41,41,,,,,,,,,,,,,,,,,,,,,,12284,12296,2002, citations,entry_citation,5133,218033,1,,entry citation,,22257244,12369816,,,"NMR Solution Structure of ATTp, an Arabidopsis thaliana Trypsin Inhibitor",published,journal,Biochemistry,,41,41,,,,,,,,,,,,,,,,,,,,,,12284,12296,2002, citations,entry_citation,5134,218048,1,,entry citation,,22055466,12060684,,,Solution Structure of dAATAA and dAAUAA DNA Bulges,published,journal,Nucleic Acids Res.,,30,12,,,,,,,,,,,,,,,,,,,,,,2669,2677,2002, citations,entry_citation,5135,218072,1,,entry citation,,22055466,12060684,,,Solution Structure of dAATAA and dAAUAA DNA Bulges,published,journal,Nucleic Acids Res.,,30,12,,,,,,,,,,,,,,,,,,,,,,2669,2677,2002, citations,entry_citation,5136,218096,1,,entry citation,,22269625,12381305,,,"Structural and Immunological Characterization of Heteroclitic Peptide Analogues Corresponding to the 600-612 Region of the HIV Envelope gp41 Glycoprotein",published,journal,J. Mol. Biol.,,323,3,,,,,,,,,,,,,,,,,,,,,,503,521,2002, citations,entry_citation,5137,218115,1,,entry citation,,22269625,12381305,,,"Structural and Immunological Characterization of Heteroclitic Peptide Analogues Corresponding to the 600-612 Region of the HIV Envelope gp41 Glycoprotein",published,journal,J. Mol. Biol.,,323,3,,,,,,,,,,,,,,,,,,,,,,503,521,2002, citations,entry_citation,5138,218134,1,,entry citation,,22269625,12381305,,,"Structural and Immunological Characterization of Heteroclitic Peptide Analogues Corresponding to the 600-612 Region of the HIV Envelope gp41 Glycoprotein",published,journal,J. Mol. Biol.,,323,3,,,,,,,,,,,,,,,,,,,,,,503,521,2002, citations,entry_citation,5139,218153,1,,entry citation,,22269625,12381305,,,"Structural and Immunological Characterization of Heteroclitic Peptide Analogues Corresponding to the 600-612 Region of the HIV Envelope gp41 Glycoprotein",published,journal,J. Mol. Biol.,,323,3,,,,,,,,,,,,,,,,,,,,,,503,521,2002, citations,entry_citation,5249,220534,1,,entry citation,,,12237467,,,"Zinc substituted Desulfovibrio gigas desulforedoxin: resolving subunit degeneracy with non-symmetric pseudocontact shifts",published,journal,Protein Sci.,,11,10,,,,,,,,,,,,,,,,,,,,,,2464,2470,2002, citations,entry_citation,5250,220557,1,,entry citation,,,,,,"1H, 13C and 15N resonance assignment of the RNA-binding domain dimer form Bacillus subtilis transcriptional antiterminator GlcT",published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,Ref1,5145,218275,2,,reference citation,,,10525406,,"Moore RC, Lee IY, Silverman GL, Harrison PM, Strome R, Heinrich C, Karunaratne A, Pasternak SH, Chishti MA, Liang Y, Mastrangelo P, Wang K, Smit AF, Katamine S, Carlson GA, Cohen FE, Prusiner SB, Melton DW, Tremblay P, Hood LE, Westaway D. Ataxia in prion protein (PrP)-deficient mice is associated with upregulation of the novel PrP-like protein doppel. J Mol Biol. 1999 Oct 1;292(4):797-817.",Ataxia in prion protein (PrP)-deficient mice is associated with upregulation of the novel PrP-like protein doppel.,published,journal,J. Mol. Biol.,Journal of molecular biology,292,4,,0022-2836,,,,,,,,,,,,,,,,,,,,797,817,1999,"The novel locus Prnd is 16 kb downstream of the mouse prion protein (PrP) gene Prnp and encodes a 179 residue PrP-like protein designated doppel (Dpl). Prnd generates major transcripts of 1.7 and 2.7 kb as well as some unusual chimeric transcripts generated by intergenic splicing with Prnp. Like PrP, Dpl mRNA is expressed during embryogenesis but, in contrast to PrP, it is expressed minimally in the CNS. Unexpectedly, Dpl is upregulated in the CNS of two PrP-deficient (Prnp(0/0)) lines of mice, both of which develop late-onset ataxia, suggesting that Dpl may provoke neurodegeneration. Dpl is the first PrP-like protein to be described in mammals, and since Dpl seems to cause neurodegeneration similar to PrP, the linked expression of the Prnp and Prnd genes may play a previously unrecognized role in the pathogenesis of prion diseases or other illnesses." citations,entry_citation,5147,218299,1,,entry citation,,,11493688,,,"A Novel Metallothionein Containing a Zinc Finger within a Four-metal Cluster Protects a Bacterium from Zinc Toxicity",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,98,17,,,,,,,,,,,,,,,,,,,,,,9593,9598,2001, citations,entry_citation,5148,218323,1,,entry citation,,21633978,11772001,,,"NMR Structure of the [2Fe-2S] Ferredoxin Domain from Soluble Methane Monooxygenase Reductase and Interaction with its Hydroxylase",published,journal,Biochemistry,,41,1,,,,,,,,,,,,,,,,,,,,,,42,51,2002, citations,entry_citation,5149,218362,1,,entry citation,,,11888275,,,"NMR Structure of the Second Intracellular Loop of the alpha2A adrenergic receptor: evidence for a Novel Cytoplasmic Helix",published,journal,Biochemistry,,41,11,,,,,,,,,,,,,,,,,,,,,,3596,3604,2002, citations,entry_citation,515,218378,1,,entry citation,,,,,"Reed, Jennifer, de Ropp, Jeffrey S., Trewhella, Jill, Glass, David B., Liddle, William K., Bradbury, E. Morton, Kinzel, Volker, Walsh, Donal A., ""Conformational analysis of PKI(5-22)amide, the active inhibitory fragment of the inhibitor protein of the cyclic AMP-dependent protein kinase,"" Biochem. J. 264, 371-380 (1989).","Conformational analysis of PKI(5-22)amide, the active inhibitory fragment of the inhibitor protein of the cyclic AMP-dependent protein kinase",published,journal,Biochem. J.,,264,,,,,,,,,,,,,,,,,,,,,,,371,380,1989, citations,entry_citation,5150,218392,1,,entry citation,,,11888275,,,"NMR Structure of the Second Intracellular Loop of the alpha2A adrenergic receptor: evidence for a Novel Cytoplasmic Helix",published,journal,Biochemistry,,41,11,,,,,,,,,,,,,,,,,,,,,,3596,3604,2002, citations,entry_citation,5151,218408,1,,entry citation,,,11266631,,,"Designed Protein G Core Variants Fold to Native-like Structures: Sequence Selection by ORBIT Tolerates Variation in Backbone Specification",published,journal,Protein Sci.,,10,,,,,,,,,,,,,,,,,,,,,,,450,454,2001, citations,entry_citation,5152,218431,1,,entry citation,,,11266631,,,"Designed Protein G Core Variants Fold to Native-like Structures: Sequence Selection by ORBIT Tolerates Variation in Backbone Specification",published,journal,Protein Sci.,,10,,,,,,,,,,,,,,,,,,,,,,,450,454,2001, citations,entry_citation,5153,218455,1,,entry citation,,,,,,"Binding of the MMP-3 catalytic domain to N-TIMP-1 is driven by a large gain in entropy that includes modest contributions from the hydrophobic effect and the TIMP-1 backbone",in press,journal,J. Mol. Biol.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5154,218481,1,,entry citation,,20384870,10926526,,,"Tissue Inhibitor of Metalloproteinases-1 undergoes Microsecond to Millisecond Motions at sites of Matrix Metalloproteinase-induced fit",published,journal,J. Mol. Biol.,,301,2,,,,,,,,,,,,,,,,,,,,,,537,552,2000, citations,entry_citation,5155,218500,1,,entry citation,,,11478859,,,"Solution Structure and Interaction Surface of the C-terminal Domain from p47: A Major p97-cofactor Involved in SNARE Disassembly",published,journal,J. Mol. Biol.,,311,,,,,,,,,,,,,,,,,,,,,,,255,263,2001, citations,entry_citation,5156,218524,1,,entry citation,,21590353,11733019,,,"Structural and Biochemical Characterization of Neuronal Calretinin Domain I-II (residues 1-100). Comparison to Homologous Calbindin D28k Domain I-II (residues 1-93)",published,journal,Eur. J. Biochem.,,268,23,,,,,,,,,,,,,,,,,,,,,,6229,6237,2001, citations,ref-1,5156,218525,2,,reference citation,,,10600467,,"Palczewska M, Groves P, Kuznicki J. Use of Pichia pastoris for the expression, purification, and characterization of rat calretinin ""EF-hand"" domains. Protein Expr Purif. 1999 Dec;17(3):465-76.","Use of Pichia pastoris for the expression, purification, and characterization of rat calretinin ""EF-hand"" domains.",published,journal,Protein Expr. Purif.,Protein expression and purification,17,3,,1046-5928,,,,,,,,,,,,,,,,,,,,465,476,1999,"Calretinin (CR) is a calcium-binding, neuronal protein of undefined function. Related proteins either buffer intracellular calcium concentrations or are involved in calcium-signaling pathways. We transformed three CR gene fragment sequences, corresponding to its three complementary domains (I-II, III-IV, and V-VI), into Pichia pastoris. High yields of extracellular expression, of more than 200 mg/liter, were achieved. Simple purification protocols provide high yields of homogenous proteins: dialysis and DEAE-cellulose chromatography for domains I-II and III-IV or ammonium sulfate precipitation and octyl-Sepharose chromatography for domain V-VI. To our knowledge, this is the first report of the expression of an EF-hand protein using P. pastoris. Direct comparison of the purified yields of domain I-II indicates a approximately 20-fold improvement over Escherichia coli. N-terminal amino acid sequencing confirmed our gene products and two anti-calretinin antibodies recognized the appropriate domains. All three CR domains bind (45)Ca and the domain containing EF-hands V and VI seems to have a lower calcium capacity than the other domains. Circular dichroism indicates a high helix content for each of the domains. Calcium-induced structural changes in the first two domains, followed by tryptophan fluorescence, correspond with previous studies, while tyrosine emission fluorescence indicates calcium-induced structural changes also occur in domain V-VI. The methods and expression levels achieved are suitable for future NMR labeling of the proteins, with (15)N and (13)C, and structure-function studies that will help to further understand CR function." citations,ref-2,5156,218526,3,,reference citation,,,,,"Kay, L. E., Keifer, P. & Saarinen, T. (1992) Pure Absorption Gradient Enhanced Heteronuclear Single Quantum Correlation Spectroscopy with Improved Sensitivity, J. Am. Chem. Soc. 114, 10663-10665.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref-3,5156,218527,4,,reference citation,,,,,"Palmer, A. G., Cavanagh, J., Wright, P. E. & Rance, M. (1991) Sensitivity Improvement in Proton-Detected 2-Dimensional Heteronuclear Correlation Nmr-Spectroscopy, J. Magn. Reson. 93, 151-170.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5251,220571,1,,entry citation,,22001373,11889129,,,"Structural Rearrangement of Human Lymphotactin, a C Chemokine, under Physiological Solution Conditions",published,journal,J. Biol. Chem.,,277,20,,,,,,,,,,,,,,,,,,,,,,17863,17870,2002, citations,entry_citation,5252,220586,1,,entry citation,,22047884,12051946,,,"Structural Differences in the NOE-derived Structure of G-T Mismatched DNA relative to Normal DNA are Correlated with Differences in (13)C Relaxation-based Internal Dynamics",published,journal,J. Mol. Biol.,,319,1,,,,,,,,,,,,,,,,,,,,,,191,207,2002, citations,ref-4,5156,218528,5,,reference citation,,,8019138,,"Schleucher J, Schwendinger M, Sattler M, Schmidt P, Schedletzky O, Glaser SJ, Sorensen OW, Griesinger C. A general enhancement scheme in heteronuclear multidimensional NMR employing pulsed field gradients. J Biomol NMR. 1994 Mar;4(2):301-6.",A general enhancement scheme in heteronuclear multidimensional NMR employing pulsed field gradients.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,4,2,,0925-2738,,,,,,,,,,,,,,,,,,,,301,306,1994,"General pulse sequence elements that achieve sensitivity-enhanced coherence transfer from a heteronucleus to protons of arbitrary multiplicity are introduced. The building blocks are derived from the sensitivity-enhancement scheme introduced by Cavanagh et al. ((1991) J. Magn. Reson., 91, 429-436), which was used in conjunction with gradient coherence selection by Kay et al. ((1992) J. Am. Chem. Soc., 114, 10663-10665), as well as from a multiple-pulse sequence effecting a heteronuclear planar coupling Hamiltonian. The building blocks are incorporated into heteronuclear correlation experiments, in conjunction with coherence selection by the formation of a heteronuclear gradient echo. This allows for efficient water suppression without the need for water presaturation. The methods are demonstrated in HSQC-type experiments on a sample of a decapeptide in H2O. The novel pulse sequence elements can be incorporated into multidimensional experiments." citations,ref-5,5156,218529,6,,reference citation,,,,,"Grzesiek, S. & Bax, A. (1992) Improved 3D Triple-Resonance NMR Techniques Applied to a 31 kDa Protein, J. Magn. Reson. 96, 432-440.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref-6,5156,218530,7,,reference citation,,,,,"Kay, L. E., Ikura, M., Tschudin, R. & Bax, A. (1990) 3-Dimensional Triple-Resonance NMR-Spectroscopy of Isotopically Enriched Proteins, J. Magn. Reson. 89, 496-514.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref-7,5156,218531,8,,reference citation,,,,,"Clubb, R. T., Thanabal, V. & Wagner, G. (1992) A Constant-Time Three-Dimensional Triple-Resonance Pulse Scheme to Correlate Intraresidue {+1}H{+N},{+15}N,and {+13}C' Chemical Shifts in {+15}N-{+13}C-Labeled Proteins, J. Magn. Reson. 97, 213-217.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref-8,5156,218532,9,,reference citation,,,,,"Kay, L. E., Xu, G. Y. & Yamazaki, T. (1994) Enhanced-Sensitivity Triple-Resonance Spectroscopy with Minimal H2O Saturation, J. Magn. Reson. Ser.A 109, 129-133.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref-9,5156,218533,10,,reference citation,,,,,"Sattler, M., Schleucher, J. & Griesinger, C. (1999) Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients, Prog. Nucl. Magn. Reson. Spect. 34, 93-158.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref-10,5156,218534,11,,reference citation,,,,,"Muhandiram, D. R. & Kay, L. E. (1994) Gradient-Enhanced Triple-Resonance 3-Dimensional Nmr Experiments With Improved Sensitivity, J. Magn. Reson. Ser.B 103, 203-216.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref-11,5156,218535,12,,reference citation,,,,,"Wittekind, M. & Mueller, L. (1993) HNCACB, a High-Sensitivity 3D NMR Experiment to Correlate Amide-Proton and Nitrogen Resonances with the Alpha-Carbon and Beta-Carbon Resonances in Proteins, J. Magn. Reson. Ser.B 101, 201-205.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref-12,5156,218536,13,,reference citation,,,,,"Grzesiek, S. & Bax, A. (1992) An Efficient Experiment For Sequential Backbone Assignment of Medium-Sized Isotopically Enriched Proteins, J. Magn. Reson. 99, 201-207.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref-13,5156,218537,14,,reference citation,,,8477186,,"Grzesiek S, Bax A. Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N-enriched proteins. J Biomol NMR. 1993 Mar;3(2):185-204.",Amino acid type determination in the sequential assignment procedure of uniformly 13C/15N-enriched proteins.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,3,2,,0925-2738,,,,,,,,,,,,,,,,,,,,185,204,1993,"Experiments and procedures are described that greatly alleviate the sequential assignment process of uniformly 13C/15N-enriched proteins by determining the type of amino acid from experiments that correlate side chain with backbone amide resonances. A recently proposed 3D NMR experiment, CBCA(CO)NH, correlates C alpha and C beta resonances to the backbone amide 1H and 15N resonances of the next residue (Grzesiek, S. and Bax, A. (1992) J. Am. Chem. Soc., 114, 6291-6293). An extension of this experiment is described which correlates the proton H beta and H alpha resonances to the amide 1H and 15N resonances of the next amino acid, and a detailed product operator description is given. A simple 2D-edited constant-time HSQC experiment is described which rapidly identifies H beta and C beta resonances of aromatic or Asn/Asp residues. The extent to which combined knowledge of the C alpha and C beta chemical shift values determines the amino acid type is investigated, and it is demonstrated that the combined C alpha and C beta chemical shifts of three or four adjacent residues usually are sufficient for defining a unique position in the protein sequence." citations,ref-14,5156,218538,15,,reference citation,,,7812158,,"Kuboniwa H, Grzesiek S, Delaglio F, Bax A. Measurement of HN-H alpha J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods. J Biomol NMR. 1994 Nov;4(6):871-8.",Measurement of HN-H alpha J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,4,6,,0925-2738,,,,,,,,,,,,,,,,,,,,871,878,1994,"Two new methods are described for the measurement of three-bond JHNH alpha couplings in proteins isotopically enriched with 15N. Both methods leave the water magnetization in an unsaturated state, parallel to the z-axis, and therefore offer significant enhancements in sensitivity for rapidly exchanging backbone amide protons. The J couplings can be measured either from a set of constant-time 2D 1H-15N HMQC spectra, which are modulated in intensity by JHNH alpha, or from a water-flip-back version of the 3D HNHA experiment. The method is demonstrated for a sample of calcium-free calmodulin. Residues Lys75-Asp80 have JHNH alpha values in the 6-7 Hz range, suggesting that a break in the 'central helix' occurs at the same position as previously observed in solution NMR studies of Ca(2+)-ligated calmodulin." citations,ref-15,5156,218539,16,,reference citation,,,,,"Sattler, M., Maurer, M., Schleucher, J. & Griesinger, C. (1995) A Simultaneous N-15,H-1-HSQC and C-13,H-1-HSQC With Sensitivity Enhancement and a Heteronuclear Gradient-Echo, J. Biomol. NMR 5, 97-102.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5157,218557,1,,entry citation,,21845977,11856360,,,"Solution Structure of a Hydrophobic Analogue of the Winter Flounder Antifreeze Protein",published,journal,Eur. J. Biochem.,,269,4,,,,,,,,,,,,,,,,,,,,,,1259,1266,2002, citations,entry_citation,5253,220604,1,,entry citation,,22047884,12051946,,,"Structural Differences in the NOE-derived Structure of G-T Mismatched DNA relative to Normal DNA are Correlated with Differences in (13)C Relaxation-based Internal Dynamics",published,journal,J. Mol. Biol.,,319,1,,,,,,,,,,,,,,,,,,,,,,191,207,2002, citations,entry_citation,5254,220622,1,,entry citation,,,,,,"1H and 13C assigned chemical shifts for chromogranin A, catestatin fragment",published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5255,220635,1,,entry citation,,,8756320,,,Ancestral beta/gamma-crystallin precursor structure in a yeast killer toxin,published,journal,Nat. Struct. Biol.,,3,8,,,,,,,,,,,,,,,,,,,,,,622,665,1996, citations,ref_1,5157,218558,2,,reference citation,,,9688560,,"Haymet, A.D.J., Ward, L.G., Harding, M.M. & Knight, C.A. (1998) Valine substituted winter flounder antifreeze - preservation of ice growth hysteresis, FEBS Lett., 430, 301-306.",Valine substituted winter flounder 'antifreeze': preservation of ice growth hysteresis.,published,journal,FEBS Lett.,FEBS letters,430,3,,0014-5793,,,,,,,,,,,,,,,,,,,,301,306,1998,"Three mutant polypeptides of the type I 37-residue winter flounder 'antifreeze' protein have been synthesized. All four threonine residues in the native peptide were been mutated to serine, valine and glycine respectively and two additional salt bridges were incorporated into the sequences in order to improve aqueous solubility. The peptides were analyzed by nanoliter osmometry, the 'ice hemisphere' test, the 'crystal habit' test, measurement of ice growth hysteresis and CD spectroscopy. While the valine and serine mutants retain the alpha-helical structure, only the valine mutant retains 'antifreeze' activity similar to that of the native protein. These data show that the threonine hydroxyl groups do not play a crucial role in the accumulation of the native 'antifreeze' protein at the ice/water interface and the inhibition of ice growth below the equilibrium melting temperature." citations,entry_citation,5158,218584,1,,entry citation,,21581530,11724558,,,"Conformational and Dynamic Characterization of the Molten Globule State of an Apomyoglobin Mutant with an Altered Folding Pathway",published,journal,Biochemistry,,40,48,,,,,,,,,,,,,,,,,,,,,,14459,14467,2001, citations,entry_citation,5159,218605,1,,entry citation,,21880665,11883781,,,"Letter to the Editor: Sequence-specific Resonance Assignment of the Second Ran-binding Domain of Human RanBP2",published,journal,J. Biomol. NMR,,22,2,,,,,,,,,,,,,,,,,,,,,,185,186,2002, citations,ref_1,5159,218606,2,,reference citation,,,7603572,,"Yokoyama et al. 1995, Nature 376,184-188.",A giant nucleopore protein that binds Ran/TC4.,published,journal,Nature,Nature,376,6536,,0028-0836,,,,,,,,,,,,,,,,,,,,184,188,1995,"Ran/TC4 is a small nuclear G protein that forms a complex with the chromatin-bound guanine nucleotide release factor RCC1 (ref. 2). Loss of RCC1 causes defects in cell cycle progression, RNA export and nuclear protein import. Some of these can be suppressed by overexpression of Ran/TC4 (ref. 1), suggesting that Ran/TC4 functions downstream of RCC1. We have searched for proteins that bind Ran/TC4 by using a two-hybrid screen, and here we report the identification of RanBP2, a novel protein of 3,224 residues. This giant protein comprises an amino-terminal 700-residue leucine-rich region, four RanBP1-homologous (refs 9, 10) domains, eight zinc-finger motifs similar to those of NUP153 (refs 11, 12), and a carboxy terminus with high homology to cyclophilin. The molecule contains the XFXFG pentapeptide motif characteristic of nuclear pore complex (NPC) proteins, and immunolocalization suggests that RanBP2 is a constituent of the NPC. The fact that NLS-mediated nuclear import can be inhibited by an antibody directed against RanBP2 supports a functional role in protein import through the NPC." citations,ref_2,5159,218607,3,,reference citation,,,7775481,,"Wu et al. 1995, J. Biol. Chem. 270,14209-14213.","Nup358, a cytoplasmically exposed nucleoporin with peptide repeats, Ran-GTP binding sites, zinc fingers, a cyclophilin A homologous domain, and a leucine-rich region.",published,journal,J. Biol. Chem.,The Journal of biological chemistry,270,23,,0021-9258,,,,,,,,,,,,,,,,,,,,14209,14213,1995,"The Ras-related nuclear protein, Ran, has been implicated in nuclear transport. By screening a HeLa cell lambda expression library with Ran-GTP and sequencing overlapping cDNA clones, we have obtained the derived primary structure of a protein with a calculated molecular mass of 358 kDa. Using antibodies raised against an expressed segment of this protein, we obtained punctate nuclear surface staining by immunofluorescence microscopy that is characteristic for nucleoporins. Electron microscopy of immunogold-decorated rat liver nuclear envelopes sublocalized the 358-kDa protein at (or near) the tip of the cytoplasmic fibers of the nuclear pore complex (NPC). In agreement with current convention, this protein was therefore termed Nup358 (for nucleoporin of 358 kDa). Nup358 contains a leucine-rich region, four potential Ran binding sites (i.e. Ran binding protein 1 homologous domains) flanked by nucleoporin-characteristic FXFG or FG repeats, eight zinc finger motifs, and a C-terminal cyclophilin A homologous domain. Consistent with the location of Nup358 at the cytoplasmic fibers of the NPC, we found decoration with Ran-gold at only the cytoplasmic side of the NPC. Thus, Nup358 is the first nucleoporin shown to contain binding sites for two of three soluble nuclear transport factors so far isolated, namely karyopherin and Ran-GTP." citations,ref_3,5159,218608,4,,reference citation,,,10078529,,"Vetter et al. 1999, Nature 398,39-46.",Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: implications for nuclear transport.,published,journal,Nature,Nature,398,6722,,0028-0836,,,,,,,,,,,,,,,,,,,,39,46,1999,"The protein Ran is a small GTP-binding protein that binds to two types of effector inside the cell: Ran-binding proteins, which have a role in terminating export processes from the nucleus to the cytoplasm, and importin-beta-like molecules that bind cargo proteins during nuclear transport. The Ran-binding domain is a conserved sequence motif found in several proteins that participate in these transport processes. The Ran-binding protein RanBP2 contains four of these domains and constitutes a large part of the cytoplasmic fibrils that extend from the nuclear-pore complex. The structure of Ran bound to a non-hydrolysable GTP analogue (Ran x GppNHp) in complex with the first Ran-binding domain (RanBD1) of human RanBP2 reveals not only that RanBD1 has a pleckstrin-homology domain fold, but also that the switch-I region of Ran x GppNHp resembles the canonical Ras GppNHp structure and that the carboxy terminus of Ran is wrapped around RanBD1, contacting a basic patch on RanBD1 through its acidic end. This molecular 'embrace' enables RanBDs to sequester the Ran carboxy terminus, triggering the dissociation of Ran x GTP from importin-beta-related transport factors and facilitating GTP hydrolysis by the GTPase-activating protein ranGAP. Such a mechanism represents a new type of switch mechanism and regulatory protein-protein interaction for a Ras-related protein." citations,entry_citation,5256,220648,1,,entry citation,,22075324,12079344,,,"Solution Conformations of Unmodified and A(37)N(6)-dimethylallyl Modified Anticodon Stem-loops of Escherichia coli tRNA (Phe)",published,journal,J. Mol. Biol.,,319,5,,,,,,,,,,,,,,,,,,,,,,1015,1034,2002, citations,entry_citation,5257,220671,1,,entry citation,,,9108730,,,"Conformation of thymosin beta-9 in water/fluoroalcohol solution determined by NMR spectroscopy",published,journal,Biopolymers,,41,6,,,,,,,,,,,,,,,,,,,,,,623,634,1997, citations,entry_citation,5259,220684,1,,entry citation,,22075324,12079344,,,"Solution Conformations of Unmodified and A(37)N(6)-dimethylallyl Modified Anticodon Stem-loops of Escherichia coli tRNA (Phe)",published,journal,J. Mol. Biol.,,319,5,,,,,,,,,,,,,,,,,,,,,,1015,1034,2002, citations,entry_citation,5260,220708,1,,entry citation,,,12237467,,,"Zinc substituted Desulfovibrio gigas desulforedoxin: resolving subunit degeneracy with non-symmetric pseudocontact shifts",published,journal,Protein Sci.,,11,10,,,,,,,,,,,,,,,,,,,,,,2464,2470,2002, citations,entry_citation,5261,220731,1,,entry citation,,22090783,12095254,,,The Nuclease A Inhibitor represents a new Variation of the Rare PR-1 Fold,published,journal,J. Mol. Biol.,,320,4,,,,,,,,,,,,,,,,,,,,,,771,782,2002, citations,ref_4,5159,218609,5,,reference citation,,,15826666,,"J.P. Geyer, R. Doeker, W. Kremer, X. Zhao, J. Kuhlmann and H.R. Kalbitzer ""Solution Structure of the Ran-binding Domain 2 of RanBP2 and its Interaction with the C Terminus of Ran"", J Mol Biol (2005) 348, 711-725.",Solution structure of the Ran-binding domain 2 of RanBP2 and its interaction with the C terminus of Ran.,published,journal,J. Mol. Biol.,Journal of molecular biology,348,3,,0022-2836,,,,,,,,,,,,,,,,,,,,711,725,2005,"The termination of export processes from the nucleus to the cytoplasm in higher eukaryotes is mediated by binding of the small GTPase Ran as part of the export complexes to the Ran-binding domains (RanBD) of Ran-binding protein 2 (RanBP2) of the nuclear pore complex. So far, the structures of the first RanBD of RanBP2 and of RanBP1 in complexes with Ran have been known from X-ray crystallographic studies. Here we report the NMR solution structure of the uncomplexed second RanBD of RanBP2. The structure shows a pleckstrin homology (PH) fold featuring two almost orthogonal beta-sheets consisting of three and four strands and an alpha-helix sitting on top. This is in contrast to the RanBD in the crystal structure complexes in which one beta-strand is missing. That is probably due to the binding of the C-terminal alpha-helix of Ran to the RanBD in these complexes. To analyze the interaction between RanBD2 and the C terminus of Ran, NMR-titration studies with peptides comprising the six or 28 C-terminal residues of Ran were performed. While the six-residue peptide alone does not bind to RanBD2 in a specific manner, the 28-residue peptide, including the entire C-terminal helix of Ran, binds to RanBD2 in a manner analogous to the crystal structures. By solving the solution structure of the 28mer peptide alone, we confirmed that it adopts a stable alpha-helical structure like in native Ran and therefore serves as a valid model of the Ran C terminus. These results support current models that assume recognition of the transport complexes by the RanBDs through the Ran C terminus that is exposed in these complexes." citations,entry_citation,516,218637,1,,entry citation,,,,,"Theriault, Y., Boulanger, Y., Saunders, J.K., ""Secondary Structure of the Human Growth Hormone Releasing Factor (GRF 1-29) by Two-Dimensional 1H-NMR Spectroscopy,"" Biopolymers 27, 1897-1904 (1988).","Secondary Structure of the Human Growth Hormone Releasing Factor (GRF 1-29) by Two-Dimensional 1H-NMR Spectroscopy",published,journal,Biopolymers,,27,,,,,,,,,,,,,,,,,,,,,,,1897,1904,1988, citations,entry_citation,5160,218650,1,,entry citation,,,11277936,,,"Solution structure of microcin J25, the single macrocyclic antimicrobial peptide from Escherichia coli",published,journal,Eur. J. Biochem.,,268,,,,,,,,,,,,,,,,,,,,,,,2124,2133,2001, citations,entry_citation,5161,218668,1,,entry citation,,21661495,11802714,,,"Characterization of the ATP-binding Domain of the Sarco(endo)plasmic Reticulum Ca(2+)-ATPase: Probing Nucleotide Binding By Multidimensional NMR",published,journal,Biochemistry,,41,4,,,,,,,,,,,,,,,,,,,,,,1156,1164,2002, citations,entry_citation,5162,218688,1,,entry citation,,21986774,11991360,,,"Letter to the Editor: 1H, 13C, and 15N Resonance Assignments and Secondary Structure of the PWI Domain from SRm160 using Reduced Dimensionality NMR",published,journal,J. Biomol. NMR,,22,3,,,,,,,,,,,,,,,,,,,,,,299,300,2002, citations,entry_citation,5163,218701,1,,entry citation,,21556002,11699644,,,"NMR Structure of Desulfovibrio gigas Rubredoxin: a Model for studying Protein Stabilization by Compatible Solutes",published,journal,Extremophiles,,5,5,,,,,,,,,,,,,,,,,,,,,,303,311,2001, citations,entry_citation,5164,218719,1,,entry citation,,21914663,11917010,,,NMR Structure of a Parallel-stranded DNA Duplex at Atomic Resolution,published,journal,Nucleic Acids Res.,,30,7,,,,,,,,,,,,,,,,,,,,,,1500,1511,2002, citations,entry_citation,5165,218738,1,,entry citation,,21843898,11854485,,,An NMR Approach to Structural Proteomics,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,99,4,,,,,,,,,,,,,,,,,,,,,,1825,1830,2002, citations,entry_citation,5166,218757,1,,entry citation,,21843898,11854485,,,An NMR Approach to Structural Proteomics,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,99,4,,,,,,,,,,,,,,,,,,,,,,1825,1830,2002, citations,entry_citation,5167,218781,1,,entry citation,,21986769,11991355,,,High-resolution NMR Structure of an AT-rich DNA Sequence,published,journal,J. Biomol. NMR,,22,3,,,,,,,,,,,,,,,,,,,,,,265,280,2002, citations,entry_citation,5169,218803,1,,entry citation,,21836431,11847272,,,"The Solution Structure of Human Beta2-microglobulin reveals the Prodromes of its Amyloid Transition",published,journal,Protein Sci.,,11,3,,,,,,,,,,,,,,,,,,,,,,487,499,2002, citations,entry_citation,517,218824,1,,entry citation,,,,,"Han, Kyou-Hoon, Niu, Chien-Hua, Roller, Peter P., Ferretti, James A., ""Conformation of the Second Disulfide Loop in Human Transforming Growth Factor-alpha Studied by Two-Dimensional NMR Spectroscopy,"" Biopolymers 27, 923-937 (1988).","Conformation of the Second Disulfide Loop in Human Transforming Growth Factor-alpha Studied by Two-Dimensional NMR Spectroscopy",published,journal,Biopolymers,,27,,,,,,,,,,,,,,,,,,,,,,,923,937,1988, citations,entry_citation,5170,218837,1,,entry citation,,21860383,11871662,,,"NMR Structure and Dynamics of the RNA-binding Site for the Histone mRNA Stem-Loop Binding Protein",published,journal,RNA,,8,1,,,,,,,,,,,,,,,,,,,,,,83,96,2002, citations,entry_citation,5171,218860,1,,entry citation,,21830327,11841215,,,"A Highly Destabilizing Mutation, G37A, of the Bovine Pancreatic Trypsin Inhibitor Retains the Average Native Conformation but Greatly Increases Local Flexibility",published,journal,Biochemistry,,41,7,,,,,,,,,,,,,,,,,,,,,,2237,2245,2002, citations,entry_citation,5172,218879,1,,entry citation,,21929523,11933230,,,"NMR Solution Structure, Backbone Mobility, and Homology Modeling of C-Type Cytochromes from Gram-positive Bacteria",published,journal,Chembiochem,,3,4,,,,,,,,,,,,,,,,,,,,,,299,310,2002, citations,entry_citation,5173,218905,1,,entry citation,,,14572630,,,"Solution structure of epiregulin and the effect of its C-terminal domain for receptor binding affinity",published,journal,FEBS Lett.,,553,3,,,,,,,,,,,,,,,,,,,,,,232,238,2003, citations,entry_citation,5174,218918,1,,entry citation,,22204429,12215502,,,"Molecular structure of the GARP family of plant Myb-related DNA binding motifs of the Arabidopsis response regulators",published,journal,Plant Cell,,14,9,,,,,,,,,,,,,,,,,,,,,,2015,2029,2002, citations,entry_citation,5175,218931,1,,entry citation,,21592567,11734001,,,"Solution NMR Structure of the Myosin Phosphatase Inhibitor Protein CPI-17 Shows Phosphorylation-induced Conformational Changes Responsible for Activation",published,journal,J. Mol. Biol.,,314,4,,,,,,,,,,,,,,,,,,,,,,839,849,2001, citations,entry_citation,5176,218945,1,,entry citation,,,11434766,,,"Solution structure of the squash trypsin inhibitor MCoTI-II. A new family for cyclic knottins.",published,journal,Biochemistry,,40,27,,,,,,,,,,,,,,,,,,,,,,7973,7983,2001, citations,entry_citation,5177,218963,1,,entry citation,,21880669,11885570,,,"Letter to the Editor: Backbone and Side-chain 1H, 15N, and 13C Assignments for Chick Cofilin",published,journal,J. Biomol. NMR,,22,2,,,,,,,,,,,,,,,,,,,,,,193,194,2002, citations,entry_citation,5262,220747,1,,entry citation,,21925710,11928808,,,"The Col-1 Module of Human Matrix Metalloproteinase-2 (MMP-2): Structural/Functional Relatedness between Gelatin-binding Fibronectin Type II Modules and Lysine-binding Kringle Domains",published,journal,Biol. Chem.,,383,1,,,,,,,,,,,,,,,,,,,,,,137,148,2002, citations,entry_citation,5263,220766,1,,entry citation,,,,,,"Letter to the Editor: Assignment of the 1H, 13C, and 15N resonances of the 22,5 kDa CBM28 module of the cellulase Cel5I of Clostridium cellulolyticum",published,journal,J. Biomol. NMR,,23,2,,,,,,,,,,,,,,,,,,,,,,157,158,2002, citations,entry_citation,5264,220779,1,,entry citation,,21864161,11741980,,,"The Solution Structures of the Human beta-Defensins lead to a Better Understanding of the Potent Bactericidal Activity of HBD3 against Staphylococcus aureus",published,journal,J. Biol. Chem.,,277,10,,,,,,,,,,,,,,,,,,,,,,8279,8289,2002, citations,Reference_1,5177,218964,2,,reference citation,,,1699599,,"Abe H, Endo T, Yamamoto K, Obinata T. Sequence of cDNAs encoding actin depolymerizing factor and cofilin of embryonic chicken skeletal muscle: two functionally distinct actin-regulatory proteins exhibit high structural homology. Biochemistry. 1990 Aug 14;29(32):7420-5.",Sequence of cDNAs encoding actin depolymerizing factor and cofilin of embryonic chicken skeletal muscle: two functionally distinct actin-regulatory proteins exhibit high structural homology.,published,journal,Biochemistry,Biochemistry,29,32,,0006-2960,,,,,,,,,,,,,,,,,,,,7420,7425,1990,"Two actin-regulatory proteins of 19 and 20 kDa are involved in the regulation of actin assembly in developing chicken skeletal muscle. They are homologous with actin depolymerizing factor (ADF) and cofilin, a pH-dependent actin-modulating protein, which were originally discovered in chicken and mammalian brain, respectively. In this study, full-length cDNA clones were isolated by screening a lambda gt11 cDNA library constructed from poly(A+) RNA of embryonic chicken skeletal muscle with the antibodies specific for each protein, and their complete sequences were determined. The chicken cofilin cDNA encoded a protein of 166 amino acids, the sequence of which had over 80% identity with that of porcine brain cofilin. The amino acid sequence of the ADF was 165 amino acids and showed about 70% identity with either chicken or mammalian cofilin, in spite of the fact that ADF and cofilin are functionally distinct. Like chicken and mammalian cofilin, ADF contained a sequence similar to the nuclear transport signal sequence of SV40 large T antigen. ADF and cofilin shared a hexapeptide identical with the amino-terminal sequence of tropomyosin as well as the regions homologous to other actin-regulatory proteins, including depactin, gelsolin, and profilin. The overall nucleotide sequences and Southern blot analysis of genomic DNA, however, indicated that the two proteins were derived from different genes." citations,Reference_2,5177,218965,3,,reference citation,,,8520220,,"Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR. 1995 Nov;6(3):277-93.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,Reference_3,5177,218966,4,,reference citation,,,,,"Bartels, C., Xia, T.-H., Billeter, M., Guntert, P., and Wuthrich, K. (1995) J. Biomol. NMR 5, 1-10.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5178,218997,1,,entry citation,,21638383,11600504,,,"Solution Structure of the Fibronectin type III Domain from Bacillus circulans WL-12 Chitinase A1",published,journal,J. Biol. Chem.,,277,2,,,,,,,,,,,,,,,,,,,,,,1388,1397,2002, citations,entry_citation,5179,219012,1,,entry citation,,21882787,11885979,,,"Solution Structure of N-terminal SH3 Domain of Vav and the Recognition Site for Grb2 C-terminal SH3 Domain",published,journal,J. Biomol. NMR,,22,1,,,,,,,,,,,,,,,,,,,,,,37,46,2002, citations,entry_citation,5180,219026,1,,entry citation,,,11316794,,,"Recruitment of the transcriptional machinery through GAL11P:structure and interactions of the GAL4 dimerization domain",published,journal,Genes Dev.,Genes & Development,15,8,,,,,,,,,,,,,,,,,,,,,,1007,1020,2001, citations,entry_citation,5181,219060,1,,entry citation,,21880666,11883782,,,"Letter to the Editor: Virtually Complete 1H, 13C and 15N Resonance Assignments of the Second Family 4 Xylan Binding Module of Rhodothermus marinus xylanase 10A",published,journal,J. Biomol. NMR,,22,2,,,,,,,,,,,,,,,,,,,,,,187,188,2002, citations,entry_citation,5182,219087,1,,entry citation,,21986773,11991359,,,"Letter to the Editor: Semi-automated Backbone Resonance Assignments of the Extracellular Ligand-binding Domain of an Ionotropic Glutamate Receptor",published,journal,J. Biomol. NMR,,22,3,,,,,,,,,,,,,,,,,,,,,,297,298,2002, citations,entry_citation,5183,219104,1,,entry citation,,22016650,12021452,,,"BetaCore, a Designed Water Soluble Four-stranded Antiparallel Beta-sheet Protein",published,journal,Protein Sci.,,11,6,,,,,,,,,,,,,,,,,,,,,,1539,1551,2002, citations,ref_1,5183,219105,2,,reference citation,,,10891073,,"Carulla, N.; Woodward, C.; Barany, G. Synthesis and Characterization of a b-Hairpin Peptide That Represents a 'Core Module' of Bovine Pancreatic Trypsin Inhibitor (BPTI). Biochemistry, 39, 7927-7937 (2000).",Synthesis and characterization of a beta-hairpin peptide that represents a 'core module' of bovine pancreatic trypsin inhibitor (BPTI).,published,journal,Biochemistry,Biochemistry,39,27,,0006-2960,,,,,,,,,,,,,,,,,,,,7927,7937,2000,"A new strategy for the design and construction of peptide fragments that can achieve defined, nativelike secondary structure is presented. The strategy is based upon the hypothesis that 'core elements' of a protein, synthesized in a single polypeptide molecule, will favor nativelike structure, and that by incorporating a cross-link, nativelike core structure will dominate the ensemble as the more extended conformations are excluded. 'Core elements' are the elements of packed secondary structure that contain the slowest exchanging backbone amide protons in the native protein. The 'core elements' in bovine pancreatic trypsin inhibitor (BPTI) are the two long strands of antiparallel beta-sheet (residues 18-24 and 29-35) and the small beta-bridge (residues 43-44). To test the design strategy, we synthesized an 'oxidized core module', which contains the antiparallel strands connected by a modified reverse turn (A27 replaced by D), a natural disulfide cross-link at the open end of the hairpin, and N- and C-termini blocking groups. A peptide with identical sequence but lacking the disulfide cross-link at the open end was used as the 'reduced core module' control. The conformational behavior of both peptides was examined using (1)H NMR spectroscopy. Chemical shift dispersion, chemical shift deviation from random coil values, sequential and long-range NOEs, and H/D amide exchange rates were compared for the two peptides. We conclude that the ensemble of oxidized and reduced core module conformations samples both nativelike 4:4 and non-native 3:5 beta-hairpin structure, and that the oxidized module samples nativelike structure for a greater fraction of the time than the reduced module." citations,ref_2,5183,219106,3,,reference citation,,,11562191,,"Carulla, N.; Woodward, C.; Barany, G. Toward New Designed Proteins Derived from Bovine Pancreatic Trypsin Inhibitor (BPTI): Covalent Cross-Linking of Two 'Core Modules' by Oxime-Forming Ligation. Bioconjugate Chemistry, 12, 726-741 (2001).",Toward new designed proteins derived from bovine pancreatic trypsin inhibitor (BPTI): covalent cross-linking of two 'core modules' by oxime-forming ligation.,published,journal,Bioconjug. Chem.,Bioconjugate chemistry,12,5,,1043-1802,,,,,,,,,,,,,,,,,,,,726,741,,"A 25-residue disulfide-cross-linked peptide, termed 'oxidized core module' (OxCM), that includes essentially all of the secondary structural elements of bovine pancreatic trypsin inhibitor (BPTI) most refractory to hydrogen exchange, was shown previously to favor nativelike beta-sheet structure [Carulla, N., Woodward, C., and Barany, G. (2000) Synthesis and Characterization of a beta-Hairpin Peptide That Represents a 'Core Module' of Bovine Pancreatic Trypsin Inhibitor (BPTI). Biochemistry 39, 7927-7937]. The present work prepares to explore the hypothesis that the energies of nativelike conformations, relative to other possible conformations, could be decreased further by covalent linkage of two OxCMs. Optimized syntheses of six approximately 50-residue OxCM dimers are reported herein, featuring appropriate monomer modifications followed by oxime-forming ligation chemistry to create covalent cross-links at various positions and with differing lengths. Several side reactions were recognized through this work, and modified procedures to lessen or mitigate their occurrence were developed. Particularly noteworthy, guanidine or urea denaturants that were included as peptide-solubilizing components for some reaction mixtures were proven to form adducts with glyoxylyl moieties, thus affecting rates and outcomes. All six synthetic OxCM dimers were characterized by 1D (1)H NMR; three of them showed considerable chemical shift dispersion suggestive of self-association and mutual stabilization between the monomer units." citations,entry_citation,5184,219131,1,,entry citation,,,,,,Inverse active site of scorpion toxin BeKm,in preparation,journal,Nat. Struct. Biol.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref-1,5184,219132,2,,reference citation,,,,,"Bartels C., Xia T.-H., Billeter M., Guntert P. & Wuthrich K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules, J. Biomol. NMR (1995) 6, 1-10.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref-2,5184,219133,3,,reference citation,,,9367762,,"Guntert P., Mumenthaler C. & Wuthrich K. Torsion angle dynamics for NMR structure calculation with new program DYANA, J. Mol. Biol. (1997) 273, 283-298.",Torsion angle dynamics for NMR structure calculation with the new program DYANA.,published,journal,J. Mol. Biol.,Journal of molecular biology,273,1,,0022-2836,,,,,,,,,,,,,,,,,,,,283,298,1997,"The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from distance constraints and torsion angle constraints collected by nuclear magnetic resonance (NMR) experiments performs simulated annealing by molecular dynamics in torsion angle space and uses a fast recursive algorithm to integrate the equations of motions. Torsion angle dynamics can be more efficient than molecular dynamics in Cartesian coordinate space because of the reduced number of degrees of freedom and the concomitant absence of high-frequency bond and angle vibrations, which allows for the use of longer time-steps and/or higher temperatures in the structure calculation. It also represents a significant advance over the variable target function method in torsion angle space with the REDAC strategy used by the predecessor program DIANA. DYANA computation times per accepted conformer in the ""bundle"" used to represent the NMR structure compare favorably with those of other presently available structure calculation algorithms, and are of the order of 160 seconds for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300 computer. Test calculations starting from conformers with random torsion angle values further showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures." citations,ref-3,5184,219134,4,,reference citation,,,,,"Schaumann T., Braun W. & Wuthrich K. (1990) The program FANTOM for energy refinement of polypeptides and proteins using a Newton-Raphson minimizer in torsion angle space, Biopolymers 29, 679-694.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref-4,5184,219135,5,,reference citation,,,8744573,,"Koradi R., Billiter M. & Wutrich, K (1996) MOLMOL: a program for display and analysis of macromolecular structures, J. Mol. Graphics 14, 51-55.",MOLMOL: a program for display and analysis of macromolecular structures.,published,journal,,Journal of molecular graphics,14,1,,0263-7855,,,,,,,,,,,,,,,,,,,,51,32,1996,"MOLMOL is a molecular graphics program for display, analysis, and manipulation of three-dimensional structures of biological macromolecules, with special emphasis on nuclear magnetic resonance (NMR) solution structures of proteins and nucleic acids. MOLMOL has a graphical user interface with menus, dialog boxes, and on-line help. The display possibilities include conventional presentation, as well as novel schematic drawings, with the option of combining different presentations in one view of a molecule. Covalent molecular structures can be modified by addition or removal of individual atoms and bonds, and three-dimensional structures can be manipulated by interactive rotation about individual bonds. Special efforts were made to allow for appropriate display and analysis of the sets of typically 20-40 conformers that are conventionally used to represent the result of an NMR structure determination, using functions for superimposing sets of conformers, calculation of root mean square distance (RMSD) values, identification of hydrogen bonds, checking and displaying violations of NMR constraints, and identification and listing of short distances between pairs of hydrogen atoms." citations,ref-5,5184,219136,6,,reference citation,,,11136720,,"Korolkova YV, Kozlov SA, Lipkin AV, Pluzhnikov KA, Hadley JK, Filippov AK, Brown DA, Angelo K, Strobaek D, Jespersen T, Olesen SP, Jensen BS, Grishin EV. An ERG channel inhibitor from the scorpion Buthus eupeus. J. Biol. Chem. 2001 Mar 30;276(13):9868-76",An ERG channel inhibitor from the scorpion Buthus eupeus.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,276,13,,0021-9258,,,,,,,,,,,,,,,,,,,,9868,9876,2001,"The isolation of the peptide inhibitor of M-type K(+) current, BeKm-1, from the venom of the Central Asian scorpion Buthus eupeus has been described previously (Fillipov A. K., Kozlov, S. A., Pluzhnikov, K. A., Grishin, E. V., and Brown, D. A. (1996) FEBS Lett. 384, 277-280). Here we report the cloning, expression, and selectivity of BeKm-1. A full-length cDNA of 365 nucleotides encoding the precursor of BeKm-1 was isolated using the rapid amplification of cDNA ends polymerase chain reaction technique from mRNA obtained from scorpion telsons. Sequence analysis of the cDNA revealed that the precursor contains a signal peptide of 21 amino acid residues. The mature toxin consists of 36 amino acid residues. BeKm-1 belongs to the family of scorpion venom potassium channel blockers and represents a new subgroup of these toxins. The recombinant BeKm-1 was produced as a Protein A fusion product in the periplasm of Escherichia coli. After cleavage and high performance liquid chromatography purification, recombinant BeKm-1 displayed the same properties as the native toxin. Three BeKm-1 mutants (R27K, F32K, and R27K/F32K) were generated, purified, and characterized. Recombinant wild-type BeKm-1 and the three mutants partly inhibited the native M-like current in NG108-15 at 100 nm. The effect of the recombinant BeKm-1 on different K(+) channels was also studied. BeKm-1 inhibited hERG1 channels with an IC(50) of 3.3 nm, but had no effect at 100 nm on hEAG, hSK1, rSK2, hIK, hBK, KCNQ1/KCNE1, KCNQ2/KCNQ3, KCNQ4 channels, and minimal effect on rELK1. Thus, BeKm-1 was shown to be a novel specific blocker of hERG1 potassium channels." citations,entry_citation,5185,219157,1,,entry citation,,21880667,11883783,,,"Letter to the Editor: 1H, 13C, and 15N Resonance Assignment of the Vascular Endothelial Growth Factor Receptor-binding Domain in Complex with a Receptor-blocking Peptide",published,journal,J. Biomol. NMR,,22,2,,,,,,,,,,,,,,,,,,,,,,189,190,2002, citations,entry_citation,5186,219173,1,,entry citation,,21880667,11883783,,,"1H, 13C, and 15N Resonance Assignment of the Vascular Endothelial Growth Factor Receptor-binding Domain in Complex with a Receptor-blocking Peptide",published,journal,J. Biomol. NMR,,22,2,,,,,,,,,,,,,,,,,,,,,,189,190,2002, citations,ref_1,5186,219174,2,,reference citation,,,9336848,,"Fairbrother WJ, Champe MA, Christinger HW, Keyt BA, Starovasnik MA. 1H, 13C, and 15N backbone assignment and secondary structure of the receptor-binding domain of vascular endothelial growth factor. Protein Sci. 1997 Oct;6(10):2250-60.","1H, 13C, and 15N backbone assignment and secondary structure of the receptor-binding domain of vascular endothelial growth factor.",published,journal,Protein Sci.,Protein science : a publication of the Protein Society,6,10,,0961-8368,,,,,,,,,,,,,,,,,,,,2250,2260,1997,"Nearly complete sequence-specific 1H, 13C, and 15N resonance assignments are reported for the backbone atoms of the receptor-binding domain of vascular endothelial growth factor (VEGF), a 23-kDa homodimeric protein that is a major regulator of both normal and pathological angiogenesis. The assignment strategy relied on the use of seven 3D triple-resonance experiments [HN(CO)CA, HNCA, HNCO, (HCA)CONH, HN(COCA)HA, HN(CA)HA, and CBCA-(CO)NH] and a 3D 15N-TOCSY-HSQC experiment recorded on a 0.5 mM (12 mg/mL) sample at 500 MHz, pH 7.0, 45 degrees C. Under these conditions, 15N relaxation data show that the protein has a rotational correlation time of 15.0 ns. Despite this unusually long correlation time, assignments were obtained for 94 of the 99 residues; 8 residues lack amide 1H and 15N assignments, presumably due to rapid exchange of the amide 1H with solvent under the experimental conditions used. The secondary structure of the protein was deduced from the chemical shift indices of the 1H alpha, 13C alpha, 13C beta, and 13CO nuclei, and from analysis of backbone NOEs observed in a 3D 15N-NOESY-HSQC spectrum. Two helices and a significant amount of beta-sheet structure were identified, in general agreement with the secondary structure found in a recently determined crystal structure of a similar VEGF construct [Muller YA et al., 1997, Proc Natl Acad Sci USA 94:7192-7197]." citations,entry_citation,5187,219189,1,,entry citation,,22147549,12153045,,,"Letter to the Editor: Complete 1H, 13C, and 15N assignments of the N-terminal DNA binding domain of the TraR protein",published,journal,J. Biomol. NMR,,23,2,,,,,,,,,,,,,,,,,,,,,,161,162,2002, citations,entry_citation,5188,219216,1,,entry citation,,22423982,12535689,,,"Solution Structure of Paralytic Peptide of Silkworm, Bombyx mori",published,journal,Peptides,,23,12,,,,,,,,,,,,,,,,,,,,,,2111,2116,2002, citations,entry_citation,5189,219231,1,,entry citation,,21880668,11883784,,,"Letter to the Editor: 1H, 15N and 13C Resonance Assignments of Rabbit Apo-S100A11",published,journal,J. Biomol. NMR,,22,2,,,,,,,,,,,,,,,,,,,,,,191,192,2002, citations,entry_citation,5265,220799,1,,entry citation,,,11997013,,,"Solution structure of moricin, an antibacterial peptide, isolated from the silkworm Bombyx mori",published,journal,FEBS Lett.,,518,,,,,,,,,,,,,,,,,,,,,,,33,38,2002, citations,reference_1,5189,219232,2,,reference citation,,,8520220,,"Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR. 1995 Nov;6(3):277-93.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,reference_2,5189,219233,3,,reference citation,,,,,"Garrett, D.S., Powers, R., Gronenborn, A.M. and Clore, G.M. (1991) J. Magn. Reson., 95, 214-220.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5190,219262,1,,entry citation,,21880670,11883785,,,"Letter to the Editor: Backbone NMR Assignments of Ribosome Recycling Factors from Escherichia coli and Thermotoga maritima",published,journal,J. Biomol. NMR,,22,2,,,,,,,,,,,,,,,,,,,,,,195,196,2002, citations,entry_citation,5191,219275,1,,entry citation,,21880670,11883785,,,"Letter to the Editor: Backbone NMR Assignments of Ribosome Recycling Factors from Escherichia coli and Thermotoga maritima",published,journal,J. Biomol. NMR,,22,2,,,,,,,,,,,,,,,,,,,,,,195,196,2002, citations,entry_citation,5192,219288,1,,entry citation,,,12023801,,,"Letter to the Editor: The NMR-derived Conformation of Neuropeptide F from Moniezia expansa",published,journal,J. Biomol. Struct. Dyn.,,19,6,,,,,,,,,,,,,,,,,,,,,,991,998,2002, citations,entry_citation,5193,219303,1,,entry citation,,21535551,11680852,,,"A mutant viral RNA promoter with an altered conformation retains efficient recognition by a viral RNA replicase through a solution-exposed adenine.",published,journal,RNA,,7,10,,,,,,,,,,,,,,,,,,,,,,1476,1485,2001, citations,entry_citation,5194,219325,1,,entry citation,,21630172,11754837,,,"Three-dimensional Structure of the Synaptotagmin 1 C2B-domain: Synaptotagmin 1 as a Phospholipid Binding Machine",published,journal,Neuron,,32,6,,,,,,,,,,,,,,,,,,,,,,1057,1069,2001, citations,entry_citation,5196,219351,1,,entry citation,,22478819,12429019,,,"The Three-dimensional Structural Surface of Two Beta-sheet Scorpion Toxins Mimics that of an Alpha-Helical Dihydropyridine Receptor Segment",published,journal,Biochem. J.,,370,2,,,,,,,,,,,,,,,,,,,,,,517,527,2003, citations,entry_citation,5197,219366,1,,entry citation,,,10397798,,,"Helix protensity of a polypeptide containing helix 1 of the mouse prion protein studied by NMR and CD spectroscopy",published,journal,Biopolymers,,51,2,,,,,,,,,,,,,,,,,,,,,,145,152,1999, citations,entry_citation,5198,219390,1,,entry citation,,21856773,11866530,,,"Solution Structure of a Phage-derived Peptide Antagonist in Complex with Vascular Endothelial Growth Factor",published,journal,J. Mol. Biol.,,316,3,,,,,,,,,,,,,,,,,,,,,,769,787,2002, citations,entry_citation,5199,219405,1,,entry citation,,,,,,"Solution structure of the fungal plant disease resistance-triggering protein NIP1 shows a novel b sheet fold",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5200,219433,1,,entry citation,,22322782,12435387,,,"Determination of the Secondary Structure in Solution of the Escherichia coli DnaA DNA-binding Domain",published,journal,Biochem. Biophys. Res. Commun.,,299,1,,,,,,,,,,,,,,,,,,,,,,42,48,2002, citations,entry_citation,5201,219448,1,,entry citation,,21895760,11748219,,,"Selection and Structure of Ion-selective Ligands for Platelet Integrin Alpha IIbbeta3",published,journal,J. Biol. Chem.,,277,12,,,,,,,,,,,,,,,,,,,,,,10298,10305,2002, citations,entry_citation,5202,219467,1,,entry citation,,21882796,11885989,,,"Letter to the Editor: Assignment of the 1H, 13C and 15N Resonances of the Catalytic Domain of the Rat 2',3'-cyclic Nucleotide 3'-phosphodiesterase",published,journal,J. Biomol. NMR,,22,1,,,,,,,,,,,,,,,,,,,,,,99,100,2002, citations,entry_citation,5203,219493,1,,entry citation,,21646529,11786023,,,"Solution Structure and Functional Analysis of the Cysteine-rich C1 Domain of Kinase Suppressor of Ras (KSR)",published,journal,J. Mol. Biol.,,315,3,,,,,,,,,,,,,,,,,,,,,,435,446,2002, citations,entry_citation,5204,219517,1,,entry citation,,,12270713,,,NMR Structures of 36 and 73-residue Fragments of the Calreticulin P-domain,published,journal,J. Mol. Biol.,,322,4,,,,,,,,,,,,,,,,,,,,,,773,784,2002, citations,entry_citation,5205,219538,1,,entry citation,,,12270713,,,NMR Structures of 36 and 73-residue Fragments of the Calreticulin P-domain,published,journal,J. Mol. Biol.,,322,4,,,,,,,,,,,,,,,,,,,,,,773,784,2002, citations,entry_citation,5206,219558,1,,entry citation,,,9519411,,,"A novel calcium-sensitive switch revealed by the structure of human S100B in the calcium-bound form",published,journal,Structure,,6,2,,,,,,,,,,,,,,,,,,,,,,211,222,1998, citations,entry_citation,5207,219584,1,,entry citation,,21651052,11790829,,,The EF-hand Domain: A Globally Cooperative Structural unit,published,journal,Protein Sci.,,11,2,,,,,,,,,,,,,,,,,,,,,,198,205,2002, citations,ref-1,5207,219585,2,,reference citation,,,1841711,,"Guntert P, Wuthrich K. Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints. J Biomol NMR. 1991 Nov;1(4):447-56.",Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,1,4,,0925-2738,,,,,,,,,,,,,,,,,,,,447,456,1991,"A new strategy for NMR structure calculations of proteins with the variable target function method (Braun, W. and Go, N. (1985) J. Mol. Biol., 186, 611) is described, which makes use of redundant dihedral angle constraints (REDAC) derived from preliminary calculations of the complete structure. The REDAC approach reduces the computation time for obtaining a group of acceptable conformers with the program DIANA 5-100-fold, depending on the complexity of the protein structure, and retains good sampling of conformation space." citations,entry_citation,5266,220817,1,,entry citation,,22056595,12061723,,,"Letter to the Editor: 1H, 15N and 13C Assignments of the Targeting (FAT) Domain of Focal Adhesion Kinase",published,journal,J. Biomol. NMR,,23,1,,,,,,,,,,,,,,,,,,,,,,75,76,2002, citations,entry_citation,5267,220844,1,,entry citation,,22056594,12061722,,,"Letter to the Editor: 1H, 13C, 15N NMR sequence-specific resonance assignment of a Clostridium thermocellum type II cohesin module",published,journal,J. Biomol. NMR,,23,1,,,,,,,,,,,,,,,,,,,,,,73,74,2002, citations,ref-2,5207,219586,3,,reference citation,,,1847217,,"Guntert P, Braun W, Wuthrich K. Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA. J Mol Biol. 1991 Feb 5;217(3):517-30.","Efficient computation of three-dimensional protein structures in solution from nuclear magnetic resonance data using the program DIANA and the supporting programs CALIBA, HABAS and GLOMSA.",published,journal,J. Mol. Biol.,Journal of molecular biology,217,3,,0022-2836,,,,,,,,,,,,,,,,,,,,517,530,1991,"A novel procedure for efficient computation of three-dimensional protein structures from nuclear magnetic resonance (n.m.r.) data in solution is described, which is based on using the program DIANA in combination with the supporting programs CALIBA, HABAS and GLOMSA. The first part of this paper describes the new programs DIANA. CALIBA and GLOMSA. DIANA is a new, fully vectorized implementation of the variable target function algorithm for the computation of protein structures from n.m.r. data. Its main advantages, when compared to previously available programs using the variable target function algorithm, are a significant reduction of the computation time, and a novel treatment of experimental distance constraints involving diastereotopic groups of hydrogen atoms that were not individually assigned. CALIBA converts the measured nuclear Overhauser effects into upper distance limits and thus prepares the input for the previously described program HABAS and for DIANA. GLOMSA is used for obtaining individual assignments for pairs of diastereotopic substituents by comparison of the experimental constraints with preliminary results of the structure calculations. With its general outlay, the presently used combination of the four programs is particularly user-friendly. In the second part of the paper, initial results are presented on the influence of the novel DIANA treatment of diastereotopic protons on the quality of the structures obtained, and a systematic study of the central processing unit times needed for the same protein structure calculation on a range of different, commonly available computers is described." citations,ref-3,5207,219587,4,,reference citation,,,,,"G. Gippert. New computational methods for 3D NMR analysis and protein structure determination in high-dimensional internal coordinate space. Ph.D Thesis, The Scripps Research Institute, 1995.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5208,219608,1,,entry citation,,21880671,11883786,,,"Letter to the Editor: 1H, 13C and 15N Resonance Assignments for the Perdeuterated 22 kD Palm-thumb Domain of DNA Polymerase Beta",published,journal,J. Biomol. NMR,,22,2,,,,,,,,,,,,,,,,,,,,,,197,198,2002, citations,entry_citation,5209,219633,1,,entry citation,,,12467578,,,Mapping of the interaction interface of DNA polymerase beta with XRCC1,published,journal,Structure,,10,12,,,,,,,,,,,,,,,,,,,,,,1709,1720,2002, citations,entry_citation,5210,219657,1,,entry citation,,,11768384,,,"The Solution Structure of the Viral-Binding Domain of Tva, the Cellular Receptor for Subgroup A Avian Leukosis and Sarcoma Virus",published,journal,FEBS Lett.,,509,2,,,,,,,,,,,,,,,,,,,,,,161,168,2001, citations,entry_citation,5211,219678,1,,entry citation,,21681399,11823424,,,"A ""three-pronged"" Binding Mechanism for the SAP/SH2D1A SH2 Domain: Structural Basis and Relevance to the XLP Syndrome",published,journal,EMBO J.,,21,3,,,,,,,,,,,,,,,,,,,,,,314,323,2002, citations,entry_citation,5212,219699,1,,entry citation,,21681399,11823424,,,"A ""three-pronged"" Binding Mechanism for the SAP/SH2D1A SH2 Domain: Structural Basis and Relevance to the XLP Syndrome",published,journal,EMBO J.,EMBO Journal,21,3,,,,,,,,,,,,,,,,,,,,,,314,323,2002, citations,entry_citation,5213,219723,1,,entry citation,,21614397,11747441,,,Copper Trafficking: The Solution Structure of Bacillus subtilis CopZ,published,journal,Biochemistry,,40,51,,,,,,,,,,,,,,,,,,,,,,15660,15668,2001, citations,entry_citation,5214,219745,1,,entry citation,,,,,,"Stabilization of the helical structural of Y2-selective analogues of neuropeptide Y by lactam bridges",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5215,219771,1,,entry citation,,22010296,12014969,,,"Stabilization of the Helical Structure of Y2-selective Analogues of Neuropeptide Y by Lactam Bridges",published,journal,J. Med. Chem.,,45,11,,,,,,,,,,,,,,,,,,,,,,2310,2318,2002, citations,entry_citation,5216,219792,1,,entry citation,,22010296,12014969,,,"Stabilization of the Helical Structure of Y2-selective Analogues of Neuropeptide Y by Lactam Bridges",published,journal,J. Med. Chem.,,45,11,,,,,,,,,,,,,,,,,,,,,,2310,2318,2002, citations,entry_citation,5217,219813,1,,entry citation,,22313337,12426397,,,"Solution Structure and DNA-binding Properties of the C-Terminal Domain of UvrC from E. coli",published,journal,EMBO J.,,21,22,,,,,,,,,,,,,,,,,,,,,,6257,6266,2002, citations,entry_citation,5218,219833,1,,entry citation,,22012546,12018484,,,"Letter to the Editor: backbone 1H, 13C, 15N resonance assignments of the N-terminal 24 kDa fragment of the gyrase B subunit from E. coli",published,journal,J. Biomol. NMR,,22,4,,,,,,,,,,,,,,,,,,,,,,369,370,2002, citations,ref_1,5218,219834,2,,reference citation,,,8589602,,"Wishart D.S., Bigam C.G., Yao J., Abildgaard F., Dyson H.J., Oldfield E., Markley J.L., Sykes B.D., ""1H, 13C and 15N Chemical Shift Referencing in Biomolecular NMR,"" J. Biomol. NMR, 6, 135-40 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,5219,219849,1,,entry citation,,21986775,11991361,,,"Letter to the Editor: Base excision repair: NMR backbone assignments of Escherichia coli formamidopyrimidine-DNA glycosylase",published,journal,J. Biomol. NMR,,22,3,,,,,,,,,,,,,,,,,,,,,,301,302,2002, citations,entry_citation,5220,219875,1,,entry citation,,21986766,,,,Solution Structure and Dynamics of Melanoma Inhibitory Activity Protein,published,journal,J. Biomol. NMR,,22,3,,,,,,,,,,,,,,,,,,,,,,211,223,2002, citations,entry_citation,5221,219893,1,,entry citation,,22012548,12018486,,,"Letter to the Editor: Backbone 1H, 13C, and 15N resonance assignments for the C-Terminal Region of Ku86 (Ku86CTR)",published,journal,J. Biomol. NMR,,22,4,,,,,,,,,,,,,,,,,,,,,,373,374,2002, citations,entry_citation,5222,219921,1,,entry citation,,22012549,12018487,,,"Letter to the Editor: 1H, 15N and 13C resonance assignments and secondary structure of Tryparedoxin-I from Crithidia fasciculata",published,journal,J. Biomol. NMR,,22,4,,,,,,,,,,,,,,,,,,,,,,375,376,2002, citations,entry_citation,5223,219937,1,,entry citation,,21952327,11955060,,,"Structural Investigation of the Binding of a Herpesviral Protein to the SH3 Domain of Tyrosine Kinase Lck",published,journal,Biochemistry,,41,16,,,,,,,,,,,,,,,,,,,,,,5120,5130,2002, citations,entry_citation,5224,219965,1,,entry citation,,22012547,12018485,,,"Letter to the Editor: 1H, 13C and 15N resonance assignments of the C-terminal domain of human lamin A/C",published,journal,J. Biomol. NMR,,22,4,,,,,,,,,,,,,,,,,,,,,,371,372,2002, citations,entry_citation,5225,219990,1,,entry citation,,,,,,"Solution Structure of the Peptidyl-Prolyl-cis/trans-Isomerase Parvulin 10 of Escherichia coli",in preparation,journal,J. Mol. Biol.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5226,220025,1,,entry citation,,22012554,12018492,,,"Letter to the Editor: 1H, 15N and 13C resonance assignments and secondary structure of the Ssh10b from Hyperthermphilic Archaeon Sulfolobus shibatae",published,journal,J. Biomol. NMR,,22,4,,,,,,,,,,,,,,,,,,,,,,385,386,2002, citations,ref_1,5226,220026,2,,reference citation,,,10869069,,"Xue H, Guo R, Wen Y, Liu D, Huang L. An abundant DNA binding protein from the hyperthermophilic archaeon Sulfolobus shibatae affects DNA supercoiling in a temperature-dependent fashion. J Bacteriol. 2000 Jul;182(14):3929-33.",An abundant DNA binding protein from the hyperthermophilic archaeon Sulfolobus shibatae affects DNA supercoiling in a temperature-dependent fashion.,published,journal,J. Bacteriol.,Journal of bacteriology,182,14,,0021-9193,,,,,,,,,,,,,,,,,,,,3929,3933,2000,"The DNA binding protein Ssh10b, a member of the Sac10b family, has been purified from the hyperthermophilic archaeon Sulfolobus shibatae. Ssh10b constitutes about 4% of the cellular protein. Electrophoretic mobility shift assays showed that Ssh10b first bound a double-stranded DNA fragment with an estimated binding size of approximately approximately 12 bp, forming distinct shifts, until the DNA was coated with the protein. Binding of more Ssh10b resulted in the formation of smears of lower mobilities. The migration pattern of the smearing Ssh10b-DNA complexes was affected by temperature, whereas that of complexes associated with the distinct shifts was not. Interestingly, Ssh10b was capable of constraining negative DNA supercoils in a temperature-dependent fashion. While the ability of the protein to constrain supercoils was weak at 25 degrees C, it was enhanced substantially at 45 degrees C or higher temperatures (up to 80 degrees C). Taken together, our data suggest that archaeal proteins of the Sac10b family may affect the topology of chromosomal DNA in thermophilic archaea at their growth temperatures." citations,entry_citation,5227,220053,1,,entry citation,,21840684,11851407,,,Dissection of the Pathway of Molecular Recognition by Calmodulin,published,journal,Biochemistry,,41,8,,,,,,,,,,,,,,,,,,,,,,2599,2608,2002, citations,entry_citation,5228,220078,1,,entry citation,,22012550,12018488,,,"Letter to the Editor: Assignment of a 15 kDa protein complex formed between the p160 coactivator ACTR and the CREB binding protein",published,journal,J. Biomol. NMR,,22,4,,,,,,,,,,,,,,,,,,,,,,377,378,2002, citations,entry_citation,5231,220119,1,,entry citation,,,19888686,,,Resonance assignments for stromelysin complexed with a beta-sulfonyl hydroxamate inhibitor,published,journal,Biomol. NMR Assignments,,3,2,,,,,,,,,,,,,,,,,,,,,,183,186,2009, citations,ref_1,5231,220120,2,,reference citation,,,8520220,,"Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR. 1995 Nov;6(3):277-93.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref_2,5231,220121,3,,reference citation,,,11462827,,"Moseley HN, Monleon D, Montelione GT. Automatic determination of protein backbone resonance assignments from triple resonance nuclear magnetic resonance data. Methods Enzymol. 2001;339:91-108.",Automatic determination of protein backbone resonance assignments from triple resonance nuclear magnetic resonance data.,published,journal,Meth. Enzymol.,Methods in enzymology,339,,,0076-6879,,,,,,,,,,,,,,,,,,,,91,108,2001, citations,entry_citation,5232,220149,1,,entry citation,,22012551,12018489,,,"Letter to the Editor: 1H, 13C, and 15N resonance assignments of the DNA-binding domain of the essential protein Cdc13 complexed with single-stranded telomeric DNA",published,journal,J. Biomol. NMR,,22,4,,,,,,,,,,,,,,,,,,,,,,379,380,2002, citations,entry_citation,5233,220189,1,,entry citation,,,,,,"Letter to the Editor: NMR assignment of human ASC2, a self contained protein interaction domain involved in apoptosis and inflammation",published,journal,J. Biomol. NMR,,23,2,,,,,,,,,,,,,,,,,,,,,,151,152,2002, citations,entry_citation,5234,220205,1,,entry citation,,22012552,12018490,,,"Letter to the Editor: Backbone resonance assignment of the 2H, 13C, 15N labelled 32kDa Central Domain of Escherichia coli TyrR",published,journal,J. Biomol. NMR,,22,4,,,,,,,,,,,,,,,,,,,,,,381,382,2002, citations,entry_citation,5235,220226,1,,entry citation,,22012555,12018493,,,"Letter to the Editor: Resonance assignment and secondary structure determination of a C-terminal fragment of the Lupus Autoantigen (La) protein containing a putative RNA recognition motif (RRM)",published,journal,J. Biomol. NMR,,22,4,,,,,,,,,,,,,,,,,,,,,,387,388,2002, citations,entry_citation,5236,220240,1,,entry citation,,,12590144,,,"Solution Structure and Function of the ""Tandem Inactivation Domain"" of the Neuronal A-type Potassium Channel Kv1.4.",published,journal,J. Biol. Chem.,,278,,,,,,,,,,,,,,,,,,,,,,,16142,16150,2003, citations,entry_citation,5237,220258,1,,entry citation,,,14503865,,,"NMR studies of the interaction of a type II dihydrofolate reductase with pyridine nucleotides reveal unexpected phosphatase and reductase activity",published,journal,Biochemistry,,42,38,,,,,,,,,,,,,,,,,,,,,,11150,11160,2003, citations,entry_citation,5268,220871,1,,entry citation,,22075127,11959852,,,Structure of the Antimicrobial Peptide Tachystatin A,published,journal,J. Biol. Chem.,,277,26,,,,,,,,,,,,,,,,,,,,,,23651,23657,2002, citations,entry_citation,5269,220887,1,,entry citation,,22056593,12061721,,,"Letter to the Editor: Assignment of the 1H, 13C, and 15N signals of Synechocystis sp. PCC 6803 methemoglobin",published,journal,J. Biomol. NMR,,23,1,,,,,,,,,,,,,,,,,,,,,,71,72,2002, citations,entry_citation,5270,220911,1,,entry citation,,22147548,12153044,,,"Letter to the Editor: Backbone 1H, 15N and 13C Resonance Assignments of YqgF, an Escherichia coli Protein of unknown Structure and Function",published,journal,J. Biomol. NMR,,23,2,,,,,,,,,,,,,,,,,,,,,,159,160,2002, citations,entry_citation,5271,220933,1,,entry citation,,,12237467,,,"Zinc substituted Desulfovibrio gigas desulforedoxin: resolving subunit degeneracy with non-symmetric pseudocontact shifts",published,journal,Protein Sci.,,11,10,,,,,,,,,,,,,,,,,,,,,,2464,2470,2002, citations,unlabeled_citation,5272,220959,1,,entry citation,,,11856311,,,"Comparative structure analysis of proteinase inhibitors from the desert locust, Schistocerca gregaria",published,journal,Eur. J. Biochem.,,269,2,,,,,,,,,,,,,,,,,,,,,,527,537,2002, citations,ref-1,5237,220259,2,,reference citation,,,8520220,,"Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR. 1995 Nov;6(3):277-93.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref-2,5237,220260,3,,reference citation,,,,,"Johnson, B. A. and Blevins, R. A. (1994) J. Biomol. NMR, 4, 603-614.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5238,220282,1,,entry citation,,,9634701,,,"Solution structure of the heparin-binding domain of vascular endothelial growth factor",published,journal,Structure,,6,5,,,,,,,,,,,,,,,,,,,,,,637,649,1998, citations,entry_citation,5239,220297,1,,entry citation,,22056592,12061720,,,"Letter to the Editor: Sequential NMR Assignment of the Ferri-cytochrome c3 from Desulfovibrio vulgaris Hildenborough",published,journal,J. Biomol. NMR,,23,1,,,,,,,,,,,,,,,,,,,,,,69,70,2002, citations,entry_citation,5240,220313,1,,entry citation,,,15147188,,,"Solution structure and backbone dynamics of the K18G/R82E Alicyclobacillus acidocaldarius thioredoxin mutant: a molecular analysis of its reduced thermal stability.",published,journal,Biochemistry,,43,20,,,,,,,,,,,,,,,,,,,,,,6043,6058,2004, citations,ref_1,5240,220314,2,,reference citation,,,11391017,,"Pedone E, Saviano M, Rossi M, Bartolucci S. A single point mutation (Glu85Arg) increases the stability of the thioredoxin from Escherichia coli. Protein Eng. 2001 Apr;14(4):255-60.",A single point mutation (Glu85Arg) increases the stability of the thioredoxin from Escherichia coli.,published,journal,Protein Eng.,Protein engineering,14,4,,0269-2139,,,,,,,,,,,,,,,,,,,,255,260,2001,"Glu85 in the Escherichia coli thioredoxin, which is localized in the loop between beta4 and beta5, was substituted with the Arg present in the corresponding position in Bacillus acidocaldarius thioredoxin. This suggested that it could play an important role in the structure and thermostability of this protein owing to its involvement in numerous interactions. The effects of the mutation on the biophysical properties were analysed by circular dichroism, spectrofluorimetry and limited proteolysis, supported by molecular dynamics data. As modelling predicted, an increase in stability for E85R due to additional H-bonds between the beta5 and alpha4 regions was observed." citations,ref_2,5240,220315,3,,reference citation,,,10632710,,"Nicastro G, De Chiara C, Pedone E, Tato M, Rossi M, Bartolucci S. NMR solution structure of a novel thioredoxin from Bacillus acidocaldarius possible determinants of protein stability. Eur J Biochem. 2000 Jan;267(2):403-13.",NMR solution structure of a novel thioredoxin from Bacillus acidocaldarius possible determinants of protein stability.,published,journal,Eur. J. Biochem.,European journal of biochemistry / FEBS,267,2,,0014-2956,,,,,,,,,,,,,,,,,,,,403,413,2000,"The thioredoxin (Trx) from Bacillus acidocaldarius (BacTrx), an eubacterium growing optimally at 333 K, is the first Trx described to date from a moderate thermophilic source. To understand the molecular basis of its thermostability, the three-dimensional structure in the oxidized form was determined by NMR methods. A total of 2276 1H-NMR derived distance constraints along with 23 hydrogen-bonds, 72 phi and 27 chi1 torsion angle restraints, were used in a protocol employing simulated annealing followed by restrained molecular dynamics and restrained energy minimization. BacTrx consists of a well-defined core region of five strands of beta-sheet, surrounded by four exposed alpha-helices, features shared by other members of the thioredoxin family. The BacTrx 3D structure was compared with the Escherichia coli Trx (EcTrx) determined by X-ray crystallographic diffraction, and a number of structural differences were observed that may contribute to its thermostabilty. The results of structural analysis indicated that protein stability is due to cumulative effects, the main factor being an increased number of ionic interactions cross-linking different secondary structural elements and clamping the C-terminal alpha-helix to the core of the protein." citations,ref_3,5240,220316,4,,reference citation,,,9359865,,"Bartolucci S, Guagliardi A, Pedone E, De Pascale D, Cannio R, Camardella L, Rossi M, Nicastro G, de Chiara C, Facci P, Mascetti G, Nicolini C. Thioredoxin from Bacillus acidocaldarius: characterization, high-level expression in Escherichia coli and molecular modelling. Biochem J. 1997 Nov 15;328 ( Pt 1):277-85.","Thioredoxin from Bacillus acidocaldarius: characterization, high-level expression in Escherichia coli and molecular modelling.",published,journal,Biochem. J.,The Biochemical journal,328 ( Pt 1),,,0264-6021,,,,,,,,,,,,,,,,,,,,277,285,1997,"The thioredoxin (Trx) from Bacillus acidocaldarius (BacTrx) was purified to homogeneity by anion-exchange chromatography and gel-filtration chromatography, based on its ability to catalyse the dithiothreitol-dependent reduction of bovine insulin disulphides. The protein has a molecular mass of 11577 Da, determined by electrospray mass spectrometry, a pI of 4.2, and its primary structure was obtained by automated Edman degradation after cleavage with trypsin and cyanogen bromide. The sequences of known bacterial Trxs were aligned at the active site: BacTrx has an identity ranging from 45 to 53% with all sequences except that of the unusual Anabaena strain 7120 Trx (37% identity). The gene coding for BacTrx was isolated by a strategy based on PCR gene amplification and cloned in a plasmid downstream of a lac-derived promoter sequence; the recombinant clone was used as the expression vector for Escherichia coli. The expression was optimized by varying both the time of cell growth and the time of exposure to the inducer isopropyl beta-d-thiogalactoside; expressed BacTrx represents approx. 5% of the total cytosolic protein. CD spectra and differential scanning calorimetry measurements demonstrated that BacTrx is endowed with a higher conformational heat stability than the Trx from E. coli. Nanogravimetry experiments showed a lower content of bound water in BacTrx than in E. coli Trx, and a transition temperature approx. 10 degrees C higher for BacTrx. The three-dimensional model of the oxidized form of BacTrx was constructed by a comparative molecular modelling technique, using E. coli Trx and Anabaena strain 7120 Trx as reference proteins. Increased networks of ion-pairs and shorter loops emerged as major features of the BacTrx structure compared with those of the template proteins. The findings are discussed in the light of the current knowledge about molecular determinants of protein stability." citations,entry_citation,5241,220341,1,,entry citation,,,15147188,,,"Solution structure and backbone dynamics of the K18G/R82E Alicyclobacillus acidocaldarius thioredoxin mutant: a molecular analysis of its reduced thermal stability.",submitted,journal,Biochemistry,,43,20,,,,,,,,,,,,,,,,,,,,,,6043,6058,2004, citations,ref_1,5241,220342,2,,reference citation,,,11391017,,"Pedone E, Saviano M, Rossi M, Bartolucci S. A single point mutation (Glu85Arg) increases the stability of the thioredoxin from Escherichia coli. Protein Eng. 2001 Apr;14(4):255-60.",A single point mutation (Glu85Arg) increases the stability of the thioredoxin from Escherichia coli.,published,journal,Protein Eng.,Protein engineering,14,4,,0269-2139,,,,,,,,,,,,,,,,,,,,255,260,2001,"Glu85 in the Escherichia coli thioredoxin, which is localized in the loop between beta4 and beta5, was substituted with the Arg present in the corresponding position in Bacillus acidocaldarius thioredoxin. This suggested that it could play an important role in the structure and thermostability of this protein owing to its involvement in numerous interactions. The effects of the mutation on the biophysical properties were analysed by circular dichroism, spectrofluorimetry and limited proteolysis, supported by molecular dynamics data. As modelling predicted, an increase in stability for E85R due to additional H-bonds between the beta5 and alpha4 regions was observed." citations,entry_citation,5557,227155,1,,entry citation,,22269916,12357033,,,Solution Structure and Dynamics of the Outer Membrane Enzyme PagP by NMR,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,99,21,,,,,,,,,,,,,,,,,,,,,,13560,13565,2002, citations,ref_2,5241,220343,3,,reference citation,,,10632710,,"Nicastro G, De Chiara C, Pedone E, Tato M, Rossi M, Bartolucci S. NMR solution structure of a novel thioredoxin from Bacillus acidocaldarius possible determinants of protein stability. Eur J Biochem. 2000 Jan;267(2):403-13.",NMR solution structure of a novel thioredoxin from Bacillus acidocaldarius possible determinants of protein stability.,published,journal,Eur. J. Biochem.,European journal of biochemistry / FEBS,267,2,,0014-2956,,,,,,,,,,,,,,,,,,,,403,413,2000,"The thioredoxin (Trx) from Bacillus acidocaldarius (BacTrx), an eubacterium growing optimally at 333 K, is the first Trx described to date from a moderate thermophilic source. To understand the molecular basis of its thermostability, the three-dimensional structure in the oxidized form was determined by NMR methods. A total of 2276 1H-NMR derived distance constraints along with 23 hydrogen-bonds, 72 phi and 27 chi1 torsion angle restraints, were used in a protocol employing simulated annealing followed by restrained molecular dynamics and restrained energy minimization. BacTrx consists of a well-defined core region of five strands of beta-sheet, surrounded by four exposed alpha-helices, features shared by other members of the thioredoxin family. The BacTrx 3D structure was compared with the Escherichia coli Trx (EcTrx) determined by X-ray crystallographic diffraction, and a number of structural differences were observed that may contribute to its thermostabilty. The results of structural analysis indicated that protein stability is due to cumulative effects, the main factor being an increased number of ionic interactions cross-linking different secondary structural elements and clamping the C-terminal alpha-helix to the core of the protein." citations,ref_3,5241,220344,4,,reference citation,,,9359865,,"Bartolucci S, Guagliardi A, Pedone E, De Pascale D, Cannio R, Camardella L, Rossi M, Nicastro G, de Chiara C, Facci P, Mascetti G, Nicolini C. Thioredoxin from Bacillus acidocaldarius: characterization, high-level expression in Escherichia coli and molecular modelling. Biochem J. 1997 Nov 15;328 ( Pt 1):277-85.","Thioredoxin from Bacillus acidocaldarius: characterization, high-level expression in Escherichia coli and molecular modelling.",published,journal,Biochem. J.,The Biochemical journal,328 ( Pt 1),,,0264-6021,,,,,,,,,,,,,,,,,,,,277,285,1997,"The thioredoxin (Trx) from Bacillus acidocaldarius (BacTrx) was purified to homogeneity by anion-exchange chromatography and gel-filtration chromatography, based on its ability to catalyse the dithiothreitol-dependent reduction of bovine insulin disulphides. The protein has a molecular mass of 11577 Da, determined by electrospray mass spectrometry, a pI of 4.2, and its primary structure was obtained by automated Edman degradation after cleavage with trypsin and cyanogen bromide. The sequences of known bacterial Trxs were aligned at the active site: BacTrx has an identity ranging from 45 to 53% with all sequences except that of the unusual Anabaena strain 7120 Trx (37% identity). The gene coding for BacTrx was isolated by a strategy based on PCR gene amplification and cloned in a plasmid downstream of a lac-derived promoter sequence; the recombinant clone was used as the expression vector for Escherichia coli. The expression was optimized by varying both the time of cell growth and the time of exposure to the inducer isopropyl beta-d-thiogalactoside; expressed BacTrx represents approx. 5% of the total cytosolic protein. CD spectra and differential scanning calorimetry measurements demonstrated that BacTrx is endowed with a higher conformational heat stability than the Trx from E. coli. Nanogravimetry experiments showed a lower content of bound water in BacTrx than in E. coli Trx, and a transition temperature approx. 10 degrees C higher for BacTrx. The three-dimensional model of the oxidized form of BacTrx was constructed by a comparative molecular modelling technique, using E. coli Trx and Anabaena strain 7120 Trx as reference proteins. Increased networks of ion-pairs and shorter loops emerged as major features of the BacTrx structure compared with those of the template proteins. The findings are discussed in the light of the current knowledge about molecular determinants of protein stability." citations,entry_citation,5242,220369,1,,entry citation,,22090785,12095256,,,Solution Structure of the Pro-hormone Convertase 1 Pro-domain From Mus musculus,published,journal,J. Mol. Biol.,,320,4,,,,,,,,,,,,,,,,,,,,,,801,812,2002, citations,entry_citation,5243,220388,1,,entry citation,,21952362,11955617,,,1H NMR Study of a 17-mer DNA Duplex,published,journal,Biochim. Biophys. Acta,,1574,1,,,,,,,,,,,,,,,,,,,,,,93,99,2002, citations,entry_citation,5244,220405,1,,entry citation,,22012553,12018491,,,"Letter to the Editor: Backbone Assignments for Endonuclease V from Bacteriophage T4 with deuterium labeling",published,journal,J. Biomol. NMR,,22,4,,,,,,,,,,,,,,,,,,,,,,383,384,2002, citations,entry_citation,5245,220434,1,,entry citation,,,11790104,,,"Structure of hybrid backbone methylphosphonate DNA heteroduplexes: effect of R and S stereochemistry.",published,journal,Biochemistry,,41,3,,,,,,,,,,,,,,,,,,,,,,827,838,2002, citations,ref_1,5245,220435,2,,reference citation,,,1821645,,"Ferguson DM, Kollman PA. Application of free-energy decomposition to determine the relative stability of R and S oligodeoxyribonucleotide methylphosphonates. Antisense Res Dev. 1991 Fall;1(3):243-54.",Application of free-energy decomposition to determine the relative stability of R and S oligodeoxyribonucleotide methylphosphonates.,published,journal,Antisense Res. Dev.,Antisense research and development,1,3,,1050-5261,,,,,,,,,,,,,,,,,,,,243,254,1991,"The stereoselective stability of oligodeoxyribonucleotide methylphosphonates is examined using free-energy computer simulations. These modified phosphate linkages have the potential to be important antisense therapeutics that can be targeted on specific sequences of single- and double-stranded DNA, as well as crucial RNA messages. The stability of hybrid duplexes that contain these modified linkages is known experimentally to depend on the configuration of the chiral phosphonate center. Free-energy decomposition calculations were performed on three DNA oligomers to determine the origin of the structural interactions and physical properties that influence the relative stability of R and S methylphosphonate diastereomers. The strategy applied used free-energy decomposition methods to evaluate the free-energy contributions from selected groups. The results indicated that only three groups have a steric effect on the stability: the C2' and C3' substituents on the S diastereomer (5' side) and the C5' substituents on the R diastereomer (3' side). The balance considerably favors the R configuration in all the isomers studied and is not sequence dependent. The electrostatic effects were much more variable and were shown to be dependent on the conformation of duplex. The solvent interactions, however, were consistent and contributed favorably to the stability of the R over the S diastereomer. This favorable solvation energy for the R diastereomer was surprising (since the methyl group is more solvent exposed in this configuration) and was further supported by ab initio and associated free-energy calculations. This study concludes that oligonucleotides containing R-methylphosphonate linkages will normally form more stable duplexes than the corresponding S diastereomer irrespective of sequence, but also points that conformational changes may allow for a reversal in stability." citations,ref_2,5245,220436,3,,reference citation,,,8036171,,"Vyazovkina EV, Savchenko EV, Lokhov SG, Engels JW, Wickstrom E, Lebedev AV. Synthesis of specific diastereomers of a DNA methylphosphonate heptamer, d(CpCpApApApCpA), and stability of base pairing with the normal DNA octamer d(TPGPTPTPTPGPGPC). Nucleic Acids Res. 1994 Jun 25;22(12):2404-9.","Synthesis of specific diastereomers of a DNA methylphosphonate heptamer, d(CpCpApApApCpA), and stability of base pairing with the normal DNA octamer d(TPGPTPTPTPGPGPC).",published,journal,Nucleic Acids Res.,Nucleic acids research,22,12,,0305-1048,,,,,,,,,,,,,,,,,,,,2404,2409,1994,"DNA methylphosphonates are candidate derivatives for use in antisense DNA therapy. Their efficacy is limited by weak hybridization. One hypothesis to explain this phenomenon holds that one configuration of the chiral methylphosphonate linkage, Rp, permits stronger base pairing than the other configuration, Sp. To test this hypothesis, four specific pairs of Rp and Sp diastereomers of the DNA methylphosphonate heptamer d(CpCpApApApCpA) were prepared by block coupling of different combinations of individual diastereomers of d(CpCpApA) and d(ApCpA). Each pair of the diastereomers of the heptamer was separated into individual diastereomes using affinity chromatography on a Lichrosorb-NH2 silica column with a covalently attached complementary normal DNA octamer, d(pTpGpTpTpTpGpGpC). The stabilities of complementary complexes of phosphodiester d(TpGpTpTpTpGpGpC) with 8 individual diastereomers of methylphosphonate d(CpCpApApApCpA) were studied by measuring their melting temperatures (Tm). A direct correlation of Tm values with the number of Rp methylphosphonate centers in the heptamer was found: the more Rp centers, the higher the stability of the complex. Tm values for the diastereomers with 6 all-Rp or all-Sp methylphosphonate centers were found to be 30.5 degrees and 12.5 degrees C, respectively, in 100 mM NaCl, 10 mM Na2HPO4, 1 mM EDTA, pH 7.0 with 15 microM of each oligomer. On the average, each substitution of one Rp-center to an Sp-center in the heptamer decreased the Tm by 3 degrees C. Under the same conditions, the Tm of the normal DNA heptamer with its complement was 21 degrees C. These results are consistent with the model that all-Rp methylphosphonate DNAs hybridize much more tightly to complementary normal DNA than do racemic methylphosphonate DNAs, and may therefore exhibit greater potency as antisense inhibitors." citations,entry_citation,5246,220461,1,,entry citation,,21856752,11866509,,,"Chiral Mutagenesis of Insulin's Hidden Receptor-binding Surface: Structure of an Allo-isoleucine(A2) Analogue",published,journal,J. Mol. Biol.,,316,3,,,,,,,,,,,,,,,,,,,,,,435,441,2002, citations,entry_citation,5247,220485,1,,entry citation,,,,,,"Letter to the Editor: Sequence-specific chemical shift assignment of Calcium-loaded murine Mts1",published,journal,J. Biomol. NMR,,23,2,,,,,,,,,,,,,,,,,,,,,,153,154,2002, citations,entry_citation,5248,220513,1,,entry citation,,,11786999,,,"NMR Solution Structure of the Isolated Apo Pin1 WW Domain: Comaprison to the X-Ray Crystal Structures of Pin 1",published,journal,Biopolymers,,63,2,,,,,,,,,,,,,,,,,,,,,,111,121,2002, citations,citation_1,5649,229418,2,,reference citation,,,12522297,,,Random Coil Proton Chemical Shifts of Deoxyribonucleic Acids,published,journal,J. Biomol. NMR,,24,4,,,,,,,,,,,,,,,,,,,,,,329,337,2002, citations,ref_1,5275,221018,2,,reference citation,,,11462006,,"Dormitzer PR, Greenberg HB, Harrison SC. Proteolysis of monomeric recombinant rotavirus VP4 yields an oligomeric VP5* core. J Virol. 2001 Aug;75(16):7339-50.",Proteolysis of monomeric recombinant rotavirus VP4 yields an oligomeric VP5* core.,published,journal,J. Virol.,Journal of virology,75,16,,0022-538X,,,,,,,,,,,,,,,,,,,,7339,7350,2001,"Rotavirus particles are activated for cell entry by trypsin cleavage of the outer capsid spike protein, VP4, into a hemagglutinin, VP8*, and a membrane penetration protein, VP5*. We have purified rhesus rotavirus VP4, expressed in baculovirus-infected insect cells. Purified VP4 is a soluble, elongated monomer, as determined by analytical ultracentrifugation. Trypsin cleaves purified VP4 at a number of sites that are protected on the virion and yields a heterogeneous group of protease-resistant cores of VP5*. The most abundant tryptic VP5* core is trimmed past the N terminus associated with activation for virus entry into cells. Sequential digestion of purified VP4 with chymotrypsin and trypsin generates homogeneous VP8* and VP5* cores (VP8CT and VP5CT, respectively), which have the authentic trypsin cleavages in the activation region. VP8CT is a soluble monomer composed primarily of beta-sheets. VP5CT forms sodium dodecyl sulfate-resistant dimers. These results suggest that trypsinization of rotavirus particles triggers a rearrangement in the VP5* region of VP4 to yield the dimeric spikes observed in icosahedral image reconstructions from electron cryomicroscopy of trypsinized rotavirus virions. The solubility of VP5CT and of trypsinized rotavirus particles suggests that the trypsin-triggered conformational change primes VP4 for a subsequent rearrangement that accomplishes membrane penetration. The domains of VP4 defined by protease analysis contain all mapped neutralizing epitopes, sialic acid binding residues, the heptad repeat region, and the membrane permeabilization region. This biochemical analysis of VP4 provides sequence-specific structural information that complements electron cryomicroscopy data and defines targets and strategies for atomic-resolution structural studies." citations,ref_2,5275,221019,3,,reference citation,,,,,"Guntert,P., Dotsch,V., Wider,G. and Wuthrich,K. Processing of multi-dimensional NMR data with the new software PROSA. J. Biomol. NMR, 2, 619-629 (1992).",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_3,5275,221020,4,,reference citation,,,,,"Bartels,C., Xia,T.-H., Billeter,M., Guntert,P. and Wuthrich,K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J. Biomol. NMR, 5, 1-10 (1995).",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_4,5275,221021,5,,reference citation,,,9367762,,"Guntert P, Mumenthaler C, Wuthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J Mol Biol. 1997 Oct 17;273(1):283-98.",Torsion angle dynamics for NMR structure calculation with the new program DYANA.,published,journal,J. Mol. Biol.,Journal of molecular biology,273,1,,0022-2836,,,,,,,,,,,,,,,,,,,,283,298,1997,"The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from distance constraints and torsion angle constraints collected by nuclear magnetic resonance (NMR) experiments performs simulated annealing by molecular dynamics in torsion angle space and uses a fast recursive algorithm to integrate the equations of motions. Torsion angle dynamics can be more efficient than molecular dynamics in Cartesian coordinate space because of the reduced number of degrees of freedom and the concomitant absence of high-frequency bond and angle vibrations, which allows for the use of longer time-steps and/or higher temperatures in the structure calculation. It also represents a significant advance over the variable target function method in torsion angle space with the REDAC strategy used by the predecessor program DIANA. DYANA computation times per accepted conformer in the ""bundle"" used to represent the NMR structure compare favorably with those of other presently available structure calculation algorithms, and are of the order of 160 seconds for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300 computer. Test calculations starting from conformers with random torsion angle values further showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures." citations,ref_5,5275,221022,6,,reference citation,,,10212987,,"Cornilescu G, Delaglio F, Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J Biomol NMR. 1999 Mar;13(3):289-302.",Protein backbone angle restraints from searching a database for chemical shift and sequence homology.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,13,3,,0925-2738,,,,,,,,,,,,,,,,,,,,289,302,1999,"Chemical shifts of backbone atoms in proteins are exquisitely sensitive to local conformation, and homologous proteins show quite similar patterns of secondary chemical shifts. The inverse of this relation is used to search a database for triplets of adjacent residues with secondary chemical shifts and sequence similarity which provide the best match to the query triplet of interest. The database contains 13C alpha, 13C beta, 13C', 1H alpha and 15N chemical shifts for 20 proteins for which a high resolution X-ray structure is available. The computer program TALOS was developed to search this database for strings of residues with chemical shift and residue type homology. The relative importance of the weighting factors attached to the secondary chemical shifts of the five types of resonances relative to that of sequence similarity was optimized empirically. TALOS yields the 10 triplets which have the closest similarity in secondary chemical shift and amino acid sequence to those of the query sequence. If the central residues in these 10 triplets exhibit similar phi and psi backbone angles, their averages can reliably be used as angular restraints for the protein whose structure is being studied. Tests carried out for proteins of known structure indicate that the root-mean-square difference (rmsd) between the output of TALOS and the X-ray derived backbone angles is about 15 degrees. Approximately 3% of the predictions made by TALOS are found to be in error." citations,ref_6,5275,221023,7,,reference citation,,,9757107,,"Brunger AT, Adams PD, Clore GM, DeLano WL, Gros P, Grosse-Kunstleve RW, Jiang JS, Kuszewski J, Nilges M, Pannu NS, Read RJ, Rice LM, Simonson T, Warren GL. Crystallography and NMR system: A new software suite for macromolecular structure Determination. Acta Crystallogr D Biol Crystallogr. 1998 Sep;1(54): 905-21.",Crystallography & NMR system: A new software suite for macromolecular structure determination.,published,journal,Acta Crystallogr. D Biol. Crystallogr.,"Acta crystallographica. Section D, Biological crystallography",54,Pt 5,,0907-4449,,,,,,,,,,,,,,,,,,,,905,921,1998,"A new software suite, called Crystallography & NMR System (CNS), has been developed for macromolecular structure determination by X-ray crystallography or solution nuclear magnetic resonance (NMR) spectroscopy. In contrast to existing structure-determination programs, the architecture of CNS is highly flexible, allowing for extension to other structure-determination methods, such as electron microscopy and solid-state NMR spectroscopy. CNS has a hierarchical structure: a high-level hypertext markup language (HTML) user interface, task-oriented user input files, module files, a symbolic structure-determination language (CNS language), and low-level source code. Each layer is accessible to the user. The novice user may just use the HTML interface, while the more advanced user may use any of the other layers. The source code will be distributed, thus source-code modification is possible. The CNS language is sufficiently powerful and flexible that many new algorithms can be easily implemented in the CNS language without changes to the source code. The CNS language allows the user to perform operations on data structures, such as structure factors, electron-density maps, and atomic properties. The power of the CNS language has been demonstrated by the implementation of a comprehensive set of crystallographic procedures for phasing, density modification and refinement. User-friendly task-oriented input files are available for nearly all aspects of macromolecular structure determination by X-ray crystallography and solution NMR." citations,entry_citation,5276,221068,1,,entry citation,,22047862,12051857,,,"Interaction of Kazal-type Inhibitor Domains with Serine Proteinases: Biochemical and Structural Studies",published,journal,J. Mol. Biol.,,318,2,,,,,,,,,,,,,,,,,,,,,,533,546,2002, citations,entry_citation,5279,221123,1,,entry citation,,,,,,"A Quick Solution Structure Determination of the Fully Oxidized Double Mutant K9-10A Cytochrome c7 from Desulfuromonas acetoxidans and Mechanistic Implications",published,journal,J. Biomol. NMR,,22,1,,,,,,,,,,,,,,,,,,,,,,107,122,2002, citations,entry_citation,5280,221144,1,,entry citation,,,,,,"Letter to the Editor: Assignments of the 1H, 13C, and 15N, resonances of the winged helix domain of the proto-oncoprotein c-Qin (FoxG1B)",published,journal,J. Biomol. NMR,,23,3,,,,,,,,,,,,,,,,,,,,,,243,244,2002, citations,ref_1,5280,221145,2,,reference citation,,,7831308,,"Chang HW, Li J, Kretzschmar D, Vogt PK. Avian cellular homolog of the qin oncogene. Proc Natl Acad Sci U S A. 1995 Jan 17;92(2):447-51.",Avian cellular homolog of the qin oncogene.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,92,2,,0027-8424,,,,,,,,,,,,,,,,,,,,447,451,1995,"We have isolated chicken cDNA clones of the c-qin gene, the cellular counterpart of the v-qin (Chinese for ""avian"") oncogene of avian sarcoma virus 31. There are several differences between the cellular and the viral qin sequences: (i) two nonconservative amino acid substitutions in the Qin coding region; (ii) a truncation in the carboxyl terminus of the viral protein due to a premature stop codon; (iii) a partial Gag sequence fused to the amino terminus of viral Qin; and (iv) eight cell-coded amino acids which link the cellular Qin coding domain to the viral Gag domain. We have also characterized the expression pattern of c-qin in chicken embryos by in situ hybridization and by Northern blot analysis. c-qin is abundantly expressed in the developing brain, and this expression is restricted to the telencephalon of early embryos." citations,entry_citation,5281,221179,1,,entry citation,,,,,,A peptide mimetic of human interferon (IFN)-beta,submitted,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5282,221195,1,,entry citation,,22333288,12449414,,,"Refinement of d(GCGAAGC) Hairpin Structure Using One- and Two-bond Residual Dipolar Couplings",published,journal,J. Biomol. NMR,,24,1,,,,,,,,,,,,,,,,,,,,,,1,14,2002, citations,entry_citation,5283,221218,1,,entry citation,,22079438,12084067,,,"Structure of Human Immunodeficiency Virus Type 1 Vpr(34-51) Peptide in Micelle containing Aqueous Solution",published,journal,Eur. J. Biochem.,,269,13,,,,,,,,,,,,,,,,,,,,,,3264,3269,2002, citations,entry_citation,5284,221240,1,,entry citation,,,,,,"Solution structure of human intestinal fatty acid binding protein with a naturally-occurring single amino acid substitution (A54T) that is associated with altered lipid metabolism",published,journal,Biochemistry,,42,24,,,,,,,,,,,,,,,,,,,,,,7339,7349,2003, citations,entry_citation,5285,221261,1,,entry citation,,,,,,"Solution structure of human intestinal fatty acid binding protein with a naturally-occurring single amino acid substitution (A54T) that is associated with altered lipid metabolism",published,journal,Biochemistry,,42,24,,,,,,,,,,,,,,,,,,,,,,7339,7347,2003, citations,entry_citation,5286,221282,1,,entry citation,,21988207,11904288,,,"A Direct Test of the Reductionist Approach to Structural Studies of Calmodulin Activity: Relevance of Peptide Models of Target Proteins",published,journal,J. Biol. Chem.,,277,19,,,,,,,,,,,,,,,,,,,,,,16351,16354,2002, citations,entry_citation,5287,221304,1,,entry citation,,21988207,11904288,,,"A Direct Test of the Reductionist Approach to Structural Studies of Calmodulin Activity: Relevance of Peptide Models of Target Proteins",published,journal,J. Biol. Chem.,,277,19,,,,,,,,,,,,,,,,,,,,,,16351,16354,2002, citations,entry_citation,5288,221320,1,,entry citation,,22056596,12061724,,,"Letter to the Editor: Assignment of Backbone 1H, 13C, and 15N Resonances of Human Grb7-SH2 Domain in Complex with a Phosphorylated Peptide Ligand",published,journal,J. Biomol. NMR,,23,1,,,,,,,,,,,,,,,,,,,,,,77,78,2002, citations,entry_citation,5289,221343,1,,entry citation,,21986604,11991205,,,"Investigation of Penetratin Peptides. Part 1: The Environment Dependent Conformational Properties of Penetratin and two of its Derivatives",published,journal,J. Pept. Sci.,,8,4,,,,,,,,,,,,,,,,,,,,,,151,171,2002, citations,entry_citation,5290,221362,1,,entry citation,,21986604,11991205,,,"Investigation of Penetratin Peptides. Part 1: The Environment Dependent Conformational Properties of Penetratin and two of its Derivatives",published,journal,J. Pept. Sci.,,8,4,,,,,,,,,,,,,,,,,,,,,,151,171,2002, citations,entry_citation,5291,221379,1,,entry citation,,21986604,11991205,,,"Investigation of Penetratin Peptides. Part 1: The Environment Dependent Conformational Properties of Penetratin and two of its Derivatives",published,journal,J. Pept. Sci.,,8,4,,,,,,,,,,,,,,,,,,,,,,151,171,2002, citations,entry_citation,5292,221396,1,,entry citation,,22028569,11979279,,,Designing a 20-residue Protein,published,journal,Nat. Struct. Biol.,,9,6,,,,,,,,,,,,,,,,,,,,,,425,430,2002,First linear 20-residue peptide to display protein-like folding behavior. citations,entry_citation,5293,221416,1,,entry citation,,22142190,12146954,,,"NMR Identification and Characterization of the Flexible Regions in the 160 kDa Molten Globule-like Aggregate of Barstar at low pH",published,journal,Biochemistry,,41,31,,,,,,,,,,,,,,,,,,,,,,9885,9899,2002, citations,entry_citation,5294,221447,1,,entry citation,,21976992,11980477,,,"Structure of the Beta Subunit of Translation Initiation Factor 2 from the Archaeon Methanococcus jannaschii: A Representative of the eIF2beta/eIF5 Family of Proteins",submitted,journal,Biochemistry,,41,18,,,,,,,,,,,,,,,,,,,,,,5730,5742,2002, citations,entry_citation,5295,221472,1,,entry citation,,,,,,"Probing the sweet determinants of brazzein: Wild-type brazzein and a tasteless variant, brazzein-ins(R(18a)-I(18b)), exhibit different pH-dependent NMR chemical shifts",published,journal,Biochem. Biophys. Res. Commun.,,335,1,,,,,,,,,,,,,,,,,,,,,,256,263,2005, citations,entry_citation,5296,221487,1,,entry citation,,,,,,"Probing the sweet determinants of brazzein: Wild-type brazzein and a tasteless variant, brazzein-ins(R(18a)-I(18b)), exhibit different pH-dependent NMR chemical shifts",published,journal,Biochem. Biophys. Res. Commun.,,335,1,,,,,,,,,,,,,,,,,,,,,,256,263,2005, citations,entry_citation,5297,221502,1,,entry citation,,22155869,12130667,,,"The Structure of a Replication Initiator unites Diverse aspects of Nucleic Acid Metabolism",published,journal,Proc. Natl. Acad. Sci. U.S.A.,,99,16,,,,,,,,,,,,,,,,,,,,,,10310,10315,2002, citations,entry_citation,5298,221541,1,,entry citation,,,,,,"Solution structure of the closed form of a peptidyl-prolyl isomerase reveals the mechanism of protein folding",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5299,221566,1,,entry citation,,,11804586,,,"The Mad2 Spindle Checkpoint Protein Undergoes Similar Major Conformational Changes upon Binding to Either Mad1 or Cdc20",published,journal,Mol. Cell,,9,,,,,,,,,,,,,,,,,,,,,,,59,71,2002, citations,entry_citation,53,221594,1,,entry citation,,,,,"Strop, Petr, Wider, Gerhard, Wuthrich, Kurt, ""Assignment of the 1H Nuclear Magnetic Resonance Spectrum of the Proteinase Inhibitor IIA from Bull Seminal Plasma by Two-dimensional Nuclear Magnetic Resonance at 500 MHz,"" J. Mol. Biol. 166, 641-667 (1983).","Assignment of the 1H Nuclear Magnetic Resonance Spectrum of the Proteinase Inhibitor IIA from Bull Seminal Plasma by Two-dimensional Nuclear Magnetic Resonance at 500 MHz",published,journal,J. Mol. Biol.,,166,,,,,,,,,,,,,,,,,,,,,,,641,667,1983, citations,entry_citation,530,221608,1,,entry citation,,,,,"Wang, Jinfeng, Hinck, Andrew P., Loh, Stewart N., Markley, John L., ""Two-Dimensional NMR Studies of Staphylococcal Nuclease: Evidence for Conformational Heterogeneity from Hydrogen-1, Carbon-13, and Nitrogen-15 Spin System Assignments of the Aromatic Amino Acids in the Nuclease H124L-Thymidine 3',5'-Bisphosp,"" Biochemistry 29, 4242-4253 (1990).","Two-Dimensional NMR Studies of Staphylococcal Nuclease: Evidence for Conformational Heterogeneity from Hydrogen-1, Carbon-13, and Nitrogen-15 Spin System Assignments of the Aromatic Amino Acids in the Nuclease H124L-Thymidine 3',5'-Bisphosp",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,4242,4253,1990, citations,entry_citation,5300,221621,1,,entry citation,,,,,,"Letter to the Editor: Backbone 1H, 15N and 13C assignments for the 21 kDa Caenorhabditis elegans homologue of 'brain-specific' protein",published,journal,J. Biomol. NMR,,28,1,,,,,,,,,,,,,,,,,,,,,,91,92,2004, citations,ref-1,5300,221622,2,,reference citation,,,9217263,,"Zimmerman, D. E., Kulikowski, C. A., Huang, Y., Feng, W., Tashiro, M., Shimotakahara, S., Chien, C. Y., Powers, R., and Montelione, G. T. J. Mol. Biol. 269, 592-610, (1997).",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5301,221658,1,,entry citation,,22166449,12175243,,,"Principles of Mucin Architecture: Structural Studies on Synthetic Glycopeptides Bearing Clustered Mono-,Di, Tri-, and Hexasacchraride Glycodomains",published,journal,J. Am. Chem. Soc.,,124,33,,,,,,,,,,,,,,,,,,,,,,9833,9844,2002, citations,entry_citation,5302,221678,1,,entry citation,,22602215,12717720,,,"Conformational Preferences of the Amylin Nucleation Site in SDS Micelles: An NMR Study",published,journal,Biopolymers,,69,1,,,,,,,,,,,,,,,,,,,,,,29,41,2003, citations,entry_citation,5303,221696,1,,entry citation,,22767615,12885241,,,"High-resolution Solution Structure of the Beryllofluoride-activated NtrC Receiver Domain",published,journal,Biochemistry,,42,30,,,,,,,,,,,,,,,,,,,,,,9081,9090,2003, citations,entry_citation,5304,221726,1,,entry citation,,21952326,11955059,,,"Solution Structure of a Monoheme Ferrocytochrome c from Shewanella putrefaciens and Structural Analysis of Sequence-similar Proteins: Functional Implications",published,journal,Biochemistry,,41,16,,,,,,,,,,,,,,,,,,,,,,5112,5119,2002, citations,entry_citation,5305,221751,1,,entry citation,,22147550,12153046,,,"Letter to the Editor: 1H, 13C and 15N backbone resonance assignment of the peptidyl-prolyl cis-trans isomerase Pin1",published,journal,J. Biomol. NMR,,23,2,,,,,,,,,,,,,,,,,,,,,,163,164,2002, citations,entry_citation,5306,221773,1,,entry citation,,21957254,11959990,,,Structural Basis for Recruitment of CBP/p300 by Hypoxia-inducible Factor-1 alpha,published,journal,Proc. Natl. Acad. Sci. U. S. A.,,99,8,,,,,,,,,,,,,,,,,,,,,,5367,5372,2002, citations,entry_citation,5307,221794,1,,entry citation,,,,,,Basic Pancreatic Trypsin Inhibitor,submitted,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5308,221815,1,,entry citation,,22130999,12135359,,,"Solution Structure and Dynamics of the Human-Escherichia coli Thioredoxin Chimera: Insights into Thermodynamic Stability",published,journal,Biochemistry,,41,30,,,,,,,,,,,,,,,,,,,,,,9376,9388,2002, citations,entry_citation,5309,221832,1,,entry citation,,22147551,12153047,,,"Letter to the Editor: 1H, 15N and 13C assignments of FLIN4, an intramolecular LMO4:ldb1 complex",published,journal,J. Biomol. NMR,,23,2,,,,,,,,,,,,,,,,,,,,,,165,166,2002, citations,entry_citation,531,221866,1,,entry citation,,,,,"Heald, S.L., Harding, Matthew W., Handschumacher, R.E., Armitage, Ian M., ""1H NMR Studies on Bovine Cyclophilin: Preliminary Structural Characterization of Its Complex with Cyclosporin A,"" Biochemistry 29, 4466-4478 (1990).","1H NMR Studies on Bovine Cyclophilin: Preliminary Structural Characterization of Its Complex with Cyclosporin A",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,4466,4478,1990, citations,entry_citation,5310,221879,1,,entry citation,,,8181064,,,"Nuclear magnetic resonance structure of an SH2 domain of phospholipase C-gamma 1 complexed with a high affinity binding peptide",published,journal,Cell,,77,3,,,,,,,,,,,,,,,,,,,,,,461,472,1994, citations,ref_1,5310,221880,2,,reference citation,,,2831461,,"Stahl ML, Ferenz CR, Kelleher KL, Kriz RW, Knopf JL. Sequence similarity of phospholipase C with the non-catalytic region of src. Nature. 1988 Mar 17;332(6161):269-72.",Sequence similarity of phospholipase C with the non-catalytic region of src.,published,journal,Nature,Nature,332,6161,,0028-0836,,,,,,,,,,,,,,,,,,,,269,272,1988,"The production of the second messenger molecules diacylglycerol and inositol 1,4,5-trisphosphate is mediated by activated phosphatidylinositol-specific phospholipase C (PLC) enzymes. Here we report the cloning of a bovine brain complementary DNA encoding an enzyme PLC-148 that is characterized by calcium-dependent and phosphatidylinositol-specific phospholipase C activity when expressed in mammalian cells. Bovine brain messenger RNA contains a 7.5-kilobase transcript corresponding to the isolated cDNA; a related transcript of the same size is present in mRNA from some but not all human cell lines tested. Southern blot analysis of the bovine genome indicated that one or possibly two genes hybridize to the cloned PLC-148 cDNA. There is a striking sequence similarity between specific regions of PLC-148 and the non-catalytic domain of the non-receptor tyrosine kinases. The newly characterized crk transforming gene of the avian sarcoma virus CT10 also contains extensive sequence similarities with PLC-148." citations,ref_2,5310,221881,3,,reference citation,,,8384875,,"Piccione E, Case RD, Domchek SM, Hu P, Chaudhuri M, Backer JM, Schlessinger J, Shoelson SE. Phosphatidylinositol 3-kinase p85 SH2 domain specificity defined by direct phosphopeptide/SH2 domain binding. Biochemistry. 1993 Apr 6;32(13):3197-202.",Phosphatidylinositol 3-kinase p85 SH2 domain specificity defined by direct phosphopeptide/SH2 domain binding.,published,journal,Biochemistry,Biochemistry,32,13,,0006-2960,,,,,,,,,,,,,,,,,,,,3197,3202,1993,"We have developed a competition binding assay to quantify relative affinities of isolated Src-homology 2 (SH2) domains for phosphopeptide sequences. Eleven synthetic 11-12-amino acid phosphopeptides containing YMXM or YVXM recognition motifs bound to a PI 3-kinase p85 SH2 domain with highest affinities, including sequences surrounding phosphorylated tyrosines of the PDGF, CSF-1/c-Fms, and kit-encoded receptors, IRS-1, and polyoma middle T antigens; matched, unphosphorylated sequences did not bind. A scrambled YMXM phosphopeptide or sequences corresponding to the GAP or PLC-gamma SH2 domain binding motifs of the PDGF, FGF, and EGF receptors bound to the p85 SH2 domain with 30-100-fold reduced affinity, indicating that this affinity range confers specificity. Binding specificity was appropriately reversed with an SH2 domain from PLC-gamma: a phosphopeptide corresponding to the site surrounding PDGF receptor Tyr1021 binds with approximately 40-fold higher affinity than a YMXM-phosphopeptide. We conclude that essential features of specific phosphoprotein/SH2 domain interactions can be reconstituted using truncated versions of both the phosphoprotein (a phosphopeptide) and cognate SH2 domain-containing protein (the SH2 domain). SH2 domain binding specificity results from differences in affinity conferred by the linear sequence surrounding phosphotyrosine." citations,ref_3,5310,221882,4,,reference citation,,,,,"Brunger, A.T. (1992) X-PLOR Version 3.1: A System for X-Ray Crystallography and NMR (New Haven, Connecticut: Yale University Press).",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_4,5310,221883,5,,reference citation,,,3078736,,"Miguel Giacchella R. [The history of the discovery of anesthesia. Progress is the attainment of utopia] Rev Soc Odontol La Plata. 1988 Apr;1(1):29-30.",[The history of the discovery of anesthesia. Progress is the attainment of utopia],published,journal,,Revista de la Sociedad Odontolagica de La Plata,1,1,,,,,,,,,,,,,,,,,,,,,,29,30,1988, citations,entry_citation,5311,221903,1,,entry citation,,,,,,"Letter to the Editor: 1H, 15N and 13C assignments of the Pseudomonas effector protein, AvrPto",published,journal,J. Biomol. NMR,,23,3,,,,,,,,,,,,,,,,,,,,,,247,248,2002, citations,entry_citation,5312,221932,1,,entry citation,,22057822,12062427,,,"Zinc is required for Structural Stability of the C-terminus of Archaeal Translation Initiation Factor aIF2beta",published,journal,FEBS Lett.,,517,1-3,,,,,,,,,,,,,,,,,,,,,,155,158,2002, citations,entry_citation,5313,221955,1,,entry citation,,,,,,"Letter to the Editor: Sequence-specific resonance assignment of the rat Gap Junction 43 kDa carboxyl terminal domain",published,journal,J. Biomol. NMR,,23,3,,,,,,,,,,,,,,,,,,,,,,245,246,2002, citations,entry_citation,5314,221968,1,,entry citation,,,,,,"Letter to the editor: Assignment of backbone 1H, 13C, and 15N Resonances of the SH2 Domain of Human Grb14",published,journal,J. Biomol. NMR,,24,3,,,,,,,,,,,,,,,,,,,,,,275,276,2002, citations,entry_citation,5315,221991,1,,entry citation,,22280969,12392550,,,"Ribosome-associated Factor Y adopts a Fold resembling a Double-stranded RNA Binding Domain Scaffold",published,journal,Eur. J. Biochem.,,269,21,,,,,,,,,,,,,,,,,,,,,,5182,5191,2002, citations,entry_citation,5316,222026,1,,entry citation,,,12032547,,,Structure of the N-terminal 283-Residue Fragment of the HIV-1 Gag Polyprotein,published,journal,Nat. Struct. Biol.,,9,7,,,,,,,,,,,,,,,,,,,,,,537,543,2002, citations,entry_citation,5317,222043,1,,entry citation,,,11738049,,,Solution structure of a telomeric DNA complex of human TRF1,published,journal,Structure,,9,,,,,,,,,,,,,,,,,,,,,,,1237,1251,2001, citations,entry_citation,5318,222066,1,,entry citation,,,8181064,,,"Nuclear magnetic resonance structure of an SH2 domain of phospholipase C-gamma 1 complexed with a high affinity binding peptide",published,journal,Cell,,77,3,,,,,,,,,,,,,,,,,,,,,,461,472,1994, citations,ref_1,5318,222067,2,,reference citation,,,88156963,,"Stahl ML, Ferenz CR, Kelleher KL, Kriz RW, Knopf JL. Sequence similarity of phospholipase C with the non-catalytic region of src. Nature. 1988 Mar 17;332(6161):269-72.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_2,5318,222068,3,,reference citation,,,93213786,,"Piccione E, Case RD, Domchek SM, Hu P, Chaudhuri M, Backer JM, Schlessinger J, Shoelson SE. Phosphatidylinositol 3-kinase p85 SH2 domain specificity defined by direct phosphopeptide/SH2 domain binding. Biochemistry. 1993 Apr 6;32(13):3197-202.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_3,5318,222069,4,,reference citation,,,,,"Brunger, A.T. (1992) X-PLOR Version 3.1: A System for X-Ray Crystallography and NMR (New Haven, Connecticut: Yale University Press).",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_4,5318,222070,5,,reference citation,,,90212257,,"Miguel Giacchella R. [The history of the discovery of anesthesia. Progress is the attainment of utopia] Rev Soc Odontol La Plata. 1988 Apr;1(1):29-30.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5319,222085,1,,entry citation,,,11934897,,,"Structure and backbone dynamics of apo- and holo-cellular retinol-binding protein in solution",published,journal,J. Biol. Chem.,,277,24,,,,,,,,,,,,,,,,,,,,,,21983,21997,2002, citations,entry_citation,532,222111,1,,entry citation,,,,,"Heald, S.L., Harding, Matthew W., Handschumacher, R.E., Armitage, Ian M., ""1H NMR Studies on Bovine Cyclophilin: Preliminary Structural Characterization of Its Complex with Cyclosporin A,"" Biochemistry 29, 4466-4478 (1990).","1H NMR Studies on Bovine Cyclophilin: Preliminary Structural Characterization of Its Complex with Cyclosporin A",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,4466,4478,1990, citations,entry_citation,5320,222124,1,,entry citation,,,,,,Solution structure of fatty acid-binding protein from human brain,published,journal,Mol. Cell. Biochem.,,239,,,,,,,,,,,,,,,,,,,,,,,61,68,2002, citations,entry_citation,5321,222146,1,,entry citation,,22148823,12153712,,,Solution Structure of a SRP19 Binding Domain in Human SRP RNA,published,journal,J. Biochem. (Tokyo),,132,2,,,,,,,,,,,,,,,,,,,,,,177,182,2002, citations,entry_citation,5322,222175,1,,entry citation,,15390258,,,,"Solution Structure of gamma-bungarotoxin: The functional significance of amino acid residues flanking the RGD motif in integrin binding",published,journal,Proteins,,,,,,,,,,,,,,,,,,,,,,,,,,,2004, citations,entry_citation,5323,222190,1,,entry citation,,,11969412,,,Structure and Dynamics of a beta-Helical Antifreeze Protein,published,journal,Biochemistry,,41,,,,,,,,,,,,,,,,,,,,,,,5515,5525,2002, citations,entry_citation,5324,222210,1,,entry citation,,,,,,"Letters to the Editor: 1H, 15N and 13C assignments of the regulatory domains of a calcium-dependent protein kinase (CDPK)",published,journal,J. Biomol. NMR,,23,3,,,,,,,,,,,,,,,,,,,,,,249,250,2002, citations,entry_citation,5325,222231,1,,entry citation,,22217954,12011089,,,"Solution Structure of Plant Nonspecific Lipid Transfer Protein-2 from Rice (Oryza sativa)",published,journal,J. Biol. Chem.,,277,38,,,,,,,,,,,,,,,,,,,,,,35267,35273,2002, citations,ref_1,5325,222232,2,,reference citation,,,12056799,,"Liu YJ, Samuel D, Lin CH, Lyu PC. Biochem. Biophys. Res. Commun. 294 535-540 (2002)",Purification and characterization of a novel 7-kDa non-specific lipid transfer protein-2 from rice (Oryza sativa).,published,journal,Biochem. Biophys. Res. Commun.,Biochemical and biophysical research communications,294,3,,0006-291X,,,,,,,,,,,,,,,,,,,,535,540,2002,"A novel 7-kDa non-specific lipid transfer protein-2 (nsLTP2) has been isolated from rice (Oryza sativa) seeds. In contrast to nsLTP1s, few nsLTP2s have been purified and characterized. Complete amino acid sequence of rice nsLTP2 was determined by N-terminal Edman degradation of the intact protein as well as the peptide fragments resulted from trypsin digestions. Rice nsLTP2 consists of 69 amino acid residues with eight conserved cysteines forming four disulfide bonds. The secondary structure of rice nsLTP2 is predominantly alpha-helical as determined by circular dichroism spectroscopy. Cysteine pairings of nsLTP2 have one miss match at Cys(35)-X-Cys(37) motif compared to nsLTP1. Primary structure analysis of various plant nsLTP2s revealed an interesting conservation of sequence features among nsLTP2 family." citations,entry_citation,5326,222249,1,,entry citation,,21966003,11969414,,,"Structure of Ala24/Asp61 --> Asp24/Asn61 Substituted Subunit C of Escherichia coli ATP Synthase: Implications for the Mechanism of Proton Transport and Rotary Movement in the F0 Complex",published,journal,Biochemistry,,41,17,,,,,,,,,,,,,,,,,,,,,,5537,5547,2002, citations,entry_citation,5327,222278,1,,entry citation,,21957241,11959977,,,"From the Cover: Structural basis for Hif-1alpha/CBP Recognition in the Cellular Hypoxic Response",published,journal,Proc. Natl. Acad. Sci. U.S.A.,,99,8,,,,,,,,,,,,,,,,,,,,,,5271,5276,2002, citations,entry_citation,5328,222301,1,,entry citation,,,,,,Solution NMR structure of the BRCT domain from Thermus thermophilus DNA ligase,submitted,journal,J. Biomol. NMR,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,reference_citation,5343,222611,1,,entry citation,,,12269815,,,"Solution structure of a novel chromoprotein derived from apo-neocarzinostatin and a synthetic chromophore.",published,journal,Biochemistry,,41,39,,,,,,,,,,,,,,,,,,,,,,11731,11739,2002, citations,ref-1,5328,222302,2,,reference citation,,,8520220,,"Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. J. Biomol. NMR 6, 277-293, (1995).",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref-2,5328,222303,3,,reference citation,,,9217263,,"Zimmerman, D. E., Kulikowski, C. A., Huang, Y., Feng, W., Tashiro, M., Shimotakahara, S., Chien, C. Y., Powers, R., and Montelione, G. T. J. Mol. Biol. 269, 592-610, (1997).",Automated analysis of protein NMR assignments using methods from artificial intelligence.,published,journal,J. Mol. Biol.,Journal of molecular biology,269,4,,0022-2836,,,,,,,,,,,,,,,,,,,,592,610,1997,"An expert system for determining resonance assignments from NMR spectra of proteins is described. Given the amino acid sequence, a two-dimensional 15N-1H heteronuclear correlation spectrum and seven to eight three-dimensional triple-resonance NMR spectra for seven proteins, AUTOASSIGN obtained an average of 98% of sequence-specific spin-system assignments with an error rate of less than 0.5%. Execution times on a Sparc 10 workstation varied from 16 seconds for smaller proteins with simple spectra to one to nine minutes for medium size proteins exhibiting numerous extra spin systems attributed to conformational isomerization. AUTOASSIGN combines symbolic constraint satisfaction methods with a domain-specific knowledge base to exploit the logical structure of the sequential assignment problem, the specific features of the various NMR experiments, and the expected chemical shift frequencies of different amino acids. The current implementation specializes in the analysis of data derived from the most sensitive of the currently available triple-resonance experiments. Potential extensions of the system for analysis of additional types of protein NMR data are also discussed." citations,ref-3,5328,222304,4,,reference citation,,,11462827,,"Moseley, H.N., Monleon, D., Montelione, G.T. Methods Enzymol, 339, 91-108, (2001).",Automatic determination of protein backbone resonance assignments from triple resonance nuclear magnetic resonance data.,published,journal,Meth. Enzymol.,Methods in enzymology,339,,,0076-6879,,,,,,,,,,,,,,,,,,,,91,108,2001, citations,entry_citation,5329,222324,1,,entry citation,,22199947,12211038,,,"NMR Structure of Conserved Eukaryotic Protein ZK652.3 from C. elegans: A Ubiquitin-like fold",published,journal,Proteins,,48,4,,,,,,,,,,,,,,,,,,,,,,733,736,2002, citations,entry_citation,5330,222343,1,,entry citation,,,11934897,,,"Structure and backbone dynamics of apo- and holo-cellular retinol-binding protein in solution",published,journal,J. Biol. Chem.,,277,24,,,,,,,,,,,,,,,,,,,,,,21983,21997,2002, citations,entry_citation,5331,222368,1,,entry citation,,,11934897,,,"Structure and backbone dynamics of apo- and holo-cellular retinol-binding protein in solution",published,journal,J. Biol. Chem.,,277,24,,,,,,,,,,,,,,,,,,,,,,21983,21997,2002, citations,entry_citation,5332,222395,1,,entry citation,,21976996,11980481,,,"Structure and Calcium-binding Studies of a Recoverin Mutant (E85Q) in an Allosteric Intermediate State",published,journal,Biochemistry,,41,18,,,,,,,,,,,,,,,,,,,,,,5776,5787,2002, citations,entry_citation,5333,222417,1,,entry citation,,22050881,12054869,,,"Redox-coupled Conformational Alternations in Cytochrome c3 from D. vulgaris Miyazaki F on the Basis of its Reduced Solution Structure",published,journal,J. Mol. Biol.,,319,3,,,,,,,,,,,,,,,,,,,,,,767,778,2002, citations,entry_citation,5334,222444,1,,entry citation,,,,,,"Backbone 1H, 13C, and 15N resonance assignments and secondary structure of the D54A mutant of HTLV-I capsid protein",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_1,5334,222445,2,,reference citation,,,11243788,,"Cornilescu, C. C., Bouamr, F., Yao, X., Carter, C. & Tjandra, N. (2001) J. Mol. Biol., 306, 783-797.",Structural analysis of the N-terminal domain of the human T-cell leukemia virus capsid protein.,published,journal,J. Mol. Biol.,Journal of molecular biology,306,4,,0022-2836,,,,,,,,,,,,,,,,,,,,783,797,2001,"The N-terminal domain of the retroviral capsid (CA) protein is one of the least conserved regions encoded in the genome. Surprisingly, the three-dimensional structures of the CA from different genera exhibit alpha-helical structural features that are highly conserved. The N-terminal residues of the human immunodeficiency virus type 1 (HIV-1) and Rous sarcoma virus (RSV) capsid proteins form a beta-hairpin. To determine if this feature is conserved in the retroviral family, we cloned, expressed, purified, and solved the structure of a N-terminal 134 amino acid fragment (CA(134)) from the human T-cell leukemia virus type 1 (HTLV-I) using high resolution nuclear magnetic resonance (NMR) spectroscopy. The CA(134) fragment contains an N-terminal beta-hairpin and a central coiled-coil-like structure composed of six alpha-helices. The N-terminal Pro1 residue contacts Asp54 in the helical cluster through a salt bridge. Thus, the beta-hairpin is conserved and the helical cluster is structurally similar to other retroviral CA domains. However, although the same Asp residue defines the orientation of the hairpin in both the HTLV-1 and HIV-1 CA proteins, the HTLV-I hairpin is oriented away, rather than towards, the helical core. Significant differences were also detected in the spatial orientation and helical content of the long centrally located loop connecting the helices in the core. It has been proposed that the salt bridge allows the formation of a CA-CA interface that is important for the assembly of the conical cores that are characteristic of HIV-1. As HTLV-I forms spherical cores, the salt-bridge feature is apparently not conserved for this function although its role in determining the orientation of the beta-hairpin may be critical, along with the central loop. Comparison of three-dimensional structures is expected to elucidate the relationships between the retroviral capsid protein structure and its function." citations,Primary_publication,5343,222612,2,,reference citation,,,,,,To be announced,in preparation,journal,J. Am. Chem. Soc.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_1,5343,222613,3,,reference citation,,,8369747,,"N. Sakata, S. Minamitani, T. Kanbe, M. Hori, M. Hirama, and K. Edo, The amino acid sequence of neocarzinostatin apoprotein deduced from the base sequence of the gene. Biol. Pharm. Bull., 1993, 16, 26.","The amino acid sequence of neocarzinostatin apoprotein deduced from the base sequence of the gene.",published,journal,"Biol. Pharm, Bull.",,16,1,,,,,,,,,,,,,,,,,,,,,,26,28,1993, citations,entry_citation,5344,222641,1,,entry citation,,,12269815,,,"Solution Structure of a Novel Chromoprotein dervived from apo-Neocarzinostatin and a Synthetic Chromophore",published,journal,Biochemistry,,41,39,,,,,,,,,,,,,,,,,,,,,,11731,11739,2002, citations,entry_citation,5558,227180,1,,entry citation,,,11427895,,,"The SAND domain structure defines a novel DNA-binding fold in transcriptional regulation",published,journal,Nat. Struct. Biol.,,8,7,,,,,,,,,,,,,,,,,,,,,,626,633,2001, citations,ref_2,5334,222446,3,,reference citation,,,8520220,,"Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J. & Bax, A. (1995) J. Biomol. NMR, 6, 277-293.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref_3,5334,222447,4,,reference citation,,,10212987,,"Cornilescu, G., Delaglio, F. & Bax, A. (1999) J. Biomol. NMR, 13, 289-302.",Protein backbone angle restraints from searching a database for chemical shift and sequence homology.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,13,3,,0925-2738,,,,,,,,,,,,,,,,,,,,289,302,1999,"Chemical shifts of backbone atoms in proteins are exquisitely sensitive to local conformation, and homologous proteins show quite similar patterns of secondary chemical shifts. The inverse of this relation is used to search a database for triplets of adjacent residues with secondary chemical shifts and sequence similarity which provide the best match to the query triplet of interest. The database contains 13C alpha, 13C beta, 13C', 1H alpha and 15N chemical shifts for 20 proteins for which a high resolution X-ray structure is available. The computer program TALOS was developed to search this database for strings of residues with chemical shift and residue type homology. The relative importance of the weighting factors attached to the secondary chemical shifts of the five types of resonances relative to that of sequence similarity was optimized empirically. TALOS yields the 10 triplets which have the closest similarity in secondary chemical shift and amino acid sequence to those of the query sequence. If the central residues in these 10 triplets exhibit similar phi and psi backbone angles, their averages can reliably be used as angular restraints for the protein whose structure is being studied. Tests carried out for proteins of known structure indicate that the root-mean-square difference (rmsd) between the output of TALOS and the X-ray derived backbone angles is about 15 degrees. Approximately 3% of the predictions made by TALOS are found to be in error." citations,ref_4,5334,222448,5,,reference citation,,,,,"Garrett, D. S., Powers, R., Gronenborn, A. M. & Clore, G. M. (1991) J. Magn. Reson, 95, 214-220.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5335,222465,1,,entry citation,,22199977,12211008,,,"NMR Structure of the Eschericia coli Protein YacG: A Novel Sequence Motif in the Zinc-finger Family of Proteins",published,journal,Proteins,,49,2,,,,,,,,,,,,,,,,,,,,,,289,293,2002, citations,ref_1,5335,222466,2,,reference citation,,,,,"Brunger AT. X-PLOR Version 3.1: a system for X-ray crystallography and NMR. New Haven, CY:Yale University Press; 1992.382 p.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5337,222486,1,,entry citation,,,,,,Comparison of functional domains in vertebrate-type ferredoxins,submitted,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5338,222510,1,,entry citation,,,11896403,,,"Cysteine-rich module structure reveals a fulcrum for integrin rearrangement upon activation",published,journal,Nat. Struct. Biol.,,9,,,,,,,,,,,,,,,,,,,,,,,282,287,2002, citations,entry_citation,5339,222527,1,,entry citation,,,11922844,,,"Low Temperature Solution Structures and Base Pair Stacking of Double Helical d(CGTACG)(2)",published,journal,J. Biomol. Struct. Dyn.,,19,5,,,,,,,,,,,,,,,,,,,,,,907,917,2002, citations,entry_citation,5340,222543,1,,entry citation,,,,,,"Solution Structure for BID, and Intracellular Amplifier of Apoptotic Signaling",submitted,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_1,5340,222544,2,,reference citation,,,10089877,,"Chou JJ, Li H, Salvesen GS, Yuan J, Wagner G. Solution structure of BID, an intracellular amplifier of apoptotic signaling. Cell. 1999 Mar 5;96(5):615-24.","Solution structure of BID, an intracellular amplifier of apoptotic signaling.",published,journal,Cell,Cell,96,5,,0092-8674,,,,,,,,,,,,,,,,,,,,615,624,1999,"We report the solution structure of BID, an intracellular cross-talk agent that can amplify FAS/TNF apoptotic signal through the mitochondria death pathway after Caspase 8 cleavage. BID contains eight alpha helices where two central hydrophobic helices are surrounded by six amphipathic ones. The fold resembles poreforming bacterial toxins and shows similarity to BCL-XL although sequence homology to BCL-XL is limited to the 16-residue BH3 domain. Furthermore, we modeled a complex of BCL-XL and BID by aligning the BID and BAK BH3 motifs in the known BCL-XL-BAK BH3 complex. Additionally, we show that the overall structure of BID is preserved after cleavage by Caspase 8. We propose that BID has both BH3 domain-dependent and -independent modes of action in inducing mitochondrial damage." citations,ref_2,5340,222545,3,,reference citation,,,9727492,,"Li H, Zhu H, Xu CJ, Yuan J. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell. 1998 Aug 21;94(4):491-501.",Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis.,published,journal,Cell,Cell,94,4,,0092-8674,,,,,,,,,,,,,,,,,,,,491,501,1998,"We report here that BID, a BH3 domain-containing proapoptotic Bcl2 family member, is a specific proximal substrate of Casp8 in the Fas apoptotic signaling pathway. While full-length BID is localized in cytosol, truncated BID (tBID) translocates to mitochondria and thus transduces apoptotic signals from cytoplasmic membrane to mitochondria. tBID induces first the clustering of mitochondria around the nuclei and release of cytochrome c independent of caspase activity, and then the loss of mitochondrial membrane potential, cell shrinkage, and nuclear condensation in a caspase-dependent fashion. Coexpression of BclxL inhibits all the apoptotic changes induced by tBID. Our results indicate that BID is a mediator of mitochondrial damage induced by Casp8." citations,entry_citation,5341,222558,1,,entry citation,,,,,,"1H, 13C, and 15N assignment of the N-terminal, catalytic domain of the replication initiation protein from the geminivirus TYLCV",published,journal,J. Biomol. NMR,,24,1,,,,,,,,,,,,,,,,,,,,,,73,74,2002, citations,entry_citation,5342,222593,1,,entry citation,,22502270,12616630,,,"NMR Structure of the Single QALGGH Zinc Finger Domain from the Arabidopsis thaliana SUPERMAN Protein",published,journal,Chembiochem,,4,2-3,,,,,,,,,,,,,,,,,,,,,,171,180,2003, citations,ref_1,5344,222642,2,,reference citation,,,8369747,,"N. Sakata, S. Minamitani, T. Kanbe, M. Hori, M. Hirama, and K. Edo, The amino acid sequence of neocarzinostatin apoprotein deduced from the base sequence of the gene. Biol. Pharm. Bull., 1993, 16, 26.",The amino acid sequence of neocarzinostatin apoprotein deduced from the base sequence of the gene.,published,journal,Biol. Pharm. Bull.,Biological & pharmaceutical bulletin,16,1,,0918-6158,,,,,,,,,,,,,,,,,,,,26,28,1993,"A segment of the neocarzinostatin apoprotein gene corresponding to T30 to A91 of the protein was amplified using a polymerase chain reaction (PCR) with total DNA from Streptomyces carzinostaticus subsp. neocarzinostaticus E-793 (ATCC 15944) as the template and with 5'- and 3'-primers synthesized in consideration of the codon usage of streptomyces. The PCR product was cloned, sequenced and confirmed to direct an amino acid sequence reasonably well matching that reported. Using the PCR product as a probe, we cloned a DNA segment (2580 bp) spanning an open reading frame (ORF) for preapoprotein (leader peptide plus apoprotein) and its upstream and downstream flanking regions. The amino acid sequence deduced from the base sequence of the DNA clearly identified those amino acid residues which had remained inconsistent among different research groups. The base sequence homology with other apoprotein genes of related antibiotics was analyzed and was found to be limited within the structural gene." citations,entry_citation,5345,222661,1,,entry citation,,,12065400,,,"PLASTICITY IN PROTEIN-DNA RECOGNITION: LAC REPRESSOR INTERACTS WITH ITS NATURAL OPERATOR THROUGH ALTERNATIVE CONFORMATIONS OF ITS DNA-BINDING DOMAIN",published,journal,EMBO J.,,21,12,,,,,,,,,,,,,,,,,,,,,,2866,2876,2002, citations,entry_citation,5346,222684,1,,entry citation,,,14661951,,,"Solution Structure of a Novel Disintegrin, Salmosin from Agkistrondon halys Venom",published,journal,Biochemistry,,42,49,,,,,,,,,,,,,,,,,,,,,,14408,14415,2003, citations,entry_citation,5347,222701,1,,entry citation,,22422596,12534276,,,"Solution Structure of the RNase H Domain of the HIV-1 Reverse Transcriptase in the Presence of Magnesium",published,journal,Biochemistry,,42,3,,,,,,,,,,,,,,,,,,,,,,639,650,2003, citations,entry_citation,5348,222729,1,,entry citation,,,,,,"Solution structure of ascidian trypsin inhibitor determined by nuclear magnetic resonance spectroscopy",published,journal,Biochemistry,,41,,,,,,,,,,,,,,,,,,,,,,,10657,10664,2002, citations,entry_citation,5349,222747,1,,entry citation,,,,,,Lock and Key Binding of the HOX YPWM Peptide to the PBX Homeodomain,published,journal,J. Biol. Chem.,,278,,,,,,,,,,,,,,,,,,,,,,,1053,1058,2003, citations,entry_citation,5350,222765,1,,entry citation,,22223355,12238601,,,"Letter to the Editor: 1H, 15N, and 13C Resonance Assignments of Low Molecular Weight Human Cytoplasmic Protein Tyrosine Phosphatase-A (HCPTP-A)",published,journal,J. Biomol. NMR,,23,3,,,,,,,,,,,,,,,,,,,,,,251,252,2002, citations,ref_1,5350,222766,2,,reference citation,,,7727361,,"Logan TM, Zhou MM, Nettesheim DG, Meadows RP, Van Etten RL, Fesik SW. Solution structure of a low molecular weight protein tyrosine phosphatase. Biochemistry. 1994 Sep 20;33(37):11087-96.",Solution structure of a low molecular weight protein tyrosine phosphatase.,published,journal,Biochemistry,Biochemistry,33,37,,0006-2960,,,,,,,,,,,,,,,,,,,,11087,11096,1994,"Protein tyrosine phosphatases (PTPs) are important enzymes involved in signal transduction, cell cycle regulation, and the control of differentiation. Despite the importance of this class of enzymes in the control of critical cell processes, very little structural information is available for this family of proteins. In this paper, we present the first solution structure of a protein tyrosine phosphatase. This protein is a low molecular weight cytosolic PTP that was initially isolated from bovine heart. The structure that was determined from 1747 NMR-derived restraints consists of a central four-stranded parallel beta-sheet surrounded by four alpha-helices and a short 3(10) helix. The phosphate binding site, identified by chemical shift changes upon the addition of the competitive inhibitors phosphate and vanadate, is in a loop region connecting the C-terminal end of the first beta-strand with the first alpha-helix. Residues in the second, fourth, and fifth alpha-helices and in some of the loop regions connecting the elements of regular secondary structure also contribute to the binding site. The structure determined here is consistent with previous mutagenesis and chemical modification studies conducted on this protein." citations,entry_citation,5351,222780,1,,entry citation,,,12441112,,,"Transient Structure Formation in Unfolded Acyl-coenzyme A-binding Protein Observed by Site-directed Spin Labelling",published,journal,J. Mol. Biol.,,324,2,,,,,,,,,,,,,,,,,,,,,,349,357,2002, citations,entry_citation,5352,222802,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N resonance assignment of Bacillus agaradhaerens family 11 xylanase",published,journal,J. Biomol. NMR,,23,4,,,,,,,,,,,,,,,,,,,,,,333,334,2002, citations,ref_1_PubMed,5352,222803,2,,reference citation,,,10381409,,"Sabini E, Sulzenbacher G, Dauter M, Dauter Z, Jorgensen PL, Schulein M, Dupont C, Davies GJ, Wilson KS. Catalysis and specificity in enzymatic glycoside hydrolysis: a 2,5B conformation for the glycosyl-enzyme intermediate revealed by the structure of the Bacillus agaradhaerens family 11 xylanase. Chem Biol. 1999 Jul;6(7):483-92.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5353,222818,1,,entry citation,,,,,,"Letter to the Editor: 1H, 15N and 13C resonance assignments of yeast Saccharomyces cerevisiae calmodulin in the Ca2+-free state",published,journal,J. Biomol. NMR,,23,4,,,,,,,,,,,,,,,,,,,,,,323,324,2002, citations,entry_citation,5354,222845,1,,entry citation,,22266135,12377121,,,"Structure and Interactions of PAS kinase N-terminal PAS domain: Model for Intramolecular Kinase Regulation",published,journal,Structure,,10,10,,,,,,,,,,,,,,,,,,,,,,1349,1361,2002, citations,ref-1,5354,222846,2,,reference citation,,,,,"Johnson, B. A., and Blevins, R.A.(1994), Journal of Biomolecular NMR, 4:603-614.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref1,5374,223257,2,,reference citation,,,12074150,,"Fernandez-Tornero, C., Ramon A., Navarro, M.L., Varela, J. & Gimenez-Gallego (2002) Biotechniques,in press",Synthesis of proteins with disulfide bonds in E. coli using defined culture media.,published,journal,BioTechniques,BioTechniques,32,6,,0736-6205,,,,,,,,,,,,,,,,,,,,1238,1242,2002, citations,entry_citation,5375,223283,1,,entry citation,,22195730,12206780,,,"NMR Structures of Two Variants of Bovine Pancreatic Trypsin Inhibitor (BPTI) reveal Unexpected Influence of Mutations on Protein Structure and Stability",published,journal,J. Mol. Biol.,,321,4,,,,,,,,,,,,,,,,,,,,,,647,658,2002, citations,entry_citation,5376,223301,1,,entry citation,,22206956,12217702,,,"Structure and Orientation of a G Protein Fragment in the Receptor Bound State from Residual Dipolar Couplings",published,journal,J. Mol. Biol.,,322,2,,,,,,,,,,,,,,,,,,,,,,441,461,2002, citations,entry_citation,5377,223322,1,,entry citation,,,,,,"Letter to the Editor: Assignments of 1H, 13C and 15N resonances of human Ca2+-S100B in complex with the TRTK-12 peptide",published,journal,J. Biomol. NMR,,23,3,,,,,,,,,,,,,,,,,,,,,,255,256,2002, citations,entry_citation,5387,223515,1,,entry citation,,,11456950,,,Validation of protein structure from preparations of encapsulated proteins dissolved in low viscosity fluids,published,journal,J. Am. Chem. Soc.,,123,11,,,,,,,,,,,,,,,,,,,,,,2691,2692,2001, citations,ref-2,5354,222847,3,,reference citation,,,8520220,,"F. Delaglio, S. Grzesiek, G. W. Vuister, G. Zhu, J. Pfeifer and A. Bax (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR. 6, 277-293.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,entry_citation,5355,222863,1,,entry citation,,,,,,"Letter to the Editor: Backbone resonance assignments of the 25kD N-terminal ATPase domain from the Hsp90 chaperone",published,journal,J. Biomol. NMR,,23,4,,,,,,,,,,,,,,,,,,,,,,327,328,2002, citations,ref_1,5355,222864,2,,reference citation,,,11868271,,"Pearl LH, Prodromou C. Structure, function, and mechanism of the Hsp90 molecular chaperone. Adv Protein Chem. 2001;59:157-86.","Structure, function, and mechanism of the Hsp90 molecular chaperone.",published,journal,Adv. Protein Chem.,Advances in protein chemistry,59,,,0065-3233,,,,,,,,,,,,,,,,,,,,157,186,2001, citations,ref_2,5355,222865,3,,reference citation,,,9230303,,"Prodromou C, Roe SM, O'Brien R, Ladbury JE, Piper PW, Pearl LH. Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell. 1997 Jul 11;90(1):65-75.",Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone.,published,journal,Cell,Cell,90,1,,0092-8674,,,,,,,,,,,,,,,,,,,,65,75,1997,"Hsp90 molecular chaperones in eukaryotic cells play essential roles in the folding and activation of a range of client proteins involved in cell cycle regulation, steroid hormone responsiveness, and signal transduction. The biochemical mechanism of Hsp90 is poorly understood, and the involvement of ATP in particular is controversial. Crystal structures of complexes between the N-terminal domain of the yeast Hsp90 chaperone and ADP/ATP unambiguously identify a specific adenine nucleotide binding site homologous to the ATP-binding site of DNA gyrase B. This site is the same as that identified for the antitumor agent geldanamycin, suggesting that geldanamycin acts by blocking the binding of nucleotides to Hsp90 and not the binding of incompletely folded client polypeptides as previously suggested. These results finally resolve the question of the direct involvement of ATP in Hsp90 function." citations,entry_citation,5356,222894,1,,entry citation,,22213508,12224922,,,Structure of a De Novo Designed Protein Model of Radical Enzymes,published,journal,J. Am. Chem. Soc.,,124,37,,,,,,,,,,,,,,,,,,,,,,10952,10953,2002, citations,entry_citation,5357,222909,1,,entry citation,,,,,,Structure and fold of tm1112,in preparation,journal,J. Mol. Biol.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5358,222925,1,,entry citation,,,,,,"Structural and Dynamic Investigations of Macromolecular Recognition Processes by Nuclear Magnetic Resonance Spectroscopy",published,thesis,,,,,,,,,,,,,,,,,,,,,,Rutgers University,"Piscataway, NJ",U. S. A.,,,,1996, citations,entry_citation,5359,222938,1,,entry citation,,,,,,"Structural and Dynamic Investigations of Macromolecular Recognition Processes by Nuclear Magnetic Resonance Spectroscopy",published,thesis,,,,,,,,,,,,,,,,,,,,,,Rutgers University,"Piscataway, NJ",U. S. A.,,,,1996, citations,entry_citation,5360,222951,1,,entry citation,,22325495,12437347,,,"Solution NMR Structure and Backbone Dynamics of the PsaE Subunit of the Photosystem I from Synechocystis sp. PCC 6803",published,journal,Biochemistry,,41,47,,,,,,,,,,,,,,,,,,,,,,13902,13914,2002, citations,entry_citation,5361,222971,1,,entry citation,,21605735,11738049,,,Solution Structure of a Telomeric DNA Complex of Human TRF1,published,journal,Structure,,9,12,,,,,,,,,,,,,,,,,,,,,,1237,1251,2001, citations,entry_citation,5362,222991,1,,entry citation,,,,,,"Letter to the Editor: 1H, 15N and 13C Backbone resonance assignments of the 40 kDa LicT-CAT-PRD1 protein",published,journal,J. Biomol. NMR,,23,4,,,,,,,,,,,,,,,,,,,,,,325,326,2002, citations,entry_citation,5363,223017,1,,entry citation,,22541931,12654265,,,"Monomeric Complex of Human Orphan Estrogen Related Receptor 2 with DNA: A Pseudo-dimer Interface Mediates Extended Half-site Recognition",published,journal,J. Mol. Biol.,,327,4,,,,,,,,,,,,,,,,,,,,,,819,832,2003, citations,entry_citation,5364,223055,1,,entry citation,,,11875519,,,Structure of the C-terminal FG-nucleoporin binding domain of Tap/NXF1,published,journal,Nat. Struct. Biol.,,9,4,,,,,,,,,,,,,,,,,,,,,,247,251,2002, citations,entry_citation,5365,223074,1,,entry citation,,,,,,"Letters to the Editor: 1H, 15N, 13C resonance assignments for the DNA-binding domain of myocyte nuclear factor (Foxk1)",published,journal,J. Biomol. NMR,,24,1,,,,,,,,,,,,,,,,,,,,,,75,76,2002, citations,entry_citation,5366,223104,1,,entry citation,,21989951,11993989,,,Solution Structure of the Vam7P PX Domain,published,journal,Biochemistry,,41,19,,,,,,,,,,,,,,,,,,,,,,5956,5962,2002, citations,ref_1,5382,223424,2,,reference citation,,,11418136,,"Stauffer, M.E., Young, J.K., Helms, G.L.., and Evans, J.N.S. FEBS Letters 499 (2001), 182-186.",Chemical shift mapping of shikimate-3-phosphate binding to the isolated N-terminal domain of 5-enolpyruvylshikimate-3-phosphate synthase.,published,journal,FEBS Lett.,FEBS letters,499,1-2,,0014-5793,,,,,,,,,,,,,,,,,,,,182,186,2001,"To facilitate evaluation of enzyme-ligand complexes in solution, we have isolated the 26-kDa N-terminal domain of 5-enolpyruvylshikimate-3-phosphate (EPSP) synthase for analysis by NMR spectroscopy. The isolated domain is capable of binding the substrate shikimate-3-phosphate (S3P), and this letter reports the localization of the S3P binding site using chemical shift mapping. Based on the NMR data, we propose that Ser23, Arg27, Ser197, and Tyr200 are directly involved in S3P binding. We also describe changes in the observed nuclear Overhauser effects (NOEs) that are consistent with a partial conformational change in the N-terminal domain upon S3P binding." citations,entry_citation,5383,223437,1,,entry citation,,22163955,12173928,,,The CXCR3 Binding Chemokine IP-10/CXCL10: Structure and Receptor Interactions,published,journal,Biochemistry,,41,33,,,,,,,,,,,,,,,,,,,,,,10418,10425,2002, citations,entry_citation,5384,223452,1,,entry citation,,22358980,12270941,,,"Ferric Ions are Essential for the Biological Activity of the Hormone Glycine-extended Gastrin",published,journal,J. Biol. Chem.,,277,50,,,,,,,,,,,,,,,,,,,,,,48602,48609,2002, citations,ref_1,5366,223105,2,,reference citation,,,11993989,,"Lu J., Garcia J., Dulubova I, Sudhof TC, Rizo J. Solution structure of the Vam7p PX Domain Biochemistry, 2002 May 14:41(19):5956-62",Solution structure of the Vam7p PX domain.,published,journal,Biochemistry,Biochemistry,41,19,,0006-2960,,,,,,,,,,,,,,,,,,,,5956,5962,2002,"PX domains have been recently found to act as phosphoinositide binding modules. In the yeast SNARE protein Vam7p, the PX domain binds to PtdIns(3)P and is required for vacuolar targeting. To gain insight into how PX domains function, the solution structure of the ligand-free Vam7p PX domain has been determined by NMR spectroscopy. The Vam7p PX domain has the same overall alpha/beta fold observed in the structures of the ligand-free p47(phox) PX domain and the PtdIns(3)P-bound p40(phox) PX domain, exhibiting several similarities and differences with these two PX domains. Most striking is the similarity between the Vam7p and p40(phox) PX domains in a subset of secondary structure elements despite the low level of sequence identity between them, suggesting that these elements form a conserved core in the PX domain fold. These similarities and the observation that a putative PtdIns(3)P binding site is already formed in the apo Vam7p PX domains suggest that ligand binding does not induce major conformational changes, contrary to what was previously thought. The proposed ligand binding site of the Vam7p PX domain includes basic side chains from the conserved structural core that also participate in PtdIns(3)P binding to the p40(phox) PX domain, and basic side chains from a variable loop that probably inserts into the membrane. These results indicate that PX domains contain a combination of conserved and variable features that allow them to have a common function and at the same time exhibit distinct specificities, mechanisms of regulation, or modes of interaction with effector molecules." citations,entry_citation,5368,223127,1,,entry citation,,22223356,12238602,,,"Letter to the Editor: 1H, 15N, and 13C Assignments of Full Length Human ADP Ribosylation Factor 1 (ARF1) using Triple Resonance Connectivities and Dipolar Couplings",published,journal,J. Biomol. NMR,,23,3,,,,,,,,,,,,,,,,,,,,,,253,254,2002, citations,entry_citation,5369,223145,1,,entry citation,,,12015147,,,"A New Zinc Binding Fold Underlines the Versatility of Zinc Binding Modules in Protein Evolution",published,journal,Structure,,10,5,,,,,,,,,,,,,,,,,,,,,,636,648,2002, citations,entry_citation,537,223169,1,,entry citation,,,,,"Hunkapiller, Michael W., Forgac, Michael D., Yu, Ellen Ho, Richards, John H., ""13C NMR Studies of the Binding of Soybean Trypsin Inhibitor to Trypsin,"" Biochem. Biophys. Res. Commun. 87 (1), 25-31 (1979).",13C NMR Studies of the Binding of Soybean Trypsin Inhibitor to Trypsin,published,journal,Biochem. Biophys. Res. Commun.,,87,1,,,,,,,,,,,,,,,,,,,,,,25,31,1979, citations,entry_citation,5370,223182,1,,entry citation,,,12079334,,,"Structure of a Beta-Alanine-Linked Polyamide Bound to a Full Helical Turn of Purine Tract DNA in the 1:1 Motif",published,journal,J. Mol. Biol.,,320,1,,,,,,,,,,,,,,,,,,,,,,55,71,2002, citations,entry_citation,5371,223207,1,,entry citation,,,11992125,,,"Metal binding and base ionization in the U6 RNA intramolecular stem-loop structure",published,journal,Nat. Struct. Biol.,,9,6,,,,,,,,,,,,,,,,,,,,,,431,435,2002, citations,entry_citation,5372,223220,1,,entry citation,,22648577,12764601,,,"Structure-function Relationship of Reduced Cytochrome c Probed by Complete Solution Structure Determination in 30% Acetonitrile/Water Solution",published,journal,J. Biol. Inorg. Chem.,Journal of Biological Inorganic Chemistry,8,,,,,,,,,,,,,,,,,,,,,,,527,539,2003, citations,ref_1,5372,223221,2,,reference citation,,,2539854,,"Wand, A. J.; Stefano, D. L. D. Biochemistry 1989, 28, 186-194.",Proton resonance assignments of horse ferrocytochrome c.,published,journal,Biochemistry,Biochemistry,28,1,,0006-2960,,,,,,,,,,,,,,,,,,,,186,194,1989,"Two-dimensional nuclear magnetic resonance (NMR) spectroscopy was used to assign the proton resonances of horse ferrocytochrome c. Assignments were based on the main chain directed (MCD) and sequential assignment procedures. The fundamental units of the MCD approach, the main-chain NH-C alpha H-C beta H J-coupled subspin systems of each amino acid residue (NAB sets), were defined by analysis of direct and relayed coherence transfer spectra. Recognition of main-chain NOE connectivity patterns specified in the MCD algorithm then allowed NAB sets to be aligned in their proper juxtaposition within secondary structural units. The units of secondary structure were placed within the polypeptide sequence of identification of a small number of side-chain J-coupled spin systems, found by direct recognition in 2D spectra of some J-coupled spin systems and by pairwise comparisons of the J-correlated spectra of six homologous cytochromes c having a small number of known amino acid differences. The placement of a given segment in this way defines the amino acid identity of all its NAB sets. This foreknowledge allowed the vast majority of the side-chain resonances to be discerned in J-correlated spectra. Extensive confirmation of the assignments derives internally from multiple main-chain NOE connectivities and their consistency following temperature-induced changes of the chemical shifts of NOE-correlated protons. The observed patterns of main-chain NOEs provide some structural information and suggest small but potentially significant differences between the solution structure observed by NMR and that defined earlier in crystallographic studies at 2.8-A resolution." citations,ref_2,5372,223222,3,,reference citation,,,10499099,,"Banci, L.; Bertini, I.; Huber, J. G.; Spyroulias, G. A.; Turano, P. J. Biol. Inorg. Chem. 1999, 4, 21-31.",Solution structure of reduced horse heart cytochrome c.,published,journal,J. Biol. Inorg. Chem.,Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry,4,1,,0949-8257,,,,,,,,,,,,,,,,,,,,21,31,1999,"In the frame of a broad study on the structural differences between the two redox forms of cytochromes to be related to the electron transfer process, the NMR solution structure of horse heart cytochrome c in the reduced form has been determined. The structural data obtained in the present work are compared to those already available in the literature on the same protein and the presence of conformational differences is discussed in the light of the experimental method employed for the structure determination. Redox-state dependent changes are analyzed and in particular they are related to the role of propionate-7 of the heme. Also some hydrogen bonds are changed upon reduction of the heme iron. A substantial similarity is observed for the backbone fold, independently of the oxidation state. At variance, some meaningful differences are observed in the orientation of a few side chains. These changes are related to those found in the case of the highly homologous cytochrome c from Saccharomyces cerevisiae. The exchangeability of the NH protons has been investigated and found to be smaller than in the case of the oxidized protein. We think that this is a characteristic of reduced cytochromes and that mobility is a medium for molecular recognition in vivo." citations,entry_citation,5373,223242,1,,entry citation,,,,,,"Letter to the Editor: Sequence-specific NMR resonance assignments for Human Interleukin-5",published,journal,J. Biomol. NMR,,23,4,,,,,,,,,,,,,,,,,,,,,,329,330,2002, citations,entry_citation,5374,223256,1,,entry citation,,,,,,"Letter to the Editor: Assignment of 1H and 15N resonances and secondary structure of the recombinant RicC3 of 2S albumin storage protein from ricinus communis",published,journal,J. Biomol. NMR,,23,4,,,,,,,,,,,,,,,,,,,,,,331,332,2002, citations,reference_1,5377,223323,2,,reference citation,,,9519411,,"Smith SP, Shaw GS. A novel calcium-sensitive switch revealed by the structure of human S100B in the calcium-bound form. Structure. 1998 Feb 15;6(2):211-22.",A novel calcium-sensitive switch revealed by the structure of human S100B in the calcium-bound form.,published,journal,Structure,"Structure (London, England : 1993)",6,2,,0969-2126,,,,,,,,,,,,,,,,,,,,211,222,1998,"BACKGROUND: S100B is a homodimeric member of the EF-hand calcium-binding protein superfamily. The protein has been implicated in cellular processes such as cell differentiation and growth, plays a role in cytoskeletal structure and function, and may have a role in neuropathological diseases, such as Alzheimers. The effects of S100B are mediated via its interaction with target proteins. While several studies have suggested that this interaction is propagated through a calcium-induced conformational change, leading to the exposure of a hydrophobic region of S100B, the molecular details behind this structural alteration remain unclear. RESULTS: The solution structure of calcium-saturated human S100B (Ca(2+)-S100B) has been determined by heteronuclear NMR spectroscopy. Ca(2+)-S100B forms a well defined globular structure comprising four EF-hand calcium-binding sites and an extensive hydrophobic dimer interface. A comparison of Ca(2+)-S100B with apo S100B and Ca(2+)-calbindin D9k indicates that while calcium-binding to S100B results in little change in the site I EF-hand, it induces a backbone reorientation of the N terminus of the site II EF-hand. This reorientation leads to a dramatic change in the position of helix III relative to the other helices. CONCLUSIONS: The calcium-induced reorientation of calcium-binding site II results in the increased exposure of several hydrophobic residues in helix IV and the linker region. While following the general mechanism of calcium modulatory proteins, whereby a hydrophobic target site is exposed, the 'calcium switch' observed in S100B appears to be unique from that of other EF-hand proteins and may provide insights into target specificity among calcium modulatory proteins." citations,reference_2,5377,223324,3,,reference citation,,,8520220,,"Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR. 1995 Nov;6(3):277-93.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,reference_3,5377,223325,4,,reference citation,,,,,"Garrett, D.S., Powers, R., Gronenborn, A.M., Clore, G.M. (1991) J. Mag. Res. 95:214-220""",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5378,223350,1,,entry citation,,22435922,12547204,,,NMR Structure of a Variant Human Prion Protein with Two Disulfide Bridges,published,journal,J. Mol. Biol.,,326,1,,,,,,,,,,,,,,,,,,,,,,225,234,2003, citations,entry_citation,5379,223372,1,,entry citation,,22255077,12367532,,,"Bovine Pancreatic Polypeptide (bPP) undergoes Significant changes in Conformation and Dynamics upon Binding to DPC Micelles",published,journal,J. Mol. Biol.,,322,5,,,,,,,,,,,,,,,,,,,,,,1117,1133,2002, citations,ref_1,5379,223373,2,,reference citation,,,,,"Bartels, C., Xia, T.-h., Billeter, M., Guntert, P. & Wuthrich, K. (1995). The program XEASY for computer-supported spectral analysis of biological macromolecules. J. Biomol. NMR 6, 1-10.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_2,5379,223374,3,,reference citation,,,,,"Weiner, P. K., Kollman, P. A., Nguyen, D. T. & Case, D. A. (1986). An all-atom force field for simulations of proteins and nucleic acids. J. Comput. Chem. 7, 230-52.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_3,5379,223375,4,,reference citation,,,9367762,,"Guntert, P., Mumenthaler, C. & Wuthrich, K. (1997). Torsion Angle Dynamics For NMR Structure Calculation With the New Program Dyana. J. Mol. Biol. 273, 283-298.",Torsion angle dynamics for NMR structure calculation with the new program DYANA.,published,journal,J. Mol. Biol.,Journal of molecular biology,273,1,,0022-2836,,,,,,,,,,,,,,,,,,,,283,298,1997,"The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from distance constraints and torsion angle constraints collected by nuclear magnetic resonance (NMR) experiments performs simulated annealing by molecular dynamics in torsion angle space and uses a fast recursive algorithm to integrate the equations of motions. Torsion angle dynamics can be more efficient than molecular dynamics in Cartesian coordinate space because of the reduced number of degrees of freedom and the concomitant absence of high-frequency bond and angle vibrations, which allows for the use of longer time-steps and/or higher temperatures in the structure calculation. It also represents a significant advance over the variable target function method in torsion angle space with the REDAC strategy used by the predecessor program DIANA. DYANA computation times per accepted conformer in the ""bundle"" used to represent the NMR structure compare favorably with those of other presently available structure calculation algorithms, and are of the order of 160 seconds for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300 computer. Test calculations starting from conformers with random torsion angle values further showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures." citations,entry_citation,538,223393,1,,entry citation,,,,,"Hunkapiller, Michael W., Forgac, Michael D., Yu, Ellen Ho, Richards, John H., ""13C NMR Studies of the Binding of Soybean Trypsin Inhibitor to Trypsin,"" Biochem. Biophys. Res. Commun. 87 (1), 25-31 (1979).",13C NMR Studies of the Binding of Soybean Trypsin Inhibitor to Trypsin,published,journal,Biochem. Biophys. Res. Commun.,,87,1,,,,,,,,,,,,,,,,,,,,,,25,31,1979, citations,entry_citation,5381,223406,1,,entry citation,,22195730,12206780,,,"NMR Structures of Two Variants of Bovine Pancreatic Trypsin Inhibitor (BPTI) reveal Unexpected Influence of Mutations on Protein Structure and Stability",published,journal,J. Mol. Biol.,,321,4,,,,,,,,,,,,,,,,,,,,,,647,658,2002, citations,entry_citation,5382,223423,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C, and 15N backbone resonance assignments of the C-terminal domain of 5'-enolpyruvylshikimate-3-phosphate synthase",published,journal,J. Biomol. NMR,,24,3,,,,,,,,,,,,,,,,,,,,,,269,270,2002, citations,entry_citation,5385,223466,1,,entry citation,,22387755,12498794,,,"Solution Structure of a DNA Duplex containing 8-hydroxy-2'-deoxyguanosine Opposite Deoxyguanosine",published,journal,J. Mol. Biol.,,325,3,,,,,,,,,,,,,,,,,,,,,,433,442,2003, citations,entry_citation,5388,223537,1,,entry citation,,,,,,"Letter to the Editor: 1H,13C and 15N resonance assignments of Gads C-terminal SH3 domain in complex with an RXXK motif-containing peptide derived from SLP-76",published,journal,J. Biomol. NMR,,24,2,,,,,,,,,,,,,,,,,,,,,,161,162,2002, citations,ref_1,5388,223538,2,,reference citation,,,8589602,,"Wishart DS, Bigam CG, Yao J, Abildgaard F, Dyson HJ, Oldfield E, Markley JL, SykesBD. 1H, 13C and 15N chemical shift referencing in biomolecular NMR. J. Biomol. NMR, 6 (1995) 135-140.","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,5389,223564,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N resonance assignments of the ribosome-associated cold shock response protein Yfia of Escherichia coli",published,journal,J. Biomol. NMR,,23,4,,,,,,,,,,,,,,,,,,,,,,335,336,2002, citations,entry_citation,539,223595,1,,entry citation,,,,,"Hunkapiller, Michael W., Forgac, Michael D., Yu, Ellen Ho, Richards, John H., ""13C NMR Studies of the Binding of Soybean Trypsin Inhibitor to Trypsin,"" Biochem. Biophys. Res. Commun. 87 (1), 25-31 (1979).",13C NMR Studies of the Binding of Soybean Trypsin Inhibitor to Trypsin,published,journal,Biochem. Biophys. Res. Commun.,,87,1,,,,,,,,,,,,,,,,,,,,,,25,31,1979, citations,entry_citation,5390,223608,1,,entry citation,,22349943,12460581,,,"H-NS Oligomerization Domain Structure Reveals the Mechanism for High Order Self-association of the Intact Protein",published,journal,J. Mol. Biol.,,324,4,,,,,,,,,,,,,,,,,,,,,,841,850,2002, citations,entry_citation,5391,223629,1,,entry citation,,21348196,11453696,,,"Solution Structure of the Tumor Necrosis Factor Receptor-1 Death Domain",published,journal,J. Mol. Biol.,,310,4,,,,,,,,,,,,,,,,,,,,,,895,906,2001, citations,entry_citation,5392,223647,1,,entry citation,,,12590579,,,"Solution structure and DNA binding property of the fifth HMG box domain in comparison with the first HMG box domain in human upstream binding factor",published,journal,Biochemistry,,42,7,,,,,,,,,,,,,,,,,,,,,,1930,1938,2003, citations,entry_citation,5393,223666,1,,entry citation,,,,,,"Letter to the Editor: Sequence-specific (1H, 15N, 13C) resonance assignment of the N-terminal domain of the Cyclase-associated Protein (CAP) from Dictyostelium discoideum",published,journal,J. Biomol. NMR,,23,4,,,,,,,,,,,,,,,,,,,,,,337,338,2002, citations,entry_citation,5394,223691,1,,entry citation,,22337323,12426583,,,"Sculpting of the Spliceosomal Branch Site Recognition Motif by a Conserved Pseudouridine",published,journal,Nat. Struct. Biol.,,9,12,,,,,,,,,,,,,,,,,,,,,,958,965,2002, citations,entry_citation,5395,223712,1,,entry citation,,22337323,12426583,,,"Sculpting of the Spliceosomal Branch Site Recognition Motif by a Conserved Pseudouridine",published,journal,Nat. Struct. Biol.,,9,12,,,,,,,,,,,,,,,,,,,,,,958,965,2002, citations,entry_citation,5396,223735,1,,entry citation,,,,,,"Letters to the Editor: NMR-based solution structure of the complex of Lactobacillus casei dihydrofolate reductase with trimethoprim and NADPH",published,journal,J. Biomol. NMR,,24,1,,,,,,,,,,,,,,,,,,,,,,67,70,2002, citations,entry_citation,5397,223773,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N resonance assignments of an affibody-target complex",published,journal,J. Biomol. NMR,,24,3,,,,,,,,,,,,,,,,,,,,,,271,272,2002, citations,entry_citation,5398,223804,1,,entry citation,,22186946,12161745,,,"3-Methyladenine DNA Glycosylase I is an Unexpected Helix-hairpin-helix Superfamily Member",published,journal,Nat. Struct. Biol.,,9,9,,,,,,,,,,,,,,,,,,,,,,659,664,2002, citations,entry_citation,5399,223824,1,,entry citation,,,,,,"Letters to the Editor: New NMR assignments chemical shift and secondary structure conservation of the PNT/SAM domains from the Ets family of transcription factors",published,journal,J. Biomol. NMR,,24,1,,,,,,,,,,,,,,,,,,,,,,71,72,2002, citations,entry_citation,540,223851,1,,entry citation,,,,,"Hunkapiller, Michael W., Forgac, Michael D., Yu, Ellen Ho, Richards, John H., ""13C NMR Studies of the Binding of Soybean Trypsin Inhibitor to Trypsin,"" Biochem. Biophys. Res. Commun. 87 (1), 25-31 (1979).",13C NMR Studies of the Binding of Soybean Trypsin Inhibitor to Trypsin,published,journal,Biochem. Biophys. Res. Commun.,,87,1,,,,,,,,,,,,,,,,,,,,,,25,31,1979, citations,entry_citation,5400,223864,1,,entry citation,,,12898626,,,"Selection of D-amino-acid peptides that bind to Alzheimer's disease amyloid peptide abeta 1-42 by mirror image phage display",published,journal,ChemBioChem,,4,8,,,,,,,,,,,,,,,,,,,,,,748,753,2003, citations,entry_citation,5401,223880,1,,entry citation,,22333295,12449421,,,"Chemical Shift and Secondary Structure Conservation of the PNT/SAM Domains from the ets Family of Transcription Factors",published,journal,J. Biomol. NMR,,24,1,,,,,,,,,,,,,,,,,,,,,,71,72,2002, citations,entry_citation,5402,223904,1,,entry citation,,,,,,"Letter to the Editor: 1H, 15N and 13C resonance assignments of the SH2 domain of Bruton's tyrosine kinase",published,journal,J. Biomol. NMR,,24,2,,,,,,,,,,,,,,,,,,,,,,163,164,2002, citations,entry_citation,5403,223917,1,,entry citation,,22269622,12381302,,,"TROSY-NMR Studies of the 91 kDa TRAP Protein reveal Allosteric Control of a Gene Regulatory Protein by Ligand-altered Flexibility",published,journal,J. Mol. Biol.,,323,3,,,,,,,,,,,,,,,,,,,,,,463,473,2002, citations,ref_1,5403,223918,2,,reference citation,,,7525975,,"Antson, A. A., Brzozowski, A. M., Dodson, E. J., Dauter, Z., Wilson, K. S., Kurecki, T., Otridge, J. & Gollnick, P. (1994). J. Mol. Biol. 244, 1-5.",11-fold symmetry of the trp RNA-binding attenuation protein (TRAP) from Bacillus subtilis determined by X-ray analysis.,published,journal,J. Mol. Biol.,Journal of molecular biology,244,1,,0022-2836,,,,,,,,,,,,,,,,,,,,1,5,1994,"The trp RNA-binding attenuation protein (TRAP) of Bacillus subtilis has been crystallized and examined by crystallography using X-ray synchrotron radiation diffraction data. Crystals of TRAP complexed with L-tryptophan belong to space group C2 with a = 156.8 A, b = 114.05 A, c = 105.9 A, beta = 118.2 degrees. Crystals of a potential heavy-atom derivative of TRAP complexed with 5-bromo-L-tryptophan grow in the same space group with similar cell dimensions. X-ray data for the native crystals and for the derivative have been collected to 2.9 A and 2.2 A resolution, respectively. Peaks in the self-rotation function and in the Patterson synthesis could only be explained by two 11-subunit oligomers (each formed by an 11-fold axis of symmetry) in the asymmetric unit lying with the 11-fold rotation axes parallel to each other. The consequence is that the TRAP molecule has 11-fold symmetry and contains 11 subunits." citations,entry_citation,5411,224133,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5559,227204,1,,entry citation,,,,,,NMR Structure of the 3' Stem-Loop from Human U4 snRNA,published,journal,Nucleic Acids Res.,,30,20,,,,,,,,,,,,,,,,,,,,,,4371,4379,2002, citations,ref_2,5403,223919,3,,reference citation,,,10499579,,"Antson, A. A., Dodson, E. J., Dodson, G., Greaves, R. B., Chen, X. & Gollnick, P. (1999). Nature 401, 235-42.","Structure of the trp RNA-binding attenuation protein, TRAP, bound to RNA.",published,journal,Nature,Nature,401,6750,,0028-0836,,,,,,,,,,,,,,,,,,,,235,242,1999,"The trp RNA-binding attenuation protein (TRAP) regulates expression of the tryptophan biosynthetic genes of several bacilli by binding single-stranded RNA. The binding sequence is composed of eleven triplet repeats, predominantly GAG, separated by two or three non-conserved nucleotides. Here we present the crystal structure of a complex of TRAP and a 53-base single-stranded RNA containing eleven GAG triplets, revealing that each triplet is accommodated in a binding pocket formed by beta-strands. In the complex, the RNA has an extended structure without any base-pairing and binds to the protein mostly by specific protein-base interactions. Eleven binding pockets on the circular TRAP 11-mer form a belt with a diameter of about 80 A. This simple but elegant mechanism of arresting the RNA segment by encircling it around a protein disk is applicable to both transcription, when TRAP binds the nascent RNA, and to translation, when TRAP binds the same sequence within a non-coding leader region of the messenger RNA." citations,ref_3,5403,223920,4,,reference citation,,,7715723,,"Antson, A. A., Otridge, J., Brzozowski, A. M., Dodson, E. J., Dodson, G. G., Wilson, K. S., Smith, T. M., Yang, M., Kurecki, T. & Gollnick, P. (1995). Nature 374, 693-700.",The structure of trp RNA-binding attenuation protein.,published,journal,Nature,Nature,374,6524,,0028-0836,,,,,,,,,,,,,,,,,,,,693,700,1995,"The crystal structure of the trp RNA-binding attenuation protein of Bacclius subtilis solved at 1.8 A resolution reveals a novel structural arrangement in which the eleven subunits are stabilized through eleven intersubunit beta-sheets to form a beta-wheel with a large central hole. The nature of the binding of L-tryptophan in clefts between adjacent beta-sheets in the beta-wheel suggests that this binding induces conformational changes in the flexible residues 25-33 and 49-52. It is argued that upon binding, the messenger RNA target forms a matching circle in which eleven U/GAG repeats are bound to the surface of the protein ondecamer modified by the binding of L-tryptophan." citations,ref_4,5403,223921,5,,reference citation,,,9383185,,"Babitzke, P. (1997). Mol. Microbiol. 26, 1-9.",Regulation of tryptophan biosynthesis: Trp-ing the TRAP or how Bacillus subtilis reinvented the wheel.,published,journal,Mol. Microbiol.,Molecular microbiology,26,1,,0950-382X,,,,,,,,,,,,,,,,,,,,1,9,1997,"The Bacillus subtilis tryptophan biosynthetic genes are regulated by TRAP. Radiographic crystallography indicates that the TRAP complex contains 11 identical subunits arranged in a doughnut-like structure termed the beta-wheel. The trpEDCFBA operon is regulated by an attenuation mechanism in which tryptophan-activated TRAP binds to 11 (G/U)AG repeats in the trp leader transcript. TRAP binding blocks formation of an anti-terminator structure, thereby promoting the formation of an overlapping terminator, resulting in transcription termination preceding the structural genes. When TRAP is not activated, it is unable to bind to the transcript, which allows anti-terminator formation and, hence, transcription of the operon. TRAP is also responsible for regulating translation of trpEand trpG. TRAP binding to trp operon readthrough transcripts promotes refolding of the RNA such that the trpE Shine-Dalgarno sequence is sequestered in a hairpin, thus inhibiting TrpE synthesis. In the case of trpG, TRAP binds to nine repeats that overlap the ribosome-binding site, thereby blocking translation." citations,ref_5,5403,223922,6,,reference citation,,,,,"Cavanagh, J. (1996). Protein NMR spectroscopy : principles and practice, Academic Press, San Diego.",,published,book,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_6,5403,223923,7,,reference citation,,,10369778,,"Chen, X., Antson, A. A., Yang, M., Li, P., Baumann, C., Dodson, E. J., Dodson, G. G. & Gollnick, P. (1999). J. Mol. Biol. 289, 1003-16.",Regulatory features of the trp operon and the crystal structure of the trp RNA-binding attenuation protein from Bacillus stearothermophilus.,published,journal,J. Mol. Biol.,Journal of molecular biology,289,4,,0022-2836,,,,,,,,,,,,,,,,,,,,1003,1016,1999,"Characterization of both the cis and trans -acting regulatory elements indicates that the Bacillus stearothermophilustrp operon is regulated by an attenuation mechanism similar to that which controls the trp operon in Bacillus subtilis. Secondary structure predictions indicate that the leader region of the trp mRNA is capable of folding into terminator and anti- terminator RNA structures. B. stearothermophilus also encodes an RNA-binding protein with 77% sequence identity with the RNA-binding protein (TRAP) that regulates attenuation in B. subtilis. The X-ray structure of this protein has been determined in complex with L-tryptophan at 2.5 A resolution. Like the B. subtilis protein, B. stearothermophilus TRAP has 11 subunits arranged in a ring-like structure. The central cavities in these two structures have different sizes and opposite charge distributions, and packing within the B. stearothermophilus TRAP crystal form does not generate the head-to-head dimers seen in the B. subtilis protein, suggesting that neither of these properties is functionally important. However, the mode of L-tryptophan binding and the proposed RNA binding surfaces are similar, indicating that both proteins are activated by l -tryptophan and bind RNA in essentially the same way. As expected, the TRAP:RNA complex from B. stearothermophilus is significantly more thermostable than that from B. subtilis, with optimal binding occurring at 70 degrees C." citations,ref_7,5403,223924,8,,reference citation,,,7836324,,"Hoffman, R. J. & Gollnick, P. (1995). J. Bacteriol. 177, 839-42.",The mtrB gene of Bacillus pumilus encodes a protein with sequence and functional homology to the trp RNA-binding attenuation protein (TRAP) of Bacillus subtilis.,published,journal,J. Bacteriol.,Journal of bacteriology,177,3,,0021-9193,,,,,,,,,,,,,,,,,,,,839,842,1995,"The mtrB gene from Bacillus pumilus encodes a 76-amino-acid polypeptide with 77% identity to the trp RNA-binding attenuation protein (TRAP) from Bacillus subtilis. B. pumilus TRAP binds trp leader RNA from either B. subtilis or B. pumilus in a tryptophan-dependent manner. Altering threonine 52 to alanine eliminated RNA-binding activity of B. pumilus TRAP." citations,entry_citation,5412,224147,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5413,224161,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5414,224175,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5415,224189,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,ref_8,5403,223925,9,,reference citation,,,3133360,,"Kuroda, M. I., Henner, D. & Yanofsky, C. (1988). J. Bacteriol. 170, 3080-8.",cis-acting sites in the transcript of the Bacillus subtilis trp operon regulate expression of the operon.,published,journal,J. Bacteriol.,Journal of bacteriology,170,7,,0021-9193,,,,,,,,,,,,,,,,,,,,3080,3088,1988,"Transcription of the trp operon of Bacillus subtilis is regulated by attenuation. A trpE'-'lacZ gene fusion preceded by the wild-type trp promoter-leader region was used to analyze regulation. Overproduction of the trp leader transcript in trans from a multicopy plasmid caused constitutive expression of the chromosomal trpE'-'lacZ fusion, presumably by titrating a negative regulatory factor encoded by the mtr locus. Subsegments of the trp leader region cloned onto the multicopy plasmid were examined for their abilities to elevate beta-galactosidase activity. An RNA segment spanning the portion of the leader transcript that forms the promoter-proximal strand of the proposed antiterminator structure was most active in this trans test. The data suggest that the mtr gene product, when activated by tryptophan, binds to this RNA segment and prevents formation of the antiterminator. In this manner, the trans-acting factor promotes formation of the RNA structure that causes transcription termination. Secondary-structure predictions for the leader segment of the trp operon transcript suggest that if the mtr factor bound this RNA segment in a nonterminated transcript, the ribosome-binding site for the first structural gene, trpE, could be sequestered in a stable RNA structure. We tested this possibility by comparing transcriptional and translational fusions containing the initial segments of the trp operon. Our findings suggest that the mtr product causes both transcription attenuation and inhibition of translation of trpE mRNA. Inhibition of translation initiation would reduce ribosome density on trpE mRNA, perhaps making it more labile. Consistent with this interpretation, the addition of tryptophan to mtr+ cultures increased the rate of trpE'-'lacZ mRNA decay." citations,ref_9,5403,223926,10,,reference citation,,,9811843,,"Salzmann, M., Pervushin, K., Wider, G., Senn, H. & Wuthrich, K. (1998). Proc. Natl. Acad. Sci. U. S. A. 95, 13585-90.",TROSY in triple-resonance experiments: new perspectives for sequential NMR assignment of large proteins.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,95,23,,0027-8424,,,,,,,,,,,,,,,,,,,,13585,13590,1998,"The NMR assignment of 13C, 15N-labeled proteins with the use of triple resonance experiments is limited to molecular weights below approximately 25,000 Daltons, mainly because of low sensitivity due to rapid transverse nuclear spin relaxation during the evolution and recording periods. For experiments that exclusively correlate the amide proton (1HN), the amide nitrogen (15N), and 13C atoms, this size limit has been previously extended by additional labeling with deuterium (2H). The present paper shows that the implementation of transverse relaxation-optimized spectroscopy ([15N,1H]-TROSY) into triple resonance experiments results in several-fold improved sensitivity for 2H/13C/15N-labeled proteins and approximately twofold sensitivity gain for 13C/15N-labeled proteins. Pulse schemes and spectra recorded with deuterated and protonated proteins are presented for the [15N, 1H]-TROSY-HNCA and [15N, 1H]-TROSY-HNCO experiments. A theoretical analysis of the HNCA experiment shows that the primary TROSY effect is on the transverse relaxation of 15N, which is only little affected by deuteration, and predicts sensitivity enhancements that are in close agreement with the experimental data." citations,ref_10,5403,223927,11,,reference citation,,,10605091,,"Salzmann, M., Wider, G., Pervushin, K. & Wuthrich, K. (1999). J. Biomol. NMR 15, 181-4.","Improved sensitivity and coherence selection for [15N,1H]-TROSY elements in triple resonance experiments.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,15,2,,0925-2738,,,,,,,,,,,,,,,,,,,,181,184,1999,"In experiments with proteins of molecular weights around 100 kDa the implementation of [15N,1H]-TROSY-elements in [15N]-constant-time triple resonance experiments yields sensitivity enhancements of one to two orders of magnitude. An additional gain of 10 to 20% may be obtained with the use of 'sensitivity enhancement elements'. This paper describes a novel sensitivity enhancement scheme which is based on concatenation of the 13C alpha-->15N magnetization transfer with the ST2-PT element, and which enables proper TROSY selection of the 15N multiplet components." citations,ref_11,5403,223928,12,,reference citation,,,11914485,,"Hopcroft NH, Wendt AL, Gollnick P, Antson AA. Specificity of TRAP-RNA interactions: crystal structures of two complexes with different RNA sequences. Acta Crystallogr D Biol Crystallogr. 2002 Apr;58(Pt 4):615-21.",Specificity of TRAP-RNA interactions: crystal structures of two complexes with different RNA sequences.,published,journal,Acta Crystallogr. D Biol. Crystallogr.,"Acta crystallographica. Section D, Biological crystallography",58,Pt 4,,0907-4449,,,,,,,,,,,,,,,,,,,,615,621,2002,"The trp RNA-binding attenuation protein (TRAP) regulates expression of the tryptophan biosynthetic genes in bacilli by binding to the leader region of the nascent trp operon mRNA. When activated by binding tryptophan, the 11-subunit circular TRAP molecule binds to a target sequence consisting of 11 (G/U)AG repeats, separated by two or three variable 'spacer' nucleotides. Reported here are two crystal structures of TRAP bound to RNAs containing 11 GAG repeats separated by UU and CC spacer nucleotides, determined at 1.75 and 2.50 A resolution, respectively. These show the spacer regions of the RNA molecules to be highly flexible, making no direct hydrogen-bonding contacts with the protein. Comparison of these structures with the previous structure of TRAP bound to (GAGAU)(10)GAG RNA, in which the spacer nucleotides stack with each other close to the protein surface, shows that the RNA can adopt different conformations depending on the sequence of the spacer regions. This gives insight into the structural basis of the specificity of TRAP and into the mechanism of binding." citations,entry_citation,5404,223944,1,,entry citation,,,12070337,,,Mapping the surface of Escherichia coli peptide deformylase by NMR with organic solvents.,published,journal,Protein Sci.,,11,7,,,,,,,,,,,,,,,,,,,,,,1850,1853,2002, citations,entry_citation,5405,223975,1,,entry citation,,,,,,"Structural duality of a peptide fragment from sheep prion protein spanning helix 1 and beta-strand 2: a potential nucleation site for conformational transition to PrPSc",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5406,223996,1,,entry citation,,22564832,12678434,,,"Expression and Characterization of Recombinant Human Cytochrome c in E. coli",published,journal,J. Bioenerg. Biomembr.,,34,,,,,,,,,,,,,,,,,,,,,,,423,431,2002, citations,entry_citation,5407,224029,1,,entry citation,,22314689,12427019,,,Solution Structure and Characterization of the Heme Chaperone CcmE,published,journal,Biochemistry,,41,46,,,,,,,,,,,,,,,,,,,,,,13587,13594,2002, citations,entry_citation,5408,224057,1,,entry citation,,22140452,12144788,,,"Solution Structure of the DFF-C Domain of DFF45/ICAD. A Structural Basis for the Regulation of Apoptotic DNA Fragmentation",published,journal,J. Mol. Biol.,,321,2,,,,,,,,,,,,,,,,,,,,,,317,327,2002, citations,entry_citation,5409,224082,1,,entry citation,,,,,,"Letter to the Editor: Resonance Assignment and Topology of the 2H, 13C, 15N labeled 29 kDa N-terminal Fragment of the Polypyrimidine Tract Binding Protein (PTB)",published,journal,J. Biomol. NMR,,24,1,,,,,,,,,,,,,,,,,,,,,,79,80,2002, citations,entry_citation,541,224103,1,,entry citation,,,,,"Hunkapiller, Michael W., Forgac, Michael D., Yu, Ellen Ho, Richards, John H., ""13C NMR Studies of the Binding of Soybean Trypsin Inhibitor to Trypsin,"" Biochem. Biophys. Res. Commun. 87 (1), 25-31 (1979).",13C NMR Studies of the Binding of Soybean Trypsin Inhibitor to Trypsin,published,journal,Biochem. Biophys. Res. Commun.,,87,1,,,,,,,,,,,,,,,,,,,,,,25,31,1979, citations,entry_citation,5410,224116,1,,entry citation,,,12538900,,,"Amino Acid Sequence and Homology Modeling of Obtustatin, a Novel non-RGD-containing short Disintegrin isolated from the Venom of Vipera lebetina obtusa",published,journal,Protein Sci.,,12,,,,,,,,,,,,,,,,,,,,,,,366,371,2003, citations,entry_citation,5416,224203,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5417,224217,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5418,224231,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5419,224245,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5420,224259,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5421,224273,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5422,224287,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5423,224301,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5424,224315,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5425,224329,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5426,224343,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5427,224357,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5428,224371,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5429,224385,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,543,224399,1,,entry citation,,,,,"Moore, Geoffrey R., Williams, Robert J. P., ""Nuclear-Magnetic-Resonance Studies of Eucaryotic Cytochrome c Assignment of Resonances of Aliphatic Amino Acids,"" Eur. J. Biochem. 103, 503-512 (1980).","Nuclear-Magnetic-Resonance Studies of Eucaryotic Cytochrome c Assignment of Resonances of Aliphatic Amino Acids",published,journal,Eur. J. Biochem.,,103,,,,,,,,,,,,,,,,,,,,,,,503,512,1980, citations,entry_citation,5430,224415,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5431,224429,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5432,224443,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5433,224457,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5434,224471,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5435,224485,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5436,224499,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5437,224513,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5438,224527,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5439,224541,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,544,224555,1,,entry citation,,,,,"Moore, Geoffrey R., Williams, Robert J. P., ""Nuclear-Magnetic-Resonance Studies of Eucaryotic Cytochrome c Assignment of Resonances of Aliphatic Amino Acids,"" Eur. J. Biochem. 103, 503-512 (1980).","Nuclear-Magnetic-Resonance Studies of Eucaryotic Cytochrome c Assignment of Resonances of Aliphatic Amino Acids",published,journal,Eur. J. Biochem.,,103,,,,,,,,,,,,,,,,,,,,,,,503,512,1980, citations,entry_citation,5440,224571,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5441,224585,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5442,224599,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5443,224613,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5444,224627,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5445,224641,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5446,224655,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5447,224669,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5448,224683,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5449,224697,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,545,224711,1,,entry citation,,,,,"Moore, Geoffrey R., Williams, Robert J. P., ""Nuclear-Magnetic-Resonance Studies of Eucaryotic Cytochrome c Assignment of Resonances of Aliphatic Amino Acids,"" Eur. J. Biochem. 103, 503-512 (1980).","Nuclear-Magnetic-Resonance Studies of Eucaryotic Cytochrome c Assignment of Resonances of Aliphatic Amino Acids",published,journal,Eur. J. Biochem.,,103,,,,,,,,,,,,,,,,,,,,,,,503,512,1980, citations,entry_citation,5450,224727,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5451,224741,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5452,224756,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5453,224771,1,,entry citation,,22515402,12627950,,,"NMR Determination of pKa Values for Asp, Glu, His, and Lys Mutants at Each Variable Contiguous Enzyme-inhibitor Contact Position of the Turkey Ovomucoid Third Domain",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2847,2856,2003, citations,entry_citation,5454,224786,1,,entry citation,,,,,,"NMR solution structure and dynamics of motilin in isotropic phospholipid bicellar solution",published,journal,J. Biomol. NMR,,24,2,,,,,,,,,,,,,,,,,,,,,,103,112,2002, citations,entry_citation,5455,224803,1,,entry citation,,22382442,12495037,,,"Letter to the Editor: 1H, 13C and 15N Resonance Assignments of the Human Phosphatase PRL-3",published,journal,J. Biomol. NMR,,24,2,,,,,,,,,,,,,,,,,,,,,,169,170,2002, citations,entry_citation,5456,224826,1,,entry citation,,,,,,"Letter to the Editor: Backbone 1H, 13C, and 15N resonance assignments of the von Willebrand factor A3 domain",published,journal,J. Biomol. NMR,,24,4,,,,,,,,,,,,,,,,,,,,,,357,358,2002, citations,entry_citation,5457,224840,1,,entry citation,,,,,,A 3D doubly sensitivity enhanced X-filtered TOCSY-TOCSY experiment,published,journal,J. Biomol. NMR,,24,2,,,,,,,,,,,,,,,,,,,,,,155,160,2002, citations,entry_citation,5458,224857,1,,entry citation,,,,,,"Letter to the Editor: Backbone 1H, 13C, and 15N assignments of the ribosome recycling factor from Thermus thermophillus",published,journal,J. Biomol. NMR,,24,1,,,,,,,,,,,,,,,,,,,,,,81,82,2002, citations,entry_citation,5476,225245,1,,entry citation,,,12924940,,,"Structures of phage-display peptides that bind to the malarial surface protein, apical membrane antigen 1, and block erythrocyte invasion",published,journal,Biochemistry,,42,33,,,,,,,,,,,,,,,,,,,,,,9915,9923,2003,"Biochemistry, ASAP Article 10.1021/bi034376b S0006-2960(03)04376-9 Web Release Date: July 30, 2003 http://pubs.acs.org/cgi-bin/asap.cgi/bichaw/asap/abs/bi034376b.html" citations,entry_citation,5477,225265,1,,entry citation,,,12924940,,,"Structures of phage-display peptides that bind to the malarial surface protein, apical membrane antigen 1, and block erythrocyte invasion",published,journal,Biochemistry,,42,33,,,,,,,,,,,,,,,,,,,,,,9915,9923,2003,"Biochemistry, ASAP Article 10.1021/bi034376b S0006-2960(03)04376-9 Web Release Date: July 30, 2003 http://pubs.acs.org/cgi-bin/asap.cgi/bichaw/asap/abs/bi034376b.html" citations,ref_1,5458,224858,2,,reference citation,,,12086623,,"Ito K, Fujiwara T, Toyoda T, Nakamura Y. Elongation Factor G Paricipates in Ribosome Disassembly by Interacting with Ribosome Recycling Factor at Their tRNA-Mimicry Domains. Mol Cell. 2002 Jun;9(6):1263-72",Elongation factor G participates in ribosome disassembly by interacting with ribosome recycling factor at their tRNA-mimicry domains.,published,journal,Mol. Cell,Molecular cell,9,6,,1097-2765,,,,,,,,,,,,,,,,,,,,1263,1272,2002,"Elongation factor G (EF-G) is a G protein with motor function that drives two target molecules, a tRNA in the translating ribosome and the ribosome recycling factor (RRF) in the post-termination complex. How G protein motor action is transmitted to RRF is unknown. Thermus thermophilus RRF is nonfunctional in Escherichia coli. It became functional upon introducing a plasmid expressing E. coli EF-G with surface changes in its tRNA-mimic domain or by replacing the E. coli EF-G tRNA-mimic domain by the Thermus domain. Thermus RRF could also be activated by introducing surface substitutions in its anticodon arm-mimic region. These gain-of-function phenotypes depend on the combination of heterologous EF-G and RRF alleles. These mutational studies suggest that EF-G motor action is transmitted to RRF by specific surface contacts between the domains that mimic the anticodon arm." citations,ref_2,5458,224859,3,,reference citation,,,11214182,,"Fujiwara T, Ito K, Nakamura Y. Functional mapping of ribosome-contact sites in the ribosome recycling factor: a structural view from a tRNA mimic. RNA. 2001 Jan;7(1):64-70",Functional mapping of ribosome-contact sites in the ribosome recycling factor: a structural view from a tRNA mimic.,published,journal,RNA,"RNA (New York, N.Y.)",7,1,,1355-8382,,,,,,,,,,,,,,,,,,,,64,70,2001,"Ribosome recycling factor (RRF) is required for disassembly of the posttermination complex of the ribosome after release of polypeptides. The crystal structure of RRF resembles a tRNA shape, with an architecturally different flexibility compared with tRNA, but its structure-and-function relationships are unknown. We here found that an RRF variant defective in ribosome binding regains the binding capacity through 20 independent secondary changes occurring in three topologically distinct regions of RRF. Because two of these regions are equivalent to the tip of the anticodon stem and the upper surface of the acceptor stem of tRNA, RRF may interact with the ribosome in a way similar to tRNA, spanning 30S and 50S subunits, to exert its action for splitting the ribosome." citations,ref_3,5458,224860,4,,reference citation,,,11073219,,"Toyoda T, Tin OF, Ito K, Fujiwara T, Kumasaka T, Yamamoto M, Garber MB, Nakamura Y. Crystal structure combined with genetic analysis of the Thermus thermophilus ribosome recycling factor shows that a flexible hinge may act as a functional switch. RNA. 2000 Oct;6(10):1432-44",Crystal structure combined with genetic analysis of the Thermus thermophilus ribosome recycling factor shows that a flexible hinge may act as a functional switch.,published,journal,RNA,"RNA (New York, N.Y.)",6,10,,1355-8382,,,,,,,,,,,,,,,,,,,,1432,1444,2000,"Ribosome recycling factor (RRF), in concert with elongation factor EF-G, is required for disassembly of the posttermination complex of the ribosome after release of polypeptides. The crystal structure of Thermus thermophilus RRF was determined at 2.6 A resolution. It is a tRNA-like L-shaped molecule consisting of two domains: a long three-helix bundle (domain 1) and a three-layer beta/alpha/beta sandwich (domain 2). Although the individual domain structures are similar to those of Thermotoga maritima RRF (Selmer et al., Science, 1999, 286:2349-2352), the interdomain angle differs by 33 degrees in two molecules, suggesting that the hinge between two domains is potentially flexible and responsive to different conditions of crystal packing. The hinge connects hydrophobic junctions of domains 1 and 2. The structure-based genetic analysis revealed the strong correlation between the hinge flexibility and the in vivo function of RRF. First, altering the hinge flexibility by making alanine or serine substitutions for large-size residues conserved at the hinge loop and nearby in domain 1 frequently gave rise to gain of function except a Pro residue conserved at the hinge loop. Second, the hinge defect resulting from a too relaxed hinge structure can be compensated for by secondary alterations in domain 1 that seem to increase the hydrophobic contact between domain 1 and the hinge loop. These results show that the hinge flexibility is vital for the function of RRF and that the steric interaction between the hinge loop and domains 1 and 2 restricts the interdomain angle and/or the hinge flexibility. These results indicate that RRF possesses an architectural difference from tRNA regardless of a resemblance to tRNA shape: RRF has a ""gooseneck"" elbow, whereas the tRNA elbow is rigid, and the direction of flex of RRF and tRNA is at a nearly right angle to each other. Moreover, surface electrostatic potentials of the two RRF proteins are dissimilar and do not mimic the surface potential of tRNA or EF-G. These properties will add a new insight into RRF, suggesting that RRF is more than a simple tRNA mimic." citations,entry_citation,5459,224888,1,,entry citation,,22590463,12588869,,,"High Precision NMR Structure and Function of the RING-H2 Finger Domain of EL5, a Rice Protein whose Expression is Increased upon Exposure to Pathogen-derived Oligosaccahrides",published,journal,J. Biol. Chem.,,278,17,,,,,,,,,,,,,,,,,,,,,,15341,15348,2003, citations,entry_citation,546,224901,1,,entry citation,,,,,"Moore, Geoffrey R., Williams, Robert J. P., ""Nuclear-Magnetic-Resonance Studies of Eucaryotic Cytochrome c Assignment of Resonances of Aliphatic Amino Acids,"" Eur. J. Biochem. 103, 503-512 (1980).","Nuclear-Magnetic-Resonance Studies of Eucaryotic Cytochrome c Assignment of Resonances of Aliphatic Amino Acids",published,journal,Eur. J. Biochem.,,103,,,,,,,,,,,,,,,,,,,,,,,503,512,1980, citations,entry_citation,5461,224917,1,,entry citation,,22337317,12402030,,,"Structural Characterization of a Proline-driven Conformational Switch within the Itk SH2 Domain",published,journal,Nat. Struct. Biol.,,9,12,,,,,,,,,,,,,,,,,,,,,,900,905,2002, citations,ref_1,5461,224918,2,,reference citation,,,10986122,,"Brazin KN, Fulton DB, Andreotti AH J Mol Biol. 2000 Sep 22;302(3):607-23.",A specific intermolecular association between the regulatory domains of a Tec family kinase.,published,journal,J. Mol. Biol.,Journal of molecular biology,302,3,,0022-2836,,,,,,,,,,,,,,,,,,,,607,623,2000,"Interleukin-2 tyrosine kinase (Itk), is a T-cell specific tyrosine kinase of the Tec family. We have examined a novel intermolecular interaction between the SH3 and SH2 domains of Itk. In addition to the interaction between the isolated domains, we have found that the dual SH3/SH2 domain-containing fragment of Itk self-associates in a specific manner in solution. Tec family members contain the SH3, SH2 and catalytic domains common to many kinase families but are distinguished by a unique amino-terminal sequence, which contains a proline-rich stretch. Previous work has identified an intramolecular regulatory association between the proline-rich region and the adjacent SH3 domain of Itk. The intermolecular interaction between the SH3 and SH2 domains of Itk that we describe provides a possible mechanism for displacement of this intramolecular regulatory sequence, a step that may be required for full Tec kinase activation. Additionally, localization of the interacting surfaces on both the SH3 and SH2 domains by chemical shift mapping has provided information about the molecular details of this recognition event. The interaction involves the conserved aromatic binding pocket of the SH3 domain and a newly defined binding surface on the SH2 domain. The interacting residues on the SH2 domain do not conform to the consensus motif for an SH3 proline-rich ligand. Interestingly, we note a striking correlation between the SH2 residues that mediate this interaction and those residues that, when mutated in the Tec family member Btk, cause the hereditary immune disorder, X-linked agamaglobulinemia." citations,entry_citation,5478,225285,1,,entry citation,,,12924940,,,"Structures of phage-display peptides that bind to the malarial surface protein, apical membrane antigen 1, and block erythrocyte invasion",published,journal,Biochemistry,,42,33,,,,,,,,,,,,,,,,,,,,,,9915,9923,2003,"Biochemistry, ASAP Article 10.1021/bi034376b S0006-2960(03)04376-9 Web Release Date: July 30, 2003 http://pubs.acs.org/cgi-bin/asap.cgi/bichaw/asap/abs/bi034376b.html" citations,entry_citation,5479,225305,1,,entry citation,,,12924940,,,"Structures of phage-display peptides that bind to the malarial surface protein, apical membrane antigen 1, and block erythrocyte invasion",published,journal,Biochemistry,,42,33,,,,,,,,,,,,,,,,,,,,,,9915,9923,2003,"Biochemistry, ASAP Article 10.1021/bi034376b S0006-2960(03)04376-9 Web Release Date: July 30, 2003 http://pubs.acs.org/cgi-bin/asap.cgi/bichaw/asap/abs/bi034376b.html" citations,entry_citation,548,225325,1,,entry citation,,,,,"Saudek, Vladimir, Pelton, John T., ""Sequence-Specific 1H NMR Assignment and Secondary Structure of Neuropeptide Y in Aqueous Solution,"" Biochemistry 29, 4509-4515 (1990).","Sequence-Specific 1H NMR Assignment and Secondary Structure of Neuropeptide Y in Aqueous Solution",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,4509,4515,1990, citations,entry_citation,5480,225339,1,,entry citation,,,12885399,,,"Two distinct calcium-calmodulin interactions with N-terminal regions of the olfactory and rod cyclic nucleotide-gated channels characterized by NMR spectroscopy",published,journal,FEBS Lett.,,548,1-3,,,,,,,,,,,,,,,,,,,,,,11,16,2003, citations,ref_2,5461,224919,3,,reference citation,,,11830645,,"Brazin KN, Mallis RJ, Fulton DB, Andreotti AH. Regulation of the tyrosine kinase Itk by the peptidyl-prolyl isomerase cyclophilin A. Proc Natl Acad Sci U S A. 2002 Feb 19;99(4):1899-904.",Regulation of the tyrosine kinase Itk by the peptidyl-prolyl isomerase cyclophilin A.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,99,4,,0027-8424,,,,,,,,,,,,,,,,,,,,1899,1904,2002,"Interleukin-2 tyrosine kinase (Itk) is a nonreceptor protein tyrosine kinase of the Tec family that participates in the intracellular signaling events leading to T cell activation. Tec family members contain the conserved SH3, SH2, and catalytic domains common to many kinase families, but they are distinguished by unique sequences outside of this region. The mechanism by which Itk and related Tec kinases are regulated is not well understood. Our studies indicate that Itk catalytic activity is inhibited by the peptidyl prolyl isomerase activity of cyclophilin A (CypA). NMR structural studies combined with mutational analysis show that a proline-dependent conformational switch within the Itk SH2 domain regulates substrate recognition and mediates regulatory interactions with the active site of CypA. CypA and Itk form a stable complex in Jurkat T cells that is disrupted by treatment with cyclosporin A. Moreover, the phosphorylation levels of Itk and a downstream substrate of Itk, PLCgamma1, are increased in Jurkat T cells that have been treated with cyclosporin A. These findings support a novel mode of tyrosine kinase regulation for a Tec family member and provide a molecular basis for understanding a cellular function of the ubiquitous peptidyl prolyl isomerase, CypA." citations,entry_citation,5462,224947,1,,entry citation,,,,,,"Letter to the Editor: 1H, 15N and 13C Backbone Assignment of MJ1267, an ATP-binding cassette",published,journal,J. Biomol. NMR,,24,2,,,,,,,,,,,,,,,,,,,,,,167,168,2002, citations,entry_citation,5463,224969,1,,entry citation,,15150739,14759560,,,"Conformational preferences and activities of peptides from the catecholamine release-inhibitory (catestatin) region of chromogranin A.",published,journal,Regul. Pept.,,118,1-2,,,,,,,,,,,,,,,,,,,,,,75,87,2004, citations,entry_citation,5464,224988,1,,entry citation,,,,,,Solution Structure of a CCHC Zinc Finger from MOZ,published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5465,225011,1,,entry citation,,,14674747,,,"Solution structure of human saposin C: pH-dependent interaction with phospholipid vesicles.",published,journal,Biochemistry,,42,50,,,,,,,,,,,,,,,,,,,,,,14729,14740,2003, citations,entry_citation,5466,225031,1,,entry citation,,22505586,12617658,,,Structural Model for an Alkaline form of Ferricytochrome C,published,journal,J. Am. Chem. Soc.,,125,10,,,,,,,,,,,,,,,,,,,,,,2913,2922,2003, citations,entry_citation,5467,225052,1,,entry citation,,,15062083,,,Structure of a helically extended SH3 domain of the T cell adapter protein ADAP,published,journal,"Structure (Cambridge, MA, U. S.)",,12,4,,,,,,,,,,,,,,,,,,,,,,603,610,2004, citations,entry_citation,5468,225078,1,,entry citation,,,,,,"Letter to the Editor: Backbone HN, N, Ca, C', and Cb assignment of the 6-phosphogluconolactonase, a 266-residue enzyme of the pentose-phosphate pathway from human parasite Trypanosoma brucei.",published,journal,J. Biomol. NMR,,25,3,,,,,,,,,,,,,,,,,,,,,,249,250,2003, citations,entry_citation,5469,225096,1,,entry citation,,,,,,"Inhibitory Specificity Change of Ovomucoid Third Domain of Silver Pheasant upon Introduction of an Engineered Cys14-Cys39 Bond",published,journal,Biochemistry,,42,,,,,,,,,,,,,,,,,,,,,,,2524,2534,2003, citations,entry_citation,547,225112,1,,entry citation,,,,,"Ikura, Mitsuhiko, Kay, Lewis E., Bax, Ad, ""A Novel Approach for Sequential Assignment of 1H, 13C, and 15N Spectra of Larger Proteins: Heteronuclear Triple-Resonance Three-Dimensional NMR Spectroscopy. Application to Calmodulin,"" Biochemistry 29, 4659-4667 (1990).","A Novel Approach for Sequential Assignment of 1H, 13C, and 15N Spectra of Larger Proteins: Heteronuclear Triple-Resonance Three-Dimensional NMR Spectroscopy. Application to Calmodulin",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,4659,4667,1990, citations,entry_citation,5470,225125,1,,entry citation,,,,,,"Inhibitory Specificity Change of Ovomucoid Third Domain of Silver Pheasant upon Introduction of an Engineered Cys14-Cys39 Bond",published,journal,Biochemistry,,42,,,,,,,,,,,,,,,,,,,,,,,2524,2534,2003, citations,entry_citation,5471,225141,1,,entry citation,,22176724,,,,"Four-dimensional NMR Spectroscopy of a 723-residue Protein: Chemical Shift Assignments and Secondary Structure of Malate Synthase G",published,journal,J. Am. Chem. Soc.,,124,,,,,,,,,,,,,,,,,,,,,,,10025,10035,2002, citations,entry_citation,5472,225165,1,,entry citation,,22652003,12767219,,,"Two Conformational States of Turkey Ovomucoid Third Domain at low pH: Three-dimensional Structures, Internal Dynamics, and Interconversion Kinetics and Thermodynamics",published,journal,Biochemistry,,42,21,,,,,,,,,,,,,,,,,,,,,,6380,6391,2003,cis-trans isomerization of prolyl peptide bond. citations,entry_citation,5473,225181,1,,entry citation,,22652003,12767219,,,"Two Conformational States of Turkey Ovomucoid Third Domain at Low pH: Three-dimensional Structures, Internal Dynamics, and Interconversion Kinetics and Thermodynamics",published,journal,Biochemistry,,42,21,,,,,,,,,,,,,,,,,,,,,,6380,6391,2003,cis-trans isomerization of prolyl peptide bond. citations,entry_citation,5474,225197,1,,entry citation,,,,,,"Letter to the Editor: Backbone resonance assignment of the 298 amino acid catalytic domain of protein tyrosine phosphatase 1B (PTP1B)",published,journal,J. Biomol. NMR,,24,2,,,,,,,,,,,,,,,,,,,,,,165,166,2002, citations,1,5474,225198,2,,reference citation,,,8128219,,"Barford, D., Flint, A.J., Tonks,N.K. (1994) Science, 263, 1397-1404.",Crystal structure of human protein tyrosine phosphatase 1B.,published,journal,Science,"Science (New York, N.Y.)",263,5152,,0036-8075,,,,,,,,,,,,,,,,,,,,1397,1404,1994,"Protein tyrosine phosphatases (PTPs) constitute a family of receptor-like and cytoplasmic signal transducing enzymes that catalyze the dephosphorylation of phosphotyrosine residues and are characterized by homologous catalytic domains. The crystal structure of a representative member of this family, the 37-kilodalton form (residues 1 to 321) of PTP1B, has been determined at 2.8 A resolution. The enzyme consists of a single domain with the catalytic site located at the base of a shallow cleft. The phosphate recognition site is created from a loop that is located at the amino-terminus of an alpha helix. This site is formed from an 11-residue sequence motif that is diagnostic of PTPs and the dual specificity phosphatases, and that contains the catalytically essential cysteine and arginine residues. The position of the invariant cysteine residue within the phosphate binding site is consistent with its role as a nucleophile in the catalytic reaction. The structure of PTP1B should serve as a model for other members of the PTP family and as a framework for understanding the mechanism of tyrosine dephosphorylation." citations,entry_citation,5475,225227,1,,entry citation,,,,,,"Homology predicted structure and comparison with the secondary structure from NMR data for plastocyanin from the cyanobacterium synechocystis sp. PCC 6803",published,journal,Inorg. Chim. Acta,,275-276,,,,,,,,,,,,,,,,,,,,,,,73,89,1998, citations,entry_citation,5497,225740,1,,entry citation,,,,,,"Letter to the Editor: 1H, 15N and 13C assignments of the carboxy-terminal domain of the transmembrane electron transfer protein DsbD",published,journal,J. Biomol. NMR,,24,4,,,,,,,,,,,,,,,,,,,,,,359,360,2002, citations,ref_1,5480,225340,2,,reference citation,,,10493800,,"Elshorst B, Hennig M, Forsterling H, Diener A, Maurer M, Schulte P, Schwalbe H, Griesinger C, Krebs J, Schmid H, Vorherr T, Carafoli E. NMR solution structure of a complex of calmodulin with a binding peptide of the Ca2+ pump. Biochemistry. 1999 Sep 21;38(38):12320-32.",NMR solution structure of a complex of calmodulin with a binding peptide of the Ca2+ pump.,published,journal,Biochemistry,Biochemistry,38,38,,0006-2960,,,,,,,,,,,,,,,,,,,,12320,12332,1999,"The three-dimensional structure of the complex between calmodulin (CaM) and a peptide corresponding to the N-terminal portion of the CaM-binding domain of the plasma membrane calcium pump, the peptide C20W, has been solved by heteronuclear three-dimensional nuclear magnetic resonance (NMR) spectroscopy. The structure calculation is based on a total of 1808 intramolecular NOEs and 49 intermolecular NOEs between the peptide C20W and calmodulin from heteronuclear-filtered NOESY spectra and a half-filtered experiment, respectively. Chemical shift differences between free Ca(2+)-saturated CaM and its complex with C20W as well as the structure calculation reveal that C20W binds solely to the C-terminal half of CaM. In addition, comparison of the methyl resonances of the nine assigned methionine residues of free Ca(2+)-saturated CaM with those of the CaM/C20W complex revealed a significant difference between the N-terminal and the C-terminal domain; i.e., resonances in the N-terminal domain of the complex were much more similar to those reported for free CaM in contrast to those in the C-terminal half which were significantly different not only from the resonances of free CaM but also from those reported for the CaM/M13 complex. As a consequence, the global structure of the CaM/C20W complex is unusual, i.e., different from other peptide calmodulin complexes, since we find no indication for a collapsed structure. The fine modulation in the peptide protein interface shows a number of differences to the CaM/M13 complex studied by Ikura et al. [Ikura, M., Clore, G. M., Gronenborn, A. M., Zhu, G., Klee, C. B., and Bax, A. (1992) Science 256, 632-638]. The unusual binding mode to only the C-terminal half of CaM is in agreement with the biochemical observation that the calcium pump can be activated by the C-terminal half of CaM alone [Guerini, D., Krebs, J., and Carafoli, E. (1984) J. Biol. Chem. 259, 15172-15177]." citations,ref_2,5480,225341,3,,reference citation,,,7552747,,"Zhang M, Tanaka T, Ikura M. Calcium-induced conformational transition revealed by the solution structure of apo calmodulin. Nat Struct Biol. 1995 Sep;2(9):758-67.",Calcium-induced conformational transition revealed by the solution structure of apo calmodulin.,published,journal,Nat. Struct. Biol.,Nature structural biology,2,9,,1072-8368,,,,,,,,,,,,,,,,,,,,758,767,1995,"The solution structure of Ca(2+)-free calmodulin has been determined by NMR spectroscopy, and is compared to the previously reported structure of the Ca(2+)-saturated form. The removal of Ca2+ causes the interhelical angles of four EF-hand motifs to increase by 36 degrees-44 degrees. This leads to major changes in surface properties, including the closure of the deep hydrophobic cavity essential for target protein recognition. Concerted movements of helices A and D with respect to B and C, and of helices E and H with respect to F and G are likely responsible for the cooperative Ca(2+)-binding property observed between two adjacent EF-hand sites in the amino- and carboxy-terminal domains." citations,ref_3,5480,225342,4,,reference citation,,,1519061,,"Meador WE, Means AR, Quiocho FA. Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex. Science. 1992 Aug 28;257(5074):1251-5.",Target enzyme recognition by calmodulin: 2.4 A structure of a calmodulin-peptide complex.,published,journal,Science,"Science (New York, N.Y.)",257,5074,,0036-8075,,,,,,,,,,,,,,,,,,,,1251,1255,1992,"The crystal structure of calcium-bound calmodulin (Ca(2+)-CaM) bound to a peptide analog of the CaM-binding region of chicken smooth muscle myosin light chain kinase has been determined and refined to a resolution of 2.4 angstroms (A). The structure is compact and has the shape of an ellipsoid (axial ratio approximately 2:1). The bound CaM forms a tunnel diagonal to its long axis that engulfs the helical peptide, with the hydrophobic regions of CaM melded into a single area that closely covers the hydrophobic side of the peptide. There is a remarkably high pseudo-twofold symmetry between the closely associated domains. The central helix of the native CaM is unwound and expanded into a bend between residues 73 and 77. About 185 contacts (less than 4 A) are formed between CaM and the peptide, with van der Waals contacts comprising approximately 80% of this total." citations,ref_4,5480,225343,5,,reference citation,,,7552748,,"Kuboniwa H, Tjandra N, Grzesiek S, Ren H, Klee CB, Bax A. Solution structure of calcium-free calmodulin. Nat Struct Biol. 1995 Sep;2(9):768-76.",Solution structure of calcium-free calmodulin.,published,journal,Nat. Struct. Biol.,Nature structural biology,2,9,,1072-8368,,,,,,,,,,,,,,,,,,,,768,776,1995,"The three-dimensional structure of calmodulin in the absence of Ca2+ has been determined by three- and four-dimensional heteronuclear NMR experiments, including ROE, isotope-filtering combined with reverse labelling, and measurement of more than 700 three-bond J-couplings. In analogy with the Ca(2+)-ligated state of this protein, it consists of two small globular domains separated by a flexible linker, with no stable, direct contacts between the two domains. In the absence of Ca2+, the four helices in each of the two globular domains form a highly twisted bundle, capped by a short anti-parallel beta-sheet. This arrangement is qualitatively similar to that observed in the crystal structure of the Ca(2+)-free N-terminal domain of troponin C." citations,ref_5,5480,225344,6,,reference citation,,,7803388,,"Cook WJ, Walter LJ, Walter MR. Drug binding by calmodulin: crystal structure of a calmodulin-trifluoperazine complex. Biochemistry. 1994 Dec 27;33(51):15259-65.",Drug binding by calmodulin: crystal structure of a calmodulin-trifluoperazine complex.,published,journal,Biochemistry,Biochemistry,33,51,,0006-2960,,,,,,,,,,,,,,,,,,,,15259,15265,1994,"The crystal structure of calmodulin (CaM) bound to trifluoperazine (TFP) has been determined and refined to a resolution of 2.45 A. Only one TFP is bound to CaM, but that is sufficient to cause distortion of the central alpha-helix and juxtaposition of the N- and C-terminal domains similar to that seen in CaM-polypeptide complexes. The drug makes extensive contacts with residues in the C-terminal domain of CaM but only a few contacts with one residue in the N-terminal domain. The structure suggests that substrate binding to the C-terminal domain is sufficient to cause the conformational changes in calmodulin that lead to activation of its targets." citations,entry_citation,5491,225627,1,,entry citation,,,12676931,,,"Structural basis for new pattern of the conserved amino acid residues related to chitin-binding in the antifungal peptide from the coconut rhinoceros beetle, Oryctes rhinoceros",published,journal,J. Biol. Chem.,,278,,,,,,,,,,,,,,,,,,,,,,,22820,22827,2003, citations,entry_citation,5492,225644,1,,entry citation,,22415474,12527309,,,"Charge-Charge Interactions are Key Determinants of the pK Values of Ionizable Groups in Ribonuclease Sa (pI=3.5) and a Basic Variant (pI=10.2)",published,journal,J. Mol. Biol.,,325,5,,,,,,,,,,,,,,,,,,,,,,1077,1092,2003, citations,entry_citation,5493,225660,1,,entry citation,,,,10.1023/A:1021670007096,,"Letter to the Editor: Backbone 1H, 15N and 13C resonance assignments of the Staphylococcus aureus acyl carrier protein synthase (AcpS)",published,journal,J. Biomol. NMR,,24,3,,,,,,,,,,,,,,,,,,,,,,273,274,2002, citations,entry_citation,5494,225680,1,,entry citation,,22229374,12130641,,,"NMR Structure of PW2 bound to SDS Micelles. A Tryptophan-rich Anticocidial Peptide selected from Phage Display Libraries",published,journal,J. Biol. Chem.,,277,39,,,,,,,,,,,,,,,,,,,,,,36351,36356,2002, citations,entry_citation,5495,225702,1,,entry citation,,22709212,12824480,,,"Recombinant Production and Solution Structure of PcTx1, the Specific Peptide Inhibitor of ASIC1a Proton-gated Cation Channels",published,journal,Protein Sci.,,12,7,,,,,,,,,,,,,,,,,,,,,,1332,1343,2003, citations,ref_6,5480,225345,7,,reference citation,,,1474585,,"Chattopadhyaya R, Meador WE, Means AR, Quiocho FA. Calmodulin structure refined at 1.7 A resolution. J Mol Biol. 1992 Dec 20;228(4):1177-92.",Calmodulin structure refined at 1.7 A resolution.,published,journal,J. Mol. Biol.,Journal of molecular biology,228,4,,0022-2836,,,,,,,,,,,,,,,,,,,,1177,1192,1992,"We have determined and refined the crystal structure of a recombinant calmodulin at 1.7 A resolution. The structure was determined by molecular replacement, using the 2.2 A published native bovine brain structure as the starting model. The final crystallographic R-factor, using 14,469 reflections in the 10.0 to 1.7 A range with structure factors exceeding 0.5 sigma, is 0.216. Bond lengths and bond angle distances have root-mean-square deviations from ideal values of 0.009 A and 0.032 A, respectively. The final model consists of 1279 non-hydrogen atoms, including four calcium ions, 1130 protein atoms, including three Asp118 side-chain atoms in double conformation, 139 water molecules and one ethanol molecule. The electron densities for residues 1 to 4 and 148 of calmodulin are poorly defined, and not included in our model, except for main-chain atoms of residue 4. The calmodulin structure from our crystals is very similar to the earlier 2.2 A structure described by Babu and coworkers with a root-mean-square deviation of 0.36 A. Calmodulin remains a dumb-bell-shaped molecule, with similar lobes and connected by a central alpha-helix. Each lobe contains three alpha-helices and two Ca2+ binding EF hand loops, with a short antiparallel beta-sheet between adjacent EF hand loops and one non-EF hand loop. There are some differences in the structure of the central helix. The crystal packing is extensively studied, and facile crystal growth along the z-axis of the triclinic crystals is explained. Herein, we describe hydrogen bonding in the various secondary structure elements and hydration of calmodulin." citations,ref_7,5480,225346,8,,reference citation,,,7634090,,"Vandonselaar M, Hickie RA, Quail JW, Delbaere LT. Trifluoperazine-induced conformational change in Ca(2+)-calmodulin. Nat Struct Biol. 1994 Nov;1(11):795-801.",Trifluoperazine-induced conformational change in Ca(2+)-calmodulin.,published,journal,Nat. Struct. Biol.,Nature structural biology,1,11,,1072-8368,,,,,,,,,,,,,,,,,,,,795,801,1994,"Here we show that, as a consequence of binding the drug trifluoperazine, a major conformational movement occurs in Ca(2+)-calmodulin (CaM). The tertiary structure changes from an elongated dumb-bell, with exposed hydrophobic surfaces, to a compact globular form which can no longer interact with its target enzymes. It is likely that inactivation of Ca(2+)-CaM by trifluoperazine is due to this major tertiary-structural alteration in Ca(2+)-CaM, which is initiated and stabilized by drug binding. This conformational change is similar to that which occurs on the binding of Ca(2+)-CaM to target peptides. Two hydrophobic binding pockets, created by amino acid residues adjacent to Ca(2+)-coordinating residues, form the key recognition sites on Ca(2+)-CaM for both inhibitors and target enzymes." citations,ref_8,5480,225347,9,,reference citation,,,9438860,,"Wall ME, Clarage JB, Phillips GN. Motions of calmodulin characterized using both Bragg and diffuse X-ray scattering. Structure. 1997 Dec 15;5(12):1599-612.",Motions of calmodulin characterized using both Bragg and diffuse X-ray scattering.,published,journal,Structure,"Structure (London, England : 1993)",5,12,,0969-2126,,,,,,,,,,,,,,,,,,,,1599,1612,1997,"BACKGROUND: Calmodulin is a calcium-activated regulatory protein which can bind to many different targets. The protein resembles a highly flexible dumbbell, and bends in the middle as it binds. This and other motions must be understood to formulate a realistic model of calmodulin function. RESULTS: Using the Bragg reflections from X-ray crystallography, a multiple-conformer refinement of a calmodulin-peptide complex shows anisotropic displacements, with high variations of dihedral angles in several nonhelical domains: the flexible linker; three of the four calcium-binding sites (including both of the N-terminal sites); and a turn connecting the C-terminal EF-hand calcium-binding domains. Three-dimensional maps of the large scale diffuse X-ray scattering data show isotropic liquid-like motions with an unusually small correlation length. Three-dimensional maps of the small scale diffuse streaks show highly coupled, anisotropic motions along the head-to-tail molecular packing direction in the unit cell. There is also weak coupling perpendicular to the head-to-tail packing direction, particularly across a cavity occupied by the disordered linker domain of the molecule. CONCLUSIONS: Together, the Bragg and diffuse scattering present a self-consistent description of the motions in the flexible linker of calmodulin. The other mobile regions of the protein are also of great interest. In particular, the high variations in the calcium-binding sites are likely to influence how strongly they bind ions. This is especially important in the N-terminal sites, which regulate the activity of the molecule." citations,ref_10,5480,225348,10,,reference citation,,,9514729,,"Osawa M, Swindells MB, Tanikawa J, Tanaka T, Mase T, Furuya T, Ikura M. Solution structure of calmodulin-W-7 complex: the basis of diversity in molecular recognition. J Mol Biol. 1998 Feb 13;276(1):165-76.",Solution structure of calmodulin-W-7 complex: the basis of diversity in molecular recognition.,published,journal,J. Mol. Biol.,Journal of molecular biology,276,1,,0022-2836,,,,,,,,,,,,,,,,,,,,165,176,1998,"The solution structure of calcium-bound calmodulin (CaM) complexed with an antagonist, N-(6-aminohexyl)-5-chloro-1-naphthalenesulfonamide (W-7), has been determined by multidimensional NMR spectroscopy. The structure consists of one molecule of W-7 binding to each of the two domains of CaM. In each domain, the W-7 chloronaphthalene ring interacts with four methionine methyl groups and other aliphatic or aromatic side-chains in a deep hydrophobic pocket, the site responsible for CaM binding to CaM-dependent enzymes such as myosin light chain kinases (MLCKs) and CaM kinase II. This competitive binding at the same site between W-7 and CaM-dependent enzymes suggests the mechanism by which W-7 inhibits CaM to activate the enzymes. The orientation of the W-7 naphthalene ring in the N-terminal pocket is rotated approximately 40 degrees with respect to that in the C-terminal pocket. The W-7 ring orientation differs significantly from the Trp800 indole ring of smooth muscle MLCK bound to the C-terminal pocket and the phenothiazine ring of trifluoperazine bound to the N or C-terminal pocket. These comparative structural analyses demonstrate that the two hydrophobic pockets of CaM can accommodate a variety of bulky aromatic rings, which provides a plausible structural basis for the diversity in CaM-mediated molecular recognition." citations,ref_11,5480,225349,11,,reference citation,,,10467092,,"Osawa M, Tokumitsu H, Swindells MB, Kurihara H, Orita M, Shibanuma T, Furuya T, Ikura M. A novel target recognition revealed by calmodulin in complex with Ca2+-calmodulin-dependent kinase kinase. Nat Struct Biol. 1999 Sep;6(9):819-24.",A novel target recognition revealed by calmodulin in complex with Ca2+-calmodulin-dependent kinase kinase.,published,journal,Nat. Struct. Biol.,Nature structural biology,6,9,,1072-8368,,,,,,,,,,,,,,,,,,,,819,824,1999,"The structure of calcium-bound calmodulin (Ca2+/CaM) complexed with a 26-residue peptide, corresponding to the CaM-binding domain of rat Ca2+/CaM-dependent protein kinase kinase (CaMKK), has been determined by NMR spectroscopy. In this complex, the CaMKK peptide forms a fold comprising an alpha-helix and a hairpin-like loop whose C-terminus folds back on itself. The binding orientation of this CaMKK peptide by the two CaM domains is opposite to that observed in all other CaM-target complexes determined so far. The N- and C-terminal hydrophobic pockets of Ca2+/CaM anchor Trp 444 and Phe 459 of the CaMKK peptide, respectively. This 14-residue separation between two key hydrophobic groups is also unique among previously determined CaM complexes. The present structure represents a new and distinct class of Ca2+/CaM target recognition that may be shared by other Ca2+/CaM-stimulated proteins." citations,ref_15,5480,225350,12,,reference citation,,,8520220,,"Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR. 1995 Nov;6(3):277-93.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref_16,5480,225351,13,,reference citation,,,,,"Johnson, B. and Blevins R.A.(1994) J.Biomol.NMR, 4, 603-614 A computer program for the visualisation and analysis of NMR data.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5481,225384,1,,entry citation,,,,,,Solution structure of the yeast ubiquitin-like modifier protein Hub1,published,journal,J. Struct. Funct. Genomics,,4,1,,,,,,,,,,,,,,,,,,,,,,25,30,2003,"Ubiquitin-like modifier protein involved in polarized morphogenesis of S. cerevisae. The paper can be accessed at: http://www.kluweronline.com/issn/1345-711X" citations,ref_1,5481,225385,2,,reference citation,,,,,"Brunger AT. X-PLOR Version 3.1: a system for X-ray crystallography and NMR. New Haven, CY:Yale University Press; 1992.382 p.",,published,book,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5482,225405,1,,entry citation,,,,,,"Letter to the Editor: Assignment of 1H, 13C and 15N resonances of the N-terminal microtubule-binding domain of human doublecortin",published,journal,J. Biomol. NMR,,25,1,,,,,,,,,,,,,,,,,,,,,,81,82,2003, citations,ref_1,5482,225406,2,,reference citation,,,8520220,,"Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR. 1995 Nov;6(3):277-93.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref_2,5482,225407,3,,reference citation,,,,,"Goddard, TD., Kneller DG. Sparky3, University of california, San Francisco.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5483,225436,1,,entry citation,,22541932,12654266,,,"NMR Structure of Citrobacter freundii AmpD, Comparison with Bacteriophage T7 Lysozyme and Homology with PGRP Domains",published,journal,J. Mol. Biol.,,327,4,,,,,,,,,,,,,,,,,,,,,,833,842,2003, citations,ref_1,5483,225437,2,,reference citation,,,,,"Edvards Liepinsh, Catherine Genereux, Dominique Dehareng, Bernard Joris and Gottfried Otting, NMR structure of AmpD: structural conservation of peptidoglycan recognition proteins.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5484,225472,1,,entry citation,,,,,,"Letter to the Editor: Backbone NMR assignments of the metal-free UreE from Bacillus pasteurii",published,journal,J. Biomol. NMR,,24,4,,,,,,,,,,,,,,,,,,,,,,361,362,2002, citations,entry_citation,5485,225496,1,,entry citation,,22709226,12824494,,,"Solution Structure and Thermal Stability of Ribosomal Protein L30e from Hyperthermophilic Archaeon Thermococcus celer",published,journal,Protein Sci.,,12,7,,,,,,,,,,,,,,,,,,,,,,1483,1495,2003, citations,entry_citation,5486,225521,1,,entry citation,,,,,,"Solution and micelle-bound structures of tachyplesin I and its active aromatic linear derivatives",published,journal,Biochemistry,,41,,,,,,,,,,,,,,,,,,,,,,,12359,12368,2002, citations,ref_1,5486,225522,2,,reference citation,,,9882437,,"Rao AG. Conformation and antimicrobial activity of linear derivatives of tachyplesin lacking disulfide bonds. Arch Biochem Biophys. 1999 Jan 1;361(1):127-34.",Conformation and antimicrobial activity of linear derivatives of tachyplesin lacking disulfide bonds.,published,journal,Arch. Biochem. Biophys.,Archives of biochemistry and biophysics,361,1,,0003-9861,,,,,,,,,,,,,,,,,,,,127,134,1999,"Tachyplesin is a potent antimicrobial peptide isolated from the hemocytes of the horseshoe crab, Tachypleus tridentatus. Previous studies have shown that the 17-residue peptide has an intrinsic amphipathic structure conferred by two antiparallel beta-sheets held rigidly by two disulfide bonds. Taking its short length into account and the potential of such a small polypeptide to take on multiple conformational states, one may assume that the disulfide bonds are relevant determinants of function. However, in order to gain a global perspective on the tolerance of cysteine residues in tachyplesin to amino acid substitutions, a series of linear peptides have been synthesized and their physicochemical properties analyzed. In these linear peptides, the cysteines have been replaced with amino acids possessing different side-chain properties, i.e., aliphatic hydrophobic (Ala, Leu, Ile, Val, and Met), aromatic hydrophobic (Phe and Tyr), and acidic (Asp). Activity assays using natural and synthetic membranes, and conformational measurements, highlight the subtle influence and variability of the amino acid side-chain properties on peptide structure. While an unequivocal interpretation of the results will have to await more refined structural measurements, our results indicate that a rigidly held disulfide-bonded beta-pleated sheet structure may not be absolutely essential for antimicrobial activity. Furthermore, the results challenge the accepted dogma of structure-activity relationships among antimicrobial peptides and suggest that the maintenance of peptide hydrophobic-hydrophilic balance may be a critical parameter, in addition to structure, in the design of peptides with pharmaceutical relevance." citations,ref_2,5486,225523,3,,reference citation,,,8490053,,"Tamamura H, Kuroda M, Masuda M, Otaka A, Funakoshi S, Nakashima H, Yamamoto N, Waki M, Matsumoto A, Lancelin JM, et al. A comparative study of the solution structures of tachyplesin I and a novel anti-HIV synthetic peptide, T22 ([Tyr5,12, Lys7]-polyphemusin II), determined by nuclear magnetic resonance. Biochim Biophys Acta. 1993 May 13;1163(2):209-16.","A comparative study of the solution structures of tachyplesin I and a novel anti-HIV synthetic peptide, T22 ([Tyr5,12, Lys7]-polyphemusin II), determined by nuclear magnetic resonance.",published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1163,2,,0006-3002,,,,,,,,,,,,,,,,,,,,209,216,1993,"The solution structure of tachyplesin I, which was isolated from membrane acid extracts of the hemocytes from the Japanese horseshoe crab (Tachypleus tridentatus), was determined by nuclear magnetic resonance (NMR) and distance geometry calculation. Tachyplesin I takes an antiparallel beta-sheet structure with a type-II beta-turn. Recently, among more than 20 synthetic peptides associated with tachyplesin and its isopeptide (polyphemusin), we found that a novel compound, which we designated as T22 ([Tyr5,12, Lys7]-polyphemusin II), strongly inhibited the human immunodeficiency virus (HIV)-1-induced cytopathic effect and viral antigen expression. The solution structure of T22 was investigated using NMR, and its secondary structure was confirmed to be similar to that of tachyplesin I. The anti-parallel beta-sheet structure and the several amino-acid side chains on the plane of the beta-sheet of T22 are thought to be associated with the expression of anti-HIV activity." citations,entry_citation,5487,225543,1,,entry citation,,,,,,"Solution and micelle-bound structures of tachyplesin I and its active aromatic linear derivatives",published,journal,Biochemistry,,41,,,,,,,,,,,,,,,,,,,,,,,12359,12368,2002, citations,ref_1,5487,225544,2,,reference citation,,,9882437,,"Rao AG. Conformation and antimicrobial activity of linear derivatives of tachyplesin lacking disulfide bonds. Arch Biochem Biophys. 1999 Jan 1;361(1):127-34.",Conformation and antimicrobial activity of linear derivatives of tachyplesin lacking disulfide bonds.,published,journal,Arch. Biochem. Biophys.,Archives of biochemistry and biophysics,361,1,,0003-9861,,,,,,,,,,,,,,,,,,,,127,134,1999,"Tachyplesin is a potent antimicrobial peptide isolated from the hemocytes of the horseshoe crab, Tachypleus tridentatus. Previous studies have shown that the 17-residue peptide has an intrinsic amphipathic structure conferred by two antiparallel beta-sheets held rigidly by two disulfide bonds. Taking its short length into account and the potential of such a small polypeptide to take on multiple conformational states, one may assume that the disulfide bonds are relevant determinants of function. However, in order to gain a global perspective on the tolerance of cysteine residues in tachyplesin to amino acid substitutions, a series of linear peptides have been synthesized and their physicochemical properties analyzed. In these linear peptides, the cysteines have been replaced with amino acids possessing different side-chain properties, i.e., aliphatic hydrophobic (Ala, Leu, Ile, Val, and Met), aromatic hydrophobic (Phe and Tyr), and acidic (Asp). Activity assays using natural and synthetic membranes, and conformational measurements, highlight the subtle influence and variability of the amino acid side-chain properties on peptide structure. While an unequivocal interpretation of the results will have to await more refined structural measurements, our results indicate that a rigidly held disulfide-bonded beta-pleated sheet structure may not be absolutely essential for antimicrobial activity. Furthermore, the results challenge the accepted dogma of structure-activity relationships among antimicrobial peptides and suggest that the maintenance of peptide hydrophobic-hydrophilic balance may be a critical parameter, in addition to structure, in the design of peptides with pharmaceutical relevance." citations,ref_2,5487,225545,3,,reference citation,,,8490053,,"Tamamura H, Kuroda M, Masuda M, Otaka A, Funakoshi S, Nakashima H, Yamamoto N, Waki M, Matsumoto A, Lancelin JM, et al. A comparative study of the solution structures of tachyplesin I and a novel anti-HIV synthetic peptide, T22 ([Tyr5,12, Lys7]-polyphemusin II), determined by nuclear magnetic resonance. Biochim Biophys Acta. 1993 May 13;1163(2):209-16.","A comparative study of the solution structures of tachyplesin I and a novel anti-HIV synthetic peptide, T22 ([Tyr5,12, Lys7]-polyphemusin II), determined by nuclear magnetic resonance.",published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1163,2,,0006-3002,,,,,,,,,,,,,,,,,,,,209,216,1993,"The solution structure of tachyplesin I, which was isolated from membrane acid extracts of the hemocytes from the Japanese horseshoe crab (Tachypleus tridentatus), was determined by nuclear magnetic resonance (NMR) and distance geometry calculation. Tachyplesin I takes an antiparallel beta-sheet structure with a type-II beta-turn. Recently, among more than 20 synthetic peptides associated with tachyplesin and its isopeptide (polyphemusin), we found that a novel compound, which we designated as T22 ([Tyr5,12, Lys7]-polyphemusin II), strongly inhibited the human immunodeficiency virus (HIV)-1-induced cytopathic effect and viral antigen expression. The solution structure of T22 was investigated using NMR, and its secondary structure was confirmed to be similar to that of tachyplesin I. The anti-parallel beta-sheet structure and the several amino-acid side chains on the plane of the beta-sheet of T22 are thought to be associated with the expression of anti-HIV activity." citations,entry_citation,5488,225564,1,,entry citation,,,,,,"Solution and micelle-bound structures of tachyplesin I and its active aromatic linear derivatives",published,journal,Biochemistry,,41,,,,,,,,,,,,,,,,,,,,,,,12359,12368,2002, citations,ref_1,5488,225565,2,,reference citation,,,9882437,,"Rao AG. Conformation and antimicrobial activity of linear derivatives of tachyplesin lacking disulfide bonds. Arch Biochem Biophys. 1999 Jan 1;361(1):127-34.",Conformation and antimicrobial activity of linear derivatives of tachyplesin lacking disulfide bonds.,published,journal,Arch. Biochem. Biophys.,Archives of biochemistry and biophysics,361,1,,0003-9861,,,,,,,,,,,,,,,,,,,,127,134,1999,"Tachyplesin is a potent antimicrobial peptide isolated from the hemocytes of the horseshoe crab, Tachypleus tridentatus. Previous studies have shown that the 17-residue peptide has an intrinsic amphipathic structure conferred by two antiparallel beta-sheets held rigidly by two disulfide bonds. Taking its short length into account and the potential of such a small polypeptide to take on multiple conformational states, one may assume that the disulfide bonds are relevant determinants of function. However, in order to gain a global perspective on the tolerance of cysteine residues in tachyplesin to amino acid substitutions, a series of linear peptides have been synthesized and their physicochemical properties analyzed. In these linear peptides, the cysteines have been replaced with amino acids possessing different side-chain properties, i.e., aliphatic hydrophobic (Ala, Leu, Ile, Val, and Met), aromatic hydrophobic (Phe and Tyr), and acidic (Asp). Activity assays using natural and synthetic membranes, and conformational measurements, highlight the subtle influence and variability of the amino acid side-chain properties on peptide structure. While an unequivocal interpretation of the results will have to await more refined structural measurements, our results indicate that a rigidly held disulfide-bonded beta-pleated sheet structure may not be absolutely essential for antimicrobial activity. Furthermore, the results challenge the accepted dogma of structure-activity relationships among antimicrobial peptides and suggest that the maintenance of peptide hydrophobic-hydrophilic balance may be a critical parameter, in addition to structure, in the design of peptides with pharmaceutical relevance." citations,entry_citation,5496,225715,1,,entry citation,,,,,,"Letter to the Editor: NMR structure of ubiquitin-like domain in PARKIN: Gene product of familial Parkinson's disease",published,journal,J. Biomol. NMR,,25,2,,,,,,,,,,,The 40th Japanese NMR conference,Kyoto,,Japan,2001-11-14,2001-11-16,p62,,,,,153,156,2003,"The entry was first published as a conference abstract, then submitted to JBNMR." citations,entry_citation,5538,226704,1,,entry citation,,22727213,12842472,,,Structural Variation in PWWP Domains,published,journal,J. Mol. Biol.,,330,3,,,,,,,,,,,,,,,,,,,,,,571,576,2003, citations,ref_2,5488,225566,3,,reference citation,,,8490053,,"Tamamura H, Kuroda M, Masuda M, Otaka A, Funakoshi S, Nakashima H, Yamamoto N, Waki M, Matsumoto A, Lancelin JM, et al. A comparative study of the solution structures of tachyplesin I and a novel anti-HIV synthetic peptide, T22 ([Tyr5,12, Lys7]-polyphemusin II), determined by nuclear magnetic resonance. Biochim Biophys Acta. 1993 May 13;1163(2):209-16.","A comparative study of the solution structures of tachyplesin I and a novel anti-HIV synthetic peptide, T22 ([Tyr5,12, Lys7]-polyphemusin II), determined by nuclear magnetic resonance.",published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1163,2,,0006-3002,,,,,,,,,,,,,,,,,,,,209,216,1993,"The solution structure of tachyplesin I, which was isolated from membrane acid extracts of the hemocytes from the Japanese horseshoe crab (Tachypleus tridentatus), was determined by nuclear magnetic resonance (NMR) and distance geometry calculation. Tachyplesin I takes an antiparallel beta-sheet structure with a type-II beta-turn. Recently, among more than 20 synthetic peptides associated with tachyplesin and its isopeptide (polyphemusin), we found that a novel compound, which we designated as T22 ([Tyr5,12, Lys7]-polyphemusin II), strongly inhibited the human immunodeficiency virus (HIV)-1-induced cytopathic effect and viral antigen expression. The solution structure of T22 was investigated using NMR, and its secondary structure was confirmed to be similar to that of tachyplesin I. The anti-parallel beta-sheet structure and the several amino-acid side chains on the plane of the beta-sheet of T22 are thought to be associated with the expression of anti-HIV activity." citations,entry_citation,5489,225582,1,,reference citation,,,8490053,,,"A comparative study of the solution structures of tachyplesin I and a novel anti-HIV synthetic peptide, T22 ([Tyr5,12, Lys7]-polyphemusin II), determined by nuclear magnetic resonance.",published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1163,2,,0006-3002,,,,,,,,,,,,,,,,,,,,209,216,1993,"The solution structure of tachyplesin I, which was isolated from membrane acid extracts of the hemocytes from the Japanese horseshoe crab (Tachypleus tridentatus), was determined by nuclear magnetic resonance (NMR) and distance geometry calculation. Tachyplesin I takes an antiparallel beta-sheet structure with a type-II beta-turn. Recently, among more than 20 synthetic peptides associated with tachyplesin and its isopeptide (polyphemusin), we found that a novel compound, which we designated as T22 ([Tyr5,12, Lys7]-polyphemusin II), strongly inhibited the human immunodeficiency virus (HIV)-1-induced cytopathic effect and viral antigen expression. The solution structure of T22 was investigated using NMR, and its secondary structure was confirmed to be similar to that of tachyplesin I. The anti-parallel beta-sheet structure and the several amino-acid side chains on the plane of the beta-sheet of T22 are thought to be associated with the expression of anti-HIV activity." citations,ref_1,5489,225583,2,,reference citation,,,8490053,,"Rao AG. Conformation and antimicrobial activity of linear derivatives of tachyplesin lacking disulfide bonds. Arch Biochem Biophys. 1999 Jan 1;361(1):127-34.","A comparative study of the solution structures of tachyplesin I and a novel anti-HIV synthetic peptide, T22 ([Tyr5,12, Lys7]-polyphemusin II), determined by nuclear magnetic resonance.",published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1163,2,,0006-3002,,,,,,,,,,,,,,,,,,,,209,216,1993,"The solution structure of tachyplesin I, which was isolated from membrane acid extracts of the hemocytes from the Japanese horseshoe crab (Tachypleus tridentatus), was determined by nuclear magnetic resonance (NMR) and distance geometry calculation. Tachyplesin I takes an antiparallel beta-sheet structure with a type-II beta-turn. Recently, among more than 20 synthetic peptides associated with tachyplesin and its isopeptide (polyphemusin), we found that a novel compound, which we designated as T22 ([Tyr5,12, Lys7]-polyphemusin II), strongly inhibited the human immunodeficiency virus (HIV)-1-induced cytopathic effect and viral antigen expression. The solution structure of T22 was investigated using NMR, and its secondary structure was confirmed to be similar to that of tachyplesin I. The anti-parallel beta-sheet structure and the several amino-acid side chains on the plane of the beta-sheet of T22 are thought to be associated with the expression of anti-HIV activity." citations,ref_2,5489,225584,3,,reference citation,,,8490053,,"Tamamura H, Kuroda M, Masuda M, Otaka A, Funakoshi S, Nakashima H, Yamamoto N, Waki M, Matsumoto A, Lancelin JM, et al. A comparative study of the solution structures of tachyplesin I and a novel anti-HIV synthetic peptide, T22 ([Tyr5,12, Lys7]-polyphemusin II), determined by nuclear magnetic resonance. Biochim Biophys Acta. 1993 May 13;1163(2):209-16.","A comparative study of the solution structures of tachyplesin I and a novel anti-HIV synthetic peptide, T22 ([Tyr5,12, Lys7]-polyphemusin II), determined by nuclear magnetic resonance.",published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1163,2,,0006-3002,,,,,,,,,,,,,,,,,,,,209,216,1993,"The solution structure of tachyplesin I, which was isolated from membrane acid extracts of the hemocytes from the Japanese horseshoe crab (Tachypleus tridentatus), was determined by nuclear magnetic resonance (NMR) and distance geometry calculation. Tachyplesin I takes an antiparallel beta-sheet structure with a type-II beta-turn. Recently, among more than 20 synthetic peptides associated with tachyplesin and its isopeptide (polyphemusin), we found that a novel compound, which we designated as T22 ([Tyr5,12, Lys7]-polyphemusin II), strongly inhibited the human immunodeficiency virus (HIV)-1-induced cytopathic effect and viral antigen expression. The solution structure of T22 was investigated using NMR, and its secondary structure was confirmed to be similar to that of tachyplesin I. The anti-parallel beta-sheet structure and the several amino-acid side chains on the plane of the beta-sheet of T22 are thought to be associated with the expression of anti-HIV activity." citations,entry_citation,5490,225600,1,,entry citation,,,12943529,,,"Mutational epitope analysis of Pru av 1 and Api g 1, the major allergens of cherry (Prunus avium) and celery (Apium graveolens): correlating IgE reactivity with three-dimensional structure",published,journal,Biochem. J.,,376,1,,,,,,,,,,,,,,,,,,,,,,97,107,2003, citations,ref_1,5490,225601,2,,reference citation,,,,,"K. Schweimer, H. Sticht, J. Nerkamp, M. Boehm, M. Breitenbach, S. Vieths and P. Roesch: NMR Spectroscopy Reveals Common Structural Features of the Birch Pollen Allergen Bet v 1 and the Cherry Allergen Pru a 1 Appl. Magn. Reson. 17, 449-464 (1999)",,published,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_2,5490,225602,3,,reference citation,,11061231,,,"P. Neudecker, K. Schweimer, J. Nerkamp, M. Boehm, S. Scheurer, S. Vieths, H. Sticht and P. Roesch: Sequence-specific 1H, 13C and 15N resonance assignments of the major cherry allergen Pru a 1 J. Biomol. NMR 18, 71-72 (2000)",,published,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_3,5490,225603,4,,reference citation,,11287426,,,"P. Neudecker, K. Schweimer, J. Nerkamp, S. Scheurer, S. Vieths, H. Sticht and P. Roesch: Allergic cross-reactivity made visible: solution structure of the major cherry allergen Pru av 1 J. Biol. Chem. 276, 22756-22763 (2001)",,published,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_4,5490,225604,5,,reference citation,,11824757,,,"P. Neudecker, H. Sticht and P. Roesch: Improving the efficiency of the Gaussian conformational database potential for the refinement of protein and nucleic acid structures J. Biomol. NMR. 21, 373-375 (2001)",,published,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_1,5497,225741,2,,reference citation,,,10760137,,"Gordon EH, Page MD, Willis AC, Ferguson SI Escherichia coli DipZ: anatomy of a transmembrane protein disulphide reductase in which three pairs of cysteine residues, one in each of three domains, contribute differentially to function. MolMicrobiol. 2000 Mar:35(6):1360-74","Escherichia coli DipZ: anatomy of a transmembrane protein disulphide reductase in which three pairs of cysteine residues, one in each of three domains, contribute differentially to function.",published,journal,Mol. Microbiol.,Molecular microbiology,35,6,,0950-382X,,,,,,,,,,,,,,,,,,,,1360,1374,2000,"DipZ is a bacterial cytoplasmic membrane protein that transfers reducing power from the cytoplasm to the periplasm so as to facilitate the formation of correct disulphide bonds and c-type cytochromes in the latter compartment. Topological analysis using gene fusions between the Escherichia coli dipZ and either E. coli phoA or lacZ shows that DipZ has a highly hydrophobic central domain comprising eight transmembrane alpha-helices plus periplasmic globular N-terminal and C-terminal domains. The previously assigned translational start codon for the E. coli DipZ was shown to be incorrect and the protein to be larger than previously thought. The experimentally determined translational start position indicates that an additional alpha-helix at the N-terminus acts as a cleavable signal peptide so that the N-terminus of the mature protein is located in the periplasm. The newly assigned 5' end of the dipZ gene was shown to be preceded by a functional ribosome-binding site. The hydrophobic central domain and both of the periplasmic globular domains each have a pair of highly conserved cysteine residues, and it was shown by site directed mutagenesis that all six conserved cysteine residues contribute to DipZ function." citations,entry_citation,5498,225757,1,,entry citation,,22159732,,,,"Diverse Recognition of Non-PxxP Peptide Ligands by the SH3 Domains from p67(phox), Grb2 and Pex13p",published,journal,EMBO J.,,21,16,,,,,,,,,,,,,,,,,,,,,,4268,4276,2002, citations,ref_1,5498,225758,2,,reference citation,,,8520220,,"Delaglio, F. et al. J. Biomol. NMR 6, 277-293 (1995).",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref_2,5498,225759,3,,reference citation,,,9671561,,"Markley, J.L. et al. J. Mol. Biol. 280, 933-952 (1998).",Recommendations for the presentation of NMR structures of proteins and nucleic acids.,published,journal,J. Mol. Biol.,Journal of molecular biology,280,5,,0022-2836,,,,,,,,,,,,,,,,,,,,933,952,1998,"The recommendations presented here are designed to support easier communication of NMR data and NMR structures of proteins and nucleic acids through unified nomenclature and reporting standards. Much of this document pertains to the reporting of data in journal articles; however, in the interest of the future development of structural biology, it is desirable that the bulk of the reported information be stored in computer-accessible form and be freely accessible to the scientific community in standardized formats for data exchange. These recommendations stem from an IUPAC-IUBMB-IUPAB inter-union venture with the direct involvement of ICSU and CODATA. The Task Group has reviewed previous formal recommendations and has extended them in the light of more recent developments in the field of biomolecular NMR spectroscopy. Drafts of the recommendations presented here have been examined critically by more than 50 specialists in the field and have gone through two rounds of extensive modification to incorporate suggestions and criticisms." citations,entry_citation,5499,225775,1,,entry citation,,22287446,12196542,,,"PDZ7 of Glutamate Receptor Interacting Protein Binds to its Target via a Novel Hydrophobic Surface Area",published,journal,J. Biol. Chem.,,277,43,,,,,,,,,,,,,,,,,,,,,,41140,41146,2002, citations,entry_citation,55,225795,1,,entry citation,,,,,"Clore, G. Marius, Sukumaran, Dinesh K., Gronenborn, Angela M., Teeter, Martha M., Whitlow, Marc, Jones, Berne L., ""Nuclear Magnetic Resonance Study of the Solution Structure of alpha 1-Purothionin (Sequential Resonance Assignment, Secondary Structure and Low Resolution Tertiary Structure),"" J. Mol. Biol. 193, 571-578 (1987).","Nuclear Magnetic Resonance Study of the Solution Structure of alpha 1-Purothionin (Sequential Resonance Assignment, Secondary Structure and Low Resolution Tertiary Structure)",published,journal,J. Mol. Biol.,,193,,,,,,,,,,,,,,,,,,,,,,,571,578,1987, citations,entry_citation,5500,225808,1,,entry citation,,,,,,Parkin binds the Rpn10 subunit of 26S proteasomes with the ubiquitin-like domain,published,journal,EMBO Rep.,,4,3,,,,,,,,,,,,,,,,,,,,,,301,306,2003, citations,entry_citation,5501,225832,1,,entry citation,,22241871,12138110,,,"The Solution Structure of Human Hepcidin, a Peptide Hormone with Antimicrobial Activity that is Involved in Iron Uptake and Hereditary Hemochromatosis",published,journal,J. Biol. Chem.,,277,40,,,,,,,,,,,,,,,,,,,,,,37597,37603,2002, citations,entry_citation,5502,225848,1,,entry citation,,22241871,12138110,,,"The Solution Structure of Human Hepcidin, a Peptide Hormone with Antimicrobial Activity that is Involved in Iron Uptake and Hereditary Hemochromatosis",published,journal,J. Biol. Chem.,,277,40,,,,,,,,,,,,,,,,,,,,,,37597,37603,2002, citations,entry_citation,5503,225864,1,,entry citation,,22466550,12578356,,,C-terminal Half of Human Centrin 2 Behaves like a Regulatory EF-hand Domain,published,journal,Biochemistry,,42,6,,,,,,,,,,,,,,,,,,,,,,1439,1450,2003, citations,entry_citation,5504,225883,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N chemical shift assignments of the SH2 domain of the Csk homologous kinase",published,journal,J. Biomol. NMR,,24,4,,,,,,,,,,,,,,,,,,,,,,363,364,2002, citations,entry_citation,5505,225912,1,,entry citation,,22413164,12525159,,,"Backbone Dynamics of Reduced Plastocyanin from the Cyanobacterium Anabaena variabilis: Regions Involved in Electron Transfer have Enhanched Mobility",published,journal,Biochemistry,Biochemistry,42,2,,,,,,,,,,,,,,,,,,,,,,320,330,2003, citations,entry_citation,5539,226732,1,,entry citation,,,14653811,,,"Solution Structure and Stability of the Full-Length Excisionase from Bacteriophage HK022",published,journal,Eur. J. Biochem.,,270,24,,,,,,,,,,,,,,,,,,,,,,4846,4858,2003, citations,ref_1,5505,225913,2,,reference citation,,,8679527,,"U. Badsberg, A. M. M. Jorgensen, H. Gesmar, J. J. Led, J. M. Hammerstad-Petersen, L. L. Jespersen, J. Ulstrup Solution Structure of Reduced Plastocyanin from the Blue-Green Alga Anabaene Variabilis Biochem J. 35, 7021-7031 (1996)",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_2,5505,225914,3,,reference citation,,,,,"L. Ma, J. J. Led. Detrmination by High Field NMR Spectroscopy of the Longitudinal Electron Relaxation Rate in Cu(II) Plastocyanin from Anabaena variabilis. J. Am. Chem. Soc. 122,7823-7824 (2000)",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_3,5505,225915,4,,reference citation,,,,,"L. Ma, A. M. M. Jorgensen, G. O. Sorensen, J. Ulstrup, J. J. Led Elucidation of the Paramagnetic R1 Relaxation of Heteronuclei and Protons in Cu(II) Plastocyanin from Anabaena variabilis. J. A. Chem. Soc. 122, 9473-9485 (2000)",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_4,5505,225916,5,,reference citation,,,11330808,,"L. Ma, E. Philipp, J. J. Led. Determination of the Electron Self-Exchange Rates of Blue Copper Proteins by Super-WEFT NMR Spectroscopy. J. Biomol. NMR 19, 199-208 (2001)",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_5,5505,225917,6,,reference citation,,,,,"M. R. Jensen, D. F. Hansen, J. J. Led A General Method for Determining the Electron Self-Exchange Rates of Blue Copper proteins by longitudinal NMR Relaxation. J. Am. Chem. Soc. 124, 4093-4096 (2002)",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5506,225947,1,,entry citation,,,,,,"Resonance assignments of the central complement control protein module pair of human decay accelerating factor (DAF)",published,journal,J. Biomol. NMR,,23,,,,,,,,,,,,,,,,,,,,,,,167,168,2002, citations,ref_1,5506,225948,2,,reference citation,,,11034410,,"Brodbeck, W.G., Mold, C., Atkinson, J.P. and Medof, M.E. (2000) J. Immunol., 165, 3999-4006.",Cooperation between decay-accelerating factor and membrane cofactor protein in protecting cells from autologous complement attack.,published,journal,J. Immunol.,"Journal of immunology (Baltimore, Md. : 1950)",165,7,,0022-1767,,,,,,,,,,,,,,,,,,,,3999,4006,2000,"Decay-accelerating factor (DAF or CD55) and membrane cofactor protein (MCP or CD46) function intrinsically in the membranes of self cells to prevent activation of autologous complement on their surfaces. How these two regulatory proteins cooperate on self-cell surfaces to inhibit autologous complement attack is unknown. In this study, a GPI-anchored form of MCP was generated. The ability of this recombinant protein and that of naturally GPI-anchored DAF to incorporate into cell membranes then was exploited to examine the combined functions of DAF and MCP in regulating complement intermediates assembled from purified alternative pathway components on rabbit erythrocytes. Quantitative studies with complement-coated rabbit erythrocyte intermediates constituted with each protein individually or the two proteins together demonstrated that DAF and MCP synergize the actions of each other in preventing C3b deposition on the cell surface. Further analyses showed that MCP's ability to catalyze the factor I-mediated cleavage of cell-bound C3b is inhibited in the presence of factors B and D and is restored when DAF is incorporated into the cells. Thus, the activities of DAF and MCP, when present together, are greater than the sum of the two proteins individually, and DAF is required for MCP to catalyze the cleavage of cell-bound C3b in the presence of excess factors B and D. These data are relevant to xenotransplantation, pharmacological inhibition of complement in inflammatory diseases, and evasion of tumor cells from humoral immune responses." citations,ref_2,5506,225949,3,,reference citation,,,11516162,,"Lin, F., Immormino, R.M. and Medof, M.E. (2001) Arch. Biochem. Biophys., 393, 67-72.",Bulk production and functional analyses of mouse CD55's native and deglycosylated active domains.,published,journal,Arch. Biochem. Biophys.,Archives of biochemistry and biophysics,393,1,,0003-9861,,,,,,,,,,,,,,,,,,,,67,72,2001,"We report the use of methylotrophic yeast Pichia pastoris as a host to efficiently express complement control protein repeats (CCPs) 1-4 of mouse decay accelerating factor (DAF, CD55) as a soluble protein. With this system, the mouse DAF CCP1-4-active-domain-containing module linked to a 6x His tag at its C terminus was secreted into the culture supernatant at 15 mg/L after 24 h of induction with methanol. A mouse DAF CCP1-4 mutant protein in which its two potential N-glycosylation sites were deleted by changing Asn(187) and Asn(262) to Gln was also produced. Using Ni(2+)-immobilized agarose affinity chromatography, the recombinant mouse DAF modules with their 6x His tags could be one-step isolated to SDS-PAGE purity. Polyclonal antibody against native mouse DAF CCP1-4 was raised by immunizing NZW rabbits with the purified product. Measurements of the bioactivities of the wild-type and mutant mouse DAF proteins in C3b uptake assays showed no differences in regulatory activities in either the classical or the alternative pathways. With the use of the mutant DAF protein, small rod-shaped crystals were produced and preliminary data obtained. The production of large quantities of functional recombinant mouse DAF CCP1-4 modules and their antibody offers the opportunity to study DAF structure and DAF function in vivo." citations,entry_citation,5507,225969,1,,entry citation,,22090787,12095258,,,"Native State Hydrogen Exchange Study of Suppressor and Pathogenic Variants of Transthyretin",published,journal,J. Mol. Biol.,,320,4,,,,,,,,,,,,,,,,,,,,,,821,832,2002, citations,entry_citation,5508,225987,1,,entry citation,,22090787,12095258,,,"Native State Hydrogen Exchange Study of Suppressor and Pathogenic Variants of Transthyretin",published,journal,J. Mol. Biol.,,320,4,,,,,,,,,,,,,,,,,,,,,,821,832,2002, citations,entry_citation,5509,226004,1,,entry citation,,22090787,12095258,,,"Native State Hydrogen Exchange Study of Suppressor and Pathogenic Variants of Transthyretin",published,journal,J. Mol. Biol.,,320,4,,,,,,,,,,,,,,,,,,,,,,821,832,2002, citations,entry_citation,5510,226021,1,,entry citation,,22090787,12095258,,,"Native State Hydrogen Exchange Study of Suppressor and Pathogenic Variants of Transthyretin",published,journal,J. Mol. Biol.,,320,4,,,,,,,,,,,,,,,,,,,,,,821,832,2002, citations,entry_citation,5511,226038,1,,entry citation,,,,,,"Letter to the Editor: Backbone 1H, 13C, and 15N resonance assignments for the 21 kDa GTPase Rac1 complexed to GDP and Mg2+",published,journal,J. Biomol. NMR,,27,1,,,,,,,,,,,,,,,,,,,,,,87,88,2003, citations,entry_citation,5512,226066,1,,entry citation,,,,,,Letter to the Editor: Solution structure of chicken liver basic type fatty acid binding protein,published,journal,J. Biomol. NMR,,25,2,,,,,,,,,,,,,,,,,,,,,,157,160,2003, citations,entry_citation,5513,226080,1,,entry citation,,,,,,"Letter to the Editor: NMR assignment of the full-length ribosomal protein L11 from Thermotoga maritima",published,journal,J. Biomol. NMR,,25,2,,,,,,,,,,,,,,,,,,,,,,163,164,2003, citations,ref_1,5513,226081,2,,reference citation,,,11519754,,"Markus MA, Triantafillidou D, Choli-Papadopoulou T, Torchia DA. 1H, 15N, and 13C assignments and secondary structure identification for full-length ribosomal protein L11 from Thermus thermophilus. J Biomol NMR. 2001 Jul;20(3):293-4.","1H, 15N, and 13C assignments and secondary structure identification for full-length ribosomal protein L11 from Thermus thermophilus.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,20,3,,0925-2738,,,,,,,,,,,,,,,,,,,,293,294,2001, citations,entry_citation,5541,226784,1,,entry citation,,,,,,"Letter to the Editor: NMR assignment and structural characterization of the fatty acid binding protein from the flight muscle of Locusta migratoria",published,journal,J. Biomol. NMR,,25,4,,,,,,,,,,,,,,,,,,,,,,355,356,2003, citations,ref_2,5513,226082,3,,reference citation,,,10338213,,"Wimberly BT, Guymon R, McCutcheon JP, White SW, Ramakrishnan V. A detailed view of a ribosomal active site: the structure of the L11-RNA complex. Cell. 1999 May 14;97(4):491-502.",A detailed view of a ribosomal active site: the structure of the L11-RNA complex.,published,journal,Cell,Cell,97,4,,0092-8674,,,,,,,,,,,,,,,,,,,,491,502,1999,"We report the crystal structure of a 58 nucleotide fragment of 23S ribosomal RNA bound to ribosomal protein L11. This highly conserved ribonucleoprotein domain is the target for the thiostrepton family of antibiotics that disrupt elongation factor function. The highly compact RNA has both familiar and novel structural motifs. While the C-terminal domain of L11 binds RNA tightly, the N-terminal domain makes only limited contacts with RNA and is proposed to function as a switch that reversibly associates with an adjacent region of RNA. The sites of mutations conferring resistance to thiostrepton and micrococcin line a narrow cleft between the RNA and the N-terminal domain. These antibiotics are proposed to bind in this cleft, locking the putative switch and interfering with the function of elongation factors." citations,ref_3,5513,226083,4,,reference citation,,,9398519,,"Hinck AP, Markus MA, Huang S, Grzesiek S, Kustonovich I, Draper DE, Torchia DA. The RNA binding domain of ribosomal protein L11: three-dimensional structure of the RNA-bound form of the protein and its interaction with 23 S rRNA. J Mol Biol. 1997 Nov 21;274(1):101-13.",The RNA binding domain of ribosomal protein L11: three-dimensional structure of the RNA-bound form of the protein and its interaction with 23 S rRNA.,published,journal,J. Mol. Biol.,Journal of molecular biology,274,1,,0022-2836,,,,,,,,,,,,,,,,,,,,101,113,1997,"The three-dimensional solution structure has been determined by NMR spectroscopy of the 75 residue C-terminal domain of ribosomal protein L11 (L11-C76) in its RNA-bound state. L11-C76 recognizes and binds tightly to a highly conserved 58 nucleotide domain of 23 S ribosomal RNA, whose secondary structure consists of three helical stems and a central junction loop. The NMR data reveal that the conserved structural core of the protein, which consists of a bundle of three alpha-helices and a two-stranded parallel beta-sheet four residues in length, is nearly the same as the solution structure determined for the non-liganded form of the protein. There are however, substantial chemical shift perturbations which accompany RNA binding, the largest of which map onto an extended loop which bridges the C-terminal end of alpha-helix 1 and the first strand of parallel beta-sheet. Substantial shift perturbations are also observed in the N-terminal end of alpha-helix 1, the intervening loop that bridges helices 2 and 3, and alpha-helix 3. The four contact regions identified by the shift perturbation data also displayed protein-RNA NOEs, as identified by isotope-filtered three-dimensional NOE spectroscopy. The shift perturbation and NOE data not only implicate helix 3 as playing an important role in RNA binding, but also indicate that regions flanking helix 3 are involved as well. Loop 1 is of particular interest as it was found to be flexible and disordered for L11-C76 free in solution, but not in the RNA-bound form of the protein, where it appears rigid and adopts a specific conformation as a result of its direct contact to RNA." citations,entry_citation,5514,226113,1,,entry citation,,,,,,"Letter to the editor: Backbone HN, N, Ca and Cb assignment of the GFPuv mutant",published,journal,J. Biomol. NMR,,25,2,,,,,,,,,,,,,,,,,,,,,,161,162,2003, citations,entry_citation,5515,226135,1,,entry citation,,,,,,"1H, 13C and 15N resonance assignment of the Dishevelled DIX domain",in preparation,journal,J. Biomol. NMR,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5516,226162,1,,entry citation,,22410155,12522304,,,"Letter to the Editor: Assignment of the 1H, 13C and 15N Resonances of the Coxsackievirus and Adenovirus Receptor Domain 1",published,journal,J. Biomol. NMR,,24,4,,,,,,,,,,,,,,,,,,,,,,365,366,2002, citations,Bergelson_1997,5516,226163,2,,reference citation,,,9036860,,"Bergelson JM, Cunningham JA, Droguett G, Kurt-Jones EA, Krithivas A, Hong JS, Horwitz MS, Crowell RL, Finberg RW. Isolation of a common receptor for Coxsackie B viruses and adenoviruses 2 and 5. Science. 1997 Feb 28;275(5304):1320-3.",Isolation of a common receptor for Coxsackie B viruses and adenoviruses 2 and 5.,published,journal,Science,"Science (New York, N.Y.)",275,5304,,0036-8075,,,,,,,,,,,,,,,,,,,,1320,1323,1997,"A complementary DNA clone has been isolated that encodes a coxsackievirus and adenovirus receptor (CAR). When transfected with CAR complementary DNA, nonpermissive hamster cells became susceptible to coxsackie B virus attachment and infection. Furthermore, consistent with previous studies demonstrating that adenovirus infection depends on attachment of a viral fiber to the target cell, CAR-transfected hamster cells bound adenovirus in a fiber-dependent fashion and showed a 100-fold increase in susceptibility to virus-mediated gene transfer. Identification of CAR as a receptor for these two unrelated and structurally distinct viral pathogens is important for understanding viral pathogenesis and has implications for therapeutic gene delivery with adenovirus vectors." citations,entry_citation,5517,226178,1,,entry citation,,22699289,12815265,,,"Sequence-specific Assignment of the B-Myb DNA-binding Domain (B-MybR2R3) bound to a 16 Base-pair DNA Target Site Corresponding to a Regulatory Site from the tom-1 Gene",published,journal,J. Biomol. NMR,,26,4,,,,,,,,,,,,,,,,,,,,,,375,376,2003,"NMR studies of the minimal DNA-binding domain of chicken B-Myb (B-MybR2R3) when bound to a double stranded 16-mer DNA target containing the 6 base-pair sequence required for DNA binding by Myb proteins, 5'-AACGGA-3'""" citations,ref_1,5517,226179,2,,reference citation,,,,,"Bartels, C., Xia, T., Billeter, M., Guntert, P. and Wuthrich K. (1995) J. Biol. NMR 6, 1-10. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5518,226201,1,,entry citation,,22617602,12731859,,,"Protein Inhibitors of Serine Proteinases: Role of Backbone Structure and Dynamics in Controlling the Hydrolysis Constant",published,journal,Biochemistry,,42,18,,,,,,,,,,,,,,,,,,,,,,5186,5194,2003, citations,entry_citation,5519,226225,1,,entry citation,,22617602,12731859,,,"Protein Inhibitors of Serine Proteinases: Role of Backbone Structure and Dynamics in Controlling the Hydrolysis Constant",published,journal,Biochemistry,,42,18,,,,,,,,,,,,,,,,,,,,,,5186,5194,2003, citations,entry_citation,5520,226249,1,,entry citation,,22617602,12731859,,,"Protein Inhibitors of Serine Proteinases: Role of Backbone Structure and Dynamics in Controlling the Hydrolysis Constant",published,journal,Biochemistry,,42,18,,,,,,,,,,,,,,,,,,,,,,5186,5194,2003, citations,entry_citation,5521,226299,1,,entry citation,,22617602,12731859,,,"Protein Inhibitors of Serine Proteinases: Role of Backbone Structure and Dynamics in Controlling the Hydrolysis Constant",published,journal,Biochemistry,,42,18,,,,,,,,,,,,,,,,,,,,,,5186,5194,2003, citations,entry_citation,5522,226346,1,,entry citation,,,,,,"Letter to Editor: Backbone 1H, 15N, and 13C resonance assignments of the repeated domain of human beta ig-h3",published,journal,J. Biomol. NMR,,24,4,,,,,,,,,,,,,,,,,,,,,,367,368,2002, citations,entry_citation,554,226747,1,,entry citation,,,,,"Kline, Allen D., Justice, Richard M., Jr., ""Complete Sequence-Specific 1H NMR Assignments for Human Insulin,"" Biochemistry 29, 2906-2913 (1990).",Complete Sequence-Specific 1H NMR Assignments for Human Insulin,published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,2906,2913,1990, citations,entry_citation,5540,226760,1,,entry citation,,22538553,12652141,,,"Letter to the Editor: 1H, 13C and 15N Assignment of the Hydroquinone form of Flavodoxin from Desulfovibrio vulgaris (Hildenborough) and Comparison of the Chemical Shift Differences with Respect to the Oxidized State",published,journal,J. Biomol. NMR,,25,3,,,,,,,,,,,,,,,,,,,,,,257,258,2003, citations,ref_1,5522,226347,2,,reference citation,,,10906123,,"Kim JE, Kim SJ, Lee BH, Park RW, Kim KS, Kim IS, Identification of motifs for cell adhesion within the repeated domains of transforming growth factor-beta-induced gene, betaig-h3 J Biol Chem. 2000 Oct 6;275(40):30907-15","Identification of motifs for cell adhesion within the repeated domains of transforming growth factor-beta-induced gene, betaig-h3.",published,journal,J. Biol. Chem.,The Journal of biological chemistry,275,40,,0021-9258,,,,,,,,,,,,,,,,,,,,30907,30915,2000,"betaig-h3 is a transforming growth factor-beta-inducible cell adhesion molecule that has four characteristic homologous repeated domains. We made recombinant betaig-h3 proteins, which were highly active in mediating human corneal epithelial (HCE) cell adhesion and spreading. The 2nd and the 4th repeated domains were sufficient to mediate HCE cell adhesion. A sequence analysis showed that aspartic acid (Asp) and isoleucine (Ile) of the 2nd and the 4th domains are highly conserved in many fasciclin 1 homologous (fas-1) domains. Substitution mutational study identified these two amino acids are essential for cell adhesion. Synthetic peptides containing Asp and Ile, NKDIL and EPDIM derived from the 2nd and the 4th domains, respectively, almost completely blocked cell adhesion mediated by not only wild type betaig-h3 but also each of the 2nd and the 4th domains. These peptides alone were fully active in mediating cell adhesion. In addition, we demonstrated the functional receptor for betaig-h3 is alpha(3)beta(1) integrin. These results, therefore, establish the essential motifs within the 2nd and the 4th domains of betaig-h3, which interact with alpha(3)beta(1) integrin to mediate HCE cell adhesion to betaig-h3 and suggest that other proteins containing Asp-Ile in their fas-1 domains could possibly function as cell adhesion molecules." citations,entry_citation,5523,226371,1,,entry citation,,,,,,"Conformational Features of Human Melanin-Concentrating Hormone: a NMR and Computational Analysis",in press,journal,Chem. Biochem.,European Journal of Chemical Biology,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5524,226388,1,,entry citation,,,,,,"Letter to the Editor: Resonance Assignment and Topology of a Clostridial Repetitive Oligopeptide (CROP) Region of Toxin A from Clostridium difficile",published,journal,J. Biomol. NMR,,25,1,,,,,,,,,,,,,,,,,,,,,,83,84,2003, citations,entry_citation,5525,226427,1,,entry citation,,22403688,12515557,,,"A Cys3His Zinc-binding Domain from Nup475/Tristetraprolin: A Novel Fold with a Disklike Structure",published,journal,Biochemistry,,42,1,,,,,,,,,,,,,,,,,,,,,,217,221,2003, citations,entry_citation,5527,226457,1,,entry citation,,22344611,12228241,,,"Function and Solution Structure of Huwentoxin-IV, a Potent Nueronal Tetrodotoxin (TTX)-sensitive Sodium Channel Antagonist from Chinese Bird Spider Selenocosmia huwena",published,journal,J. Biol. Chem.,,277,49,,,,,,,,,,,,,,,,,,,,,,47564,47571,2002, citations,entry_citation,5528,226472,1,,entry citation,,22656697,12771209,,,"Solution Structure of the Influenza A Virus cRNA Promoter: Implications for Differential Recognition of Viral Promoter Structures by RNA-dependent RNA Polymerase",published,journal,Nucleic Acids Res.,,31,11,,,,,,,,,,,,,,,,,,,,,,2824,2832,2003, citations,entry_citation,5529,226499,1,,entry citation,,22593395,12706725,,,"The Mechanism of Interaction of Sweet Proteins with the T1R2-T1R3 Receptor: Evidence from the Solution Structure of G16A-MNEI",published,journal,J. Mol. Biol.,,328,3,,,,,,,,,,,,,,,,,,,,,,683,692,2003, citations,entry_citation,5530,226522,1,,entry citation,,,14643656,,,"Naturally occurring modifications restricts the anticodon domain conformational space of tRNA-PHE",published,journal,J. Mol. Biol.,,334,5,,,,,,,,,,,,,,,,,,,,,,901,918,2003, citations,entry_citation,5531,226546,1,,entry citation,,,14643656,,,"Naturally occurring modifications restricts the anticodon domain conformational space of tRNA-PHE",published,journal,J. Mol. Biol.,,334,5,,,,,,,,,,,,,,,,,,,,,,901,918,2003, citations,entry_citation,5532,226572,1,,entry citation,,22289677,12379843,,,"Structure of the Tsg101 UEV Domain in Complex with the PTAP Motif of the HIV-1 p6 Protein",published,journal,Nat. Struct. Biol.,,9,11,,,,,,,,,,,,,,,,,,,,,,812,817,2002, citations,entry_citation,5534,226599,1,,entry citation,,22478854,12590574,,,"Global Structure and Dynamics of Human Apolipoprotein CII in Complex with Micelles: Evidence for Increased Mobility of the Helix involved in the Activation of Lipoprotein Lipase",published,journal,Biochemistry,,42,7,,,,,,,,,,,,,,,,,,,,,,1872,1889,2003, citations,ref_1,5534,226600,2,,reference citation,,,14512728,,"Larsson, G., Martinez, G., Schleucher, J., Wijmenga, S.S. (2002) Detection of nanosecond internal motion and determination of overall tumbling times from NMR relaxation data; submitted",Detection of nano-second internal motion and determination of overall tumbling times independent of the time scale of internal motion in proteins from NMR relaxation data.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,27,4,,0925-2738,,,,,,,,,,,,,,,,,,,,291,312,2003,"The usual analysis of (15)N relaxation data of proteins is straightforward as long as the assumption can be made that the backbone of most residues only undergoes fast (ps), small amplitude internal motions. If this assumption cannot be made, as for example for proteins which undergo domain motions or for unfolded or partially folded proteins, one needs a method to establish for each residue whether it undergoes fast (ps) or slow (ns) internal motion. Even then it is impossible to determine the correct overall tumbling time, tau(m)(0), via the usual method from the ratio of the longitudinal and transverse relaxation times, if the majority of residues do not undergo fast, small amplitude internal motions. The latter problem is solved when tau(m)(0) can be determined independent of the time scale, tau(i), or the amplitude, S(2), of the internal motion. We propose a new protocol, called PINATA, for analyzing (15)N relaxation data acquired at minimally two field strengths, where no a priori assumption about time scales or amplitude of internal motions needs to be made, and overall tumbling can either be isotropic or anisotropic. The protocol involves four steps. First, for each residue, it is detected whether it undergoes ps- or ns-internal motion, via the combination of the ratio of the longitudinal relaxation time at two fields and the hetero-nuclear NOE. Second, for each residue tau(m)(0) and the exchange broadening, Rex, are iteratively determined. The accuracy of the determination of tau(m)(0) is ca. +/-0.5 ns and of Rex ca +/- 0.7 s(-1), when the relaxation data are of good quality and tau(m)(0)>5 ns, S(2)>0.3, and tau(i)< approximately 3 ns. Third, given tau(m)(0) and Rex, step 1 is repeated to iteratively improve on the internal motion and obtain better estimates of the internal parameter values. Fourth, final time scales and amplitudes for internal motions are determined via grid search based fitting and chi(2)-analysis. The protocol was successfully tested on synthetic and experimental data sets. The synthetic dataset mimics internal motions on either fast or slow time scales, or a combination of both, of either small- or large amplitude, superimposed onto anisotropic overall motion. The procedures are incorporated into MATLAB scripts, which are available on request." citations,ref_2,5534,226601,3,,reference citation,,,,,"Larsson, Wijmenga, Schleucher: J. Biomol. NMR 14 (1999), 169-174",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,spin-lock HCANH citations,entry_citation,5535,226632,1,,entry citation,,,12547203,,,Solution Structure of the R3H Domain from Human Subp-2,published,journal,J. Mol. Biol.,,326,1,,,,,,,,,,,,,,,,,,,,,,217,223,2003, citations,reference_1,5535,226633,2,,reference citation,,,12547203,,"Edvards Liepinsh, Ainars Leonchiks, Anatoly Sharipo, Laurent Guignard and Gottfried Otting. Solution structure of the R3H domain from human Subp-2 J. Biol. Chem., submitted.",Solution structure of the R3H domain from human Smubp-2.,published,journal,J. Mol. Biol.,Journal of molecular biology,326,1,,0022-2836,,,,,,,,,,,,,,,,,,,,217,223,2003,"The R3H domain is a conserved sequence motif, identified in over 100 proteins, that is thought to be involved in polynucleotide-binding, including DNA, RNA and single-stranded DNA. In this work the 3D structure of the R3H domain from human Smubp-2 was determined by NMR spectroscopy. It is the first 3D structure determination of an R3H domain. The fold presents a small motif, consisting of a three-stranded antiparallel beta-sheet and two alpha-helices, which is related to the structures of the YhhP protein and the C-terminal domain of the translational initiation factor IF3. The similarities are non-trivial, as the amino acid identities are below 10%. Three conserved basic residues cluster on the same face of the R3H domain and could play a role in nucleic acid recognition. An extended hydrophobic area at a different site of the molecular surface could act as a protein-binding site. A strong correlation between conservation of hydrophobic amino acids and side-chain solvent protection indicates that the structure of the Smubp-2 R3H domain is representative of R3H domains in general." citations,entry_citation,5536,226650,1,,entry citation,,,17172296,,,"Folding stability and cooperativity of the three forms of 1-110 residues fragment of staphylococcal nuclease",published,journal,Biophys. J.,,92,6,,,,,,,,,,,,,,,,,,,,,,2090,2107,2007, citations,citation,5536,226651,2,,reference citation,,,12850150,,,"Native-like partially folded conformations and folding process revealed in the N-terminal large fragments of staphylococcal nuclease: a study by NMR spectroscopy",published,journal,J. Mol. Biol.,,330,4,,,,,,,,,,,,,,,,,,,,,,821,837,2003, citations,entry_citation,5537,226677,1,,entry citation,,22269617,12381297,,,The Structure of an FF Domain from Human HYPA/FBP11,published,journal,J. Mol. Biol.,,323,3,,,,,,,,,,,,,,,,,,,,,,411,416,2002, citations,ref_1,5541,226785,2,,reference citation,,,8174560,,"R.G.H.J. Maatman, M. Degano, H.T.B. Van Moerkerk, W.J. Van Marrewijk, D.J. Van der Horst, J.C. Sacchettini, and J.H. Veerkamp (1994) Primary structure and binding characteristics of locust and human muscle fatty-acid-binding proteins. Eur. J. Biochem. 221, 801-810.",Primary structure and binding characteristics of locust and human muscle fatty-acid-binding proteins.,published,journal,Eur. J. Biochem.,European journal of biochemistry / FEBS,221,2,,0014-2956,,,,,,,,,,,,,,,,,,,,801,810,1994,"The conservation between muscle fatty-acid-binding proteins (M-FABP) of Locusta migratoria flight muscle and human skeletal muscle was investigated. The locust M-FABP cDNA (632 bp) was isolated by 5' and 3' rapid amplification of cDNA ends. The identities of the locust and human M-FABP on the cDNA and protein levels were 54% and 42%, respectively. The predicted amino acid sequence of locust M-FABP indicated a molecular mass of 14935 Da and isoelectric point 6.1. The locust M-FABP was expressed in Escherichia coli, purified by (NH4)2SO4 precipitation, anion-exchange and gel-filtration chromatographies and compared with the recombinant human M-FABP with respect to immunological and binding properties. In spite of the high sequence similarity, the proteins did not show immunological cross-reactivity. The binding parameters of locust M-FABP were analyzed with radiolabeled oleic acid by the Lipidex assay and titration microcalorimetry. Both methods revealed a Kd for oleic acid of 0.5 microM and a binding stoichiometry of 1 mol fatty acid/mol FABP. The delta H, delta G and delta S for oleic acid binding were -146 kJ.mol-1 and -36 J.mol-1 and -369 J.mol-1.K-1 respectively. All the information obtained from binding, fluorescence and displacement studies indicated that locust M-FABP has binding characteristics similar to human M-FABP. Finally the recombinant locust M-FABP was crystallized with and without oleic acid. All crystals were trigonal in the P3(1)21 space group. The unit cell dimensions were a = b = 5.89 nm and c = 14.42 nm." citations,entry_citation,5542,226811,1,,entry citation,,22731168,12846839,,,"Structure and Positioning Comparison of Two Variants of Penetratin in Two Different Membrane Mimicking Systems by NMR",published,journal,Eur. J. Biochem.,,270,14,,,,,,,,,,,,,,,,,,,,,,3055,3063,2003, citations,entry_citation,5543,226825,1,,entry citation,,22731168,12846839,,,"Structure and Positioning Comparison of Two Variants of Penetratin in Two Different Membrane Mimicking Systems by NMR",published,journal,Eur. J. Biochem.,,270,14,,,,,,,,,,,,,,,,,,,,,,3055,3063,2003, citations,entry_citation,5544,226842,1,,entry citation,,,12470955,,,"Solution NMR structure of S100B bound to the high-affinity target peptide TRTK-12",published,journal,J. Mol. Biol.,,324,5,,,,,,,,,,,,,,,,,,,,,,1003,1014,2002, citations,entry_citation,5545,226862,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N resonance assignments of the C-terminal domain of insulin-like growth factor binding protein-6 (IGFBP-6)",published,journal,J. Biomol. NMR,,25,3,,,,,,,,,,,,,,,,,,,,,,251,252,2003, citations,entry_citation,5547,226877,1,,entry citation,,,,,,"Letter to the Editor: Backbone 1H, 15N and 13C resonance assignments of the 28 kDa mature form of streptopain*",published,journal,J. Biomol. NMR,,25,2,,,,,,,,,,,,,,,,,,,,,,165,166,2003, citations,entry_citation,5548,226921,1,,entry citation,,22255077,12367532,,,"Bovine Pancreatic Polypeptide (bPP) Undergoes Significant Changes in Conformation and Dynamics upon Binding to DPC Micelles",published,journal,J. Mol. Biol.,,322,5,,,,,,,,,,,,,,,,,,,,,,1117,1133,2002, citations,ref_1,5548,226922,2,,reference citation,,,,,"Bartels, C., Xia, T.-h., Billeter, M., Guntert, P. & Wuthrich, K. (1995). The program XEASY for computer-supported spectral analysis of biological macromolecules. J. Biomol. NMR 6, 1-10.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_2,5548,226923,3,,reference citation,,,,,"Weiner, P. K., Kollman, P. A., Nguyen, D. T. & Case, D. A. (1986). An all-atom force field for simulations of proteins and nucleic acids. J. Comput. Chem. 7, 230-52.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_3,5548,226924,4,,reference citation,,,9367762,,"Guntert, P., Mumenthaler, C. & Wuthrich, K. (1997). Torsion Angle Dynamics For NMR Structure Calculation With the New Program Dyana. J. Mol. Biol. 273, 283-298.",Torsion angle dynamics for NMR structure calculation with the new program DYANA.,published,journal,J. Mol. Biol.,Journal of molecular biology,273,1,,0022-2836,,,,,,,,,,,,,,,,,,,,283,298,1997,"The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from distance constraints and torsion angle constraints collected by nuclear magnetic resonance (NMR) experiments performs simulated annealing by molecular dynamics in torsion angle space and uses a fast recursive algorithm to integrate the equations of motions. Torsion angle dynamics can be more efficient than molecular dynamics in Cartesian coordinate space because of the reduced number of degrees of freedom and the concomitant absence of high-frequency bond and angle vibrations, which allows for the use of longer time-steps and/or higher temperatures in the structure calculation. It also represents a significant advance over the variable target function method in torsion angle space with the REDAC strategy used by the predecessor program DIANA. DYANA computation times per accepted conformer in the ""bundle"" used to represent the NMR structure compare favorably with those of other presently available structure calculation algorithms, and are of the order of 160 seconds for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300 computer. Test calculations starting from conformers with random torsion angle values further showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures." citations,entry_citation,5549,226959,1,,entry citation,,22064968,12069594,,,"Key Motif to Gain Selectivity at the Neuropeptide Y5-receptor: Structure and Dynamics of Micelle-bound [Ala31,Pro32]-NPY",published,journal,Biochemistry,,41,25,,,,,,,,,,,,,,,,,,,,,,8031,8042,2002, citations,entry_citation,555,226986,1,,entry citation,,,,,"Kline, Allen D., Justice, Richard M., Jr., ""Complete Sequence-Specific 1H NMR Assignments for Human Insulin,"" Biochemistry 29, 2906-2913 (1990).",Complete Sequence-Specific 1H NMR Assignments for Human Insulin,published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,2906,2913,1990, citations,entry_citation,5550,226999,1,,entry citation,,20574507,11124908,,,"Structure and Dynamics of Micelle-bound Neuropeptide Y: Comparison with Unligated NPY and Implications for Receptor Selection",published,journal,J. Mol. Biol.,,305,2,,,,,,,,,,,,,,,,,,,,,,307,329,2001, citations,entry_citation,5551,227032,1,,entry citation,,22571157,12684009,,,"Homologous Proteins with Different Folds: The Three-dimensional Structures of Domains One and Six of the Multiple Kazal-type Inhibitor LEKTI",published,journal,J. Mol. Biol.,Journal of Molecular Biology,328,1,,,,,,,,,,,,,,,,,,,,,,205,219,2003, citations,entry_citation,5552,227047,1,,entry citation,,22465240,12575935,,,"Solution Structure of the MAPK Phosphotase PAC-1: Catalytic Domain. Insights into Substrate-induced Enzymatic Activation of MKP",published,journal,Structure,,11,2,,,,,,,,,,,,,,,,,,,,,,155,164,2003, citations,entry_citation,5553,227068,1,,entry citation,,22470239,12582241,,,"A Single-nucleotide Natural Variation (U4 to C4) in an Influenza A Virus Promoter Exhibits a Large Structural Change: Implications for Differential Viral RNA Synthesis by RNA-dependent RNA Polymerase",published,journal,Nucleic Acids Res.,,31,4,,,,,,,,,,,,,,,,,,,,,,1216,1223,2003, citations,entry_citation,5554,227089,1,,entry citation,,22325811,12437929,,,"Structure of the N-WASP EVH1 Domain-WIP Complex: Insight into the Molecular Basis of Wiskott-Aldrich Syndrome",published,journal,Cell,,111,4,,,,,,,,,,,,,,,,,,,,,,565,576,2002, citations,entry_citation,556,227229,1,,entry citation,,,,,"Weiss, Michael A., Nguyen, Dzung T., Khait, Igor, Inouye, Ken, Frank, Bruce H., Beckage, Michael, O'Shea, Erin, Shoelson, Steven E., Karplus, Martin, Neuringer, Leo J., ""Two-Dimensional NMR and Photo-CIDNP Studies of the Insulin Monomer: Assignment of Aromatic Resonances with Application to Protein Folding, Structure, and Dynamics,"" Biochemistry 28, 9855-9873 (1989).","Two-Dimensional NMR and Photo-CIDNP Studies of the Insulin Monomer: Assignment of Aromatic Resonances with Application to Protein Folding, Structure, and Dynamics",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,9855,9873,1989, citations,entry_citation,5560,227242,1,,entry citation,,,,,,"Letter to the Editor: NMR assignment of the conserved hypothetical protein TM1290 of Thermotoga maritima",published,journal,J. Biomol. NMR,,25,2,,,,,,,,,,,,,,,,,,,,,,167,168,2003, citations,entry_citation,5561,227267,1,,entry citation,,,12538893,,,NMR Solution Structure of the Activation Domain of Human Procarboxipeptidase A2,published,journal,Protein Sci.,,12,2,,,,,,,,,,,,,,,,,,,,,,296,305,2003, citations,ref_1,5561,227268,2,,reference citation,,,7896805,,"Catasus Ll, Vendrell J, Aviles FX, Carreira S, Puigserver & Billeter M. The sequence and conformation of human pancratic procarboxipeptidase A2. cDNA cloning, sequence analysis, and 3D model. J. Biol. Chem. 270, 6651-6657 (1995).","The sequence and conformation of human pancreatic procarboxypeptidase A2. cDNA cloning, sequence analysis, and three-dimensional model.",published,journal,J. Biol. Chem.,The Journal of biological chemistry,270,12,,0021-9258,,,,,,,,,,,,,,,,,,,,6651,6657,1995,"A full-length cDNA clone coding for human pancreatic preprocarboxypeptidase A2 has been isolated from a lambda gt 11 human pancreatic library. Expression clones were identified by specific interaction with antisera raised against the native protein. The open reading frame of the polynucleotide sequence is 1254 base pairs in length and encodes a protein of 417 amino acids. This cDNA includes a short leader signal peptide of 16 amino acids and a 94-amino acid-long activation segment. The amino acid sequence shows 89% identity to that of rat procarboxypeptidase A2, the only A2 form sequenced so far, and 64% identity to that of human procarboxypeptidase A1. The newly determined sequence was modeled to the three-dimensional crystal structures of both bovine carboxypeptidase A and porcine procarboxypeptidase A1 by a novel distance geometry approach. Biases in the modeling were avoided by relying exclusively on automatic procedures and by using random structures as starting points. Information taken from the known homologous structures refers only to the backbone since no explicit data describing the conformation of side chains were transferred. Ten structures of human carboxypeptidase A2 were determined on the basis of each of the two known crystal structures. The root-mean-square distance for the backbone atoms between the 10 structures and their mean for 237 selected residues is 0.7 A when starting from the bovine protein and 0.8 A for 251 selected residues when starting from the porcine protein. The 94 residue-long activation segment was also determined in the modeling based on the porcine zymogen; its structure is well defined but not its orientation with respect to the enzyme moiety. The model obtained for human procarboxypeptidase A2 is discussed with respect to the specificity and activation of the enzyme." citations,entry_citation,5562,227290,1,,entry citation,,22533216,12646170,,,"NMR Study of Hexanucleotide d(CCGCGG)2 Containing Two Triplet Repeats of Fragile X Syndrome",published,journal,Biochem. Biophys. Res. Commun.,,303,1,,,,,,,,,,,,,,,,,,,,,,81,90,2003, citations,entry_citation,5563,227306,1,,entry citation,,,14622405,,,"ParG, a protein required for active partition of bacterial plasmids, has a dimeric ribbon-helix-helix structure",published,journal,Mol. Microbiol.,,50,4,,,,,,,,,,,,,,,,,,,,,,1141,1153,2003, citations,reference_1,5563,227307,2,,reference citation,,,10931346,,"Hayes F. The partition system of multidrug resistance plasmid TP228 includes a novel protein that epitomizes an evolutionarily distinct subgroup of the ParA superfamily. Mol Microbiol. 2000 Aug;37(3):528-41.",The partition system of multidrug resistance plasmid TP228 includes a novel protein that epitomizes an evolutionarily distinct subgroup of the ParA superfamily.,published,journal,Mol. Microbiol.,Molecular microbiology,37,3,,0950-382X,,,,,,,,,,,,,,,,,,,,528,541,2000,"The segregational stability of bacterial, low-copy-number plasmids is promoted primarily by active partition. The plasmid-specified components of the prototypical P1 plasmid partition system consist of two proteins, ParA (44.3 kDa) and ParB (38.5 kDa), which, in conjunction with integration host factor, form a nucleoprotein complex at the plasmid partition site, parS. This complex is the probable substrate for the directed temporal and spatial intracellular movement of plasmids before cell division. The genetic organization of the partition cassette of the multidrug resistance plasmid TP228 differs markedly from that of the P1 paradigm. The TP228 system includes a novel member (ParF; 22.0 kDa) of the ParA superfamily of ATPases, of which the P1 ParA protein is the archetype. However, the ParF protein and its immediate relatives form a discrete subgroup of the ParA superfamily, which evolutionarily is more related to the MinD subgroup of cell division proteins than to ParA of P1. The TP228 and P1 partition modules differ further in that the former does not include a parB homologue, but does specify a protein (ParG; 8.6 kDa) unrelated to ParB. Homologues of the parF gene are widely disseminated on eubacterial genomes, suggesting that ParF-mediated partition may be a common mechanism by which plasmid segregational stability is achieved." citations,entry_citation,5564,227321,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N resonance assignments of the kinase-interacting FHA domain of Arabidopsis thaliana kinase-associated protein phosphatase",published,journal,J. Biomol. NMR,,25,3,,,,,,,,,,,,,,,,,,,,,,253,254,2003, citations,entry_citation,5565,227349,1,,entry citation,,,,,,Disulfide pairings and structure of porcine beta-microseminoprotein,published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5566,227363,1,,entry citation,,,,,,"Letter to the Editor: 1H, 15N and 13C resonance assignments for the PTB domain of the signaling protein Shc",published,journal,J. Biomol. NMR,,25,3,,,,,,,,,,,,,,,,,,,,,,255,256,2003, citations,entry_citation,5567,227376,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N Resonance Assignments of a Viral SET domain Histone Lysine Methyltransferase",published,journal,J. Biomol. NMR,,26,3,,,,,,,,,,,,,,,,,,,,,,279,280,2003, citations,entry_citation,5568,227389,1,,entry citation,,22603295,12717036,,,"A Novel Member of the Split Betaaalphabeta Fold: Solution Structure of the Hypothetical Protein YML108W from Saccharomyces cerevisiae",published,journal,Protein Sci.,,12,5,,,,,,,,,,,,,,,,,,,,,,1136,1140,2003, citations,entry_citation,5569,227415,1,,entry citation,,22361676,12473458,,,"Heat Capacities and a Snapshot of the Energy Landscape in Protein GB1 from the Pre-denaturation Temperature Dependence of Backbone NH Nanosecond Fluctuations",published,journal,J. Mol. Biol.,,325,1,,,,,,,,,,,,,,,,,,,,,,149,162,2003, citations,ref_1,5569,227416,2,,reference citation,,,,,"Johnson, B.A., Blevins, R.A.; NMRView: A computer program for the visualization and analysis of NMR data J. Biomol. NMR, Vol. 4, 1994, pp.603-614.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_2,5569,227417,3,,reference citation,,,8589604,,"N.A.Farrow, O.Zhang, A.Szabo, D.A.Torchia, L.E.Kay, Spectral density function mapping using 15N relaxation data exclusively. Journal of Biomol NMR, Vol.6, 1995, pp 153-162.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_3,5569,227418,4,,reference citation,,,11700091,,"D.Idiyatullin, V.Daragan, K.H.Mayo, Improved Measurement of 15N-{H} NOEs in the Presence of H(N)-Water Proton Chemical Exchange, Journal of Magnetic Resonance, Vol. 153, No. 1,2001, pp.138-143.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5650,229431,1,,entry citation,,,,,,NMR structure of the ribosomal protein L23 from Thermus Thermophilus,published,journal,J. Biomol. NMR,,26,2,,,,,,,,,,,,,,,,,,,,,,131,137,2003, citations,entry_citation,557,227532,1,,entry citation,,,,,"Weiss, Michael A., Nguyen, Dzung T., Khait, Igor, Inouye, Ken, Frank, Bruce H., Beckage, Michael, O'Shea, Erin, Shoelson, Steven E., Karplus, Martin, Neuringer, Leo J., ""Two-Dimensional NMR and Photo-CIDNP Studies of the Insulin Monomer: Assignment of Aromatic Resonances with Application to Protein Folding, Structure, and Dynamics,"" Biochemistry 28, 9855-9873 (1989).","Two-Dimensional NMR and Photo-CIDNP Studies of the Insulin Monomer: Assignment of Aromatic Resonances with Application to Protein Folding, Structure, and Dynamics",published,journal,Biochemistry,,28,,,,,,,,,,,,,,,,,,,,,,,9855,9873,1989, citations,entry_citation,5570,227545,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C, and 15N NMR assignments of the hypothetical Nudix protein DR0079 from the extremely radiation-resistant bacterium Deinococcus radiodurans",published,journal,J. Biomol. NMR,,25,2,,,,,,,,,,,,,,,,,,,,,,169,170,2003, citations,entry_citation,5571,227571,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N assignment of the hydroquinone form of flavodoxin from Desulfovibrio vulgaris (Hildenborough) and comparison of the chemical shift differences with respect to the oxidized state",published,journal,J. Biomol. NMR,,25,3,,,,,,,,,,,,,,,,,,,,,,257,258,2003, citations,entry_citation,5572,227595,1,,entry citation,,20372205,10917537,,,"Beta-helix structure and ice-binding properties of a hyperactive antifreeze protein from an insect",published,journal,Nature,,406,6793,,,,,,,,,,,,,,,,,,,,,,325,328,2000, citations,entry_citation,5573,227608,1,,entry citation,,22549853,12662938,,,"Spruce Budworm Antifreeze Protein: Changes in Structure and Dynamics at Low Temperature",published,journal,J. Mol. Biol.,,327,5,,,,,,,,,,,,,,,,,,,,,,1155,1168,2003, citations,ref_1,5573,227609,2,,reference citation,,10917537,,,"Graether S., Kuiper M., Gagne S., Walker V., Jia Z., Sykes B., and Davies P., Beta-helix structure and ice-binding properties of a hyperactive antifreeze protein from an insect. Nature 2000 Jul 20;406(6793): 325-328",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5574,227621,1,,entry citation,,,11245256,,,Lipid induced conformation of the tachykinin peptide Kassinin,published,journal,J. Biomol. Struct. Dyn.,,18,4,,,,,,,,,,,,,,,,,,,,,,611,625,2001,"Journal of Biomolecular Structure and dynamics, Vol 18,Issue number 4(2001),611-625." citations,entry_citation,5575,227638,1,,entry citation,,22411914,12524318,,,Solution Structure of the Tachykinin Peptide Eledoisin,published,journal,Biophys. J.,,84,1,,,,,,,,,,,,,,,,,,,,,,655,664,2003,"Biophysical Journal Vol:84(1), 2003" citations,entry_citation,5576,227656,1,,entry citation,,,12730684,,,"ATP-induced Conformational Changes of the Nucleotide-binding Domain of Na, K-ATPase",published,journal,Nat. Struct. Biol.,,10,6,,,,,,,,,,,,,,,,,,,,,,468,474,2003, citations,entry_citation,5577,227678,1,,entry citation,,,12730684,,,"ATP-induced Conformational Changes of the Nucleotide-binding Domain of Na, K-ATPase",published,journal,Nat. Struct. Biol.,,10,6,,,,,,,,,,,,,,,,,,,,,,468,474,2003, citations,entry_citation,5578,227697,1,,entry citation,,22734647,12850148,,,"Two Homologous Rat Cellular Retinol-binding Proteins Differ in Local Conformational Flexibility",published,journal,J. Mol. Biol.,,330,4,,,,,,,,,,,,,,,,,,,,,,799,812,2003, citations,entry_citation,5579,227727,1,,entry citation,,22734647,12850148,,,"Two Homologous Rat Cellular Retinol-binding Proteins Differ in Local Conformational Flexibility",published,journal,J. Mol. Biol.,,330,4,,,,,,,,,,,,,,,,,,,,,,799,812,2003, citations,entry_citation,558,227755,1,,entry citation,,,,,"Baillargeon, Mary Welch, Laskowski, Jr., Michael, Neves, Darrow E., Porubcan, Michael A., Santini, Robert E., Markley, John L., ""Soybean Trypsin Inhibitor (Kunitz) and Its Complex with Trypsin. Carbon-13 Nuclear Magnetic Resonance Studies of the Reactive Site Arginine,"" Biochemistry 19 (25), 5703-5710 (1980).","Soybean Trypsin Inhibitor (Kunitz) and Its Complex with Trypsin. Carbon-13 Nuclear Magnetic Resonance Studies of the Reactive Site Arginine",published,journal,Biochemistry,,19,25,,,,,,,,,,,,,,,,,,,,,,5703,5710,1980, citations,entry_citation,5580,227768,1,,entry citation,,22566040,12562773,,,"NMR Study of Mersacidin and Lipid II Interaction in Dodecylphosphocholine Micelles: Conformational Changes are a Key to Antimicrobial Activity",published,journal,J. Biol. Chem.,,278,15,,,,,,,,,,,,,,,,,,,,,,13110,13117,2003, citations,X-ray_structure,5580,227769,2,,reference citation,,,10818347,,"Schneider TR, Karcher J, Pohl E, Lubini P, Sheldrick GM. Ab initio structure determination of the lantibiotic mersacidin. Acta Crystallogr D Biol Crystallogr. 2000 Jun;56 (Pt 6):705-13.",Ab initio structure determination of the lantibiotic mersacidin.,published,journal,Acta Crystallogr. D Biol. Crystallogr.,"Acta crystallographica. Section D, Biological crystallography",56,Pt 6,,0907-4449,,,,,,,,,,,,,,,,,,,,705,713,2000,"The crystal structure of mersacidin, a potential novel antibiotic against methicillin- and vancomycin-resistant Staphylococcus aureus strains, has been determined by ab initio methods. Despite all crystals being merohedrally twinned, an accurate structural model with an R value of 13.4% has been obtained at atomic resolution. With six molecules in the asymmetric unit and no atom heavier than sulfur, the structure corresponds to a protein of 120 amino acids and is the largest approximately equal-atom unknown structure solved by direct methods. In the crystal, the molecule assumes a compact fold different from that found by NMR in solution. Comparison of the NCS-related molecules reveals regions of variable flexibility. The region highly homologous to the related antibiotic actagardine is very rigid and possibly defines an essential building block of this class of new antibacterial substances." citations,NMR_structure,5580,227770,3,,reference citation,,,9119018,,"Prasch T, Naumann T, Markert RL, Sattler M, Schubert W, Schaal S, Bauch M, Kogler H, Griesinger C. Constitution and solution conformation of the antibiotic mersacidin determined by NMR and molecular dynamics. Eur J Biochem. 1997 Mar 1;244(2):501-12.",Constitution and solution conformation of the antibiotic mersacidin determined by NMR and molecular dynamics.,published,journal,Eur. J. Biochem.,European journal of biochemistry / FEBS,244,2,,0014-2956,,,,,,,,,,,,,,,,,,,,501,512,1997,"The solution structure of the tetracyclic lantibiotic mersacidin in methanol (CD3OH) has been determined by NMR followed by distance bound driven dynamics and subsequent restrained molecular dynamics simulations combined with an iterative relaxation matrix approach and alternatively by a simulated annealing protocol. The molecular dynamics simulations were performed with the AMBER program system and with the INSIGHT program package. The distance bound driven dynamics calculation was conducted using a modified version of the DISGEO II program. The interproton distance restraints were derived from jump symmetrized rotating-frame Overhauser enhancement and exchange (JS-ROESY) spectra, which yield optimum sensitivity for medium-sized molecules like mersacidin. The connectivities via the sulfide bridges were unambiguously confirmed by heteronuclear NMR techniques (heteronuclear single quantum coherence and heteronuclear multiple bond correlation methods). Due to the tetracyclic structure, mersacidin exhibits a rather rigid globular shape, which neither belongs to the duramycin nor to the nisin structure type lantibiotics. The resulting structures for the simulated annealing protocol of restrained and subsequent free molecular dynamics were compared and found to be very similar." citations,entry_citation,5581,227790,1,,entry citation,,22566040,12562773,,,"NMR Study of Mersacidin and Lipid II Interaction in Dodecylphosphocholine Micelles: Conformational Changes are a Key to Antimicrobial Activity",published,journal,J. Biol. Chem.,,278,15,,,,,,,,,,,,,,,,,,,,,,13110,13117,2003, citations,X-ray_structure,5581,227791,2,,reference citation,,,10818347,,"Schneider TR, Karcher J, Pohl E, Lubini P, Sheldrick GM. Ab initio structure determination of the lantibiotic mersacidin. Acta Crystallogr D Biol Crystallogr. 2000 Jun;56 (Pt 6):705-13.",Ab initio structure determination of the lantibiotic mersacidin.,published,journal,Acta Crystallogr. D Biol. Crystallogr.,"Acta crystallographica. Section D, Biological crystallography",56,Pt 6,,0907-4449,,,,,,,,,,,,,,,,,,,,705,713,2000,"The crystal structure of mersacidin, a potential novel antibiotic against methicillin- and vancomycin-resistant Staphylococcus aureus strains, has been determined by ab initio methods. Despite all crystals being merohedrally twinned, an accurate structural model with an R value of 13.4% has been obtained at atomic resolution. With six molecules in the asymmetric unit and no atom heavier than sulfur, the structure corresponds to a protein of 120 amino acids and is the largest approximately equal-atom unknown structure solved by direct methods. In the crystal, the molecule assumes a compact fold different from that found by NMR in solution. Comparison of the NCS-related molecules reveals regions of variable flexibility. The region highly homologous to the related antibiotic actagardine is very rigid and possibly defines an essential building block of this class of new antibacterial substances." citations,NMR_structure,5581,227792,3,,reference citation,,,9119018,,"Prasch T, Naumann T, Markert RL, Sattler M, Schubert W, Schaal S, Bauch M, Kogler H, Griesinger C. Constitution and solution conformation of the antibiotic mersacidin determined by NMR and molecular dynamics. Eur J Biochem. 1997 Mar 1;244(2):501-12.",Constitution and solution conformation of the antibiotic mersacidin determined by NMR and molecular dynamics.,published,journal,Eur. J. Biochem.,European journal of biochemistry / FEBS,244,2,,0014-2956,,,,,,,,,,,,,,,,,,,,501,512,1997,"The solution structure of the tetracyclic lantibiotic mersacidin in methanol (CD3OH) has been determined by NMR followed by distance bound driven dynamics and subsequent restrained molecular dynamics simulations combined with an iterative relaxation matrix approach and alternatively by a simulated annealing protocol. The molecular dynamics simulations were performed with the AMBER program system and with the INSIGHT program package. The distance bound driven dynamics calculation was conducted using a modified version of the DISGEO II program. The interproton distance restraints were derived from jump symmetrized rotating-frame Overhauser enhancement and exchange (JS-ROESY) spectra, which yield optimum sensitivity for medium-sized molecules like mersacidin. The connectivities via the sulfide bridges were unambiguously confirmed by heteronuclear NMR techniques (heteronuclear single quantum coherence and heteronuclear multiple bond correlation methods). Due to the tetracyclic structure, mersacidin exhibits a rather rigid globular shape, which neither belongs to the duramycin nor to the nisin structure type lantibiotics. The resulting structures for the simulated annealing protocol of restrained and subsequent free molecular dynamics were compared and found to be very similar." citations,entry_citation,5582,227812,1,,entry citation,,22566040,12562773,,,"NMR Study of Mersacidin and Lipid II Interaction in Dodecylphosphocholine Micelles: Conformational Changes are a Key to Antimicrobial Activity",published,journal,J. Biol. Chem.,,278,15,,,,,,,,,,,,,,,,,,,,,,13110,13117,2003, citations,X-ray_structure,5582,227813,2,,reference citation,,,10818347,,"Schneider TR, Karcher J, Pohl E, Lubini P, Sheldrick GM. Ab initio structure determination of the lantibiotic mersacidin. Acta Crystallogr D Biol Crystallogr. 2000 Jun;56 (Pt 6):705-13.",Ab initio structure determination of the lantibiotic mersacidin.,published,journal,Acta Crystallogr. D Biol. Crystallogr.,"Acta crystallographica. Section D, Biological crystallography",56,Pt 6,,0907-4449,,,,,,,,,,,,,,,,,,,,705,713,2000,"The crystal structure of mersacidin, a potential novel antibiotic against methicillin- and vancomycin-resistant Staphylococcus aureus strains, has been determined by ab initio methods. Despite all crystals being merohedrally twinned, an accurate structural model with an R value of 13.4% has been obtained at atomic resolution. With six molecules in the asymmetric unit and no atom heavier than sulfur, the structure corresponds to a protein of 120 amino acids and is the largest approximately equal-atom unknown structure solved by direct methods. In the crystal, the molecule assumes a compact fold different from that found by NMR in solution. Comparison of the NCS-related molecules reveals regions of variable flexibility. The region highly homologous to the related antibiotic actagardine is very rigid and possibly defines an essential building block of this class of new antibacterial substances." citations,NMR_structure,5582,227814,3,,reference citation,,,9119018,,"Prasch T, Naumann T, Markert RL, Sattler M, Schubert W, Schaal S, Bauch M, Kogler H, Griesinger C. Constitution and solution conformation of the antibiotic mersacidin determined by NMR and molecular dynamics. Eur J Biochem. 1997 Mar 1;244(2):501-12.",Constitution and solution conformation of the antibiotic mersacidin determined by NMR and molecular dynamics.,published,journal,Eur. J. Biochem.,European journal of biochemistry / FEBS,244,2,,0014-2956,,,,,,,,,,,,,,,,,,,,501,512,1997,"The solution structure of the tetracyclic lantibiotic mersacidin in methanol (CD3OH) has been determined by NMR followed by distance bound driven dynamics and subsequent restrained molecular dynamics simulations combined with an iterative relaxation matrix approach and alternatively by a simulated annealing protocol. The molecular dynamics simulations were performed with the AMBER program system and with the INSIGHT program package. The distance bound driven dynamics calculation was conducted using a modified version of the DISGEO II program. The interproton distance restraints were derived from jump symmetrized rotating-frame Overhauser enhancement and exchange (JS-ROESY) spectra, which yield optimum sensitivity for medium-sized molecules like mersacidin. The connectivities via the sulfide bridges were unambiguously confirmed by heteronuclear NMR techniques (heteronuclear single quantum coherence and heteronuclear multiple bond correlation methods). Due to the tetracyclic structure, mersacidin exhibits a rather rigid globular shape, which neither belongs to the duramycin nor to the nisin structure type lantibiotics. The resulting structures for the simulated annealing protocol of restrained and subsequent free molecular dynamics were compared and found to be very similar." citations,entry_citation,5583,227834,1,,entry citation,,22456786,12568610,,,"Synthesis and NMR Structure of P41icf, a Potent Inhibitor of Human Cathepsin L",published,journal,J. Am. Chem. Soc.,,125,6,,,,,,,,,,,,,,,,,,,,,,1508,1517,2003, citations,entry_citation,5584,227855,1,,entry citation,,22469432,12581200,,,A Simple Protocol to study Blue Copper Proteins by NMR,published,journal,Eur. J. Biochem.,,270,4,,,,,,,,,,,,,,,,,,,,,,600,609,2003, citations,entry_citation,5651,229470,1,,entry citation,,22683847,12798690,,,"Determinants of Intra Versus Intermolecular Self-association within the Regulatory Domains of Rlk and Itk",published,journal,J. Mol. Biol.,,329,5,,,,,,,,,,,,,,,,,,,,,,1011,1020,2003, citations,entry_citation,5652,229485,1,,entry citation,,,,,,"Solution Structure of CnErg1 (Ergtoxin), a HERG Specific Scorpion Toxin",published,journal,FEBS Lett.,,539,,,,,,,,,,,,,,,,,,,,,,,138,142,2003, citations,ref_1,5584,227856,2,,reference citation,,,11456890,,"Bertini I, Ciurli S, Dikiy A, Fernandez CO, Luchinat C, Safarov N, Shumilin S, The first solution structure of a paramagnetic copper(II) protein: the case of oxidized plastocyanin from the cyanobacterium Synechocystis PCC6803 J Am Chem Soc. 2001 Mar 14, 123(10):2405-13",The first solution structure of a paramagnetic copper(II) protein: the case of oxidized plastocyanin from the cyanobacterium Synechocystis PCC6803.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,123,10,,0002-7863,,,,,,,,,,,,,,,,,,,,2405,2413,2001,"The NMR solution structure of oxidized plastocyanin from the cyanobacterium Synechocystis PCC6803 is here reported. The protein contains paramagnetic copper(II), whose electronic relaxation times are quite unfavorable for NMR solution studies. The structure has been solved on the basis of 1041 meaningful NOESY cross-peaks, 18 1D NOEs, 26 T(1) values, 96 dihedral angle constraints, and 18 H-bonds. The detection of broad hyperfine-shifted signals and their full assignment allowed the identification of the copper(II) ligands and the determination of the Cu-S-C-H dihedral angle for the coordinated cysteine. The global root-mean-square deviation from the mean structure for the solution structure family is 0.72 +/- 0.14 and 1.16 +/- 0.17 A for backbone and heavy atoms, respectively. The structure is overall quite satisfactory and represents a breakthrough, in that it includes paramagnetic copper proteins among the metalloproteins for which solution structures can be afforded. The comparison with the available X-ray structure of a triple mutant is also performed." citations,entry_citation,5585,227880,1,,entry citation,,22439744,12419800,,,"Isolation, Structure, and Activity of GID, a Novel Alpha 4/7-conotoxin with an Extended N-terminal Sequence",published,journal,J. Biol. Chem.,,278,5,,,,,,,,,,,,,,,,,,,,,,3137,3144,2003, citations,entry_citation,5586,227900,1,,entry citation,,22363258,1245247,,,"Molecular Recognition in Purine-Rich Internal Loops: Thermodynamic, Structural, and Dynamic Consequences of Purine for Adenine Substitutions in 5'(rGGCAAGCCU)2",published,journal,Biochemistry,,41,50,,,,,,,,,,,,,,,,,,,,,,14978,14987,2002, citations,entry_citation,5587,227920,1,,entry citation,,22363258,1245247,,,"Molecular Recognition in Purine-Rich Internal Loops: Thermodynamic, Structural, and Dynamic Consequences of Purine for Adenine Substitutions in 5'(rGGCAAGCCU)2",published,journal,Biochemistry,,41,50,,,,,,,,,,,,,,,,,,,,,,14978,14987,2002, citations,entry_citation,5588,227940,1,,entry citation,,22363258,1245247,,,"Molecular Recognition in Purine-Rich Internal Loops: Thermodynamic, Structural, and Dynamic Consequences of Purine for Adenine Substitutions in 5'(rGGCAAGCCU)2",published,journal,Biochemistry,,41,50,,,,,,,,,,,,,,,,,,,,,,14978,14987,2002, citations,entry_citation,5589,227960,1,,entry citation,,,,,,"Solution structure of Vibrio cholorae protein VC0424: A variation of the Ferredoxin-like fold",published,journal,Protein Sci.,,12,,,,,,,,,,,,,,,,,,,,,,,1562,1566,2003, citations,ref_1,5589,227961,2,,reference citation,,,,,"Brunger AT. X-PLOR Version 3.1: a system for X-ray crystallography and NMR. New Haven, CY:Yale University Press; 1992.382 p.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,559,227999,1,,entry citation,,,,,"Baillargeon, Mary Welch, Laskowski, Jr., Michael, Neves, Darrow E., Porubcan, Michael A., Santini, Robert E., Markley, John L., ""Soybean Trypsin Inhibitor (Kunitz) and Its Complex with Trypsin. Carbon-13 Nuclear Magnetic Resonance Studies of the Reactive Site Arginine,"" Biochemistry 19 (25), 5703-5710 (1980).","Soybean Trypsin Inhibitor (Kunitz) and Its Complex with Trypsin. Carbon-13 Nuclear Magnetic Resonance Studies of the Reactive Site Arginine",published,journal,Biochemistry,,19,25,,,,,,,,,,,,,,,,,,,,,,5703,5710,1980, citations,entry_citation,5590,228012,1,,entry citation,,22760842,12878845,,,"Letter to the Editor: 1H, 13C and 15N Resonance Assignments of Rice Telomere Binding Domain from Oryza sativa",published,journal,J. Biomol. NMR,,27,1,,,,,,,,,,,,,,,,,,,,,,89,90,2003, citations,entry_citation,5591,228038,1,,entry citation,,,,,,"Sequence specific assignment of part of the myosin binding site of myosin binding protein C",in preparation,journal,J. Biomol. NMR,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5592,228067,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N resonance assignments of the SAND domains from glucocorticoid modulatory element binding proteins-1 and -2",published,journal,J. Biomol. NMR,,25,3,,,,,,,,,,,,,,,,,,,,,,259,260,2003, citations,entry_citation,5593,228092,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N backbone resonance assignments of the SAND domains from glucocorticoid modulatory element binding proteins-1 and -2",published,journal,J. Biomol. NMR,,25,3,,,,,,,,,,,,,,,,,,,,,,259,260,2003, citations,entry_citation,5594,228109,1,,entry citation,,22547248,12627222,,,"Structural Insights into the U-box, a Domain Associated with Multi-ubiquitination",published,journal,Nat. Struct. Biol.,,10,,,,,,,,,,,,,,,,,,,,,,,250,255,2003, citations,entry_citation,5595,228142,1,,entry citation,,,15014237,,,"Letter to the Editor: 1H, 13C, 15N backbone and sidechain resonance assignments of apo-NosL, a novel copper(I) binding protein from the nitrous oxide reductase gene cluster of Achromobacter cycloclastes",published,journal,J. Biomol. NMR,,29,2,,,,,,,,,,,,,,,,,,,,,,211,212,2004, citations,ref_1,5595,228143,2,,reference citation,,,11293413,,"McGuirl MA, Bollinger JA, Cosper N, Scott RA, Dooley DM. Expression, purification, and characterization of NosL, a novel Cu(I) protein of the nitrous oxide reductase (nos) gene cluster. J Biol Inorg Chem. 2001 Feb;6(2):189-95.","Expression, purification, and characterization of NosL, a novel Cu(I) protein of the nitrous oxide reductase (nos) gene cluster.",published,journal,J. Biol. Inorg. Chem.,Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry,6,2,,0949-8257,,,,,,,,,,,,,,,,,,,,189,195,2001,"NosL, one of the accessory proteins of the nos (nitrous oxide reductase) gene cluster, has been heterologously expressed, purified, and characterized. NosL is a monomeric protein of 18,540 MW that specifically and stoichiometrically binds Cu(I). The copper ion in NosL is ligated by a Cys residue, and one Met and one His are thought to serve as the other ligands. While it is possible to oxidize Cu(I)-NosL with ferricyanide, the Cu(II) ion thus formed appears to dissociate from the protein. The function of Cu(I)NosL is not yet known, but the data indicate that NosL does not act as an electron transfer partner to nitrous oxide reductase. NosL is encoded on the same transcript as three other gene products (NosD, NosF, and NosY). These have been shown to be required for assembly of the active site in nitrous oxide reductase, which is thought to be a copper cluster. Accordingly, it is possible that NosL is a copper chaperone involved in metallocenter assembly." citations,entry_citation,560,228317,1,,entry citation,,,,,"Baillargeon, Mary Welch, Laskowski, Jr., Michael, Neves, Darrow E., Porubcan, Michael A., Santini, Robert E., Markley, John L., ""Soybean Trypsin Inhibitor (Kunitz) and Its Complex with Trypsin. Carbon-13 Nuclear Magnetic Resonance Studies of the Reactive Site Arginine,"" Biochemistry 19 (25), 5703-5710 (1980).","Soybean Trypsin Inhibitor (Kunitz) and Its Complex with Trypsin. Carbon-13 Nuclear Magnetic Resonance Studies of the Reactive Site Arginine",published,journal,Biochemistry,,19,25,,,,,,,,,,,,,,,,,,,,,,5703,5710,1980, citations,ref_2,5595,228144,3,,reference citation,,,9720302,,"McGuirl MA, Nelson LK, Bollinger JA, Chan YK, Dooley DM. The nos (nitrous oxide reductase) gene cluster from the soil bacterium Achromobacter cycloclastes: cloning, sequence analysis, and expression. J Inorg Biochem. 1998 Jul;70(3-4):155-69.","The nos (nitrous oxide reductase) gene cluster from the soil bacterium Achromobacter cycloclastes: cloning, sequence analysis, and expression.",published,journal,J. Inorg. Biochem.,Journal of inorganic biochemistry,70,3-4,,0162-0134,,,,,,,,,,,,,,,,,,,,155,169,1998,"The nitrous oxide (N2O) reductase (nos) gene cluster from Achromobacter cycloclastes has been cloned and sequenced. Seven protein coding regions corresponding to nosR, nosZ (structural N2O reductase gene), nosD, nosF, nosY, nosL, and nosX are detected, indicating a genetic organization similar to that of Rhizobium meliloti. To aid homology studies, nosR from R. meliloti has also been sequenced. Comparison of the deduced amino acid sequences with corresponding sequences from other organisms has also allowed structural and functional inferences to be made. The heterologous expression of NosD, NosZ (N2O reductase), and NosL is also reported. A model of the CuA site in N2O reductase, based on the crystal structure of this site in bovine heart cytochrome c oxidase, is presented. The model suggests that a His residue of the CuA domain may be a ligand to the catalytic CuZ site. In addition, the origin of the spectroscopically-observed Cys coordination to CuZ is discussed in terms of the sequence alignment of seven N2O reductases." citations,entry_citation,5596,228171,1,,entry citation,,,,,,"Letter to the Editor: Resonance assignments for the hypothetical protein yggU from Escherichia coli",published,journal,J. Biomol. NMR,,27,3,,,,,,,,,,,,,,,,,,,,,,285,286,2003, citations,ref_1,5596,228172,2,,reference citation,,,12060747,,"Szyperski T., Yeh D.C., Sukumaran D.K., Moseley H.N., Montelione G.T. Proc. Natl. Acad. Sci. USA (2002) 99, 8009-14",Reduced-dimensionality NMR spectroscopy for high-throughput protein resonance assignment.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,99,12,,0027-8424,,,,,,,,,,,,,,,,,,,,8009,8014,2002,"A suite of reduced-dimensionality (13)C,(15)N,(1)H-triple-resonance NMR experiments is presented for rapid and complete protein resonance assignment. Even when using short measurement times, these experiments allow one to retain the high spectral resolution required for efficient automated analysis. ""Sampling limited"" and ""sensitivity limited"" data collection regimes are defined, respectively, depending on whether the sampling of the indirect dimensions or the sensitivity of a multidimensional NMR experiments per se determines the minimally required measurement time. We show that reduced-dimensionality NMR spectroscopy is a powerful approach to avoid the ""sampling limited regime""--i.e., a standard set of ten experiments proposed here allows one to effectively adapt minimal measurement times to sensitivity requirements. This is of particular interest in view of the greatly increased sensitivity of NMR spectrometers equipped with cryogenic probes. As a step toward fully automated analysis, the program AUTOASSIGN has been extended to provide sequential backbone and (13)C(beta) resonance assignments from these reduced-dimensionality NMR data." citations,ref_2,5596,228173,3,,reference citation,,,8520220,,"Delaglio F., Grzesiek S., Vuister G.W., Zhu G., Pfeifer J., Bax A. J. Biomol. NMR. (1995) 6, 277-293.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref_3,5596,228174,4,,reference citation,,,,,"T. D. Goddard and D. G. Kneller, SPARKY 3, 3, University of California, San Francisco",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_4,5596,228175,5,,reference citation,,,9217263,,"Zimmerman D.E., Kulikowski C.A., Huang Y., Feng W., Tashiro M., Shimotakahara S., Chien C., Powers R., Montelione G.T. J. Mol. Biol. (1997) 269, 592-610",Automated analysis of protein NMR assignments using methods from artificial intelligence.,published,journal,J. Mol. Biol.,Journal of molecular biology,269,4,,0022-2836,,,,,,,,,,,,,,,,,,,,592,610,1997,"An expert system for determining resonance assignments from NMR spectra of proteins is described. Given the amino acid sequence, a two-dimensional 15N-1H heteronuclear correlation spectrum and seven to eight three-dimensional triple-resonance NMR spectra for seven proteins, AUTOASSIGN obtained an average of 98% of sequence-specific spin-system assignments with an error rate of less than 0.5%. Execution times on a Sparc 10 workstation varied from 16 seconds for smaller proteins with simple spectra to one to nine minutes for medium size proteins exhibiting numerous extra spin systems attributed to conformational isomerization. AUTOASSIGN combines symbolic constraint satisfaction methods with a domain-specific knowledge base to exploit the logical structure of the sequential assignment problem, the specific features of the various NMR experiments, and the expected chemical shift frequencies of different amino acids. The current implementation specializes in the analysis of data derived from the most sensitive of the currently available triple-resonance experiments. Potential extensions of the system for analysis of additional types of protein NMR data are also discussed." citations,ref_5,5596,228176,6,,reference citation,,,,,"Huang, Y.J. (2001). Automated determination of protein structures from NMR data by iterative analysis of self-consistent contact patterns, PhD thesis, Rutgers University, New Brunswick, NJ.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_6,5596,228177,7,,reference citation,,,,,see: www_nmr.cabm.rutgers.edu/NMRsoftware/nmr-software.html,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5600,228330,1,,entry citation,,22580601,12693931,,,Hydrogen Bonds in Rubredoxins from Mesophilic and Hyperthermophilic Organisms,published,journal,Biochemistry,,42,15,,,,,,,,,,,,,,,,,,,,,,4357,4372,2003, citations,entry_citation,5673,229972,1,,entry citation,,22515400,12627948,,,"NMR Solution Structure of the Glucagon Antagonist [desHis(1), desPhe(6), Glu(9)] Glucagon Amide in the Presence of Perdeuterated Dodecylphosphocholine Micelles",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2825,2835,2003, citations,ref_7,5596,228178,8,,reference citation,,,10212987,,"Cornilescu, G., Delaglio, F., Bax, A. (1999) J. Biomol. NMR 13, 289-302.",Protein backbone angle restraints from searching a database for chemical shift and sequence homology.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,13,3,,0925-2738,,,,,,,,,,,,,,,,,,,,289,302,1999,"Chemical shifts of backbone atoms in proteins are exquisitely sensitive to local conformation, and homologous proteins show quite similar patterns of secondary chemical shifts. The inverse of this relation is used to search a database for triplets of adjacent residues with secondary chemical shifts and sequence similarity which provide the best match to the query triplet of interest. The database contains 13C alpha, 13C beta, 13C', 1H alpha and 15N chemical shifts for 20 proteins for which a high resolution X-ray structure is available. The computer program TALOS was developed to search this database for strings of residues with chemical shift and residue type homology. The relative importance of the weighting factors attached to the secondary chemical shifts of the five types of resonances relative to that of sequence similarity was optimized empirically. TALOS yields the 10 triplets which have the closest similarity in secondary chemical shift and amino acid sequence to those of the query sequence. If the central residues in these 10 triplets exhibit similar phi and psi backbone angles, their averages can reliably be used as angular restraints for the protein whose structure is being studied. Tests carried out for proteins of known structure indicate that the root-mean-square difference (rmsd) between the output of TALOS and the X-ray derived backbone angles is about 15 degrees. Approximately 3% of the predictions made by TALOS are found to be in error." citations,ref_8,5596,228179,9,,reference citation,,,9367762,,"Guntert P, Mumenthaler C, Wuthrich K. (1997) J. Mol. Biol. 273, 283-98.",Torsion angle dynamics for NMR structure calculation with the new program DYANA.,published,journal,J. Mol. Biol.,Journal of molecular biology,273,1,,0022-2836,,,,,,,,,,,,,,,,,,,,283,298,1997,"The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from distance constraints and torsion angle constraints collected by nuclear magnetic resonance (NMR) experiments performs simulated annealing by molecular dynamics in torsion angle space and uses a fast recursive algorithm to integrate the equations of motions. Torsion angle dynamics can be more efficient than molecular dynamics in Cartesian coordinate space because of the reduced number of degrees of freedom and the concomitant absence of high-frequency bond and angle vibrations, which allows for the use of longer time-steps and/or higher temperatures in the structure calculation. It also represents a significant advance over the variable target function method in torsion angle space with the REDAC strategy used by the predecessor program DIANA. DYANA computation times per accepted conformer in the ""bundle"" used to represent the NMR structure compare favorably with those of other presently available structure calculation algorithms, and are of the order of 160 seconds for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300 computer. Test calculations starting from conformers with random torsion angle values further showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures." citations,ref_9,5596,228180,10,,reference citation,,,,,see: nmr.cit.nih.gov/xplor_nih/,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_10,5596,228181,11,,reference citation,,,,,"see: www_nmr.cabm.rutgers.edu/NMRsoftware/nmr-software.html""",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5597,228246,1,,entry citation,,22422606,12534286,,,"Structure and Dynamics of Reduced Bacillus pasteurii Cytochrome c: Oxidation State Dependent Properties and Implications for Electron Transfer Processes",published,journal,Biochemistry,,42,3,,,,,,,,,,,,,,,,,,,,,,739,745,2003, citations,entry_citation,5598,228270,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N resonance assignments of domain 1 of receptor associated protein",published,journal,J. Biomol. NMR,,26,2,,,,,,,,,,,,,,,,,,,,,,187,188,2003, citations,entry_citation,5599,228283,1,,entry citation,,22616165,12729745,,,The Tertiary Structure and Backbone Dynamics of Human Prolactin,published,journal,J. Mol. Biol.,,328,5,,,,,,,,,,,,,,,,,,,,,,1105,1121,2003, citations,reference_1,5599,228284,2,,reference citation,,,8520220,,"F. Delaglio, S. Grzesiek, G. W. Vuister, G. Zhu, J. Pfeifer and A. Bax: NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J.Biomol. NMR. 6, 277-293 (1995)",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,reference_2,5599,228285,3,,reference citation,,,,,"J. Vavanagh, W. J. Fairbrother, A. G. Palmer, N. J. Skelton; Protein NMR spectroscopy : principles and practice. Academic Press, New York (1996) pp 175-176",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,reference_3,5599,228286,4,,reference citation,,,,,"T. D. Goddard and D. G. Kneller, SPARKY 3, University of California, San Francisco",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,reference_4,5599,228287,5,,reference citation,,,,,"NMRView: A computer program for the visualization and analysis of NMR data (1994) B. A. Johnson and R. A. Blevins, J. Biomol. NMR 4:603-614",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,reference_5,5599,228288,6,,reference citation,,,12051947,,"Protein NMR Structure Determination with Automated NOE Assignment using the New Software CANDID and the Torsion Angle Dynamics Algorithm DYANA. Herrmann T., Guntert P. & Wuthrich K. J. Mol. Biol. 2002 May 24; 319(1): 209-227.",Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA.,published,journal,J. Mol. Biol.,Journal of molecular biology,319,1,,0022-2836,,,,,,,,,,,,,,,,,,,,209,227,2002,"Combined automated NOE assignment and structure determination module (CANDID) is a new software for efficient NMR structure determination of proteins by automated assignment of the NOESY spectra. CANDID uses an iterative approach with multiple cycles of NOE cross-peak assignment and protein structure calculation using the fast DYANA torsion angle dynamics algorithm, so that the result from each CANDID cycle consists of exhaustive, possibly ambiguous NOE cross-peak assignments in all available spectra and a three-dimensional protein structure represented by a bundle of conformers. The input for the first CANDID cycle consists of the amino acid sequence, the chemical shift list from the sequence-specific resonance assignment, and listings of the cross-peak positions and volumes in one or several two, three or four-dimensional NOESY spectra. The input for the second and subsequent CANDID cycles contains the three-dimensional protein structure from the previous cycle, in addition to the complete input used for the first cycle. CANDID includes two new elements that make it robust with respect to the presence of artifacts in the input data, i.e. network-anchoring and constraint-combination, which have a key role in de novo protein structure determinations for the successful generation of the correct polypeptide fold by the first CANDID cycle. Network-anchoring makes use of the fact that any network of correct NOE cross-peak assignments forms a self-consistent set; the initial, chemical shift-based assignments for each individual NOE cross-peak are therefore weighted by the extent to which they can be embedded into the network formed by all other NOE cross-peak assignments. Constraint-combination reduces the deleterious impact of artifact NOE upper distance constraints in the input for a protein structure calculation by combining the assignments for two or several peaks into a single upper limit distance constraint, which lowers the probability that the presence of an artifact peak will influence the outcome of the structure calculation. CANDID test calculations were performed with NMR data sets of four proteins for which high-quality structures had previously been solved by interactive protocols, and they yielded comparable results to these reference structure determinations with regard to both the residual constraint violations, and the precision and accuracy of the atomic coordinates. The CANDID approach has further been validated by de novo NMR structure determinations of four additional proteins. The experience gained in these calculations shows that once nearly complete sequence-specific resonance assignments are available, the automated CANDID approach results in greatly enhanced efficiency of the NOESY spectral analysis. The fact that the correct fold is obtained in cycle 1 of a de novo structure calculation is the single most important advance achieved with CANDID, when compared with previously proposed automated NOESY assignment methods that do not use network-anchoring and constraint-combination." citations,JBNMR_citation,5627,229005,2,,reference citation,,,,,,"Letter to the Editor: Assignment of the 1H, 13C and 15N Resonances of the LpxC Deacetylase from Aquifex aeolicus in Complex with the Substrate-Analog Inhibitor TU-514",,journal,J. Biomol. NMR,,28,2,,,,,,,,,,,,,,,,,,,,,,201,202,2004, citations,Reference_1,5600,228331,2,,reference citation,,,12693931,,"Hydrogen bonds in Rubredoxins from mesophilic and hyperthermophilic organisms, Biochemistry, in preparation",Hydrogen bonds in rubredoxins from mesophilic and hyperthermophilic organisms.,published,journal,Biochemistry,Biochemistry,42,15,,0006-2960,,,,,,,,,,,,,,,,,,,,4357,4372,2003,"The extent and strength of the hydrogen bond networks in rubredoxins from the hyperthermophile Pyrococcus furiosus (PfRd), and its mesophilic analogue Clostridium pasteurianum (CpRd), are examined and compared using NMR spectroscopy. NMR parameters examined in this study include through-hydrogen bond (h3)J(NC)(') scalar couplings and (1)H, (13)C, and (15)N chemical shifts, as well as covalent (1)J(NH) and (1)J(NC)(') scalar couplings. These parameters have allowed the characterization in solution of 12 hydrogen bonds in each protein. Despite a 83% sequence homology and a low RMSD for the backbone heavy atoms (0.648 A) in the crystalline state, subtle, but definite, changes have been identified in the detailed hydrogen-bonding patterns. CpRd shows an increased number of hydrogen bonds in the triple-stranded beta-sheet and an additional hydrogen bond in the multiple-turn segment including residues 14-32. On the other hand, PfRd exhibits an overall strengthening of N-H...O=C hydrogen bonds in the loops involved at the metal binding site as well as evidence for an additional NH...S(Cys) hydrogen bond involving the alanine residue 44. These data, as well as temperature dependence of the NMR parameters, suggest that the particular NMR hydrogen bond pattern found in the hyperthermophile rubredoxin leads to an increased stabilization at the metal binding pocket. It seems to result from a subtle redistribution of hydrogen-bonding interactions between the triple-stranded beta-sheet and the actual metal binding site." citations,entry_citation,5601,228365,1,,entry citation,,22580601,12693931,,,Hydrogen Bonds in Rubredoxins from Mesophilic and Hyperthermophilic Organisms,published,journal,Biochemistry,,42,15,,,,,,,,,,,,,,,,,,,,,,4357,4372,2003, citations,entry_citation,5602,228401,1,,entry citation,,,,,,"Letter to the Editor: Complete resonance assignments for the nudix hydrolase DR2356 of Deinococcus radiodurans",published,journal,J. Biomol. NMR,,27,2,,,,,,,,,,,,,,,,,,,,,,181,182,2003, citations,entry_citation,5603,228415,1,,entry citation,,22703861,12707255,,,Solution Structure of Human Proguanylin: The Role of a Hormone Prosequence,published,journal,J. Biol. Chem.,,278,26,,,,,,,,,,,,,,,,,,,,,,24118,24124,2003, citations,ref_1,5603,228416,2,,reference citation,,,,,"Johnson, B. A. & Blevins, R. A. (1994). NMRView: A computer program for the visualization and analysis of NMR data. J. Biomol. NMR 4, 603-614.""",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5604,228446,1,,entry citation,,22305097,12417201,,,"A new-zinc protein coordination site in intracellular metal trafficking: solution structure of the apo and Zn(II) forms of ZntA (46-118)",published,journal,J. Mol. Biol.,,323,5,,,,,,,,,,,,,,,,,,,,,,883,897,2002, citations,ref_1,5604,228447,2,,reference citation,,,12417201,,"A New Zinc-protein Coordination Site in Intracellular Metal Trafficking: Solution Structure of the Apo and Zn(II) forms of ZntA(46-118) Lucia Banci, Ivano Bertini, Simone Ciofi-Baffoni, Lydia A. Finney, Caryn E. Outten, Thomas V. O'Halloran Journal of Molecular Biology, Vol. 323, No. 5, Nov 2002, pp. 883-897 (doi: 10.1016/S0022-2836(02)01007-0)",A new zinc-protein coordination site in intracellular metal trafficking: solution structure of the Apo and Zn(II) forms of ZntA(46-118).,published,journal,J. Mol. Biol.,Journal of molecular biology,323,5,,0022-2836,,,,,,,,,,,,,,,,,,,,883,897,2002,"Zinc, a metal ion that functions in a wide variety of catalytic and structural sites in metalloproteins, is shown here to adopt a novel coordination environment in the Escherichia coli transport protein ZntA. The ZntA protein is a P-type ATPase that pumps zinc out of the cytoplasm and into the periplasm. It is physiologically selective for Zn(II) and functions with metalloregulatory proteins in the cell to keep the zinc quota within strict limits. Yet, the N-terminal cytoplasmic domain contains a region that is highly homologous to the yeast Cu(I) metallochaperone Atx1. To investigate how the structure of this region may influence its function, this fragment, containing residues 46-118, has been cloned out of the gene and overexpressed. We report here the solution structure of this fragment as determined by NMR. Both the apo and Zn(II)-ZntA(46-118) structures have been determined. It contains a previously unknown protein coordination site for zinc that includes two cysteine residues, Cys59 and Cys62, and a carboxylate residue, Asp58. The solvent accessibility of this site is also remarkably high, a feature that increasingly appears to be a characteristic of domains of heavy metal ion transport proteins. The participation of Asp58 in this ZntA metal ion binding site may play an important role in modulating the relative affinities and metal exchange rates for Zn(II)/Pb(II)/Cd(II) as compared with other P-type ATPases, which are selective for Cu(I) or Ag(I)." citations,entry_citation,5605,228470,1,,entry citation,,,,,,"Letter to the Editor: Sequence-specific 1H, 13C and 15N resonance assignments of SAM22, an allergenic stress-induced protein from soy bean",published,journal,J. Biomol. NMR,,26,2,,,,,,,,,,,,,,,,,,,,,,191,192,2003, citations,HI0719_paper,5606,228508,1,,entry citation,,22403672,12515541,,,"Solution Structure and Functional Ligand Screening of HI0719, a Highly Conserved Protein from Bacteria to Humans in the YjgF/YER057c/UK114 Family",published,journal,Biochemistry,Biochemistry,42,1,,,,,,,,,,,,,,,,,,,,,,80,89,2003, citations,entry_citation,5607,228524,1,,entry citation,,22554011,12667090,,,"NMR Structure and Backbone Dynamics of the Extended Second Transmembrane Domain of the Human Neuronal Glycine Receptor alpha1 Subunit",published,journal,Biochemistry,,42,13,,,,,,,,,,,,,,,,,,,,,,3989,3995,2003, citations,entry_citation,5608,228550,1,,entry citation,,,12646193,,,Contryphan-Vn: a modulator of Ca2+-dependent K+ channels.,published,journal,Biochem. Biophys. Res. Commun.,,303,1,,,,,,,,,,,,,,,,,,,,,,238,246,2003, citations,entry_citation,5609,228576,1,,entry citation,,22476988,12482862,,,"Disulfide Folding Pathways of Cystine Knot Proteins: Tying the Knot within the Circular Backbone of the Cyclotides",published,journal,J. Biol. Chem.,,278,8,,,,,,,,,,,,,,,,,,,,,,6314,6322,2003, citations,entry_citation,561,228591,1,,entry citation,,,,,"Baillargeon, Mary Welch, Laskowski, Jr., Michael, Neves, Darrow E., Porubcan, Michael A., Santini, Robert E., Markley, John L., ""Soybean Trypsin Inhibitor (Kunitz) and Its Complex with Trypsin. Carbon-13 Nuclear Magnetic Resonance Studies of the Reactive Site Arginine,"" Biochemistry 19 (25), 5703-5710 (1980).","Soybean Trypsin Inhibitor (Kunitz) and Its Complex with Trypsin. Carbon-13 Nuclear Magnetic Resonance Studies of the Reactive Site Arginine",published,journal,Biochemistry,,19,25,,,,,,,,,,,,,,,,,,,,,,5703,5710,1980, citations,entry_citation,5610,228604,1,,entry citation,,,12534273,,,"The Structure of the Carboxyl Terminus of Striated alpha-Tropomyosin in Solution Reveals an Unusual Parallel Arrangement of Interacting alpha-Helices",published,journal,Biochemistry,,42,3,,,,,,,,,,,,,,,,,,,,,,614,619,2003, citations,entry_citation,5611,228626,1,,entry citation,,,14645089,,,"Three-dimensional structure of the Mammalian tachykinin Peptide neurokinin a bound to lipid micelles",published,journal,Biophys. J.,,85,6,,,,,,,,,,,,,,,,,,,,,,4002,4011,2003, citations,entry_citation,5612,228642,1,,entry citation,,22730903,12846570,,,"Structure of Petunia hybrida Defensin 1, a Novel Plant Defensin with Five Disulfide Bonds",published,journal,Biochemistry,,42,27,,,,,,,,,,,,,,,,,,,,,,8214,8222,2003, citations,entry_citation,5613,228660,1,,entry citation,,,,,,"Stability of cyclic beta-hairins: asymmetric contributions from side chains of a hydrogen-bonded cross-strand residue pair",in press,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5628,229039,1,,entry citation,,,,,,"Letter to the Editor: 1H, 15N and 13C resonance assignments of the highly conserved 19kDa C-terminal domain from human Elongation Factor 1Bgamma",published,journal,J. Biomol. NMR,,26,2,,,,,,,,,,,,,,,,,,,,,,189,190,2003, citations,entry_citation,5629,229057,1,,entry citation,,,16819590,,,MTH187 from Methanobacterium thermoautotrophicum has three HEAT-like Repeats,published,journal,J. Biomol. NMR,,35,2,,,,,,,,,,,,,,,,,,,,,,149,154,2006, citations,entry_citation,5674,229994,1,,entry citation,,,,,,Three-Dimensional Solution Structure of Hainantoxin-Iv by 2D 1H-NMR,submitted,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5715,230950,1,,entry citation,,,15014231,,,"Binding ability of a HHP-tagged protein towards Ni(2+) studied by paramagnetic NMR relaxation: The possibility of obtaining long-range structure information.",published,journal,J. Biomol. NMR,,29,2,,,,,,,,,,,,,,,,,,,,,,175,185,2004, citations,ref_1,5613,228661,2,,reference citation,,,11456574,,"Cochran AG, Tong RT, Starovasnik MA, Park EJ, McDowell RS, Theaker JE, Skelton NJ. A minimal peptide scaffold for beta-turn display: optimizing a strand position in disulfide-cyclized beta-hairpins. J Am Chem Soc. 2001 Jan 31;123(4):625-32.",A minimal peptide scaffold for beta-turn display: optimizing a strand position in disulfide-cyclized beta-hairpins.,published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,123,4,,0002-7863,,,,,,,,,,,,,,,,,,,,625,632,2001,"Phage display of peptide libraries has become a powerful tool for the evolution of novel ligands that bind virtually any protein target. However, the rules governing conformational preferences in natural peptides are poorly understood, and consequently, structure-activity relationships in these molecules can be difficult to define. In an effort to simplify this process, we have investigated the structural stability of 10-residue, disulfide-constrained beta-hairpins and assessed their suitability as scaffolds for beta-turn display. Using disulfide formation as a probe, relative free energies of folding were measured for 19 peptides that differ at a one strand position. A tryptophan substitution promotes folding to a remarkable degree. NMR analysis confirms that the measured energies correlate well with the degree of beta-hairpin structure in the disulfide-cyclized peptides. Reexamination of a subset of the strand substitutions in peptides with different turn sequences reveals linear free energy relationships, indicating that turns and strand-strand interactions make independent, additive contributions to hairpin stability. Significantly, the tryptophan strand substitution is highly stabilizing with all turns tested, and peptides that display model turns or the less stable C'-C' ' turn of CD4 on this tryptophan ""stem"" are highly structured beta-hairpins in water. Thus, we have developed a small, structured beta-turn scaffold, containing only natural L-amino acids, that may be used to display peptide libraries of limited conformational diversity on phage." citations,entry_citation,5614,228680,1,,entry citation,,22353257,12475246,,,"Sheared A(anti)*A(anti) base Pairs in a Destabilizing 2 x 2 Internal Loop: The NMR Structure of 5'(rGGCAAGCCU)(2)",published,journal,Biochemistry,,41,50,,,,,,,,,,,,,,,,,,,,,,14969,14977,2002, citations,entry_citation,5615,228699,1,,entry citation,,,12740396,,,"Structural analysis of the DNA-binding domain of the Erwinia amylovora RcsB protein and its interaction with the RcsAB box",published,journal,J. Biol. Chem.,,278,20,,,,,,,,,,,,,,,,,,,,,,17752,17759,2003, citations,ref-1,5615,228700,2,,reference citation,,,11908496,,"Pristovsek P, Ruterjans H, Jerala R. Semiautomatic sequence-specific assignment of proteins based on the tertiary structure--the program st2nmr. J Comput Chem. 2002 Feb;23(3):335-40.",Semiautomatic sequence-specific assignment of proteins based on the tertiary structure--the program st2nmr.,published,journal,,Journal of computational chemistry,23,3,,0192-8651,,,,,,,,,,,,,,,,,,,,335,340,2002,"The sequence-specific assignment of resonances is still the most time-consuming procedure that is necessary as the first step in high-resolution NMR studies of proteins. In many cases a reliable three-dimensional (3D) structure of the protein is available, for example, from X-ray spectroscopy or homology modeling. Here we introduce the st2nmr program that uses the 3D structure and Nuclear Overhauser Effect spectroscopy (NOESY) peak list(s) to evaluate and optimize trial sequence-specific assignments of spin systems derived from correlation spectra to residues of the protein. A distance-dependent target function that scores trial assignments based on the presence of expected NOESY crosspeaks is optimized in a Monte Carlo fashion. The performance of the program st2nmr is tested on real NMR data of an alpha-helical (cytochrome c) and beta-sheet (lipocalin) protein using homology models and/or X-ray structures; it succeeded in completely reproducing the correct sequence-specific assignments in most cases using 2D and/or 15N/13C Nuclear Overhauser Effect (NOE) data. Additionally to amino acid residues the program can also handle ligands that are bound to the protein, such as heme, and can be used as a complementary tool to fully automated assignment procedures." citations,entry_citation,5616,228717,1,,entry citation,,,12460579,,,"Solution Structure and Ligand Recognition of the WW Domain Pair of the Yeast Splicing Factor Prp40",published,journal,J. Mol. Biol.,,324,,,,,,,,,,,,,,,,,,,,,,,807,822,2002, citations,entry_citation,5617,228744,1,,entry citation,,22515401,12627949,,,"Anticarcinogenic Bowman Birk Inhibitor Isolated from Snail Medic Seeds (Medicago scutellata): Solution Structure and Analysis of Self-association Behavior",published,journal,Biochemistry,,42,10,,,,,,,,,,,,,,,,,,,,,,2836,2846,2003, citations,entry_citation,5618,228761,1,,entry citation,,22651145,12766392,,,"A Strategy to Obtain Backbone Resonance Assignments of Deuterated Proteins in the Presence of Incomplete Amide (2)H/(1)H Back-exchange",published,journal,J. Biomol. NMR,,25,4,,,,,,,,,,,,,,,,,,,,,,291,311,2003, citations,entry_citation,5619,228780,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N resonance assignments for methionine sulfoxide reductase B from Bacillus subtilis",published,journal,J. Biomol. NMR,,27,2,,,,,,,,,,,,,,,,,,,,,,183,184,2003, citations,entry_citation,562,228804,1,,entry citation,,,,,"Baillargeon, Mary Welch, Laskowski, Jr., Michael, Neves, Darrow E., Porubcan, Michael A., Santini, Robert E., Markley, John L., ""Soybean Trypsin Inhibitor (Kunitz) and Its Complex with Trypsin. Carbon-13 Nuclear Magnetic Resonance Studies of the Reactive Site Arginine,"" Biochemistry 19 (25), 5703-5710 (1980).","Soybean Trypsin Inhibitor (Kunitz) and Its Complex with Trypsin. Carbon-13 Nuclear Magnetic Resonance Studies of the Reactive Site Arginine",published,journal,Biochemistry,,19,25,,,,,,,,,,,,,,,,,,,,,,5703,5710,1980, citations,entry_citation,5620,228817,1,,entry citation,,,,,,"Solution structure of ribosomal protein S28E from Methanobacterium Thermoautotrophicum",published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5621,228854,1,,entry citation,,,,,,"Solution structure of hypothetical protein dimer encoded by the Yoag gene from Escherichia coli""",published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5622,228880,1,,entry citation,,22718516,12834352,,,"Structural and Functional Characterization of a Thioredoxin-like Protein (Mt0807) from Methanobacterium thermoautotrophicum",published,journal,Biochemistry,,42,26,,,,,,,,,,,,,,,,,,,,,,8001,8010,2003, citations,entry_citation,5623,228901,1,,entry citation,,,,,,"Letter to the Editor: Assignments of 1H, 15N and 13C resonances of the proline-rich matrix protein of Moloney Murine Leukemia Virus (MA MoMuLV)",published,journal,J. Biomol. NMR,,25,3,,,,,,,,,,,,,,,,,,,,,,261,262,2003, citations,entry_citation,5624,228930,1,,entry citation,,,12600987,,,"A Conserved Structural Motif at the N-terminal of Bacterial Translation Initiation Factor IF2",published,journal,J. Biol. Chem.,,278,18,,,,,,,,,,,,,,,,,,,,,,16320,16328,2003, citations,entry_citation,5625,228955,1,,entry citation,,,16527248,,,"Solution structures of tetrahaem ferricytochrome c3 from Desulfovibrio vulgaris (Hildenborough) and its K45Q mutant: The molecular basis of cooperativity",published,journal,Biochim. Biophys. Acta.,,1757,2,,,,,,,,,,,,,,,,,,,,,,143,153,2006, citations,entry_citation,5626,228980,1,,entry citation,,,,,,"Letter to the editor: 1H 13C and 15N backbone resonance assignments of the N-terminal domain of Drosophila GCM protein",published,journal,J. Biomol. NMR,,26,3,,,,,,,,,,,,,,,,,,,,,,277,278,2003, citations,entry_citation,5627,229004,1,,entry citation,,22768440,12833153,,,Structure of the LpxC Deacetylase with a Bound Substrate-analog Inhibitor,published,journal,Nat. Struct. Biol.,,10,8,,,,,,,,,,,,,,,,,,,,,,645,651,2003, citations,entry_citation,5645,229361,1,,entry citation,,,14675814,,,Random coil carbon chemical shifts of deoxyribonucleic acids,published,journal,J. Magn. Reson.,,166,1,,,,,,,,,,,,,,,,,,,,,,11,18,2004, citations,citation,5629,229058,2,,reference citation,,,11017201,,"Christendat D, Yee A, Dharamsi A, Kluger Y, Savchenko A, Cort JR, Booth V, Mackereth CD, Saridakis V, Ekiel I, Kozlov G, Maxwell KL, Wu N, McIntosh LP, Gehring K, Kennedy MA, Davidson AR, Pai EF, Gerstein M, Edwards AM, Arrowsmith CH. Structural proteomics of an archaeon. Nat Struct Biol. 2000 Oct;7(10):903-9.",Structural proteomics of an archaeon.,published,journal,Nat. Struct. Biol.,Nature structural biology,7,10,,1072-8368,,,,,,,,,,,,,,,,,,,,903,909,2000,"A set of 424 nonmembrane proteins from Methanobacterium thermoautotrophicum were cloned, expressed and purified for structural studies. Of these, approximately 20% were found to be suitable candidates for X-ray crystallographic or NMR spectroscopic analysis without further optimization of conditions, providing an estimate of the number of the most accessible structural targets in the proteome. A retrospective analysis of the experimental behavior of these proteins suggested some simple relations between sequence and solubility, implying that data bases of protein properties will be useful in optimizing high throughput strategies. Of the first 10 structures determined, several provided clues to biochemical functions that were not detectable from sequence analysis, and in many cases these putative functions could be readily confirmed by biochemical methods. This demonstrates that structural proteomics is feasible and can play a central role in functional genomics." citations,entry_citation,563,229108,1,,entry citation,,,,,"Baillargeon, Mary Welch, Laskowski, Jr., Michael, Neves, Darrow E., Porubcan, Michael A., Santini, Robert E., Markley, John L., ""Soybean Trypsin Inhibitor (Kunitz) and Its Complex with Trypsin. Carbon-13 Nuclear Magnetic Resonance Studies of the Reactive Site Arginine,"" Biochemistry 19 (25), 5703-5710 (1980).","Soybean Trypsin Inhibitor (Kunitz) and Its Complex with Trypsin. Carbon-13 Nuclear Magnetic Resonance Studies of the Reactive Site Arginine",published,journal,Biochemistry,,19,25,,,,,,,,,,,,,,,,,,,,,,5703,5710,1980, citations,entry_citation,5630,229121,1,,entry citation,,,15930006,,,"High-quality homology models derived from NMR and X-ray structures of E. coli proteins YgdK and Suf E suggest that all members of the YgdK/Suf E protein family are enhancers of cysteine desulfurases",published,journal,Protein Sci.,,14,6,,,,,,,,,,,,,,,,,,,,,,1597,1608,2005, citations,entry_citation,5631,229136,1,,entry citation,,22486575,12446668,,,"Origins of PDZ Domain Ligand Specificity: Structure Determination and Mutagenesis of the Erbin PDZ Domain",published,journal,J. Biol. Chem.,,278,9,,,,,,,,,,,,,,,,,,,,,,7645,7654,2003, citations,entry_citation,5632,229166,1,,entry citation,,22426914,12525685,,,"Mutations Linked to Dyskeratosis congenita Cause Changes in the Structural Equilibrium in Telomerase RNA",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,100,2,,,,,,,,,,,,,,,,,,,,,,449,454,2003, citations,entry_citation,5633,229189,1,,entry citation,,22513943,12519766,,,"The solution structure of molt-inhibiting hormone from the Kuruma prawn Marsupenaeus japonicus",published,journal,J. Biol. Chem.,,278,11,,,,,,,,,,,,,,,,,,,,,,9620,9623,2003, citations,entry_citation,5634,229207,1,,entry citation,,,14675814,,,Random coil carbon chemical shifts of deoxyribonucleic acids,published,journal,J. Magn. Reson.,,166,1,,,,,,,,,,,,,,,,,,,,,,11,18,2004, citations,citation_1,5634,229208,2,,reference citation,,,12522297,,,Random Coil Proton Chemical Shifts of Deoxyribonucleic Acids,published,journal,J. Biomol. NMR,,24,4,,,,,,,,,,,,,,,,,,,,,,329,337,2002, citations,entry_citation,5635,229221,1,,entry citation,,,14675814,,,Random coil carbon chemical shifts of deoxyribonucleic acids,published,journal,J. Magn. Reson.,,166,1,,,,,,,,,,,,,,,,,,,,,,11,18,2004, citations,citation_1,5635,229222,2,,reference citation,,,12522297,,,Random Coil Proton Chemical Shifts of Deoxyribonucleic Acids,published,journal,J. Biomol. NMR,,24,4,,,,,,,,,,,,,,,,,,,,,,329,337,2002, citations,entry_citation,5636,229235,1,,entry citation,,,14675814,,,Random coil carbon chemical shifts of deoxyribonucleic acids,published,journal,J. Magn. Reson.,,166,1,,,,,,,,,,,,,,,,,,,,,,11,18,2004, citations,citation_1,5636,229236,2,,reference citation,,,12522297,,,Random Coil Proton Chemical Shifts of Deoxyribonucleic Acids,published,journal,J. Biomol. NMR,,24,4,,,,,,,,,,,,,,,,,,,,,,329,337,2002, citations,entry_citation,5637,229249,1,,entry citation,,,14675814,,,Random coil carbon chemical shifts of deoxyribonucleic acids,published,journal,J. Magn. Reson.,,166,1,,,,,,,,,,,,,,,,,,,,,,11,18,2004, citations,citation_1,5637,229250,2,,reference citation,,,12522297,,,Random Coil Proton Chemical Shifts of Deoxyribonucleic Acids,published,journal,J. Biomol. NMR,,24,4,,,,,,,,,,,,,,,,,,,,,,329,337,2002, citations,entry_citation,5638,229263,1,,entry citation,,,14675814,,,Random coil carbon chemical shifts of deoxyribonucleic acids,published,journal,J. Magn. Reson.,,166,1,,,,,,,,,,,,,,,,,,,,,,11,18,2004, citations,citation_1,5638,229264,2,,reference citation,,,12522297,,,Random Coil Proton Chemical Shifts of Deoxyribonucleic Acids,published,journal,J. Biomol. NMR,,24,4,,,,,,,,,,,,,,,,,,,,,,329,337,2002, citations,entry_citation,5639,229277,1,,entry citation,,,14675814,,,Random coil carbon chemical shifts of deoxyribonucleic acids,published,journal,J. Magn. Reson.,,166,1,,,,,,,,,,,,,,,,,,,,,,11,18,2004, citations,citation_1,5639,229278,2,,reference citation,,,12522297,,,Random Coil Proton Chemical Shifts of Deoxyribonucleic Acids,published,journal,J. Biomol. NMR,,24,4,,,,,,,,,,,,,,,,,,,,,,329,337,2002, citations,entry_citation,5640,229291,1,,entry citation,,,14675814,,,Random coil carbon chemical shifts of deoxyribonucleic acids,published,journal,J. Magn. Reson.,,166,1,,,,,,,,,,,,,,,,,,,,,,11,18,2004, citations,citation_1,5640,229292,2,,reference citation,,,12522297,,,Random Coil Proton Chemical Shifts of Deoxyribonucleic Acids,published,journal,J. Biomol. NMR,,24,4,,,,,,,,,,,,,,,,,,,,,,329,337,2002, citations,entry_citation,5641,229305,1,,entry citation,,,14675814,,,Random coil carbon chemical shifts of deoxyribonucleic acids,published,journal,J. Magn. Reson.,,166,1,,,,,,,,,,,,,,,,,,,,,,11,18,2004, citations,citation_1,5641,229306,2,,reference citation,,,12522297,,,Random Coil Proton Chemical Shifts of Deoxyribonucleic Acids,published,journal,J. Biomol. NMR,,24,4,,,,,,,,,,,,,,,,,,,,,,329,337,2002, citations,entry_citation,5642,229319,1,,entry citation,,,14675814,,,Random coil carbon chemical shifts of deoxyribonucleic acids,published,journal,J. Magn. Reson.,,166,1,,,,,,,,,,,,,,,,,,,,,,11,18,2004, citations,citation_1,5642,229320,2,,reference citation,,,12522297,,,Random Coil Proton Chemical Shifts of Deoxyribonucleic Acids,published,journal,J. Biomol. NMR,,24,4,,,,,,,,,,,,,,,,,,,,,,329,337,2002, citations,entry_citation,5643,229333,1,,entry citation,,,14675814,,,Random coil carbon chemical shifts of deoxyribonucleic acids,published,journal,J. Magn. Reson.,,166,1,,,,,,,,,,,,,,,,,,,,,,11,18,2004, citations,citation_1,5643,229334,2,,reference citation,,,12522297,,,Random Coil Proton Chemical Shifts of Deoxyribonucleic Acids,published,journal,J. Biomol. NMR,,24,4,,,,,,,,,,,,,,,,,,,,,,329,337,2002, citations,entry_citation,5644,229347,1,,entry citation,,,14675814,,,Random coil carbon chemical shifts of deoxyribonucleic acids,published,journal,J. Magn. Reson.,,166,1,,,,,,,,,,,,,,,,,,,,,,11,18,2004, citations,citation_1,5644,229348,2,,reference citation,,,12522297,,,Random Coil Proton Chemical Shifts of Deoxyribonucleic Acids,published,journal,J. Biomol. NMR,,24,4,,,,,,,,,,,,,,,,,,,,,,329,337,2002, citations,ref_1,5652,229486,2,,reference citation,,,10224238,,"Gurrola GB, Rosati B, Rocchetti M, Pimienta G, Zaza A, Arcangeli A, Olivotto M, Possani LD, Wanke E. A toxin to nervous, cardiac, and endocrine ERG K+ channels isolated from Centruroides noxius scorpion venom. FASEB J. 1999 May;13(8):953-62.","A toxin to nervous, cardiac, and endocrine ERG K+ channels isolated from Centruroides noxius scorpion venom.",published,journal,FASEB J.,The FASEB journal : official publication of the Federation of American Societies for Experimental Biology,13,8,,0892-6638,,,,,,,,,,,,,,,,,,,,953,962,1999,"Toxins isolated from a variety of venoms are tools for probing the physiological function and structure of ion channels. The ether-a-go-go-related genes (erg) codify for the K+ channels (ERG), which are crucial in neurons and are impaired in human long-QT syndrome and Drosophila 'seizure' mutants. We have isolated a peptide from the scorpion Centruroides noxius Hoffmann that has no sequence homologies with other toxins, and demonstrate that it specifically inhibits (IC50=16+/-1 nM) only ERG channels of different species and distinct histogenesis. These results open up the possibility of investigating ERG channel structure-function relationships and novel pharmacological tools with potential therapeutic efficacy." citations,ref_2,5652,229487,3,,reference citation,,,11023354,,"Scaloni A, Bottiglieri C, Ferrara L, Corona M, Gurrola GB, Batista C, Wanke E, Possani LD. Disulfide bridges of ergtoxin, a member of a new sub-family of peptide blockers of the ether-a-go-go-related K+ channel. FEBS Lett. 2000 Aug 18;479(3):156-7. No abstract available.","Disulfide bridges of ergtoxin, a member of a new sub-family of peptide blockers of the ether-a-go-go-related K+ channel.",published,journal,FEBS Lett.,FEBS letters,479,3,,0014-5793,,,,,,,,,,,,,,,,,,,,156,157,2000, citations,entry_citation,5653,229503,1,,entry citation,,,,,,"The solution structure of molt-inhibiting hormone from the kuruma prawn Marsupenaeus japonicus",in press,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref-1,5653,229504,2,,reference citation,,,8801521,,"Yang WJ, Aida K, Terauchi A, Sonobe H, Nagasawa H. Amino acid sequence of a peptide with molt-inhibiting activity from the kuruma prawn Penaeus japonicus. Peptides. 1996;17(2):197-202.",Amino acid sequence of a peptide with molt-inhibiting activity from the kuruma prawn Penaeus japonicus.,published,journal,Peptides,Peptides,17,2,,0196-9781,,,,,,,,,,,,,,,,,,,,197,202,1996,"Six major peptides (Pej-SGP-I-VI) that belong to the CHH family have been isolated from the sinus gland extracts of the kuruma prawn Penaeus japonicus. By in vitro assay using the Y-organ of the crayfish Procambarus clarkii, Pej-SGP-IV was found to be active in inhibiting ecdysteroid synthesis. We determined the complete amino acid sequence. Pej-SGP-IV consists of 77 amino acid residues, with both free aimno- and carboxyl-termini. The sequence of Pej-SGP-IV shows considerable similarity to that of MIH of the shore crab Carcinus maenas and less similarity to Pej-SGP-III, whose sequence has been previously determined." citations,entry_citation,5654,229532,1,,entry citation,,22289676,12379842,,,Core Mutations Switch Monomeric Protein GB1 into an Intertwined Tetramer,published,journal,Nat. Struct. Biol.,,9,11,,,,,,,,,,,,,,,,,,,,,,877,885,2002, citations,entry_citation,5655,229560,1,,entry citation,,,12578359,,,Structural basis for a lethal mutation in U6 RNA,published,journal,Biochemistry,,42,6,,,,,,,,,,,,,,,,,,,,,,1470,1477,2003, citations,entry_citation,5656,229577,1,,entry citation,,,14718654,,,"Validation of helical tilt angles in the solution NMR structure of the Z domain of Staphylococcal protein A by combined analysis of residual dipolar coupling and NOE data.",published,journal,Protein Sci.,,13,2,,,,,,,,,,,,,,,,,,,,,,549,554,2004, citations,entry_citation,5657,229597,1,,entry citation,,,,,,NMR structure for VT212,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5658,229611,1,,entry citation,,,,,,"Backbone and Ile-delta1, Leu, Val methyl 1H, 13C, and 15N NMR chemical shift assignments for human interferon-stimulated gene 15 protein",in press,journal,Biomol. NMR Assign.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_1,5658,229612,2,,reference citation,,,9217263,,"Zimmerman DE, Kulikowski CA, Huang Y, Feng W, Tashiro M, Shimotakahara S, Chien C, Powers R, Montelione GT. Automated analysis of protein NMR assignments using methods from artificial intelligence. J Mol Biol. 1997 Jun 20;269(4):592-610.",Automated analysis of protein NMR assignments using methods from artificial intelligence.,published,journal,J. Mol. Biol.,Journal of molecular biology,269,4,,0022-2836,,,,,,,,,,,,,,,,,,,,592,610,1997,"An expert system for determining resonance assignments from NMR spectra of proteins is described. Given the amino acid sequence, a two-dimensional 15N-1H heteronuclear correlation spectrum and seven to eight three-dimensional triple-resonance NMR spectra for seven proteins, AUTOASSIGN obtained an average of 98% of sequence-specific spin-system assignments with an error rate of less than 0.5%. Execution times on a Sparc 10 workstation varied from 16 seconds for smaller proteins with simple spectra to one to nine minutes for medium size proteins exhibiting numerous extra spin systems attributed to conformational isomerization. AUTOASSIGN combines symbolic constraint satisfaction methods with a domain-specific knowledge base to exploit the logical structure of the sequential assignment problem, the specific features of the various NMR experiments, and the expected chemical shift frequencies of different amino acids. The current implementation specializes in the analysis of data derived from the most sensitive of the currently available triple-resonance experiments. Potential extensions of the system for analysis of additional types of protein NMR data are also discussed." citations,ref_2,5658,229613,3,,reference citation,,,11462827,,"Moseley HN, Monleon D, Montelione GT. Automatic determination of protein backbone resonance assignments from triple resonance nuclear magnetic resonance data. Methods Enzymol. 2001;339:91-108.",Automatic determination of protein backbone resonance assignments from triple resonance nuclear magnetic resonance data.,published,journal,Meth. Enzymol.,Methods in enzymology,339,,,0076-6879,,,,,,,,,,,,,,,,,,,,91,108,2001, citations,entry_citation,5659,229635,1,,entry citation,,,,,,"Letter to the Editor: Backbone 1H, 15N and 13C assignments for the human rhinovirus 3C protease (serotype 14)",published,journal,J. Biomol. NMR,,26,1,,,,,,,,,,,,,,,,,,,,,,85,86,2003, citations,entry_citation,5660,229658,1,,entry citation,,,,,,"Insights into the Alkaline Transformation of Ferricyt c from 1H NMR Study in 30% Acetonitrile-Water",published,journal,Protein Sci.,,10,11,,,,,,,,,,,,,,,,,,,,,,2291,2300,2001,"The V* form described in the citation is a histidine-ligated conformer of ferricyt c and not hydroxide-ligated cyt c. This was proved later and submitted for publication by the same authors in Journal of Inorganic Biochemistry in 2003." citations,ref_1,5660,229659,2,,reference citation,,,,,"Wilson MT, Greenwood C (1996) In: Scott RA, Mauk AG (eds) Cytochrome c: A Multidisciplinary Approach. University Science Books, Sausalito, California p 738.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5691,230385,1,,entry citation,,,14627742,,,"Solution NMR structure of the 30S ribosomal protein S28E from Pyrococcus horikoshii.",published,journal,Protein Sci.,,12,12,,,,,,,,,,,,,,,,,,,,,,2823,2830,2003, citations,entry_citation,5716,230975,1,,entry citation,,,,,,"Solution Structure and Design of Dithiophosphate Backbone Aptamers Targeting Transcription Factor NF-kB",published,journal,Bioorg. Chem.,,30,6,,,,,,,,,,,,,,,,,,,,,,396,419,2002, citations,ref_2,5660,229660,3,,reference citation,,,9558351,,"Pollock WBR, Rosell FI, Twitchett MB, Dumont ME, Mauk AG (1998) Biochemistry 37: 6124-6131.",Bacterial expression of a mitochondrial cytochrome c. Trimethylation of lys72 in yeast iso-1-cytochrome c and the alkaline conformational transition.,published,journal,Biochemistry,Biochemistry,37,17,,0006-2960,,,,,,,,,,,,,,,,,,,,6124,6131,1998,"Saccharomyces cerevisiae iso-1-cytochrome c has been expressed in Escherichia coli by coexpression of the genes encoding the cytochrome (CYC1) and yeast cytochrome c heme lyase (CYC3). Construction of this expression system involved cloning the two genes in parallel into the vector pUC18 to give the plasmid pBPCYC1(wt)/3. Transcription was directed by two promoters, Lac and Trc, that were located upstream from CYC1. Both proteins were expressed in the cytoplasm of E. coli cells harboring the plasmid. Semianaerobic cultures grown in a fermentor produced 15 mg of recombinant iso-1-cytochrome c per liter of culture. Attempts to increase production by addition of IPTG suppressed the number of copies of the CYC1 gene within the population. Wild-type iso-1-cytochrome c expressed with pBPCYC1(wt)/3 in E. coli was compared to the same protein expressed in yeast. At neutral pH, the two proteins exhibit indistinguishable spectroscopic and physical (Tm, Em') characteristics. However, electrospray mass spectrometry revealed that the lysyl residue at position 72 is not trimethylated by E. coli as it is by S. cerevisiae. Interestingly, the pKa of the alkaline transition of the protein expressed in E. coli is approximately 0.6 pKa unit lower than that observed for the cytochrome expressed in yeast (8.5-8.7). 1H NMR spectroscopy of the bacterially expressed cytochrome collected at high pH revealed the presence of a third alkaline conformer that is not observed in the corresponding spectrum of the cytochrome expressed in yeast. These observations suggest that Lys72 can serve as an axial ligand to the heme iron of alkaline iso-1-ferricytochrome c if it is not modified posttranscriptionally to trimethyllysine." citations,ref_3,5660,229661,4,,reference citation,,,10880578,,"Russell BS, Melenkivitz R, Bren KL (2000) Proc. Natl. Acad. Sci. U.S.A. 97: 8312-8317.",NMR investigation of ferricytochrome c unfolding: detection of an equilibrium unfolding intermediate and residual structure in the denatured state.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,97,15,,0027-8424,,,,,,,,,,,,,,,,,,,,8312,8317,2000,"Horse ferricytochrome c (cyt c) undergoes exchange of one of its axial heme ligands (Met-80) for one or more non-native ligands under denaturing conditions. We have used (1)H NMR spectroscopy to detect two conformations of paramagnetic cyt c with non-native heme ligation through a range of urea concentrations. One non-native form is an equilibrium unfolding intermediate observed under partially denaturing conditions and is attributed to replacement of Met-80 with one or more Lys side chains. The second non-native form, in which the native Met ligand is replaced by a His, is observed under strongly denaturing conditions. Thermodynamic analysis of these data indicates a relatively small DeltaG (17 kJ/mol) for the transition from native to the Lys-ligated intermediate and a significantly larger DeltaG (47 kJ/mol) for the transition from native to the His-ligated species. Although CD and fluorescence data indicate that the equilibrium unfolding of cyt c is a two-state process, these NMR results implicate an intermediate with His-Lys ligation." citations,entry_citation,5661,229685,1,,entry citation,,,,,,"Letter to the Editor: Rapid backbone 1H, 13C, and 15N assignment of the V1 domain of human PKC iota using the new program IBIS",published,journal,J. Biomol. NMR,,26,4,,,,,,,,,,,,,,,,,,,,,,373,374,2003, citations,entry_citation,5662,229711,1,,entry citation,,,12595264,,,"Distinctive solution conformation of phosphatase inhibitor CPI-17 substituted with aspartate at the phosphorylation-site threonine residue.",published,journal,J. Mol. Biol.,,326,5,,,,,,,,,,,,,,,,,,,,,,1539,1547,2003, citations,entry_citation,5663,229724,1,,entry citation,,,12595264,,,"Distinctive solution conformation of phosphatase inhibitor CPI-17 substituted with aspartate at the phosphorylation-site threonine residue.",published,journal,J. Mol. Biol.,,326,5,,,,,,,,,,,,,,,,,,,,,,1539,1547,2003, citations,entry_citation,5664,229737,1,,entry citation,,22744256,12859187,,,"Solution Structure and Dynamics of Oxytetracycline Polyketide Synthase Acyl Carrier Protein from Streptomyces rimosus",published,journal,Biochemistry,,42,28,,,,,,,,,,,,,,,,,,,,,,8423,8433,2003,"The paper reports a high resolution solution structure and dynamics of the oxytetracycline acyl carrier protein. Complete proton and nitrogen chemical shift assignments were achieved using 15N labelled ACP." citations,ref_1,5664,229738,2,,reference citation,,,8163168,,"Kim ES, Bibb MJ, Butler MJ, Hopwood DA, Sherman DH. Sequences of the oxytetracycline polyketide synthase-encoding otc genes from Streptomyces rimosus. Gene. 1994 Apr 8;141(1):141-2.",Sequences of the oxytetracycline polyketide synthase-encoding otc genes from Streptomyces rimosus.,published,journal,Gene,Gene,141,1,,0378-1119,,,,,,,,,,,,,,,,,,,,141,142,1994,"The complete nucleotide sequences of the Streptomyces rimosus oxytetracycline (oxyTc) polyketide synthase (PKS)-encoding genes (otcY) has been determined, revealing three open reading frames. The deduced amino-acid sequences correspond to the presumed heterodimeric beta-ketoacyl synthase and acyl carrier protein found in other type-II (multicomponent) PKS systems that specify construction of acetate-derived polyketide antibiotics." citations,entry_citation,5665,229759,1,,entry citation,,,14525985,,,"Solution structure of the dimeric zinc binding domain of the chaperone ClpX.",published,journal,J. Biol. Chem.,,278,49,,,,,,,,,,,,,,,,,,,,,,48991,48996,2003, citations,entry_citation,5666,229784,1,,entry citation,,,,,,"Letter to the Editor: 1H, 15N and 13C backbone assignment of the Green Fluorescent Protein (GFP)",published,journal,J. Biomol. NMR,,26,3,,,,,,,,,,,,,,,,,,,,,,281,282,2003, citations,entry_citation,5667,229798,1,,entry citation,,22692433,12657633,,,The Structure of the Zinc Finger Domain from Human Splicing Factor ZNF265 Fold,published,journal,J. Biol. Chem.,,278,25,,,,,,,,,,,,,,,,,,,,,,22805,22811,2003, citations,entry_citation,5668,229822,1,,entry citation,,22638406,12654914,,,"A Novel Zinc Snap Motif Conveys Structural Stability to 3-Methyladenine DNA Glycosylase I",published,journal,J. Biol. Chem.,,278,21,,,,,,,,,,,,,,,,,,,,,,19442,19446,2003, citations,entry_citation,5669,229862,1,,entry citation,,22651060,12644454,,,"Structure and Ubiquitin Interactions of the Conserved Zinc Finger Domain of Npl4",published,journal,J. Biol. Chem.,,278,22,,,,,,,,,,,,,,,,,,,,,,20225,20234,2003, citations,ref-3,5670,229896,4,,reference citation,,,9008363,,"Laskowski RA, Rullmannn JA, MacArthur MW, Kaptein R, Thornton JM. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J Biomol NMR. 1996 Dec;8(4):477-86.",AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,8,4,,0925-2738,,,,,,,,,,,,,,,,,,,,477,486,1996,"The AQUA and PROCHECK-NMR programs provide a means of validating the geometry and restraint violations of an ensemble of protein structures solved by solution NMR. The outputs include a detailed breakdown of the restraint violations, a number of plots in PostScript format and summary statistics. These various analyses indicate both the degree of agreement of the model structures with the experimental dat, and the quality of their geometrical properties. They are intended to be of use both to support ongoing NMR structure determination and in the validation of the final results." citations,entry_citation,5671,229922,1,,entry citation,,22699281,12815257,,,"Overall Structure and Sugar Dynamics of a DNA Dodecamer from Homo- and Heteronuclear Dipolar Couplings and 31P Chemical Shift Anisotropy",published,journal,J. Biomol. NMR,,26,4,,,,,,,,,,,,,,,,,,,,,,297,315,2003, citations,ref_1,5669,229863,2,,reference citation,,,12411482,,"Meyer HH, Wang Y, Warren G. Direct binding of ubiquitin conjugates by the mammalian p97 adaptor complexes, p47 and Ufd1-Npl4. EMBO J. 2002 Nov 1;21(21):5645-52.","Direct binding of ubiquitin conjugates by the mammalian p97 adaptor complexes, p47 and Ufd1-Npl4.",published,journal,EMBO J.,The EMBO journal,21,21,,0261-4189,,,,,,,,,,,,,,,,,,,,5645,5652,2002,"The multiple functions of the p97/Cdc48p ATPase can be explained largely by adaptors that link its activity to different cellular pathways, but how these adaptors recognize different substrates is unclear. Here we present evidence that the mammalian adaptors, p47 and Ufd1-Npl4, both bind ubiquitin conjugates directly and so link p97 to ubiquitylated substrates. In the case of Ufd1-Npl4, which is involved in endoplasmic reticulum (ER)-associated degradation and nuclear envelope reassembly, binding to ubiquitin is mediated through a putative zinc finger in Npl4. This novel domain (NZF) is conserved in metazoa and is both present and functional in other proteins. In the case of p47, which is involved in the reassembly of the ER, the nuclear envelope and the Golgi apparatus, binding is mediated by a UBA domain. Unlike Ufd1-Npl4, it binds ubiquitin only when complexed with p97, and binds mono- rather than polyubiquitin conjugates. The UBA domain is required for the function of p47 in mitotic Golgi reassembly. Together, these data suggest that ubiquitin recognition is a common feature of p97-mediated reactions." citations,ref_2,5669,229864,3,,reference citation,,,11781570,,"Hetzer M, Meyer HH, Walther TC, Bilbao-Cortes D, Warren G, Mattaj IW. Distinct AAA-ATPase p97 complexes function in discrete steps of nuclear assembly. Nat Cell Biol. 2001 Dec;3(12):1086-91.",Distinct AAA-ATPase p97 complexes function in discrete steps of nuclear assembly.,published,journal,Nat. Cell Biol.,Nature cell biology,3,12,,1465-7392,,,,,,,,,,,,,,,,,,,,1086,1091,2001,"Although nuclear envelope (NE) assembly is known to require the GTPase Ran, the membrane fusion machinery involved is uncharacterized. NE assembly involves formation of a reticular network on chromatin, fusion of this network into a closed NE and subsequent expansion. Here we show that p97, an AAA-ATPase previously implicated in fusion of Golgi and transitional endoplasmic reticulum (ER) membranes together with the adaptor p47, has two discrete functions in NE assembly. Formation of a closed NE requires the p97-Ufd1-Npl4 complex, not previously implicated in membrane fusion. Subsequent NE growth involves a p97-p47 complex. This study provides the first insights into the molecular mechanisms and specificity of fusion events involved in NE formation." citations,ref_3,5669,229865,4,,reference citation,,,11740563,,"Ye Y, Meyer HH, Rapoport TA. The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol. Nature. 2001 Dec 6;414(6864):652-6.",The AAA ATPase Cdc48/p97 and its partners transport proteins from the ER into the cytosol.,published,journal,Nature,Nature,414,6864,,0028-0836,,,,,,,,,,,,,,,,,,,,652,656,2001,"In eukaryotic cells, incorrectly folded proteins in the endoplasmic reticulum (ER) are exported into the cytosol and degraded by the proteasome. This pathway is co-opted by some viruses. For example, the US11 protein of the human cytomegalovirus targets the major histocompatibility complex class I heavy chain for cytosolic degradation. How proteins are extracted from the ER membrane is unknown. In bacteria and mitochondria, members of the AAA ATPase family are involved in extracting and degrading membrane proteins. Here we demonstrate that another member of this family, Cdc48 in yeast and p97 in mammals, is required for the export of ER proteins into the cytosol. Whereas Cdc48/p97 was previously known to function in a complex with the cofactor p47 (ref. 5) in membrane fusion, we demonstrate that its role in ER protein export requires the interacting partners Ufd1 and Npl4. The AAA ATPase interacts with substrates at the ER membrane and is needed to release them as polyubiquitinated species into the cytosol. We propose that the Cdc48/p97-Ufd1-Npl4 complex extracts proteins from the ER membrane for cytosolic degradation." citations,ref_4,5669,229866,5,,reference citation,,,10811609,,"Meyer HH, Shorter JG, Seemann J, Pappin D, Warren G. A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways. EMBO J. 2000 May 15;19(10):2181-92.","A complex of mammalian ufd1 and npl4 links the AAA-ATPase, p97, to ubiquitin and nuclear transport pathways.",published,journal,EMBO J.,The EMBO journal,19,10,,0261-4189,,,,,,,,,,,,,,,,,,,,2181,2192,2000,"The AAA-ATPase, p97/Cdc48p, has been implicated in many different pathways ranging from membrane fusion to ubiquitin-dependent protein degradation. Binding of the p47 complex directs p97 to act in the post-mitotic fusion of Golgi membranes. We now describe another binding complex comprising mammalian Ufd1 and Npl4. Yeast Ufd1p is required for ubiquitin-dependent protein degradation whereas yeast Npl4p has been implicated in nuclear transport. In rat liver cytosol, Ufd1 and Npl4 form a binary complex, which exists either alone or bound to p97. Ufd1/Npl4 competes with p47 for binding to p97 and so inhibits Golgi membrane fusion. This suggests that it is involved in another cellular function catalysed by p97, the most likely being ubiquitin-dependent events during mitosis. The fact that the binding of p47 and Ufd1/Npl4 is mutually exclusive suggests that these protein complexes act as adapters, directing a basic p97 activity into different cellular pathways." citations,entry_citation,5670,229893,1,,entry citation,,,12600207,,,Structural Characterization of Hellethionins from helleborus purpurascens,published,journal,Biochemistry,,42,8,,,,,,,,,,,,,,,,,,,,,,2404,2411,2003, citations,ref-1,5670,229894,2,,reference citation,,,,,"Goddard T.D. and Kneller D.G.; Sparky 3; University of California, San Francisco",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref-2,5670,229895,3,,reference citation,,,8744573,,"Koradi R, Billeter M, Wuthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J Mol Graph. 1996 Feb;14(1):51-5, 29-32.",MOLMOL: a program for display and analysis of macromolecular structures.,published,journal,,Journal of molecular graphics,14,1,,0263-7855,,,,,,,,,,,,,,,,,,,,51,32,1996,"MOLMOL is a molecular graphics program for display, analysis, and manipulation of three-dimensional structures of biological macromolecules, with special emphasis on nuclear magnetic resonance (NMR) solution structures of proteins and nucleic acids. MOLMOL has a graphical user interface with menus, dialog boxes, and on-line help. The display possibilities include conventional presentation, as well as novel schematic drawings, with the option of combining different presentations in one view of a molecule. Covalent molecular structures can be modified by addition or removal of individual atoms and bonds, and three-dimensional structures can be manipulated by interactive rotation about individual bonds. Special efforts were made to allow for appropriate display and analysis of the sets of typically 20-40 conformers that are conventionally used to represent the result of an NMR structure determination, using functions for superimposing sets of conformers, calculation of root mean square distance (RMSD) values, identification of hydrogen bonds, checking and displaying violations of NMR constraints, and identification and listing of short distances between pairs of hydrogen atoms." citations,entry_citation,5672,229952,1,,entry citation,,21065343,11133274,,,"Automatic Assignment of NOESY Cross Peaks and Determination of the Protein Structure of a New World Scorpion Neurotoxin Using NOAH/DIAMOD",published,journal,J. Magn. Reson.,,148,1,,,,,,,,,,,,,,,,,,,,,,35,46,2001, citations,ref_1,5674,229995,2,,reference citation,,,12098779,,"Liu ZH, Chen P, Liang SP. Synthesis and oxidative refolding of hainantoxin-IV. Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao (Shanghai). 2002 Jul;34(4):516-9.",Synthesis and oxidative refolding of hainantoxin-IV.,published,journal,Sheng Wu Hua Xue Yu Sheng Wu Wu Li Xue Bao,Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica,34,4,,0582-9879,,,,,,,,,,,,,,,,,,,,516,519,2002,"Hainantoxin-IV, a neutoxic peptide from the spider Selenocosimia hainana, was synthesized by solid-phase method with fluorenylmethyoxycarbonyl amino acids (Fmoc-AA). Reverse-phase HPLC was used to monitor the oxidative folding of synthetic Hainantoxin-IV under different reaction conditions in order to find optimal conditions for renaturation of synthetic Hainantoxin-IV. The best renaturation yield was received in 5 mmol/L GSH and 0.5 mmol/L GSSG at pH 8.0 in 0.1 mol/L Tris-HCl and 0.1 mol/L NaCl buffer. The renaturated Hainantoxin-IV was monitored with MALDI-TOF MS reverse-phase HPLC and isolated mouse phrenic nerve-diaphragm preparation." citations,entry_citation,5675,230015,1,,entry citation,,,,,,Three-Dimensional Solution Structure of HAINANTOXIN-I by 2D 1H-NMR,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5676,230032,1,,entry citation,,,12919322,,,"Synthesis and Characterization of Pi4, a Scorpion Toxin from Pandinus imperator that acts on K+ Channels",published,journal,Eur. J. Biochem.,,270,17,,,,,,,,,,,,,,,,,,,,,,3583,3592,2003, citations,entry_citation,5677,230050,1,,entry citation,,,14662767,,,"NMR solution structure of the focal adhesion targeting domain of focal adhesion kinase in complex with a paxillin LD peptide: evidence for a two-site binding model.",published,journal,J. Biol. Chem.,,279,9,,,,,,,,,,,,,,,,,,,,,,8441,8451,2004, citations,entry_citation,5678,230066,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C, and 15N resonance assignments of the hepatocyte nuclear factor 6alpha (HNF-6alpha)",published,journal,J. Biomol. NMR,,28,4,,,,,,,,,,,,,,,,,,,,,,401,402,2004, citations,entry_citation,5679,230081,1,,entry citation,,22760843,12878846,,,"Letter to the Editor: 1H, 13C and 15N Chemical Shift Assignment of Xylan-binding Domain from Streptomyces olivaceoviridis E-86 Beta-xylanase",published,journal,J. Biomol. NMR,,27,1,,,,,,,,,,,,,,,,,,,,,,91,92,2003, citations,entry_citation,568,230112,1,,entry citation,,,,,"Allerhand, Adam, Dill, Kilian, Goux, Warren J., ""Applications of Natural-Abundance Carbon-13 NMR to Studies of Proteins and Glycoproteins,"" NMR and Biochemistry , 31-50 (1979).","Applications of Natural-Abundance Carbon-13 NMR to Studies of Proteins and Glycoproteins",published,journal,NMR and Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,31,50,1979, citations,entry_citation,5680,230125,1,,entry citation,,,,,,"Letter to the Editor: Sequence-specific assignment and secondary structure determination of the 195-residue complex formed by the Mycobacterium tuberculosis proteins CFP-10 and ESAT-6.",published,journal,J. Biomol. NMR,,30,2,,,,,,,,,,,,,,,,,,,,,,225,226,2004, citations,entry_citation,5681,230151,1,,entry citation,,22619798,12733903,,,Four-stranded DNA Structure Stabilized by a Novel C:G:A:T Tetrad,published,journal,J. Am. Chem. Soc.,,125,19,,,,,,,,,,,,,,,,,,,,,,5654,5662,2003, citations,entry_citation,5682,230170,1,,entry citation,,,15096641,,,"Solution Structure of 30S Ribosomal Protein S27E from Archaeoglobus Fulgidus: RS27_ARCFU: a novel fold",published,journal,Protein Sci.,,13,,,,,,,,,,,,,,,,,,,,,,,1407,1416,2004, citations,entry_citation,5683,230190,1,,entry citation,,,14997575,,,"NMR structure of the hypothetical protein AQ-1857 encoded by the YI57 gene from Aquifex aeolicus reveals a novel protein fold.",published,journal,Proteins,,54,4,,,,,,,,,,,,,,,,,,,,,,794,796,2004, citations,entry_citation,5684,230204,1,,entry citation,,,,,,1H and 15N Assigned Chemical Shifts for MTH1821,published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,2003, citations,entry_citation,5685,230224,1,,entry citation,,,12578358,,,"Solution structure of the carboxyl-terminal domain of RAP74 and NMR characterization of the FCP1-binding sites of RAP74 and human TFIIB",published,journal,Biochemistry,,42,6,,,,,,,,,,,,,,,,,,,,,,1460,1469,2003, citations,entry_citation,5686,230253,1,,entry citation,,,14739642,,,"Letter to the Editor: Backbone 1H, 13C and 15N resonance assignments of the response regulator HP1043 from Helicobactor pylori",published,journal,J. Biomol. NMR,,28,1,,,,,,,,,,,,,,,,,,,,,,85,86,2004, citations,entry_citation,5687,230278,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N resonance assignments of S-824, a de novo four_helix bundle from a designed combinatorial library",published,journal,J. Biomol. NMR,,27,4,,,,,,,,,,,,,,,,,,,,,,395,396,2003, citations,reference_1,5687,230279,2,,reference citation,,,12493832,,"Wei Y, Liu T, Sazinsky SL, Moffet DA, Pelczer I, Hecht MH. Stably folded de novo proteins from a designed combinatorial library. Protein Sci. 2003 Jan;12(1):92-102.",Stably folded de novo proteins from a designed combinatorial library.,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,12,1,,0961-8368,,,,,,,,,,,,,,,,,,,,92,102,2003,"Binary patterning of polar and nonpolar amino acids has been used as the key design feature for constructing large combinatorial libraries of de novo proteins. Each position in a binary patterned sequence is designed explicitly to be either polar or nonpolar; however, the precise identities of these amino acids are varied extensively. The combinatorial underpinnings of the ""binary code"" strategy preclude explicit design of particular side chains at specified positions. Therefore, packing interactions cannot be specified a priori. To assess whether the binary code strategy can nonetheless produce well-folded de novo proteins, we constructed a second-generation library based upon a new structural scaffold designed to fold into 102-residue four-helix bundles. Characterization of five proteins chosen arbitrarily from this new library revealed that (1) all are alpha-helical and quite stable; (2) four of the five contain an abundance of tertiary interactions indicative of well-ordered structures; and (3) one protein forms a well-folded structure with native-like features. The proteins from this new 102-residue library are substantially more stable and dramatically more native-like than those from an earlier binary patterned library of 74-residue sequences. These findings demonstrate that chain length is a crucial determinant of structural order in libraries of de novo four-helix bundles. Moreover, these results show that the binary code strategy--if applied to an appropriately designed structural scaffold--can generate large collections of stably folded and/or native-like proteins." citations,entry_citation,5688,230308,1,,entry citation,,22592268,12705830,,,NMR Structure of the Cathelin-like Domain of the Protegrin-3 Precursor,published,journal,Biochemistry,,42,16,,,,,,,,,,,,,,,,,,,,,,4669,4680,2003, citations,entry_citation,5689,230335,1,,entry citation,,22874487,14512737,,,"Letter to the Editor: 1H, 13C and 15N Backbone Assignments of the Pheromone Binding Protein from the Silk Moth Antheraea polyphemus (ApolPBP)",published,journal,J. Biomol. NMR,,27,4,,,,,,,,,,,,,,,,,,,,,,393,394,2003, citations,entry_citation,569,230352,1,,entry citation,,,,,"Poulsen, Flemming M., Hoch, Jeffrey C., Dobson, Christopher M., ""A Structural Study of the Hydrophobic Box Region of Lysozyme in Solution Using Nuclear Overhauser Effects,"" Biochemistry 19, 2597-2607 (1980).","A Structural Study of the Hydrophobic Box Region of Lysozyme in Solution Using Nuclear Overhauser Effects",published,journal,Biochemistry,,19,,,,,,,,,,,,,,,,,,,,,,,2597,2607,1980, citations,entry_citation,5690,230365,1,,entry citation,,,,,,"Bacterial expession of isotope labeled snake neurotoxin, disulfide-rich protein",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref-1,5690,230366,2,,reference citation,,,,,"Bartels C., Xia T.-H., Billeter M., Guntert P. & Wuthrich K. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules, J. Biomol. NMR (1995) 6, 1-10.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref-1,5691,230386,2,,reference citation,,,9679194,,"Kawarabayasi et al. (1998) DNA Res. 5, 55-76","Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.",published,journal,DNA Res.,DNA research : an international journal for rapid publication of reports on genes and genomes,5,2,,1340-2838,,,,,,,,,,,,,,,,,,,,55,76,1998,"The complete sequence of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3, has been determined by assembling the sequences of the physical map-based contigs of fosmid clones and of long polymerase chain reaction (PCR) products which were used for gap-filling. The entire length of the genome was 1,738,505 bp. The authenticity of the entire genome sequence was supported by restriction analysis of long PCR products, which were directly amplified from the genomic DNA. As the potential protein-coding regions, a total of 2061 open reading frames (ORFs) were assigned, and by similarity search against public databases, 406 (19.7%) were related to genes with putative function and 453 (22.0%) to the sequences registered but with unknown function. The remaining 1202 ORFs (58.3%) did not show any significant similarity to the sequences in the databases. Sequence comparison among the assigned ORFs in the genome provided evidence that a considerable number of ORFs were generated by sequence duplication. By similarity search, 11 ORFs were assumed to contain the intein elements. The RNA genes identified were a single 16S-23S rRNA operon, two 5S rRNA genes and 46 tRNA genes including two with the intron structure. All the assigned ORFs and RNA coding regions occupied 91.25% of the whole genome. The data presented in this paper are available on the internet at http:@www.nite.go.jp." citations,ref-2,5691,230387,3,,reference citation,,,8520220,,"Delaglio F., Grzesiek S., Vuister G.W., Zhu G., Pfeifer J., Bax A. J. Biomol. NMR. (1995) 6, 277-293.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref-3,5691,230388,4,,reference citation,,,,,"T. D. Goddard and D. G. Kneller, SPARKY 3, University of California, San Francisco.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref-4,5691,230389,5,,reference citation,,,9217263,,"Zimmerman D.E., Kulikowski C.A., Huang Y., Feng W., Tashiro M., Shimotakahara S., Chien C., Powers R., Montelione G.T. J. Mol. Biol. (1997) 269, 592-610",Automated analysis of protein NMR assignments using methods from artificial intelligence.,published,journal,J. Mol. Biol.,Journal of molecular biology,269,4,,0022-2836,,,,,,,,,,,,,,,,,,,,592,610,1997,"An expert system for determining resonance assignments from NMR spectra of proteins is described. Given the amino acid sequence, a two-dimensional 15N-1H heteronuclear correlation spectrum and seven to eight three-dimensional triple-resonance NMR spectra for seven proteins, AUTOASSIGN obtained an average of 98% of sequence-specific spin-system assignments with an error rate of less than 0.5%. Execution times on a Sparc 10 workstation varied from 16 seconds for smaller proteins with simple spectra to one to nine minutes for medium size proteins exhibiting numerous extra spin systems attributed to conformational isomerization. AUTOASSIGN combines symbolic constraint satisfaction methods with a domain-specific knowledge base to exploit the logical structure of the sequential assignment problem, the specific features of the various NMR experiments, and the expected chemical shift frequencies of different amino acids. The current implementation specializes in the analysis of data derived from the most sensitive of the currently available triple-resonance experiments. Potential extensions of the system for analysis of additional types of protein NMR data are also discussed." citations,ref-5,5691,230390,6,,reference citation,,,,,"Huang, Y.J. (2001). Automated determination of protein structures from NMR data by iterative analysis of self-consistent contact patterns, PhD thesis, Rutgers University, New Brunswick, NJ.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref-6,5691,230391,7,,reference citation,,,,,see: www-nmr.cabm.rutgers.edu/NMRsoftware/nmr_software.html,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref-7,5691,230392,8,,reference citation,,,10212987,,"Cornilescu, G., Delaglio, F., Bax, A. (1999) J. Biomol. NMR 13, 289-302.",Protein backbone angle restraints from searching a database for chemical shift and sequence homology.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,13,3,,0925-2738,,,,,,,,,,,,,,,,,,,,289,302,1999,"Chemical shifts of backbone atoms in proteins are exquisitely sensitive to local conformation, and homologous proteins show quite similar patterns of secondary chemical shifts. The inverse of this relation is used to search a database for triplets of adjacent residues with secondary chemical shifts and sequence similarity which provide the best match to the query triplet of interest. The database contains 13C alpha, 13C beta, 13C', 1H alpha and 15N chemical shifts for 20 proteins for which a high resolution X-ray structure is available. The computer program TALOS was developed to search this database for strings of residues with chemical shift and residue type homology. The relative importance of the weighting factors attached to the secondary chemical shifts of the five types of resonances relative to that of sequence similarity was optimized empirically. TALOS yields the 10 triplets which have the closest similarity in secondary chemical shift and amino acid sequence to those of the query sequence. If the central residues in these 10 triplets exhibit similar phi and psi backbone angles, their averages can reliably be used as angular restraints for the protein whose structure is being studied. Tests carried out for proteins of known structure indicate that the root-mean-square difference (rmsd) between the output of TALOS and the X-ray derived backbone angles is about 15 degrees. Approximately 3% of the predictions made by TALOS are found to be in error." citations,entry_citation,5712,230898,1,,entry citation,,,,,,"Letter to the Editor: Backbone resonance assignment of human eukaryotic translation initiation factor 4E (eIF4E) in complex with 7-methylguanosine diphosphate (m7GDP) and a 17-amino acid peptide derived from human eIF4GII",published,journal,J. Biomol. NMR,,27,3,,,,,,,,,,,,,,,,,,,,,,279,280,2003, citations,ref-8,5691,230393,9,,reference citation,,,9367762,,"Guntert P, Mumenthaler C, Wuthrich K. (1997) J. Mol. Biol. 273, 283-98.",Torsion angle dynamics for NMR structure calculation with the new program DYANA.,published,journal,J. Mol. Biol.,Journal of molecular biology,273,1,,0022-2836,,,,,,,,,,,,,,,,,,,,283,298,1997,"The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from distance constraints and torsion angle constraints collected by nuclear magnetic resonance (NMR) experiments performs simulated annealing by molecular dynamics in torsion angle space and uses a fast recursive algorithm to integrate the equations of motions. Torsion angle dynamics can be more efficient than molecular dynamics in Cartesian coordinate space because of the reduced number of degrees of freedom and the concomitant absence of high-frequency bond and angle vibrations, which allows for the use of longer time-steps and/or higher temperatures in the structure calculation. It also represents a significant advance over the variable target function method in torsion angle space with the REDAC strategy used by the predecessor program DIANA. DYANA computation times per accepted conformer in the ""bundle"" used to represent the NMR structure compare favorably with those of other presently available structure calculation algorithms, and are of the order of 160 seconds for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300 computer. Test calculations starting from conformers with random torsion angle values further showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures." citations,ref-9,5691,230394,10,,reference citation,,,,,see: www-nmr.cabm.rutgers.edu/NMRsoftware/nmr_software.html,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5692,230447,1,,entry citation,,22708834,12794636,,,"Structural and Functional Insights into PINCH LIM4 Domain-mediated Integrin Signaling",published,journal,Nat. Struct. Biol.,,10,7,,,,,,,,,,,,,,,,,,,,,,558,564,2003, citations,entry_citation,5693,230469,1,,entry citation,,,,,,"Letter to the Editor: Backbone assignments of Grb2 complexed with ligand peptides for SH3 and SH2 domains",published,journal,J. Biomol. NMR,,27,2,,,,,,,,,,,,,,,,,,,,,,185,186,2003, citations,ref_1,5693,230470,2,,reference citation,,,8520220,,"Delaglio, F. et al. J. Biomol. NMR 6, 277-293 (1995).",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,entry_citation,5694,230494,1,,entry citation,,,15296744,,,10-residue folded peptide designed by segment statistics,published,journal,Structure (Camb),,12,8,,,,,,,,,,,,,,,,,,,,,,1507,1518,2004, citations,entry_citation,5695,230508,1,,entry citation,,,,,,Solution Structure of the Product of the S. Cerevisiae YHR087W Gene,published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5696,230532,1,,entry citation,,,15062084,,,"Solution Structure of ZASP PDZ Domain; Implications for Sarcomere Ultrastructure and Enigma Family Redundancy",published,journal,"Structure (Cambridge, MA, U. S.)",,12,4,,,,,,,,,,,,,,,,,,,,,,611,622,2004, citations,entry_citation,5697,230562,1,,entry citation,,,15062084,,,"Solution Structure of ZASP PDZ Domain; Implications for Sarcomere Ultrastructure and Enigma Family Redundancy",published,journal,"Structure (Cambridge, MA, U. S.)",,12,4,,,,,,,,,,,,,,,,,,,,,,611,622,2004, citations,entry_citation,5698,230582,1,,entry citation,,22812265,12930992,,,"Solution Structure of the C-terminal Domain from Poly(A)-binding Protein in Trypanosoma cruzi: A Vegetal PABC Domain",published,journal,Protein Sci.,,12,9,,,,,,,,,,,,,,,,,,,,,,1925,1933,2003, citations,entry_citation,5699,230610,1,,entry citation,,22708093,12824064,,,"Structure of the N-terminal Extension of Human Aspartyl-tRNA Synthetase: Implications for its Biological Function",published,journal,Int. J. Biochem. Cell Biol.,,35,11,,,,,,,,,,,,,,,,,,,,,,1548,1557,2003, citations,entry_citation,5700,230627,1,,entry citation,,,12815266,,,"Backbone 1H, 13C and 15N resonance assignments for the 25.8 kDa DNA binding domain of the human p63 protein",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,26,4,,,,,,,,,,,,,,,,,,,,,,377,378,2003, citations,entry_citation,5701,230646,1,,entry citation,,22699291,12815267,,,"Letter to the Editor: Assignment of 1H, 13C and 15N Resonances of the Catalytic Domain of Guanine Nucleotide Exchange Factor SopE2 from Salmonella dublin",published,journal,J. Biomol. NMR,,26,4,,,,,,,,,,,,,,,,,,,,,,379,380,2003, citations,ref-1,5701,230647,2,,reference citation,,,10735884,,"Bakshi CS, Singh VP, Wood MW, Jones PW, Wallis TS, Galyov EE. Identification of SopE2, a Salmonella secreted protein which is highly homologous to SopE and involved in bacterial invasion of epithelial cells. J Bacteriol. 2000 Apr;182(8):2341-4.","Identification of SopE2, a Salmonella secreted protein which is highly homologous to SopE and involved in bacterial invasion of epithelial cells.",published,journal,J. Bacteriol.,Journal of bacteriology,182,8,,0021-9193,,,,,,,,,,,,,,,,,,,,2341,2344,2000,"Type III secreted Sop protein effectors are delivered into target eukaryotic cells and elicit cellular responses underlying Salmonella pathogenicity. In this work, we have identified another secreted protein, SopE2, and showed that SopE2 is an important invasion-associated effector. SopE2 is encoded by the sopE2 gene which is present and conserved in pathogenic strains of Salmonella. SopE2 is highly homologous to SopE, a protein encoded by a gene within a temperate bacteriophage and present in only some pathogenic strains." citations,entry_citation,5713,230920,1,,entry citation,,,,,,"Influence of pH on NMR structure and stability of the human prion protein globular domain",in preparation,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5714,230933,1,,entry citation,,22775036,12893083,,,Initiation of Repair of A/G Mismatches is Modulated by Sequence Context,published,journal,DNA Repair,,2,8,,,,,,,,,,,,,,,,,,,,,,863,878,2003, citations,entry_citation,5717,230994,1,,entry citation,,,,,,"Solution Structure and Design of Dithiophosphate Backbone Aptamers Targeting Transcription Factor NF-kB",published,journal,Bioorg. Chem.,,30,6,,,,,,,,,,,,,,,,,,,,,,396,419,2002, citations,ref-2,5701,230648,3,,reference citation,,,11440999,,"Friebel A, Ilchmann H, Aepfelbacher M, Ehrbar K, Machleidt W, Hardt WD.SopE and SopE2 from Salmonella typhimurium activate different sets of RhoGTPases of the host cell. J Biol Chem. 2001 Sep 7;276(36):34035-40.",SopE and SopE2 from Salmonella typhimurium activate different sets of RhoGTPases of the host cell.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,276,36,,0021-9258,,,,,,,,,,,,,,,,,,,,34035,34040,2001,"The bacterial enteropathogen Salmonella typhimurium employs a specialized type III secretion system to inject toxins into host cells, which trigger signaling cascades leading to cell death in macrophages, secretion of pro-inflammatory cytokines, or rearrangements of the host cell cytoskeleton and thus to bacterial invasion. Two of the injected toxins, SopE and the 69% identical protein SopE2, are highly efficient guanine nucleotide exchange factors for the RhoGTPase Cdc42 of the host cell. However, it has been a puzzle why S. typhimurium might employ two toxins with redundant function. We hypothesized that SopE and SopE2 might have different specificities for certain host cellular RhoGTPases. In vitro guanine nucleotide exchange assays and surface plasmon resonance measurements revealed that SopE is an efficient guanine nucleotide exchange factor for Cdc42 and Rac1, whereas SopE2 was interacting efficiently only with Cdc42, but not with Rac1. Affinity precipitation of Cdc42.GTP and Rac1.GTP from lysates and characteristic cytoskeletal rearrangements of infected tissue culture cells confirmed that SopE is highly efficient at activating Cdc42 and Rac1 in vivo, whereas SopE2 was efficiently activating Cdc42, but not Rac1. We conclude that the translocated effector proteins SopE and SopE2 allow S. typhimurium to specifically activate different sets of RhoGTPase signaling cascades." citations,entry_citation,5702,230682,1,,entry citation,,,,,,"1H, 13C, and 15N Chemical Shift Assignments for Omega-atracotoxin-Hv1a at pH 6.0",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,Ref_1,5702,230683,2,,reference citation,,,9228949,,"Fletcher JI, Smith R, O'Donoghue SI, Nilges M, Connor M, Howden ME, Christie MJ, King GF. The structure of a novel insecticidal neurotoxin, omega-atracotoxin-HV1, from the venom of an Australian funnel web spider. Nat Struct Biol. 1997 Jul;4(7):559-66.","The structure of a novel insecticidal neurotoxin, omega-atracotoxin-HV1, from the venom of an Australian funnel web spider.",published,journal,Nat. Struct. Biol.,Nature structural biology,4,7,,1072-8368,,,,,,,,,,,,,,,,,,,,559,566,1997,"A family of potent insecticidal toxins has recently been isolated from the venom of Australian funnel web spiders. Among these is the 37-residue peptide omega-atracotoxin-HV1 (omega-ACTX-HV1) from Hadronyche versuta. We have chemically synthesized and folded omega-ACTX-HV1, shown that it is neurotoxic, ascertained its disulphide bonding pattern, and determined its three-dimensional solution structure using NMR spectroscopy. The structure consists of a solvent-accessible beta-hairpin protruding from a disulphide-bonded globular core comprising four beta-turns. The three intramolecular disulphide bonds from a cystine knot motif similar to that seen in several other neurotoxic peptides. Despite limited sequence identity, omega-ACTX-HV1 displays significant structural homology with the omega-agatoxins and omega-conotoxins, both of which are vertebrate calcium channel antagonists; however, in contrast with these toxins, we show that omega-ACTX-HV1 inhibits insect, but not mammalian, voltage-gated calcium channel currents." citations,Ref_2,5702,230684,3,,reference citation,,,11313356,,"Tedford HW, Fletcher JI, King GF. Functional significance of the beta hairpin in the insecticidal neurotoxin omega-atracotoxin-Hv1a. J Biol Chem. 2001 Jul 13;276(28):26568-76.",Functional significance of the beta hairpin in the insecticidal neurotoxin omega-atracotoxin-Hv1a.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,276,28,,0021-9258,,,,,,,,,,,,,,,,,,,,26568,26576,2001,"omega-Atracotoxin-Hv1a is an insect-specific neurotoxin whose phylogenetic specificity derives from its ability to antagonize insect, but not vertebrate, voltage-gated calcium channels. In order to help understand its mechanism of action and to enhance its utility as a lead compound for insecticide development, we used a combination of protein engineering and site-directed mutagenesis to probe the toxin for key functional regions. First, we constructed a Hairpinless mutant in which the C-terminal beta-hairpin, which is highly conserved in this family of neurotoxins, was excised without affecting the fold of the residual disulfide-rich core of the toxin. The Hairpinless mutant was devoid of insecticidal activity, indicating the functional importance of the hairpin. We subsequently developed a highly efficient system for production of recombinant toxin and then probed the hairpin for key functional residues using alanine-scanning mutagenesis followed by a second round of mutagenesis based on initial ""hits"" from the alanine scan. This revealed that two spatially proximal residues, Asn(27) and Arg(35), form a contiguous molecular surface that is essential for toxin activity. We propose that this surface of the beta-hairpin is a key site for interaction of the toxin with insect calcium channels." citations,entry_citation,5703,230701,1,,entry citation,,22588902,12702812,,,"Structure of the U6 RNA Intramolecular Stem-loop Harboring an SP-phosphorothioate Modification",published,journal,RNA,,9,5,,,,,,,,,,,,,,,,,,,,,,533,542,2003, citations,citation,5704,230723,1,,entry citation,,,,,,"1H, 15N and 13C resonance assignment of the hypothetical protein mth677from Mthanobacterium thermoautotrophicum",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5705,230743,1,,entry citation,,,14739640,,,"New NMR experiments for RNA nucleobase resonance assignment and chemical shift analysis of an RNA UUCG tetraloop",published,journal,J. Biomol. NMR,,28,1,,,,,,,,,,,,,,,,,,,,,,69,79,2004, citations,entry_citation,5706,230759,1,,entry citation,,22568288,12682015,,,"Structural Basis for Antibiotic Recognition by the TipA Class of Multidrug-resistance Transcriptional Regulators",published,journal,EMBO J.,,22,8,,,,,,,,,,,,,,,,,,,,,,1824,1834,2003, citations,entry_citation,5707,230786,1,,entry citation,,,15037075,,,"Solution Structure, Dynamics, and Hydrodynamics of the Calcium-bound Cross-reactive Birch Pollen Allergen Bet v 4 Reveal a Canonical Monomeric Two-EF-hand Assembly with a Regulatory Function",published,journal,J. Mol. Biol.,,336,5,,,,,,,,,,,,,,,,,,,,,,1141,1157,2004, citations,entry_citation,5708,230811,1,,entry citation,,22603289,12717030,,,"Solution Structure of the N-terminal Amphitropic Domain of Escherichia coli Glucose-specific Enzyme IIA in Membrane-mimetic Micelles",published,journal,Protein Sci.,,12,5,,,,,,,,,,,,,,,,,,,,,,1087,1096,2003, citations,entry_citation,5709,230834,1,,entry citation,,22699292,12815268,,,"Letter to the Editor: 1H, 15N and 13C Resonance Assignments of the TPR Domain of hSGT",published,journal,J. Biomol. NMR,,26,4,,,,,,,,,,,,,,,,,,,,,,381,382,2003, citations,entry_citation,5710,230854,1,,entry citation,,,14673079,,,"Structure of Mth11/Mth Rpp29, an essential protein subunit of archaeal and eukaryotic RNase P",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,100,26,,,,,,,,,,,,,,,,,,,,,,15398,15403,2003, citations,entry_citation,5711,230868,1,,entry citation,,,,,,"Solution structure and backbone dynamics of the biotinylation domain of Helicobacter pylori biotin-carboxyl carrier protein",published,journal,B. Korean Chem. Soc.,,29,2,,,,,,,,,,,,,,,,,,,,,,347,351,2008, citations,entry_citation,5718,231012,1,,entry citation,,,,,,"Solution Structure and Design of Dithiophosphate Backbone Aptamers Targeting Transcription Factor NF-kB",published,journal,Bioorg. Chem.,,30,6,,,,,,,,,,,,,,,,,,,,,,396,419,2002, citations,entry_citation,5719,231031,1,,entry citation,,22760844,12878847,,,"Letter to the Editor: Resonance Assignment and Secondary Structure of an N-terminal Fragment of the Human La Protein",published,journal,J. Biomol. NMR,,27,1,,,,,,,,,,,,,,,,,,,,,,93,94,2003, citations,entry_citation,5720,231044,1,,entry citation,,,12009888,,,"Domain Flexibility in Ligand-Free and Inhibitor-Bound Escherichia coli Adenylate Kinase Based on a Mode-Coupling Analysis of 15N Spin Relaxation",published,journal,Biochemistry,,41,20,,,,,,,,,,,,,,,,,,,,,,6271,6281,2002, citations,entry_citation,5721,231065,1,,entry citation,,,14739646,,,"Letter to the Editor: Backbone resonance assignment of an aminoglycoside-3'-phosphotransferase type IIa",published,journal,J. Biomol. NMR,,28,1,,,,,,,,,,,,,,,,,,,,,,93,94,2004, citations,entry_citation,5722,231080,1,,entry citation,,22727205,12842464,,,"Unique Features in the C-terminal Domain Provide Caltractin with Target Specificity",published,journal,J. Mol. Biol.,,330,3,,,,,,,,,,,,,,,,,,,,,,473,484,2003, citations,entry_citation,5723,231098,1,,entry citation,,22791616,12732626,,,"Correlation of the Sweetness of Variants of the Protein Brazzein with Patterns of Hydrogen Bonds Detected by NMR Spectroscopy",published,journal,J. Biol. Chem.,,278,33,,,,,,,,,,,,,,,,,,,,,,31331,31339,2003, citations,entry_citation,5724,231121,1,,entry citation,,22791616,12732626,,,"Correlation of the Sweetness of Variants of the Protein Brazzein with Patterns of Hydrogen Bonds Detected by NMR Spectroscopy",published,journal,J. Biol. Chem.,,278,33,,,,,,,,,,,,,,,,,,,,,,31331,31339,2003, citations,entry_citation,5725,231144,1,,entry citation,,22791616,12732626,,,"Correlation of the Sweetness of Variants of the Protein Brazzein with Patterns of Hydrogen Bonds Detected by NMR Spectroscopy",published,journal,J. Biol. Chem.,,278,33,,,,,,,,,,,,,,,,,,,,,,31331,31339,2003, citations,entry_citation,5726,231165,1,,entry citation,,22791616,12732626,,,"Correlation of the Sweetness of Variants of the Protein Brazzein with Patterns of Hydrogen Bonds Detected by NMR Spectroscopy",published,journal,J. Biol. Chem.,,278,33,,,,,,,,,,,,,,,,,,,,,,31331,31339,2003, citations,entry_citation,5727,231189,1,,entry citation,,22791616,12732626,,,"Correlation of the Sweetness of Variants of the Protein Brazzein with Patterns of Hydrogen Bonds Detected by NMR Spectroscopy",published,journal,J. Biol. Chem.,,278,33,,,,,,,,,,,,,,,,,,,,,,31331,31339,2003, citations,entry_citation,5728,231212,1,,entry citation,,22791616,12732626,,,"Correlation of the Sweetness of Variants of the Protein Brazzein with Patterns of Hydrogen Bonds Detected by NMR Spectroscopy",published,journal,J. Biol. Chem.,,278,33,,,,,,,,,,,,,,,,,,,,,,31331,31339,2003, citations,entry_citation,5729,231235,1,,entry citation,,22627427,12741814,,,"Solution Structure, Dynamics, and Thermodynamics of the Native State Ensemble of the Sem-5 C-terminal SH3 Domain",published,journal,Biochemistry,,42,19,,,,,,,,,,,,,,,,,,,,,,5582,5591,2003, citations,entry_citation,573,231249,1,,entry citation,,,,,"Pan, Tao, Coleman, Joseph E., ""GAL4 transcription factor is not a ""zinc finger"" but forms a Zn(II)2Cys6 binuclear cluster,"" Proc. Natl. Acad. Sci. U.S.A. 87, 2077-2081 (1990).","GAL4 transcription factor is not a ""zinc finger"" but forms a Zn(II)2Cys6 binuclear cluster",published,journal,Proc. Natl. Acad. Sci. U.S.A.,,87,,,,,,,,,,,,,,,,,,,,,,,2077,2081,1990, citations,entry_citation,5730,231262,1,,entry citation,,,12578353,,,"Solution Structure of a Cis-Opened (10R)-N6-Deoxyadenosine Adduct of (9S,10R)-(9,10)-Epoxy-7,8,9,10-tetrahydrobenzo[a]pyrene in a DNA Duplex",published,journal,Biochemistry,,42,6,,,,,,,,,,,,,,,,,,,,,,1410,1420,2003, citations,ref-1,5730,231263,2,,reference citation,,,,,"Meadows, R., Post, C.B., Luxon, B.A. and Gorenstein, D.G., University of Texas Medical Branch, Galveston, TX 77555-1157",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref-2,5730,231264,3,,reference citation,,,,,"Case, D.A., Pearlman, D.A. et al, UCSF.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5731,231288,1,,entry citation,,,,,,"Alpha and beta Conformational preferences in Fibril Forming Peptides Characterised using NMR and CD Techniques",published,journal,"Spectroscopy (Amsterdam, Neth.)",,18,1,,,,,,,,,,,,,,,,,,,,,,1,11,2004, citations,entry_citation,5732,231310,1,,entry citation,,,,,,"Alpha and beta Conformational preferences in Fibril Forming Peptides Characterised using NMR and CD Techniques",published,journal,"Spectroscopy (Amsterdam, Neth.)",,18,1,,,,,,,,,,,,,,,,,,,,,,1,11,2004, citations,entry_citation,5733,231328,1,,entry citation,,,,,,"Alpha and beta Conformational preferences in Fibril Forming Peptides Characterised using NMR and CD Techniques",published,journal,"Spectroscopy (Amsterdam, Neth.)",,18,1,,,,,,,,,,,,,,,,,,,,,,1,11,2004, citations,entry_citation,5734,231346,1,,entry citation,,,,,,"Alpha and beta Conformational preferences in Fibril Forming Peptides Characterised using NMR and CD Techniques",published,journal,"Spectroscopy (Amsterdam, Neth.)",,18,1,,,,,,,,,,,,,,,,,,,,,,1,11,2004, citations,entry_citation,5735,231364,1,,entry citation,,,15160315,,,"The Solution Structure of Rat Abeta-(1-28) and its Interaction with Zinc ion: Insights into the Scarity of Amyloid Deposition in Aged Rat Brain",published,journal,J. Biol. Inorg. Chem.,,9,5,,,,,,,,,,,,,,,,,,,,,,627,635,2004, citations,entry_citation,5736,231377,1,,entry citation,,22874490,14512740,,,"Letter to the Editor: Sequence-specific Resonance Assignments of ICln, an ion channel cloned from epithelial Cells",published,journal,J. Biomol. NMR,,27,4,,,,,,,,,,,,,,,,,,,,,,399,400,2003, citations,entry_citation,5737,231394,1,,entry citation,,22807851,12926351,,,"Structure of the Parallel-stranded DNA Quadruplex d(TTAGGGT)4 Containing the Human Telomeric Repeat: Evidence for A-tetrad Formation from NMR and Molecular Dynamics Simulations",published,journal,Org. Biomol. Chem.,Organic and Biomolecular Chemistry,1,10,,,,,,,,,,,,,,,,,,,,,,1650,1656,2003, citations,entry_citation,5738,231410,1,,entry citation,,22580599,12693929,,,"NMR Structure of a Bifunctional Rhodamine Labeled N-domain of Troponin C Complexed with the Regulatory 'Switch' Peptide from Troponin I: Implications for in situ Fluorescence Studies in Muscle Fibers",published,journal,Biochemistry,,42,15,,,,,,,,,,,,,,,,,,,,,,4333,4348,2003, citations,entry_citation,5739,231436,1,,entry citation,,22680616,12795597,,,"Wobble dC.dA Pairing 5' to the Cationic Guanine N7 8,9-Dihydro-8-(N7-guanyl)-9-Hydroxyaflatoxin B1 Adduct: Implications for Nontargeted AFB1 Mutagenesis",published,journal,Biochemistry,,42,23,,,,,,,,,,,,,,,,,,,,,,7023,7034,2003, citations,entry_citation,5740,231465,1,,entry citation,,22864623,14500880,,,"Diagnostic Chemical Shift Markers for Loop Conformation and Substrate and Cofactor Binding in Dihydrofolate Reductase Complexes",published,journal,Protein Sci.,,12,10,,,,,,,,,,,,,,,,,,,,,,2230,2238,2003, citations,entry_citation,5741,231488,1,,entry citation,,22864623,14500880,,,"Diagnostic Chemical Shift Markers for Loop Conformation and Substrate and Cofactor Binding in Dihydrofolate Reductase Complexes",published,journal,Protein Sci.,,12,10,,,,,,,,,,,,,,,,,,,,,,2230,2238,2003, citations,entry_citation,5742,231511,1,,entry citation,,,14604533,,,"Solution structure of Sco1: a thioredoxin-like protein involved in cytochrome c oxidase assembly",published,journal,"Structure (Cambridge, MA, U. S.)",,11,11,,,,,,,,,,,,,,,,,,,,,,1431,1443,2003, citations,entry_citation,5743,231543,1,,entry citation,,,14622018,,,"Structural Characterization by NMR of the Natively Unfolded Extracellular Domain of beta-Dystroglycan: Toward the Identification of the Binding Epitope for alpha-Dystroglycan",published,journal,Biochemistry,,42,46,,,,,,,,,,,,,,,,,,,,,,13717,13724,2003, citations,ref_1,5743,231544,2,,reference citation,,,11166570,,"Winder S.J. Trends Biochem Sci. 2001 Feb;26(2):118-24",The complexities of dystroglycan.,published,journal,Trends Biochem. Sci.,Trends in biochemical sciences,26,2,,0968-0004,,,,,,,,,,,,,,,,,,,,118,124,2001,"The notion of dystroglycan as a simple laminin-binding receptor is increasingly being challenged. New roles and new binding partners are continually emerging. Recent structural advances have provided exciting new insights into the precise molecular interactions between dystroglycan and other key components of the dystroglycan complex. Coupled with an increasing understanding of dystroglycan function at the molecular level, we are finally beginning to probe the complexities of dystroglycan, not only in disease, but in development, adhesion and signalling." citations,ref_2,5743,231545,3,,reference citation,,,11257514,,"Boffi A, Bozzi M, Sciandra F, Woellner C, Bigotti MG, Ilari A, Brancaccio A. Biochim Biophys Acta. 2001 Mar 9;1546(1):114-21",Plasticity of secondary structure in the N-terminal region of beta-dystroglycan.,published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1546,1,,0006-3002,,,,,,,,,,,,,,,,,,,,114,121,2001,"The secondary structure content of the N-terminal extracellular domain of beta-dystroglycan (a recombinant fragment extending from positions 654 to 750) has been quantitatively determined by means of CD and FTIR spectroscopies. The elements of secondary structure, namely an 8-10 residue long alpha-helix (10%) and two beta-strands (24%) have been assigned to specific amino acid sequences by means of a GOR constrained prediction method. The remaining 66% of the whole sequence is classified as turns or unordered. The temperature dependence of CD and FTIR spectra has been investigated in detail. A reversible, non-cooperative thermal transition is observed with both CD and FTIR spectroscopies up to 95 degrees C. The profile of the transition is typical of the unfolding of isolated peptides and corresponds to the progressive loss of the secondary structure elements of the protein with no evidence for collapsing phenomena, typical of globular proteins, upon heating." citations,ref_3,5743,231546,4,,reference citation,,,11502221,,"Sciandra F, Schneider M, Giardina B, Baumgartner S, Petrucci TC, Brancaccio A. Eur J Biochem 2001 Aug;268(16):4590-7",Identification of the beta-dystroglycan binding epitope within the C-terminal region of alpha-dystroglycan.,published,journal,Eur. J. Biochem.,European journal of biochemistry / FEBS,268,16,,0014-2956,,,,,,,,,,,,,,,,,,,,4590,4597,2001,"Dystroglycan is a receptor for extracellular matrix proteins that plays a crucial role during embryogenesis in addition to adult tissue stabilization. A precursor product of a single gene is post-translationally cleaved to form two different subunits, alpha and beta. The extracellular alpha-dystroglycan is a membrane-associated, highly glycosylated protein that binds to various extracellular matrix molecules, whereas the transmembrane beta-dystroglycan binds, via its cytosolic domain, to dystrophin and many other proteins. alpha- and beta-Dystroglycan interact tightly but noncovalently. We have previously shown that the N-terminal region of beta-dystroglycan, beta-DG(654-750), binds to the C-terminal region of murine alpha-dystroglycan independently from glycosylation. Preparing a series of deleted recombinant fragments and using solid-phase binding assays, the C-terminal sequence of alpha-dystroglycan containing the binding epitope for beta-dystroglycan has been defined more precisely. We found that a region of 36 amino acids, from position 550-585, is required for binding the extracellular region, amino acids 654-750 of beta-dystroglycan. Recently, a dystroglycan-like gene was identified in Drosophila that showed a moderate degree of conservation with vertebrate dystroglycan (31% identity, 48% similarity). Surprisingly, the Drosophila sequence contains a region showing a higher degree of identity and conservation (45% and 66%) that coincides with the 550-585 sequence of vertebrate alpha-dystroglycan. We have expressed this Drosophila dystroglycan fragment and measured its binding to the extracellular region of vertebrate (murine) beta-dystroglycan (Kd = 6 +/- 1 microM). These data confirm the proper identification of the beta-dystroglycan binding epitope and stress the importance of this region during evolution. This finding might help the rational design of dystroglycan-specific binding drugs, that could have important biomedical applications." citations,ref_4,5743,231547,5,,reference citation,,,11423118,,"Bozzi M, Veglia G, Paci M, Sciandra F, Giardina B, Brancaccio A. FEBS Lett 2001 Jun 22;499(3):210-4",A synthetic peptide corresponding to the 550-585 region of alpha-dystroglycan binds beta-dystroglycan as revealed by NMR spectroscopy.,published,journal,FEBS Lett.,FEBS letters,499,3,,0014-5793,,,,,,,,,,,,,,,,,,,,210,214,2001,"We have probed the binding of a synthetic peptide corresponding to the region 550-585 of the alpha subunit of dystroglycan with a recombinant protein fragment corresponding to the N-terminal extracellular region of beta-dystroglycan (654-750), using NMR in solution. In a 30:1 molar ratio, the peptide binds to the recombinant protein fragment in the fast/intermediate exchange regime. By monitoring the peptide intra-residue HN-Halpha peak volumes of the 2D TOCSY NMR spectra, both in the absence and in the presence of the recombinant fragment, we determined the differential binding affinities of each amino acid. We found that the residues in the region 550-565 (SWVQFNSNSQLMYGLP) are more influenced by the presence of the protein, whereas the C-terminal portion is marginally involved. These NMR results have been confirmed by solid-phase binding assays." citations,ref_5,5743,231548,6,,reference citation,,,11495245,,"Panchal SC, Bhavesh NS, Hosur RV J Biomol NMR 2001 Jun;20(2):135-47","Improved 3D triple resonance experiments, HNN and HN(C)N, for HN and 15N sequential correlations in (13C, 15N) labeled proteins: application to unfolded proteins.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,20,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,147,2001,"Two triple resonance experiments, HNN and HN(C)N, are presented which correlate HN and 15N resonances sequentially along the polypeptide chain of a doubly (13C, 15N) labeled protein. These incorporate several improvements over the previously published sequences for a similar purpose and have several novel features. The spectral characteristics enable direct identification of certain triplets of residues, which provide many starting points for the sequential assignment procedure. The experiments are sensitive and their utility has been demonstrated with a 22 kDa protein under unfolding conditions where most of the standard triple resonance experiments such as HNCA, CBCANH etc. have limited success because of poor amide, Calpha and Cbeta chemical shift dispersions." citations,entry_citation,5744,231562,1,,entry citation,,22590450,12586824,,,A Broken Alpha-helix in Folded Alpha-synuclein,published,journal,J. Biol. Chem.,,278,17,,,,,,,,,,,,,,,,,,,,,,15313,15318,2003, citations,entry_citation,5745,231582,1,,entry citation,,,8613986,,,The solution structure of bovine ferricytochrome b5 determined using heteronuclear NMR methods,published,journal,J. Biomol. NMR,,258,1,,,,,,,,,,,,,,,,,,,,,,172,189,1996, citations,entry_citation,5746,231609,1,,entry citation,,,12009888,,,"Domain Flexibility in Ligand-Free and Inhibitor-Bound Escherichia coli Adenylate Kinase Based on a Mode-Coupling Analysis of 15N Spin Relaxation",published,journal,Biochemistry,,41,20,,,,,,,,,,,,,,,,,,,,,,6271,6281,2002, citations,entry_citation,5747,231636,1,,entry citation,,22558628,12655072,,,Preorganization of Molecular Binding Sites in Designed Diiron Proteins,published,journal,Proc. Natl. Acad. Sci. U. S. A.,,100,7,,,,,,,,,,,,,,,,,,,,,,3772,3777,2003, citations,entry_citation,5748,231654,1,,entry citation,,,,,,"Letter to the Editor: Assignment of 1H, 13C, and 15N Resonances of the ARID Domain of P270",published,journal,J. Biomol. NMR,,27,3,,,,,,,,,,,,,,,,,,,,,,277,278,2003, citations,entry_citation,5749,231668,1,,entry citation,,,16115804,,,"Isolation, gene expression and solution structure of a novel moricin analogue, an antibacterial peptide from a lepidopteran insect, Spodoptera litura",published,journal,Biochim. Biophys. Acta,,1752,1,,,,,,,,,,,,,,,,,,,,,,83,92,2005, citations,entry_citation,5750,231684,1,,entry citation,,22640578,12755599,,,"BAFF/BLyS Receptor 3 Comprises a Minimal TNF Receptor-like Module that Encodes a Highly Focused Ligand-binding Site",published,journal,Biochemistry,,42,20,,,,,,,,,,,,,,,,,,,,,,5977,5983,2003, citations,citation_1,5751,231699,1,,entry citation,,22726682,12670942,,,"NMR Structure of the Netrin-like Domain (NTR) of Human Type 1 Procollagen C-Proteinase Enhancer Defines Structural Consensus of NTR Domains and Assesses Potential Proteinase Inhibitory Activity and Ligand Binding",published,journal,J. Biol. Chem.,,278,28,,,,,,,,,,,,,,,,,,,,,,25982,25989,2003, citations,entry_citation,5752,231713,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N backbone resonance assignment of the Integrin alpha2 I-domain",published,journal,J. Biomol. NMR,,27,2,,,,,,,,,,,,,,,,,,,,,,191,192,2003, citations,entry_citation,5753,231735,1,,entry citation,,22708502,12823963,,,"Towards an Understanding of the Poliovirus Replication Complex: The Solution Structure of the Soluble Domain of the Poliovirus 3A Protein",published,journal,J. Mol. Biol.,,330,2,,,,,,,,,,,,,,,,,,,,,,225,234,2003, citations,entry_citation,5754,231757,1,,entry citation,,22794757,12913419,,,"Letter to the Editor: 1H, 13C and 15N Backbone Resonance Assignment of the VASP EVH1 Domain",published,journal,J. Biomol. NMR,,27,2,,,,,,,,,,,,,,,,,,,,,,189,190,2003, citations,ref_1,5754,231758,2,,reference citation,,,,,"Ch. Bartels, T.-H. Xia, M. Billeter, P. Guntert, K. Wuthrich (1995). J. Biomol. NMR 5, 1-10",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_2,5754,231759,3,,reference citation,,,10212987,,"G. Cornilescu, F. Delaglio, A. Bax (1999). J. Biomol. NMR 13, 289-302",Protein backbone angle restraints from searching a database for chemical shift and sequence homology.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,13,3,,0925-2738,,,,,,,,,,,,,,,,,,,,289,302,1999,"Chemical shifts of backbone atoms in proteins are exquisitely sensitive to local conformation, and homologous proteins show quite similar patterns of secondary chemical shifts. The inverse of this relation is used to search a database for triplets of adjacent residues with secondary chemical shifts and sequence similarity which provide the best match to the query triplet of interest. The database contains 13C alpha, 13C beta, 13C', 1H alpha and 15N chemical shifts for 20 proteins for which a high resolution X-ray structure is available. The computer program TALOS was developed to search this database for strings of residues with chemical shift and residue type homology. The relative importance of the weighting factors attached to the secondary chemical shifts of the five types of resonances relative to that of sequence similarity was optimized empirically. TALOS yields the 10 triplets which have the closest similarity in secondary chemical shift and amino acid sequence to those of the query sequence. If the central residues in these 10 triplets exhibit similar phi and psi backbone angles, their averages can reliably be used as angular restraints for the protein whose structure is being studied. Tests carried out for proteins of known structure indicate that the root-mean-square difference (rmsd) between the output of TALOS and the X-ray derived backbone angles is about 15 degrees. Approximately 3% of the predictions made by TALOS are found to be in error." citations,ref_3,5754,231760,4,,reference citation,,,10990454,,"Ball LJ, Kuhne R, Hoffmann B, Hafner A, Schmieder P, Volkmer-Engert R, Hof M, Wahl M, Schneider-Mergener J, Walter U, Oschkinat H, Jarchau T. EMBO J. 2000 Sep 15;19(18):4903-14.",Dual epitope recognition by the VASP EVH1 domain modulates polyproline ligand specificity and binding affinity.,published,journal,EMBO J.,The EMBO journal,19,18,,0261-4189,,,,,,,,,,,,,,,,,,,,4903,4914,2000,"The Ena-VASP family of proteins act as molecular adaptors linking the cytoskeletal system to signal transduction pathways. Their N-terminal EVH1 domains use groups of exposed aromatic residues to specifically recognize 'FPPPP' motifs found in the mammalian zyxin and vinculin proteins, and ActA protein of the intracellular bacterium Listeria monocytogenes. Here, evidence is provided that the affinities of these EVH1-peptide interactions are strongly dependent on the recognition of residues flanking the core FPPPP motifs. Determination of the VASP EVH1 domain solution structure, together with peptide library screening, measurement of individual K(d)s by fluorescence titration, and NMR chemical shift mapping, revealed a second affinity-determining epitope present in all four ActA EVH1-binding motifs. The epitope was shown to interact with a complementary hydrophobic site on the EVH1 surface and to increase strongly the affinity of ActA for EVH1 domains. We propose that this epitope, which is absent in the sequences of the native EVH1-interaction partners zyxin and vinculin, may provide the pathogen with an advantage when competing for the recruitment of the host VASP and Mena proteins in the infected cell." citations,entry_citation,5755,231777,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N resonance assignments and secondary structure of the human protein tyrosine phosphatase, PRL-2",published,journal,J. Biomol. NMR,,27,4,,,,,,,,,,,,,,,,,,,,,,397,398,2003, citations,entry_citation,5756,231801,1,,entry citation,,,,,,"Letter to the Editor: Resonace Assignments for the 21 kDa engineered fluorescein-binding lipocalin FluA",published,journal,J. Biomol. NMR,,27,2,,,,,,,,,,,,,,,,,,,,,,187,188,2003, citations,entry_citation,5757,231831,1,,entry citation,,,,,,"Solid state NMR sequential resonance assignments and conformational analysis of the 2x10.4 kDa dimeric form of the Bacillus subtilis protein Crh",published,journal,J. Biomol. NMR,,27,4,,,,,,,,,,,,,,,,,,,,,,323,339,2003, citations,ref_1,5757,231832,2,,reference citation,,,11361074,,,"Evidence for a dimerisation state of the Bacillus subtilis catabolite repression HPr-like protein, Crh.",published,journal,J. Mol. Microbiol. Biotechnol.,Journal of molecular microbiology and biotechnology,3,3,,1464-1801,,,,,,,,,,,,,,,,,,,,429,432,2001,"The Bacillus subtilis catabolite repression HPr (Crh) exhibits 45% sequence identity when compared to histidine-containing protein (HPr), a phosphocarrier protein of the phosphoenolpyruvate:carbohydrate phosphotransferase system. We report here that Crh preparations contain a mixture of monomers and homodimers, whereas HPr is known to be monomeric in solution. The dissociation rate of dimers is very slow (t1/2 of about 10 hours), and the percentage of dimers in Crh preparations increases with rising temperature or protein concentration. However, at temperatures above 25 degrees C and a protein concentration of 10 mg/ml, Crh dimers slowly aggregate. Typically, NMR spectra recorded at 25 degrees C showed the coexistence of both forms of Crh, while in Crh solutions kept at 35 degrees C, almost exclusively Crh monomers could be detected. Circular dichroism analysis revealed that the monomeric and dimeric forms of Crh are well folded and exhibit the same overall structure. The physiological significance of the slow Crh monomer/dimer equilibrium remains enigmatic." citations,entry_citation,5768,232065,1,,entry citation,,22770441,12888353,,,"A Core Mutation Affecting the Folding Properties of a Soluble Domain of the ATPase Protein CopA from Bacillus subtilis",published,journal,J. Mol. Biol.,,331,2,,,,,,,,,,,,,,,,,,,,,,473,484,2003, citations,ref_2,5757,231833,3,,reference citation,,,11916384,,,"Solution structure and dynamics of Crh, the Bacillus subtilis catabolite repression HPr.",published,journal,J. Mol. Biol.,Journal of molecular biology,317,1,,0022-2836,,,,,,,,,,,,,,,,,,,,131,144,2002,"The solution structure and dynamics of the Bacillus subtilis HPr-like protein, Crh, have been investigated using NMR spectroscopy. Crh exhibits high sequence identity (45 %) to the histidine-containing protein (HPr), a phospho-carrier protein of the phosphoenolpyruvate (PEP):carbohydrate phosphotransferase system, but contains no catalytic His15, the site of PEP-dependent phosphorylation in HPr. Crh also forms a mixture of monomers and dimers in solution whereas HPr is known to be monomeric. Complete backbone and side-chain assignments were obtained for the monomeric form, and 60 % of the dimer backbone resonances; allowing the identification of the Crh dimer interface from chemical-shift mapping. The conformation of Crh was determined to a precision of 0.46(+/-0.06) A for the backbone atoms, and 1.01(+/-0.08) A for the heavy atoms. The monomer structure is similar to that of known HPr 2.67(+/-0.22) A (C(alpha) rmsd), but has a few notable differences, including a change in the orientation of one of the helices (B), and a two-residue shift in beta-sheet pairing of the N-terminal strand with the beta4 strand. This shift results in a shortening of the surface loop present in HPr and consequently provides a flatter surface in the region of dimerisation contact, which may be related to the different oligomeric nature of these two proteins. A binding site of phospho-serine(P-Ser)-Crh with catabolite control protein A (CcpA) is proposed on the basis of highly conserved surface side-chains between Crh and HPr. This binding site is consistent with the model of a dimer-dimer interaction between P-Ser-Crh and CcpA. (15)N relaxation measured in the monomeric form also identified differential local mobility in the helix B which is located in the vicinity of this site." citations,ref_3,5757,231834,4,,reference citation,,,12972249,,"Dimerization of Crh by reversible 3D domain swapping induces structural adjustments to its monomeric homologue HPr Juy, M., Penin, F., Favier, A., Galinier, A., Montserret, R., Haser, R., Deutscher, J. and Bockmann, A. (2003) submitted",Dimerization of Crh by reversible 3D domain swapping induces structural adjustments to its monomeric homologue Hpr.,published,journal,J. Mol. Biol.,Journal of molecular biology,332,4,,0022-2836,,,,,,,,,,,,,,,,,,,,767,776,2003,"The crystal structure of the regulatory protein Crh from Bacillus subtilis was solved at 1.8A resolution and showed an intertwined dimer formed by N-terminal beta1-strand swapping of two monomers. Comparison with the monomeric NMR structure of Crh revealed a domain swap induced conformational rearrangement of the putative interaction site with the repressor CcpA. The resulting conformation closely resembles that observed for the monomeric Crh homologue HPr, indicating that the Crh dimer is the active form binding to CcpA. An analogous dimer of HPr can be constructed without domain swapping, suggesting that HPr may dimerize upon binding to CcpA. Our data suggest that reversible 3D domain swapping of Crh might be an efficient regulatory mechanism to modulate its activity." citations,entry_citation,5758,231851,1,,entry citation,,,,,,"Solution structure of the hypothetical protein YqgF from Escherichia coli reveals an RNAse H fold",published,journal,J. Biomol. NMR,,27,4,,,,,,,,,,,,,,,,,,,,,,389,392,2003, citations,entry_citation,5759,231875,1,,entry citation,,22627434,12741821,,,"A Model for Effector Activity in a Highly Specific Biological Electron Transfer Complex: The Cytochrome P450cam-Putidaredoxin Couple",published,journal,Biochemistry,,42,19,,,,,,,,,,,,,,,,,,,,,,5649,5656,2003, citations,ref_1,5759,231876,2,,reference citation,,,9542996,,"Nickerson, D.P. & Wong, L.L. (1997) Protein Engineering 10, 1357-1361.",The dimerization of Pseudomonas putida cytochrome P450cam: practical consequences and engineering of a monomeric enzyme.,published,journal,Protein Eng.,Protein engineering,10,12,,0269-2139,,,,,,,,,,,,,,,,,,,,1357,1361,1997,"Cytochrome P450cam dimerizes via the formation of an intermolecular disulfide bond, complicating the storage and handling of the enzyme, particularly at higher concentrations. The dimeric enzyme is 14% less active than the monomer and forms at a slow but significant rate even at 4 degrees C [k = 1.09 x 10(-3) mM(-1) h(-1)]. To eliminate any ambiguity introduced by dimer formation and to simplify handling and storage of the enzyme, site-directed mutagenesis was used to identify C334 as the single cysteine residue responsible for the formation of the disulfide linkage and to engineer a monomeric enzyme by substituting an alanine in its place. The C334A mutant is identical with the wild-type P450cam monomer in terms of optical spectra, camphor binding and turnover activity, but shows no evidence of dimerization and aggregation even at millimolar concentrations. Preliminary 1H NMR investigations also indicate a significant improvement in the quality of spectra obtained with this mutant. (C334A)P450cam is therefore proposed as an alternative to the wild-type enzyme-a base mutant otherwise identical with the wild-type but with improved handling characteristics." citations,entry_citation,5760,231892,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C, and 15N backbone assignment of the first two Ig domains Z1Z2 of the giant muscle protein titin",published,journal,J. Biomol. NMR,,27,3,,,,,,,,,,,,,,,,,,,,,,283,284,2003, citations,ref_1,5760,231893,2,,reference citation,,,8589602,,"Wishart DS, Bigam CG, Yao J, Abildgaard F, Dyson HJ, Oldfield E, Markley JL, Sykes BD. 1H, 13C and 15N chemical shift referencing in biomolecular NMR. J Biomol NMR. 1995 Sep;6(2):135-40.","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,5761,231911,1,,entry citation,,,,,,Characterization of a gamma-adaptin ear-binding motif in enthoprotin,published,journal,FEBS Lett.,,555,3,,,,,,,,,,,,,,,,,,,,,,437,442,2003, citations,entry_citation,5762,231933,1,,entry citation,,,14725761,,,"A Closed Binding Pocket and Global Destabilization Modify the Binding Properties of an Alternatively Spliced Form of the Second PDZ Domain of PTP-BL",published,journal,"Structure (Cambridge, MA, U. S.)",,12,1,,,,,,,,,,,,,,,,,,,,,,11,20,2004, citations,entry_citation,5763,231954,1,,entry citation,,,15213438,,,"Letter to the editor: Solution structure of the hypothetical protein SAV1595 from Staphylococcus aureus, a Putative RNA Binding Protein",published,journal,J. Biomol. NMR,,29,3,,,,,,,,,,,,,,,,,,,,,,391,394,2004, citations,entry_citation,5764,231973,1,,entry citation,,,12809490,,,"Structure of the Nuclear Factor ALY: Insights into Post-transcriptional Regulatory and mRNA Nuclear Export Processes",published,journal,Biochemistry,,42,24,,,,,,,,,,,,,,,,,,,,,,7348,7357,2003, citations,entry_citation,5765,232013,1,,entry citation,,22666530,12782289,,,"NMR Studies of the Fifth Transmembrane Segment of Sarcoplasmic Reticulum Ca2+-ATPase Reveals a Hinge Close to the Ca2+-Ligating Residues",published,journal,FEBS Lett.,,544,1-3,,,,,,,,,,,,,,,,,,,,,,50,56,2003, citations,entry_citation,5766,232026,1,,entry citation,,,12911298,,,Solution Structure of the Lyase Domain of Human DNA Polymerase Lambda,published,journal,Biochemistry,,42,32,,,,,,,,,,,,,,,,,,,,,,9564,9574,2003, citations,entry_citation,5767,232046,1,,entry citation,,,14580196,,,"NMR solution structure of viscotoxin C1 from Viscum album species Coloratum ohwi: toward a structure-function analysis of viscotoxins",published,journal,Biochemistry,,42,43,,,,,,,,,,,,,,,,,,,,,,12503,12510,2003, citations,entry_citation,5769,232090,1,,entry citation,,22770441,12888353,,,"A Core Mutation Affecting the Folding Properties of a Soluble Domain of the ATPase Protein CopA from Bacillus subtilis",published,journal,J. Mol. Biol.,,331,2,,,,,,,,,,,,,,,,,,,,,,473,484,2003, citations,entry_citation,5770,232112,1,,entry citation,,,12684008,,,"Structural basis for simultaneous binding of two carboxy-terminal peptides of plant glutamate decarboxylase to calmodulin",published,journal,J. Mol. Biol.,,328,1,,,,,,,,,,,,,,,,,,,,,,193,204,2003, citations,entry_citation,5771,232143,1,,entry citation,,,,,,"Solution Structure of the disulphide-linked dimer of human intestinal trefoil factor (TFF3): the intermolecular orientation and interactions are markedly different from those of other dimeric trefoil proteins",in preparation,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5772,232156,1,,entry citation,,21911662,11914071,,,"Site-specific Characterization of the Association of Xylooligosaccharides with the CBM13 Lectin-like Xylan Binding Domain from Streptomyces lividans Xylanase 10A by NMR Spectroscopy",published,journal,Biochemistry,,41,13,,,,,,,,,,,,,,,,,,,,,,4255,4263,2002, citations,entry_citation,5773,232179,1,,entry citation,,,12559920,,,Structure of the Intact Stem and Bulge of HIV-1 Psi-RNA Stem Loop SL1,published,journal,J. Mol. Biol.,,326,,,,,,,,,,,,,,,,,,,,,,,529,542,2003, citations,entry_citation,5774,232202,1,,entry citation,,22658057,12773396,,,"Recognition of GU-rich Polyadenylation Regulatory Elements by Human CstF-64 Protein",published,journal,EMBO J.,,22,11,,,,,,,,,,,,,,,,,,,,,,2821,2830,2003, citations,entry_citation,5775,232225,1,,entry citation,,,,,,"NMR Studies of DNA Single Strands and DNA:RNA Hybrids With and Without 1-Propynylation at C5 of Oligopyrimidines",published,journal,J. Am. Chem. Soc.,,125,,,,,,,,,,,,,,,,,,,,,,,6090,6097,2003, citations,entry_citation,5776,232245,1,,entry citation,,,,,,"NMR Studies of DNA Single Strands and DNA:RNA Hybrids With and Without 1-Propynylation at C5 of Oligopyrimidines",published,journal,J. Am. Chem. Soc.,,125,,,,,,,,,,,,,,,,,,,,,,,6090,6097,2003, citations,entry_citation,5777,232267,1,,entry citation,,,,,,"NMR Studies of DNA Single Strands and DNA:RNA Hybrids With and Without 1-Propynylation at C5 of Oligopyrimidines",published,journal,J. Am. Chem. Soc.,,125,,,,,,,,,,,,,,,,,,,,,,,6090,6097,2003, citations,entry_citation,5778,232289,1,,entry citation,,22855807,12975590,,,"Letter to the Editor: 1H, 15N and 13C Chemical Shift Assignment of the Pleckstrin Homology Domain of the Human Protein Kinase B (PKB/Akt)",published,journal,J. Biomol. NMR,,27,3,,,,,,,,,,,,,,,,,,,,,,287,288,2003, citations,reference_1,5778,232290,2,,reference citation,,,1801921,,"Jones PF, Jakubowicz T, Hemmings BA. Molecular cloning of a second form of rac protein kinase. Cell Regul. 1991 Dec;2(12):1001-9.",Molecular cloning of a second form of rac protein kinase.,published,journal,Cell Regul.,Cell regulation,2,12,,1044-2030,,,,,,,,,,,,,,,,,,,,1001,1009,1991,"A novel serine/threonine protein kinase (termed rac-PK) has recently been identified and cloned from cDNA libraries derived from the human cell lines MCF-7 and WI38. A second form of this protein kinase, termed rac protein kinase beta, has been identified from cDNAs derived from the same cell lines. These two closely related forms show 90% homology, although the beta form with a predicted Mr 60,200 has a carboxyl terminal extension of 40 amino acids in comparison to the alpha form. This extension has a high serine content with 11 serine residues in the last 30 amino acids. The beta form of the protein has been shown by both in vitro translation and bacterial expression to be approximately 5000 Da larger than the alpha form. rac protein kinase beta is encoded by a 3.4-kb transcript and the alpha form is encoded by a 3.2-kb mRNA. Using gene-specific probes both transcripts were detected in all cell types analyzed, although levels of expression were different for the two forms. The catalytic domain of rac protein kinase beta shows a high degree of homology to both the protein kinase C and cyclic AMP-dependent protein kinase families, and hence rac protein kinases appear to represent a new subfamily of the second messenger serine/threonine protein kinases." citations,reference_2,5778,232291,3,,reference citation,,,,,"Pons, J.L., Malliavin, T.E. & Delsuc, M.A. (1996) J. Biomol. NMR 8, 445-452.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5779,232306,1,,entry citation,,,14747986,,,"Solution Structure of the highly acidic protein HI1450 from Haemophilus influenzae: a putative double-stranded DNA mimic",published,journal,Proteins,,54,3,,,,,,,,,,,,,,,,,,,,,,375,383,2004, citations,entry_citation,5780,232334,1,,entry citation,,22863540,14499617,,,"The Death-domain Fold of the ASC PYRIN Domain, Presenting a Basis for PYRIN/PYRIN Recognition",published,journal,J. Mol. Biol.,,332,,,,,,,,,,,,,,,,,,,,,,,1155,1163,2003, citations,entry_citation,5781,232354,1,,entry citation,,,12736318,,,"The Solution Structure of a DNA.RNA Duplex Containing 5-Propynyl U and C; Comparison with 5-Me Modifications",published,journal,Nucleic Acids Res.,,31,10,,,,,,,,,,,,,,,,,,,,,,2683,2693,2003, citations,entry_citation,5782,232375,1,,entry citation,,,14660575,,,Properties of some variants of human beta2-microglobulin and amyloidogenesis,published,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_1,5782,232376,2,,reference citation,,,11847272,,"Verdone G, Corazza A, Viglino P, Pettirossi F, Giorgetti S, Mangione P, Andreola A, Stoppini M, Bellotti V, Esposito G. Protein Sci 2002 11(3):487-99 The solution structure of human beta2-microglobulin reveals the prodromes of its amyloid transition.",The solution structure of human beta2-microglobulin reveals the prodromes of its amyloid transition.,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,11,3,,0961-8368,,,,,,,,,,,,,,,,,,,,487,499,2002,"The solution structure of human beta2-microglobulin (beta2-m), the nonpolymorphic component of class I major histocompatibility complex (MHC-I), was determined by (1)H NMR spectroscopy and restrained modeling calculations. Compared to previous structural data obtained from the NMR secondary structure of the isolated protein and the crystal structure of MHC-I, in which the protein is associated to the heavy-chain component, several differences are observed. The most important rearrangements were observed for (1) strands V and VI (loss of the C-terminal and N-terminal end, respectively), (2) interstrand loop V-VI, and (3) strand I, including the N-terminal segment (displacement outward of the molecular core). These modifications can be considered as the prodromes of the amyloid transition. Solvation of the protected regions in MHC-I decreases the tertiary packing by breaking the contiguity of the surface hydrophobic patches at the interface with heavy chain and the nearby region at the surface charge cluster of the C-terminal segment. As a result, the molecule is placed in a state in which even minor charge and solvation changes in response to pH or ionic-strength variations can easily compromise the hydrophobic/hydrophilic balance and trigger the transition into a partially unfolded intermediate that starts with unpairing of strand I and leads to polymerization and precipitation into fibrils or amorphous aggregates. The same mechanism accounts for the partial unfolding and fiber formation subsequent to Cu(2+) binding, which is shown to occur primarily at His 31 and involve partially also His 13, the next available His residue along the partial unfolding pathway." citations,ref_2,5782,232377,3,,reference citation,,,10850793,,"Esposito G, Michelutti R, Verdone G, Viglino P, Hernandez H, Robinson CV, Amoresano A, Dal Piaz F, Monti M, Pucci P, Mangione P, Stoppini M, Merlini G, Ferri G, Bellotti V. Protein Sci 2000 9(5):831-45 Removal of the N-terminal hexapeptide from human beta2-microglobulin facilitates protein aggregation and fibril formation.",Removal of the N-terminal hexapeptide from human beta2-microglobulin facilitates protein aggregation and fibril formation.,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,9,5,,0961-8368,,,,,,,,,,,,,,,,,,,,831,845,2000,"The solution structure and stability of N-terminally truncated beta2-microglobulin (deltaN6beta2-m), the major modification in ex vivo fibrils, have been investigated by a variety of biophysical techniques. The results show that deltaN6beta2-m has a free energy of stabilization that is reduced by 2.5 kcal/mol compared to the intact protein. Hydrogen exchange of a mixture of the truncated and full-length proteins at microM concentrations at pH 6.5 monitored by electrospray mass spectrometry reveals that deltaN6beta2-m is significantly less protected than its wild-type counterpart. Analysis of deltaN6beta2-m by NMR shows that this loss of protection occurs in beta strands I, III, and part of II. At mM concentration gel filtration analysis shows that deltaN6beta2-m forms a series of oligomers, including trimers and tetramers, and NMR analysis indicates that strand V is involved in intermolecular interactions that stabilize this association. The truncated species of beta2-microglobulin was found to have a higher tendency to self-associate than the intact molecule, and unlike wild-type protein, is able to form amyloid fibrils at physiological pH. Limited proteolysis experiments and analysis by mass spectrometry support the conformational modifications identified by NMR and suggest that deltaN6beta2-m could be a key intermediate of a proteolytic pathway of beta2-microglobulin. Overall, the data suggest that removal of the six residues from the N-terminus of beta2-microglobulin has a major effect on the stability of the overall fold. Part of the tertiary structure is preserved substantially by the disulfide bridge between Cys25 and Cys80, but the pairing between beta-strands far removed from this constrain is greatly perturbed." citations,entry_citation,5783,232393,1,,entry citation,,,14660575,,,Properties of some variants of human beta2-microglobulin and amyloidogenesis,published,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_1,5783,232394,2,,reference citation,,,11847272,,"Verdone G, Corazza A, Viglino P, Pettirossi F, Giorgetti S, Mangione P, Andreola A, Stoppini M, Bellotti V, Esposito G. Protein Sci 2002 11(3):487-99 The solution structure of human beta2-microglobulin reveals the prodromes of its amyloid transition.",The solution structure of human beta2-microglobulin reveals the prodromes of its amyloid transition.,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,11,3,,0961-8368,,,,,,,,,,,,,,,,,,,,487,499,2002,"The solution structure of human beta2-microglobulin (beta2-m), the nonpolymorphic component of class I major histocompatibility complex (MHC-I), was determined by (1)H NMR spectroscopy and restrained modeling calculations. Compared to previous structural data obtained from the NMR secondary structure of the isolated protein and the crystal structure of MHC-I, in which the protein is associated to the heavy-chain component, several differences are observed. The most important rearrangements were observed for (1) strands V and VI (loss of the C-terminal and N-terminal end, respectively), (2) interstrand loop V-VI, and (3) strand I, including the N-terminal segment (displacement outward of the molecular core). These modifications can be considered as the prodromes of the amyloid transition. Solvation of the protected regions in MHC-I decreases the tertiary packing by breaking the contiguity of the surface hydrophobic patches at the interface with heavy chain and the nearby region at the surface charge cluster of the C-terminal segment. As a result, the molecule is placed in a state in which even minor charge and solvation changes in response to pH or ionic-strength variations can easily compromise the hydrophobic/hydrophilic balance and trigger the transition into a partially unfolded intermediate that starts with unpairing of strand I and leads to polymerization and precipitation into fibrils or amorphous aggregates. The same mechanism accounts for the partial unfolding and fiber formation subsequent to Cu(2+) binding, which is shown to occur primarily at His 31 and involve partially also His 13, the next available His residue along the partial unfolding pathway." citations,ref_2,5783,232395,3,,reference citation,,,10850793,,"Esposito G, Michelutti R, Verdone G, Viglino P, Hernandez H, Robinson CV, Amoresano A, Dal Piaz F, Monti M, Pucci P, Mangione P, Stoppini M, Merlini G, Ferri G, Bellotti V. Protein Sci 2000 9(5):831-45 Removal of the N-terminal hexapeptide from human beta2-microglobulin facilitates protein aggregation and fibril formation.",Removal of the N-terminal hexapeptide from human beta2-microglobulin facilitates protein aggregation and fibril formation.,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,9,5,,0961-8368,,,,,,,,,,,,,,,,,,,,831,845,2000,"The solution structure and stability of N-terminally truncated beta2-microglobulin (deltaN6beta2-m), the major modification in ex vivo fibrils, have been investigated by a variety of biophysical techniques. The results show that deltaN6beta2-m has a free energy of stabilization that is reduced by 2.5 kcal/mol compared to the intact protein. Hydrogen exchange of a mixture of the truncated and full-length proteins at microM concentrations at pH 6.5 monitored by electrospray mass spectrometry reveals that deltaN6beta2-m is significantly less protected than its wild-type counterpart. Analysis of deltaN6beta2-m by NMR shows that this loss of protection occurs in beta strands I, III, and part of II. At mM concentration gel filtration analysis shows that deltaN6beta2-m forms a series of oligomers, including trimers and tetramers, and NMR analysis indicates that strand V is involved in intermolecular interactions that stabilize this association. The truncated species of beta2-microglobulin was found to have a higher tendency to self-associate than the intact molecule, and unlike wild-type protein, is able to form amyloid fibrils at physiological pH. Limited proteolysis experiments and analysis by mass spectrometry support the conformational modifications identified by NMR and suggest that deltaN6beta2-m could be a key intermediate of a proteolytic pathway of beta2-microglobulin. Overall, the data suggest that removal of the six residues from the N-terminus of beta2-microglobulin has a major effect on the stability of the overall fold. Part of the tertiary structure is preserved substantially by the disulfide bridge between Cys25 and Cys80, but the pairing between beta-strands far removed from this constrain is greatly perturbed." citations,entry_citation,5784,232409,1,,entry citation,,,14660575,,,Properties of some variants of human beta2-microglobulin and amyloidogenesis,published,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_1,5784,232410,2,,reference citation,,,11847272,,"Verdone G, Corazza A, Viglino P, Pettirossi F, Giorgetti S, Mangione P, Andreola A, Stoppini M, Bellotti V, Esposito G. Protein Sci 2002 11(3):487-99 The solution structure of human beta2-microglobulin reveals the prodromes of its amyloid transition.",The solution structure of human beta2-microglobulin reveals the prodromes of its amyloid transition.,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,11,3,,0961-8368,,,,,,,,,,,,,,,,,,,,487,499,2002,"The solution structure of human beta2-microglobulin (beta2-m), the nonpolymorphic component of class I major histocompatibility complex (MHC-I), was determined by (1)H NMR spectroscopy and restrained modeling calculations. Compared to previous structural data obtained from the NMR secondary structure of the isolated protein and the crystal structure of MHC-I, in which the protein is associated to the heavy-chain component, several differences are observed. The most important rearrangements were observed for (1) strands V and VI (loss of the C-terminal and N-terminal end, respectively), (2) interstrand loop V-VI, and (3) strand I, including the N-terminal segment (displacement outward of the molecular core). These modifications can be considered as the prodromes of the amyloid transition. Solvation of the protected regions in MHC-I decreases the tertiary packing by breaking the contiguity of the surface hydrophobic patches at the interface with heavy chain and the nearby region at the surface charge cluster of the C-terminal segment. As a result, the molecule is placed in a state in which even minor charge and solvation changes in response to pH or ionic-strength variations can easily compromise the hydrophobic/hydrophilic balance and trigger the transition into a partially unfolded intermediate that starts with unpairing of strand I and leads to polymerization and precipitation into fibrils or amorphous aggregates. The same mechanism accounts for the partial unfolding and fiber formation subsequent to Cu(2+) binding, which is shown to occur primarily at His 31 and involve partially also His 13, the next available His residue along the partial unfolding pathway." citations,ref_2,5784,232411,3,,reference citation,,,10850793,,"Esposito G, Michelutti R, Verdone G, Viglino P, Hernandez H, Robinson CV, Amoresano A, Dal Piaz F, Monti M, Pucci P, Mangione P, Stoppini M, Merlini G, Ferri G, Bellotti V. Protein Sci 2000 9(5):831-45 Removal of the N-terminal hexapeptide from human beta2-microglobulin facilitates protein aggregation and fibril formation.",Removal of the N-terminal hexapeptide from human beta2-microglobulin facilitates protein aggregation and fibril formation.,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,9,5,,0961-8368,,,,,,,,,,,,,,,,,,,,831,845,2000,"The solution structure and stability of N-terminally truncated beta2-microglobulin (deltaN6beta2-m), the major modification in ex vivo fibrils, have been investigated by a variety of biophysical techniques. The results show that deltaN6beta2-m has a free energy of stabilization that is reduced by 2.5 kcal/mol compared to the intact protein. Hydrogen exchange of a mixture of the truncated and full-length proteins at microM concentrations at pH 6.5 monitored by electrospray mass spectrometry reveals that deltaN6beta2-m is significantly less protected than its wild-type counterpart. Analysis of deltaN6beta2-m by NMR shows that this loss of protection occurs in beta strands I, III, and part of II. At mM concentration gel filtration analysis shows that deltaN6beta2-m forms a series of oligomers, including trimers and tetramers, and NMR analysis indicates that strand V is involved in intermolecular interactions that stabilize this association. The truncated species of beta2-microglobulin was found to have a higher tendency to self-associate than the intact molecule, and unlike wild-type protein, is able to form amyloid fibrils at physiological pH. Limited proteolysis experiments and analysis by mass spectrometry support the conformational modifications identified by NMR and suggest that deltaN6beta2-m could be a key intermediate of a proteolytic pathway of beta2-microglobulin. Overall, the data suggest that removal of the six residues from the N-terminus of beta2-microglobulin has a major effect on the stability of the overall fold. Part of the tertiary structure is preserved substantially by the disulfide bridge between Cys25 and Cys80, but the pairing between beta-strands far removed from this constrain is greatly perturbed." citations,entry_citation,5785,232425,1,,entry citation,,22718511,12834347,,,"Global Orientation of Bound MMP-3 and N-TIMP-1 in Solution via Residual Dipolar Couplings",published,journal,Biochemistry,,42,26,,,,,,,,,,,,,,,,,,,,,,7950,7958,2003,"Most of the backbone assignments and nearly 80% of the side chain assignments of MMP-3 when in complex with N-TIMP-1." citations,ref_1,5785,232426,2,,reference citation,,,9657677,,"Arumugam S, Hemme CL, Yoshida N, Suzuki K, Nagase H, Berjanskii M, Wu B, Van Doren SR. TIMP-1 contact sites and perturbations of stromelysin 1 mapped by NMR and a paramagnetic surface probe. Biochemistry. 1998 Jul 7;37(27):9650-7.",TIMP-1 contact sites and perturbations of stromelysin 1 mapped by NMR and a paramagnetic surface probe.,published,journal,Biochemistry,Biochemistry,37,27,,0006-2960,,,,,,,,,,,,,,,,,,,,9650,9657,1998,"Surfaces of the 173 residue catalytic domain of human matrix metalloproteinase 3 (MMP-3(DeltaC)) affected by binding of the N-terminal, 126 residue inhibitory domain of human TIMP-1 (N-TIMP-1) have been investigated using an amide-directed, NMR-based approach. The interface was mapped by a novel method that compares amide proton line broadening by paramagnetic Gd-EDTA in the presence and absence of the binding partner. The results are consistent with the X-ray model of the complex of MMP-3(DeltaC) with TIMP-1 (Gomis et al. (1997) Nature 389, 77-81). Residues Tyr155, Asn162, Val163, Leu164, His166, Ala167, Ala169, and Phe210 of MMP-3(DeltaC) are protected from broadening by the Gd-EDTA probe by binding to N-TIMP-1. N-TIMP-1-induced exposure of backbone amides of Asp238, Asn240, Gly241, and Ser244 of helix C of MMP-3(DeltaC) to Gd-EDTA confirms that the displacement of the N-terminus of MMP-3(DeltaC) occurs not only in the crystal but also in solution. These results validate comparative paramagnetic surface probing as a means of mapping protein-protein interfaces. Novel N-TIMP-1-dependent changes in hydrogen bonding near the active site of MMP-3(DeltaC) are reported. N-TIMP-1 binding causes the amide of Tyr223 of MMP-3(DeltaC) bound by N-TIMP-1 to exchange with water rapidly, implying a lack of the hydrogen bond observed in the crystal structure. The backbone amide proton of Asn162 becomes protected from rapid exchange upon forming a complex with N-TIMP-1 and could form a hydrogen bond to N-TIMP-1. N-TIMP-1 binding dramatically increases the rate of amide hydrogen exchange of Asp177 of the fifth beta strand of MMP-3(DeltaC), disrupting its otherwise stable hydrogen bond." citations,entry_citation,5786,232447,1,,entry citation,,,14739643,,,"Letter to the Editor: 1H, 15N and 13C resonance assignments for the N-cadherin prodomain",published,journal,J. Biomol. NMR,,28,1,,,,,,,,,,,,,,,,,,,,,,87,88,2004, citations,entry_citation,5787,232467,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N resonance assignments and secondary structure of the cytotoxic protein RNase 3 from oocytes of bullfrog Rana catesbeiana",published,journal,J. Biomol. NMR,,27,3,,,,,,,,,,,,,,,,,,,,,,289,290,2003, citations,entry_citation,5788,232488,1,,entry citation,,22708832,12778114,,,"Structural Basis for Negative Regulation of Hypoxia-inducible Factor-1alpha by CITED2",published,journal,Nat. Struct. Biol.,,10,7,,,,,,,,,,,,,,,,,,,,,,504,512,2003, citations,ref_1,5788,232489,2,,reference citation,,,11959990,,"Freedman SJ, Sun ZY, Poy F, Kung AL, Livingston DM, Wagner G, Eck MJ. Proc Natl Acad Sci U S A. 2002 Apr 16;99(8):5367-72.",Structural basis for recruitment of CBP/p300 by hypoxia-inducible factor-1 alpha.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,99,8,,0027-8424,,,,,,,,,,,,,,,,,,,,5367,5372,2002,"Adaptation to hypoxia is mediated by transactivation of hypoxia-responsive genes by hypoxia-inducible factor-1 (HIF-1) in complex with the CBP and p300 transcriptional coactivators. We report the solution structure of the cysteine/histidine-rich 1 (CH1) domain of p300 bound to the C-terminal transactivation domain of HIF-1 alpha. CH1 has a triangular geometry composed of four alpha-helices with three intervening Zn(2+)-coordinating centers. CH1 serves as a scaffold for folding of the HIF-1 alpha C-terminal transactivation domain, which forms a vise-like clamp on the CH1 domain that is stabilized by extensive hydrophobic and polar interactions. The structure reveals the mechanism of specific recognition of p300 by HIF-1 alpha, and shows how HIF-1 alpha transactivation is regulated by asparagine hydroxylation." citations,entry_citation,5789,232519,1,,entry citation,,22874491,14512741,,,"Letter to the Editor: 1H,15N, and 13C Chemical Shift Assignments of the Escherichia coli Nitrogen Regulatory Phosphocarrier IIA(Ntr)",published,journal,J. Biomol. NMR,,27,4,,,,,,,,,,,,,,,,,,,,,,401,402,2003, citations,entry_citation,5790,232546,1,,entry citation,,,14997575,,,"NMR structure of the hypothetical protein AQ-1857 encoded by the Y157 gene from Aquifex aeolicus reveals a novel protein fold.",published,journal,Proteins,,54,4,,,,,,,,,,,,,,,,,,,,,,794,796,2004, citations,entry_citation,5791,232572,1,,entry citation,,,15256668,,,"Structure and flexibility adaptation in nonspecific and specific protein-DNA complexes",published,journal,Science,,305,5682,,,,,,,,,,,,,,,,,,,,,,386,389,2004, citations,entry_citation,5792,232593,1,,entry citation,,22874492,14512742,,,"Letter to the Editor: NMR assignment of the 1H, 15N and 13C resonances of E. coli frataxin orthologue, CyaY",published,journal,J. Biomol. NMR,,27,4,,,,,,,,,,,,,,,,,,,,,,403,404,2003, citations,ref-1,5792,232594,2,,reference citation,,,,,"THE PROGRAM XEASY FOR COMPUTER-SUPPORTED NMR SPECTRAL-ANALYSIS OF BIOLOGICAL MACROMOLECULES Bartels C, XIA TH, BILLETER M, GUNTERT P, WUTHRICH K Journal OF BIOMOLECULAR NMR 6 (1): 1-10 JUL 1995.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref-2,5792,232595,3,,reference citation,,,8520220,,"NMRPipe: a multidimensional spectral processing system based on UNIX pipes. Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. J Biomol NMR 1995 Nov;6(3):277-93.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,entry_citation,5793,232614,1,,entry citation,,,,,,"Letter to the Editor: Backbone 1H, 13C, 15N assignments of a 42 kDa RecR homodimer",published,journal,J. Biomol. NMR,,28,2,,,,,,,,,,,,,,,,,,,,,,199,200,2004, citations,entry_citation,5794,232636,1,,entry citation,,22874493,14512743,,,"Letter to the Editor: Sequence-specific 1H, 13C and 15N resonance assignments of the SH3-SH2 domain pair of the human tyrosine kinase Lck",published,journal,J. Biomol. NMR,,27,4,,,,,,,,,,,,,,,,,,,,,,405,406,2003, citations,entry_citation,5795,232662,1,,entry citation,,,15147184,,,"Solution structure of Eucommia antifungal peptide: a novel structural model distinct with a five-disulfide motif.",published,journal,Biochemistry,,43,20,,,,,,,,,,,,,,,,,,,,,,6005,6012,2004, citations,entry_citation,5796,232682,1,,entry citation,,,15185964,,,"Solution Structure of a Putative Ribosome Binding Protein from Mycoplasma pneumoniae and Comparison to a Distant Homolog",published,journal,J. Struct. Funct. Genomics,,4,4,,,,,,,,,,,,,,,,,,,,,,235,243,2003, citations,entry_citation,5797,232709,1,,entry citation,,,,,,"Letter to the Editor: Solution structure of the hypothetical protein TA1414 from Thermoplasma acidophilum",published,journal,J. Biomol. NMR,,28,1,,,,,,,,,,,,,,,,,,,,,,81,84,2004, citations,entry_citation,5798,232722,1,,entry citation,,,,,,"Solution structure of Protein yrbA from Escherichia Coli: Northeast Structural Genomics Consortium target ER115",submitted,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5799,232744,1,,entry citation,,,14752257,,,Protein Signal Assignments using Specific Labeling and Cell-free Synthesis,published,journal,J. Biomol. NMR,,28,3,,,,,,,,,,,,,,,,,,,,,,235,247,2004, citations,entry_citation,58,232770,1,,entry citation,,,,,"van de Ven, F. J. M., Hilbers, C. W., ""Residue-specific Assignments of Resonances in the 1H Nuclear Magnetic Resonance Spectrum of Ribosomal Protein E-L30 by Systematic Application of Two-dimensional Fourier Transform Nuclear Magnetic Resonance Methods,"" J. Mol. Biol. 192, 389-417 (1986).","Residue-specific Assignments of Resonances in the 1H Nuclear Magnetic Resonance Spectrum of Ribosomal Protein E-L30 by Systematic Application of Two-dimensional Fourier Transform Nuclear Magnetic Resonance Methods",published,journal,J. Mol. Biol.,,192,,,,,,,,,,,,,,,,,,,,,,,389,417,1986, citations,entry_citation,5800,232783,1,,entry citation,,,14755165,,,"Letter to the Editor: Sequence-specific 1H, 13C, 15N resonance assignments and secondary structure of the carboxyterminal domain of the E.coli Transcription factor NusA",published,journal,J. Biomol. NMR,,28,2,,,,,,,,,,,,,,,,,,,,,,193,194,2004, citations,entry_citation,5810,233018,1,,entry citation,,,14621990,,,"A Novel Class of Cysteine Protease Inhibitors: Solution Structure of Staphostatin A from Staphylococcus aureus",published,journal,Biochemistry,,42,46,,,,,,,,,,,,,,,,,,,,,,13449,13456,2003, citations,ref_1,5810,233019,2,,reference citation,,,12207024,,"Massimi I, Park E, Rice K, Muller-Esterl W, Sauder D, McGavin MJ. J Biol Chem. 41770-41777 (2002).",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_1,5800,232784,2,,reference citation,,,11430821,,"Worbs et. al. An extended RNA binding surface through arrayed S1 and KH domains in transcription factor NusA. Mol Cell. 2001 Jun;7(6):1177-89.",An extended RNA binding surface through arrayed S1 and KH domains in transcription factor NusA.,published,journal,Mol. Cell,Molecular cell,7,6,,1097-2765,,,,,,,,,,,,,,,,,,,,1177,1189,2001,"The crystal structure of Thermotoga maritima NusA, a transcription factor involved in pausing, termination, and antitermination processes, reveals a four-domain, rod-shaped molecule. An N-terminal alpha/beta portion, a five-stranded beta-barrel (S1 domain), and two K-homology (KH) modules create a continuous spine of positive electrostatic potential, suitable for nonspecific mRNA attraction. Homology models suggest how, in addition, specific mRNA regulatory sequences can be recognized by the S1 and KH motifs. An arrangement of multiple S1 and KH domains mediated by highly conserved residues is seen, creating an extended RNA binding surface, a paradigm for other proteins with similar domain arrays. Structural and mutational analyses indicate that the motifs cooperate, modulating strength and specificity of RNA binding." citations,ref_2,5800,232785,3,,reference citation,,,11743725,,"Gopal et. al. Crystal structure of the transcription elongation/anti-termination factor NusA from Mycobacterium tuberculosis at 1.7 A resolution. J Mol Biol. 2001 Dec 14;314(5):1087-95.",Crystal structure of the transcription elongation/anti-termination factor NusA from Mycobacterium tuberculosis at 1.7 A resolution.,published,journal,J. Mol. Biol.,Journal of molecular biology,314,5,,0022-2836,,,,,,,,,,,,,,,,,,,,1087,1095,2001,"Mycobacterium tuberculosis is the cause of tuberculosis in humans, a disease that affects over a one-third of the world's population. This slow-growing pathogen has only one ribosomal RNA operon, thus making its transcriptional apparatus a fundamentally interesting target for drug discovery. NusA binds to RNA polymerase and modulates several of the ribosomal RNA transcriptional processes. Here, we report the crystal structure of NusA, and reveal that the molecule consists of four domains. They are organised as two distinct entities. The N-terminal domain (residues 1 to 99) that resembles the B chain of the Rad50cd ATP binding cassette-ATPase (ABC-ATPase) and a C-terminal module (residues 108 to 329) consisting of a ribosomal S1 protein domain followed by two K homology domains. The S1 and KH domains are tightly integrated together to form an extensive RNA-binding structure, but are flexibly tethered to the N-terminal domain. The molecule's surfaces and architecture provide insights into RNA and polymerase interactions and the mechanism of pause site discrimination. They also allow us to rationalize certain termination-defective and cold shock-sensitive mutations in the nusA gene that have been studied in Escherichia coli." citations,ref_3,5800,232786,4,,reference citation,,,11040219,,"Mah et. al. The alpha subunit of E. coli RNA polymerase activates RNA binding by NusA. Genes Dev. 2000 Oct 15;14(20):2664-75.",The alpha subunit of E. coli RNA polymerase activates RNA binding by NusA.,published,journal,Genes Dev.,Genes & development,14,20,,0890-9369,,,,,,,,,,,,,,,,,,,,2664,2675,2000,"The Escherichia coli NusA protein modulates pausing, termination, and antitermination by associating with the transcribing RNA polymerase core enzyme. NusA can be covalently cross-linked to nascent RNA within a transcription complex, but does not bind RNA on its own. We have found that deletion of the 79 carboxy-terminal amino acids of the 495-amino-acid NusA protein allows NusA to bind RNA in gel mobility shift assays. The carboxy-terminal domain (CTD) of the alpha subunit of RNA polymerase, as well as the bacteriophage lambda N gene antiterminator protein, bind to carboxy-terminal regions of NusA and enable full-length NusA to bind RNA. Binding of NusA to RNA in the presence of alpha or N involves an amino-terminal S1 homology region that is otherwise inactive in full-length NusA. The interaction of the alpha-CTD with full-length NusA stimulates termination. N may prevent termination by inducing NusA to interact with N utilization (nut) site RNA rather than RNA near the 3' end of the nascent transcript. Sequence analysis showed that the alpha-CTD contains a modified helix-hairpin-helix motif (HhH), which is also conserved in the carboxy-terminal regions of some eubacterial NusA proteins. These HhH motifs may mediate protein-protein interactions in NusA and the alpha-CTD." citations,entry_citation,5801,232811,1,,entry citation,,22877075,12869572,,,"Structural Analysis of an Epidermal Growth Factor/Transforming Growth Factor-alpha Chimera with Unique ErbB Binding Specificity specificity",published,journal,J. Biol. Chem.,,278,40,,,,,,,,,,,,,,,,,,,,,,39114,39123,2003, citations,entry_citation,5802,232836,1,,entry citation,,,15981997,,,"Mitochondrial and microsomal ferric b5 cytochromes exhibit divergent conformational plasticity in the context of a common fold",published,journal,Biochemistry,,44,26,,,,,,,,,,,,,,,,,,,,,,9308,9319,2005, citations,entry_citation,5803,232862,1,,entry citation,,,15157100,,,"NMR characterization of three-disulfide variants of lysozyme, C64A/C80A, C76A/C94A, and C30A/C115A--a marginally stable state in folded proteins.",published,journal,Biochemistry,,43,21,,,,,,,,,,,,,,,,,,,,,,6663,6669,2004, citations,ref_1,5803,232863,2,,reference citation,,,10395829,,"van den Berg B, Chung EW, Robinson CV, Dobson CM. Characterisation of the dominant oxidative folding intermediate of hen lysozyme. J Mol Biol. 1999 Jul 16;290(3):781-96.",Characterisation of the dominant oxidative folding intermediate of hen lysozyme.,published,journal,J. Mol. Biol.,Journal of molecular biology,290,3,,0022-2836,,,,,,,,,,,,,,,,,,,,781,796,1999,"Reduced denatured lysozyme has been oxidised and refolded at pH values close to neutral in an efficient way by dilution from buffers containing 8.0 M urea, and refolding intermediates were separated by reverse-phase HPLC at pH 2. By using peptic digestion in combination with high-resolution Fourier transform ion cyclotron resonance (FT-ICR) mass spectrometry (MS) and tandem MS/MS the dominant intermediate was identified to be des-[76-94]. This species has three of the four native disulphide bonds, but lacks the Cys76-Cys94 disulphide bond which connects the two folding domains in the native protein. Characterisation of des-[76-94] by 2D1H NMR shows that it has a highly native-like structure. This provides an explanation for the accumulation of this species during refolding as direct oxidation to the fully native protein will be restricted by the burial of Cys94 in the protein interior." citations,ref_2,5810,233020,3,,reference citation,,,,,"Rzychon, M., Sabat, A., Kosowska, K., Potampa, J. and Dubin, A. Mol. Microbiol. in press.(2003).",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_3,5810,233021,4,,reference citation,,,,,"Rice, K., Peralta, R., Bast, D., Azavedo, J. and McGavin, M.J. Infect. Immun., 69, (2001)",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_4,5810,233022,5,,reference citation,,,9791183,,"Coulter, S.N., Schwan, W.R., Ng, E.Y., Langhorne, M.H., Ritchie, H.D., Westbrock-Wadman, S., Hufnagle, W.O., Folger, K.R., Bayer, A.S. Stover, C.K. Mol. Microbiol., 30, (1998)",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,JBNMR_citation,5810,233023,6,,reference citation,,,,,,"Letter to the Editor: 1H, 15N and 13C NMR Resonance Assignments of Staphostatin A, a Specific Staphylococcus aureus Cysteine Proteinase Inhibitor",,journal,J. Biomol. NMR,,28,3,,,,,,,,,,,,,,,,,,,,,,295,296,2004, citations,entry_citation,6087,239302,1,,entry citation,,,20667830,,,NMR structure and ion channel activity of the p7 protein from hepatitis C virus,published,journal,J. Biol. Chem.,Journal of Biological Chemistry,,,,,,,,,,,,,,,,,,,,,,,,,,2010, citations,ref_2,5803,232864,3,,reference citation,,,11841203,,"Noda Y, Yokota A, Horii D, Tominaga T, Tanisaka Y, Tachibana H, Segawa S. NMR structural study of two-disulfide variant of hen lysozyme: 2SS[6-127, 30-115]--a disulfide intermediate with a partly unfolded structure. Biochemistry. 2002 Feb 19;41(7):2130-9.","NMR structural study of two-disulfide variant of hen lysozyme: 2SS[6-127, 30-115]--a disulfide intermediate with a partly unfolded structure.",published,journal,Biochemistry,Biochemistry,41,7,,0006-2960,,,,,,,,,,,,,,,,,,,,2130,2139,2002,"The 15N-labeled recombinant hen lysozyme and two species of two-disulfide variants, denoted as 2SS[6-127, 30-115] and 2SS[64-80, 76-94], were studied by means of NMR spectroscopy. The former variant contains two disulfide bridges in the alpha-domain, while the latter has one disulfide bridge in the beta-domain and the other one at the interface between two domains. Resonance assignments were performed using 3D TOCSY-HSQC and NOESY-HSQC spectra. The 15N-1H-HSQC spectrum of 2SS[6-127, 30-115] was similar to that of recombinant lysozyme as a whole, although a number of cross-peaks disappeared. On the other hand, the HSQC spectrum of 2SS[64-80, 76-94] was characteristic of unfolded proteins. The structure of 2SS[6-127, 30-115] was thoroughly examined on the basis of NOE contacts determined by NMR spectroscopy. The structure of the alpha-domain was quite similar to that of authentic lysozyme, while the beta-domain was largely unstructured. However, NMR data clearly demonstrated that some residual structures exist in the beta-domain. The beta1 and beta2 strands were maintained stably as an antiparallel beta-sheet. In addition, the residues 55 and 56 were located in the vicinity of the end of the B-helix. Further, the C-helix was properly set with side-chains of I88, V92, K96, and V99 facing toward the hydrophobic core in the alpha-domain. These residual structures inherent in the amino acid sequence were evaluated concerning the folding process of lysozyme. Our experiments imply that the establishment of the backbone conformation ranging from residues 76-99 plays a key role in attaining the cooperativity between two domains required for the folding transition." citations,entry_citation,5804,232885,1,,entry citation,,,15157100,,,"NMR characterization of three-disulfide variants of lysozyme, C64A/C80A, C76A/C94A, and C30A/C115A--a marginally stable state in folded proteins.",published,journal,Biochemistry,,43,21,,,,,,,,,,,,,,,,,,,,,,6663,6669,2004, citations,ref_1,5804,232886,2,,reference citation,,,10395829,,"van den Berg B, Chung EW, Robinson CV, Dobson CM. Characterisation of the dominant oxidative folding intermediate of hen lysozyme. J Mol Biol. 1999 Jul 16;290(3):781-96.",Characterisation of the dominant oxidative folding intermediate of hen lysozyme.,published,journal,J. Mol. Biol.,Journal of molecular biology,290,3,,0022-2836,,,,,,,,,,,,,,,,,,,,781,796,1999,"Reduced denatured lysozyme has been oxidised and refolded at pH values close to neutral in an efficient way by dilution from buffers containing 8.0 M urea, and refolding intermediates were separated by reverse-phase HPLC at pH 2. By using peptic digestion in combination with high-resolution Fourier transform ion cyclotron resonance (FT-ICR) mass spectrometry (MS) and tandem MS/MS the dominant intermediate was identified to be des-[76-94]. This species has three of the four native disulphide bonds, but lacks the Cys76-Cys94 disulphide bond which connects the two folding domains in the native protein. Characterisation of des-[76-94] by 2D1H NMR shows that it has a highly native-like structure. This provides an explanation for the accumulation of this species during refolding as direct oxidation to the fully native protein will be restricted by the burial of Cys94 in the protein interior." citations,ref_2,5804,232887,3,,reference citation,,,11841203,,"Noda Y, Yokota A, Horii D, Tominaga T, Tanisaka Y, Tachibana H, Segawa S. NMR structural study of two-disulfide variant of hen lysozyme: 2SS[6-127, 30-115]--a disulfide intermediate with a partly unfolded structure. Biochemistry. 2002 Feb 19;41(7):2130-9.","NMR structural study of two-disulfide variant of hen lysozyme: 2SS[6-127, 30-115]--a disulfide intermediate with a partly unfolded structure.",published,journal,Biochemistry,Biochemistry,41,7,,0006-2960,,,,,,,,,,,,,,,,,,,,2130,2139,2002,"The 15N-labeled recombinant hen lysozyme and two species of two-disulfide variants, denoted as 2SS[6-127, 30-115] and 2SS[64-80, 76-94], were studied by means of NMR spectroscopy. The former variant contains two disulfide bridges in the alpha-domain, while the latter has one disulfide bridge in the beta-domain and the other one at the interface between two domains. Resonance assignments were performed using 3D TOCSY-HSQC and NOESY-HSQC spectra. The 15N-1H-HSQC spectrum of 2SS[6-127, 30-115] was similar to that of recombinant lysozyme as a whole, although a number of cross-peaks disappeared. On the other hand, the HSQC spectrum of 2SS[64-80, 76-94] was characteristic of unfolded proteins. The structure of 2SS[6-127, 30-115] was thoroughly examined on the basis of NOE contacts determined by NMR spectroscopy. The structure of the alpha-domain was quite similar to that of authentic lysozyme, while the beta-domain was largely unstructured. However, NMR data clearly demonstrated that some residual structures exist in the beta-domain. The beta1 and beta2 strands were maintained stably as an antiparallel beta-sheet. In addition, the residues 55 and 56 were located in the vicinity of the end of the B-helix. Further, the C-helix was properly set with side-chains of I88, V92, K96, and V99 facing toward the hydrophobic core in the alpha-domain. These residual structures inherent in the amino acid sequence were evaluated concerning the folding process of lysozyme. Our experiments imply that the establishment of the backbone conformation ranging from residues 76-99 plays a key role in attaining the cooperativity between two domains required for the folding transition." citations,entry_citation,5805,232908,1,,entry citation,,,14622001,,,NMR Structure of an Archaeal Homologue of RNase P Protein Rpp29,published,journal,Biochemistry,,42,46,,,,,,,,,,,,,,,,,,,,,,13541,13550,2003, citations,entry_citation,5806,232934,1,,entry citation,,22853153,12842879,,,"Solution Structure of the Recombinant Penaeidin-3, a Shrimp Antimicrobial Peptide",published,journal,J. Biol. Chem.,,278,38,,,,,,,,,,,,,,,,,,,,,,36859,36867,2003, citations,entry_citation,5807,232954,1,,entry citation,,,14739644,,,"Lette to the Editor: Assignments of 1H and 15N resonances of the bacteriophage lambda capsid stabilizing protein gpD",published,journal,J. Biomol. NMR,,28,1,,,,,,,,,,,,,,,,,,,,,,89,90,2004, citations,ref_1,5807,232955,2,,reference citation,,,10700283,,"Yang F, Forrer P, Dauter Z, Conway JF, Cheng N, Cerritelli ME, Steven AC, Pluckthun A, Wlodawer A. Nat. Struct. Biol. 7, 230-237(2000).",Novel fold and capsid-binding properties of the lambda-phage display platform protein gpD.,published,journal,Nat. Struct. Biol.,Nature structural biology,7,3,,1072-8368,,,,,,,,,,,,,,,,,,,,230,237,2000,"The crystal structure of gpD, the capsid-stabilizing protein of bacteriophage lambda, was solved at 1.1 A resolution. Data were obtained from twinned crystals in space group P21 and refined with anisotropic temperature factors to an R-factor of 0.098 (Rfree = 0. 132). GpD (109 residues) has a novel fold with an unusually low content of regular secondary structure. Noncrystallographic trimers with substantial intersubunit interfaces were observed. The C-termini are well ordered and located on one side of the trimer, relatively far from its three-fold axis. The N-termini are disordered up to Ser 15, which is close to the three-fold axis and on the same side as the C-termini. A density map of the icosahedral viral capsid at 15 A resolution, obtained by cryo-electron microscopy and image reconstruction, reveals gpD trimers, seemingly indistinguishable from the ones seen in the crystals, at all three-fold sites. The map further reveals that the side of the trimer that binds to the capsid is the side on which both termini reside. Despite this orientation of the gpD trimer, fusion proteins connected by linker peptides to either terminus bind to the capsid, allowing protein and peptide display." citations,entry_citation,5808,232969,1,,entry citation,,,14705930,,,"Extension of the binding motif of the Sin3 Interacting Domain of the mad family proteins",published,journal,Biochemistry,,43,1,,,,,,,,,,,,,,,,,,,,,,46,54,2004, citations,entry_citation,5809,232995,1,,entry citation,,22802787,12922170,,,"Solution 1H NMR Study of the Active Site Molecular Structure and Magnetic Properties of the Cyanomet Complex of the Isolated Alpha-chain from Human Hemoglobin A",published,journal,Biochim. Biophys. Acta,,1650,1-2,,,,,,,,,,,,,,,,,,,,,,59,72,2003, citations,entry_citation,5811,233041,1,,entry citation,,,15269237,,,"Side chain-side chain interactions of arginine with tyrosine and aspartic acid in Arg/Gly/Tyr-rich domains within plant glycine-rich RNA binding proteins",published,journal,J. Biochem.,,136,1,,,,,,,,,,,,,,,,,,,,,,29,37,2004,"quasi-repetitive arginine/glycine/ tyrosine-rich domains within glycine-rich RNA binding protein" citations,entry_citation,5812,233059,1,,entry citation,,,15269237,,,"Side chain-side chain interactions of arginine with tyrosine and aspartic acid in Arg/Gly/Tyr-rich domains within plant glycine-rich RNA binding proteins",published,journal,J. Biochem.,,136,1,,,,,,,,,,,,,,,,,,,,,,29,37,2004,"quasi-repetitive arginine/glycine/ tyrosine-rich domains within glycine-rich RNA binding protein" citations,entry_citation,5813,233073,1,,entry citation,,,14514665,,,"Structural basis for the function of the N terminal domain of the ATPase CopA from Bacillus subtilis",published,journal,J. Biol. Chem.,,278,50,,,,,,,,,,,,,,,,,,,,,,50506,50513,2003, citations,entry_citation,5814,233102,1,,entry citation,,,14755167,,,"Letter to the Editor: The C-terminal domain of Viral IAP associated factor (cVIAF) is a structural homologue of phosducin: Resonance assignments and secondary structure of the C-terminal domain of VIAF",published,journal,J. Biomol. NMR,,28,2,,,,,,,,,,,,,,,,,,,,,,197,198,2004, citations,entry_citation,5815,233132,1,,entry citation,,22656956,12750469,,,"Structure of the Coat Protein in fd Filamentous Bacteriophage Particles Determined by Solid-state NMR Spectroscopy",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,100,11,,,,,,,,,,,,,,,,,,,,,,6458,6463,2003, citations,ref_1,5815,233133,2,,reference citation,,,12750469,,"Zeri AC, Mesleh MF, Nevzorov AA, Opella SJ. Proc Natl Acad Sci U S A. 2003 May 27;100(11)",Structure of the coat protein in fd filamentous bacteriophage particles determined by solid-state NMR spectroscopy.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,100,11,,0027-8424,,,,,,,,,,,,,,,,,,,,6458,6463,2003,"The atomic resolution structure of fd coat protein determined by solid-state NMR spectroscopy of magnetically aligned filamentous bacteriophage particles differs from that previously determined by x-ray fiber diffraction. Most notably, the 50-residue protein is not a single curved helix, but rather is a nearly ideal straight helix between residues 7 and 38, where there is a distinct kink, and then a straight helix with a different orientation between residues 39 and 49. Residues 1-5 have been shown to be mobile and unstructured, and proline 6 terminates the helix. The structure of the coat protein in virus particles, in combination with the structure of the membrane-bound form of the same protein in bilayers, also recently determined by solid-state NMR spectroscopy, provides insight into the viral assembly process. In addition to their roles in molecular biology and biotechnology, the filamentous bacteriophages continue to serve as model systems for the development of experimental methods for determining the structures of proteins in biological supramolecular assemblies. New NMR results include the complete sequential assignment of the two-dimensional polarization inversion spin-exchange at the magic angle spectrum of a uniformly 15N-labeled 50-residue protein in a 1.6 x 107 Da particle in solution, and the calculation of the three-dimensional structure of the protein from orientational restraints with an accuracy equivalent to an rms deviation of approximately 1A." citations,entry_citation,5816,233152,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N backbone resonance assignments of the dimeric yeast peroxiredoxin YLR109w",published,journal,J. Biomol. NMR,,28,1,,,,,,,,,,,,,,,,,,,,,,95,96,2004, citations,ref_1,5816,233153,2,,reference citation,,,10391912,,"Verdoucq L, Vignols F, Jacquot JP, Chartier Y, Meyer Y. In vivo characterization of a thioredoxin h target protein defines a new peroxiredoxin family. J Biol Chem. 1999 Jul 9;274(28):19714-22.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5817,233179,1,,entry citation,,22680620,12795601,,,"Nuclear Magnetic Resonance Structure of a Prototype Lin12-Notch Repeat Module from Human Notch1",published,journal,Biochemistry,,42,23,,,,,,,,,,,,,,,,,,,,,,7061,7067,2003, citations,entry_citation,5818,233201,1,,entry citation,,22721833,12837795,,,"The Solution Structure of YbcJ from Escherichia coli Reveals a Recently Discovered alphaL Motif Involved in RNA Binding",published,journal,J. Bacteriol.,,185,14,,,,,,,,,,,,,,,,,,,,,,4204,4210,2003, citations,entry_citation,5819,233225,1,,entry citation,,,14752263,,,"Letter to the editor: Complete 1H, 15N, and 13C assignment of the soluble domain of the ba3 oxidase subunit II of Thermus thermophilus in the reduced state",published,journal,J. Biomol. NMR,,28,3,,,,,,,,,,,,,,,,,,,,,,297,298,2004, citations,reference_1,5819,233226,2,,reference citation,,,8639488,,"Slutter CE, Sanders D, Wittung P, Malmstrom BG, Aasa R, Richards JH, Gray HB, Fee JA. Water-soluble, recombinant CuA-domain of the cytochrome ba3 subunit II from Thermus thermophilus. Biochemistry. 1996 Mar 19;35(11):3387-95.","Water-soluble, recombinant CuA-domain of the cytochrome ba3 subunit II from Thermus thermophilus.",published,journal,Biochemistry,Biochemistry,35,11,,0006-2960,,,,,,,,,,,,,,,,,,,,3387,3395,1996,"Recently, the genes of cytochrome ba3 from thermus thermophilus [Keightley, J.A., et al. (1995) J. Biol. Chem. 270, 20345-20358], a homolog of the heme-copper oxidase family, have been cloned. We report here expression of a truncated gene, encoding the copper A (CuA) domain of cytochrome ba3, that is regulated by a T7 RNA polymerase promoter in Escherichia coli. The CuA-containing domain is purified in high yields as a water-soluble, thermostable, purple-colored protein. Copper analysis by chemical assay, mass spectrometry, X-ray fluorescence, and EPR spin quantification show that this protein contains two copper ions bound in a mixed-valence state, indicating that the CuA site in cytochrome ba3, is a binuclear center. The absorption spectrum of the CuA site, free of the heme interference in cytochrome ba3, is similar to the spectra of other soluble fragments from the aa3-type oxidase of Parachccus denitrificans [Lappalainen, P., et al. (1993) J. Biol Chem. 268, 26416-26421] and the caa3-type oxidase of Bacillus subtilis [von Wachenfeldt, C. et al. (1994) FEBS Lett. 340, 109-113]. There are intense bands at 480 nm (3100 M(-1) cm(-1)) and 530 nm (3200 M(-1) cm(-1)), a band in the near -IR centered at 790 nm (1900 M(-1) cn(-1)), and a weaker band at 363 nm (1300M(-1) cm(-1)). The visible CD spectrum shows a positive-going band at 460 nm and a negative-going band at 527 nm, the opposite signs of which may result from the binuclear nature of the site. The secondary structure prediction from the far-UV CD spectrum indicates that this domain is predominantly beta-sheet, in agreement with the recent X-ray structure reported for the complete P. denitrificans cytochrome aa3 molecule [Iwata, S., et al. (1995) Nature 376, 660-669] and the engineered, purple CyoA protein [Wilmanns, M., et al. (1996) Proc. Natl Acad. Sci. U.S.A. 92, 11955-11959]. However, the thermostability of the fragment described here (Tm approximately 80 degrees C) and the stable binding of copper over a broad pH range (pH 3-9) suggest this protein may be uniquely suitable for detailed physical-chemical study." citations,entry_citation,5820,233258,1,,entry citation,,22919592,14556746,,,"Tertiary Structure of Thiopurine Methyltransferase from Pseudomonas syringae, a Bacterial Orthologue of a Polymorphic, Drug-metabolizing Enzyme",published,journal,J. Mol. Biol.,,333,3,,,,,,,,,,,,,,,,,,,,,,573,585,2003, citations,entry_citation,5821,233271,1,,entry citation,,,14755166,,,"Letter to the Editor: 1H, 13C and 15N assignments of single-stranded DNA binding domains from the 70 kDa subunit of Human Replication Protein A",published,journal,J. Biomol. NMR,,28,2,,,,,,,,,,,,,,,,,,,,,,195,196,2004, citations,entry_citation,5822,233286,1,,entry citation,,,14755166,,,"Letter to the Editor: 1H, 13C and 15N assignments of single-stranded DNA binding domains from the 70 kDa subunit of Human Replication Protein A",published,journal,J. Biomol. NMR,,28,2,,,,,,,,,,,,,,,,,,,,,,195,196,2004, citations,entry_citation,5823,233311,1,,entry citation,,,14755166,,,"Letter to the Editor: 1H, 13C and 15N assignments of single-stranded DNA binding domains from the 70 kDa subunit of Human Replication Protein A",published,journal,J. Biomol. NMR,,27,2,,,,,,,,,,,,,,,,,,,,,,195,196,2004, citations,entry_citation,5824,233326,1,,entry citation,,,14872133,,,"Letter to the Editor: Sequence-specific 1H, 13C and 15N resonance assignments of the C-terminal domain of KaiA, a circadian clock protein",published,journal,J. Biomol. NMR,,28,4,,,,,,,,,,,,,,,,,,,,,,403,404,2004, citations,entry_citation,5825,233352,1,,entry citation,,,14872133,,,"Letter to the Editor: Sequence-specific 1H, 13C and 15N resonance assignments of the C-terminal domain of KaiA, a circadian clock protein",published,journal,J. Biomol. NMR,,28,4,,,,,,,,,,,,,,,,,,,,,,403,404,2004, citations,entry_citation,5826,233369,1,,entry citation,,,14769802,,,"Structural characterization of the nickel-binding properties of bacillus pasteurii UreE in solution",published,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,2004, citations,entry_citation,5827,233382,1,,entry citation,,22812282,12931009,,,"Backbone and Side-chain Heteronuclear Resonance Assignments and Hyperfine NMR Shifts in Horse Cytochrome c",published,journal,Protein Sci.,,12,9,,,,,,,,,,,,,,,,,,,,,,2104,2108,2003, citations,entry_citation,6264,242729,1,,entry citation,,,15595831,,,"Solution structure of cryptdin-4, a mouse paneth cell alpha-defensin",published,journal,Biochemistry,,43,50,,,,,,,,,,,,,,,,,,,,,,15759,15766,2004, citations,entry_citation,5828,233403,1,,entry citation,,22812282,12931009,,,"Backbone and Side-chain Heteronuclear Resonance Assignments and Hyperfine NMR Shifts in Horse Cytochrome c",published,journal,Protein Sci.,,12,9,,,,,,,,,,,,,,,,,,,,,,2104,2108,2003, citations,entry_citation,5829,233424,1,,entry citation,,22812282,12931009,,,"Backbone and Side-chain Heteronuclear Resonance Assignments and Hyperfine NMR Shifts in Horse Cytochrome c",published,journal,Protein Sci.,,12,9,,,,,,,,,,,,,,,,,,,,,,2104,2108,2003, citations,entry_citation,5830,233441,1,,entry citation,,22812282,12931009,,,"Backbone and Side-chain Heteronuclear Resonance Assignments and Hyperfine NMR Shifts in Horse Cytochrome c",published,journal,Protein Sci.,,12,9,,,,,,,,,,,,,,,,,,,,,,2104,2108,2003, citations,entry_citation,5832,233457,1,,entry citation,,,,,,"Function and solution structure of hainantoxin-III, a potent neuronal TTX-sensitive sodium channel antagonist from Chinese bird spider Selenocosmia hainana",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5833,233472,1,,entry citation,,,14752264,,,"Letter to the Editor: Resonance assignments and topology of the 15N, 13C labelled 23 kDa core domain of Xenopus Mob1",published,journal,J. Biomol. NMR,,28,3,,,,,,,,,,,,,,,,,,,,,,299,300,2004, citations,entry_citation,5834,233487,1,,entry citation,,22770795,12888491,,,Solution Structure of the HIV-1 Frameshift Inducing Stem-loop RNA,published,journal,Nucleic Acids Res.,,31,15,,,,,,,,,,,,,,,,,,,,,,4326,4331,2003, citations,entry_citation,5835,233510,1,,entry citation,,,14645226,,,"Effect of N-terminal and Met23 mutations on the structure and dynamics of onconase",published,journal,J. Biol. Chem.,,279,7,,,,,,,,,,,,,,,,,,,,,,5772,5780,2004, citations,entry_citation,5836,233522,1,,entry citation,,,,,,"Backbone 1H, 13C, 15N chemical shifts and coupling constants of Yersinia pseudotuberculosis-derived mitogen",published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5837,233542,1,,entry citation,,,16687202,,,"Interaction of local anesthetics with a peptide encompassing the IV/S4-S5 linker of the Na+ channel.",published,journal,Biophys. Chem.,,123,1,,,,,,,,,,,,,,,,,,,,,,29,39,2006, citations,entry_citation,5838,233563,1,,entry citation,,,14661952,,,"Structure of the Ca(2+)/S100B/NDR Kinase Peptide Complex: Insights into S100 Target Specificity and Activation of the Kinase",published,journal,Biochemistry,,42,49,,,,,,,,,,,,,,,,,,,,,,14416,14426,2003, citations,entry_citation,5839,233589,1,,entry citation,,22855801,12975584,,,"Characterization of the Overall and Local Dynamics of a Protein with Intermediate Rotational Anisotropy: Differentiating Between Conformational Exchange and Anisotropic Diffusion in the B3 Domain of Protein G",published,journal,J. Biomol. NMR,,27,3,,,,,,,,,,,,,,,,,,,,,,261,275,2003, citations,ref_1,5839,233590,2,,reference citation,,,9054979,,"Fushman, D., Cahill, S. and Cowburn, D. (1997) J. Mol. Biol., 266, 173-194.",The main-chain dynamics of the dynamin pleckstrin homology (PH) domain in solution: analysis of 15N relaxation with monomer/dimer equilibration.,published,journal,J. Mol. Biol.,Journal of molecular biology,266,1,,0022-2836,,,,,,,,,,,,,,,,,,,,173,194,1997,"The backbone dynamics of the pleckstrin homology (PH) domain from dynamin were studied by 15N NMR relaxation (R1 and R2) and steady state heteronuclear 15N [1H] nuclear Overhauser effect measurements at 500 and 600 MHz, at protein concentrations of 1.7 mM and 300 microM, and by molecular dynamics (MD) simulations. The analysis was performed using the model-free approach. The method was extended in order to account for observed partial (equilibrium) dimerization of the protein at NMR concentrations. A model is developed that takes into account both rapid monomer-dimer exchange and anisotropy of the over-all rotation of the dimer. The data show complex dynamics of the dynamin PH domain. Internal motions in elements of the secondary structure are restricted, as inferred from the high value of the order parameter (S2 approximately 0.9) and from the local correlation time < 100 ps. Of the four extended loop regions that are disordered in the NMR-derived solution structure of the protein, loops beta 1/beta 2 and beta 5/beta 6 are involved in a large-amplitude (S2 down to 0.2 to 0.3) subnanosecond to nanosecond time-scale motion. Reorientation of the loops beta 3/beta 4 and beta 6/beta 7, in contrast, is restricted, characterized by the values of order parameter S2 approximately 0.9 more typical of the protein core. These loops, however, are involved in much slower processes of motion resulting in a conformational exchange on a microsecond to submillisecond time scale. The motions of the terminal regions (residues 1 to 10, 122 to 125) are practically unrestricted (S2 down to 0.05, characteristic times in nanosecond time scale), suggesting that these parts of the sequence do not participate in the protein fold. The analysis shows a larger sensitivity of the 15N relaxation data to protein microdynamic parameters (S2, tau loc) when protein molecular mass (tau c) increases. The use of negative values of the steady state 15N[1H] NOEs as an indicator of the residues not belonging to the folded structure is suggested. The amplitudes of local motion observed in the MD simulation are in a good-agreement with the NMR data for the amide NH groups located in the protein core." citations,entry_citation,5840,233610,1,,entry citation,,,14579314,,,"The solution structure of frenatin 3, a neuronal nitric oxide synthase inhibitor from the giant tree frog, Litoria infrafrenata",published,journal,Biopolymers,,70,3,,,,,,,,,,,,,,,,,,,,,,424,434,2003, citations,entry_citation,5841,233631,1,,entry citation,,22538551,12652139,,,"1H, (13)C and (15)N Resonance Assignments of the Kinase-interacting FHA Domain of Arabidopsis thaliana Kinase-associated Protein Phophatase",published,journal,J. Biomol. NMR,,25,3,,,,,,,,,,,,,,,,,,,,,,253,254,2003, citations,entry_citation,5842,233660,1,,entry citation,,,15522305,,,"Solution NMR structure of the iron-sulfur cluster assembly protein U (IscU) with zinc bound at the active site",published,journal,J. Mol. Biol.,,344,2,,,,,,,,,,,,,,,,,,,,,,567,583,2004, citations,ref_1,5842,233661,2,,reference citation,,,12565051,,"1: Schwieters CD, Kuszewski JJ, Tjandra N, Marius Clore G. J Magn Reson. 2003 Jan;160(1):65-73.",The Xplor-NIH NMR molecular structure determination package.,published,journal,J. Magn. Reson.,"Journal of magnetic resonance (San Diego, Calif. : 1997)",160,1,,1090-7807,,,,,,,,,,,,,,,,,,,,65,73,2003,"We announce the availability of the Xplor-NIH software package for NMR biomolecular structure determination. This package consists of the pre-existing XPLOR program, along with many NMR-specific extensions developed at the NIH. In addition to many features which have been developed over the last 20 years, the Xplor-NIH package contains an interface with a new programmatic framework written in C++. This interface currently supports the general purpose scripting languages Python and TCL, enabling rapid development of new tools, such as new potential energy terms and new optimization methods. Support for these scripting languages also facilitates interaction with existing external programs for structure analysis, structure manipulation, visualization, and spectral analysis." citations,entry_citation,5843,233699,1,,entry citation,,,,,,"Letter to the Editor: Structure of the hypothetical protein At3g17210 from Arabidopsis thaliana",published,journal,J. Biomol. NMR,,28,4,,,,,,,,,,,,,,,,,,,,,,397,400,2004, citations,entry_citation,5844,233728,1,,entry citation,,,17117882,,,FAST-NMR: functional annotation screening technology using NMR spectroscopy,published,journal,J. Am. Chem. Soc.,,128,47,,,,,,,,,,,,,,,,,,,,,,15292,15299,2006, citations,entry_citation,5882,234693,1,,entry citation,,,15017143,,,"Letter to the Editor: Sequence-specific backbone NMR assignments for the C-terminal globular domain of EMILIN-1.",published,journal,J. Biomol. NMR,,29,1,,,,,,,,,,,,,,,,,,,,,,91,92,2004, citations,entry_citation,5883,234718,1,,entry citation,,,15134435,,,"How C-Terminal Carboxyamidation Alters the Biological Activity of Peptides from the Venom of the Eumenine Solitary WasP",published,journal,Biochemistry,,43,19,,,,,,,,,,,,,,,,,,,,,,5608,5617,2004, citations,entry_citation,5884,234738,1,,entry citation,,,14872137,,,"Letter to Editor: Assignment of 1H, 13C and 15N resonances of the AXH domain of the transcription factor HBP1",published,journal,J. Biomol. NMR,,28,4,,,,,,,,,,,,,,,,,,,,,,411,412,2004, citations,ref-1,5844,233729,2,,reference citation,,,9679194,,"Kawarabayasi et al. (1998) DNA Res. 5, 55-76","Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.",published,journal,DNA Res.,DNA research : an international journal for rapid publication of reports on genes and genomes,5,2,,1340-2838,,,,,,,,,,,,,,,,,,,,55,76,1998,"The complete sequence of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3, has been determined by assembling the sequences of the physical map-based contigs of fosmid clones and of long polymerase chain reaction (PCR) products which were used for gap-filling. The entire length of the genome was 1,738,505 bp. The authenticity of the entire genome sequence was supported by restriction analysis of long PCR products, which were directly amplified from the genomic DNA. As the potential protein-coding regions, a total of 2061 open reading frames (ORFs) were assigned, and by similarity search against public databases, 406 (19.7%) were related to genes with putative function and 453 (22.0%) to the sequences registered but with unknown function. The remaining 1202 ORFs (58.3%) did not show any significant similarity to the sequences in the databases. Sequence comparison among the assigned ORFs in the genome provided evidence that a considerable number of ORFs were generated by sequence duplication. By similarity search, 11 ORFs were assumed to contain the intein elements. The RNA genes identified were a single 16S-23S rRNA operon, two 5S rRNA genes and 46 tRNA genes including two with the intron structure. All the assigned ORFs and RNA coding regions occupied 91.25% of the whole genome. The data presented in this paper are available on the internet at http:@www.nite.go.jp." citations,ref-2,5844,233730,3,,reference citation,,,8520220,,"Delaglio F., Grzesiek S., Vuister G.W., Zhu G., Pfeifer J., Bax A. J. Biomol. NMR. (1995) 6, 277-293.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref-3,5844,233731,4,,reference citation,,,,,"T. D. Goddard and D. G. Kneller, SPARKY 3, University of California, San Francisco.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref-4,5844,233732,5,,reference citation,,,9217263,,"Zimmerman D.E., Kulikowski C.A., Huang Y., Feng W., Tashiro M., Shimotakahara S., Chien C., Powers R., Montelione G.T. J. Mol. Biol. (1997) 269, 592-610",Automated analysis of protein NMR assignments using methods from artificial intelligence.,published,journal,J. Mol. Biol.,Journal of molecular biology,269,4,,0022-2836,,,,,,,,,,,,,,,,,,,,592,610,1997,"An expert system for determining resonance assignments from NMR spectra of proteins is described. Given the amino acid sequence, a two-dimensional 15N-1H heteronuclear correlation spectrum and seven to eight three-dimensional triple-resonance NMR spectra for seven proteins, AUTOASSIGN obtained an average of 98% of sequence-specific spin-system assignments with an error rate of less than 0.5%. Execution times on a Sparc 10 workstation varied from 16 seconds for smaller proteins with simple spectra to one to nine minutes for medium size proteins exhibiting numerous extra spin systems attributed to conformational isomerization. AUTOASSIGN combines symbolic constraint satisfaction methods with a domain-specific knowledge base to exploit the logical structure of the sequential assignment problem, the specific features of the various NMR experiments, and the expected chemical shift frequencies of different amino acids. The current implementation specializes in the analysis of data derived from the most sensitive of the currently available triple-resonance experiments. Potential extensions of the system for analysis of additional types of protein NMR data are also discussed." citations,ref-5,5844,233733,6,,reference citation,,,,,"Huang, Y.J. (2001). Automated determination of protein structures from NMR data by iterative analysis of self-consistent contact patterns, PhD thesis, Rutgers University, New Brunswick, NJ.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref-6,5844,233734,7,,reference citation,,,12495027,,"Baran, M.; Moseley, H.N.B.; Sahota, G.; Montelione, G.T. J. Biomol. NMR 2002, 24: 113-121. SPINS: Standardized ProteIn NMR Storage. A data dictionary and object-oriented relational database for archiving protein NMR spectra.",SPINS: standardized protein NMR storage. A data dictionary and object-oriented relational database for archiving protein NMR spectra.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,24,2,,0925-2738,,,,,,,,,,,,,,,,,,,,113,121,2002,"Modern protein NMR spectroscopy laboratories have a rapidly growing need for an easily queried local archival system of raw experimental NMR datasets. SPINS (Standardized ProteIn Nmr Storage) is an object-oriented relational database that provides facilities for high-volume NMR data archival, organization of analyses, and dissemination of results to the public domain by automatic preparation of the header files required for submission of data to the BioMagResBank (BMRB). The current version of SPINS coordinates the process from data collection to BMRB deposition of raw NMR data by standardizing and integrating the storage and retrieval of these data in a local laboratory file system. Additional facilities include a data mining query tool, graphical database administration tools, and a NMRStar v2. 1.1 file generator. SPINS also includes a user-friendly internet-based graphical user interface, which is optionally integrated with Varian VNMR NMR data collection software. This paper provides an overview of the data model underlying the SPINS database system, a description of its implementation in Oracle, and an outline of future plans for the SPINS project." citations,ref-7,5844,233735,8,,reference citation,,,,,see: www-nmr.cabm.rutgers.edu/NMRsoftware/nmr_software.html,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5885,234755,1,,entry citation,,22835172,12954331,,,The Structure of Docking Domains in Modular Polyketide Synthases,published,journal,Chem. Biol.,,10,8,,,,,,,,,,,,,,,,,,,,,,723,731,2003, citations,entry_citation,5886,234786,1,,entry citation,,,15600369,,,"Conformational change of H+-ATPase beta monomer revealed on segmental isotope labeling NMR spectroscopy",published,journal,J. Am. Chem. Soc.,,126,50,,,,,,,,,,,,,,,,,,,,,,16632,16638,2004, citations,ref-8,5844,233736,9,,reference citation,,,10212987,,"Cornilescu, G., Delaglio, F., Bax, A. (1999) J. Biomol. NMR 13, 289-302.",Protein backbone angle restraints from searching a database for chemical shift and sequence homology.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,13,3,,0925-2738,,,,,,,,,,,,,,,,,,,,289,302,1999,"Chemical shifts of backbone atoms in proteins are exquisitely sensitive to local conformation, and homologous proteins show quite similar patterns of secondary chemical shifts. The inverse of this relation is used to search a database for triplets of adjacent residues with secondary chemical shifts and sequence similarity which provide the best match to the query triplet of interest. The database contains 13C alpha, 13C beta, 13C', 1H alpha and 15N chemical shifts for 20 proteins for which a high resolution X-ray structure is available. The computer program TALOS was developed to search this database for strings of residues with chemical shift and residue type homology. The relative importance of the weighting factors attached to the secondary chemical shifts of the five types of resonances relative to that of sequence similarity was optimized empirically. TALOS yields the 10 triplets which have the closest similarity in secondary chemical shift and amino acid sequence to those of the query sequence. If the central residues in these 10 triplets exhibit similar phi and psi backbone angles, their averages can reliably be used as angular restraints for the protein whose structure is being studied. Tests carried out for proteins of known structure indicate that the root-mean-square difference (rmsd) between the output of TALOS and the X-ray derived backbone angles is about 15 degrees. Approximately 3% of the predictions made by TALOS are found to be in error." citations,ref-9,5844,233737,10,,reference citation,,,9367762,,"Guntert P, Mumenthaler C, Wuthrich K. (1997) J. Mol. Biol. 273, 283-98.",Torsion angle dynamics for NMR structure calculation with the new program DYANA.,published,journal,J. Mol. Biol.,Journal of molecular biology,273,1,,0022-2836,,,,,,,,,,,,,,,,,,,,283,298,1997,"The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from distance constraints and torsion angle constraints collected by nuclear magnetic resonance (NMR) experiments performs simulated annealing by molecular dynamics in torsion angle space and uses a fast recursive algorithm to integrate the equations of motions. Torsion angle dynamics can be more efficient than molecular dynamics in Cartesian coordinate space because of the reduced number of degrees of freedom and the concomitant absence of high-frequency bond and angle vibrations, which allows for the use of longer time-steps and/or higher temperatures in the structure calculation. It also represents a significant advance over the variable target function method in torsion angle space with the REDAC strategy used by the predecessor program DIANA. DYANA computation times per accepted conformer in the ""bundle"" used to represent the NMR structure compare favorably with those of other presently available structure calculation algorithms, and are of the order of 160 seconds for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300 computer. Test calculations starting from conformers with random torsion angle values further showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures." citations,ref-10,5844,233738,11,,reference citation,,,,,see: www-nmr.cabm.rutgers.edu/NMRsoftware/nmr_software.html,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5845,233782,1,,entry citation,,,,,,"Backbone and side chain 1H, 13C, and 15N chemical shift assignments for S. aureus protein MW2441 / SACOL2532. Northeast Structural Genomics Target ZR31.",published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5846,233813,1,,entry citation,,,15103637,,,"NMR Structure of the Hypothetical protein NMA1147 from Neisseria meningitidis reveals a distinct 5-helix bundle.",published,journal,Proteins,,55,3,,,,,,,,,,,,,,,,,,,,,,756,758,2004, citations,entry_citation,5847,233838,1,,entry citation,,,15023339,,,"Structure and mechanism of action of Sda, an inhibitor of the histidine kinases that regulate initiation of sporulation in Bacillus subtilis",published,journal,Mol. Cell.,,13,5,,,,,,,,,,,,,,,,,,,,,,689,701,2004, citations,entry_citation,5848,233868,1,,entry citation,,22853138,12835321,,,Structure of the Male Determinant Factor for Brassica Self-incompatibility,published,journal,J. Biol. Chem.,,278,38,,,,,,,,,,,,,,,,,,,,,,36389,36395,2003, citations,entry_citation,5849,233886,1,,entry citation,,,,,,Solution structure of the PCI domain,submitted,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5850,233907,1,,entry citation,,,16195543,,,"Solution structure of the low-molecular-weight protein tyrosine phosphatase from Tritrichomonas foetus reveals a flexible phosphate binding loop",published,journal,Protein Sci.,,14,10,,,,,,,,,,,,,,,,,,,,,,2515,2525,2005, citations,citation_1,5850,233908,2,,reference citation,,,12501188,,,"Kinetic and spectroscopic studies of Tritrichomonas foetus low-molecular weight phosphotyrosyl phosphatase. Hydrogen bond networks and electrostatic effects",published,journal,Biochemistry,,41,52,,,,,,,,,,,,,,,,,,,,,,15601,15609,2002, citations,entry_citation,5851,233929,1,,entry citation,,22753809,12736264,,,"CCHX Zinc Finger Derivatives Retain the Ability to Bind Zn(II) and Mediate Protein-DNA Interactions",published,journal,J. Biol. Chem.,Journal of Biological Chemistry,278,30,,,,,,,,,,,,,,,,,,,,,,28011,28018,2003, citations,entry_citation,5852,233954,1,,entry citation,,22684532,12782785,,,"NMR Structure of the Active Conformation of the Varkud Satellite Ribozyme Cleavage Site",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,100,12,,,,,,,,,,,,,,,,,,,,,,7003,7008,2003, citations,entry_citation,5853,233993,1,,entry citation,,,14752267,,,"Letter to the Editor: Sequential 1H, 15N and 13C NMR assignment of human Calbindin D28k",published,journal,J. Biomol. NMR,,28,3,,,,,,,,,,,,,,,,,,,,,,305,306,2004, citations,entry_citation,5854,234012,1,,entry citation,,,14752265,,,"Letter to the Editor: 1H , 13C, and 15N backbone assignments and secondary structure for the 60.8 kD dimer of the NAD+ synthetase from Bacillus subtilis",published,journal,J. Biomol. NMR,,28,3,,,,,,,,,,,,,,,,,,,,,,301,302,2004, citations,entry_citation,5887,234810,1,,entry citation,,,14556747,,,Solution NMR study of the interaction between NTF2 and nucleoporin FxFG repeats,published,journal,J. Mol. Biol.,,333,3,,,,,,,,,,,,,,,,,,,,,,587,603,2003, citations,entry_citation,5888,234842,1,,entry citation,,,14556747,,,Solution NMR study of the interaction between NTF2 and nucleoporin FxFG repeats,published,journal,J. Mol. Biol.,,333,3,,,,,,,,,,,,,,,,,,,,,,587,603,2003, citations,entry_citation,5889,234867,1,,entry citation,,,14556747,,,Solution NMR study of the interaction between NTF2 and nucleoporin FxFG repeats,published,journal,J. Mol. Biol.,,333,3,,,,,,,,,,,,,,,,,,,,,,587,603,2003, citations,entry_citation,5890,234885,1,,entry citation,,,14715660,,,"The NMR-derived Solution Structure of a New Cationic Antimicrobial Peptide from the Skin Secretion of the Anuran Hyla punctata",published,journal,J. Biol. Chem.,,279,13,,,,,,,,,,,,,,,,,,,,,,13018,13026,2004, citations,entry_citation,5891,234909,1,,entry citation,,,,,,"1H, 15N and 13C NMR Assignments and Secondary Structure of a Hyperthermophile DNA-binding Protein Predicted to contain an Extended Coiled Coil Domain",in preparation,journal,J. Biomol. NMR,,,,,,,,,,,,,,,,,,,,,,,,,,,2003, citations,reference_1,5854,234013,2,,reference citation,,,8520220,,"Delaglio, F., Grzesiek, S., Vuister, G.W., Zhu, G., Pfeifer, J., and Bax, A. (1995) J. Biomol. NMR, 6, 277-293.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,reference_2,5854,234014,3,,reference citation,,,,,"Garrett, D.S., Powers, R., Gronenborn A., and Clore, G.M. (1991) J. Magn. Reson., 95, 214-220.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5856,234046,1,,entry citation,,,14755170,,,"Letter to the Editor: Backbone Resonance Assignments of Human Adult Hemoglobin in the Carbonmonoxy Form",published,journal,J. Biomol. NMR,,28,2,,,,,,,,,,,,,,,,,,,,,,203,204,2004, citations,reference_1,5856,234047,2,,reference citation,,,8589602,,"Wishart, S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. M. ""1H, 13C and 15N chemical shift referencing in biomolecular NMR"", J. Biomol. NMR. 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,5857,234066,1,,entry citation,,,16085652,,,"Structural analysis of Siah1-Siah-interacting protein interactions and insights into the assembly of an E3 ligase multiprotein complex",published,journal,J. Biol. Chem.,,280,40,,,,,,,,,,,,,,,,,,,,,,34278,34287,2005, citations,entry_citation,5858,234095,1,,entry citation,,,14733549,,,"Characterization of us-ms Dynamics of Proteins Using a Combined Analysis of 15N NMR Relaxation and Chemical Shift: Conformational Exchange in Plastocyanin Induced by Histidine Protonations",published,journal,J. Am. Chem. Soc.,,126,3,,,,,,,,,,,,,,,,,,,,,,753,765,2004, citations,ref_1,5858,234096,2,,reference citation,,,12525159,,"Ma L, Hass MA, Vierick N, Kristensen SM, Ulstrup J, Led JJ. Biochemistry 2003, 42,320-330.",Backbone dynamics of reduced plastocyanin from the cyanobacterium Anabaena variabilis: regions involved in electron transfer have enhanced mobility.,published,journal,Biochemistry,Biochemistry,42,2,,0006-2960,,,,,,,,,,,,,,,,,,,,320,330,2003,"The dynamics of the backbone of the electron-transfer protein plastocyanin from the cyanobacterium Anabaena variabilis were determined from the (15)N and (13)C(alpha) R(1) and R(2) relaxation rates and steady-state [(1)H]-(15)N and [(1)H]-(13)C nuclear Overhauser effects (NOEs) using the model-free approach. The (13)C relaxation studies were performed using (13)C in natural abundance. Overall, it is found that the protein backbone is rigid. However, the regions that are important for the function of the protein show moderate mobility primarily on the microsecond to millisecond time scale. These regions are the ""northern"" hydrophobic site close to the metal site, the metal site itself, and the ""eastern"" face of the molecule. In particular, the mobility of the latter region is interesting in light of recent findings indicating that residues also on the eastern face of plastocyanins from prokaryotes are important for the function of the protein. The study also demonstrates that relaxation rates and NOEs of the (13)C(alpha) nuclei of proteins are valuable supplements to the conventional (15)N relaxation measurements in studies of protein backbone dynamics." citations,entry_citation,5859,234151,1,,entry citation,,,14531661,,,Structure of Antibacterial Peptide Microcin J25: A 21-Residue Lariat Protoknot,published,journal,J. Am. Chem. Soc.,,125,41,,,,,,,,,,,,,,,,,,,,,,12382,12383,2003, citations,ref_1,5859,234152,2,,reference citation,,,9679194,,"Kawarabayasi et al. (1998) DNA Res. 5, 55-76","Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.",published,journal,DNA Res.,DNA research : an international journal for rapid publication of reports on genes and genomes,5,2,,1340-2838,,,,,,,,,,,,,,,,,,,,55,76,1998,"The complete sequence of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3, has been determined by assembling the sequences of the physical map-based contigs of fosmid clones and of long polymerase chain reaction (PCR) products which were used for gap-filling. The entire length of the genome was 1,738,505 bp. The authenticity of the entire genome sequence was supported by restriction analysis of long PCR products, which were directly amplified from the genomic DNA. As the potential protein-coding regions, a total of 2061 open reading frames (ORFs) were assigned, and by similarity search against public databases, 406 (19.7%) were related to genes with putative function and 453 (22.0%) to the sequences registered but with unknown function. The remaining 1202 ORFs (58.3%) did not show any significant similarity to the sequences in the databases. Sequence comparison among the assigned ORFs in the genome provided evidence that a considerable number of ORFs were generated by sequence duplication. By similarity search, 11 ORFs were assumed to contain the intein elements. The RNA genes identified were a single 16S-23S rRNA operon, two 5S rRNA genes and 46 tRNA genes including two with the intron structure. All the assigned ORFs and RNA coding regions occupied 91.25% of the whole genome. The data presented in this paper are available on the internet at http:@www.nite.go.jp." citations,entry_citation,5892,234940,1,,entry citation,,,16245938,,,"Solution structure, stability, and nucleic acid binding of the hyperthermophile protein Sso10b2",published,journal,Biochemistry,,44,43,,,,,,,,,,,,,,,,,,,,,,14217,14230,2005, citations,entry_citation,5893,234957,1,,entry citation,,22878800,14516200,,,"Unusual Ca(2+)-calmodulin Binding Interactions of the Microtubule-associated Protein F-STOP",published,journal,Biochemistry,,42,39,,,,,,,,,,,,,,,,,,,,,,11484,11493,2003, citations,entry_citation,6281,243125,1,,entry citation,,,11832227,,,Three-Dimensional Structure of the Complexin/SNARE Complex,published,journal,Neuron,,33,,,,,,,,,,,,,,,,,,,,,,,397,409,2002, citations,ref_2,5859,234153,3,,reference citation,,,8520220,,"Delaglio F., Grzesiek S., Vuister G.W., Zhu G., Pfeifer J., Bax A. J. Biomol. NMR. (1995) 6, 277-293.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref_3,5859,234154,4,,reference citation,,,,,"T. D. Goddard and D. G. Kneller, SPARKY 3, University of California, San Francisco.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_4,5859,234155,5,,reference citation,,,,,"Huang, Y.J. (2001). Automated determination of protein structures from NMR data by iterative analysis of self-consistent contact patterns, PhD thesis, Rutgers University, New Brunswick, NJ.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_5,5859,234156,6,,reference citation,,,,,see: www-nmr.cabm.rutgers.edu/NMRsoftware/nmr_software.html,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_6,5859,234157,7,,reference citation,,,9367762,,"Guntert P, Mumenthaler C, Wuthrich K. (1997) J. Mol. Biol. 273, 283-98.",Torsion angle dynamics for NMR structure calculation with the new program DYANA.,published,journal,J. Mol. Biol.,Journal of molecular biology,273,1,,0022-2836,,,,,,,,,,,,,,,,,,,,283,298,1997,"The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from distance constraints and torsion angle constraints collected by nuclear magnetic resonance (NMR) experiments performs simulated annealing by molecular dynamics in torsion angle space and uses a fast recursive algorithm to integrate the equations of motions. Torsion angle dynamics can be more efficient than molecular dynamics in Cartesian coordinate space because of the reduced number of degrees of freedom and the concomitant absence of high-frequency bond and angle vibrations, which allows for the use of longer time-steps and/or higher temperatures in the structure calculation. It also represents a significant advance over the variable target function method in torsion angle space with the REDAC strategy used by the predecessor program DIANA. DYANA computation times per accepted conformer in the ""bundle"" used to represent the NMR structure compare favorably with those of other presently available structure calculation algorithms, and are of the order of 160 seconds for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300 computer. Test calculations starting from conformers with random torsion angle values further showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures." citations,entry_citation,5860,234191,1,,entry citation,,22583854,12696888,,,"Structure of Subtilosin A, an Antimicrobial Peptide from Bacillus subtilis with Unusual Posttranslational Modifications Linking Cysteine Sulfurs to alpha-Carbons of Phenylalanine and Threonine",published,journal,J. Am. Chem. Soc.,,125,16,,,,,,,,,,,,,,,,,,,,,,4726,4727,2003, citations,ref_1,5860,234192,2,,reference citation,,,12696888,,"Kawulka K, Sprules T, McKay RT, Mercier P, Diaper CM, Zuber P, Vederas JC. J Am Chem Soc. 2003 Apr 23;125(16):4726-7.","Structure of subtilosin A, an antimicrobial peptide from Bacillus subtilis with unusual posttranslational modifications linking cysteine sulfurs to alpha-carbons of phenylalanine and threonine.",published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,125,16,,0002-7863,,,,,,,,,,,,,,,,,,,,4726,4727,2003,"The complete primary and three-dimensional solution structures of subtilosin A (1), a bacteriocin from Bacillus subtilis, were determined by multidimensional NMR studies on peptide produced using isotopically labeled [(13)C,(15)N]medium derived from Anabaena sp. grown on sodium [(13)C]bicarbonate and [(15)N]nitrate. Additional samples of 1 were also generated by separate incorporations of [U-(13)C,(15)N]phenylalanine and [U-(13)C,(15)N]threonine using otherwise unlabeled media. The results demonstrate that in addition to having a cyclized peptide backbone (N and C termini), three cross-links are formed between the sulfurs of Cys13, Cys7, and Cys4 and the alpha-positions of Phe22, Thr28, and Phe31, respectively. Such posttranslational linkage of a thiol to the alpha-carbon of an amino acid residue is very unusual in natural peptides or proteins. Subtilosin A (1) belongs to a new class of bacteriocins." citations,entry_citation,5861,234208,1,,entry citation,,,14752268,,,"Letter to the Editor: Backbone 1H, 13C and 15N resonance assignments for the 18.7 kDa GTPase domain of Escherichia coli MnmE protein",published,journal,J. Biomol. NMR,,28,3,,,,,,,,,,,,,,,,,,,,,,307,308,2004, citations,entry_citation,5862,234230,1,,entry citation,,,14872135,,,"Letter to the Editor: Assignment of 1H, 13C and 15N resonances of the death doamin of TRADD",published,journal,J. Biomol. NMR,,28,4,,,,,,,,,,,,,,,,,,,,,,407,408,2004, citations,entry_citation,5863,234251,1,,entry citation,,,14872134,,,"Letter to the Editor: Backbone HN, N, CA, C' and CB chemical shift assignments and Secondary Structure of FkpA, a 245-residue peptidyl- prolyl cis/trans isomerase with chaperone activity",published,journal,J. Biomol. NMR,,28,4,,,,,,,,,,,,,,,,,,,,,,405,406,2004, citations,ref_1,5998,237371,2,,reference citation,,,12024217,,"da Silva AC, Ferro JA, Reinach FC, Farah CS, Furlan LR, Quaggio RB, Monteiro-Vitorello CB, Van Sluys MA, Almeida NF, Alves LM, do Amaral AM, Bertolini MC, Camargo LE, Camarotte G, Cannavan F, Cardozo J, Chambergo F, Ciapina LP, Cicarelli RM, Coutinho LL, Cursino-Santos JR, El-Dorry H, Faria JB, Ferreira AJ, Ferreira RC, Ferro MI, Formighieri EF, Franco MC, Greggio CC, Gruber A, Katsuyama AM, Kishi LT, Leite RP, Lemos EG, Lemos MV, Locali EC, Machado MA, Madeira AM, Martinez-Rossi NM, Martins EC, Meidanis J, Menck CF, Miyaki CY, Moon DH, Moreira LM, Novo MT, Okura VK, Oliveira MC, Oliveira VR, Pereira HA, Rossi A, Sena JA, Silva C, de Souza RF, Spinola LA, Takita MA, Tamura RE, Teixeira EC, Tezza RI, Trindade dos Santos M, Truffi D, Tsai SM, White FF, Setubal JC, Kitajima JP. Nature, 417(6887), 459-463(2002)",Comparison of the genomes of two Xanthomonas pathogens with differing host specificities.,published,journal,Nature,Nature,417,6887,,0028-0836,,,,,,,,,,,,,,,,,,,,459,463,2002,"The genus Xanthomonas is a diverse and economically important group of bacterial phytopathogens, belonging to the gamma-subdivision of the Proteobacteria. Xanthomonas axonopodis pv. citri (Xac) causes citrus canker, which affects most commercial citrus cultivars, resulting in significant losses worldwide. Symptoms include canker lesions, leading to abscission of fruit and leaves and general tree decline. Xanthomonas campestris pv. campestris (Xcc) causes black rot, which affects crucifers such as Brassica and Arabidopsis. Symptoms include marginal leaf chlorosis and darkening of vascular tissue, accompanied by extensive wilting and necrosis. Xanthomonas campestris pv. campestris is grown commercially to produce the exopolysaccharide xanthan gum, which is used as a viscosifying and stabilizing agent in many industries. Here we report and compare the complete genome sequences of Xac and Xcc. Their distinct disease phenotypes and host ranges belie a high degree of similarity at the genomic level. More than 80% of genes are shared, and gene order is conserved along most of their respective chromosomes. We identified several groups of strain-specific genes, and on the basis of these groups we propose mechanisms that may explain the differing host specificities and pathogenic processes." citations,entry_citation,6443,246561,1,,entry citation,,,,,,"Solution NMR structure of At5g01610, an Arabdopsis protein containing DUF538 domain",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_1,5863,234252,2,,reference citation,,,10748201,,"Kathrin Ramm, A.P., The Periplasmic Escherichia coli Peptidylprolyl cis,trans-Isomerase FkpA. II. ISOMERASE-INDEPENDENT CHAPERONE ACTIVITY IN VITRO. J. Biol. Chem., 2000. 275: p. 17106-17113.","The periplasmic Escherichia coli peptidylprolyl cis,trans-isomerase FkpA. II. Isomerase-independent chaperone activity in vitro.",published,journal,J. Biol. Chem.,The Journal of biological chemistry,275,22,,0021-9258,,,,,,,,,,,,,,,,,,,,17106,17113,2000,"We recently identified FkpA by selecting for the increased yield of antibody single-chain Fv (scFv) fragments in phage display, even of those not containing cis-prolines. We have now investigated the properties of FkpA in vitro. The peptidylprolyl cis-trans-isomerase activity of FkpA was found to be among the highest of any such enzyme with a protein substrate, yet FkpA is not able to enhance the proline-limited refolding rate of the disulfide-free hu4D5-8 scFv fragment, probably due to inaccessibility of Pro-L95. Nevertheless, the yield of the soluble and functional scFv fragment was dramatically increased in vitro in the presence of FkpA. Similar effects were observed for an scFv fragment devoid of cis-prolines. We are thus forced to conclude that the observed folding-assisting function is independent of the isomerase activity of the protein. The beneficial effect of FkpA was found to be due to two components. First, FkpA interacts with early folding intermediates, thus preventing their aggregation. Additionally, it has the ability to reactivate inactive protein, possibly also by binding to a partially unfolded species that may exist in equilibrium with the aggregated form, which may thus be released on a productive pathway. These in vitro measurements therefore fully reflect the in vivo results from periplasmic overexpression of FkpA." citations,ref_2,5863,234253,3,,reference citation,,,11428902,,"Kathrin Ramm, A.P., High Enzymatic Activity and Chaperone Function are Mechanistically Related Features of the Dimeric E. coli Peptidyl-prolyl-isomerase FkpA. Journal of Molecular Biology, 2001. 310(2): p. 485-498.",High enzymatic activity and chaperone function are mechanistically related features of the dimeric E. coli peptidyl-prolyl-isomerase FkpA.,published,journal,J. Mol. Biol.,Journal of molecular biology,310,2,,0022-2836,,,,,,,,,,,,,,,,,,,,485,498,2001,"We have recently described the existence of a chaperone activity for the dimeric peptidyl-prolyl cis/trans isomerase FkpA from the periplasm of Escherichia coli that is independent of its isomerase activity. We have now investigated the molecular mechanism of these two activities in vitro in greater detail. The isomerase activity with a protein substrate (RNaseT1) is characterized by a 100-fold higher k(cat)/K(M) value than with a short tetrapeptide substrate. This enhanced activity with a protein is due to an increased affinity towards the protein substrate mediated by a polypeptide-binding site that is distinct from the active site. The chaperone activity is also mediated by interaction of folding and unfolding intermediates with a binding site that is most likely identical to the polypeptide-binding site which enhances catalysis. Both activities are thus mechanistically related, being based on the transient interaction with this high-affinity polypeptide-binding site. Only the isomerase activity, but not the chaperone activity, with the substrate citrate synthase can be inhibited by FK520. Experiments with the isolated domains of FkpA imply that both the isomerase and the chaperone site are located on the highly conserved FKBP domain. The additional amino-terminal domain mediates the dimerization and thus places the two active sites of the FKBP domains in juxtaposition, such that they can simultaneously interact with a protein, and this is required for full catalytic activity." citations,entry_citation,5864,234294,1,,entry citation,,,15317475,,,"Three dimensional structure of mammalian tachykinin peptide neurokinin B bound to lipid micelles",published,journal,J. Biomol. Struct. Dyn.,,22,2,,,,,,,,,,,,,,,,,,,,,,137,148,2004, citations,entry_citation,5865,234310,1,,entry citation,,,15146482,,,"Solution structure of BmKK2, a new potassium channel blocker from the venom of chinese scorpion Buthus martensi Karsch",published,journal,Proteins,,55,4,,,,,,,,,,,,,,,,,,,,,,835,845,2004, citations,entry_citation,5866,234329,1,,entry citation,,22820173,12939141,,,"Solution Structure and NH Exchange Studies of the MutT Pyrophosphohydrolase Complexed with Mg(2+) and 8-oxo-dGMP, a Tightly Bound Product",published,journal,Biochemistry,,42,34,,,,,,,,,,,,,,,,,,,,,,10140,10154,2003, citations,entry_citation,5867,234357,1,,entry citation,,,,,,Solution Structure of the third SH3 domain of human intersectin 2(KIAA1256),submitted,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5868,234378,1,,entry citation,,,15885096,,,Solution structure and backbone dynamics of the XPC-binding domain of the human DNA repair protein hHR23B.,published,journal,FEBS J.,,272,10,,,,,,,,,,,,,,,,,,,,,,2467,2476,2005, citations,entry_citation,5869,234398,1,,entry citation,,,12900418,,,"Solution Conformation of alphaA-conotoxin EIVA, a Potent Neuromuscular Nicotinic Acetylcholine Receptor Antagonist from Conus ermineus",published,journal,J. Biol. Chem.,,278,43,,,,,,,,,,,,,,,,,,,,,,42208,42213,2003, citations,entry_citation,5870,234417,1,,entry citation,,,15015041,,,Structural Study of Cu(I)-Bleomycin,published,journal,J. Biol. Inorg. Chem.,,9,3,,,,,,,,,,,,,,,,,,,,,,323,334,2004, citations,entry_citation,5871,234438,1,,entry citation,,,15017144,,,"Letter to the Editor: Sequence-specific 1H, 13C and 15N resonance assignments of Ara h 6, an allergenic 2S albumin from peanut",published,journal,J. Biomol. NMR,,29,1,,,,,,,,,,,,,,,,,,,,,,93,94,2004, citations,entry_citation,5872,234451,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C, and 15N resonance assignments of human RGSZ1",published,journal,J. Biomol. NMR,,28,4,,,,,,,,,,,,,,,,,,,,,,409,410,2004, citations,entry_citation,5873,234470,1,,entry citation,,22930671,14568532,,,"Solution Structural Study of BlaI : Implications for the Repression of Genes Involved in Beta-lactam Antibiotic Resistance",published,journal,J. Mol. Biol.,,333,,,,,,,,,,,,,,,,,,,,,,,711,720,2003, citations,entry_citation,5874,234496,1,,entry citation,,,14752269,,,"Complete backbone resonance assignments of p47: the 41kDa adaptor protein of the AAA ATPase p97",published,journal,J. Biomol. NMR,,28,3,,,,,,,,,,,,,,,,,,,,,,309,310,2004, citations,entry_citation,5875,234520,1,,entry citation,,22879646,14516749,,,"A Protein Contortionist: Core Mutations of GB1 that Induce Dimerization and Domain Swapping",published,journal,J. Mol. Biol.,,333,1,,,,,,,,,,,,,,,,,,,,,,141,152,2003, citations,entry_citation,5876,234557,1,,entry citation,,,14752269,,,"Letter to the Editor: Complete backbone resonance assignments of p47: the 41kDa adaptor protein of the AAA ATPase p97",published,journal,J. Biomol. NMR,,28,3,,,,,,,,,,,,,,,,,,,,,,309,310,2004, citations,entry_citation,5877,234581,1,,entry citation,,,15288792,,,"Structure of the coat protein in Pf1 bacteriophage determined by solid-state NMR spectroscopy.",published,journal,J. Mol. Biol.,,341,3,,,,,,,,,,,,,,,,,,,,,,869,879,2004, citations,entry_citation,5878,234604,1,,entry citation,,,14752266,,,"Letter to the Editor: 1H, 13C and 15N resonance assignments of the region 1463-1617 of the mouse p53 Binding Protein 1 (53BP1)",published,journal,J. Biomol. NMR,,28,3,,,,,,,,,,,,,,,,,,,,,,303,304,2004, citations,entry_citation,5879,234638,1,,entry citation,,,15159389,,,NMR Structure of a Type IVb pilin from Salmonella typhi and its assembly into pilus,published,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,2004, citations,entry_citation,5880,234655,1,,entry citation,,,,,,Solution structure of the retroviral Gag MA-like domain of RIKEN cDNA 3110009E22,submitted,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5881,234676,1,,entry citation,,,12970353,,,"Structural basis for tetrodotoxin-resistant sodium channel binding by mu-conotoxin SmIIIA",published,journal,J. Biol. Chem.,,278,47,,,,,,,,,,,,,,,,,,,,,,46805,46813,2003, citations,ref_1,5893,234958,2,,reference citation,,,3000422,,"2: Roberts DM, Crea R, Malecha M, Alvarado-Urbina G, Chiarello RH, Watterson DM. Chemical synthesis and expression of a calmodulin gene designed for site-specific mutagenesis. Biochemistry. 1985 Sep 10;24(19):5090-8.",Chemical synthesis and expression of a calmodulin gene designed for site-specific mutagenesis.,published,journal,Biochemistry,Biochemistry,24,19,,0006-2960,,,,,,,,,,,,,,,,,,,,5090,5098,1985,"A gene coding for a calmodulin was synthesized and expressed in Escherichia coli. The gene was produced by the enzymatic ligation of 61 chemically synthesized DNA fragments. The gene possesses 27 unique, regularly spaced, restriction endonuclease cleavage sites to facilitate gene mutagenesis by the replacement of specific gene segments with synthetic double-stranded DNA. An expression vector containing the calmodulin gene was used to transform E. coli. Purification and characterization of calmodulin (VU-1 calmodulin) expressed by these transformants showed that it lacks two posttranslational modifications: an amino-terminal blocking group and N epsilon, N epsilon, N epsilon-trimethyllysine at position 115. The cyclic nucleotide phosphodiesterase activator properties of VU-1, higher plant, and vertebrate calmodulins were not statistically different. However, VU-1 calmodulin was found to activate nicotinamide adenine dinucleotide (NAD) kinase to a maximal level that was at least 3-fold higher than that found with higher plant and vertebrate calmodulins. This higher level of activation is also characteristic of calmodulins from Dictyostelium discoideum and Chlamydomonas reinhardtii [Roberts, D. M., Burgess, W. H., & Watterson, D. M. (1984) Plant Physiol. 75, 796-798; Marshak, D. R., Clarke, M., Roberts, D. M., & Watterson, D. M. (1984) Biochemistry 23, 2891-2899]. The only common feature among Dictyostelium, Chlamydomonas, and VU-1 calmodulins not found in higher plant and vertebrate calmodulins is an unmethylated lysine at position 115. The results indicate that the lack of methylation of lysine-115 may contribute to the maximal level of NAD kinase activation.(ABSTRACT TRUNCATED AT 250 WORDS)" citations,entry_citation,5894,234980,1,,entry citation,,,15260482,,,"The N-terminal domain of the Drosophila histone mRNA binding protein, SLBP, is intrinsically disordered with nascent helical structure.",published,journal,Biochemistry,,43,29,,,,,,,,,,,,,,,,,,,,,,9390,9400,2004, citations,ref_1,5894,234981,2,,reference citation,,,12189204,,"Battle DJ, Doudna JA. Specificity of RNA-RNA helix recognition. Proc Natl Acad Sci U S A. 2002 Sep 3;99(18):11676-81. Epub 2002 Aug 20.",Specificity of RNA-RNA helix recognition.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,99,18,,0027-8424,,,,,,,,,,,,,,,,,,,,11676,11681,2002,"Functional RNAs often form compact structures characterized by closely packed helices. Crystallographic analysis of several large RNAs revealed a prevalent interaction in which unpaired adenosine residues dock into the minor groove of a receptor helix. This A-minor motif, potentially the most important element responsible for global RNA architecture, has also been suggested to contribute to the fidelity of protein synthesis by discriminating against near-cognate tRNAs on the ribosome. The specificity of A-minor interactions is fundamental to RNA tertiary structure formation, as well as to their proposed role in translational accuracy. To investigate A-minor motif specificity, we analyzed mutations in an A-minor interaction within the Tetrahymena group I self-splicing intron. Thermodynamic and x-ray crystallographic results show that the A-minor interaction strongly prefers canonical base pairs over base mismatches in the receptor helix, enabling RNA interhelical packing through specific recognition of Watson-Crick minor groove geometry." citations,ref_2,5894,234982,3,,reference citation,,,10571029,,"Dominski Z, Marzluff WF. Formation of the 3' end of histone mRNA. Gene. 1999 Oct 18;239(1):1-14. Review.",Formation of the 3' end of histone mRNA.,published,journal,Gene,Gene,239,1,,0378-1119,,,,,,,,,,,,,,,,,,,,1,14,1999,"All metazoan messenger RNAs, with the exception of the replication-dependent histone mRNAs, terminate at the 3' end with a poly(A) tail. Replication-dependent histone mRNAs end instead in a conserved 26-nucleotide sequence that contains a 16-nucleotide stem-loop. Formation of the 3' end of histone mRNA occurs by endonucleolytic cleavage of pre-mRNA releasing the mature mRNA from the chromatin template. Cleavage requires several trans-acting factors, including a protein, the stem-loop binding protein (SLBP), which binds the 26-nucleotide sequence; and a small nuclear RNP, U7 snRNP. There are probably additional factors also required for cleavage. One of the functions of the SLBP is to stabilize binding of the U7 snRNP to the histone pre-mRNA. In the nucleus, both U7 snRNP and SLBP are present in coiled bodies, structures that are associated with histone genes and may play a direct role in histone pre-mRNA processing in vivo. One of the major regulatory events in the cell cycle is regulation of histone pre-mRNA processing, which is at least partially mediated by cell-cycle regulation of the levels of the SLBP protein." citations,ref_3,5894,234983,4,,reference citation,,,12192062,,"Dominski Z, Yang XC, Raska CS, Santiago C, Borchers CH, Duronio RJ, Marzluff WF. 3' end processing of Drosophila melanogaster histone pre-mRNAs: requirement for phosphorylated Drosophila stem-loop binding protein and coevolution of the histone pre-mRNA processing system. Mol Cell Biol. 2002 Sep;22(18):6648-60.",3' end processing of Drosophila melanogaster histone pre-mRNAs: requirement for phosphorylated Drosophila stem-loop binding protein and coevolution of the histone pre-mRNA processing system.,published,journal,Mol. Cell. Biol.,Molecular and cellular biology,22,18,,0270-7306,,,,,,,,,,,,,,,,,,,,6648,6660,2002,"Synthetic pre-mRNAs containing the processing signals encoded by Drosophila melanogaster histone genes undergo efficient and faithful endonucleolytic cleavage in nuclear extracts prepared from Drosophila cultured cells and 0- to 13-h-old embryos. Biochemical requirements for the in vitro cleavage are similar to those previously described for the 3' end processing of mammalian histone pre-mRNAs. Drosophila 3' end processing does not require ATP and occurs in the presence of EDTA. However, in contrast to mammalian processing, Drosophila processing generates the final product ending four nucleotides after the stem-loop. Cleavage of the Drosophila substrates is abolished by depleting the extract of the Drosophila stem-loop binding protein (dSLBP), indicating that both dSLBP and the stem-loop structure in histone pre-mRNA are essential components of the processing machinery. Recombinant dSLBP expressed in insect cells by using the baculovirus system efficiently complements the depleted extract. Only the RNA-binding domain plus the 17 amino acids at the C terminus of dSLBP are required for processing. The full-length dSLBP expressed in insect cells is quantitatively phosphorylated on four residues in the C-terminal region. Dephosphorylation of the recombinant dSLBP reduces processing activity. Human and Drosophila SLBPs are not interchangeable and strongly inhibit processing in the heterologous extracts. The RNA-binding domain of the dSLBP does not substitute for the RNA-binding domain of the human SLBP in histone pre-mRNA processing in mammalian extracts. In addition to the stem-loop structure and dSLBP, 3' processing in Drosophila nuclear extracts depends on the presence of a short stretch of purines located ca. 20 nucleotides downstream from the stem, and an Sm-reactive factor, most likely the Drosophila counterpart of vertebrate U7 snRNP." citations,ref_4,5894,234984,5,,reference citation,,,,,"Grzesiek, S. and Bax, A. (1992) J. Magn. Reson. 99, 201-207.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_5,5894,234985,6,,reference citation,,,,,"Grzesiek, S., Anglister, J. and Bax, A. (1993) J. Magn. Reson. B 101, 114-119.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_6,5894,234986,7,,reference citation,,,12473341,,"Marzluff WF, Duronio RJ. Histone mRNA expression: multiple levels of cell cycle regulation and important developmental consequences. Curr Opin Cell Biol. 2002 Dec;14(6):692-9. Review.",Histone mRNA expression: multiple levels of cell cycle regulation and important developmental consequences.,published,journal,Curr. Opin. Cell Biol.,Current opinion in cell biology,14,6,,0955-0674,,,,,,,,,,,,,,,,,,,,692,699,2002,"Histone mRNA metabolism is tightly coupled to cell cycle progression and to rates of DNA synthesis. The recent identification of several novel proteins involved in histone gene transcription and pre-mRNA processing has shed light on the variety of mechanisms cells employ to achieve this coupling." citations,ref_7,5894,234987,8,,reference citation,,,12242288,,"Sanchez R, Marzluff WF. The stem-loop binding protein is required for efficient translation of histone mRNA in vivo and in vitro. Mol Cell Biol. 2002 Oct;22(20):7093-104.",The stem-loop binding protein is required for efficient translation of histone mRNA in vivo and in vitro.,published,journal,Mol. Cell. Biol.,Molecular and cellular biology,22,20,,0270-7306,,,,,,,,,,,,,,,,,,,,7093,7104,2002,"Metazoan replication-dependent histone mRNAs end in a conserved stem-loop rather than in the poly(A) tail found on all other mRNAs. The 3' end of histone mRNA binds a single class of proteins, the stem-loop binding proteins (SLBP). In Xenopus, there are two SLBPs: xSLBP1, the homologue of the mammalian SLBP, which is required for processing of histone pre-mRNA, and xSLBP2, which is expressed only during oogenesis and is bound to the stored histone mRNA in Xenopus oocytes. The stem-loop is required for efficient translation of histone mRNAs and substitutes for the poly(A) tail, which is required for efficient translation of other eucaryotic mRNAs. When a rabbit reticulocyte lysate is programmed with uncapped luciferase mRNA ending in the histone stem-loop, there is a three- to sixfold increase in translation in the presence of xSLBP1 while xSLBP2 has no effect on translation. Neither SLBP affected the translation of a luciferase mRNA ending in a mutant stem-loop that does not bind SLBP. Capped luciferase mRNAs ending in the stem-loop were injected into Xenopus oocytes after overexpression of either xSLBP1 or xSLBP2. Overexpression of xSLBP1 in the oocytes stimulated translation, while overexpression of xSLBP2 reduced translation of the luciferase mRNA ending in the histone stem-loop. A small region in the N-terminal portion of xSLBP1 is required to stimulate translation both in vivo and in vitro. An MS2-human SLBP1 fusion protein can activate translation of a reporter mRNA ending in an MS2 binding site, indicating that xSLBP1 only needs to be recruited to the 3' end of the mRNA but does not need to be directly bound to the histone stem-loop to activate translation." citations,ref_8,5894,234988,9,,reference citation,,,11157774,,"Sullivan E, Santiago C, Parker ED, Dominski Z, Yang X, Lanzotti DJ, Ingledue TC, Marzluff WF, Duronio RJ. Drosophila stem loop binding protein coordinates accumulation of mature histone mRNA with cell cycle progression. Genes Dev. 2001 Jan 15;15(2):173-87.",Drosophila stem loop binding protein coordinates accumulation of mature histone mRNA with cell cycle progression.,published,journal,Genes Dev.,Genes & development,15,2,,0890-9369,,,,,,,,,,,,,,,,,,,,173,187,2001,"Replication-associated histone genes encode the only metazoan mRNAs that lack polyA tails, ending instead in a conserved 26-nt sequence that forms a stem-loop. Most of the regulation of mammalian histone mRNA is posttranscriptional and mediated by this unique 3' end. Stem-loop-binding protein (SLBP) binds to the histone mRNA 3' end and is thought to participate in all aspects of histone mRNA metabolism, including cell cycle regulation. To examine SLBP function genetically, we have cloned the gene encoding Drosophila SLBP (dSLBP) by a yeast three-hybrid method and have isolated mutations in dSLBP. dSLBP function is required both zygotically and maternally. Strong dSLBP alleles cause zygotic lethality late in development and result in production of stable histone mRNA that accumulates in nonreplicating cells. These histone mRNAs are cytoplasmic and have polyadenylated 3' ends like other polymerase II transcripts. Hypomorphic dSLBP alleles support zygotic development but cause female sterility. Eggs from these females contain dramatically reduced levels of histone mRNA, and mutant embryos are not able to complete the syncytial embryonic cycles. This is in part because of a failure of chromosome condensation at mitosis that blocks normal anaphase. These data demonstrate that dSLBP is required in vivo for 3' end processing of histone pre-mRNA, and that this is an essential function for development. Moreover, dSLBP-dependent processing plays an important role in coupling histone mRNA production with the cell cycle." citations,ref_9,5894,234989,10,,reference citation,,,7899087,,"Williams AS, Marzluff WF. The sequence of the stem and flanking sequences at the 3' end of histone mRNA are critical determinants for the binding of the stem-loop binding protein. Nucleic Acids Res. 1995 Feb 25;23(4):654-62.",The sequence of the stem and flanking sequences at the 3' end of histone mRNA are critical determinants for the binding of the stem-loop binding protein.,published,journal,Nucleic Acids Res.,Nucleic acids research,23,4,,0305-1048,,,,,,,,,,,,,,,,,,,,654,662,1995,"Complexes of different electrophoretic mobility containing the stem-loop binding protein, a 45 kDa protein, bound to the stem-loop at the 3' end of histone mRNA, are present in both nuclear and cytoplasmic extracts from mammalian cells. We have determined the effect of changes in the loop, in the stem and in the flanking sequences on the affinity of the SLBP for the 3' end of histone mRNA. The sequence of the stem is particularly critical for SLBP binding. Specific sequences both 5' and 3' of the stem-loop are also required for high-affinity binding. Expanding the four base loop by one or two uridines reduced but did not abolish SLBP binding. RNA footprinting experiments show that the flanking sequences on both sides of the stem-loop are critical for efficient binding, but that cleavages in the loop do not abolish binding. Thus all three regions of the RNA sequence contribute to SLBP binding, suggesting that the 26 nt at the 3' end of histone mRNA forms a defined tertiary structure recognized by the SLBP." citations,ref_10,5894,234990,11,,reference citation,,,1737021,,"Wishart DS, Sykes BD, Richards FM. The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry. 1992 Feb 18;31(6):1647-51.",The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy.,published,journal,Biochemistry,Biochemistry,31,6,,0006-2960,,,,,,,,,,,,,,,,,,,,1647,1651,1992,"Previous studies by Wishart et al. [Wishart, D. S., Sykes, B. D., & Richards, F. M. (1991) J. Mol. Biol. (in press)] have demonstrated that 1H NMR chemical shifts are strongly dependent on the character and nature of protein secondary structure. In particular, it has been found that the 1H NMR chemical shift of the alpha-CH proton of all 20 naturally occurring amino acids experiences an upfield shift (with respect to the random coil value) when in a helical configuration and a comparable downfield shift when in a beta-strand extended configuration. On the basis of these observations, a technique is described for rapidly and quantitatively determining the identity, extent, and location of secondary structural elements in proteins based on the simple inspection of the alpha-CH 1H resonance assignments. A number of examples are provided to demonstrate both the simplicity and the accuracy of the technique. This new method is found to be almost as accurate as the more traditional NOE-based methods of determining secondary structure and could prove to be particularly useful in light of the recent development of sequential assignment techniques which are now almost NOE-independent [Ikura, M., Kay, L. E., & Bax, A. (1990) Biochemistry 29, 4659-4667]. We suggest that this new procedure should not necessarily be seen as a substitute to existing rigorous methods for secondary structure determination but, rather, should be viewed as a complement to these approaches." citations,entry_citation,5895,235013,1,,entry citation,,,14621986,,,"Location of the Zn2+ binding site on S100B as determined by NMR spectroscopy and site-directed mutagenesis",published,journal,Biochemistry,,42,46,,,,,,,,,,,,,,,,,,,,,,13410,13421,2003, citations,entry_citation,5896,235042,1,,entry citation,,22878800,14516200,,,"Unusual Ca(2+)-calmodulin Binding Interactions of the Microtubule-associated Protein F-STOP",published,journal,Biochemistry,,42,39,,,,,,,,,,,,,,,,,,,,,,11484,11493,2003, citations,entry_citation,6008,237653,1,,entry citation,,,,,,"Structure of the Plasminogen Kringle 4 Binding Calcium Bound Form of the C-type Lectin-like Domain of Tetranectin",published,journal,Biochemistry,,43,27,,,,,,,,,,,,,,,,,,,,,,8636,8643,2004, citations,entry_citation,6009,237669,1,,entry citation,,,15214802,,,NMR structure of the thrombin-binding DNA aptamer stabilized by Sr2+,published,journal,J. Biomol. Struct. Dyn.,,22,1,,,,,,,,,,,,,,,,,,,,,,25,33,2004, citations,entry_citation,6010,237691,1,,entry citation,,,15723348,,,"NMR structure of the conserved hypothetical protein TM0979 from Thermotoga maritima",published,journal,Proteins,,59,2,,,,,,,,,,,,,,,,,,,,,,387,390,2005, citations,ref_1,5896,235043,2,,reference citation,,,3000422,,"Roberts DM, Crea R, Malecha M, Alvarado-Urbina G, Chiarello RH, Watterson DM. Chemical synthesis and expression of a calmodulin gene designed for site-specific mutagenesis. Biochemistry. 1985 24(19):5090-8.",Chemical synthesis and expression of a calmodulin gene designed for site-specific mutagenesis.,published,journal,Biochemistry,Biochemistry,24,19,,0006-2960,,,,,,,,,,,,,,,,,,,,5090,5098,1985,"A gene coding for a calmodulin was synthesized and expressed in Escherichia coli. The gene was produced by the enzymatic ligation of 61 chemically synthesized DNA fragments. The gene possesses 27 unique, regularly spaced, restriction endonuclease cleavage sites to facilitate gene mutagenesis by the replacement of specific gene segments with synthetic double-stranded DNA. An expression vector containing the calmodulin gene was used to transform E. coli. Purification and characterization of calmodulin (VU-1 calmodulin) expressed by these transformants showed that it lacks two posttranslational modifications: an amino-terminal blocking group and N epsilon, N epsilon, N epsilon-trimethyllysine at position 115. The cyclic nucleotide phosphodiesterase activator properties of VU-1, higher plant, and vertebrate calmodulins were not statistically different. However, VU-1 calmodulin was found to activate nicotinamide adenine dinucleotide (NAD) kinase to a maximal level that was at least 3-fold higher than that found with higher plant and vertebrate calmodulins. This higher level of activation is also characteristic of calmodulins from Dictyostelium discoideum and Chlamydomonas reinhardtii [Roberts, D. M., Burgess, W. H., & Watterson, D. M. (1984) Plant Physiol. 75, 796-798; Marshak, D. R., Clarke, M., Roberts, D. M., & Watterson, D. M. (1984) Biochemistry 23, 2891-2899]. The only common feature among Dictyostelium, Chlamydomonas, and VU-1 calmodulins not found in higher plant and vertebrate calmodulins is an unmethylated lysine at position 115. The results indicate that the lack of methylation of lysine-115 may contribute to the maximal level of NAD kinase activation.(ABSTRACT TRUNCATED AT 250 WORDS)" citations,ref_2,5896,235044,3,,reference citation,,,11413126,,"Bosc C, Frank R, Denarier E, Ronjat M, Schweitzer A, Wehland J, Job D. Identification of novel bifunctional calmodulin-binding and microtubule-stabilizing motifs in STOP proteins. J Biol Chem. 2001 276(33):30904-13.",Identification of novel bifunctional calmodulin-binding and microtubule-stabilizing motifs in STOP proteins.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,276,33,,0021-9258,,,,,,,,,,,,,,,,,,,,30904,30913,2001,"Although microtubules are intrinsically labile tubulin assemblies, many cell types contain stable polymers, resisting depolymerizing conditions such as exposure to the cold or the drug nocodazole. This microtubule stabilization is largely due to polymer association with STOP proteins. There are several STOP variants, some with capacity to induce microtubule resistance to both the cold and nocodazole, others with microtubule cold stabilizing activity only. These microtubule-stabilizing effects of STOP proteins are inhibited by calmodulin and we now demonstrate that they are determined by two distinct kinds of repeated modular sequences (Mn and Mc), both containing a calmodulin-binding peptide, but displaying different microtubule stabilizing activities. Mn modules induce microtubule resistance to both the cold and nocodazole when expressed in cells. Mc modules, which correspond to the STOP central repeats, have microtubule cold stabilizing activity only. Mouse neuronal STOPs, which induce both cold and drug resistance in cellular microtubules, contain three Mn modules and four Mc modules. Compared with neuronal STOPs, the non-neuronal F-STOP lacks multiple Mn modules and this corresponds with an inability to induce nocodazole resistance. STOP modules represent novel bifunctional calmodulin-binding and microtubule-stabilizing sequences that may be essential for the generation of the different patterns of microtubule stabilization observed in cells." citations,entry_citation,5897,235064,1,,entry citation,,22863537,14499614,,,"Solution Structure of the BHRF1 Protein from Epstein-Barr Virus, a Homolog of Human Bcl-2",published,journal,J. Mol. Biol.,,332,5,,,,,,,,,,,,,,,,,,,,,,1123,1130,2003, citations,entry_citation,5898,235077,1,,entry citation,,,15379554,,,"Solution structure of the human oncogenic protein gankyrin containing seven ankyrin repeats and analysis of its structure--function relationship.",published,journal,Biochemistry,,43,38,,,,,,,,,,,,,,,,,,,,,,12152,12161,2004, citations,entry_citation,5899,235097,1,,entry citation,,22758621,12875849,,,"The NMR Solution Structure of BeF(3)(-)-activated Spo0F Reveals the Conformational Switch in a Phosphorelay System",published,journal,J. Mol. Biol.,,331,1,,,,,,,,,,,,,,,,,,,,,,245,254,2003, citations,entry_citation,5900,235116,1,,entry citation,,,15096630,,,"Backbone dynamics of complement control protein (CCP) modules reveals mobility in binding surfaces.",published,journal,Protein Sci.,,13,5,,,,,,,,,,,,,,,,,,,,,,1238,1250,2004, citations,entry_citation,5901,235135,1,,entry citation,,,14744132,,,"Solution Structure of a CCHHC Domain of Neural Zinc Finger Factor-1 and its Implications for DNA Binding",published,journal,Biochemistry,,43,4,,,,,,,,,,,,,,,,,,,,,,898,903,2004, citations,entry_citation,5902,235165,1,,entry citation,,,15017145,,,"Letter to Editor: Sequence specific 1H, 13C and 15N Resonance Assignments of the Hath-Domain of Human Hepatoma-Derived Growth Factor",published,journal,J. Biomol. NMR,,29,1,,,,,,,,,,,,,,,,,,,,,,95,96,2004, citations,ref_1,5902,235166,2,,reference citation,,,12006088,,"Dietz F, Franken S, Yoshida K, Nakamura H, Kappler J, Gieselmann V. The family of hepatoma-derived growth factor proteins: characterization of a new member HRP-4 and classification of its subfamilies. Biochem J. 2002 Sep 1;366(Pt 2):491-500.",The family of hepatoma-derived growth factor proteins: characterization of a new member HRP-4 and classification of its subfamilies.,published,journal,Biochem. J.,The Biochemical journal,366,Pt 2,,0264-6021,,,,,,,,,,,,,,,,,,,,491,500,2002,"Hepatoma-derived growth factor (HDGF)-related proteins (HRPs) comprise a family of polypeptides named after HDGF, which was identified by its mitogenic activity towards fibroblasts. In the present study, we describe a hitherto unknown HRP, termed HRP-4. The cDNA of bovine HRP-4 (bHRP-4) predicts a polypeptide of 235 amino acids. Northern- and Western-blot analyses of various bovine tissues demonstrated that HRP-4 is only expressed in the testis. Recombinantly produced bHRP-4 and murine HDGF (mHDGF) histidine-tagged polypeptides display growth-factor activity for cultured primary human fibroblasts at an optimum concentration of 1 ng/ml in serum-free medium. The growth-factor activity declines with increasing concentrations to reach background levels at 1 microg/ml. The expression of the fusion proteins, bHRP-4-green fluorescent protein and mHDGF-green fluorescent protein, in HEK-293 cells demonstrates nuclear localization of the proteins. bHRP-4 and mHDGF bind to the glycosaminoglycans heparin and heparan sulphate, but not to chondroitin sulphate. Affinity constants determined for these interactions are between 6 and 42 nM. Comparison of the bHRP-4 amino acid sequence with HRP-1-3 and p52/75/lens epithelium-derived growth factor (LEDGF) shows that these proteins share a conserved N-terminal part of 91 amino acids but have C-termini of different lengths and charge. This demonstrates the modular structure of these proteins and allows its classification into three groups based on charge, size and sequence comparison. HRP-4, HRP-1 and HDGF are small acidic proteins, HRP-3 is a small basic protein, and HRP-2 and p52/75/LEDGF are larger basic proteins." citations,entry_citation,6011,237715,1,,entry citation,,,,,,"Letter to the Editor: Solution structure of a homodimeric hypothetical protein, At5g22580, a structural genomics target from Arabidopsis Thaliana",published,journal,J. Biomol. NMR,,29,3,,,,,,,,,,,,,,,,,,,,,,387,390,2004, citations,entry_citation,6012,237733,1,,entry citation,,,14761955,,,Human Sgt1 binds to HSP90 through the CS domain and not the TPR domain,published,journal,J. Biol. Chem.,,279,16,,,,,,,,,,,,,,,,,,,,,,16511,16517,2004, citations,entry_citation,6013,237752,1,,entry citation,,,15243185,,,"Letter to the editor: 1H, 13C and 15N resonance assignments of the third spectrin repeat of alpha-actinin-4",published,journal,J. Biomol. NMR,,29,4,,,,,,,,,,,,,,,,,,,,,,533,534,2004, citations,ref_2,5902,235167,3,,reference citation,,,11751870,,"Kishima Y, Yamamoto H, Izumoto Y, Yoshida K, Enomoto H, Yamamoto M, Kuroda T, Ito H, Yoshizaki K, Nakamura H. Hepatoma-derived growth factor stimulates cell growth after translocation to the nucleus by nuclear localization signals. J Biol Chem. 2002 Mar 22;277(12):10315-22. Epub 2001 Dec 18.",Hepatoma-derived growth factor stimulates cell growth after translocation to the nucleus by nuclear localization signals.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,277,12,,0021-9258,,,,,,,,,,,,,,,,,,,,10315,10322,2002,"Hepatoma-derived growth factor (HDGF) is the original member of the HDGF family of proteins, which contains a well-conserved N-terminal amino acid sequence (homologous to the amino terminus of HDGF; hath) and nuclear localization signals (NLSs) in gene-specific regions other than the hath region. In addition to a bipartite NLS in a gene-specific region, an NLS-like sequence is also found in the hath region. In cells expressing green fluorescence protein (GFP)-HDGF, green fluorescence was observed in the nucleus, whereas it was detected in the cytoplasm of cells expressing GFP-HDGF with both NLSs mutated or deleted. GFP-hath protein (GFP-HATH) was distributed mainly in the nucleus, although some was present in the cytoplasm, whereas GFP-HDGF with a deleted hath region (HDGFnonHATH) was found only in the nucleus. Exogenously supplied GFP-HDGF was internalized and translocated to the nucleus. GFP-HATH was internalized, whereas GFP-HDGFnonHATH was not. Overexpression of HDGF stimulated DNA synthesis and cellular proliferation, although HDGF with both NLSs deleted did not. Overexpression of HDGFnonHATH caused a significant stimulation of DNA synthesis, whereas that of hath protein did not. HDGF containing the NLS sequence of p53 instead of the bipartite NLS did not stimulate DNA synthesis, and truncated forms without the C- or N-terminal side of NLS2 did not. These findings suggest that the gene-specific region, at least the bipartite NLS sequence and the N- and C-terminal neighboring portions, is essential for the mitogenic activity of HDGF after nuclear translocation." citations,ref_3,5902,235168,4,,reference citation,,,12842472,,"Slater LM, Allen MD, Bycroft M. Structural variation in PWWP domains. J Mol Biol. 2003 Jul 11;330(3):571-6.",Structural variation in PWWP domains.,published,journal,J. Mol. Biol.,Journal of molecular biology,330,3,,0022-2836,,,,,,,,,,,,,,,,,,,,571,576,2003,"The PWWP domain is a ubiquitous eukaryotic protein module characterised by a region of sequence similarity of approximately 80 amino acids containing a highly conserved PWWP motif. It is frequently found in proteins associated with chromatin. We have determined the structure of a PWWP domain from the S. pombe protein SPBC215.07c using NMR spectroscopy. The structure is composed of a five stranded beta barrel followed by two alpha helices. Comparison to the recently reported structure of a homologous domain from the mammalian DNA methyltransferase Dnmt3b reveals substantial differences both in the C-terminal helical region and in the PWWP motif." citations,ref_4,5902,235169,5,,reference citation,,,11481329,,"Everett AD, Stoops T, McNamara CA. Nuclear targeting is required for hepatoma-derived growth factor-stimulated mitogenesis in vascular smooth muscle cells. J Biol Chem. 2001 Oct 5;276(40):37564-8. Epub 2001 Jul 31.",Nuclear targeting is required for hepatoma-derived growth factor-stimulated mitogenesis in vascular smooth muscle cells.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,276,40,,0021-9258,,,,,,,,,,,,,,,,,,,,37564,37568,2001,"We recently identified hepatoma-derived growth factor (HDGF) as a nuclear targeted vascular smooth muscle cell (VSM) mitogen that is expressed in developing vascular lesions. In the present study, VSM in culture express endogenous HDGF only in the nucleus and target a green fluorescent protein (GFP)-HDGF fusion to the nucleus. To define the features of the HDGF molecule that are essential for nuclear localization and mitogenic function, deletion and site-directed mutagenesis were performed. Deletion analysis identified the carboxyl-terminal half of HDGF to be responsible for nuclear targeting in VSM. Overexpression of tagged HDGF proteins with point mutations in the putative bipartite nuclear localization sequence in the carboxyl terminus demonstrated that single Lys --> Asn mutations randomized HDGF expression to both the nucleus and cytoplasm similar to the empty vector. Importantly, the Lys --> Asn mutation of all three lysines blocked nuclear entry. Point mutation of a p34(cdc2) kinase consensus motif within the nuclear localization sequence had no effect on nuclear targeting. Moreover, nuclear entry was essential for the HDGF mitogenic effect, as transfection with the triple Lys --> Asn mutant HA-HDGF significantly attenuated bromodeoxyuridine uptake when compared with transfection with wild type HA-HDGF. We conclude that HDGF contains a true bipartite nuclear localization sequence with all three lysines necessary for nuclear targeting. Nuclear targeting of HDGF is required for HDGF stimulation of DNA replication in VSM." citations,entry_citation,5903,235198,1,,entry citation,,,15017146,,,"Letter to the Editor: 1H, 13C and 15N backbone resonance assignments of the Hyaluronan-binding domain of CD44",published,journal,J. Biomol. NMR,,29,1,,,,,,,,,,,,,,,,,,,,,,97,98,2004, citations,entry_citation,5904,235211,1,,entry citation,,,,,,NMR study of inhibitor-1a - a protein inhibitor of protein phosphatase-1,published,thesis,,,,,,,,,,,,,,,,,,,,,,Univ. of Yang-Ming,Taipei,Taiwan,,,,2003, citations,entry_citation,5905,235234,1,,entry citation,,,,,,"Thermodynamics of Hydrophobic Core Packing in the Thermophile proteins Sac7d and Sso7d",in preparation,journal,J. Mol. Biol.,,,,,,,,,,,,,,,,,,,,,,,,,,,,"These assignments are being deposited for each of the four wild-type and mutant proteins used in this study." citations,references_1,5905,235235,2,,reference citation,,,12666159,,"Bosch D, Campillo M, Pardo L. J Comput Chem. 2003 Apr 30;24(6):682-91",Binding of proteins to the minor groove of DNA: what are the structural and energetic determinants for kinking a basepair step?,published,journal,,Journal of computational chemistry,24,6,,0192-8651,,,,,,,,,,,,,,,,,,,,682,691,2003,"The structural and energetic determinants for kinking a basepair step by minor groove-insertion of the protein side chains of PurR, LacI, LEF-1, IHF, Sac7d, and Sso7d, have been calculated by molecular dynamics/potential of mean force simulations. The structural determinants of the kinked structures are: two contiguous furanose rings achieve different conformations, in the region of C3'endo (A-DNA) and C2'endo (B-DNA); the chi torsion angle always takes values characteristic of the C2'endo conformation of B-DNA, independently of sugar puckering; and protein side chain insertion increases slide (from negative to positive values), rise, and roll, and decreases twist. The energetic determinants of DNA kinking are: the conformational transition of the sugar-phosphate backbone is not energetically demanding; the relative importance of the interbase parameters in the free energy penalty is slide, followed by twist and rise, and concluding with shift and roll; and the characteristic increase of roll and decrease of twist, upon side chain insertion, tends to stabilize the process of DNA kinking." citations,references_13,5905,235246,13,,reference citation,,,9224936,,"Kulms D, Schafer G, Hahn U. Biol Chem. 1997 Jun;378(6):545-51.",Overproduction of Sac7d and Sac7e reveals only Sac7e to be a DNA-binding protein with ribonuclease activity from the extremophilic archaeon Sulfolobus acidocaldarius.,published,journal,Biol. Chem.,Biological chemistry,378,6,,1431-6730,,,,,,,,,,,,,,,,,,,,545,551,1997,"Genomic DNA from Sulfolobus acidocaldarius was screened using a degenerate oligodeoxyribonucleotide, derived from the sequence of 16 N-terminal amino acids from SaRD protein. SaRD protein was previously isolated in our laboratory and identified as a protein from S. acidocaldarius exhibiting ribonuclease activity as well as DNA-binding properties. On the basis of Southern hybridization analysis two genes from S. acidocaldarius have been cloned, sequenced and overproduced in Escherichia coli. The deduced amino acid sequences revealed that one gene encodes Sac7d and the other one Sac7e; two small, previously described basic proteins from S. acidocaldarius, and furthermore the N-termini of Sac7e and SaRD are identical. Northern blot analysis demonstrated that the genes are transcribed separately. After expression of sac7d and sac7e genes in E. coli it was shown that only recombinant Sac7e protein exhibits RNase activity and is catalytically indistinguishable from SaRD protein. Western blot analysis using a polyclonal antiserum raised against purified SaRD protein further confirmed that Sac7e and SaRD are identical proteins endowed with RNase activity and DNA-binding properties. A new RNA cleavage mechanism has to be postulated for Sac7e since, in contrast to common RNases (e.g. RNase A and T1), no histidines are present in the amino acid sequence. Differences between the very closely related 7 kDa proteins from two Sulfolobus strains converting DNA-binding proteins into RNases are pointed out and discussed, whereas substitutions of Glu by Gln (S. solfataricus) or by Lys (S. acidocaldarius) seem to be crucial." citations,references_2,5905,235236,3,,reference citation,,,12060682,,"Napoli A, Zivanovic Y, Bocs C, Buhler C, Rossi M, Forterre P, Ciaramella M. Nucleic Acids Res. 2002 Jun 15;30(12):2656-62.","DNA bending, compaction and negative supercoiling by the architectural protein Sso7d of Sulfolobus solfataricus.",published,journal,Nucleic Acids Res.,Nucleic acids research,30,12,,1362-4962,,,,,,,,,,,,,,,,,,,,2656,2662,2002,"Members of the Sso7d/Sac7d family are small, abundant, non-specific DNA-binding proteins of the hyperthermophilic Archaea SULFOLOBUS: Crystal structures of these proteins in complex with oligonucleotides showed that they induce changes in the helical twist and marked DNA bending. On this basis they have been suggested to play a role in organising chromatin structures in these prokaryotes, which lack histones. We report functional in vitro assays to investigate the effects of the observed Sso7d-induced structural modifications on DNA geometry and topology. We show that binding of multiple Sso7d molecules to short DNA fragments induces significant curvature and reduces the stiffness of the complex. Sso7d induces negative supercoiling of DNA molecules of any topology (relaxed, positively or negatively supercoiled) and in physiological conditions of temperature and template topology. Binding of Sso7d induces compaction of positively supercoiled and relaxed DNA molecules, but not of negatively supercoiled ones. Finally, Sso7d inhibits the positive supercoiling activity of the thermophile-specific enzyme reverse gyrase. The proposed biological relevance of these observations is that these proteins might model the behaviour of DNA in constrained chromatin environments." citations,references_3,5905,235237,4,,reference citation,,,11398456,,"Edmondson SP, Shriver JW. Methods Enzymol. 2001;334:129-45.",DNA binding proteins Sac7d and Sso7d from Sulfolobus.,published,journal,Meth. Enzymol.,Methods in enzymology,334,,,0076-6879,,,,,,,,,,,,,,,,,,,,129,145,2001, citations,references_4,5905,235238,5,,reference citation,,,11106160,,"Bedell JL, McCrary BS, Edmondson SP, Shriver JW. Protein Sci. 2000 Oct;9(10):1878-88.",The acid-induced folded state of Sac7d is the native state.,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,9,10,,0961-8368,,,,,,,,,,,,,,,,,,,,1878,1888,2000,"Sac7d unfolds at low pH in the absence of salt, with the greatest extent of unfolding obtained at pH 2. We have previously shown that the acid unfolded protein is induced to refold by decreasing the pH to 0 or by addition of salt (McCrary BS, Bedell J. Edmondson SP, Shriver JW, 1998, J Mol Biol 276:203-224). Both near-ultraviolet circular dichroism spectra and ANS fluorescence enhancements indicate that the acid- and salt-induced folded states have a native fold and are not molten globular. 1H,15N heteronuclear single quantum coherence NMR spectra confirm that the native, acid-, and salt-induced folded states are essentially identical. The most significant differences in amide 1H and 15N chemical shifts are attributed to hydrogen bonding to titrating carboxyl side chains and through-bond inductive effects. The 1H NMR chemical shifts of protons affected by ring currents in the hydrophobic core of the acid- and salt-induced folded states are identical to those observed in the native. The radius of gyration of the acid-induced folded state at pH 0 is shown to be identical to that of the native state at pH 7 by small angle X-ray scattering. We conclude that acid-induced collapse of Sac7d does not lead to a molten globule but proceeds directly to the native state. The folding of Sac7d as a function of pH and anion concentration is summarized with a phase diagram that is similar to those observed for other proteins that undergo acid-induced folding except that the A-state is encompassed by the native state. These results demonstrate that formation of a molten globule is not a general property of proteins that are refolded by acid." citations,references_5,5905,235239,6,,reference citation,,,11031116,,"Su S, Gao YG, Robinson H, Liaw YC, Edmondson SP, Shriver JW, Wang AH. J Mol Biol. 2000 Oct 27;303(3):395-403.",Crystal structures of the chromosomal proteins Sso7d/Sac7d bound to DNA containing T-G mismatched base-pairs.,published,journal,J. Mol. Biol.,Journal of molecular biology,303,3,,0022-2836,,,,,,,,,,,,,,,,,,,,395,403,2000,"Sso7d and Sac7d are two small chromatin proteins from the hyperthermophilic archaeabacterium Sulfolobus solfataricus and Sulfolobus acidocaldarius, respectively. The crystal structures of Sso7d-GTGATCGC, Sac7d-GTGATCGC and Sac7d-GTGATCAC have been determined and refined at 1.45 A, 2.2 A and 2.2 A, respectively, to investigate the DNA binding property of Sso7d/Sac7d in the presence of a T-G mismatch base-pair. Detailed structural analysis revealed that the intercalation site includes the T-G mismatch base-pair and Sso7d/Sac7d bind to that mismatch base-pair in a manner similar to regular DNA. In the Sso7d-GTGATCGC complex, a new inter-strand hydrogen bond between T2O4 and C14N4 is formed and well-order bridging water molecules are found. The results suggest that the less stable DNA stacking site involving a T-G mismatch may be a preferred site for protein side-chain intercalation." citations,references_6,5905,235240,7,,reference citation,,,8520220,,"Delaglio, F. et al. J. Biomol. NMR 6, 277-293 (1995).",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,entry_citation,5908,235304,1,,entry citation,,,,,,"Thermodynamics of Hydrophobic Core Packing in the Thermophile Proteins Sac7d and Sso7d",in preparation,journal,J. Mol. Biol.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6014,237769,1,,entry citation,,,15243187,,,"Letter to the Editor: 1H, 13C and 15N backbone resonance assignments of matrilysin (MMP7) complexed with a sulfonamide hydroxamate-type inhibitor",published,journal,J. Biomol. NMR,,29,3,,,,,,,,,,,,,,,,,,,,,,537,538,2004, citations,entry_citation,6015,237795,1,,entry citation,,,15213454,,,"Letter to the Editor: Sequence specific assignment of domain C1 of the N-terminal myosin-binding site of human cardiac myosin binding protein C (MyBP-C)",published,journal,J. Biomol. NMR,,29,3,,,,,,,,,,,,,,,,,,,,,,431,432,2004, citations,entry_citation,6016,237822,1,,entry citation,,,,,,"Letter to the Editor: Backbone resonance assignments of the 45.3 kDa catalytic domain of human BACE1",published,journal,J. Biomol. NMR,,29,3,,,,,,,,,,,,,,,,,,,,,,425,426,2004, citations,references_7,5905,235241,8,,reference citation,,,10343384,,"Hunenberger PH, McCammon JA. Biophys Chem. 1999 Apr 5;78(1-2):69-88.",Effect of artificial periodicity in simulations of biomolecules under Ewald boundary conditions: a continuum electrostatics study.,published,journal,Biophys. Chem.,Biophysical chemistry,78,1-2,,0301-4622,,,,,,,,,,,,,,,,,,,,69,88,1999,"Ewald and related methods are nowadays routinely used in explicit-solvent simulations of biomolecules, although they impose an artificial periodicity in systems which are inherently non-periodic. The consequences of this approximation should be assessed, since they may crucially affect the reliability of computer simulations under Ewald boundary conditions. In the present study we use a method based on continuum electrostatics to investigate the nature and magnitude of possible periodicity-induced artifacts on the potentials of mean force for conformational equilibria in biomolecules. Three model systems and pathways are considered: polyalanine oligopeptides (unfolding), a DNA tetranucleotide (separation of the strands), and the protein Sac7d (conformations from a molecular dynamics simulation). Artificial periodicity may significantly affect these conformational equilibria, in each case stabilizing the most compact conformation of the biomolecule. Three factors enhance periodicity-induced artifacts: (i) a solvent of low dielectric permittivity; (ii) a solute size which is non-negligible compared to the size of the unit cell; and (iii) a non-neutral solute. Neither the neutrality of the solute nor the absence of charge pairs at distances exceeding half the edge of the unit cell do guarantee the absence of artifacts." citations,references_8,5905,235242,9,,reference citation,,,9917414,,"de Bakker PI, Hunenberger PH, McCammon JA. J Mol Biol. 1999 Jan 29;285(4):1811-30.",Molecular dynamics simulations of the hyperthermophilic protein sac7d from Sulfolobus acidocaldarius: contribution of salt bridges to thermostability.,published,journal,J. Mol. Biol.,Journal of molecular biology,285,4,,0022-2836,,,,,,,,,,,,,,,,,,,,1811,1830,1999,"Hyperthermophilic proteins often possess an increased number of surface salt bridges compared with their mesophilic homologues. However, salt bridges are generally thought to be of minor importance in protein stability at room temperature. In an effort to understand why this may no longer be true at elevated temperatures, we performed molecular dynamics simulations of the hyperthermophilic protein Sac7d at 300 K, 360 K, and 550 K. The three trajectories are stable on the nanosecond timescale, as evidenced by the analysis of several time-resolved properties. The simulations at 300 K and (to a lesser extent) 360 K are also compatible with nuclear Overhauser effect-derived distances. Raising the temperature from 300 K to 360 K results in a less favourable protein-solvent interaction energy, and a more favourable intraprotein interaction energy. Both effects are almost exclusively electrostatic in nature and dominated by contributions due to charged side-chains. The reduced solvation is due to a loss of spatial and orientational structure of water around charged side-chains, which is a consequence of the increased thermal motion in the solvent. The favourable change in the intraprotein Coulombic interaction energy is essentially due to the tightening of salt bridges. Assuming that charged side-chains are on average more distant from one another in the unfolded state than in the folded state, it follows that salt bridges may contribute to protein stability at elevated temperatures because (i) the solvation free energy of charged side-chains is more adversely affected in the unfolded state than in the folded state by an increase in temperature, and (ii) due to the tightening of salt bridges, unfolding implies a larger unfavourable increase in the intraprotein Coulombic energy at higher temperature. Possible causes for the unexpected stability of the protein at 550 K are also discussed." citations,references_10,5905,235243,10,,reference citation,,,9731772,,"Gao YG, Su SY, Robinson H, Padmanabhan S, Lim L, McCrary BS, Edmondson SP, Shriver JW, Wang AH. Nat Struct Biol. 1998 Sep;5(9):782-6.",The crystal structure of the hyperthermophile chromosomal protein Sso7d bound to DNA.,published,journal,Nat. Struct. Biol.,Nature structural biology,5,9,,1072-8368,,,,,,,,,,,,,,,,,,,,782,786,1998,"Sso7d and Sac7d are two small (approximately 7,000 Mr), but abundant, chromosomal proteins from the hyperthermophilic archaeabacteria Sulfolobus solfataricus and S. acidocaldarius respectively. These proteins have high thermal, acid and chemical stability. They bind DNA without marked sequence preference and increase the Tm of DNA by approximately 40 degrees C. Sso7d in complex with GTAATTAC and GCGT(iU)CGC + GCGAACGC was crystallized in different crystal lattices and the crystal structures were solved at high resolution. Sso7d binds in the minor groove of DNA and causes a single-step sharp kink in DNA (approximately 60 degrees) by the intercalation of the hydrophobic side chains of Val 26 and Met 29. The intercalation sites are different in the two complexes. Observations of this novel DNA binding mode in three independent crystal lattices indicate that it is not a function of crystal packing." citations,references_11,5905,235244,11,,reference citation,,,9515968,,"Robinson H, Gao YG, McCrary BS, Edmondson SP, Shriver JW, Wang AH. Nature. 1998 Mar 12;392(6672):202-5.",The hyperthermophile chromosomal protein Sac7d sharply kinks DNA.,published,journal,Nature,Nature,392,6672,,0028-0836,,,,,,,,,,,,,,,,,,,,202,205,1998,"The proteins Sac7d and Sso7d belong to a class of small chromosomal proteins from the hyperthermophilic archaeon Sulfolobus acidocaldarius and S. solfactaricus, respectively. These proteins are extremely stable to heat, acid and chemical agents. Sac7d binds to DNA without any particular sequence preference and thereby increases its melting temperature by approximately 40 degrees C. We have now solved and refined the crystal structure of Sac7d in complex with two DNA sequences to high resolution. The structures are examples of a nonspecific DNA-binding protein bound to DNA, and reveal that Sac7d binds in the minor groove, causing a sharp kinking of the DNA helix that is more marked than that induced by any sequence-specific DNA-binding proteins. The kink results from the intercalation of specific hydrophobic side chains of Sac7d into the DNA structure, but without causing any significant distortion of the protein structure relative to the uncomplexed protein in solution." citations,references_12,5905,235245,12,,reference citation,,,9514720,,"McCrary BS, Bedell J, Edmondson SP, Shriver JW. J Mol Biol. 1998 Feb 13;276(1):203-24.",Linkage of protonation and anion binding to the folding of Sac7d.,published,journal,J. Mol. Biol.,Journal of molecular biology,276,1,,0022-2836,,,,,,,,,,,,,,,,,,,,203,224,1998,"The temperature, pH, and salt dependence of the folding of recombinant Sac7d from the hyperthermophile Sulfolobus acidocaldarius is mapped using multi-dimensional differential scanning calorimetry (DSC) and folding progress surfaces followed by circular dichroism. Linkage relations are derived to explain the observed dependencies, and it is shown that the data can be explained by the linkage of at least two protonation reactions and two anion binding sites to a two-state unfolding process. Circular dichroism spectra indicate that a native-like fold is stabilized at acid pH by anion binding. An apparent binding isotherm surface (folding progress versus pH and salt) is used to obtain intrinsic chloride binding constants as a function of pH for both sites. A saddle is predicted in the folding progress surface (progress versus temperature and pH) at low salt with a minimum near pH 2 and 20 degrees C with approximately 25% of the protein folded. The position of the saddle is sensitive to the intrinsic delta C degrees of unfolding and provides a third measure of delta C degrees independent of that obtained by a Kirchoff plot of DSC data and chemical denaturation. The observed enthalpy of unfolding approaches zero near the saddle making the unfolding largely invisible to DSC under these conditions. The linkage analysis demonstrates that the delta C degrees for unfolding obtained from a Kirchoff plot of DSC data should be distinguished from the intrinsic delta C degrees of unfolding. It is shown that the discrepancy between the free energy of unfolding for Sac7d obtained by DSC and that obtained by chemical denaturation may be explained by the linkage of protonation and anion binding to protein folding. The linkage analysis demonstrates the limitations of using the delta Hcal/ delta Hvh ratio an indication of two-state unfolding." citations,citation_1,5940,236036,2,,reference citation,,,14557255,,,"Direct determination of the interleukin-6 binding epitope of the interleukin-6 receptor by NMR spectroscopy",published,journal,J. Biol. Chem.,,279,1,,,,,,,,,,,,,,,,,,,,,,571,576,2004, citations,entry_citation,5941,236049,1,,entry citation,,,14640680,,,"Structure-based design of an indolicidin peptide analogue with increased protease stability",published,journal,Biochemistry,,42,48,,,,,,,,,,,,,,,,,,,,,,14130,14138,2003, citations,references_14,5905,235247,14,,reference citation,,,8980686,,"McCrary BS, Edmondson SP, Shriver JW. J Mol Biol. 1996 Dec 13;264(4):784-805.",Hyperthermophile protein folding thermodynamics: differential scanning calorimetry and chemical denaturation of Sac7d.,published,journal,J. Mol. Biol.,Journal of molecular biology,264,4,,0022-2836,,,,,,,,,,,,,,,,,,,,784,805,1996,"Recombinant Sac7d protein from the thermoacidophile Sulfolobus acidocaldarius is shown to be stable towards acid, thermal and chemical denaturation. The protein maintains a compact native fold between pH 0 and 10 in 0.3 M KCl and 25 degrees C as indicated by near and far UV circular dichroism spectra. Thermal unfolding followed by differential scanning calorimetry (DSC) occurs as a reversible, two-state transition from pH 0 to 10, with a maximal Tm of 90.7 degrees C between pH 5 and 9. At pH 0 the protein unfolds with a Tm of 63.3 degrees C. Plots of the enthalpy of unfolding as a function of Tm are linear and yield an anomalously low delta Cp of 497 (+/-20) cal deg-1 mol-1 using the Kirchhoff relation. Guanidine hydrochloride and urea-induced chemical denaturation of Sac7d occur reversibly and can be followed by circular dichroism. Global non-linear regression of the chemical denaturation data constrained by DSC determined values for delta Hm and Tm yields a delta Cp of unfolding of 858 (+/-21) cal deg-1 mol-1. The higher delta Cp is in good agreement with that predicted from the buried polar and apolar surface areas using the NMR solution structure. It is similar to values reported for mesophile proteins of comparable size, indicating that the packing and change in solvent-accessible surface area on unfolding are not unusual. Similarly, guanidine hydrochloride and urea m-values are in good agreement with those expected for a protein of 66 residues. Possible explanations for the difference in delta Cp determined by application of the Kirchhoff relation to DSC data and that determined by the global fit are discussed. Protein stability curves defined by either delta Cp values are similar to those observed for small mesophile proteins. Although the protein is thermally stable, it is marginally stable thermodynamically with a free energy of unfolding of 1.6 (+/-0.1) kcal mol-1 at the growth temperature of 80 degrees C. The large number of potential ion pairs on the surface of this hyperthermophile protein do not result in an inordinate increase in stability. Post-translational modification, possibly lysine monomethylation, appears to be the single most important stabilizing factor that distinguishes the native hyperthermophile protein from small mesophile proteins. Additional stabilization in vivo is expected from compatible osmolytes (polyamines) and DNA-binding." citations,references_15,5905,235248,15,,reference citation,,,8672437,,"McAfee JG, Edmondson SP, Zegar I, Shriver JW. Biochemistry. 1996 Apr 2;35(13):4034-45.",Equilibrium DNA binding of Sac7d protein from the hyperthermophile Sulfolobus acidocaldarius: fluorescence and circular dichroism studies.,published,journal,Biochemistry,Biochemistry,35,13,,0006-2960,,,,,,,,,,,,,,,,,,,,4034,4045,1996,"The thermodynamics of the binding of the Sac7d protein of Sulfolobus acidocaldarius to double-stranded DNA has been characterized using spectroscopic signals arising from both the protein and the DNA. Ligand binding density function analysis has been used to demonstrate that the fractional change in protein intrinsic tryptophan fluorescence quenching that occurs upon DNA binding is equal to the fraction of protein bound. Reverse titration data have been fit directly to the McGhee-von Hippel model [McGhee, J., & von Hippel, P. (1974) J. Mol. Biol. 86, 469-489] using nonlinear regression. Sac7d binds noncooperatively to poly(dGdC) x poly(dGdC) with an intrinsic affinity of 6.5 x 10(6) M(-1) and a site size of 4 base pairs in 1 mM KH2PO4 and 50 mM KC1 (pH 6.8). Some binding sequence preference is noted, with the binding to poly(dIdC) x poly(dIdC) over 10-fold stronger than to poly(DAdT) x poly(dAdT). The binding is largely driven by the polyelectrolyte effect and is consistent with a release of 4.4 monovalent cations from DNA upon complex formation or the formation of 5 ion pairs at the protein-DNA interface. Extrapolation of salt back-titration data to 1 M KC1 indicates a -2.2 kcal/mol nonelectrostatic contribution to the binding free energy. A van't Hoff analysis of poly(dGdC) x poly(dGdC) binding shows that the binding enthalpy is approximately zero and the process is entropically driven. The affinity decreases slightly between pH 5.4 and 8.0. There is no significant difference between the binding parameters of recombinant Sac7d and native Sac7 proteins, indicating that methylation of the native protein has no effect on the DNA binding function. The binding of Sac7d to various DNAs leads to a significant increase in the DNA long-wavelength circular dichroism (CD) band, the intensity of which shows a sigmoidal dependence on Sac7d concentration. The sigmoidal CD binding isotherm can be quantitatively modeled by a conformational transition in the DNA that is cooperatively induced when protein monomers are bound within a given number of base pairs, ranging from zero for poly(dIdC) x poly(dIdC) to 8 or less for poly(dAdG) x poly(dCdT)." citations,references_16,5905,235249,16,,reference citation,,,7577913,,"Edmondson SP, Qiu L, Shriver JW. Biochemistry. 1995 Oct 17;34(41):13289-304.",Solution structure of the DNA-binding protein Sac7d from the hyperthermophile Sulfolobus acidocaldarius.,published,journal,Biochemistry,Biochemistry,34,41,,0006-2960,,,,,,,,,,,,,,,,,,,,13289,13304,1995,"The Sac7 proteins from the hyperthermophile Sulfolobus acidocaldarius are a heterogeneous mixture of small, thermostable, nonspecific DNA-binding proteins. One of these proteins, Sac7d, has been overexpressed in Escherichia coli to provide a homogeneous preparation for structure, stability, and function studies. We present here essentially complete sequence-specific 1H NMR assignments for Sac7d, a delineation of secondary structural elements, and the high-resolution solution structure obtained from a full relaxation matrix refinement. The final structure provides an excellent fit to the NMR data with an NOE R-factor of 0.27 for backbone NOEs. The structure has a compact globular fold with 82% of the sequence involved in regular secondary structure: an antiparallel two-stranded beta-ribbon with a tight turn, followed by a short 3(10) helix, an antiparallel three-stranded beta-sheet, another short 3(10) helix, and finally four turns of alpha-helix. The amphipathic alpha-helix packs across the hydrophobic face of the three-stranded beta-sheet in an open-faced sandwich arrangement with at least one turn of the helix exposed beyond the sheet. The hydrophobic face of the beta-ribbon packs against a corner of the twisted beta-sheet. The single tryptophan responsible for the 88% fluorescence quenching upon DNA binding is exposed on the surface of the three-stranded beta-sheet. Lysines 5 and 7, whose monomethylation may be associated with enhanced thermostability, are highly solvent exposed along the inner edge of the two-stranded ribbon. The structure of Sac7d differs in many respects from that reported for the homologous native Sso7d [Baumann et al. (1994) Nature Struct. Biol. 1, 808] with a backbone RMSD greater than 3.0 A, largely due to the packing and length of the C-terminal alpha-helix which may be important in Sac7d DNA binding." citations,references_17,5905,235250,17,,reference citation,,,7632679,,"McAfee JG, Edmondson SP, Datta PK, Shriver JW, Gupta R. Biochemistry. 1995 Aug 8;34(31):10063-77.","Gene cloning, expression, and characterization of the Sac7 proteins from the hyperthermophile Sulfolobus acidocaldarius.",published,journal,Biochemistry,Biochemistry,34,31,,0006-2960,,,,,,,,,,,,,,,,,,,,10063,10077,1995,"The genes for two Sac7 DNA-binding proteins, Sac7d and Sac7e, from the extremely thermophilic archaeon Sulfolobus acidocaldarius have been cloned into Escherichia coli and sequenced. The sac7d and sac7e open reading frames encode 66 amino acid (7608 Da) and 65 amino acid (7469 Da) proteins, respectively. Southern blots indicate that these are the only two Sac7 protein genes in S. acidocaldarius, each present as a single copy. Sac7a, b, and c proteins appear to be carboxy-terminal modified Sac7d species. The transcription initiation and termination regions of the sac7d and sac7e genes have been identified along with the promoter elements. Potential ribosome binding sites have been identified downstream of the initiator codons. The sac7d gene has been expressed in E. coli, and various physical properties of the recombinant protein have been compared with those of native Sac7. The UV absorbance spectra and extinction coefficients, the fluorescence excitation and emission spectra, the circular dichroism, and the two-dimensional double-quantum filtered 1H NMR spectra of the native and recombinant species are essentially identical, indicating essentially identical local and global folds. The recombinant and native proteins bind and stabilize double-stranded DNA with a site size of 3.5 base pairs and an intrinsic binding constant of 2 x 10(7) M-1 for poly[dGdC].poly[dGdC] in 0.01 M KH2PO4 at pH 7.0. The availability of the recombinant protein permits a direct comparison of the thermal stabilities of the methylated and unmethylated forms of the protein. Differential scanning calorimetry demonstrates that the native protein is extremely thermostable and unfolds reversibly at pH 6.0 with a Tm of approximately 100 degrees C, while the recombinant protein unfolds at 92.7 degrees C." citations,entry_citation,5906,235270,1,,entry citation,,,14872138,,,"Letter to Editor: 1H, 15N, and 13C resonance Assignments of DARPP-32 (dopamine and cAMP-regulated phosphoprotein, Mr. 32,000) - a protein inhibitor of protein phosphatase-1",published,journal,J. Biomol. NMR,,28,4,,,,,,,,,,,,,,,,,,,,,,413,414,2004, citations,entry_citation,5907,235283,1,,entry citation,,,15016365,,,"Solution structure of the C-terminal domain of Ku80 suggests important sites for protein-protein interactions.",published,journal,Structure (Camb),,12,3,,,,,,,,,,,,,,,,,,,,,,495,502,2004, citations,references_1,5908,235305,2,,reference citation,,,12666159,,"Bosch D, Campillo M, Pardo L. J Comput Chem. 2003 Apr 30;24(6):682-91",Binding of proteins to the minor groove of DNA: what are the structural and energetic determinants for kinking a basepair step?,published,journal,,Journal of computational chemistry,24,6,,0192-8651,,,,,,,,,,,,,,,,,,,,682,691,2003,"The structural and energetic determinants for kinking a basepair step by minor groove-insertion of the protein side chains of PurR, LacI, LEF-1, IHF, Sac7d, and Sso7d, have been calculated by molecular dynamics/potential of mean force simulations. The structural determinants of the kinked structures are: two contiguous furanose rings achieve different conformations, in the region of C3'endo (A-DNA) and C2'endo (B-DNA); the chi torsion angle always takes values characteristic of the C2'endo conformation of B-DNA, independently of sugar puckering; and protein side chain insertion increases slide (from negative to positive values), rise, and roll, and decreases twist. The energetic determinants of DNA kinking are: the conformational transition of the sugar-phosphate backbone is not energetically demanding; the relative importance of the interbase parameters in the free energy penalty is slide, followed by twist and rise, and concluding with shift and roll; and the characteristic increase of roll and decrease of twist, upon side chain insertion, tends to stabilize the process of DNA kinking." citations,references_2,5908,235306,3,,reference citation,,,12060682,,"Napoli A, Zivanovic Y, Bocs C, Buhler C, Rossi M, Forterre P, Ciaramella M. Nucleic Acids Res. 2002 Jun 15;30(12):2656-62.","DNA bending, compaction and negative supercoiling by the architectural protein Sso7d of Sulfolobus solfataricus.",published,journal,Nucleic Acids Res.,Nucleic acids research,30,12,,1362-4962,,,,,,,,,,,,,,,,,,,,2656,2662,2002,"Members of the Sso7d/Sac7d family are small, abundant, non-specific DNA-binding proteins of the hyperthermophilic Archaea SULFOLOBUS: Crystal structures of these proteins in complex with oligonucleotides showed that they induce changes in the helical twist and marked DNA bending. On this basis they have been suggested to play a role in organising chromatin structures in these prokaryotes, which lack histones. We report functional in vitro assays to investigate the effects of the observed Sso7d-induced structural modifications on DNA geometry and topology. We show that binding of multiple Sso7d molecules to short DNA fragments induces significant curvature and reduces the stiffness of the complex. Sso7d induces negative supercoiling of DNA molecules of any topology (relaxed, positively or negatively supercoiled) and in physiological conditions of temperature and template topology. Binding of Sso7d induces compaction of positively supercoiled and relaxed DNA molecules, but not of negatively supercoiled ones. Finally, Sso7d inhibits the positive supercoiling activity of the thermophile-specific enzyme reverse gyrase. The proposed biological relevance of these observations is that these proteins might model the behaviour of DNA in constrained chromatin environments." citations,references_3,5908,235307,4,,reference citation,,,11398456,,"Edmondson SP, Shriver JW. Methods Enzymol. 2001;334:129-45.",DNA binding proteins Sac7d and Sso7d from Sulfolobus.,published,journal,Meth. Enzymol.,Methods in enzymology,334,,,0076-6879,,,,,,,,,,,,,,,,,,,,129,145,2001, citations,references_4,5908,235308,5,,reference citation,,,11106160,,"Bedell JL, McCrary BS, Edmondson SP, Shriver JW. Protein Sci. 2000 Oct;9(10):1878-88.",The acid-induced folded state of Sac7d is the native state.,published,journal,Protein Sci.,Protein science : a publication of the Protein Society,9,10,,0961-8368,,,,,,,,,,,,,,,,,,,,1878,1888,2000,"Sac7d unfolds at low pH in the absence of salt, with the greatest extent of unfolding obtained at pH 2. We have previously shown that the acid unfolded protein is induced to refold by decreasing the pH to 0 or by addition of salt (McCrary BS, Bedell J. Edmondson SP, Shriver JW, 1998, J Mol Biol 276:203-224). Both near-ultraviolet circular dichroism spectra and ANS fluorescence enhancements indicate that the acid- and salt-induced folded states have a native fold and are not molten globular. 1H,15N heteronuclear single quantum coherence NMR spectra confirm that the native, acid-, and salt-induced folded states are essentially identical. The most significant differences in amide 1H and 15N chemical shifts are attributed to hydrogen bonding to titrating carboxyl side chains and through-bond inductive effects. The 1H NMR chemical shifts of protons affected by ring currents in the hydrophobic core of the acid- and salt-induced folded states are identical to those observed in the native. The radius of gyration of the acid-induced folded state at pH 0 is shown to be identical to that of the native state at pH 7 by small angle X-ray scattering. We conclude that acid-induced collapse of Sac7d does not lead to a molten globule but proceeds directly to the native state. The folding of Sac7d as a function of pH and anion concentration is summarized with a phase diagram that is similar to those observed for other proteins that undergo acid-induced folding except that the A-state is encompassed by the native state. These results demonstrate that formation of a molten globule is not a general property of proteins that are refolded by acid." citations,references_5,5908,235309,6,,reference citation,,,11031116,,"Su S, Gao YG, Robinson H, Liaw YC, Edmondson SP, Shriver JW, Wang AH. J Mol Biol. 2000 Oct 27;303(3):395-403.",Crystal structures of the chromosomal proteins Sso7d/Sac7d bound to DNA containing T-G mismatched base-pairs.,published,journal,J. Mol. Biol.,Journal of molecular biology,303,3,,0022-2836,,,,,,,,,,,,,,,,,,,,395,403,2000,"Sso7d and Sac7d are two small chromatin proteins from the hyperthermophilic archaeabacterium Sulfolobus solfataricus and Sulfolobus acidocaldarius, respectively. The crystal structures of Sso7d-GTGATCGC, Sac7d-GTGATCGC and Sac7d-GTGATCAC have been determined and refined at 1.45 A, 2.2 A and 2.2 A, respectively, to investigate the DNA binding property of Sso7d/Sac7d in the presence of a T-G mismatch base-pair. Detailed structural analysis revealed that the intercalation site includes the T-G mismatch base-pair and Sso7d/Sac7d bind to that mismatch base-pair in a manner similar to regular DNA. In the Sso7d-GTGATCGC complex, a new inter-strand hydrogen bond between T2O4 and C14N4 is formed and well-order bridging water molecules are found. The results suggest that the less stable DNA stacking site involving a T-G mismatch may be a preferred site for protein side-chain intercalation." citations,entry_citation,5965,236549,1,,entry citation,,,15096633,,,"Solution structures of the C-terminal headpiece subdomains of human villin and advillin, evaluation of headpiece F-actin-binding requirements",published,journal,Protein Sci.,,13,5,,,,,,,,,,,,,,,,,,,,,,1276,1287,2004, citations,entry_citation,5966,236564,1,,entry citation,,,15096633,,,"Solution structures of the C-terminal headpiece subdomains of human villin and advillin, evaluation of headpiece F-actin-binding requirements",published,journal,Protein Sci.,,13,5,,,,,,,,,,,,,,,,,,,,,,1276,1287,2004, citations,entry_citation,5967,236579,1,,entry citation,,,12933791,,,"Solution structure of the mature HIV-1 protease monomer: Insight into the tertiary fold and stability of a precursor",published,journal,J. Biol. Chem.,,278,44,,,,,,,,,,,,,,,,,,,,,,43311,43319,2003, citations,entry_citation,5968,236597,1,,entry citation,,,14660664,,,"The NMR Structure Dematin Headpiece Reveals a Dynamic Loop that is Conformationally Altered Upon Phosphorylation at a Distal Site",published,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,references_6,5908,235310,7,,reference citation,,,8520220,,"Delaglio, F. et al. J. Biomol. NMR 6, 277-293 (1995).",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,references_7,5908,235311,8,,reference citation,,,10343384,,"Hunenberger PH, McCammon JA. Biophys Chem. 1999 Apr 5;78(1-2):69-88.",Effect of artificial periodicity in simulations of biomolecules under Ewald boundary conditions: a continuum electrostatics study.,published,journal,Biophys. Chem.,Biophysical chemistry,78,1-2,,0301-4622,,,,,,,,,,,,,,,,,,,,69,88,1999,"Ewald and related methods are nowadays routinely used in explicit-solvent simulations of biomolecules, although they impose an artificial periodicity in systems which are inherently non-periodic. The consequences of this approximation should be assessed, since they may crucially affect the reliability of computer simulations under Ewald boundary conditions. In the present study we use a method based on continuum electrostatics to investigate the nature and magnitude of possible periodicity-induced artifacts on the potentials of mean force for conformational equilibria in biomolecules. Three model systems and pathways are considered: polyalanine oligopeptides (unfolding), a DNA tetranucleotide (separation of the strands), and the protein Sac7d (conformations from a molecular dynamics simulation). Artificial periodicity may significantly affect these conformational equilibria, in each case stabilizing the most compact conformation of the biomolecule. Three factors enhance periodicity-induced artifacts: (i) a solvent of low dielectric permittivity; (ii) a solute size which is non-negligible compared to the size of the unit cell; and (iii) a non-neutral solute. Neither the neutrality of the solute nor the absence of charge pairs at distances exceeding half the edge of the unit cell do guarantee the absence of artifacts." citations,references_8,5908,235312,9,,reference citation,,,9917414,,"de Bakker PI, Hunenberger PH, McCammon JA. J Mol Biol. 1999 Jan 29;285(4):1811-30.",Molecular dynamics simulations of the hyperthermophilic protein sac7d from Sulfolobus acidocaldarius: contribution of salt bridges to thermostability.,published,journal,J. Mol. Biol.,Journal of molecular biology,285,4,,0022-2836,,,,,,,,,,,,,,,,,,,,1811,1830,1999,"Hyperthermophilic proteins often possess an increased number of surface salt bridges compared with their mesophilic homologues. However, salt bridges are generally thought to be of minor importance in protein stability at room temperature. In an effort to understand why this may no longer be true at elevated temperatures, we performed molecular dynamics simulations of the hyperthermophilic protein Sac7d at 300 K, 360 K, and 550 K. The three trajectories are stable on the nanosecond timescale, as evidenced by the analysis of several time-resolved properties. The simulations at 300 K and (to a lesser extent) 360 K are also compatible with nuclear Overhauser effect-derived distances. Raising the temperature from 300 K to 360 K results in a less favourable protein-solvent interaction energy, and a more favourable intraprotein interaction energy. Both effects are almost exclusively electrostatic in nature and dominated by contributions due to charged side-chains. The reduced solvation is due to a loss of spatial and orientational structure of water around charged side-chains, which is a consequence of the increased thermal motion in the solvent. The favourable change in the intraprotein Coulombic interaction energy is essentially due to the tightening of salt bridges. Assuming that charged side-chains are on average more distant from one another in the unfolded state than in the folded state, it follows that salt bridges may contribute to protein stability at elevated temperatures because (i) the solvation free energy of charged side-chains is more adversely affected in the unfolded state than in the folded state by an increase in temperature, and (ii) due to the tightening of salt bridges, unfolding implies a larger unfavourable increase in the intraprotein Coulombic energy at higher temperature. Possible causes for the unexpected stability of the protein at 550 K are also discussed." citations,references_10,5908,235313,10,,reference citation,,,9731772,,"Gao YG, Su SY, Robinson H, Padmanabhan S, Lim L, McCrary BS, Edmondson SP, Shriver JW, Wang AH. Nat Struct Biol. 1998 Sep;5(9):782-6.",The crystal structure of the hyperthermophile chromosomal protein Sso7d bound to DNA.,published,journal,Nat. Struct. Biol.,Nature structural biology,5,9,,1072-8368,,,,,,,,,,,,,,,,,,,,782,786,1998,"Sso7d and Sac7d are two small (approximately 7,000 Mr), but abundant, chromosomal proteins from the hyperthermophilic archaeabacteria Sulfolobus solfataricus and S. acidocaldarius respectively. These proteins have high thermal, acid and chemical stability. They bind DNA without marked sequence preference and increase the Tm of DNA by approximately 40 degrees C. Sso7d in complex with GTAATTAC and GCGT(iU)CGC + GCGAACGC was crystallized in different crystal lattices and the crystal structures were solved at high resolution. Sso7d binds in the minor groove of DNA and causes a single-step sharp kink in DNA (approximately 60 degrees) by the intercalation of the hydrophobic side chains of Val 26 and Met 29. The intercalation sites are different in the two complexes. Observations of this novel DNA binding mode in three independent crystal lattices indicate that it is not a function of crystal packing." citations,references_11,5908,235314,11,,reference citation,,,9515968,,"Robinson H, Gao YG, McCrary BS, Edmondson SP, Shriver JW, Wang AH. Nature. 1998 Mar 12;392(6672):202-5.",The hyperthermophile chromosomal protein Sac7d sharply kinks DNA.,published,journal,Nature,Nature,392,6672,,0028-0836,,,,,,,,,,,,,,,,,,,,202,205,1998,"The proteins Sac7d and Sso7d belong to a class of small chromosomal proteins from the hyperthermophilic archaeon Sulfolobus acidocaldarius and S. solfactaricus, respectively. These proteins are extremely stable to heat, acid and chemical agents. Sac7d binds to DNA without any particular sequence preference and thereby increases its melting temperature by approximately 40 degrees C. We have now solved and refined the crystal structure of Sac7d in complex with two DNA sequences to high resolution. The structures are examples of a nonspecific DNA-binding protein bound to DNA, and reveal that Sac7d binds in the minor groove, causing a sharp kinking of the DNA helix that is more marked than that induced by any sequence-specific DNA-binding proteins. The kink results from the intercalation of specific hydrophobic side chains of Sac7d into the DNA structure, but without causing any significant distortion of the protein structure relative to the uncomplexed protein in solution." citations,entry_citation,5969,236627,1,,entry citation,,,15640161,,,"Solution NMR structure investigation for releasing mechanism of neocarzinostatin chromophore from holoprotein.",published,journal,J. Biol. Chem.,,280,12,,,,,,,,,,,,,,,,,,,,,,11340,11346,2005, citations,references_12,5908,235315,12,,reference citation,,,9514720,,"McCrary BS, Bedell J, Edmondson SP, Shriver JW. J Mol Biol. 1998 Feb 13;276(1):203-24.",Linkage of protonation and anion binding to the folding of Sac7d.,published,journal,J. Mol. Biol.,Journal of molecular biology,276,1,,0022-2836,,,,,,,,,,,,,,,,,,,,203,224,1998,"The temperature, pH, and salt dependence of the folding of recombinant Sac7d from the hyperthermophile Sulfolobus acidocaldarius is mapped using multi-dimensional differential scanning calorimetry (DSC) and folding progress surfaces followed by circular dichroism. Linkage relations are derived to explain the observed dependencies, and it is shown that the data can be explained by the linkage of at least two protonation reactions and two anion binding sites to a two-state unfolding process. Circular dichroism spectra indicate that a native-like fold is stabilized at acid pH by anion binding. An apparent binding isotherm surface (folding progress versus pH and salt) is used to obtain intrinsic chloride binding constants as a function of pH for both sites. A saddle is predicted in the folding progress surface (progress versus temperature and pH) at low salt with a minimum near pH 2 and 20 degrees C with approximately 25% of the protein folded. The position of the saddle is sensitive to the intrinsic delta C degrees of unfolding and provides a third measure of delta C degrees independent of that obtained by a Kirchoff plot of DSC data and chemical denaturation. The observed enthalpy of unfolding approaches zero near the saddle making the unfolding largely invisible to DSC under these conditions. The linkage analysis demonstrates that the delta C degrees for unfolding obtained from a Kirchoff plot of DSC data should be distinguished from the intrinsic delta C degrees of unfolding. It is shown that the discrepancy between the free energy of unfolding for Sac7d obtained by DSC and that obtained by chemical denaturation may be explained by the linkage of protonation and anion binding to protein folding. The linkage analysis demonstrates the limitations of using the delta Hcal/ delta Hvh ratio an indication of two-state unfolding." citations,references_13,5908,235316,13,,reference citation,,,9224936,,"Kulms D, Schafer G, Hahn U. Biol Chem. 1997 Jun;378(6):545-51.",Overproduction of Sac7d and Sac7e reveals only Sac7e to be a DNA-binding protein with ribonuclease activity from the extremophilic archaeon Sulfolobus acidocaldarius.,published,journal,Biol. Chem.,Biological chemistry,378,6,,1431-6730,,,,,,,,,,,,,,,,,,,,545,551,1997,"Genomic DNA from Sulfolobus acidocaldarius was screened using a degenerate oligodeoxyribonucleotide, derived from the sequence of 16 N-terminal amino acids from SaRD protein. SaRD protein was previously isolated in our laboratory and identified as a protein from S. acidocaldarius exhibiting ribonuclease activity as well as DNA-binding properties. On the basis of Southern hybridization analysis two genes from S. acidocaldarius have been cloned, sequenced and overproduced in Escherichia coli. The deduced amino acid sequences revealed that one gene encodes Sac7d and the other one Sac7e; two small, previously described basic proteins from S. acidocaldarius, and furthermore the N-termini of Sac7e and SaRD are identical. Northern blot analysis demonstrated that the genes are transcribed separately. After expression of sac7d and sac7e genes in E. coli it was shown that only recombinant Sac7e protein exhibits RNase activity and is catalytically indistinguishable from SaRD protein. Western blot analysis using a polyclonal antiserum raised against purified SaRD protein further confirmed that Sac7e and SaRD are identical proteins endowed with RNase activity and DNA-binding properties. A new RNA cleavage mechanism has to be postulated for Sac7e since, in contrast to common RNases (e.g. RNase A and T1), no histidines are present in the amino acid sequence. Differences between the very closely related 7 kDa proteins from two Sulfolobus strains converting DNA-binding proteins into RNases are pointed out and discussed, whereas substitutions of Glu by Gln (S. solfataricus) or by Lys (S. acidocaldarius) seem to be crucial." citations,references_14,5908,235317,14,,reference citation,,,8980686,,"McCrary BS, Edmondson SP, Shriver JW. J Mol Biol. 1996 Dec 13;264(4):784-805.",Hyperthermophile protein folding thermodynamics: differential scanning calorimetry and chemical denaturation of Sac7d.,published,journal,J. Mol. Biol.,Journal of molecular biology,264,4,,0022-2836,,,,,,,,,,,,,,,,,,,,784,805,1996,"Recombinant Sac7d protein from the thermoacidophile Sulfolobus acidocaldarius is shown to be stable towards acid, thermal and chemical denaturation. The protein maintains a compact native fold between pH 0 and 10 in 0.3 M KCl and 25 degrees C as indicated by near and far UV circular dichroism spectra. Thermal unfolding followed by differential scanning calorimetry (DSC) occurs as a reversible, two-state transition from pH 0 to 10, with a maximal Tm of 90.7 degrees C between pH 5 and 9. At pH 0 the protein unfolds with a Tm of 63.3 degrees C. Plots of the enthalpy of unfolding as a function of Tm are linear and yield an anomalously low delta Cp of 497 (+/-20) cal deg-1 mol-1 using the Kirchhoff relation. Guanidine hydrochloride and urea-induced chemical denaturation of Sac7d occur reversibly and can be followed by circular dichroism. Global non-linear regression of the chemical denaturation data constrained by DSC determined values for delta Hm and Tm yields a delta Cp of unfolding of 858 (+/-21) cal deg-1 mol-1. The higher delta Cp is in good agreement with that predicted from the buried polar and apolar surface areas using the NMR solution structure. It is similar to values reported for mesophile proteins of comparable size, indicating that the packing and change in solvent-accessible surface area on unfolding are not unusual. Similarly, guanidine hydrochloride and urea m-values are in good agreement with those expected for a protein of 66 residues. Possible explanations for the difference in delta Cp determined by application of the Kirchhoff relation to DSC data and that determined by the global fit are discussed. Protein stability curves defined by either delta Cp values are similar to those observed for small mesophile proteins. Although the protein is thermally stable, it is marginally stable thermodynamically with a free energy of unfolding of 1.6 (+/-0.1) kcal mol-1 at the growth temperature of 80 degrees C. The large number of potential ion pairs on the surface of this hyperthermophile protein do not result in an inordinate increase in stability. Post-translational modification, possibly lysine monomethylation, appears to be the single most important stabilizing factor that distinguishes the native hyperthermophile protein from small mesophile proteins. Additional stabilization in vivo is expected from compatible osmolytes (polyamines) and DNA-binding." citations,references_15,5908,235318,15,,reference citation,,,8672437,,"McAfee JG, Edmondson SP, Zegar I, Shriver JW. Biochemistry. 1996 Apr 2;35(13):4034-45.",Equilibrium DNA binding of Sac7d protein from the hyperthermophile Sulfolobus acidocaldarius: fluorescence and circular dichroism studies.,published,journal,Biochemistry,Biochemistry,35,13,,0006-2960,,,,,,,,,,,,,,,,,,,,4034,4045,1996,"The thermodynamics of the binding of the Sac7d protein of Sulfolobus acidocaldarius to double-stranded DNA has been characterized using spectroscopic signals arising from both the protein and the DNA. Ligand binding density function analysis has been used to demonstrate that the fractional change in protein intrinsic tryptophan fluorescence quenching that occurs upon DNA binding is equal to the fraction of protein bound. Reverse titration data have been fit directly to the McGhee-von Hippel model [McGhee, J., & von Hippel, P. (1974) J. Mol. Biol. 86, 469-489] using nonlinear regression. Sac7d binds noncooperatively to poly(dGdC) x poly(dGdC) with an intrinsic affinity of 6.5 x 10(6) M(-1) and a site size of 4 base pairs in 1 mM KH2PO4 and 50 mM KC1 (pH 6.8). Some binding sequence preference is noted, with the binding to poly(dIdC) x poly(dIdC) over 10-fold stronger than to poly(DAdT) x poly(dAdT). The binding is largely driven by the polyelectrolyte effect and is consistent with a release of 4.4 monovalent cations from DNA upon complex formation or the formation of 5 ion pairs at the protein-DNA interface. Extrapolation of salt back-titration data to 1 M KC1 indicates a -2.2 kcal/mol nonelectrostatic contribution to the binding free energy. A van't Hoff analysis of poly(dGdC) x poly(dGdC) binding shows that the binding enthalpy is approximately zero and the process is entropically driven. The affinity decreases slightly between pH 5.4 and 8.0. There is no significant difference between the binding parameters of recombinant Sac7d and native Sac7 proteins, indicating that methylation of the native protein has no effect on the DNA binding function. The binding of Sac7d to various DNAs leads to a significant increase in the DNA long-wavelength circular dichroism (CD) band, the intensity of which shows a sigmoidal dependence on Sac7d concentration. The sigmoidal CD binding isotherm can be quantitatively modeled by a conformational transition in the DNA that is cooperatively induced when protein monomers are bound within a given number of base pairs, ranging from zero for poly(dIdC) x poly(dIdC) to 8 or less for poly(dAdG) x poly(dCdT)." citations,entry_citation,597,236645,1,,entry citation,,,,,"Steinmetz, Wayne E., Moonen, Chrit, Kumar, Anil, Lazdunski, Michel, Visser, Leon, Carlsson, Fritz H.H., Wuthrich, Kurt, ""1H Nuclear-Magnetic-Resonance Studies of the Conformation of Cardiotoxin VII2 from Naja mossambica mossambica,"" Eur. J. Biochem. 120, 467-475 (1981).","1H Nuclear-Magnetic-Resonance Studies of the Conformation of Cardiotoxin VII2 from Naja mossambica mossambica",published,journal,Eur. J. Biochem.,,120,,,,,,,,,,,,,,,,,,,,,,,467,475,1981, citations,entry_citation,5970,236658,1,,entry citation,,,14687565,,,"The Solution Structure of Ribosomal Protein L18 from Bacillus stearothermophilus",published,journal,J. Mol. Biol.,,335,3,,,,,,,,,,,,,,,,,,,,,,679,684,2004, citations,entry_citation,5971,236687,1,,entry citation,,,15243186,,,"Letter to the Editor: Backbone and side chain resonance assignments of domain III of tick-borne Langat flavivirus Envelope protein",published,journal,J. Biomol. NMR,,29,4,,,,,,,,,,,,,,,,,,,,,,535,536,2004, citations,references_16,5908,235319,16,,reference citation,,,7577913,,"Edmondson SP, Qiu L, Shriver JW. Biochemistry. 1995 Oct 17;34(41):13289-304.",Solution structure of the DNA-binding protein Sac7d from the hyperthermophile Sulfolobus acidocaldarius.,published,journal,Biochemistry,Biochemistry,34,41,,0006-2960,,,,,,,,,,,,,,,,,,,,13289,13304,1995,"The Sac7 proteins from the hyperthermophile Sulfolobus acidocaldarius are a heterogeneous mixture of small, thermostable, nonspecific DNA-binding proteins. One of these proteins, Sac7d, has been overexpressed in Escherichia coli to provide a homogeneous preparation for structure, stability, and function studies. We present here essentially complete sequence-specific 1H NMR assignments for Sac7d, a delineation of secondary structural elements, and the high-resolution solution structure obtained from a full relaxation matrix refinement. The final structure provides an excellent fit to the NMR data with an NOE R-factor of 0.27 for backbone NOEs. The structure has a compact globular fold with 82% of the sequence involved in regular secondary structure: an antiparallel two-stranded beta-ribbon with a tight turn, followed by a short 3(10) helix, an antiparallel three-stranded beta-sheet, another short 3(10) helix, and finally four turns of alpha-helix. The amphipathic alpha-helix packs across the hydrophobic face of the three-stranded beta-sheet in an open-faced sandwich arrangement with at least one turn of the helix exposed beyond the sheet. The hydrophobic face of the beta-ribbon packs against a corner of the twisted beta-sheet. The single tryptophan responsible for the 88% fluorescence quenching upon DNA binding is exposed on the surface of the three-stranded beta-sheet. Lysines 5 and 7, whose monomethylation may be associated with enhanced thermostability, are highly solvent exposed along the inner edge of the two-stranded ribbon. The structure of Sac7d differs in many respects from that reported for the homologous native Sso7d [Baumann et al. (1994) Nature Struct. Biol. 1, 808] with a backbone RMSD greater than 3.0 A, largely due to the packing and length of the C-terminal alpha-helix which may be important in Sac7d DNA binding." citations,references_17,5908,235320,17,,reference citation,,,7632679,,"McAfee JG, Edmondson SP, Datta PK, Shriver JW, Gupta R. Biochemistry. 1995 Aug 8;34(31):10063-77.","Gene cloning, expression, and characterization of the Sac7 proteins from the hyperthermophile Sulfolobus acidocaldarius.",published,journal,Biochemistry,Biochemistry,34,31,,0006-2960,,,,,,,,,,,,,,,,,,,,10063,10077,1995,"The genes for two Sac7 DNA-binding proteins, Sac7d and Sac7e, from the extremely thermophilic archaeon Sulfolobus acidocaldarius have been cloned into Escherichia coli and sequenced. The sac7d and sac7e open reading frames encode 66 amino acid (7608 Da) and 65 amino acid (7469 Da) proteins, respectively. Southern blots indicate that these are the only two Sac7 protein genes in S. acidocaldarius, each present as a single copy. Sac7a, b, and c proteins appear to be carboxy-terminal modified Sac7d species. The transcription initiation and termination regions of the sac7d and sac7e genes have been identified along with the promoter elements. Potential ribosome binding sites have been identified downstream of the initiator codons. The sac7d gene has been expressed in E. coli, and various physical properties of the recombinant protein have been compared with those of native Sac7. The UV absorbance spectra and extinction coefficients, the fluorescence excitation and emission spectra, the circular dichroism, and the two-dimensional double-quantum filtered 1H NMR spectra of the native and recombinant species are essentially identical, indicating essentially identical local and global folds. The recombinant and native proteins bind and stabilize double-stranded DNA with a site size of 3.5 base pairs and an intrinsic binding constant of 2 x 10(7) M-1 for poly[dGdC].poly[dGdC] in 0.01 M KH2PO4 at pH 7.0. The availability of the recombinant protein permits a direct comparison of the thermal stabilities of the methylated and unmethylated forms of the protein. Differential scanning calorimetry demonstrates that the native protein is extremely thermostable and unfolds reversibly at pH 6.0 with a Tm of approximately 100 degrees C, while the recombinant protein unfolds at 92.7 degrees C." citations,entry_citation,5909,235340,1,,entry citation,,,,,,"Thermodynamics of Hydrophobic Core Packing in the Thermophile Proteins Sac7d and Sso7d",in preparation,journal,J. Mol. Biol.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,references_1,5909,235341,2,,reference citation,,,11398456,,"Edmondson SP, Shriver JW. Methods Enzymol. 2001;334:129-45.",DNA binding proteins Sac7d and Sso7d from Sulfolobus.,published,journal,Meth. Enzymol.,Methods in enzymology,334,,,0076-6879,,,,,,,,,,,,,,,,,,,,129,145,2001, citations,references_2,5909,235342,3,,reference citation,,,11031116,,"Su S, Gao YG, Robinson H, Liaw YC, Edmondson SP, Shriver JW, Wang AH. J Mol Biol. 2000 Oct 27;303(3):395-403.",Crystal structures of the chromosomal proteins Sso7d/Sac7d bound to DNA containing T-G mismatched base-pairs.,published,journal,J. Mol. Biol.,Journal of molecular biology,303,3,,0022-2836,,,,,,,,,,,,,,,,,,,,395,403,2000,"Sso7d and Sac7d are two small chromatin proteins from the hyperthermophilic archaeabacterium Sulfolobus solfataricus and Sulfolobus acidocaldarius, respectively. The crystal structures of Sso7d-GTGATCGC, Sac7d-GTGATCGC and Sac7d-GTGATCAC have been determined and refined at 1.45 A, 2.2 A and 2.2 A, respectively, to investigate the DNA binding property of Sso7d/Sac7d in the presence of a T-G mismatch base-pair. Detailed structural analysis revealed that the intercalation site includes the T-G mismatch base-pair and Sso7d/Sac7d bind to that mismatch base-pair in a manner similar to regular DNA. In the Sso7d-GTGATCGC complex, a new inter-strand hydrogen bond between T2O4 and C14N4 is formed and well-order bridging water molecules are found. The results suggest that the less stable DNA stacking site involving a T-G mismatch may be a preferred site for protein side-chain intercalation." citations,references_3,5909,235343,4,,reference citation,,,9731772,,"Gao YG, Su SY, Robinson H, Padmanabhan S, Lim L, McCrary BS, Edmondson SP, Shriver JW, Wang AH. Nat Struct Biol. 1998 Sep;5(9):782-6.",The crystal structure of the hyperthermophile chromosomal protein Sso7d bound to DNA.,published,journal,Nat. Struct. Biol.,Nature structural biology,5,9,,1072-8368,,,,,,,,,,,,,,,,,,,,782,786,1998,"Sso7d and Sac7d are two small (approximately 7,000 Mr), but abundant, chromosomal proteins from the hyperthermophilic archaeabacteria Sulfolobus solfataricus and S. acidocaldarius respectively. These proteins have high thermal, acid and chemical stability. They bind DNA without marked sequence preference and increase the Tm of DNA by approximately 40 degrees C. Sso7d in complex with GTAATTAC and GCGT(iU)CGC + GCGAACGC was crystallized in different crystal lattices and the crystal structures were solved at high resolution. Sso7d binds in the minor groove of DNA and causes a single-step sharp kink in DNA (approximately 60 degrees) by the intercalation of the hydrophobic side chains of Val 26 and Met 29. The intercalation sites are different in the two complexes. Observations of this novel DNA binding mode in three independent crystal lattices indicate that it is not a function of crystal packing." citations,references_4,5909,235344,5,,reference citation,,,9515968,,"Robinson H, Gao YG, McCrary BS, Edmondson SP, Shriver JW, Wang AH. Nature. 1998 Mar 12;392(6672):202-5.",The hyperthermophile chromosomal protein Sac7d sharply kinks DNA.,published,journal,Nature,Nature,392,6672,,0028-0836,,,,,,,,,,,,,,,,,,,,202,205,1998,"The proteins Sac7d and Sso7d belong to a class of small chromosomal proteins from the hyperthermophilic archaeon Sulfolobus acidocaldarius and S. solfactaricus, respectively. These proteins are extremely stable to heat, acid and chemical agents. Sac7d binds to DNA without any particular sequence preference and thereby increases its melting temperature by approximately 40 degrees C. We have now solved and refined the crystal structure of Sac7d in complex with two DNA sequences to high resolution. The structures are examples of a nonspecific DNA-binding protein bound to DNA, and reveal that Sac7d binds in the minor groove, causing a sharp kinking of the DNA helix that is more marked than that induced by any sequence-specific DNA-binding proteins. The kink results from the intercalation of specific hydrophobic side chains of Sac7d into the DNA structure, but without causing any significant distortion of the protein structure relative to the uncomplexed protein in solution." citations,entry_citation,6017,237845,1,,entry citation,,,,,,Study on structure-activity relationship of S100C/A11 protein,published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,2004, citations,references_5,5909,235345,6,,reference citation,,,7577913,,"Edmondson SP, Qiu L, Shriver JW. Biochemistry. 1995 Oct 17;34(41):13289-304.",Solution structure of the DNA-binding protein Sac7d from the hyperthermophile Sulfolobus acidocaldarius.,published,journal,Biochemistry,Biochemistry,34,41,,0006-2960,,,,,,,,,,,,,,,,,,,,13289,13304,1995,"The Sac7 proteins from the hyperthermophile Sulfolobus acidocaldarius are a heterogeneous mixture of small, thermostable, nonspecific DNA-binding proteins. One of these proteins, Sac7d, has been overexpressed in Escherichia coli to provide a homogeneous preparation for structure, stability, and function studies. We present here essentially complete sequence-specific 1H NMR assignments for Sac7d, a delineation of secondary structural elements, and the high-resolution solution structure obtained from a full relaxation matrix refinement. The final structure provides an excellent fit to the NMR data with an NOE R-factor of 0.27 for backbone NOEs. The structure has a compact globular fold with 82% of the sequence involved in regular secondary structure: an antiparallel two-stranded beta-ribbon with a tight turn, followed by a short 3(10) helix, an antiparallel three-stranded beta-sheet, another short 3(10) helix, and finally four turns of alpha-helix. The amphipathic alpha-helix packs across the hydrophobic face of the three-stranded beta-sheet in an open-faced sandwich arrangement with at least one turn of the helix exposed beyond the sheet. The hydrophobic face of the beta-ribbon packs against a corner of the twisted beta-sheet. The single tryptophan responsible for the 88% fluorescence quenching upon DNA binding is exposed on the surface of the three-stranded beta-sheet. Lysines 5 and 7, whose monomethylation may be associated with enhanced thermostability, are highly solvent exposed along the inner edge of the two-stranded ribbon. The structure of Sac7d differs in many respects from that reported for the homologous native Sso7d [Baumann et al. (1994) Nature Struct. Biol. 1, 808] with a backbone RMSD greater than 3.0 A, largely due to the packing and length of the C-terminal alpha-helix which may be important in Sac7d DNA binding." citations,references_6,5909,235346,7,,reference citation,,,7632679,,"McAfee JG, Edmondson SP, Datta PK, Shriver JW, Gupta R. Biochemistry. 1995 Aug 8;34(31):10063-77.","Gene cloning, expression, and characterization of the Sac7 proteins from the hyperthermophile Sulfolobus acidocaldarius.",published,journal,Biochemistry,Biochemistry,34,31,,0006-2960,,,,,,,,,,,,,,,,,,,,10063,10077,1995,"The genes for two Sac7 DNA-binding proteins, Sac7d and Sac7e, from the extremely thermophilic archaeon Sulfolobus acidocaldarius have been cloned into Escherichia coli and sequenced. The sac7d and sac7e open reading frames encode 66 amino acid (7608 Da) and 65 amino acid (7469 Da) proteins, respectively. Southern blots indicate that these are the only two Sac7 protein genes in S. acidocaldarius, each present as a single copy. Sac7a, b, and c proteins appear to be carboxy-terminal modified Sac7d species. The transcription initiation and termination regions of the sac7d and sac7e genes have been identified along with the promoter elements. Potential ribosome binding sites have been identified downstream of the initiator codons. The sac7d gene has been expressed in E. coli, and various physical properties of the recombinant protein have been compared with those of native Sac7. The UV absorbance spectra and extinction coefficients, the fluorescence excitation and emission spectra, the circular dichroism, and the two-dimensional double-quantum filtered 1H NMR spectra of the native and recombinant species are essentially identical, indicating essentially identical local and global folds. The recombinant and native proteins bind and stabilize double-stranded DNA with a site size of 3.5 base pairs and an intrinsic binding constant of 2 x 10(7) M-1 for poly[dGdC].poly[dGdC] in 0.01 M KH2PO4 at pH 7.0. The availability of the recombinant protein permits a direct comparison of the thermal stabilities of the methylated and unmethylated forms of the protein. Differential scanning calorimetry demonstrates that the native protein is extremely thermostable and unfolds reversibly at pH 6.0 with a Tm of approximately 100 degrees C, while the recombinant protein unfolds at 92.7 degrees C." citations,entry_citation,5910,235365,1,,entry citation,,,15005619,,,"Thermodynamics of core hydrophobicity and packing in the hyperthermophile proteins Sac7d and Sso7d.",published,journal,Biochemistry,,43,10,,,,,,,,,,,,,,,,,,,,,,2840,2853,2004, citations,references_1,5910,235366,2,,reference citation,,,11398456,,"Edmondson SP, Shriver JW. Methods Enzymol. 2001;334:129-45.",DNA binding proteins Sac7d and Sso7d from Sulfolobus.,published,journal,Meth. Enzymol.,Methods in enzymology,334,,,0076-6879,,,,,,,,,,,,,,,,,,,,129,145,2001, citations,references_2,5910,235367,3,,reference citation,,,11031116,,"Su S, Gao YG, Robinson H, Liaw YC, Edmondson SP, Shriver JW, Wang AH. J Mol Biol. 2000 Oct 27;303(3):395-403.",Crystal structures of the chromosomal proteins Sso7d/Sac7d bound to DNA containing T-G mismatched base-pairs.,published,journal,J. Mol. Biol.,Journal of molecular biology,303,3,,0022-2836,,,,,,,,,,,,,,,,,,,,395,403,2000,"Sso7d and Sac7d are two small chromatin proteins from the hyperthermophilic archaeabacterium Sulfolobus solfataricus and Sulfolobus acidocaldarius, respectively. The crystal structures of Sso7d-GTGATCGC, Sac7d-GTGATCGC and Sac7d-GTGATCAC have been determined and refined at 1.45 A, 2.2 A and 2.2 A, respectively, to investigate the DNA binding property of Sso7d/Sac7d in the presence of a T-G mismatch base-pair. Detailed structural analysis revealed that the intercalation site includes the T-G mismatch base-pair and Sso7d/Sac7d bind to that mismatch base-pair in a manner similar to regular DNA. In the Sso7d-GTGATCGC complex, a new inter-strand hydrogen bond between T2O4 and C14N4 is formed and well-order bridging water molecules are found. The results suggest that the less stable DNA stacking site involving a T-G mismatch may be a preferred site for protein side-chain intercalation." citations,references_3,5910,235368,4,,reference citation,,,9731772,,"Gao YG, Su SY, Robinson H, Padmanabhan S, Lim L, McCrary BS, Edmondson SP, Shriver JW, Wang AH. Nat Struct Biol. 1998 Sep;5(9):782-6.",The crystal structure of the hyperthermophile chromosomal protein Sso7d bound to DNA.,published,journal,Nat. Struct. Biol.,Nature structural biology,5,9,,1072-8368,,,,,,,,,,,,,,,,,,,,782,786,1998,"Sso7d and Sac7d are two small (approximately 7,000 Mr), but abundant, chromosomal proteins from the hyperthermophilic archaeabacteria Sulfolobus solfataricus and S. acidocaldarius respectively. These proteins have high thermal, acid and chemical stability. They bind DNA without marked sequence preference and increase the Tm of DNA by approximately 40 degrees C. Sso7d in complex with GTAATTAC and GCGT(iU)CGC + GCGAACGC was crystallized in different crystal lattices and the crystal structures were solved at high resolution. Sso7d binds in the minor groove of DNA and causes a single-step sharp kink in DNA (approximately 60 degrees) by the intercalation of the hydrophobic side chains of Val 26 and Met 29. The intercalation sites are different in the two complexes. Observations of this novel DNA binding mode in three independent crystal lattices indicate that it is not a function of crystal packing." citations,references_4,5910,235369,5,,reference citation,,,9515968,,"Robinson H, Gao YG, McCrary BS, Edmondson SP, Shriver JW, Wang AH. Nature. 1998 Mar 12;392(6672):202-5.",The hyperthermophile chromosomal protein Sac7d sharply kinks DNA.,published,journal,Nature,Nature,392,6672,,0028-0836,,,,,,,,,,,,,,,,,,,,202,205,1998,"The proteins Sac7d and Sso7d belong to a class of small chromosomal proteins from the hyperthermophilic archaeon Sulfolobus acidocaldarius and S. solfactaricus, respectively. These proteins are extremely stable to heat, acid and chemical agents. Sac7d binds to DNA without any particular sequence preference and thereby increases its melting temperature by approximately 40 degrees C. We have now solved and refined the crystal structure of Sac7d in complex with two DNA sequences to high resolution. The structures are examples of a nonspecific DNA-binding protein bound to DNA, and reveal that Sac7d binds in the minor groove, causing a sharp kinking of the DNA helix that is more marked than that induced by any sequence-specific DNA-binding proteins. The kink results from the intercalation of specific hydrophobic side chains of Sac7d into the DNA structure, but without causing any significant distortion of the protein structure relative to the uncomplexed protein in solution." citations,entry_citation,6018,237861,1,,entry citation,,,,,,Study on structure-activity relationship of S100C/A11 protein,published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,2004, citations,references_5,5910,235370,6,,reference citation,,,7577913,,"Edmondson SP, Qiu L, Shriver JW. Biochemistry. 1995 Oct 17;34(41):13289-304.",Solution structure of the DNA-binding protein Sac7d from the hyperthermophile Sulfolobus acidocaldarius.,published,journal,Biochemistry,Biochemistry,34,41,,0006-2960,,,,,,,,,,,,,,,,,,,,13289,13304,1995,"The Sac7 proteins from the hyperthermophile Sulfolobus acidocaldarius are a heterogeneous mixture of small, thermostable, nonspecific DNA-binding proteins. One of these proteins, Sac7d, has been overexpressed in Escherichia coli to provide a homogeneous preparation for structure, stability, and function studies. We present here essentially complete sequence-specific 1H NMR assignments for Sac7d, a delineation of secondary structural elements, and the high-resolution solution structure obtained from a full relaxation matrix refinement. The final structure provides an excellent fit to the NMR data with an NOE R-factor of 0.27 for backbone NOEs. The structure has a compact globular fold with 82% of the sequence involved in regular secondary structure: an antiparallel two-stranded beta-ribbon with a tight turn, followed by a short 3(10) helix, an antiparallel three-stranded beta-sheet, another short 3(10) helix, and finally four turns of alpha-helix. The amphipathic alpha-helix packs across the hydrophobic face of the three-stranded beta-sheet in an open-faced sandwich arrangement with at least one turn of the helix exposed beyond the sheet. The hydrophobic face of the beta-ribbon packs against a corner of the twisted beta-sheet. The single tryptophan responsible for the 88% fluorescence quenching upon DNA binding is exposed on the surface of the three-stranded beta-sheet. Lysines 5 and 7, whose monomethylation may be associated with enhanced thermostability, are highly solvent exposed along the inner edge of the two-stranded ribbon. The structure of Sac7d differs in many respects from that reported for the homologous native Sso7d [Baumann et al. (1994) Nature Struct. Biol. 1, 808] with a backbone RMSD greater than 3.0 A, largely due to the packing and length of the C-terminal alpha-helix which may be important in Sac7d DNA binding." citations,references_6,5910,235371,7,,reference citation,,,7632679,,"McAfee JG, Edmondson SP, Datta PK, Shriver JW, Gupta R. Biochemistry. 1995 Aug 8;34(31):10063-77.","Gene cloning, expression, and characterization of the Sac7 proteins from the hyperthermophile Sulfolobus acidocaldarius.",published,journal,Biochemistry,Biochemistry,34,31,,0006-2960,,,,,,,,,,,,,,,,,,,,10063,10077,1995,"The genes for two Sac7 DNA-binding proteins, Sac7d and Sac7e, from the extremely thermophilic archaeon Sulfolobus acidocaldarius have been cloned into Escherichia coli and sequenced. The sac7d and sac7e open reading frames encode 66 amino acid (7608 Da) and 65 amino acid (7469 Da) proteins, respectively. Southern blots indicate that these are the only two Sac7 protein genes in S. acidocaldarius, each present as a single copy. Sac7a, b, and c proteins appear to be carboxy-terminal modified Sac7d species. The transcription initiation and termination regions of the sac7d and sac7e genes have been identified along with the promoter elements. Potential ribosome binding sites have been identified downstream of the initiator codons. The sac7d gene has been expressed in E. coli, and various physical properties of the recombinant protein have been compared with those of native Sac7. The UV absorbance spectra and extinction coefficients, the fluorescence excitation and emission spectra, the circular dichroism, and the two-dimensional double-quantum filtered 1H NMR spectra of the native and recombinant species are essentially identical, indicating essentially identical local and global folds. The recombinant and native proteins bind and stabilize double-stranded DNA with a site size of 3.5 base pairs and an intrinsic binding constant of 2 x 10(7) M-1 for poly[dGdC].poly[dGdC] in 0.01 M KH2PO4 at pH 7.0. The availability of the recombinant protein permits a direct comparison of the thermal stabilities of the methylated and unmethylated forms of the protein. Differential scanning calorimetry demonstrates that the native protein is extremely thermostable and unfolds reversibly at pH 6.0 with a Tm of approximately 100 degrees C, while the recombinant protein unfolds at 92.7 degrees C." citations,entry_citation,5911,235390,1,,entry citation,,,14967026,,,"NMR Solution Structure of a Peptide from the mdm-2 Binding Domain of the p53 Protein that is Selectively Cytotoxic to Cancer Cells",published,journal,Biochemistry,,43,7,,,,,,,,,,,,,,,,,,,,,,1854,1861,2004, citations,entry_citation,5912,235411,1,,entry citation,,,14672664,,,The 3D solution structure of the C-terminal region of Ku86 (Ku86CTR),published,journal,J. Mol. Biol.,,335,2,,,,,,,,,,,,,,,,,,,,,,573,582,2004, citations,entry_citation,5913,235434,1,,entry citation,,,15182366,,,"NMR solution structure of Cn12, a novel peptide from the Mexican scorpion Centruroides noxius with a typical beta-toxin sequence but with alpha-like physiological activity",published,journal,Eur. J. Biochem.,,271,12,,,,,,,,,,,,,,,,,,,,,,2504,2516,2004, citations,entry_citation,5914,235455,1,,entry citation,,,14990485,,,"A Multidimensional 1H NMR Investigation of the Conformation of Methionine-enkephalin in Fast-tumbling Bicelles",published,journal,Biophys. J.,,86,3,,,,,,,,,,,,,,,,,,,,,,1587,1600,2004, citations,entry_citation,5915,235474,1,,entry citation,,,14990485,,,"A Multidimensional 1H NMR Investigation of the Conformation of Methionine-enkephalin in Fast-tumbling Bicelles Conformation",published,journal,Biophys. J.,,86,3,,,,,,,,,,,,,,,,,,,,,,1587,1600,2004, citations,entry_citation,5916,235495,1,,entry citation,,,15134435,,,"How C-Terminal Carboxyamidation Alters the Biological Activity of Peptides from the Venom of the Eumenine Solitary WasP",published,journal,Biochemistry,,43,19,,,,,,,,,,,,,,,,,,,,,,5608,5617,2004, citations,entry_citation,5917,235519,1,,entry citation,,,,,,"Using condon optimization, chaperone co-expression, and rational mutagenesis for production and NMR assignments of Human eIF2a",published,journal,J. Biomol. NMR,,28,4,,,,,,,,,,,,,,,,,,,,,,357,367,2004, citations,entry_citation,5918,235534,1,,entry citation,,,15165855,,,"Multiple time-scale backbone dynamics of homologous thermophilic and mesophilic ribonuclease HI enzymes",published,journal,J. Mol. Biol.,,339,4,,,,,,,,,,,,,,,,,,,,,,855,871,2004, citations,Ref._1,5918,235535,2,,reference citation,,,10090773,,"Hollien J, Marqusee S. A thermodynamic comparison of mesophilic and thermophilic ribonucleases H. Biochemistry. 1999 Mar 23;38(12):3831-6.",A thermodynamic comparison of mesophilic and thermophilic ribonucleases H.,published,journal,Biochemistry,Biochemistry,38,12,,0006-2960,,,,,,,,,,,,,,,,,,,,3831,3836,1999,"The mechanisms by which thermophilic proteins attain their increased thermostability remain unclear, as usually the sequence and structure of these proteins are very similar to those of their mesophilic homologues. To gain insight into the basis of thermostability, we have determined protein stability curves describing the temperature dependence of the free energy of unfolding for two ribonucleases H, one from the mesophile Escherichia coli and one from the thermophile Thermus thermophilus. The circular dichroism signal was monitored as a function of temperature and guanidinium chloride concentration, and the resulting free energies of unfolding were fit to the Gibbs-Helmholtz equation to obtain a set of thermodynamic parameters for these proteins. Although the maximal stabilities for these proteins occur at similar temperatures, the heat capacity of unfolding for T. thermophilus RNase H is lower, resulting in a smaller temperature dependence of the free energy of unfolding and therefore a higher thermal melting temperature. In addition, the stabilities of these proteins are similar at the optimal growth temperatures for their respective organisms, suggesting that a balance of thermodynamic stability and flexibility is important for function." citations,entry_citation,5972,236714,1,,entry citation,,,14643666,,,"Solution Structure of the C-terminal Antiparallel Coiled-coil Domain of Escherichia Coli Osmosensor ProP",published,journal,J. Mol. Biol.,,334,5,,,,,,,,,,,,,,,,,,,,,,1063,1076,2003, citations,entry_citation,5973,236734,1,,entry citation,,,14993605,,,Solution Structure of Dengue Virus Capsid Protein Reveals another Fold,published,journal,Proc. Natl. Acad. Sci. U. S. A.,,101,10,,,,,,,,,,,,,,,,,,,,,,3414,3419,2004, citations,entry_citation,5974,236758,1,,entry citation,,,15014239,,,"Letter to the Editor: Assignment of the 1H, 13C and 15N resonances of the catalytic domain of guanine nucleotide exchange factor BopE from Burkholderia pseudomallei",published,journal,J. Biomol. NMR,,29,2,,,,,,,,,,,,,,,,,,,,,,215,216,2004, citations,Ref._2,5918,235536,3,,reference citation,,,10570131,,"Hollien J, Marqusee S. Structural distribution of stability in a thermophilic enzyme. Proc Natl Acad Sci U S A. 1999 Nov 23;96(24):13674-8.",Structural distribution of stability in a thermophilic enzyme.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,96,24,,0027-8424,,,,,,,,,,,,,,,,,,,,13674,13678,1999,"Stability parameters for individual residues in Thermus thermophilus cysteine-free RNase H were determined by native state hydrogen exchange, thus providing a unique comparison of regional thermodynamics between thermophilic and mesophilic homologues. The general distribution of stability in the thermophilic protein is similar to that of its mesophilic homologue, with a proportional increase in stability for almost all residues. As a consequence, the residue-specific stabilities of the two proteins are remarkably similar under conditions where their global stabilities are the same. These results indicate that T. thermophilus RNase H is stabilized in a delocalized fashion, preserving a finely tuned balance of stabilizing interactions throughout the structure. Therefore, although protein stability can be altered by single amino acid substitution, evolution for optimal function may require more subtle and delocalized mechanisms." citations,entry_citation,5919,235554,1,,entry citation,,,12527295,,,"The solution structure of the loop E region of the 5S rRNA from spinach chloroplasts",published,journal,J. Mol. Biol.,,325,,,,,,,,,,,,,,,,,,,,,,,843,856,2003, citations,entry_citation,5920,235585,1,,entry citation,,,14627811,,,"Solution structure and DNA binding of the effector domain from the global regulator PrrA (RegA) from R. sphaeroides: insights into binding specificity",published,journal,Nucleic Acids Res.,,31,23,,,,,,,,,,,,,,,,,,,,,,6778,6787,2003, citations,entry_citation,5921,235600,1,,entry citation,,,15017147,,,"Letter to the ditor: NMR assignment of TM1442, a putative anti-sigma factor antagonist from Thermotoga maritima",published,journal,J. Biomol. NMR,,29,1,,,,,,,,,,,,,,,,,,,,,,99,100,2004, citations,entry_citation,5922,235616,1,,entry citation,,,12902341,,,"Structure of the HERG K+ channel S5P extracellular linker: Role of an amphipathic alpha-helix in c-type inactivation",published,journal,J. Biol. Chem.,,278,43,,,,,,,,,,,,,,,,,,,,,,42136,42148,2003, citations,entry_citation,5923,235635,1,,entry citation,,,16300404,,,Structural comparison of the unstable drkN SH3 domain and a stable mutant,published,journal,Biochemistry,,44,47,,,,,,,,,,,,,,,,,,,,,,15550,15560,2005, citations,entry_citation,5924,235651,1,,entry citation,,,14662767,,,"NMR solution structure of the focal adhesion targeting domain of focal adhesion kinase in complex with a paxillin LD peptide: evidence for a two site binding model",published,journal,J. Biol. Chem.,,279,9,,,,,,,,,,,,,,,,,,,,,,8441,8451,2004, citations,entry_citation,5925,235681,1,,entry citation,,,16300404,,,Structural comparison of the unstable drkN SH3 domain and a stable mutant,published,journal,Biochemistry,,44,47,,,,,,,,,,,,,,,,,,,,,,15550,15560,2005, citations,entry_citation,5926,235697,1,,entry citation,,,11716736,,,"A Dipolar Coupling Based Strategy for Simultaneous Resonance Assignment and Structure Determination of Protein Backbones",published,journal,J. Am. Chem. Soc.,,123,47,,,,,,,,,,,,,,,,,,,,,,11791,11796,2001, citations,entry_citation,5927,235716,1,,entry citation,,,15212545,,,NMR Structure of a Cyclic Polyamide-DNA Complex,published,journal,J. Am. Chem. Soc.,,126,25,,,,,,,,,,,,,,,,,,,,,,7958,7966,2004, citations,entry_citation,5928,235735,1,,entry citation,,,15014234,,,"Letter to the Editor: NMR assignment of the hypothetical ENTH-VHS domain At3g16270 from Arabidopsis thaliana",published,journal,J. Biomol. NMR,,29,2,,,,,,,,,,,,,,,,,,,,,,205,206,2004, citations,entry_citation,5929,235765,1,,entry citation,,,15014235,,,"Letter to the Editor: NMR assignment of the hypothetical rhodanese domain At4g01050 from Arabidopsis thaliana",published,journal,J. Biomol. NMR,,29,2,,,,,,,,,,,,,,,,,,,,,,207,208,2004, citations,entry_citation,5930,235796,1,,entry citation,,,15014236,,,"Letter to the Editor: Backbone 1H, 15N and 13C resonance assignments of [agr]-ADT and [bgr]-ADT",published,journal,J. Biomol. NMR,,29,2,,,,,,,,,,,,,,,,,,,,,,209,210,2004, citations,citation_Wishart(1995),5930,235797,2,,reference citation,,,8589602,,"J. Biomol. NMR, 6 (1995) 135-140.","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,5931,235812,1,,entry citation,,,12534276,,,"Solution structure of the RNase H domain of the HIV-1 reverse transciptase in the presence of magnesium.",published,journal,Biochemistry,,42,3,,,,,,,,,,,,,,,,,,,,,,639,650,2003, citations,entry_citation,5932,235841,1,,entry citation,,,14624001,,,"YNMG tetraloop formation by a dyskeratosis congenita mutation in human telomerase RNA",published,journal,RNA,,9,12,,,,,,,,,,,,,,,,,,,,,,1446,1455,2003, citations,entry_citation,5933,235873,1,,entry citation,,,15544813,,,"Solution structure of the dimeric SAM domain of MAPKKK Ste11 and its interactions with the adaptor protein Ste50 from the budding yeast: implications for Ste11 activation and signal transmission through the Ste50-Ste11 complex",published,journal,J. Mol. Biol.,,344,4,,,,,,,,,,,,,,,,,,,,,,1071,1087,2004, citations,entry_citation,5934,235901,1,,entry citation,,,12149447,,,"De novo determination of peptide structure with solid-state magic-angle spinning NMR spectroscopy",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,99,,,,,,,,,,,,,,,,,,,,,,,10260,10265,2002, citations,entry_citation,5935,235916,1,,entry citation,,,,,,"Sequence-specific 1H, 13C and 15N resonance assignments of rat liver fructose-2,6-bisphosphatase domain",published,journal,J. Biomol. NMR,,27,3,,,,,,,,,,,,,,,,,,,,,,281,282,2003, citations,entry_citation,5975,236771,1,,entry citation,,,12767223,,,"Effect of temperature and the F27W mutation on the Ca2+ activated structural transition of trout cardiac troponin C",published,journal,Biochemistry,,42,21,,,,,,,,,,,,,,,,,,,,,,6418,6426,2003, citations,entry_citation,5976,236797,1,,entry citation,,,15213465,,,"Letter to the Editor: 1H-, 13C- and 15N-NMR assignment of the conserved hypothetical protein TM0487 from Thermotoga maritima",published,journal,J. Biomol. NMR,,29,3,,,,,,,,,,,,,,,,,,,,,,453,454,2004, citations,entry_citation,5977,236811,1,,entry citation,,,15263836,,,"NMR for Structural Proteomics of Thermotoga maritima: Screening and Sructure Determination",published,journal,J. Struct. Funct. Genomics,,5,3,,,,,,,,,,,,,,,,,,,,,,205,215,2004, citations,entry_citation,5978,236832,1,,entry citation,,,15247283,,,"Structure and function of the membrane anchor domain of hepatitis C virus nonstructural protein 5A",published,journal,J. Biol. Chem.,,279,39,,,,,,,,,,,,,,,,,,,,,,40835,40843,2004, citations,entry_citation,5979,236856,1,,entry citation,,,,,,"A Parallel Stranded DNA Duplex with an A-G Mismatch Base-Pair: (Ccataatttacc:Cctatgaaatcc)",published,journal,Recent Trends in Biophys. Res.,,,,,,,,,,,,,,,,,,,,,,,,,1,,2004, citations,ref_1,5935,235917,2,,reference citation,,,8520220,,"Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR. 1995 Nov;6(3):277-93.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref_2,5935,235918,3,,reference citation,,,,,"Johnson, B. A., and Blevins, R. A. (1994) J.Biomol.NMR 4, 603-614.",,published,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_3,5935,235919,4,,reference citation,,,8634242,,"Lee, Y. H., Ogata, C., Pflugrath, J. W., Levitt, D. G., Sarma, R., Banaszak, L. J., and Pilkis, S. J. (1996) Biochemistry 35(19), 6010-9.","Crystal structure of the rat liver fructose-2,6-bisphosphatase based on selenomethionine multiwavelength anomalous dispersion phases.",published,journal,Biochemistry,Biochemistry,35,19,,0006-2960,,,,,,,,,,,,,,,,,,,,6010,6019,1996,"The crystal structure of the recombinant fructose-2,6-bisphosphatase domain, which covers the residues between 251 and 440 of the rat liver bifunctional enzyme, 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase, was determined by multiwavelength anomalous dispersion phasing and refined at 2.5 A resolution. The selenomethionine-substituted protein was induced in the methionine auxotroph, Escherichia coli DL41DE3, purified, and crystallized in a manner similar to that of the native protein. Phase information was calculated using the multiwavelength anomalous dispersion data collected at the X-ray wavelengths near the absorption edge of the K-shell alpha electrons of selenium. The fructose-2,6-bisphosphatase domain has a core alpha/beta structure which consists of six stacked beta-strands, four parallel and two antiparallel. The core beta-sheet is surrounded by nine alpha-helices. The catalytic site, as defined by a bound phosphate ion, is positioned near the C-terminal end of the beta-sheet and close to the N-terminal end of an alpha-helix. The active site pocket is funnel-shaped. The narrow opening of the funnel is wide enough for a water molecule to pass. The key catalytic residues, including His7, His141, and Glu76, are near each other at the active site and probably function as general acids and/or bases during a catalytic cycle. The inorganic phosphate molecule is bound to an anion trap formed by Arg6, His7, Arg56, and His141. The core structure of the Fru-2,6-P2ase is similar to that of the yeast phosphoglycerate mutase and the rat prostatic acid phosphatase. However, the structure of one of the loops near the active site is completely different from the other family members, perhaps reflecting functional differences and the nanomolar range affinity of Fru-2,6-P2ase for its substrate. The imidazole rings of the two key catalytic residues, His7 and His141, are not parallel as in the yeast phosphoglycerate mutase. The crystal structure is used to interpret the existing chemical data already available for the bisphosphatase domain. In addition, the crystal structure is compared with two other proteins that belong to the histidine phosphatase family." citations,ref_4,5935,235920,5,,reference citation,,,8805587,,"Hasemann, C. A., Istvan, E. S., Uyeda, K., and Deisenhofer, J. (1996) Structure 4(9), 1017-29.","The crystal structure of the bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase reveals distinct domain homologies.",published,journal,Structure,"Structure (London, England : 1993)",4,9,,0969-2126,,,,,,,,,,,,,,,,,,,,1017,1029,1996,"BACKGROUND. Glucose homeostasis is maintained by the processes of glycolysis and gluconeogenesis. The importance of these pathways is demonstrated by the severe and life threatening effects observed in various forms of diabetes. The bifunctional enzyme 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase catalyzes both the synthesis and degradation of fructose-2,6-bisphosphate, a potent regulator of glycolysis. Thus this bifunctional enzyme plays an indirect yet key role in the regulation of glucose metabolism. RESULTS. We have determined the 2.0 A crystal structure of the rat testis isozyme of this bifunctional enzyme. The enzyme is a homodimer of 55 kDa subunits arranged in a head-to-head fashion, with each monomer consisting of independent kinase and phosphatase domains. The location of ATPgammaS and inorganic phosphate in the kinase and phosphatase domains, respectively, allow us to locate and describe the active sites of both domains. CONCLUSIONS. The kinase domain is clearly related to the superfamily of mononucleotide binding proteins, with a particularly close relationship to the adenylate kinases and the nucleotide-binding portion of the G proteins. This is in disagreement with the broad speculation that this domain would resemble phosphofructokinase. The phosphatase domain is structurally related to a family of proteins which includes the cofactor independent phosphoglycerate mutases and acid phosphatases." citations,entry_citation,5936,235939,1,,entry citation,,,15014236,,,"Letter to the Editor: Backbone 1H, 15N and 13C resonance assignments of [agr]-ADT and [bgr]-ADT",published,journal,J. Biomol. NMR,,29,2,,,,,,,,,,,,,,,,,,,,,,209,210,2004, citations,citation_Wishart(1995),5936,235940,2,,reference citation,,,8589602,,"J. Biomol. NMR, 6 (1995) 135-140.","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,5937,235955,1,,entry citation,,,14596806,,,"Structure determination and ligand interactions of the PDZ2b domain of PTP-Bas (hPTP1E): Splicing-induced modulation of ligand specificity",published,journal,J. Mol. Biol.,,334,1,,,,,,,,,,,,,,,,,,,,,,143,155,2003, citations,entry_citation,5938,235984,1,,entry citation,,,,,,"Structure-based design of an indolicidin peptide analog with increased protease stability",submitted,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,reference_1,5938,235985,2,,reference citation,,,11123901,,"Rozek A, Friedrich CL, Hancock RE. Biochemistry. 2000 Dec 26;39(51):15765-74.",,published,journal,Biochemistry,,39,51,,,,,,,,,,,,,,,,,,,,,,15765,15774,2000, citations,entry_citation,5939,236001,1,,entry citation,,,15213456,,,"Letter to the Editor: 1H, 13C and 15N resonance assignment of the human Spred2 EVH1 domain",published,journal,J. Biomol. NMR,,29,3,,,,,,,,,,,,,,,,,,,,,,435,436,2004, citations,entry_citation,5940,236035,1,,entry citation,,,,,,"Letter to the Editor: 1H, 15N, 13C Backbone Assignment of the Carboxyl Terminal Domain of the Cytokine Binding Module of the Interleukin-6 Receptor",published,journal,J. Biomol. NMR,,29,3,,,,,,,,,,,,,,,,,,,,,,407,408,2004, citations,reference_1,5941,236050,2,,reference citation,,,11123901,,"Rozek A, Friedrich CL, Hancock RE. Biochemistry. 2000 Dec 26;39(51):15765-74.",Structure of the bovine antimicrobial peptide indolicidin bound to dodecylphosphocholine and sodium dodecyl sulfate micelles.,published,journal,Biochemistry,Biochemistry,39,51,,0006-2960,,,,,,,,,,,,,,,,,,,,15765,15774,2000,"Indolicidin is a cationic, 13-residue antimicrobial peptide (ILPWKWPWWPWRR-NH(2)) which is unusually rich in tryptophan and proline. Its antimicrobial action involves the bacterial cytoplasmic membrane. Fluorescence and circular dichroism spectra demonstrated the structural similarity of indolicidin in complexes with large unilamellar phospolipid vesicles and with detergent micelles. The structure of indolicidin bound to zwitterionic dodecylphosphocholine (DPC) and anionic sodium dodecyl sulfate (SDS) micelles was determined using NMR methods and shown to represent a unique membrane-associated peptide structure. The backbone structure in DPC, well defined between residues 3 and 11, was extended, with two half-turns at residues Lys-5 and Trp-8. The backbone structure in SDS, well defined between residues 5 and 11, was also extended, but lacked the bend in the C-terminal half. Indolicidin in complexes with DPC had a central hydrophobic core composed of proline and tryptophan, which was bracketed by positively charged regions near the peptide termini. The tryptophan side chains, with one exception, folded flat against the peptide backbone, thus giving the molecule a wedge shape. Indolicidin in complexes with SDS had an arrangement of hydrophobic and cationic regions similar to that found in the presence of DPC. The tryptophan side chains were less well defined than for indolicidin in DPC and extended away from the peptide backbone. The preferred location of indolicidin in DPC micelles and lipid bilayers, analyzed using spin-label probes, was at the membrane interface." citations,entry_citation,5942,236066,1,,entry citation,,,15017148,,,"Letter to the Editor: NMR assignment of the hypothetical protein HI0004 from Haemophilus Influenzae - a putative essential gene product",published,journal,J. Biomol. NMR,,29,1,,,,,,,,,,,,,,,,,,,,,,101,102,2004, citations,ref_1,5942,236067,2,,reference citation,,,7542800,,"Whole-genome random sequencing and assembley of Haemophilus influenzae Rd. Science 269 July 28 496-512 (1995).",Whole-genome random sequencing and assembly of Haemophilus influenzae Rd.,published,journal,Science,"Science (New York, N.Y.)",269,5223,,0036-8075,,,,,,,,,,,,,,,,,,,,496,512,1995,"An approach for genome analysis based on sequencing and assembly of unselected pieces of DNA from the whole chromosome has been applied to obtain the complete nucleotide sequence (1,830,137 base pairs) of the genome from the bacterium Haemophilus influenzae Rd. This approach eliminates the need for initial mapping efforts and is therefore applicable to the vast array of microbial species for which genome maps are unavailable. The H. influenzae Rd genome sequence (Genome Sequence DataBase accession number L42023) represents the only complete genome sequence from a free-living organism." citations,entry_citation,5943,236080,1,,entry citation,,,15452438,,,"Letter to the Editor: 1H, 13C and 15N chemical shift assignments of the D2 domain of the fibroblast growth factor.",published,journal,J. Biomol. NMR,,30,1,,,,,,,,,,,,,,,,,,,,,,99,100,2004, citations,entry_citation,5944,236103,1,,entry citation,,,14500983,,,A Zinc Clasp Structure Tethers Lck to T Cell Coreceptors CD4 and CD8,published,journal,"Science (Washington, DC, U. S.)",,301,5640,,,,,,,,,,,,,,,,,,,,,,1725,1728,2003, citations,entry_citation,5945,236139,1,,entry citation,,,14500983,,,A Zinc Clasp Structure Tethers Lck to T Cell Coreceptors CD4 and CD8,published,journal,"Science (Washington, DC, U. S.)",,301,5640,,,,,,,,,,,,,,,,,,,,,,1725,1728,2003, citations,entry_citation,5946,236173,1,,entry citation,,,15213444,,,"Letter to the Editor: Complete resonance assignments of the ""donor-strand complemented"" AfaD: the afimbrial invasin from Diffusely Adherent E. coli",published,journal,J. Biomol. NMR,,29,3,,,,,,,,,,,,,,,,,,,,,,411,412,2004, citations,ref_1,5946,236174,2,,reference citation,,,8002584,,"Garcia MI, Labigne A, Le Bouguenec C. Nucleotide sequence of the afimbrial-adhesin-encoding afa-3 gene cluster and its translocation via flanking IS1 insertion sequences. J Bacteriol. 1994 Dec;176(24):7601-13.",Nucleotide sequence of the afimbrial-adhesin-encoding afa-3 gene cluster and its translocation via flanking IS1 insertion sequences.,published,journal,J. Bacteriol.,Journal of bacteriology,176,24,,0021-9193,,,,,,,,,,,,,,,,,,,,7601,7613,1994,"The afa gene clusters encode afimbrial adhesins (AFAs) that are expressed by uropathogenic and diarrhea-associated Escherichia coli strains. The plasmid-borne afa-3 gene cluster is responsible for the biosynthesis of the AFA-III adhesin that belongs to the Dr family of hemagglutinins. Reported in this work is the nucleotide sequence of the 9.2-kb insert of the recombinant plasmid pILL61, which contains the afa-3 gene cluster cloned from a cystitis-associated E. coli strain (A30). The afa-3 gene cluster was shown to contain six open reading frames, designated afaA to afaF. It was organized in two divergent transcriptional units. Five of the six Afa products showed marked homologies with proteins encoded by previously described adhesion systems that allowed us to attribute to each of them a putative function in the biogenesis of the AFA-III adhesin. AfaE was identified as the structural adhesin product, whereas AfaB and AfaC were recognized as periplasmic chaperone and outer membrane anchor proteins, respectively. The AfaA and AfaF products were shown to be homologous to the PapI-PapB transcriptional regulatory proteins. No function could be attributed to the AfaD product, the gene of which was previously shown to be dispensable for the synthesis of a functional adhesin. Upstream of the afa-3 gene cluster, a 1.2-kb region was found to be 96% identical to the RepFIB sequence of one of the enterotoxigenic E. coli plasmids (P307), suggesting a common ancestor plasmid. This region contains an integrase-like gene (int). Sequence analysis revealed the presence of an IS1 element between the int gene and the afa-3 gene cluster. Two other IS1 elements were detected and located in the vicinity of the afa-3 gene cluster by hybridization experiments. The afa-3 gene cluster was therefore found to be flanked by two IS1 elements in direct orientation and two in opposite orientations. The afa-3 gene cluster, flanked by two directly oriented IS1 elements, was shown to translocate from a recombinant plasmid to the E. coli chromosome. This translocation event occurred via IS1-specific recombination mediated by a recA-independent mechanism." citations,entry_citation,5947,236187,1,,entry citation,,,15213443,,,"Letter to the Editor: Complete resonance assignments of a 'donor strand complemented' AfaE: The afimbrial adhesin from Diffusely Adherent E. coli",published,journal,J. Biomol. NMR,,29,3,,,,,,,,,,,,,,,,,,,,,,409,410,2004, citations,entry_citation,598,236875,1,,entry citation,,,,,"Steinmetz, Wayne E., Moonen, Chrit, Kumar, Anil, Lazdunski, Michel, Visser, Leon, Carlsson, Fritz H.H., Wuthrich, Kurt, ""1H Nuclear-Magnetic-Resonance Studies of the Conformation of Cardiotoxin VII2 from Naja mossambica mossambica,"" Eur. J. Biochem. 120, 467-475 (1981).","1H Nuclear-Magnetic-Resonance Studies of the Conformation of Cardiotoxin VII2 from Naja mossambica mossambica",published,journal,Eur. J. Biochem.,,120,,,,,,,,,,,,,,,,,,,,,,,467,475,1981, citations,entry_citation,5980,236888,1,,entry citation,,,15476802,,,"Mutational and structural analysis of stem-loop IIIC of the hepatitis C virus and GB virus B internal ribosome entry sites.",published,journal,J. Mol. Biol.,,343,4,,,,,,,,,,,,,,,,,,,,,,805,817,2004, citations,entry_citation,6019,237875,1,,entry citation,,,18821773,,,A Stabilizing alpha/beta-Hydrophobic Core Greatly Contributes to Hyperthermostability of Archaeal [P62A]Ssh10b,published,journal,Biochemistry,Biochemistry,47,43,,,,,,,,,,,,,,,,,,,,,,11212,11221,2008, citations,ref_1,6019,237876,2,,reference citation,,,14523014,,,Two Conformations of Archaeal Ssh10b. The Origin of Its Temperature-dependent Interaction with DNA,published,journal,J. Biol. Chem.,The Journal of Biological Chemistry,278,51,,,,,,,,,,,,,,,,,,,,,,51015,51022,2003, citations,ref_1,5947,236188,2,,reference citation,,,12538267,,"J.P. Linge, M. Habeck, W. Rieping and M. Nilges (2003). ARIA: automated NOE assignment and NMR structure calculation. Bioinformatics 19, 315-316.",ARIA: automated NOE assignment and NMR structure calculation.,published,journal,Bioinformatics,"Bioinformatics (Oxford, England)",19,2,,1367-4803,,,,,,,,,,,,,,,,,,,,315,316,2003,"MOTIVATION: In the light of several ongoing structural genomics projects, faster and more reliable methods for structure calculation from NMR data are in great demand. The major bottleneck in the determination of solution NMR structures is the assignment of NOE peaks (nuclear Overhauser effect). Due to the high complexity of the assignment problem, most NOEs cannot be directly converted into unambiguous inter-proton distance restraints. RESULTS: We present version 1.2 of our program ARIA (Ambiguous Restraints for Iterative Assignment) for automated assignment of NOE data and NMR structure calculation. We summarize recent progress in correcting for spin diffusion with a relaxation matrix approach, representing non-bonded interactions in the force field and refining final structures in explicit solvent. We also discuss book-keeping, data exchange with spectra assignment programs and deposition of the analysed experimental data to the databases. AVAILABILITY: ARIA 1.2 is available from: http://www.pasteur.fr/recherche/unites/Binfs/aria/. SUPPLEMENTARY INFORMATION: XML DTDs (for chemical shifts and NOE crosspeaks), Python scripts for the conversion of various NMR data formats and the results of example calculations using data from the S. cerevisiae HRDC domain are available from: http://www.pasteur.fr/recherche/unites/Binfs/aria/" citations,entry_citation,5948,236213,1,,entry citation,,,,,,"Structure Analysis of Integrin alpha IIb beta 3 - Specific Disintegrin with the AKGDWN Motif",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_1,5948,236214,2,,reference citation,,,11340665,,"Guo RT, Chou LJ, Chen YC, Chen CY, Pari K, Jen CJ, Lo SJ, Huang SL, Lee CY, Chang TW, Chaung WJ. Expression in Pichia pastoris and characterization by circular dichroism and NMR of rhodostomin. Proteins. 2001 Jun 1;43(4):499-508.",Expression in Pichia pastoris and characterization by circular dichroism and NMR of rhodostomin.,published,journal,Proteins,Proteins,43,4,,0887-3585,,,,,,,,,,,,,,,,,,,,499,508,2001,"Rhodostomin (Rho) is a snake venom protein isolated from Calloselasma rhodostoma. Rho is a disintegrin that inhibits platelet aggregation by blocking the binding of fibrinogen to the integrin alpha(IIb)beta3 of platelets. Rho produced in Escherichia coli inhibited platelet aggregation with a K(I) value of 263 nM. Although functional, Rho produced in E. coli is misfolded based on our 2D and 3D NMR studies. In order to correct the folding problem, Rho was expressed in Pichia pastoris. The recombinant Rho expressed in P. pastoris inhibited platelet aggregation with a resulting K(I) value of 70 nM. This is the same potency as that of native Rho. CD analysis showed that the secondary structures of Rho are pH-independent and contain 3.5-7.9% alpha-helix, 48.2-50.5% beta-structures, and 42.3-47% coil. The sequential assignment and structure analysis of Rho were obtained using 2D and 3D 15N-edited NMR spectra. These results provide the first direct evidence that highly disulfide-bonded disintegrin can be expressed in P. pastoris with the correct fold. This evidence may serve as the basis for exploring the structure and function relationships as well as the dynamics of disintegrin and its variants." citations,entry_citation,5949,236238,1,,entry citation,,,,,,"Structure Analysis of Integrin alpha IIb beta 3 - Specific Disintegrin with the AKGDWN Motif",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_1,5949,236239,2,,reference citation,,,11340665,,"Guo RT, Chou LJ, Chen YC, Chen CY, Pari K, Jen CJ, Lo SJ, Huang SL, Lee CY, Chang TW, Chaung WJ. Expression in Pichia pastoris and characterization by circular dichroism and NMR of rhodostomin. Proteins. 2001 Jun 1;43(4):499-508.",Expression in Pichia pastoris and characterization by circular dichroism and NMR of rhodostomin.,published,journal,Proteins,Proteins,43,4,,0887-3585,,,,,,,,,,,,,,,,,,,,499,508,2001,"Rhodostomin (Rho) is a snake venom protein isolated from Calloselasma rhodostoma. Rho is a disintegrin that inhibits platelet aggregation by blocking the binding of fibrinogen to the integrin alpha(IIb)beta3 of platelets. Rho produced in Escherichia coli inhibited platelet aggregation with a K(I) value of 263 nM. Although functional, Rho produced in E. coli is misfolded based on our 2D and 3D NMR studies. In order to correct the folding problem, Rho was expressed in Pichia pastoris. The recombinant Rho expressed in P. pastoris inhibited platelet aggregation with a resulting K(I) value of 70 nM. This is the same potency as that of native Rho. CD analysis showed that the secondary structures of Rho are pH-independent and contain 3.5-7.9% alpha-helix, 48.2-50.5% beta-structures, and 42.3-47% coil. The sequential assignment and structure analysis of Rho were obtained using 2D and 3D 15N-edited NMR spectra. These results provide the first direct evidence that highly disulfide-bonded disintegrin can be expressed in P. pastoris with the correct fold. This evidence may serve as the basis for exploring the structure and function relationships as well as the dynamics of disintegrin and its variants." citations,entry_citation,595,236263,1,,entry citation,,,,,"Steinmetz, Wayne E., Moonen, Chrit, Kumar, Anil, Lazdunski, Michel, Visser, Leon, Carlsson, Fritz H.H., Wuthrich, Kurt, ""1H Nuclear-Magnetic-Resonance Studies of the Conformation of Cardiotoxin VII2 from Naja mossambica mossambica,"" Eur. J. Biochem. 120, 467-475 (1981).","1H Nuclear-Magnetic-Resonance Studies of the Conformation of Cardiotoxin VII2 from Naja mossambica mossambica",published,journal,Eur. J. Biochem.,,120,,,,,,,,,,,,,,,,,,,,,,,467,475,1981, citations,entry_citation,5950,236276,1,,entry citation,,,15865419,,,"Solution Structure and Interactions of the Escherichia coli Cell Division Activator Protein CedA",published,journal,Biochemistry,,44,18,,,,,,,,,,,,,,,,,,,,,,6738,6744,2005, citations,entry_citation,5951,236289,1,,entry citation,,,,,,1H and 15N chemical shift assignment and secondary structure of human saposin C,published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5952,236304,1,,entry citation,,,,,,"Letter to the Editor: Solution structure of the HPV-16 E2 DNA binding domain, a transcriptional regulator with a dimeric beta-barrel fold.",published,journal,J. Biomol. NMR,,30,2,,,,,,,,,,,,,,,,,,,,,,211,214,2004, citations,entry_citation,5953,236318,1,,entry citation,,,15017149,,,"Letter to the Editor: Sequential Resonance Assignments of the Extracellular Domain of the Human TGFbeta type II Receptor in Complex with Monomeric TGFbeta3",published,journal,J. Biomol. NMR,,29,1,,,,,,,,,,,,,,,,,,,,,,103,104,2004, citations,entry_citation,5954,236345,1,,entry citation,,,15017149,,,"Letter to the Editor: Sequential Resonance Assignments of the Extracellular Domain of the Human TGFbeta type II Receptor in Complex with Monomeric TGFbeta3",published,journal,J. Biomol. NMR,,29,1,,,,,,,,,,,,,,,,,,,,,,103,104,2004, citations,entry_citation,5955,236370,1,,entry citation,,,12220179,,,"Relaxation, equilibrium oligomerization and molecular symmetry of the VASP (336-380) EVH2 tetramer",published,journal,Biochemistry,,41,37,,,,,,,,,,,,,,,,,,,,,,11143,11151,2002, citations,entry_citation,5956,236396,1,,entry citation,,,15342239,,,"The NMR solution structure of a mutant of the Max b/HLH/LZ free of DNA: insights into the specific and reversible DNA binding mechanism of dimeric transcription factors.",published,journal,J. Mol. Biol.,,342,3,,,,,,,,,,,,,,,,,,,,,,813,832,2004, citations,references,5956,236397,2,,reference citation,,,12595267,,"Jean-Francois N, Frederic G, Raymund W, Benoit C, Lavigne P. Improving the thermodynamic stability of the leucine zipper of max increases the stability of its b-HLH-LZ:E-box complex. J Mol Biol. 2003 Mar 7;326(5):1577-95.",Improving the thermodynamic stability of the leucine zipper of max increases the stability of its b-HLH-LZ:E-box complex.,published,journal,J. Mol. Biol.,Journal of molecular biology,326,5,,0022-2836,,,,,,,,,,,,,,,,,,,,1577,1595,2003,"Max is a member of the b-HLH-LZ (basic region-helix1-loop-helix2-leucine zipper) family of eukaryotic transcription factors. It is the obligate partner of the related b-HLH-LZ proteins, c-Myc and Mad1, with which it forms heterodimers on target DNA. While c-Myc and Mad1 require Max for DNA-binding, Max itself can form a homodimer that recognizes E-box DNA sequences (CACGTG) in gene promoters that are targeted by c-Myc. Evidence suggests that this mode of binding by Max may repress c-Myc transcriptional activity, and this may have applications in the control of the aberrant activity of c-Myc during certain oncogenic transformations. To enhance this repressive potential of Max, we sought to stabilize Max homodimers. We have designed a double mutant (N78V/H81L) located in the coiled-coil interface of the leucine zipper domain and we demonstrate that these mutations do indeed increase the stability of the protein. The mutations also improve the stability of the complex with cognate DNA. Thermal denaturations monitored by circular dichroism reveal two transitions that are due to intermediate folding states for both the wild-type and mutant proteins; this is supported by detailed thermodynamic analyses. A formalism to characterize the temperature-dependence of the unfolding, including the effect of intermediates, is presented." citations,entry_citation,5958,236411,1,,entry citation,,,15213446,,,"Letter to the Editor: 1H, 13C and 15N resonance assignments of human microtubule-associated protein light chain-3",published,journal,J. Biomol. NMR,,29,3,,,,,,,,,,,,,,,,,,,,,,415,416,2004, citations,entry_citation,5959,236434,1,,entry citation,,,14659764,,,"Structure of human Ki67 FHA domain and its binding to a phosphoprotein fragment from hNIFK reveal unique recognition sites and new views to the structural basis of FHA domain functions",published,journal,J. Mol. Biol.,,335,1,,,,,,,,,,,,,,,,,,,,,,371,381,2004, citations,entry_citation,596,236452,1,,entry citation,,,,,"Steinmetz, Wayne E., Moonen, Chrit, Kumar, Anil, Lazdunski, Michel, Visser, Leon, Carlsson, Fritz H.H., Wuthrich, Kurt, ""1H Nuclear-Magnetic-Resonance Studies of the Conformation of Cardiotoxin VII2 from Naja mossambica mossambica,"" Eur. J. Biochem. 120, 467-475 (1981).","1H Nuclear-Magnetic-Resonance Studies of the Conformation of Cardiotoxin VII2 from Naja mossambica mossambica",published,journal,Eur. J. Biochem.,,120,,,,,,,,,,,,,,,,,,,,,,,467,475,1981, citations,entry_citation,5960,236465,1,,entry citation,,,14699046,,,From the Cover: Entropic switch regulates myristate exposure in the HIV-1 matrix protein,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,101,2,,,,,,,,,,,,,,,,,,,,,,517,522,2004, citations,entry_citation,5961,236482,1,,entry citation,,,16938309,,,"Binding site structure of one LRP-RAP complex: implications for a common ligand-receptor binding motif",published,journal,J. Mol. Biol.,,362,4,,,,,,,,,,,,,,,,,,,,,,700,716,2006, citations,reference_1,5961,236483,2,,reference citation,,,10747921,,"Andersen OM, Christensen LL, Christensen PA, Sorensen ES, Jacobsen C, Moestrup SK, Etzerodt M, Thogersen HC. Identification of the minimal functional unit in the low density lipoprotein receptor-related protein for binding the receptor-associated protein (RAP). A conserved acidic residue in the complement-type repeats is important for recognition of RAP. J Biol Chem. 2000 Jul 14;275(28):21017-24.",Identification of the minimal functional unit in the low density lipoprotein receptor-related protein for binding the receptor-associated protein (RAP). A conserved acidic residue in the complement-type repeats is important for recognition of RAP.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,275,28,,0021-9258,,,,,,,,,,,,,,,,,,,,21017,21024,2000,"The low density lipoprotein receptor-related protein (LRP), a member of the low density lipoprotein receptor family, mediates the internalization of a diverse set of ligands. The ligand binding sites are located in different regions of clusters consisting of approximately 40 residues, cysteine-rich complement-type repeats (CRs). The 39-40-kDa receptor-associated protein, a folding chaperone/escort protein required for efficient transport of functional LRP to the cell surface, is an antagonist of all identified ligands. To analyze the multisite inhibition by RAP in ligand binding of LRP, we have used an Escherichia coli expression system to produce fragments of the entire second ligand binding cluster of LRP (CR3-10). By ligand affinity chromatography and surface plasmon resonance analysis, we show that RAP binds to all two-repeat modules except CR910. CR10 differs from other repeats in cluster II by not containing a surface-exposed conserved acidic residue between Cys(IV) and Cys(V). By site-directed mutagenesis and ligand competition analysis, we provide evidence for a crucial importance of this conserved residue for RAP binding. We provide experimental evidence showing that two adjacent complement-type repeats, both containing a conserved acidic residue, represent a minimal unit required for efficient binding to RAP." citations,reference_2,5961,236484,3,,reference citation,,,9207124,,"The solution structure of the N-terminal domain of alpha2-macroglobulin receptor-associated protein. Proc Natl Acad Sci U S A. 1997 Jul 8;94(14):7521-5.",The solution structure of the N-terminal domain of alpha2-macroglobulin receptor-associated protein.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,94,14,,0027-8424,,,,,,,,,,,,,,,,,,,,7521,7525,1997,"The three-dimensional structure of the N-terminal domain (residues 18-112) of alpha2-macroglobulin receptor-associated protein (RAP) has been determined by NMR spectroscopy. The structure consists of three helices composed of residues 23-34, 39-65, and 73-88. The three helices are arranged in an up-down-up antiparallel topology. The C-terminal 20 residues were shown not to be in a well defined conformation. A structural model for the binding of RAP to the family of low-density lipoprotein receptors is proposed. It defines a role in binding for both the unordered C terminus and the structural scaffold of the core structure. Pathogenic epitopes for the rat disease Heymann nephritis, an experimental model of human membranous glomerulonephritis, have been identified in RAP and in the large endocytic receptor gp330/megalin. Here we provide the three-dimensional structure of the pathogenic epitope in RAP. The amino acid residues known to form the epitope are in a helix-loop-helix conformation, and from the structure it is possible to rationalize the published results obtained from studies of fragments of the N-terminal domain." citations,entry_citation,5962,236502,1,,entry citation,,,14745440,,,"Solution structure of domain 5 of a group II intron ribozyme reveals a new RNA motif",published,journal,Nat. Struct. Mol. Biol.,,11,2,,,,,,,,,,,,,,,,,,,,,,187,192,2004, citations,entry_citation,5963,236519,1,,entry citation,,,15014238,,,"Letter to the Editor: NMR assignment of HI1723 from Haemophilus influenzae - a sequence homologue from the iron sulfur cluster assembly (IscA) family",published,journal,J. Biomol. NMR,,29,2,,,,,,,,,,,,,,,,,,,,,,213,214,2004, citations,ref_1,5963,236520,2,,reference citation,,,7542800,,"Whole-genome random sequencing and assembley of Haemophilus influenzae Rd. Science 269 July 28 496-512 (1995).",Whole-genome random sequencing and assembly of Haemophilus influenzae Rd.,published,journal,Science,"Science (New York, N.Y.)",269,5223,,0036-8075,,,,,,,,,,,,,,,,,,,,496,512,1995,"An approach for genome analysis based on sequencing and assembly of unselected pieces of DNA from the whole chromosome has been applied to obtain the complete nucleotide sequence (1,830,137 base pairs) of the genome from the bacterium Haemophilus influenzae Rd. This approach eliminates the need for initial mapping efforts and is therefore applicable to the vast array of microbial species for which genome maps are unavailable. The H. influenzae Rd genome sequence (Genome Sequence DataBase accession number L42023) represents the only complete genome sequence from a free-living organism." citations,entry_citation,5964,236534,1,,entry citation,,,15096633,,,"Solution structures of the C-terminal headpiece subdomains of human villin and advillin, evaluation of headpiece F-actin-binding requirements",published,journal,Protein Sci.,,13,5,,,,,,,,,,,,,,,,,,,,,,1276,1287,2004, citations,citation_1,6444,246588,1,,entry citation,,,,,,Conformational Variability of MMPs: Beyond a Single 3D Structure,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,102,15,,,,,,,,,,,,,,,,,,,,,,5334,5339,2005, citations,ref_1,5980,236889,2,,reference citation,,,9882318,,"Honda M, Beard MR, Ping LH, Lemon SM. J. Virol., (1999) 73, 1165-1174.",A phylogenetically conserved stem-loop structure at the 5' border of the internal ribosome entry site of hepatitis C virus is required for cap-independent viral translation.,published,journal,J. Virol.,Journal of virology,73,2,,0022-538X,,,,,,,,,,,,,,,,,,,,1165,1174,1999,"Hepatitis C virus (HCV) initiates translation of its polyprotein under the control of an internal ribosome entry site (IRES) that comprises most of the 341-nucleotide (nt) 5' nontranslated RNA (5'NTR). A comparative analysis of related flaviviral sequences suggested that an RNA segment for which secondary structure was previously ill defined (domain II, nt 44 to 118) forms a conserved stem-loop that is located at the 5' border of the HCV IRES and thus may function in viral translation. This prediction was tested by a mutational analysis of putative helical structures that examined the impact of both covariant and noncovariant nucleotide substitutions on IRES activity in vivo and in vitro. Results of these experiments provide support for predicted base pair interactions between nt 44 to 52 and 111 to 118 and between nt 65 to 70 and 97 to 102 of the HCV 5'NTR. Substitutions at either nt 45 and 46 or nt 116 and 117 resulted in reciprocal changes in V1 nuclease cleavage patterns within the opposing strand of the putative helix, consistent with the predicted base pair interactions. IRES activity was highly dependent on maintenance of the stem-loop II structure but relatively tolerant of covariant nucleotide substitutions within predicted helical segments. Sequence alignments suggested that the deduced domain II structure is conserved within the IRESs of pestiviruses as well as the novel flavivirus GB virus B. Despite marked differences in primary nucleotide sequence within conserved helical segments, the sequences of the intervening single-stranded loop segments are highly conserved in these different viruses. This suggests that these segments of the viral RNA may interact with elements of the host translational machinery that are broadly conserved among different mammalian species." citations,entry_citation,5981,236908,1,,entry citation,,,16222560,,,"Solution structure of human dihydrofolate reductase in its complex with trimethoprim and NADPH",published,journal,J. Biomol. NMR,,33,1,,,,,,,,,,,,,,,,,,,,,,69,72,2005, citations,entry_citation,5982,236953,1,,entry citation,,,15213448,,,"Letter to the Editor: Complete 1H, 13C and 15N assignments of a monomeric, biologically active apolipoprotein E carboxyl-terminal domain",published,journal,J. Biomol. NMR,,29,3,,,,,,,,,,,,,,,,,,,,,,419,420,2004, citations,entry_citation,5983,236966,1,,entry citation,,,15243192,,,"Letter to the Editor: 1H, 13C and 15N resonance assignments of human 5,10-methenyltetrahydrofolate synthetase",published,journal,J. Biomol. NMR,,29,4,,,,,,,,,,,,,,,,,,,,,,547,548,2004, citations,entry_citation,5984,236997,1,,entry citation,,,15101973,,,Solution Structure and Domain Architecture of the Divisome Protein FtsN,published,journal,Mol. Microbiol.,,52,3,,,,,,,,,,,,,,,,,,,,,,651,660,2004, citations,entry_citation,5985,237021,1,,entry citation,,,14992691,,,"Solution Conformation of alpha-Conotoxin GIC, a Novel Potent Antagonist of alpha3beta2 Nicotinic Acetylcholine Receptors",published,journal,Biochem. J.,,380,,,,,,,,,,,,,,,,,,,,,,,347,352,2004, citations,entry_citation,5986,237039,1,,entry citation,,,,,,"Solution structure of paralytic peptide of the wild Silkmoth, Antheraea yamamai",published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,5987,237055,1,,entry citation,,,14594809,,,"Interaction of the TAZ1 domain of the CREB-binding protein with the activation domain of CITED2: Regulation by competition between intrinsically unstructured ligands for non-identical binding sites",published,journal,J. Biol. Chem.,,279,4,,,,,,,,,,,,,,,,,,,,,,3042,3049,2004, citations,entry_citation,5988,237085,1,,entry citation,,,15178256,,,NMR and MD studies on the interaction between ligand peptides and alpha-bungarotoxin,published,journal,J. Mol. Biol.,,339,5,,,,,,,,,,,,,,,,,,,,,,1169,1177,2004, citations,entry_citation,5989,237103,1,,entry citation,,,15584897,,,"Interaction of three-finger toxins with phospholipid membranes: comparison of S- and P-type cytotoxins",published,journal,Biochem. J.,,387,Pt 3,,,,,,,,,,,,,,,,,,,,,,807,815,2005,Structure determination in aqueous solution and in complex with DPC micelle. citations,ref-1,5989,237104,2,,reference citation,,,,,"Grishin E.V., Sukhikh A.P., Adamovich T.B., Ovchinnikov Y.A. ""Isolation, properties and sequence determination of the two cytotoxins from the venom of the Middle-Asian cobra Naja Naja oxiana."" Bioorg. Khim. 2:1018-1034(1976).",,published,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref-2,5989,237105,3,,reference citation,,,,,"Bartles C., Xia T., Billiter M., Guntert P., Wutrich K. ""The program XEASY for computer-supported NMR spectral analysis of biological macromolecules"" Journal of Biomolecular NMR, 1995, v.5 pp.1-10.",,published,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref-3,5989,237106,4,,reference citation,,,12051947,,"Herrmann T, Guntert P, Wuthrich K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J Mol Biol. 2002 May 24;319(1):209-27.",Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA.,published,journal,J. Mol. Biol.,Journal of molecular biology,319,1,,0022-2836,,,,,,,,,,,,,,,,,,,,209,227,2002,"Combined automated NOE assignment and structure determination module (CANDID) is a new software for efficient NMR structure determination of proteins by automated assignment of the NOESY spectra. CANDID uses an iterative approach with multiple cycles of NOE cross-peak assignment and protein structure calculation using the fast DYANA torsion angle dynamics algorithm, so that the result from each CANDID cycle consists of exhaustive, possibly ambiguous NOE cross-peak assignments in all available spectra and a three-dimensional protein structure represented by a bundle of conformers. The input for the first CANDID cycle consists of the amino acid sequence, the chemical shift list from the sequence-specific resonance assignment, and listings of the cross-peak positions and volumes in one or several two, three or four-dimensional NOESY spectra. The input for the second and subsequent CANDID cycles contains the three-dimensional protein structure from the previous cycle, in addition to the complete input used for the first cycle. CANDID includes two new elements that make it robust with respect to the presence of artifacts in the input data, i.e. network-anchoring and constraint-combination, which have a key role in de novo protein structure determinations for the successful generation of the correct polypeptide fold by the first CANDID cycle. Network-anchoring makes use of the fact that any network of correct NOE cross-peak assignments forms a self-consistent set; the initial, chemical shift-based assignments for each individual NOE cross-peak are therefore weighted by the extent to which they can be embedded into the network formed by all other NOE cross-peak assignments. Constraint-combination reduces the deleterious impact of artifact NOE upper distance constraints in the input for a protein structure calculation by combining the assignments for two or several peaks into a single upper limit distance constraint, which lowers the probability that the presence of an artifact peak will influence the outcome of the structure calculation. CANDID test calculations were performed with NMR data sets of four proteins for which high-quality structures had previously been solved by interactive protocols, and they yielded comparable results to these reference structure determinations with regard to both the residual constraint violations, and the precision and accuracy of the atomic coordinates. The CANDID approach has further been validated by de novo NMR structure determinations of four additional proteins. The experience gained in these calculations shows that once nearly complete sequence-specific resonance assignments are available, the automated CANDID approach results in greatly enhanced efficiency of the NOESY spectral analysis. The fact that the correct fold is obtained in cycle 1 of a de novo structure calculation is the single most important advance achieved with CANDID, when compared with previously proposed automated NOESY assignment methods that do not use network-anchoring and constraint-combination." citations,entry_citation,599,237124,1,,entry citation,,,,,"Steinmetz, Wayne E., Moonen, Chrit, Kumar, Anil, Lazdunski, Michel, Visser, Leon, Carlsson, Fritz H.H., Wuthrich, Kurt, ""1H Nuclear-Magnetic-Resonance Studies of the Conformation of Cardiotoxin VII2 from Naja mossambica mossambica,"" Eur. J. Biochem. 120, 467-475 (1981).","1H Nuclear-Magnetic-Resonance Studies of the Conformation of Cardiotoxin VII2 from Naja mossambica mossambica",published,journal,Eur. J. Biochem.,,120,,,,,,,,,,,,,,,,,,,,,,,467,475,1981, citations,entry_citation,5991,237137,1,,entry citation,,,15591056,,,"The structural and dynamic basis of Ets-1 DNA Binding autoinhibition",published,journal,J. Biol. Chem.,,280,8,,,,,,,,,,,,,,,,,,,,,,7088,7099,2005, citations,entry_citation,5992,237179,1,,entry citation,,,12890685,,,"1H, 13C and 15N resonance assignment and secondary structure of the C-terminal domain of the human centrin 2 in complex with a 17 residue peptide from Xeroderma Pigmentosum group C protein",published,journal,J. Biol. Chem.,,278,41,,,,,,,,,,,,,,,,,,,,,,40252,40261,2003, citations,entry_citation,5993,237207,1,,entry citation,,,,,,5-hydroxyuracil can form stable base pairs with all four bases in a DNA duplex,published,journal,Chem. Commun.,,,3,,,,,,,,,,,,,,,,,,,,,,400,402,2005, citations,entry_citation,5994,237227,1,,entry citation,,,15479620,,,Solution structure of Human Orexin-A: Regulator of Appetite and Wakefulness,published,journal,J. Biochem. Mol. Biol.,,37,5,,,,,,,,,,,,,,,,,,,,,,565,573,2004, citations,entry_citation,5995,237245,1,,entry citation,,,14872128,,,"Temperature-Dependent Spectral Density Analysis Applied to Monitoring Backbone Dynamics of Major Urinary Protein-I Complexed with the Pheromone 2-sec-butyl-4,5-dihyrothiazole.",published,journal,J. Biomol. NMR,,28,4,,,,,,,,,,,,,,,,,,,,,,369,384,2004, citations,entry_citation,5996,237292,1,,entry citation,,,14872128,,,"Temperature Dependent Spectral Density Analysis Applied to Monitoring Backbone Dynamics of Major Urinary Protein-I Complexed with the Pheromone 2-sec-butyl-4,5-dihyrothiazole",published,journal,J. Biomol. NMR,,28,4,,,,,,,,,,,,,,,,,,,,,,369,384,2004, citations,entry_citation,5997,237344,1,,entry citation,,,,,,"Improving the Accuracy of NMR Structures of Large Proteins Using Pseudocontact Shifts as Long-range Restraints",published,journal,J. Biomol. NMR,,28,3,,,,,,,,,,,,,,,,,,,,,,205,212,2004, citations,entry_citation,5998,237370,1,,entry citation,,,15213450,,,"Letter to the Editor: 1H, 15N and 13C resonance assignments of the ApaG protein of the phytopathogen Xanthomonas axonopodis pv. citri",published,journal,J. Biomol. NMR,,29,3,,,,,,,,,,,,,,,,,,,,,,423,424,2004, citations,ref_2,5998,237372,3,,reference citation,,,8520220,,"Delaglio, F. et al. J. Biomol. NMR 6, 277-293 (1995).",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,entry_citation,5999,237401,1,,entry citation,,,15213449,,,Letter to the Editor: NMR Assignments of the Drosophila Argonaute 2 PAZ domain,published,journal,J. Biomol. NMR,,29,3,,,,,,,,,,,,,,,,,,,,,,421,422,2004, citations,entry_citation,6,237431,1,,entry citation,,,,,"Wemmer, David, Kallenbach, Neville R., ""Structure of Apamin in Solution: A Two-Dimensional Nuclear Magnetic Resonance Study,"" Biochemistry 22, 1901-1906 (1983).","Structure of Apamin in Solution: A Two-Dimensional Nuclear Magnetic Resonance Study",published,journal,Biochemistry,,22,,,,,,,,,,,,,,,,,,,,,,,1901,1906,1983, citations,entry_citation,60,237442,1,,entry citation,,,,,"Kline, Allen D., Wuthrich, Kurt, ""Complete Sequence-specific 1H Nuclear Magnetic Resonance Assignments for the alpha-Amylase Polypeptide Inhibitor Tendamistat from Streptomyces tendae,"" J. Mol. Biol. 192, 869-890 (1986).","Complete Sequence-specific 1H Nuclear Magnetic Resonance Assignments for the alpha-Amylase Polypeptide Inhibitor Tendamistat from Streptomyces tendae",published,journal,J. Mol. Biol.,,192,,,,,,,,,,,,,,,,,,,,,,,869,890,1986, citations,entry_citation,600,237455,1,,entry citation,,,,,"Steinmetz, Wayne E., Moonen, Chrit, Kumar, Anil, Lazdunski, Michel, Visser, Leon, Carlsson, Fritz H.H., Wuthrich, Kurt, ""1H Nuclear-Magnetic-Resonance Studies of the Conformation of Cardiotoxin VII2 from Naja mossambica mossambica,"" Eur. J. Biochem. 120, 467-475 (1981).","1H Nuclear-Magnetic-Resonance Studies of the Conformation of Cardiotoxin VII2 from Naja mossambica mossambica",published,journal,Eur. J. Biochem.,,120,,,,,,,,,,,,,,,,,,,,,,,467,475,1981, citations,entry_citation,6000,237468,1,,entry citation,,,14615802,,,Structure and conserved RNA binding of the PAZ domain,published,journal,Nature,,426,,,,,,,,,,,,,,,,,,,,,,,468,474,2003, citations,entry_citation,6001,237484,1,,entry citation,,,15014240,,,"Letter to the Editor: 1H, 15N and 13C resonance assignments of the C345C domain of the complement component C5",published,journal,J. Biomol. NMR,,29,2,,,,,,,,,,,,,,,,,,,,,,217,218,2004, citations,ref_1,6001,237485,2,,reference citation,,,,,"J. Biomol. NMR (1995) 6, 135-140.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6002,237503,1,,entry citation,,,16679535,,,"NMR structure of the p63 SAM domain and dynamical properties of G534V and T537P pathological mutants, identified in the AEC syndrome",published,journal,Cell Biochem. Biophys.,,44,3,,,,,,,,,,,,,,,,,,,,,,475,489,2006, citations,entry_citation,6003,237539,1,,entry citation,,,15213452,,,"Letter to the Editor: Complete Resonance Assignments of Bundlin (BfpA) from the Bundle-forming Pilus of Enteropathogenic Escherichia coli",published,journal,J. Biomol. NMR,,29,3,,,,,,,,,,,,,,,,,,,,,,427,428,2004, citations,entry_citation,6004,237564,1,,entry citation,,,15213453,,,"Letter to the editor: Backbone and sidechain 1H, 13C and 15N resonance assignments of human cofilin",published,journal,J. Biomol. NMR,,29,3,,,,,,,,,,,,,,,,,,,,,,429,430,2004, citations,entry_citation,6005,237590,1,,entry citation,,,14981510,,,"Recognition of the mRNA AU-Rich Element by the Zinc Finger Domain of TIS11d",published,journal,Nat. Struct. Biol.,,11,3,,,,,,,,,,,,,,,,,,,,,,257,264,2004, citations,reference_6,6005,237591,2,,reference citation,,,7835719,,"1: Nie XF, Maclean KN, Kumar V, McKay IA, Bustin SA. Gene. 1995 Jan 23;152(2):285-6.","ERF-2, the human homologue of the murine Tis11d early response gene.",published,journal,Gene,Gene,152,2,,0378-1119,,,,,,,,,,,,,,,,,,,,285,286,1995,"A human cDNA specifying a member of the Tis11 early response gene family was cloned and sequenced. The human gene differs from its mouse homologue by encoding an additional 97 amino acids at its C-terminal end. The sequence has transactivation-like motifs, an unusual Cys-Ser-Ala-rich motif and displays sequence similarity at the extreme C-terminal end with another Tis11 family member, ERF-1." citations,reference_22,6005,237592,3,,reference citation,,,12639954,,"Nie XF, Maclean KN, Kumar V, McKay IA, Bustin SA. Gene. 1995 Jan 23;152(2):285-6.",Characteristics of the interaction of a synthetic human tristetraprolin tandem zinc finger peptide with AU-rich element-containing RNA substrates.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,278,22,,0021-9258,,,,,,,,,,,,,,,,,,,,19947,19955,2003,"Tristetraprolin (TTP) and its two known mammalian family members are tandem CCCH zinc finger proteins that can bind to AU-rich elements (AREs) in cellular mRNAs and destabilize those transcripts, apparently by initiating their deadenylation. Previous studies have shown that the approximately 70-amino acid tandem zinc finger domain of TTP is required and sufficient for RNA binding, and that the integrity of both zinc fingers is also required. However, little is known about the kinetics or structure of the peptide-RNA interaction, in part because of difficulties in obtaining soluble recombinant protein or peptides. We characterized the binding of a synthetic 73-amino acid peptide from human TTP to the tumor necrosis factor (TNF) ARE by gel mobility shift analyses and fluorescence anisotropy experiments. Both types of studies yielded a peptide-RNA dissociation constant of approximately 10 nM. Surprisingly, we found that the ""footprint"" from the TNF ARE required for peptide binding was only approximately 9 bases and that two molecules of peptide could bind to probes containing as little as 19 bases. An identical recombinant peptide exhibited gel shift characteristics similar to those of the synthetic peptide. NMR analysis of the 15N-labeled recombinant peptide suggested that its first zinc finger was structured in solution but that the second was not. The titration of oligonucleotides representing 17, 13, and even 9 bases of the TNF ARE caused an essentially identical, dramatic shift of existing resonances, and the appearance of new resonances in the peptide spectra, so that all amino acids could be assigned. These data suggest that this TTP peptide-RNA complex is structured in solution and might be amenable to NMR structure determination." citations,entry_citation,6006,237621,1,,entry citation,,,,,,Solution structure of CCAP from the fruit fly Drosophila melanogaster,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6007,237639,1,,entry citation,,,,,,"Structure of the Plasminogen Kringle 4 Binding Calcium Free Form of the C-type Lectin-like Domain of Tetranectin",published,journal,Biochemistry,,43,27,,,,,,,,,,,,,,,,,,,,,,8636,8643,2004, citations,ref_2,6019,237877,3,,reference citation,,,10869069,,"J Bacteriol. 2000 Jul;182(14):3929-33.",An abundant DNA binding protein from the hyperthermophilic archaeon Sulfolobus shibatae affects DNA supercoiling in a temperature-dependent fashion.,published,journal,J. Bacteriol.,Journal of bacteriology,182,14,,0021-9193,,,,,,,,,,,,,,,,,,,,3929,3933,2000,"The DNA binding protein Ssh10b, a member of the Sac10b family, has been purified from the hyperthermophilic archaeon Sulfolobus shibatae. Ssh10b constitutes about 4% of the cellular protein. Electrophoretic mobility shift assays showed that Ssh10b first bound a double-stranded DNA fragment with an estimated binding size of approximately approximately 12 bp, forming distinct shifts, until the DNA was coated with the protein. Binding of more Ssh10b resulted in the formation of smears of lower mobilities. The migration pattern of the smearing Ssh10b-DNA complexes was affected by temperature, whereas that of complexes associated with the distinct shifts was not. Interestingly, Ssh10b was capable of constraining negative DNA supercoils in a temperature-dependent fashion. While the ability of the protein to constrain supercoils was weak at 25 degrees C, it was enhanced substantially at 45 degrees C or higher temperatures (up to 80 degrees C). Taken together, our data suggest that archaeal proteins of the Sac10b family may affect the topology of chromosomal DNA in thermophilic archaea at their growth temperatures." citations,entry_citation,6020,237891,1,,entry citation,,,15134657,,,"Structure-activity relationships for the beta-hairpin cationic antimicrobial peptide polyphemusin I",published,journal,Biochim. Biophys. Acta,,1698,2,,,,,,,,,,,,,,,,,,,,,,239,250,2004, citations,entry_citation,6021,237908,1,,entry citation,,,15213458,,,"Letter to the Editor: Backbone 1H, 15N and 13C assignments for the subunit a of the E.coli ATP Synthase",published,journal,J. Biomol. NMR,,29,3,,,,,,,,,,,,,,,,,,,,,,439,440,2004, citations,entry_citation,6022,237927,1,,entry citation,,,14572476,,,"Structure and Metal Binding Studies of the Second Copper Binding Domain of the Menkes ATPase",published,journal,J. Struct. Biol.,,143,3,,,,,,,,,,,,,,,,,,,,,,209,218,2003, citations,entry_citation,6023,237949,1,,entry citation,,,15243184,,,"Letter to the Editor: 1H, 15N, and 13C Resonance Assignments of Calmodulin Complexed with the Calmodulin-Binding Domain of calcineurin",published,journal,J. Biomol. NMR,,29,4,,,,,,,,,,,,,,,,,,,,,,531,532,2004, citations,entry_citation,6024,237975,1,,entry citation,,,15213455,,,"Letter to the Editor: 1H, 13C and 15N backbone resonance assignments for TEM-1, a 28.9 kDa [bgr]-lactamase from E. coli",published,journal,J. Biomol. NMR,,29,3,,,,,,,,,,,,,,,,,,,,,,433,434,2004, citations,entry_citation,6025,237994,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C, 15N resonance assignments of the cytokine LECT2",published,journal,J. Biomol. NMR,,24,4,,,,,,,,,,,,,,,,,,,,,,543,544,2004, citations,entry_citation,6026,238026,1,,entry citation,,,15113213,,,"Strategy for the Study of Paramagnetic Proteins with Slow Electronic Relaxation Rates by NMR Spectroscopy: Application to Oxidized Human [2Fe-2S] Ferredoxin",published,journal,J. Am. Chem. Soc.,,126,17,,,,,,,,,,,,,,,,,,,,,,5413,5426,2004, citations,entry_citation,6027,238059,1,,entry citation,,,12006587,,,"Solution structure of mu-conotoxin PIIIA, a preferential inhibitor of persistent tetrodotoxin-sensitive sodium channels",published,journal,J. Biol. Chem.,,277,30,,,,,,,,,,,,,,,,,,,,,,27247,27255,2002, citations,entry_citation,6028,238084,1,,entry citation,,,,,,"Solution structure of ribosomal protein S17E from Methanobacterium thermoautotrophicum",published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6029,238114,1,,entry citation,,,15213457,,,"Letter to the Editor: 1H, 13C and 15N resonance assignment of the nucleotide binding domain of KdpB from Escherichia coli",published,journal,J. Biomol. NMR,,29,3,,,,,,,,,,,,,,,,,,,,,,437,438,2004, citations,entry_citation,6030,238139,1,,entry citation,,,15213457,,,"Letter to the Editor: 1H, 13C and 15N resonance assignment of the nucleotide binding domain of KdpB from Escherichia coli",published,journal,J. Biomol. NMR,,29,3,,,,,,,,,,,,,,,,,,,,,,437,438,2004, citations,entry_citation,6031,238158,1,,entry citation,,,15213460,,,"Letter to the Editor: 1H, 13C, and 15N resonance assignments of human Notch-1 calcium binding EGF domains 11-13",published,journal,J. Biomol. NMR,,29,3,,,,,,,,,,,,,,,,,,,,,,443,444,2004, citations,entry_citation,6032,238178,1,,entry citation,,,15756466,,,"Letter to the Editor: 1H, 13C and 15N resonance assignments of coactosin, a cytoskeletal regulatory protein",published,journal,J. Biomol. NMR,,30,3,,,,,,,,,,,,,,,,,,,,,,365,366,2004, citations,entry_citation,6033,238207,1,,entry citation,,,14726539,,,"NMR analysis shows that a b-type variant of hydrogenobacter thermophilus cytochrome c552 retains its native structure",published,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6034,238226,1,,entry citation,,,15213459,,,"Letter to the Editor: 1H, 15N, 13C resonance assignments and 15N-1H residual dipolar couplings for the alpha-adaptin ear-domain",published,journal,J. Biomol. NMR,,29,3,,,,,,,,,,,,,,,,,,,,,,441,442,2004, citations,entry_citation,6035,238244,1,,entry citation,,,15288782,,,"Solution structure and DNA binding of the zinc-finger domain from DNA ligase IIIalpha",published,journal,J. Mol. Biol.,,341,3,,,,,,,,,,,,,,,,,,,,,,723,738,2004, citations,entry_citation,6037,238278,1,,entry citation,,,15683869,,,"A novel short-chain peptide BmKX from the chinese scorpion Buthus martensi karsch, sequencing, gene cloning and structure determination",published,journal,Toxicon,,45,3,,,,,,,,,,,,,,,,,,,,,,309,319,2005, citations,entry_citation,6038,238295,1,,entry citation,,,,,,NMR Structure of Chemokine CXCL11/ITAC,submitted,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6039,238316,1,,entry citation,,,11373724,,,"Solution NMR Structure of a D,L-Alternating Oligonorleucine as a Model of Beta-Helix",published,journal,Biopolymers,,59,2,,,,,,,,,,,,,,,,,,,,,,110,119,2001, citations,entry_citation,6040,238337,1,,entry citation,,,15568810,,,"NMR structures of the C-terminal segment of surfactant protein B in detergent micelles and hexafluoro-2-propanol.",published,journal,Biochemistry,,43,48,,,,,,,,,,,,,,,,,,,,,,15187,15194,2004, citations,entry_citation,6041,238357,1,,entry citation,,,16075425,,,"Structure of the Antimicrobial, Cationic Hexapeptide Cyclo(RRWWRF) and Its Analogues in Solution and Bound to Detergent Micelles",published,journal,ChemBioChem,,6,9,,,,,,,,,,,,,,,,,,,,,,1654,1662,2005, citations,entry_citation,6042,238375,1,,entry citation,,,14962384,,,"The Structure of the Stemloop D Subdomain of Coxsackievirus B3 Cloverleaf RNA and its Interaction with the Proteinase 3C",published,journal,Stucture,,12,,,,,,,,,,,,,,,,,,,,,,,237,248,2004, citations,entry_citation,6043,238399,1,,entry citation,,,15243189,,,"Letter to the Editor: 1H, 13C and 15N resonance assignment of Cu(I)-Pseudoazurin from Alcaligenes faecalis S-6",published,journal,J. Biomol. NMR,,29,4,,,,,,,,,,,,,,,,,,,,,,541,542,2004, citations,entry_citation,6044,238418,1,,entry citation,,,15213463,,,"Letter to the Editor: Resonance assignment and secondary structure of the La Motif",published,journal,J. Biomol. NMR,,29,3,,,,,,,,,,,,,,,,,,,,,,449,450,2004, citations,entry_citation,6045,238432,1,,entry citation,,,,,,"Backbone 1H, 13C, and 15N Chemical Shift Assignments for Hypothetical protein PF0455",in preparation,journal,J. Biomol. NMR,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6046,238450,1,,entry citation,,,15213461,,,"Letter to the Editor: 1H, 13C and 15N resonance assignments for domain III of the West Nile Virus envelope protein",published,journal,J. Biomol. NMR,,29,3,,,,,,,,,,,,,,,,,,,,,,445,446,2004, citations,entry_citation,6047,238463,1,,entry citation,,,15213467,,,"1H, 15N, and 13C resonance assignment of the 23 kDa organomercurial lyase MerB in its free and mercury-bound forms",published,journal,J. Biomol. NMR,,29,3,,,,,,,,,,,,,,,,,,,,,,457,458,2004, citations,entry_citation,6048,238480,1,,entry citation,,,15850378,,,"The Micelle-Bound Structure of an Antimicrobial Peptide Derived from the alpha-Chain of Bovine Hemoglobin Isolated from the Tick Boophilus microplus.",published,journal,Biochemistry,,44,17,,,,,,,,,,,,,,,,,,,,,,6440,6451,2005, citations,entry_citation,6049,238503,1,,entry citation,,,15122922,,,"Paramagnetism-based Refinement Strategy for the Solution Structure of Human alpha-Parvalbumin",published,journal,Biochemistry,,43,18,,,,,,,,,,,,,,,,,,,,,,5562,5573,2004, citations,entry_citation,6050,238529,1,,entry citation,,,17340638,,,"Structural determinants responsible for the thermostability of Sso7d and its single point mutants",published,journal,Proteins,,67,3,,,,,,,,,,,,,,,,,,,,,,766,775,2007, citations,ref_1,6050,238530,2,,reference citation,,,11377427,,"The Sso7d DNA-binding protein from sulfolobus solfataricus has ribonuclease activity Febs Lett. V.497, 131, 2001",The Sso7d DNA-binding protein from Sulfolobus solfataricus has ribonuclease activity.,published,journal,FEBS Lett.,FEBS letters,497,2-3,,0014-5793,,,,,,,,,,,,,,,,,,,,131,136,2001,"Sso7d is a small, basic, abundant protein from the thermoacidophilic archaeon Sulfolobus solfataricus. Previous research has shown that Sso7d can bind double-stranded DNA without sequence specificity by placing its triple-stranded beta-sheet across the minor groove. We previously found RNase activity both in preparations of Sso7d purified from its natural source and in recombinant, purified protein expressed in Escherichia coli. This paper provides conclusive evidence that supports the assignment of RNase activity to Sso7d, shown by the total absence of activity in the single-point mutants E35L and K12L, despite the preservation of their overall structure under the assay conditions. In keeping with our observation that the residues putatively involved in RNase activity and those playing a role in DNA binding are located on different surfaces of the molecule, the activity was not impaired in the presence of DNA. If a small synthetic RNA was used as a substrate, Sso7d attacked both predicted double- and single-stranded RNA stretches, with no evident preference for specific sequences or individual bases. Apparently, the more readily attacked bonds were those intrinsically more unstable." citations,entry_citation,6051,238550,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N resonance assignments of the methionine sulfoxide reductase B from Neisseria meningitidis",published,journal,J. Biomol. NMR,,30,2,,,,,,,,,,,,,,,,,,,,,,223,224,2004, citations,ref_1,6051,238551,2,,reference citation,,,12954610,,"Antoine M. et al. (2003) J. Biol. Chem., 278, 45352-45357",Kinetic characterization of the chemical steps involved in the catalytic mechanism of methionine sulfoxide reductase A from Neisseria meningitidis.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,278,46,,0021-9258,,,,,,,,,,,,,,,,,,,,45352,45357,2003,"Oxidation of methionine into methionine sulfoxide is associated with many pathologies and is described to exert regulatory effects on protein functions. Two classes of methionine sulfoxide reductases, called MsrA and MsrB, have been described to reduce the S and the R isomers of the sulfoxide of methionine sulfoxide back to methionine, respectively. Although MsrAs and MsrBs display quite different x-ray structures, they share a similar, new catalytic mechanism that proceeds via the sulfenic acid chemistry and that includes at least three chemical steps with 1) the formation of a sulfenic acid intermediate and the concomitant release of methionine; 2) the formation of an intra-disulfide bond; and 3) the reduction of the disulfide bond by thioredoxin. In the present study, it is shown that for the Neisseria meningitidis MsrA, 1) the rate-limiting step is associated with the reduction of the Cys-51/Cys-198 disulfide MsrA bond by thioredoxin; 2) the formation of the sulfenic acid intermediate is very efficient, thus suggesting catalytic assistance via amino acids of the active site; 3) the rate-determining step in the formation of the Cys-51/Cys-198 disulfide bond is that leading to the formation of the sulfenic intermediate on Cys-51; and 4) the apparent affinity constant for methionine sulfoxide in the methionine sulfoxide reductase step is 80-fold higher than the Km value determined under steady-state conditions." citations,ref_2,6051,238552,3,,reference citation,,,,,"Bartels C. et al. (1995) J. Biomol. NMR, 6, 1-10",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_3,6051,238553,4,,reference citation,,,10964927,,"Boschi-Muller S. et al. (2000) J. Biol. Chem, 275, 35908-35913",A sulfenic acid enzyme intermediate is involved in the catalytic mechanism of peptide methionine sulfoxide reductase from Escherichia coli.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,275,46,,0021-9258,,,,,,,,,,,,,,,,,,,,35908,35913,2000,"Methionine oxidation into methionine sulfoxide is known to be involved in many pathologies and to exert regulatory effects on proteins. This oxidation can be reversed by a ubiquitous monomeric enzyme, the peptide methionine sulfoxide reductase (MsrA), whose activity in vivo requires the thioredoxin-regenerating system. The proposed chemical mechanism of Escherichia coli MsrA involves three Cys residues (positions 51, 198, and 206). A fourth Cys (position 86) is not important for catalysis. In the absence of a reducing system, 2 mol of methionine are formed per mole of enzyme for wild type and Cys-86 --> Ser mutant MsrA, whereas only 1 mol is formed for mutants in which either Cys-198 or Cys-206 is mutated. Reduction of methionine sulfoxide is shown to proceed through the formation of a sulfenic acid intermediate. This intermediate has been characterized by chemical probes and mass spectrometry analyses. Together, the results support a three-step chemical mechanism in vivo: 1) Cys-51 attacks the sulfur atom of the sulfoxide substrate leading, via a rearrangement, to the formation of a sulfenic acid intermediate on Cys-51 and release of 1 mol of methionine/mol of enzyme; 2) the sulfenic acid is then reduced via a double displacement mechanism involving formation of a disulfide bond between Cys-51 and Cys-198, followed by formation of a disulfide bond between Cys-198 and Cys-206, which liberates Cys-51, and 3) the disulfide bond between Cys-198 and Cys-206 is reduced by thioredoxin-dependent recycling system process." citations,entry_citation,6066,238872,1,,entry citation,,,15201273,,,"Structure-Activity Relationships of Hainantoxin-IV, structure determination of active and inactive sodium channel blockers",published,journal,J. Biol. Chem.,,279,36,,,,,,,,,,,,,,,,,,,,,,37734,37740,2004, citations,entry_citation,6067,238888,1,,entry citation,,,15201273,,,"Structure-Activity Relationships of Hainantoxin-IV, structure determination of active and inactive sodium channel blockers",published,journal,J. Biol. Chem.,,279,36,,,,,,,,,,,,,,,,,,,,,,37734,37740,2004, citations,entry_citation,6068,238904,1,,entry citation,,,15178255,,,"Structural Similarities of micelle-bound peptide YY (PYY) and neuropeptide Y (NPY) are related to their affinity profiles at the Y receptors.",published,journal,J. Biol. Chem.,,339,5,,,,,,,,,,,,,,,,,,,,,,1153,1168,2004, citations,ref_4,6051,238554,5,,reference citation,,,10212987,,"Cornilescu G. et al. (1999) J. Biomol. NMR, 13, 289-302",Protein backbone angle restraints from searching a database for chemical shift and sequence homology.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,13,3,,0925-2738,,,,,,,,,,,,,,,,,,,,289,302,1999,"Chemical shifts of backbone atoms in proteins are exquisitely sensitive to local conformation, and homologous proteins show quite similar patterns of secondary chemical shifts. The inverse of this relation is used to search a database for triplets of adjacent residues with secondary chemical shifts and sequence similarity which provide the best match to the query triplet of interest. The database contains 13C alpha, 13C beta, 13C', 1H alpha and 15N chemical shifts for 20 proteins for which a high resolution X-ray structure is available. The computer program TALOS was developed to search this database for strings of residues with chemical shift and residue type homology. The relative importance of the weighting factors attached to the secondary chemical shifts of the five types of resonances relative to that of sequence similarity was optimized empirically. TALOS yields the 10 triplets which have the closest similarity in secondary chemical shift and amino acid sequence to those of the query sequence. If the central residues in these 10 triplets exhibit similar phi and psi backbone angles, their averages can reliably be used as angular restraints for the protein whose structure is being studied. Tests carried out for proteins of known structure indicate that the root-mean-square difference (rmsd) between the output of TALOS and the X-ray derived backbone angles is about 15 degrees. Approximately 3% of the predictions made by TALOS are found to be in error." citations,ref_5,6051,238555,6,,reference citation,,,11677230,,"Grimaud et al. (2001) J. Biol. Chem, 276, 48915-48920",Repair of oxidized proteins. Identification of a new methionine sulfoxide reductase.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,276,52,,0021-9258,,,,,,,,,,,,,,,,,,,,48915,48920,2001,"Oxidation of methionine residues to methionine sulfoxide can lead to inactivation of proteins. Methionine sulfoxide reductase (MsrA) has been known for a long time, and its repairing function well characterized. Here we identify a new methionine sulfoxide reductase, which we referred to as MsrB, the gene of which is present in genomes of eubacteria, archaebacteria, and eucaryotes. The msrA and msrB genes exhibit no sequence similarity and, in some genomes, are fused. The Escherichia coli MsrB protein (currently predicted to be encoded by an open reading frame of unknown function named yeaA) was used for genetic, enzymatic, and mass spectrometric investigations. Our in vivo study revealed that msrB is required for cadmium resistance of E. coli, a carcinogenic compound that induces oxidative stress. Our in vitro studies, showed that (i) MsrB and MsrA enzymes reduce free methionine sulfoxide with turn-over rates of 0.6 min(-1) and 20 min(-1), respectively, (ii) MsrA and MsrB act on oxidized calmodulin, each by repairing four to six of the eight methionine sulfoxide residues initially present, and (iii) simultaneous action of both MsrA and MsrB allowed full reduction of oxidized calmodulin. A possibility is that these two ubiquitous methionine sulfoxide reductases exhibit different substrate specificity." citations,ref_6,6051,238556,7,,reference citation,,,11938352,,"Lowther, W.T. et al. (2002) Nat. Struct. Biol., 9, 348-352",The mirrored methionine sulfoxide reductases of Neisseria gonorrhoeae pilB.,published,journal,Nat. Struct. Biol.,Nature structural biology,9,5,,1072-8368,,,,,,,,,,,,,,,,,,,,348,352,2002,"Methionine sulfoxide reductases (Msr) protect against oxidative damage that can contribute to cell death. The tandem Msr domains (MsrA and MsrB) of the pilB protein from Neisseria gonorrhoeae each reduce different epimeric forms of methionine sulfoxide. The overall fold of the MsrB domain revealed by the 1.85 A crystal structure shows no resemblance to the previously determined MsrA structures from other organisms. Despite the lack of homology, the active sites show approximate mirror symmetry. In each case, conserved amino acid motifs mediate the stereo-specific recognition and reduction of the substrate. Unlike the MsrA domain, the MsrB domain activates the cysteine or selenocysteine nucleophile through a unique Cys-Arg-Asp/Glu catalytic triad. The collapse of the reaction intermediate most likely results in the formation of a sulfenic or selenenic acid moiety. Regeneration of the active site occurs through a series of thiol-disulfide exchange steps involving another active site Cys residue and thioredoxin. These observations have broad implications for modular catalysis, antibiotic drug design and continuing longevity studies in mammals." citations,ref_7,6051,238557,8,,reference citation,,,10799493,,"Moskovitz J. et al. (2000) J. Biol. Chem., 275, 14167-14172",Identification and characterization of a putative active site for peptide methionine sulfoxide reductase (MsrA) and its substrate stereospecificity.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,275,19,,0021-9258,,,,,,,,,,,,,,,,,,,,14167,14172,2000,"Peptide methionine sulfoxide reductases (MsrA) from many different organisms share a consensus amino acid sequence (GCFWG) that could play an important role in their active site. Site-directed single substitution of each of these amino acids except glycines in the yeast MsrA resulted in total loss of enzyme activity. Nevertheless, all the recombinant MsrA mutants and native proteins had a very similar circular dichroism spectrum. The demonstration that either treatment with iodoacetamide or replacement of the motif cysteine with serine leads to inactivation of the enzyme underscores the singular importance of cysteine residues in the activity of MsrA. The recombinant yeast MsrA was used for general characterization of the enzyme. Its K(m) value was similar to the bovine MsrA and appreciably lower than the K(m) of the bacterial enzyme. Also, it was shown that the enzymatic activity increased dramatically with increasing ionic strength. The recombinant yeast MsrA activity and the reduction activity of free methionine sulfoxide(s) were stereoselective toward the L-methionine S-sulfoxide and S-methyl p-tolyl sulfoxide. It was established that a methionine auxotroph yeast strain could grow on either form of L-methionine sulfoxide." citations,entry_citation,6069,238933,1,,entry citation,,,15096213,,,"NMR Solution Structure of the Precursor for Carnobacteriocin B2, an Antimicrobial Peptide from Carnobacterium piscicola.",published,journal,Eur. J. Biochem.,,271,9,,,,,,,,,,,,,,,,,,,,,,1748,1756,2004, citations,reference_citation,6087,239303,2,,reference citation,,,19009258,,,Structural and functional analysis of the HCV p7 protein.,published,journal,Methods Mol. Biol.,Methods in molecular biology,510,,,,,,,,,,,,,,,,,,,,,,,125,43,2009, citations,entry_citation,6088,239323,1,,entry citation,,,15182185,,,"DESIGN AND CHARACTERIZATION OF HELICAL PEPTIDES THAT BIND THE E6 PROTEIN OF PAPILLOMAVIRUS",published,journal,Biochemistry,,43,23,,,,,,,,,,,,,,,,,,,,,,7421,7431,2004, citations,entry_citation,6089,239341,1,,entry citation,,,15823028,,,Soluting the molecular structure of mung bean lipid transfer protein 1,published,journal,Biochemistry,,44,15,,,,,,,,,,,,,,,,,,,,,,5703,5712,2005, citations,entry_citation,6090,239355,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N resonance assignement of the reduced form of methionine sulfoxide reductase A from Escherichia coli",published,journal,J. Biomol. NMR,,30,3,,,,,,,,,,,,,,,,,,,,,,363,364,2004, citations,ref_8,6051,238558,9,,reference citation,,,11812798,,"Olry A. et al. (2002) J. Biol. Chem., 277, 12016-12022","Characterization of the methionine sulfoxide reductase activities of PILB, a probable virulence factor from Neisseria meningitidis.",published,journal,J. Biol. Chem.,The Journal of biological chemistry,277,14,,0021-9258,,,,,,,,,,,,,,,,,,,,12016,12022,2002,"PILB has been described as being involved in the virulence of bacteria of Neisseria genus. The PILB protein is composed of three subdomains. In the present study, the central subdomain (PILB-MsrA), the C terminus subdomain (PILB-MsrB), and the fused subdomain (PILB-MsrA/MsrB) of N. meningitidis were produced as folded entities. The central subdomain shows a methionine sulfoxide reductase A (MsrA) activity, whereas PILB-MsrB displays a methionine sulfoxide reductase B (MsrB) activity. The catalytic mechanism of PILB-MsrB can be divided into two steps: 1) an attack of the Cys-494 on the sulfur atom of the sulfoxide substrate, leading to formation of a sulfenic acid intermediate and release of 1 mol of methionine/mol of enzyme and 2) a regeneration of Cys-494 via formation of an intradisulfide bond with Cys-439 followed by reduction with thioredoxin. The study also shows that 1) MsrA and MsrB display opposite stereoselectivities toward the sulfoxide function; 2) the active sites of both Msrs, particularly MsrB, are rather adapted for binding protein-bound MetSO more efficiently than free MetSO; 3) the carbon Calpha is not a determining factor for efficient binding to both Msrs; and 4) the presence of the sulfoxide function is a prerequisite for binding to Msrs. The fact that the two Msrs exhibit opposite stereoselectivities argues for a structure of the active site of MsrBs different from that of MsrAs. This is further supported by the absence of sequence homology between the two Msrs in particular around the cysteine that is involved in formation of the sulfenic acid derivative. The fact that the catalytic mechanism takes place through formation of a sulfenic acid intermediate for both Msrs supports the idea that sulfenic acid chemistry is a general feature in the reduction of sulfoxides by thiols." citations,ref_9,6051,238559,10,,reference citation,,,10437782,,"Sharov V.S. et al (1999) FEBS lett., 455, 247-250",Diastereoselective reduction of protein-bound methionine sulfoxide by methionine sulfoxide reductase.,published,journal,FEBS Lett.,FEBS letters,455,3,,0014-5793,,,,,,,,,,,,,,,,,,,,247,250,1999,"Methionine sulfoxide (MetSO) in calmodulin (CaM) was previously shown to be a substrate for bovine liver peptide methionine sulfoxide reductase (pMSR, EC 1.8.4.6), which can partially recover protein structure and function of oxidized CaM in vitro. Here, we report for the first time that pMSR selectively reduces the D-sulfoxide diastereomer of CaM-bound L-MetSO (L-Met-D-SO). After exhaustive reduction by pMSR, the ratio of L-Met-D-SO to L-Met-L-SO decreased to about 1:25 for hydrogen peroxide-oxidized CaM, and to about 1:10 for free MetSO. The accumulation of MetSO upon oxidative stress and aging in vivo may be related to incomplete, diastereoselective, repair by pMSR." citations,ref_10,6051,238560,11,,reference citation,,,12913416,,"Zheng D. et al. (2003) J. Biomol. NMR, 27, 183-184","1H, 13C and 15N resonance assignments for methionine sulfoxide reductase B from Bacillus subtilis.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,27,2,,0925-2738,,,,,,,,,,,,,,,,,,,,183,184,2003, citations,entry_citation,6052,238574,1,,entry citation,,,,,,"Backbone and side chain 1H, 13C, and 15N chemical shift assignments for Haemophilus human protein HR969",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_1,6052,238575,2,,reference citation,,,12565051,,"Schwieters CD, Kuszewski JJ, Tjandra N, Marius Clore G. The Xplor-NIH NMR molecular structure determination package. J Magn Reson. 2003 Jan;160(1):65-73. PMID: 12565051",The Xplor-NIH NMR molecular structure determination package.,published,journal,J. Magn. Reson.,"Journal of magnetic resonance (San Diego, Calif. : 1997)",160,1,,1090-7807,,,,,,,,,,,,,,,,,,,,65,73,2003,"We announce the availability of the Xplor-NIH software package for NMR biomolecular structure determination. This package consists of the pre-existing XPLOR program, along with many NMR-specific extensions developed at the NIH. In addition to many features which have been developed over the last 20 years, the Xplor-NIH package contains an interface with a new programmatic framework written in C++. This interface currently supports the general purpose scripting languages Python and TCL, enabling rapid development of new tools, such as new potential energy terms and new optimization methods. Support for these scripting languages also facilitates interaction with existing external programs for structure analysis, structure manipulation, visualization, and spectral analysis." citations,entry_citation,6053,238597,1,,entry citation,,,15213462,,,"Letter to the Editer: 1H, 13C and 15N resonance assignments of the N-terminal 16 kDa domain of Escherichia coli Ada Protein",published,journal,J. Biomol. NMR,,29,3,,,,,,,,,,,,,,,,,,,,,,447,448,2004, citations,entry_citation,6054,238618,1,,entry citation,,,15213462,,,"Letter to the Editer: 1H, 13C and 15N resonance assignments of the N-terminal 16 kDa domain of Escherichia coli Ada Protein",published,journal,J. Biomol. NMR,,29,3,,,,,,,,,,,,,,,,,,,,,,447,448,2004, citations,entry_citation,6055,238634,1,,entry citation,,,15213467,,,"Letter to the Editor: 1H, 15N, and 13C resonance assignment of the 23 kDa organomercurial lyase MerB in its free and mercury-bound forms",published,journal,J. Biomol. NMR,,29,3,,,,,,,,,,,,,,,,,,,,,,457,458,2004, citations,entry_citation,6056,238668,1,,entry citation,,,15001703,,,"Structural basis for the function of a minimembrane protein subunit of yeast oligosaccharyltransferase",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,101,11,,,,,,,,,,,,,,,,,,,,,,3821,3826,2004, citations,ref-1,6056,238669,2,,reference citation,,,8520220,,"Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. J Biomol NMR. 1995 Nov;6(3):277-93",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref-2,6056,238670,3,,reference citation,,,,,"B. A. Johnson, R. A. Blevins J. Biomol. NMR 1994 4, 603-614",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6085,239258,1,,entry citation,,,15546886,,,"Bass hepcidin: Synthesis, solution structure, antimicrobial activities and synergism, and in vivo hepatic response to bacterial infections",published,journal,J. Biol. Chem.,,280,10,,,,,,,,,,,,,,,,,,,,,,9272,9282,2005, citations,entry_citation,6086,239277,1,,entry citation,,,15243188,,,"Letter to the Editor: 1H, 13C and 15N assignments of the tandem WW domains of human MAGI-1/BAP-1",published,journal,J. Biomol. NMR,,29,4,,,,,,,,,,,,,,,,,,,,,,539,540,2004, citations,ref-3,6056,238671,4,,reference citation,,,9367762,,"Guntert P, Mumenthaler C, Wuthrich K. J Mol Biol. 1997 Oct 17;273(1):283-98.",Torsion angle dynamics for NMR structure calculation with the new program DYANA.,published,journal,J. Mol. Biol.,Journal of molecular biology,273,1,,0022-2836,,,,,,,,,,,,,,,,,,,,283,298,1997,"The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from distance constraints and torsion angle constraints collected by nuclear magnetic resonance (NMR) experiments performs simulated annealing by molecular dynamics in torsion angle space and uses a fast recursive algorithm to integrate the equations of motions. Torsion angle dynamics can be more efficient than molecular dynamics in Cartesian coordinate space because of the reduced number of degrees of freedom and the concomitant absence of high-frequency bond and angle vibrations, which allows for the use of longer time-steps and/or higher temperatures in the structure calculation. It also represents a significant advance over the variable target function method in torsion angle space with the REDAC strategy used by the predecessor program DIANA. DYANA computation times per accepted conformer in the ""bundle"" used to represent the NMR structure compare favorably with those of other presently available structure calculation algorithms, and are of the order of 160 seconds for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300 computer. Test calculations starting from conformers with random torsion angle values further showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures." citations,ref-4,6056,238672,5,,reference citation,,,12538267,,"Linge JP, Habeck M, Rieping W, Nilges M. Bioinformatics. 2003 Jan 22;19(2):315-6.",ARIA: automated NOE assignment and NMR structure calculation.,published,journal,Bioinformatics,"Bioinformatics (Oxford, England)",19,2,,1367-4803,,,,,,,,,,,,,,,,,,,,315,316,2003,"MOTIVATION: In the light of several ongoing structural genomics projects, faster and more reliable methods for structure calculation from NMR data are in great demand. The major bottleneck in the determination of solution NMR structures is the assignment of NOE peaks (nuclear Overhauser effect). Due to the high complexity of the assignment problem, most NOEs cannot be directly converted into unambiguous inter-proton distance restraints. RESULTS: We present version 1.2 of our program ARIA (Ambiguous Restraints for Iterative Assignment) for automated assignment of NOE data and NMR structure calculation. We summarize recent progress in correcting for spin diffusion with a relaxation matrix approach, representing non-bonded interactions in the force field and refining final structures in explicit solvent. We also discuss book-keeping, data exchange with spectra assignment programs and deposition of the analysed experimental data to the databases. AVAILABILITY: ARIA 1.2 is available from: http://www.pasteur.fr/recherche/unites/Binfs/aria/. SUPPLEMENTARY INFORMATION: XML DTDs (for chemical shifts and NOE crosspeaks), Python scripts for the conversion of various NMR data formats and the results of example calculations using data from the S. cerevisiae HRDC domain are available from: http://www.pasteur.fr/recherche/unites/Binfs/aria/" citations,entry_citation,6057,238691,1,,entry citation,,,15123602,,,"Solution structure of the tandem SH3 domains of p47phox in an autoinhibited form.",published,journal,J. Biol. Chem.,,29,3,,,,,,,,,,,,,,,,,,,,,,451,452,2004, citations,ref-1,6057,238692,2,,reference citation,,,8520220,,"Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR. 1995 Nov;6(3):277-93.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref-2,6057,238693,3,,reference citation,,,,,"Yokochi & Inagaki, unpublished http://fermi.pharm.hokudai.ac.jp",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6058,238708,1,,entry citation,,,15452442,,,"Letter to the Editor: 1H, 13C and 15N Assignments for the Archaeglobus fulgidis protein AF2095.",published,journal,J. Biomol. NMR,,30,1,,,,,,,,,,,,,,,,,,,,,,107,108,2004, citations,entry_citation,6059,238733,1,,entry citation,,,16698549,,,GTP-Ras disrupts the intramolecular complex of C1 and RA domains of Nore1,published,journal,Structure,,14,5,,,,,,,,,,,,,,,,,,,,,,881,888,2006, citations,entry_citation,606,238756,1,,entry citation,,,,,"Brown, Larry R., Wuthrich, Kurt, ""Melittin Bound to Dodecylphosphocholine Micelles 1H-NMR Assignments and Global Conformational Features,"" Biochim. Biophys. Acta 647, 95-111 (1981).","Melittin Bound to Dodecylphosphocholine Micelles 1H-NMR Assignments and Global Conformational Features",published,journal,Biochim. Biophys. Acta,,647,,,,,,,,,,,,,,,,,,,,,,,95,111,1981, citations,entry_citation,6060,238770,1,,entry citation,,,14725761,,,"A closed binding pocket and global destabilization modify the binding properties of an alternatively spliced form of the second PDZ domain of PTP-BL",published,journal,Structure,,12,1,,,,,,,,,,,,,,,,,,,,,,11,20,2004, citations,entry_citation,6061,238791,1,,entry citation,,,15452437,,,"Characterisation of a mobile protein-binding epitope in the translocation domain of colicin E9",published,journal,J. Biomol. NMR,,30,1,,,,,,,,,,,,,,,,,,,,,,81,96,2004, citations,entry_citation,6062,238817,1,,entry citation,,,15317975,,,"Solution structure of the pseudo-5' splice site of a retroviral splicing suppressor",published,journal,RNA,,10,9,,,,,,,,,,,,,,,,,,,,,,1388,1398,2004, citations,entry_citation,6063,238836,1,,entry citation,,,15182185,,,"DESIGN AND CHARACTERIZATION OF HELICAL PEPTIDES THAT INHIBIT THE E6 PROTEIN OF PAPILLOMAVIRUS",published,journal,Biochemistry,,43,23,,,,,,,,,,,,,,,,,,,,,,7421,7431,2004, citations,entry_citation,6064,238854,1,,entry citation,,,15182185,,,"DESIGN AND CHARACTERIZATION OF HELICAL PEPTIDES THAT INHIBIT THE E6 PROTEIN OF PAPILLOMAVIRUS",published,journal,Biochemistry,,43,23,,,,,,,,,,,,,,,,,,,,,,7421,7431,2004, citations,entry_citation,6445,246611,1,,entry citation,,,,,,NMR Assignment of the Six Zinc Fingers of MTF-1 in the Free and DNA Bound States,published,journal,J. Biomol. NMR,,31,1,,,,,,,,,,,,,,,,,,,,,,94,94,2005, citations,ref_1,6069,238934,2,,reference citation,,,8520220,,"Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J. & Bax, A. J. Biomol. NMR. 6, 277-93",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref_2,6069,238935,3,,reference citation,,,,,"Johnson, B. A. & Blevins, R. A. J. Biomol. NMR. 4, 603-614",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6070,238952,1,,entry citation,,,15070353,,,"Distributed Computing and NMR Constraint-Based High-Resolution Structure Determination, Applied for Bioactive Peptide Endothelin-1 to Determine C-terminal Folding",published,journal,J. Am. Chem. Soc.,,124,14,,,,,,,,,,,,,,,,,,,,,,4504,4505,2004, citations,entry_citation,6071,238966,1,,entry citation,,,15213466,,,"Letter to the editor: 1H, 13C and 15N Resonance Assignments and the Secondary Structures of Human Coactosin Like Protein (hCLP) D123N",published,journal,J. Biomol. NMR,,29,3,,,,,,,,,,,,,,,,,,,,,,455,456,2004, citations,entry_citation,6072,238999,1,,entry citation,,,15133049,,,"NMR structure of the N-terminal domain of SUMO ligase PIAS1 and its interaction with tumor suppressor p53 and A/T-rich DNA ologomers.",published,journal,J. Biol. Chem.,,279,30,,,,,,,,,,,,,,,,,,,,,,31455,31461,2004, citations,entry_citation,6073,239013,1,,entry citation,,,15897454,,,"A prokaryotic superoxide dismutase paralog lacking two Cu ligands: From largely unstructured in solution to ordered in the crystal",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,102,21,,,,,,,,,,,,,,,,,,,,,,7541,7546,2005, citations,entry_citation,6074,239050,1,,entry citation,,,15213470,,,"Letter to the Editor: Backbone 1H, 13C and 15N resonance assignments for a 29kD Monomeric Variant of Pseudomonas aeruginosa dimethylarginine dimethylaminohydrolase",published,journal,J. Biomol. NMR,,29,3,,,,,,,,,,,,,,,,,,,,,,463,464,2004, citations,entry_citation,6075,239068,1,,entry citation,,,15213468,,,"Letter to the Editor: 1H, 13C and 15N resonance assignments of a Bacillus Subtilis arsenate reductase",published,journal,J. Biomol. NMR,,29,3,,,,,,,,,,,,,,,,,,,,,,459,460,2004, citations,entry_citation,6076,239089,1,,entry citation,,,15134450,,,"NMR Structures of Loop B RNAs from the Stem-Loop IV Domain of the Enterovirus Internal Ribosome Entry Site: A Single C to U Substitution Drastically Changes the Shape and Flexibility of RNA",published,journal,Biochemistry,,43,19,,,,,,,,,,,,,,,,,,,,,,5757,5771,2004, citations,entry_citation,6077,239118,1,,entry citation,,,15134450,,,"NMR Structures of Loop B RNAs from the Stem-Loop IV Domain of the Enterovirus Internal Ribosome Entry Site: A Single C-to-U Substitution Drastically Changes the Shape and Flexibility of RNA",published,journal,Biochemistry,,43,19,,,,,,,,,,,,,,,,,,,,,,5757,5771,2004, citations,entry_citation,6078,239144,1,,entry citation,,,15065849,,,"IA3, an Aspartic Proteinase Inhibitor from Saccharomyces cerevisiae, Is Intrinsically Unstructured in Solution.",published,journal,Biochemistry,,43,14,,,,,,,,,,,,,,,,,,,,,,4071,4081,2004, citations,entry_citation,6079,239156,1,,entry citation,,,15557810,,,"Letter to the Editor: 1H, 13C and 15N resonance assignment of the reduced form of thioredoxin h1 from Poplar, a CPPC active site variant",published,journal,J. Biomol. NMR,,30,2,,,,,,,,,,,,,,,,,,,,,,229,230,2004, citations,entry_citation,6080,239169,1,,entry citation,,,15213447,,,"Letter to the Editor: 1H, 15N, 13C resonance assignments of the human protein tyrosine phosphatase PRL-1",published,journal,J. Biomol. NMR,,29,3,,,,,,,,,,,,,,,,,,,,,,417,418,2004, citations,entry_citation,6081,239187,1,,entry citation,,,15213469,,,"Letter to the Editor: 1H, 15N and 13C Resonances of Holo Isoform 4 of Lethocerus Indicus Troponin C",published,journal,J. Biomol. NMR,,29,3,,,,,,,,,,,,,,,,,,,,,,461,462,2004, citations,citation_1,6081,239188,2,,reference citation,,,12558500,,"Qiu F, Lakey A, Agianian B, Hutchings A, Butcher GW, Labeit S, Leonard K, Bullard B. Troponin C in different insect muscle types: identification of two isoforms in Lethocerus, Drosophila and Anopheles that are specific to asynchronous flight muscle in the adult insect. Biochem J. 2003 May 1; 371(Pt 3): 811-21.","Troponin C in different insect muscle types: identification of two isoforms in Lethocerus, Drosophila and Anopheles that are specific to asynchronous flight muscle in the adult insect.",published,journal,Biochem. J.,The Biochemical journal,371,Pt 3,,0264-6021,,,,,,,,,,,,,,,,,,,,811,821,2003,"The indirect flight muscles (IFMs) of Lethocerus (giant water bug) and Drosophila (fruitfly) are asynchronous: oscillatory contractions are produced by periodic stretches in the presence of a Ca(2+) concentration that does not fully activate the muscle. The troponin complex on thin filaments regulates contraction in striated muscle. The complex in IFM has subunits that are specific to this muscle type, and stretch activation may act through troponin. Lethocerus and Drosophila have an unusual isoform of the Ca(2+)-binding subunit of troponin, troponin C (TnC), with a single Ca(2+)-binding site near the C-terminus (domain IV); this isoform is only in IFMs, together with a minor isoform with an additional Ca(2+)-binding site in the N-terminal region (domain II). Lethocerus has another TnC isoform in leg muscle which also has two Ca(2+)-binding sites. Ca(2+) binds more strongly to domain IV than to domain II in two-site isoforms. There are four isoforms in Drosophila and Anopheles (malarial mosquito), three of which are also in adult Lethocerus. A larval isoform has not been identified in Lethocerus. Different TnC isoforms are expressed in the embryonic, larval, pupal and adult stages of Drosophila; the expression of the two IFM isoforms is increased in the pupal stage. Immunoelectron microscopy shows the distribution of the major IFM isoform with one Ca(2+)-binding site is uniform along Lethocerus thin filaments. We suggest that initial activation of IFM is by Ca(2+) binding to troponin with the two-site TnC, and full activation is through the action of stretch on the complex with the one-site isoform." citations,entry_citation,6082,239217,1,,entry citation,,,15170335,,,"Solution structure of a Methionine-Rich 2S Albumin form Sunflower Seeds: Relationship to Its Allergenic and Emulsifying Properties(,).",published,journal,Biochemistry,,43,22,,,,,,,,,,,,,,,,,,,,,,6976,6986,2004, citations,entry_citation,6083,239232,1,,entry citation,,,,,,"Specific recognition between surface loop 2 (132-143) and helix 1 (144-154) within sheep prion protein from in vitro studies of synthetic peptides",submitted,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,2004, citations,entry_citation,6084,239245,1,,entry citation,,,15213439,,,"Letter to the Editor: NMR structure of a variant 434 repressor DNA-binding domain devoid of hydroxyl groups",published,journal,J. Biomol. NMR,,29,3,,,,,,,,,,,,,,,,,,,,,,395,398,2004, citations,entry_citation,6091,239379,1,,entry citation,,,14725761,,,"A closed binding pocket and global destabilization modify the binding properties of an alternatively spliced form of the second PDZ domain of PTP-BL",published,journal,Structure,,12,1,,,,,,,,,,,,,,,,,,,,,,11,20,2004, citations,entry_citation,6092,239399,1,,entry citation,,,14725761,,,"A closed binding pocket and global destabilization modify the binding properties of an alternatively spliced form of the second PDZ domain of PTP-BL",published,journal,Structure,,12,1,,,,,,,,,,,,,,,,,,,,,,11,20,2004, citations,entry_citation,6093,239419,1,,entry citation,,,14992719,,,"Structure of the regulatory hyaluronan binding domain in the inflamatory leukocyte homing receptor CD44",published,journal,Mol. Cell,,13,4,,,,,,,,,,,,,,,,,,,,,,483,496,2004, citations,entry_citation,6094,239442,1,,entry citation,,,15003457,,,"NMR structure of the 101 nucleotide core encapsidation signal of the moloney murine leukemia virus",published,journal,J. Mol. Biol.,,337,2,,,,,,,,,,,,,,,,,,,,,,427,442,2004, citations,entry_citation,6095,239464,1,,entry citation,,,15019774,,,"Solution structure of the KIX domain of CBP bound to the transactivation domain of c-Myb",published,journal,J. Mol. Biol.,,337,3,,,,,,,,,,,,,,,,,,,,,,521,534,2004, citations,entry_citation,6096,239481,1,,entry citation,,,14767079,,,"The solution structure of the pH-induced monomer of dynein light-chain LC8 from Drosophila",published,journal,Protein Sci.,,13,3,,,,,,,,,,,,,,,,,,,,,,727,734,2004, citations,entry_citation,6097,239511,1,,entry citation,,,15312772,,,The structure and biochemical properties of the human spliceosomal protein U1C,published,journal,J. Mol. Biol.,,341,1,,,,,,,,,,,,,,,,,,,,,,185,198,2004, citations,entry_citation,6098,239531,1,,entry citation,,,,,,"Structural and functional studies on transcriptional activation - Interactions of the cofactor PC4 and activator VP16",published,thesis,,,,,,,,,,,,,,,,,,,,,,Utrecht University,Utrecht,The Netherlands,,,,2003, citations,entry_citation,6099,239554,1,,entry citation,,,,,,"Structural and functional studies on transcriptional activation - Interactions of the cofactor PC4 and activator VP16",published,thesis,,,,,,,,,,,,,,,,,,,,,,Utrecht University,Utrecht,The Netherlands,,,,2003, citations,entry_citation,6100,239573,1,,entry citation,,,15243191,,,"Letter to the Editor: Backbone resonance assignments of the 18.5kDa isoform of murine myelin basic protein (MBP)",published,journal,J. Biomol. NMR,,29,4,,,,,,,,,,,,,,,,,,,,,,545,546,2004, citations,entry_citation,6101,239591,1,,entry citation,,,12115137,,,"Solution Structure of a D,L-Alternating Oligonorleucine as a Model of Double-Stranded Antiparallel beta-helix",published,journal,Biopolymers,,64,4,,,,,,,,,,,,,,,,,,,,,,198,209,2002, citations,entry_citation,6102,239609,1,,entry citation,,,,,,Structural similarity of Ybed protein from Escherichia coli to allosteric regulatory domains,published,journal,J. Bacteriol.,,186,23,,,,,,,,,,,,,,,,,,,,,,8083,8088,2004, citations,entry_citation,6103,239629,1,,entry citation,,,15155727,,,Unexpected structure of the Ca2+-regulatory region from soybean calcium-dependent protein kinase-alpha,published,journal,J. Biol. Chem.,,279,34,,,,,,,,,,,,,,,,,,,,,,35494,35502,2004, citations,entry_citation,6104,239649,1,,entry citation,,,15155727,,,Unexpected structure of the Ca2+-regulatory region from soybean calcium-dependent protein kinase-alpha,published,journal,J. Biol. Chem.,,279,34,,,,,,,,,,,,,,,,,,,,,,35494,35502,2004, citations,entry_citation,6105,239673,1,,entry citation,,,14755580,,,"Conformational and structural analysis of the equilibrium between single- and double-strand beta-helix of a D,L-alternating oligonorleucine",published,journal,Biopolymers,,73,2,,,,,,,,,,,,,,,,,,,,,,229,241,2004, citations,entry_citation,6106,239691,1,,entry citation,,,14988012,,,"Correlation between conformation and antibody binding: NMR structure of cross-reactive peptides from T. cruzi, Human and L. braziliensis",published,journal,FEBS Lett.,,560,1-3,,,,,,,,,,,,,,,,,,,,,,134,140,2004, citations,entry_citation,6107,239707,1,,entry citation,,,14988012,,,"Correlation between conformation and antibody binding: NMR structure of cross-reactive peptides from T.cruzi, Human and L. braziliensis",published,journal,FEBS Lett.,,560,1-3,,,,,,,,,,,,,,,,,,,,,,134,140,2004, citations,entry_citation,6108,239723,1,,entry citation,,,15161493,,,Structure of GlgS from Escherichia coli suggests a role in protein-protein interactions,published,journal,BMC Biol.,,2,1,,,,,,,,,,,,,,,,,,,,,,10,10,2004, citations,entry_citation,6109,239742,1,,entry citation,,,12906891,,,"BmKK4, a novel toxin from the venom of Asian scorpion Buthus martensi Karsch, inhibits potassium currents in rat hippocampal neurons in vitro",published,journal,Toxicon,,42,,,,,,,,,,,,,,,,,,,,,,,199,205,2003, citations,entry_citation,611,239762,1,,entry citation,,,,,"Inagaki, Fuyuhiko, Clayden, Nigel J., Tamiya, Nobuo, Williams, Robert J. P., ""A Proton-Magnetic-Resonance Study on the Molecular Conformation and Structure-Function Relationship of a Long Neurotoxin, Laticauda Semifasciata III from Laticauda semifasciata,"" Eur. J. Biochem. 120, 313-322 (1981).","A Proton-Magnetic-Resonance Study on the Molecular Conformation and Structure-Function Relationship of a Long Neurotoxin, Laticauda Semifasciata III from Laticauda semifasciata",published,journal,Eur. J. Biochem.,,120,,,,,,,,,,,,,,,,,,,,,,,313,322,1981, citations,entry_citation,6110,239775,1,,entry citation,,,15366933,,,Solution structure of a chimeric LEKTI domain reveals a chameleon sequence,published,journal,Biochemistry,,43,35,,,,,,,,,,,,,,,,,,,,,,11238,11247,2004, citations,entry_citation,6111,239792,1,,entry citation,,,15452439,,,"1H, 13C and 15N resonance assignments of the antifreeze protein cfAFP-501 from spruce budworm at different temperatures",published,journal,J. Biomol. NMR,,30,1,,,,,,,,,,,,,,,,,,,,,,101,102,2004, citations,citation_1,6111,239793,2,,reference citation,,,,,,NMR structure note: Solution Structure of an Antifreeze Protein CfAFP-501 from Choristoneura fumiferana,published,journal,J. Biomol. NMR,,32,3,,,,,,,,,,,,,,,,,,,,,,251,256,2005, citations,entry_citation,6112,239809,1,,entry citation,,,15024385,,,p27 binds cyclin-CDK complexes through a sequential mechanism involving binding-induced protein folding,published,journal,Nat. Struct. Mol. Biol.,,11,4,,,,,,,,,,,,,,,,,,,,,,358,364,2004, citations,entry_citation,6113,239823,1,,entry citation,,,,,,Solution Structure of the Second PDZ Domain of the Neuronal Adaptor X11alpha and its Interaction with the C-terminal Peptide of the Human Copper Chaperone for Superoxide Dismutase,published,journal,J. Biomol. NMR,,32,3,,,,,,,,,,,,,,,,,,,,,,209,218,2005, citations,entry_citation,6114,239840,1,,entry citation,,,15557806,,,"1H, 13C and 15N resonance assignment of the C-terminal BRCT domain from human BRCA1",published,journal,J. Biomol. NMR,,30,2,,,,,,,,,,,,,,,,,,,,,,221,222,2004, citations,entry_citation,6115,239858,1,,entry citation,,,15314212,,,High resolution Structure of a Picornaviral Internal Cis-acting RNA Replication Element (cre),published,journal,Proc. Natl. Acad. Sci. U.S.A.,,101,34,,,,,,,,,,,,,,,,,,,,,,12688,12693,2004, citations,entry_citation,6174,240858,1,,entry citation,,,15256595,,,Structure of the C-terminal domain of the clock protein KaiA in complex with a KaiC-derived peptide: Implications for KaiC regulation,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,101,30,,,,,,,,,,,,,,,,,,,,,,10925,10930,2004, citations,entry_citation,6175,240878,1,,entry citation,,,16736493,,,Solution structures of the first and fourth TSR domains of F-spondin,published,journal,Proteins,,64,3,,,,,,,,,,,,,,,,,,,,,,665,672,2006, citations,ref_1,6115,239859,2,,reference citation,,,12097561,,"Yang Y, Rijnbrand R, McKnight KL, Wimmer E, Paul A, Martin A, Lemon SM. J Virol. 2002 Aug;76(15):7485-94.",Sequence requirements for viral RNA replication and VPg uridylylation directed by the internal cis-acting replication element (cre) of human rhinovirus type 14.,published,journal,J. Virol.,Journal of virology,76,15,,0022-538X,,,,,,,,,,,,,,,,,,,,7485,7494,2002,"Until recently, the cis-acting signals required for replication of picornaviral RNAs were believed to be restricted to the 5' and 3' noncoding regions of the genome. However, an RNA stem-loop in the VP1-coding sequence of human rhinovirus type 14 (HRV-14) is essential for viral minus-strand RNA synthesis (K. L. McKnight and S. M. Lemon, RNA 4:1569-1584, 1998). The nucleotide sequence of the apical loop of this internal cis-acting replication element (cre) was critical for RNA synthesis, while secondary RNA structure, but not primary sequence, was shown to be important within the duplex stem. Similar cres have since been identified in other picornaviral genomes. These RNA segments appear to serve as template for the uridylylation of the genome-linked protein, VPg, providing the VPg-pUpU primer required for viral RNA transcription (A. V. Paul et al., J. Virol. 74:10359-10370, 2000). Here, we show that the minimal functional HRV-14 cre resides within a 33-nucleotide (nt) RNA segment that is predicted to form a simple stem-loop with a 14-nt loop sequence. An extensive mutational analysis involving every possible base substitution at each position within the loop segment defined the sequence that is required within this loop for efficient replication of subgenomic HRV-14 replicon RNAs. These results indicate that three consecutive adenosine residues (nt 2367 to 2369) within the 5' half of this loop are critically important for cre function and suggest that a common RNNNAARNNNNNNR loop motif exists among the cre sequences of enteroviruses and rhinoviruses. We found a direct, positive correlation between the capacity of mutated cres to support RNA replication and their ability to function as template in an in vitro VPg uridylylation reaction, suggesting that these functions are intimately linked. These data thus define more precisely the sequence and structural requirements of the HRV-14 cre and provide additional support for a model in which the role of the cre in RNA replication is to act as template for VPg uridylylation." citations,ref_2,6115,239860,3,,reference citation,,,9848654,,"McKnight KL, Lemon SM. RNA. 1998 Dec;4(12):1569-84.",The rhinovirus type 14 genome contains an internally located RNA structure that is required for viral replication.,published,journal,RNA,"RNA (New York, N.Y.)",4,12,,1355-8382,,,,,,,,,,,,,,,,,,,,1569,1584,1998,"Cis-acting RNA signals are required for replication of positive-strand viruses such as the picornaviruses. Although these generally have been mapped to the 5' and/or 3' termini of the viral genome, RNAs derived from human rhinovirus type 14 are unable to replicate unless they contain an internal cis-acting replication element (cre) located within the genome segment encoding the capsid proteins. Here, we show that the essential cre sequence is 83-96 nt in length and located between nt 2318-2413 of the genome. Using dicistronic RNAs in which translation of the P1 and P2-P3 segments of the polyprotein were functionally dissociated, we further demonstrate that translation of the cre sequence is not required for RNA replication. Thus, although it is located within a protein-coding segment of the genome, the cre functions as an RNA entity. Computer folds suggested that cre sequences could form a stable structure in either positive- or minus-strand RNA. However, an analysis of mutant RNAs containing multiple covariant and non-covariant nucleotide substitutions within these putative structures demonstrated that only the predicted positive-strand structure is essential for efficient RNA replication. The absence of detectable minus-strand synthesis from RNAs that lack the cre suggests that the cre is required for initiation of minus-strand RNA synthesis. Since a lethal 3' noncoding region mutation could be partially rescued by a compensating mutation within the cre, the cre appears to participate in a long-range RNA-RNA interaction required for this process. These data provide novel insight into the mechanisms of replication of a positive-strand RNA virus, as they define the involvement of an internally located RNA structure in the recognition of viral RNA by the viral replicase complex. Since internally located RNA replication signals have been shown to exist in several other positive-strand RNA virus families, these observations are potentially relevant to a wide array of related viruses." citations,entry_citation,6116,239875,1,,entry citation,,,15452443,,,"Backbone 1H, 13C and 15N resonance assignment of the N-terminal domain of human eRF1",published,journal,J. Biomol. NMR,,30,1,,,,,,,,,,,,,,,,,,,,,,109,110,2004, citations,entry_citation,6117,239888,1,,entry citation,,,15306028,,,"The solution structure of ChaB, a putative membrane ion antiporter regulator from Escherichia coli",published,journal,BMC Struct. Biol.,,4,1,,,,,,,,,,,,,,,,,,,,,,9,9,2004, citations,entry_citation,6118,239903,1,,entry citation,,,,,,"1H, 13C and 15N resonance assignments of poplar phloem glutaredoxin",published,journal,J. Biomol. NMR,,30,2,,,,,,,,,,,,,,,,,,,,,,219,220,2004, citations,entry_citation,6120,239919,1,,entry citation,,,11259647,,,Resonance assignments for the 18 kDa protein CC1736 from Caulobacter crescentus,published,journal,J. Biomol. NMR,,29,4,,,,,,,,,,,,,,,,,,,,,,549,550,2004, citations,ref_1,6120,239920,2,,reference citation,,,11259647,,"Nierman WC, Feldblyum TV, Laub MT, Paulsen IT, Nelson KE, Eisen JA, Heidelberg JF, Alley MR, Ohta N, Maddock JR, Potocka I, Nelson WC, Newton A, Stephens C, Phadke ND, Ely B, DeBoy RT, Dodson RJ, Durkin AS, Gwinn ML, Haft DH, Kolonay JF, Smit J, Craven MB, Khouri H, Shetty J, Berry K, Utterback T, Tran K, Wolf A, Vamathevan J, Ermolaeva M, White O, Salzberg SL, Venter JC, Shapiro L, Fraser CM, Eisen J. Related Articles, Links Free in PMC Complete genome sequence of Caulobacter crescentus. Proc Natl Acad Sci U S A. 2001 Mar 27;98(7):4136-41",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6121,239933,1,,entry citation,,,,,,"1H, 15N, and 13C chemical shift assignments of RNA repeats binding protein - CUGBP1ab",published,journal,J. Biomol. NMR,,30,3,,,,,,,,,,,,,,,,,,,,,,371,372,2004, citations,entry_citation,6122,239948,1,,entry citation,,,,,,Structural Characterization of the RNase E S1 domain and identification of its Oligonucleotide-binding and Dimerization Interfaces,published,journal,J. Mol. Biol.,,341,1,,,,,,,,,,,,,,,,,,,,,,37,54,2004, citations,entry_citation,6123,239962,1,,entry citation,,,15368576,,,"NMR and modeling studies of protein-carbohydrate interactions: synthesis, three-dimensional structure, and recognition properties of a minimum hevein domain with binding affinity for chitooligosaccharides",published,journal,ChemBioChem,,5,9,,,,,,,,,,,,,,,,,,,,,,1245,1245,2004, citations,reference-1,6123,239963,2,,reference citation,,,7607237,,"Asensio JL, Canada FJ, Bruix M, Rodriguez-Romero A, Jimenez-Barbero J. Eur J Biochem. 1995 Jun 1;230(2):621-33.",The interaction of hevein with N-acetylglucosamine-containing oligosaccharides. Solution structure of hevein complexed to chitobiose.,published,journal,Eur. J. Biochem.,European journal of biochemistry / FEBS,230,2,,0014-2956,,,,,,,,,,,,,,,,,,,,621,633,1995,"The three-dimensional structure of hevein, a small protein isolated from the latex of Hevea brasiliensis (rubber tree), in water solution has been obtained by using 1H-NMR spectroscopy and dynamic simulated annealing calculations. The average root-mean-square deviation (rmsd) of the best 20 refined structures generated using DIANA prior to simulated annealing was 0.092 nm for the backbone atoms and 0.163 nm for all heavy atoms (residues 3-41). The specific interaction of hevein with N-acetylglucosamine-containing oligosaccharides has also been analyzed by 1H-NMR. The association constants, Ka, for the binding of hevein to GlcNAc, chitobiose [GlcNAc-beta(1-->4)-GlcNAc], chitotriose [GlcNAc-beta(1-->4)-GlcNAc-beta(1-->4)-GlcNAc], and GlcNAc-alpha(1-->6)-Man have been estimated from 1H-NMR titration experiments. Since the measured Ka values for chitobiose binding are almost identical with and without calcium ions, it is shown that these cations are not required for sugar binding. The association increases in the order GlcNAc-alpha(1-->6)-Man < or = GlcNAc < chitobiose < chitotriose. The equilibrium thermodynamic parameters entropy and enthalpy of binding, delta S0 and delta H0, for the hevein-chitobiose and hevein-chitotriose associations have been obtained from van't Hoff analysis of the temperature dependence of the Ka values between 25-40 degrees C. The driving force for the binding process is provided for a negative delta H0 which is partially compensated by a negative delta S0. These negative signs seem to indicate that hydrogen bonding and van der Waals forces are the major interactions stabilizing the complex. Protein-carbohydrate nuclear Overhauser enhancements have allowed a three-dimensional model of the hevein-chitobiose complex to be built. From inspection of this model, a hydrogen bond between Ser19 and the non-reducing N-acetyl carbonyl group is suggested, as well as between Tyr30 and HO-3 of the same sugar residue. The N-acetyl methyl group of the non-reducing GlcNAc displays non-polar contacts to the aromatic Tyr30 and Trp21 residues. In addition, the higher affinities deduced for the beta-linked oligosaccharides with respect to GlcNAc and GlcNAc-alpha(1-->6)-Man can be explained by favourable stacking of the second beta-linked GlcNAc moiety and Trp21." citations,ref_1,6132,240135,2,,reference citation,,,11832487,,"Rouhier N, Gelhaye E, Jacquot JP. J Biol Chem. 2002 Apr 19;277(16):13609-14. Epub 2002 Feb 06.",Glutaredoxin-dependent peroxiredoxin from poplar: protein-protein interaction and catalytic mechanism.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,277,16,,0021-9258,,,,,,,,,,,,,,,,,,,,13609,13614,2002,"Recently, a poplar phloem peroxiredoxin (Prx) was found to accept both glutaredoxin (Grx) and thioredoxin (Trx) as proton donors. To investigate the catalytic mechanism of the Grx-dependent reduction of hydroperoxides catalyzed by Prx, a series of cysteinic mutants was constructed. Mutation of the most N-terminal conserved cysteine of Prx (Cys-51) demonstrates that it is the catalytic one. The second cysteine (Cys-76) is not essential for peroxiredoxin activity because the C76A mutant retained approximately 25% of the wild type Prx activity. Only one cysteine of the Grx active site (Cys-27) is essential for peroxiredoxin catalysis, indicating that Grx can act in this reaction either via a dithiol or a monothiol pathway. The creation of covalent heterodimers between Prx and Grx mutants confirms that Prx Cys-51 and Grx Cys-27 are the two residues involved in the catalytic mechanism. The integration of a third cysteine in position 152 of the Prx, making it similar in sequence to the Trx-dependent human Prx V, resulted in a protein that had no detectable activity with Grx but kept activity with Trx. Based on these experimental results, a catalytic mechanism is proposed to explain the Grx- and Trx-dependent activities of poplar Prx." citations,reference-2,6123,239964,3,,reference citation,,,8627629,,"Martins JC, Maes D, Loris R, Pepermans HA, Wyns L, Willem R, Verheyden P. J Mol Biol. 1996 May 3;258(2):322-33.","H NMR study of the solution structure of Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus.",published,journal,J. Mol. Biol.,Journal of molecular biology,258,2,,0022-2836,,,,,,,,,,,,,,,,,,,,322,333,1996,"The conformation in water of antimicrobial protein 2 from Amaranthus caudatus (Ac-AMP2) was determined using 1H NMR, DIANA and restrained molecular modeling. Ac-AMP2 is a 30 amino acid residue, lectin-like protein that specifically binds to chitin, a polymer of beta-1,4-N-acetyl-D-glucosamine. After sequence specific resonance assignments, a total of 198 distance restraints were collected from 2D NOESY buildup spectra at 500 MHz at pH 2, supplemented by a 2D NOESY spectrum at 600 MHz. The location of the three previously unassigned disulfide bridges was determined from preliminary DIANA structures, using a statistical analysis of intercystinyl distances. The solution structure of Ac-AMP2 is presented as a set of 26 DIANA structures, further refined by restrained molecular dynamics using a simulated annealing protocol in the AMBER force field, with a backbone r.m.s.d. for the well defined Glu3-Cys28 segment of 0.69(+/-0.12) angstroms. The main structural element is an antiparallel beta-sheet from Met13 to Lys23 including a betaI-turn over Gln17-Phel8 with a beta bulge at Gly19. In addition, a beta'I turn over Arg6-Gly7, a beta'III turn over Ser11-Gly12 and a helical turn from Gly24 to Cys28 are identified. This structure is very similar to the equivalent regions of the X-ray structure of wheat germ agglutinin and the NMR structure of hevein." citations,reference-3,6123,239965,4,,reference citation,,,9592123,,"Martins JC, Maes D, Loris R, Pepermans HA, Wyns L, Willem R, Verheyden P. J Mol Biol. 1996 May 3;258(2):322-33.",NMR investigations of protein-carbohydrate interactions: refined three-dimensional structure of the complex between hevein and methyl beta-chitobioside.,published,journal,Glycobiology,Glycobiology,8,6,,0959-6658,,,,,,,,,,,,,,,,,,,,569,577,1998,"The specific interaction of hevein with GlcNAc-containing oligosaccharides has been analyzed by1H-NMR spectroscopy. The association constants for the binding of hevein to a variety of ligands have been estimated from1H-NMR titration experiments. The association constants increase in the order GlcNAc-alpha(1-->6)-Man < GlcNAc < benzyl-beta-GlcNAc < p-nitrophenyl-beta-GlcNAc < chitobiose < p-nitrophenyl-beta-chitobioside < methyl-beta-chitobioside < chitotriose. Entropy and enthalpy of binding for different complexes have been obtained from van't Hoff analysis. The driving force for the binding process is provided by a negative DeltaH0which is partially compensated by negative DeltaS0. These negative signs indicate that hydrogen bonding and van der Waals forces are the major interactions stabilizing the complex. NOESY NMR experiments in water solution provided 475 accurate protein proton-proton distance constraints after employing the MARDIGRAS program. In addition, 15 unambiguous protein/carbohydrate NOEs were detected. All the experimental constraints were used in a refinement protocol including restrained molecular dynamics in order to determine the highly refined solution conformation of this protein-carbohydrate complex. With regard to the NMR structure of the free protein, no important changes in the protein nOe's were observed, indicating that carbohydrate-induced conformational changes are small. The average backbone rmsd of the 20 refined structures was 0.055 nm, while the heavy atom rmsd was 0.116 nm. It can be deduced that both hydrogen bonds and van der Waals contacts confer stability to the complex. A comparison of the three-dimensional structure of hevein in solution to those reported for wheat germ agglutinin (WGA) and hevein itself in the solid state has also been performed. The polypeptide conformation has also been compared to the NMR-derived structure of a smaller antifungical peptide, Ac-AMP2." citations,reference-4,6123,239966,5,,reference citation,,,10842338,,"Asensio JL, Siebert HC, von Der Lieth CW, Laynez J, Bruix M, Soedjanaamadja UM, Beintema JJ, Canada FJ, Gabius HJ, Jimenez-Barbero J. Proteins. 2000 Aug 1;40(2):218-36.","NMR investigations of protein-carbohydrate interactions: studies on the relevance of Trp/Tyr variations in lectin binding sites as deduced from titration microcalorimetry and NMR studies on hevein domains. Determination of the NMR structure of the complex between pseudohevein and N,N',N""-triacetylchitotriose.",published,journal,Proteins,Proteins,40,2,,0887-3585,,,,,,,,,,,,,,,,,,,,218,236,2000,"Model studies on lectins and their interactions with carbohydrate ligands in solution are essential to gain insights into the driving forces for complex formation and to optimize programs for computer simulations. The specific interaction of pseudohevein with N,N', N""-triacetylchitotriose has been analyzed by (1)H-NMR spectroscopy. Because of its small size, with a chain length of 45 amino acids, this lectin is a prime target to solution-structure determination by NOESY NMR experiments in water. The NMR-analysis was extended to assessment of the topology of the complex between pseudohevein and N, N',N""-triacetylchitotriose. NOESY experiments in water solution provided 342 protein proton-proton distance constraints. Binding of the ligand did not affect the pattern of the protein nuclear Overhauser effect signal noticeably, what would otherwise be indicative of a ligand-induced conformational change. The average backbone (residues 3-41) RMSD of the 20 refined structures was 1.14 A, whereas the heavy atom RMSD was 2.18 A. Two different orientations of the trisaccharide within the pseudohevein binding site are suggested, furnishing an explanation in structural terms for the lectin's capacity to target chitin. In both cases, hydrogen bonds and van der Waals contacts confer stability to the complexes. This conclusion is corroborated by the thermodynamic parameters of binding determined by NMR and isothermal titration calorimetry. The association process was enthalpically driven. In relation to hevein, the Trp/Tyr-substitution in the binding pocket has only a small effect on the free energy of binding in contrast to engineered galectin-1 and a mammalian C-type lectin. A comparison of the three-dimensional structure of pseudohevein in solution to those reported for wheat germ agglutinin (WGA) in the solid state and for hevein and WGA-B in solution has been performed, providing a data source about structural variability of the hevein domains. The experimentally derived structures and the values of the solvent accessibilities for several key residues have also been compared with conformations obtained by molecular dynamics simulations, pointing to the necessity to further refine the programs to enhance their predictive reliability and, thus, underscoring the importance of this kind of combined analysis in model systems." citations,reference-5,6123,239967,6,,reference citation,,,10903932,,"Asensio JL, Canada FJ, Siebert HC, Laynez J, Poveda A, Nieto PM, Soedjanaamadja UM, Gabius HJ, Jimenez-Barbero J. Chem Biol. 2000 Jul;7(7):529-43.",Structural basis for chitin recognition by defense proteins: GlcNAc residues are bound in a multivalent fashion by extended binding sites in hevein domains.,published,journal,Chem. Biol.,Chemistry & biology,7,7,,1074-5521,,,,,,,,,,,,,,,,,,,,529,543,2000,"BACKGROUND: Many plants respond to pathogenic attack by producing defense proteins that are capable of reversible binding to chitin, a polysaccharide present in the cell wall of fungi and the exoskeleton of insects. Most of these chitin-binding proteins include a common structural motif of 30 to 43 residues organized around a conserved four-disulfide core, known as the 'hevein domain' or 'chitin-binding' motif. Although a number of structural and thermodynamic studies on hevein-type domains have been reported, these studies do not clarify how chitin recognition is achieved. RESULTS: The specific interaction of hevein with several (GlcNAc)(n) oligomers has been studied using nuclear magnetic resonance (NMR), analytical ultracentrifugation and isothermal titration microcalorimetry (ITC). The data demonstrate that hevein binds (GlcNAc)(2-4) in 1:1 stoichiometry with millimolar affinity. In contrast, for (GlcNAc)(5), a significant increase in binding affinity is observed. Analytical ultracentrifugation studies on the hevein-(GlcNAc)(5,8) interaction allowed detection of protein-carbohydrate complexes with a ratio of 2:1 in solution. NMR structural studies on the hevein-(GlcNAc)(5) complex showed the existence of an extended binding site with at least five GlcNAc units directly involved in protein-sugar contacts. CONCLUSIONS: The first detailed structural model for the hevein-chitin complex is presented on the basis of the analysis of NMR data. The resulting model, in combination with ITC and analytical ultracentrifugation data, conclusively shows that recognition of chitin by hevein domains is a dynamic process, which is not exclusively restricted to the binding of the nonreducing end of the polymer as previously thought. This allows chitin to bind with high affinity to a variable number of protein molecules, depending on the polysaccharide chain length. The biological process is multivalent." citations,entry_citation,6125,239986,1,,entry citation,,,,,,"1H, 13C and 15N chemical shift assignments of an enolase-phosphatase, E1, from Klebsiella oxytoca",published,journal,J. Biomol. NMR,,30,3,,,,,,,,,,,,,,,,,,,,,,359,360,2004, citations,entry_citation,6126,240003,1,,entry citation,,,15023337,,,Cdc42 Regulates the Par-6 PDZ Domain Through an Allosteric CRIB-PDZ Transition,published,journal,Mol. Cell,,13,5,,,,,,,,,,,,,,,,,,,,,,665,676,2004, citations,entry_citation,6127,240023,1,,entry citation,,,15576035,,,"Phage like it HOT: solution structure of the bacteriophage P1-encoded HOT protein, a homolog of the theta subunit of E. coli DNA polymerase III",published,journal,Structure,,12,12,,,,,,,,,,,,,,,,,,,,,,2221,2231,2004, citations,entry_citation,6128,240040,1,,entry citation,,,15782178,,,Cell-free protein production and labeling protocol for NMR-based structural proteomics,published,journal,Nat. Methods,,1,2,,,,,,,,,,,,,,,,,,,,,,149,153,2004, citations,entry_citation,6169,240757,1,,entry citation,,,16075425,,,"Structure of the Antimicrobial, Cationic Hexapeptide Cyclo(RRWWRF) and Its Analogues in Solution and Bound to Detergent Micelles",published,journal,ChemBioChem,,6,9,,,,,,,,,,,,,,,,,,,,,,1654,1662,2005, citations,entry_citation,6170,240773,1,,entry citation,,,16075425,,,"Structure of the Antimicrobial, Cationic Hexapeptide Cyclo(RRWWRF) and Its Analogues in Solution and Bound to Detergent Micelles",published,journal,ChemBioChem,,6,9,,,,,,,,,,,,,,,,,,,,,,1654,1662,2005, citations,entry_citation,6171,240789,1,,entry citation,,,15304491,,,Structural analysis of the CCP modules of the GABAB receptor 1a: Only one of the two CCP modules is compactly folded,published,journal,J. Biol. Chem.,,279,46,,,,,,,,,,,,,,,,,,,,,,48292,48306,2004, citations,ref_1,6128,240041,2,,reference citation,,,8520220,,"Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR. 1995 Nov;6(3):277-93.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref_2,6128,240042,3,,reference citation,,,,,"Bartels, C., Xia, T.-H., Billeter, M., Guntert, P. and Wuthrich, K. (1995) J. Biomol. NMR, 6, 1-10.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_3,6128,240043,4,,reference citation,,,,,"Bartels, C., Guntert, P., Billeter, M. and Wuthrich, K. (1997) GARANT-A general algorithm for resonance assignment of multidimensional nuclear magnetic resonance spectra. J. Comp. Chem. 18, 139-149.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_4,6128,240044,5,,reference citation,,,10212987,,"Cornilescu G, Delaglio F, Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J Biomol NMR. 1999 Mar;13(3):289-302.",Protein backbone angle restraints from searching a database for chemical shift and sequence homology.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,13,3,,0925-2738,,,,,,,,,,,,,,,,,,,,289,302,1999,"Chemical shifts of backbone atoms in proteins are exquisitely sensitive to local conformation, and homologous proteins show quite similar patterns of secondary chemical shifts. The inverse of this relation is used to search a database for triplets of adjacent residues with secondary chemical shifts and sequence similarity which provide the best match to the query triplet of interest. The database contains 13C alpha, 13C beta, 13C', 1H alpha and 15N chemical shifts for 20 proteins for which a high resolution X-ray structure is available. The computer program TALOS was developed to search this database for strings of residues with chemical shift and residue type homology. The relative importance of the weighting factors attached to the secondary chemical shifts of the five types of resonances relative to that of sequence similarity was optimized empirically. TALOS yields the 10 triplets which have the closest similarity in secondary chemical shift and amino acid sequence to those of the query sequence. If the central residues in these 10 triplets exhibit similar phi and psi backbone angles, their averages can reliably be used as angular restraints for the protein whose structure is being studied. Tests carried out for proteins of known structure indicate that the root-mean-square difference (rmsd) between the output of TALOS and the X-ray derived backbone angles is about 15 degrees. Approximately 3% of the predictions made by TALOS are found to be in error." citations,ref_5,6128,240045,6,,reference citation,,,12051947,,"Herrmann T, Guntert P, Wuthrich K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J Mol Biol. 2002 May 24;319(1):209-27.",Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA.,published,journal,J. Mol. Biol.,Journal of molecular biology,319,1,,0022-2836,,,,,,,,,,,,,,,,,,,,209,227,2002,"Combined automated NOE assignment and structure determination module (CANDID) is a new software for efficient NMR structure determination of proteins by automated assignment of the NOESY spectra. CANDID uses an iterative approach with multiple cycles of NOE cross-peak assignment and protein structure calculation using the fast DYANA torsion angle dynamics algorithm, so that the result from each CANDID cycle consists of exhaustive, possibly ambiguous NOE cross-peak assignments in all available spectra and a three-dimensional protein structure represented by a bundle of conformers. The input for the first CANDID cycle consists of the amino acid sequence, the chemical shift list from the sequence-specific resonance assignment, and listings of the cross-peak positions and volumes in one or several two, three or four-dimensional NOESY spectra. The input for the second and subsequent CANDID cycles contains the three-dimensional protein structure from the previous cycle, in addition to the complete input used for the first cycle. CANDID includes two new elements that make it robust with respect to the presence of artifacts in the input data, i.e. network-anchoring and constraint-combination, which have a key role in de novo protein structure determinations for the successful generation of the correct polypeptide fold by the first CANDID cycle. Network-anchoring makes use of the fact that any network of correct NOE cross-peak assignments forms a self-consistent set; the initial, chemical shift-based assignments for each individual NOE cross-peak are therefore weighted by the extent to which they can be embedded into the network formed by all other NOE cross-peak assignments. Constraint-combination reduces the deleterious impact of artifact NOE upper distance constraints in the input for a protein structure calculation by combining the assignments for two or several peaks into a single upper limit distance constraint, which lowers the probability that the presence of an artifact peak will influence the outcome of the structure calculation. CANDID test calculations were performed with NMR data sets of four proteins for which high-quality structures had previously been solved by interactive protocols, and they yielded comparable results to these reference structure determinations with regard to both the residual constraint violations, and the precision and accuracy of the atomic coordinates. The CANDID approach has further been validated by de novo NMR structure determinations of four additional proteins. The experience gained in these calculations shows that once nearly complete sequence-specific resonance assignments are available, the automated CANDID approach results in greatly enhanced efficiency of the NOESY spectral analysis. The fact that the correct fold is obtained in cycle 1 of a de novo structure calculation is the single most important advance achieved with CANDID, when compared with previously proposed automated NOESY assignment methods that do not use network-anchoring and constraint-combination." citations,ref_6,6128,240046,7,,reference citation,,,12565051,,"Schwieters CD, Kuszewski JJ, Tjandra N, Marius Clore G. The Xplor-NIH NMR molecular structure determination package. J Magn Reson. 2003 Jan;160(1):65-73.",The Xplor-NIH NMR molecular structure determination package.,published,journal,J. Magn. Reson.,"Journal of magnetic resonance (San Diego, Calif. : 1997)",160,1,,1090-7807,,,,,,,,,,,,,,,,,,,,65,73,2003,"We announce the availability of the Xplor-NIH software package for NMR biomolecular structure determination. This package consists of the pre-existing XPLOR program, along with many NMR-specific extensions developed at the NIH. In addition to many features which have been developed over the last 20 years, the Xplor-NIH package contains an interface with a new programmatic framework written in C++. This interface currently supports the general purpose scripting languages Python and TCL, enabling rapid development of new tools, such as new potential energy terms and new optimization methods. Support for these scripting languages also facilitates interaction with existing external programs for structure analysis, structure manipulation, visualization, and spectral analysis." citations,entry_citation,6129,240067,1,,entry citation,,,15035611,,,Solution structure and backbone dynamics of the Cu(I) and apo forms of the second metal-binding domain of the Menkes protein ATP7A,published,journal,Biochemistry,,43,12,,,,,,,,,,,,,,,,,,,,,,3396,3403,2004, citations,entry_citation,613,240085,1,,entry citation,,,,,"Arseniev, Alexander S., Pashkov, Vladimir S., Pluzhkinov, Kirill A., Rochat, Herve, Bystrov, Vladimir F., ""The 1H Nuclear-Magnetic-Resonance Spectra and Spatial Structure of the Naja mossambica mossambica Neurotoxin III,"" Eur. J. Biochem. 118, 453-462 (1981).","The 1H Nuclear-Magnetic-Resonance Spectra and Spatial Structure of the Naja mossambica mossambica Neurotoxin III",published,journal,Eur. J. Biochem.,,118,,,,,,,,,,,,,,,,,,,,,,,453,462,1981, citations,entry_citation,6130,240098,1,,entry citation,,,15035611,,,Solution structure and backbone dynamics of the Cu(I) and apo forms of the second metal-binding domain of the Menkes protein ATP7A,published,journal,Biochemistry,,43,12,,,,,,,,,,,,,,,,,,,,,,3396,3403,2004, citations,entry_citation,6131,240114,1,,entry citation,,,,,,The comparative study on the solution structures of the oxidized boving microsomal cytochrome b5 and mutant V45H,published,journal,Protein Sci.,,13,8,,,,,,,,,,,,,,,,,,,,,,2161,2169,2004, citations,entry_citation,6132,240134,1,,entry citation,,,15452441,,,"Letter to the Editor: 1H, 13C and 15N NMR assignment of the homodimeric poplar phloem type II peroxiredoxin",published,journal,J. Biomol. NMR,,30,1,,,,,,,,,,,,,,,,,,,,,,105,106,2004, citations,entry_citation,6172,240807,1,,entry citation,,,15075318,,,Solution structures of a cyanobacterial copper metallochaperone: insight into an atypical copper binding motif,published,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,2004, citations,entry_citation,6260,242641,1,,entry citation,,,,,,NMR solution Structure of a Highly Stable de novo Heterodimeric Coiled-Coil,submitted,journal,Biopolymers,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_2,6132,240136,3,,reference citation,,,11706208,,"Rouhier N, Gelhaye E, Sautiere PE, Brun A, Laurent P, Tagu D, Gerard J, de Fay E, Meyer Y, Jacquot JP. Plant Physiol. 2001 Nov;127(3):1299-309.",Isolation and characterization of a new peroxiredoxin from poplar sieve tubes that uses either glutaredoxin or thioredoxin as a proton donor.,published,journal,Plant Physiol.,Plant physiology,127,3,,0032-0889,,,,,,,,,,,,,,,,,,,,1299,1309,2001,"A sequence coding for a peroxiredoxin (Prx) was isolated from a xylem/phloem cDNA library from Populus trichocarpa and subsequently inserted into an expression plasmid yielding the construction pET-Prx. The recombinant protein was produced in Escherichia coli cells and purified to homogeneity with a high yield. The poplar Prx is composed of 162 residues, a property that makes it the shortest plant Prx sequence isolated so far. It was shown that the protein is monomeric and possesses two conserved cysteines (Cys). The Prx degrades hydrogen peroxide and alkyl hydroperoxides in the presence of an exogenous proton donor that can be either thioredoxin or glutaredoxin (Grx). Based on this finding, we propose that the poplar protein represents a new type of Prx that differs from the so-called 2-Cys and 1-Cys Prx, a suggestion supported by the existence of natural fusion sequences constituted of a Prx motif coupled to a Grx motif. The protein was shown to be highly expressed in sieve tubes where thioredoxin h and Grx are also major proteins." citations,entry_citation,6133,240154,1,,entry citation,,,15452440,,,"Letter to the Editor: Assignment of 1H, 13C and 15N resonances of the Escherichia coli YojN Histidine-Phosphotransferase (HPt) domain.",published,journal,J. Biomol. NMR,,30,1,,,,,,,,,,,,,,,,,,,,,,103,104,2004, citations,entry_citation,6134,240170,1,,entry citation,,,15096629,,,THE NMR STRUCTURE OF A STABLE AND COMPACT ALL-beta-SHEET VARIANT OF INTESTINAL FATTY ACID-BINDING PROTEIN,published,journal,Protein Sci.,,13,5,,,,,,,,,,,,,,,,,,,,,,1227,1237,2004, citations,entry_citation,6135,240186,1,,entry citation,,,15044438,,,Structures of mu O-conotoxins from Conus marmoreus: Inhibitors of TTX-sensitive and TTX-resistant sodium channels in mammalian sensory neurons,published,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,2004, citations,entry_citation,6136,240202,1,,entry citation,,,14755164,,,"Backbone Resonance Assignment of the L-Arabinose Binding Protein in Complex with D-Galactose",published,journal,J. Biomol. NMR,,28,2,,,,,,,,,,,,,,,,,,,,,,191,192,2004, citations,entry_citation,6137,240219,1,,entry citation,,,15609998,,,Solution structure and stability against digestion of rproBnIb from rapeseed: relationship to its allergenic properties,published,journal,Biochemistry,,43,51,,,,,,,,,,,,,,,,,,,,,,16036,16045,2004, citations,ref_1,6137,240220,2,,reference citation,,,12027892,,"Palomares O, Monsalve RI, Rodriguez R, Villalba M. Recombinant pronapin precursor produced in Pichia pastoris displays structural and immunologic equivalent properties to its mature product isolated from rapeseed. Eur J Biochem. 2002 May;269(10):2538-45.",Recombinant pronapin precursor produced in Pichia pastoris displays structural and immunologic equivalent properties to its mature product isolated from rapeseed.,published,journal,Eur. J. Biochem.,European journal of biochemistry / FEBS,269,10,,0014-2956,,,,,,,,,,,,,,,,,,,,2538,2545,2002,"2S albumin storage proteins from rapeseed (Brassica napus), called napins, consist of two different polypeptide chains linked by disulphide bridges, which are derived by proteolytic cleavage from a single precursor. The precursor form of the napin BnIb (proBnIb) has been cloned using a PCR strategy and sequenced. The amino-acid sequence deduced from the clone includes 31 residues of the small chain and 75 of the large chain, which are connected by the peptide Ser-Glu-Asn. Expression of the cDNA encoding proBnIb has been carried out in the methylotrophic yeast Pichia pastoris. The induced protein was secreted to the extracellular medium at a yield of 80 mg.L(-1) of culture and was purified by means of size-exclusion chromatography and reverse phase-HPLC. Recombinant proBnIb appeared properly folded as its molecular and spectroscopic properties were equivalent to those of the mature heterodimeric protein. As 2S albumin storage proteins from Brassicaceae have been shown to be type I allergy inducers, the immunological activity of the recombinant proBnIb was analysed as a measure of its structural integrity. The immunological properties of the recombinant precursor and the natural napin were indistinguishable by immunoblotting and ELISA inhibition using polyclonal antisera and sera of patients allergic to mustard and rapeseed. In conclusion, the recombinant expression of napin precursors in P. pastoris has been shown to be a successful method for high yield production of homogeneous and properly folded proteins whose polymorphism and complex maturation process limited hitherto their availability." citations,entry_citation,6138,240234,1,,entry citation,,,,,,Hypothetical protein At2g24940.1 from Arabidopsis thaliana has a cytochrome b5 like fold,published,journal,J. Biomol. NMR,,30,2,,,,,,,,,,,,,,,,,,,,,,215,218,2004, citations,entry_citation,6139,240247,1,,entry citation,,,15247256,,,"NMR Solution Structure of Ole e 6, a major allergen from olive tree pollen",published,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,2004, citations,entry_citation,614,240269,1,,entry citation,,,,,"Arseniev, Alexander S., Pashkov, Vladimir S., Pluzhkinov, Kirill A., Rochat, Herve, Bystrov, Vladimir F., ""The 1H Nuclear-Magnetic-Resonance Spectra and Spatial Structure of the Naja mossambica mossambica Neurotoxin III,"" Eur. J. Biochem. 118, 453-462 (1981).","The 1H Nuclear-Magnetic-Resonance Spectra and Spatial Structure of the Naja mossambica mossambica Neurotoxin III",published,journal,Eur. J. Biochem.,,118,,,,,,,,,,,,,,,,,,,,,,,453,462,1981, citations,entry_citation,6140,240280,1,,entry citation,,,,,,"1H, 13C and 15N backbone assignment of a 32 kDa hypothetical protein from Arabidopsis thaliana, At3g16450.1",published,journal,J. Biomol. NMR,,30,3,,,,,,,,,,,,,,,,,,,,,,357,358,2004, citations,entry_citation,6141,240295,1,,entry citation,,,17530183,,,Automated backbone and side-chain assignment of mitochondrial matrix cyclophilin D.,published,journal,J. Biomol. NMR,,38,3,,,,,,,,,,,,,,,,,,,,,,267,267,2007, citations,entry_citation,6142,240310,1,,entry citation,,,17201406,,,Discovery and Refinement of a New Structural Class of Potent Peptide Deformylase Inhibitors,published,journal,J. Med. Chem.,,50,1,,,,,,,,,,,,,,,,,,,,,,10,20,2007, citations,entry_citation,6143,240323,1,,entry citation,,,15209504,,,The Structure and Interactions of Human Apolipoprotein C-II in Dodecyl Phosphocholine,published,journal,Biochemistry,,43,25,,,,,,,,,,,,,,,,,,,,,,8084,8093,2004, citations,entry_citation,6144,240336,1,,entry citation,,,15361862,,,The nisin-lipid II complex reveals a pyrophosphate cage that provides a blueprint for novel antibiotics,published,journal,Nat. Struct. Mol. Biol.,,11,10,,,,,,,,,,,,,,,,,,,,,,963,967,2004, citations,ref_1,6144,240337,2,,reference citation,,,12056898,,"Hsu ST, Breukink E, de Kruijff B, Kaptein R, Bonvin AM, van Nuland NA. Biochemistry. 2002 Jun 18;41(24):7670-6.",Mapping the targeted membrane pore formation mechanism by solution NMR: the nisin Z and lipid II interaction in SDS micelles.,published,journal,Biochemistry,Biochemistry,41,24,,0006-2960,,,,,,,,,,,,,,,,,,,,7670,7676,2002,"Nisin is an example of type-A lantibiotics that contain cyclic lanthionine rings and unusual dehydrated amino acids. Among the numerous pore-forming antimicrobial peptides, type-A lantibiotics form an unique family of post-translationally modified peptides. Via the recognition of cell wall precursor lipid II, nisin has the capacity to form pores against Gram-positive bacteria with an extremely high activity in the nanomolar (nM) range. Here we report a high-resolution NMR spectroscopy study of nisin/lipid II interactions in SDS micelles as a model membrane system in order to elucidate the mechanism of molecular recognition at residue level. The binding to lipid II was studied through (15)N-(1)H HSQC titration, backbone amide proton temperature coefficient analysis, and heteronuclear (15)N[(1)H]-NOE relaxation dynamics experiments. Upon the addition of lipid II, significant changes were monitored in the N-terminal part of nisin. An extremely low amide proton temperature coefficient (Delta delta/Delta T) was found for the amide proton of Ala3 (> -0.1 ppb/K) in the complex form. This suggests tight hydrogen bonding and/or isolation from the bulk solvent for this residue. Large chemical shift perturbations were also observed in the first two rings. In contrast, the C-terminal part of nisin was almost unaffected. This part of the molecule remains flexible and solvent-exposed. On the basis of our results, a multistep pore-forming mechanism is proposed. The N-terminal part of nisin first binds to lipid II, and a subsequent structural rearrangement takes place. The C-terminal part of nisin is possibly responsible for the activation of the pore formation. In light of the emerging antibiotic resistance problems, an understanding of the specific recognition mechanism of nisin with lipid II at the residue specific level may therefore aid in the development of novel antibiotics." citations,entry_citation,6145,240359,1,,entry citation,,,15361862,,,"The nisin-lipid II complex reveals a pyrophosphate cage that provides a blueprint for novel antibiotics.",published,journal,Nat. Struct. Mol. Biol.,,11,10,,,,,,,,,,,,,,,,,,,,,,963,967,2004, citations,references,6145,240360,2,,reference citation,,,12056898,,"Hsu ST, Breukink E, de Kruijff B, Kaptein R, Bonvin AM, van Nuland NA. Biochemistry. 2002 Jun 18;41(24):7670-6.",,,journal,Biochemistry,Biochemistry,41,24,,,,,,,,,,,,,,,,,,,,,,7670,7676,2002, citations,references_1,6145,240361,3,,reference citation,,,12663672,,"Breukink E, van Heusden HE, Vollmerhaus PJ, Swiezewska E, Brunner L, Walker S, Heck AJ, de Kruijff B. J Biol Chem. 2003 May 30;278(22):19898-903.",,,journal,J. Biol. Chem.,,278,22,,,,,,,,,,,,,,,,,,,,,,19898,19903,2003, citations,entry_citation,6146,240385,1,,entry citation,,,15361862,,,The nisin-lipid II complex reveals a pyrophosphate cage that provides a blueprint for novel antibiotics,published,journal,Nat Struct Mol Biol,,11,10,,,,,,,,,,,,,,,,,,,,,,963,967,2004, citations,references,6146,240386,2,,reference citation,,,12056898,,"Hsu ST, Breukink E, de Kruijff B, Kaptein R, Bonvin AM, van Nuland NA. Biochemistry. 2002 Jun 18;41(24):7670-6.",Mapping the targeted membrane pore formation mechanism by solution NMR: the nisin Z and lipid II interaction in SDS micelles.,published,journal,Biochemistry,Biochemistry,41,24,,0006-2960,,,,,,,,,,,,,,,,,,,,7670,7676,2002,"Nisin is an example of type-A lantibiotics that contain cyclic lanthionine rings and unusual dehydrated amino acids. Among the numerous pore-forming antimicrobial peptides, type-A lantibiotics form an unique family of post-translationally modified peptides. Via the recognition of cell wall precursor lipid II, nisin has the capacity to form pores against Gram-positive bacteria with an extremely high activity in the nanomolar (nM) range. Here we report a high-resolution NMR spectroscopy study of nisin/lipid II interactions in SDS micelles as a model membrane system in order to elucidate the mechanism of molecular recognition at residue level. The binding to lipid II was studied through (15)N-(1)H HSQC titration, backbone amide proton temperature coefficient analysis, and heteronuclear (15)N[(1)H]-NOE relaxation dynamics experiments. Upon the addition of lipid II, significant changes were monitored in the N-terminal part of nisin. An extremely low amide proton temperature coefficient (Delta delta/Delta T) was found for the amide proton of Ala3 (> -0.1 ppb/K) in the complex form. This suggests tight hydrogen bonding and/or isolation from the bulk solvent for this residue. Large chemical shift perturbations were also observed in the first two rings. In contrast, the C-terminal part of nisin was almost unaffected. This part of the molecule remains flexible and solvent-exposed. On the basis of our results, a multistep pore-forming mechanism is proposed. The N-terminal part of nisin first binds to lipid II, and a subsequent structural rearrangement takes place. The C-terminal part of nisin is possibly responsible for the activation of the pore formation. In light of the emerging antibiotic resistance problems, an understanding of the specific recognition mechanism of nisin with lipid II at the residue specific level may therefore aid in the development of novel antibiotics." citations,entry_citation,6173,240828,1,,entry citation,,,,,,Solution Structure of the 50S Ribosomal Protein L35Ae from Pyrococcus furiosus: Northeast Strucutral Genomics Consortium target: Pfr48,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,references_1,6146,240387,3,,reference citation,,,12663672,,"Breukink E, van Heusden HE, Vollmerhaus PJ, Swiezewska E, Brunner L, Walker S, Heck AJ, de Kruijff B. J Biol Chem. 2003 May 30;278(22):19898-903.",Lipid II is an intrinsic component of the pore induced by nisin in bacterial membranes.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,278,22,,0021-9258,,,,,,,,,,,,,,,,,,,,19898,19903,2003,"The peptidoglycan layers surrounding bacterial membranes are essential for bacterial cell survival and provide an important target for antibiotics. Many antibiotics have mechanisms of action that involve binding to Lipid II, the prenyl chain-linked donor of the peptidoglycan building blocks. One of these antibiotics, the pore-forming peptide nisin uses Lipid II as a receptor molecule to increase its antimicrobial efficacy dramatically. Nisin is the first example of a targeted membrane-permeabilizing peptide antibiotic. However, it was not known whether Lipid II functions only as a receptor to recruit nisin to bacterial membranes, thus increasing its specificity for bacterial cells, or whether it also plays a role in pore formation. We have developed a new method to produce large amounts of Lipid II and variants thereof so that we can address the role of the lipid-linked disaccharide in the activity of nisin. We show here that Lipid II is not only the receptor for nisin but an intrinsic component of the pore formed by nisin, and we present a new model for the pore complex that includes Lipid II." citations,entry_citation,6147,240417,1,,entry citation,,,15243194,,,"1H, 15N, and 13C chemical shift assignments of the Vibrio Harveyi histidine phosphotransferase protein LuxU",published,journal,J. Biomol. NMR,,29,4,,,,,,,,,,,,,,,,,,,,,,551,552,2004, citations,entry_citation,6148,240434,1,,entry citation,,,,,,"Letter to the Editor: Resonance Assignments and Secondary Structure of hPrxVI, a 25 kDa 1-Cys Human Peroxiredoxin Enzyme",published,journal,J. Biomol. NMR,,31,3,,,,,,,,,,,,,,,,,,,,,,267,268,2005, citations,entry_citation,6149,240448,1,,entry citation,,,15557809,,,"Letter to the Editor: 1H, 15N and 13C resonance assignments of complement control protein module pair 2-3 from the C4b-binding site of complement receptor type 1",published,journal,J. Biomol. NMR,,30,2,,,,,,,,,,,,,,,,,,,,,,227,228,2004, citations,entry_citation,6150,240463,1,,entry citation,,,,,,"Letter to the Editor: 1H, 15N and 13C resonance assignments of the Apo Sm14-M20(C62V) protein from Schistosoma mansoni",published,journal,J. Biomol. NMR,,29,4,,,,,,,,,,,,,,,,,,,,,,553,554,2004, citations,entry_citation,6151,240480,1,,entry citation,,,15178334,,,NMR solution Structure and position of transportan in neutral phospholipid bicelles,published,journal,FEBS Lett.,,567,2-3,,,,,,,,,,,,,,,,,,,,,,265,269,2004, citations,entry_citation,6152,240499,1,,entry citation,,,,,,"Solution structure of recombinant TIP-B1, a novel TNF inhibitory protein",published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6154,240515,1,,entry citation,,,,,,1H Assigned Chemical Shifts for FMBP-1 tandem repeat 3,published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6155,240531,1,,entry citation,,,,,,1H Assigned Chemical Shifts for FMBP-1 tandem repeat 4,published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6156,240547,1,,entry citation,,,,,,1H Assigned Chemical Shifts for FMBP-1 tandem repeat 1 in 30% (v/v) TFE and water solution,published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6157,240566,1,,entry citation,,,,,,1H Assigned Chemical Shifts for FMBP-1 tandem repeat 2,published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6158,240582,1,,entry citation,,,15713488,,,Solution structure of human saposin C in a detergent environment,published,journal,J. Mol. Biol.,,346,5,,,,,,,,,,,,,,,,,,,,,,1381,1392,2005, citations,reference_1,6158,240583,2,,reference citation,,,14674747,,"de Alba E, Weiler S, Tjandra N. Solution structure of human saposin C: pH-dependent interaction with phospholipid vesicles. Biochemistry. 2003 Dec 23;42(50):14729-40.",Solution structure of human saposin C: pH-dependent interaction with phospholipid vesicles.,published,journal,Biochemistry,Biochemistry,42,50,,0006-2960,,,,,,,,,,,,,,,,,,,,14729,14740,2003,"Saposin C binds to membranes to activate lipid degradation in lysosomes. To get insights into saposin C's function, we have determined its three-dimensional structure by NMR and investigated its interaction with phospholipid vesicles. Saposin C adopts the saposin-fold common to other members of the family. In contrast, the electrostatic surface revealed by the NMR structure is remarkably different. We suggest that charge distribution in the protein surface can modulate membrane interaction leading to the functional diversity of this family. We find that the binding of saposin C to phospholipid vesicles is a pH-controlled reversible process. The pH dependence of this interaction is sigmoidal, with an apparent pK(a) for binding close to 5.3. The pK(a) values of many solvent-exposed Glu residues are anomalously high and close to the binding pK(a). Our NMR data are consistent with the absence of a conformational change prior to membrane binding. All this information suggests that the negatively charged electrostatic surface of saposin C needs to be partially neutralized to trigger membrane binding. We have studied the membrane-binding behavior of a mutant of saposin C designed to decrease the negative charge of the electrostatic surface. The results support our conclusion on the importance of protein surface neutralization in binding. Since saposin C is a lysosomal protein and pH gradients occur in lysosomes, we propose that lipid degradation in the lysosome could be switched on and off by saposin C's reversible binding to membranes." citations,entry_citation,6159,240600,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N resonance assignments of Ca2+-free DdCAD-1: a Ca2+-dependent cell-cell adhesion molecule",published,journal,J. Biomol. NMR,,30,3,,,,,,,,,,,,,,,,,,,,,,375,376,2004, citations,ref_1,6159,240601,2,,reference citation,,,8663243,,"Wong EF, Brar SK, Sesaki H, Yang C, Siu CH. Molecular cloning and characterization of DdCAD-1, a Ca2+-dependent cell-cell adhesion molecule, in Dictyostelium discoideum. J Biol Chem. 1996 Jul 5;271(27):16399-408.","Molecular cloning and characterization of DdCAD-1, a Ca2+-dependent cell-cell adhesion molecule, in Dictyostelium discoideum.",published,journal,J. Biol. Chem.,The Journal of biological chemistry,271,27,,0021-9258,,,,,,,,,,,,,,,,,,,,16399,16408,1996,"Dictyostelium discoideum expresses EDTA-sensitive cell-cell adhesion sites soon after the initiation of development, and a Ca2+-binding protein of Mr 24,000 (designated DdCAD-1) has been implicated in this type of adhesiveness. We have previously purified DdCAD-1 to homogeneity and characterized its cell binding activity (Brar, S. K., and Siu, C.-H. (1993) J. Biol. Chem. 268, 24902-24909). In this report, we describe the cloning of DdCAD-1 cDNAs. DNA sequencing revealed a single open reading frame coding for a polypeptide containing 213 amino acids. The identity of the cDNA was confirmed by amino acid sequences of two cyanogen bromide peptides. The deduced amino acid sequence of DdCAD-1 exhibits a relatively high degree of sequence similarity with members of the cadherin family and protein S of Myxococcus xanthus. Unlike the other cadherins, the carboxyl-terminal region of DdCAD-1 contains a Ca2+-binding motif. Although analyses of the sequence suggest that the polypeptide lacks a signal peptide sequence and a transmembrane domain, immunofluorescence microscopy demonstrates the association of DdCAD-1 with the ecto-surface of the plasma membrane. To investigate the structure/function relationships of DdCAD-1, glutathione S-transferase fusion proteins containing different DdCAD-1 fragments were expressed and assayed for their 45Ca2+ and cell binding activities. These studies revealed that the cell binding activity is dependent on the amino-terminal segment and not the carboxyl-terminal Ca2+-binding domain and showed additional Ca2+-binding site(s) within the amino-terminal segment." citations,ref_2,6159,240602,3,,reference citation,,,12135922,,"Wong E, Yang C, Wang J, Fuller D, Loomis WF, Siu CH. Disruption of the gene encoding the cell adhesion molecule DdCAD-1 leads to aberrant cell sorting and cell-type proportioning during Dictyostelium development. Development. 2002 Aug;129(16):3839-50.",Disruption of the gene encoding the cell adhesion molecule DdCAD-1 leads to aberrant cell sorting and cell-type proportioning during Dictyostelium development.,published,journal,Development,"Development (Cambridge, England)",129,16,,0950-1991,,,,,,,,,,,,,,,,,,,,3839,3850,2002,"The cadA gene in Dictyostelium encodes the Ca2+-dependent cell adhesion molecule DdCAD-1, which is expressed soon after the initiation of development. To investigate the biological role of DdCAD-1, the cadA gene was disrupted by homologous recombination. The cadA-null cells showed a 50% reduction in EDTA-sensitive cell adhesion. The remaining EDTA-sensitive adhesion sites were resistant to dissociation by anti-DdCAD-1 antibody, suggesting that they were distinct adhesion sites. Cells that lacked DdCAD-1 were able to complete development and form fruiting bodies. However, they displayed abnormal slug morphology and culmination was delayed by approximately 6 hours. The yield of spores was reduced by approximately 50%. The proportion of prestalk cells in cadA(-) slugs showed a 2.5-fold increase over the parental strain. When cadA(-) cells were transfected with pcotB::GFP to label prespore cells, aberrant cell-sorting patterns in slugs became apparent. When mutant prestalk cells were mixed with wild-type prespore cells, mutant prestalk cells were unable to return to the anterior position of chimeric slugs, suggesting defects in the sorting mechanism. The wild-type phenotype was restored when cadA(-) cells were transfected with a cadA-expression vector. These results indicate that, in addition to cell-cell adhesion, DdCAD-1 plays a role in cell type proportioning and pattern formation." citations,entry_citation,6160,240616,1,,entry citation,,,15157085,,,Disulfide Bonding Arrangements in Active Forms of the Somatomedin B Domain of Human Vitronectin,published,journal,Biochemistry,,43,21,,,,,,,,,,,,,,,,,,,,,,6519,6534,2004, citations,entry_citation,6161,240631,1,,entry citation,,,15050829,,,"Two homologous domains of similar structure but different stability in the yeast linker histone, Hho1p",published,journal,J. Mol. Biol.,,338,1,,,,,,,,,,,,,,,,,,,,,,139,148,2004, citations,ref_1,6161,240632,2,,reference citation,,,15050829,,"Ali T, Coles P, Stevens TJ, Stott K, Thomas JO. J Mol Biol. 2004 Apr 16;338(1):139-48.","Two homologous domains of similar structure but different stability in the yeast linker histone, Hho1p.",published,journal,J. Mol. Biol.,Journal of molecular biology,338,1,,0022-2836,,,,,,,,,,,,,,,,,,,,139,148,2004,"The Saccharomyces cerevisiae homologue of the linker histone H1, Hho1p, has two domains that are similar in sequence to the globular domain of H1 (and variants such as H5). It is an open question whether both domains are functional and whether they play similar structural roles. Preliminary structural studies showed that the two isolated domains, GI and GII, differ significantly in stability. In 10 mM sodium phosphate (pH 7), the GI domain, like the globular domains of H1 and H5, GH1 and GH5, was stably folded, whereas GII was largely unstructured. However, at high concentrations of large tetrahedral anions (phosphate, sulphate, perchlorate), which might mimic the charge-screening effects of DNA phosphate groups, GII was folded. In view of the potential significance of these observations in relation to the role of Hho1p, we have now determined the structures of its GI and GII domains by NMR spectroscopy under conditions in which GII (like GI) is folded. The backbone r.m.s.d. over the ordered residues is 0.43 A for GI and 0.97 A for GII. Both structures show the ""winged-helix"" fold typical of GH1 and GH5 and are very similar to each other, with an r.m.s.d. over the structured regions of 1.3 A, although there are distinct differences. The potential for GII to adopt a structure similar to that of GI when Hho1p is bound to chromatin in vivo suggests that both globular domains might be functional. Whether Hho1p performs a structural role by bridging two nucleosomes remains to be determined." citations,entry_citation,6162,240647,1,,entry citation,,,15050829,,,"Two homologous domains of similar structure but different stability in the yeast linker histone, Hho1p",published,journal,J. Mol. Biol.,,338,1,,,,,,,,,,,,,,,,,,,,,,139,148,2004, citations,ref_1,6162,240648,2,,reference citation,,,15050829,,"Ali T, Coles P, Stevens TJ, Stott K, Thomas JO. J Mol Biol. 2004 Apr 16;338(1):139-48.","Two homologous domains of similar structure but different stability in the yeast linker histone, Hho1p.",published,journal,J. Mol. Biol.,Journal of molecular biology,338,1,,0022-2836,,,,,,,,,,,,,,,,,,,,139,148,2004,"The Saccharomyces cerevisiae homologue of the linker histone H1, Hho1p, has two domains that are similar in sequence to the globular domain of H1 (and variants such as H5). It is an open question whether both domains are functional and whether they play similar structural roles. Preliminary structural studies showed that the two isolated domains, GI and GII, differ significantly in stability. In 10 mM sodium phosphate (pH 7), the GI domain, like the globular domains of H1 and H5, GH1 and GH5, was stably folded, whereas GII was largely unstructured. However, at high concentrations of large tetrahedral anions (phosphate, sulphate, perchlorate), which might mimic the charge-screening effects of DNA phosphate groups, GII was folded. In view of the potential significance of these observations in relation to the role of Hho1p, we have now determined the structures of its GI and GII domains by NMR spectroscopy under conditions in which GII (like GI) is folded. The backbone r.m.s.d. over the ordered residues is 0.43 A for GI and 0.97 A for GII. Both structures show the ""winged-helix"" fold typical of GH1 and GH5 and are very similar to each other, with an r.m.s.d. over the structured regions of 1.3 A, although there are distinct differences. The potential for GII to adopt a structure similar to that of GI when Hho1p is bound to chromatin in vivo suggests that both globular domains might be functional. Whether Hho1p performs a structural role by bridging two nucleosomes remains to be determined." citations,entry_citation,6163,240663,1,,entry citation,,,,,,Letter to the editor: Backbone assignment of the dimerization and DNA-binding domain of the oncogenic transcription factor v-Myc in complex with its authentic binding partner Max,published,journal,J. Biomol. NMR,,30,3,,,,,,,,,,,,,,,,,,,,,,361,362,2004, citations,entry_citation,6165,240678,1,,entry citation,,,15358240,,,Insights into function of PSI domains from structure of the Met receptor PSI domain,published,journal,Biochem. Biophys. Res. Commun.,,321,1,,,,,,,,,,,,,,,,,,,,,,234,240,2004, citations,entry_citation,6166,240697,1,,entry citation,,,15304491,,,Structural analysis of the CCP modules of the GABAB receptor 1a: Only one of the two CCP modules is compactly folded.,published,journal,J. Biol. Chem.,,279,46,,,,,,,,,,,,,,,,,,,,,,48292,48306,2004, citations,entry_citation,6167,240715,1,,entry citation,,,,,,Structural studies on the Ca-binding domain of human nucleobindin (CALNUC),submitted,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6168,240739,1,,entry citation,,,16075425,,,"Structure of the Antimicrobial, Cationic Hexapeptide Cyclo(RRWWRF) and Its Analogues in Solution and Bound to Detergent Micelles",published,journal,ChemBioChem,,6,9,,,,,,,,,,,,,,,,,,,,,,1654,1662,2005, citations,entry_citation,6468,247107,1,,entry citation,,,,,,NMR backbone assignment of the mitogen-activated protein (MAP) kinase p38,published,journal,J. Biomol. NMR,,32,2,,,,,,,,,,,,,,,,,,,,,,175,175,2005, citations,entry_citation,6176,240894,1,,entry citation,,,15364906,,,Solution structure of a ubiquitin-like domain of tubulin-folding cofactor B,published,journal,J. Biol. Chem.,,279,45,,,,,,,,,,,,,,,,,,,,,,46787,46793,2004, citations,ref-1,6176,240895,2,,reference citation,,,8520220,,"Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR. 1995 Nov;6(3):277-93.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref-2,6176,240896,3,,reference citation,,,,,"Bartels, C., Xia, T.-H., Billeter, M., Guntert, P. and Wuthrich, K. (1995) J. Biomol. NMR, 6, 1-10.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref-3,6176,240897,4,,reference citation,,,,,"Bartels, C., Guntert, P., Billeter, M. and Wuthrich, K. (1997) J. Comp. Chem. 18, 139-149.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref-4,6176,240898,5,,reference citation,,,10212987,,"Cornilescu G, Delaglio F, Bax A. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J Biomol NMR. 1999 Mar;13(3):289-302.",Protein backbone angle restraints from searching a database for chemical shift and sequence homology.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,13,3,,0925-2738,,,,,,,,,,,,,,,,,,,,289,302,1999,"Chemical shifts of backbone atoms in proteins are exquisitely sensitive to local conformation, and homologous proteins show quite similar patterns of secondary chemical shifts. The inverse of this relation is used to search a database for triplets of adjacent residues with secondary chemical shifts and sequence similarity which provide the best match to the query triplet of interest. The database contains 13C alpha, 13C beta, 13C', 1H alpha and 15N chemical shifts for 20 proteins for which a high resolution X-ray structure is available. The computer program TALOS was developed to search this database for strings of residues with chemical shift and residue type homology. The relative importance of the weighting factors attached to the secondary chemical shifts of the five types of resonances relative to that of sequence similarity was optimized empirically. TALOS yields the 10 triplets which have the closest similarity in secondary chemical shift and amino acid sequence to those of the query sequence. If the central residues in these 10 triplets exhibit similar phi and psi backbone angles, their averages can reliably be used as angular restraints for the protein whose structure is being studied. Tests carried out for proteins of known structure indicate that the root-mean-square difference (rmsd) between the output of TALOS and the X-ray derived backbone angles is about 15 degrees. Approximately 3% of the predictions made by TALOS are found to be in error." citations,ref-5,6176,240899,6,,reference citation,,,12051947,,"Herrmann T, Guntert P, Wuthrich K. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J Mol Biol. 2002 May 24;319(1):209-27.",Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA.,published,journal,J. Mol. Biol.,Journal of molecular biology,319,1,,0022-2836,,,,,,,,,,,,,,,,,,,,209,227,2002,"Combined automated NOE assignment and structure determination module (CANDID) is a new software for efficient NMR structure determination of proteins by automated assignment of the NOESY spectra. CANDID uses an iterative approach with multiple cycles of NOE cross-peak assignment and protein structure calculation using the fast DYANA torsion angle dynamics algorithm, so that the result from each CANDID cycle consists of exhaustive, possibly ambiguous NOE cross-peak assignments in all available spectra and a three-dimensional protein structure represented by a bundle of conformers. The input for the first CANDID cycle consists of the amino acid sequence, the chemical shift list from the sequence-specific resonance assignment, and listings of the cross-peak positions and volumes in one or several two, three or four-dimensional NOESY spectra. The input for the second and subsequent CANDID cycles contains the three-dimensional protein structure from the previous cycle, in addition to the complete input used for the first cycle. CANDID includes two new elements that make it robust with respect to the presence of artifacts in the input data, i.e. network-anchoring and constraint-combination, which have a key role in de novo protein structure determinations for the successful generation of the correct polypeptide fold by the first CANDID cycle. Network-anchoring makes use of the fact that any network of correct NOE cross-peak assignments forms a self-consistent set; the initial, chemical shift-based assignments for each individual NOE cross-peak are therefore weighted by the extent to which they can be embedded into the network formed by all other NOE cross-peak assignments. Constraint-combination reduces the deleterious impact of artifact NOE upper distance constraints in the input for a protein structure calculation by combining the assignments for two or several peaks into a single upper limit distance constraint, which lowers the probability that the presence of an artifact peak will influence the outcome of the structure calculation. CANDID test calculations were performed with NMR data sets of four proteins for which high-quality structures had previously been solved by interactive protocols, and they yielded comparable results to these reference structure determinations with regard to both the residual constraint violations, and the precision and accuracy of the atomic coordinates. The CANDID approach has further been validated by de novo NMR structure determinations of four additional proteins. The experience gained in these calculations shows that once nearly complete sequence-specific resonance assignments are available, the automated CANDID approach results in greatly enhanced efficiency of the NOESY spectral analysis. The fact that the correct fold is obtained in cycle 1 of a de novo structure calculation is the single most important advance achieved with CANDID, when compared with previously proposed automated NOESY assignment methods that do not use network-anchoring and constraint-combination." citations,ref-6,6176,240900,7,,reference citation,,,12565051,,"Schwieters CD, Kuszewski JJ, Tjandra N, Marius Clore G. The Xplor-NIH NMR molecular structure determination package. J Magn Reson. 2003 Jan;160(1):65-73.",The Xplor-NIH NMR molecular structure determination package.,published,journal,J. Magn. Reson.,"Journal of magnetic resonance (San Diego, Calif. : 1997)",160,1,,1090-7807,,,,,,,,,,,,,,,,,,,,65,73,2003,"We announce the availability of the Xplor-NIH software package for NMR biomolecular structure determination. This package consists of the pre-existing XPLOR program, along with many NMR-specific extensions developed at the NIH. In addition to many features which have been developed over the last 20 years, the Xplor-NIH package contains an interface with a new programmatic framework written in C++. This interface currently supports the general purpose scripting languages Python and TCL, enabling rapid development of new tools, such as new potential energy terms and new optimization methods. Support for these scripting languages also facilitates interaction with existing external programs for structure analysis, structure manipulation, visualization, and spectral analysis." citations,entry_citation,6177,240932,1,,entry citation,,,15341728,,,Structure and RNA interactions of the N-terminal RRM domains of PTB,published,journal,Structure (Camb),,12,9,,,,,,,,,,,,,,,,,,,,,,1631,1643,2004, citations,entry_citation,6178,240960,1,,entry citation,,,15341728,,,Structure and RNA interactions of the N-terminal RRM domains of PTB,published,journal,Structure (Camb),,12,9,,,,,,,,,,,,,,,,,,,,,,1631,1643,2004, citations,entry_citation,6179,240979,1,,entry citation,,,15366933,,,The Solution structure of a chimeric LEKTI domain reveals a chameleon sequence,published,journal,Biochemistry,,43,35,,,,,,,,,,,,,,,,,,,,,,11238,11247,2004, citations,entry_citation,6180,240995,1,,entry citation,,,15366933,,,The Solution structure of a chimeric LEKTI domain reveals a chameleon sequence,published,journal,Biochemistry,,43,35,,,,,,,,,,,,,,,,,,,,,,11238,11247,2004, citations,citation_1,6181,241011,1,,entry citation,,,,,,Letter to the Editor: Resonance Assignments for the Endosomal Adaptor Protein P14,published,journal,J. Biomol. NMR,,30,3,,,,,,,,,,,,,,,,,,,,,,367,368,2004, citations,entry_citation,6182,241024,1,,entry citation,,,,,,"1H, 13C, and 15N backbone chemical shifts and 15N spin-relaxation rates for Holo-FluA(R95K)",in preparation,journal,J. Mol. Biol.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6183,241044,1,,entry citation,,,15481030,,,"NMR backbone assignment of a protein kinase catalytic domain by a combination of several approaches: Application to the catalytic subunit of cAMP-dependent protein kinase",published,journal,Chembiochem,,5,11,,,,,,,,,,,,,,,,,,,,,,1508,1516,2004, citations,ref-1,6183,241045,2,,reference citation,,,,,"Ch. Bartels, T.-H. Xia, M. Billeter, P. Guntert, K. Wuthrich (1995). J. Biomol. NMR 5, 1-10",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6184,241059,1,,entry citation,,,11772007,,,"Model for the Catalytic Domain of the Proofreading Epsilon Subunit of Escherichia coli DNA Polymerase III Based on NMR Structural Data",published,journal,Biochemistry,,41,,,,,,,,,,,,,,,,,,,,,,,94,110,2002, citations,ref-1,6184,241060,2,,reference citation,,,12667053,,"DeRose, E.F., Darden, T., Harvey, S., Gabel, S., Perrino, F. W., Schaaper, R. M., and London, R. E. Elucidation of the Epsilon-Theta Subunit Interface of Escherichia coli DNA Polymerase III by NMR Spectroscopy, Biochemistry 42, 3635-3644 (2003). Biochemistry. 2003 Apr 8;42(13):3635-44.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6185,241074,1,,entry citation,,,15062080,,,Secondary structure switching in Cro protein evolution,published,journal,Structure,,12,4,,,,,,,,,,,,,,,,,,,,,,569,581,2004, citations,entry_citation,6186,241095,1,,entry citation,,,15363786,,,Structure of DNA sequence d-TGATCA by two-dimensional nuclear magnetic resonance spectroscopy and restrained molecular dynamics,published,journal,J. Struct. Biol.,,148,1,,,,,,,,,,,,,,,,,,,,,,34,50,2004, citations,entry_citation,6187,241110,1,,entry citation,,,15704012,,,Backbone Solution Structures of Proteins Using Residual Dipolar Couplings: Application to a Novel Structural Genomics Target,published,journal,J. Struct. Funct. Genomics,Journal of Structural and Functional Genomics,5,4,,,,,,,,,,,,,,,,,,,,,,241,254,2004, citations,entry_citation,6188,241140,1,,entry citation,,,15690348,,,Different secondary structure elements as scaffolds for protein folding transition states of two homologous four-helix bundles,published,journal,Proteins,,59,1,,,,,,,,,,,,,,,,,,,,,,80,90,2005, citations,entry_citation,6189,241154,1,,entry citation,,,15498563,,,The SEP domain of p47 acts as a reversible competitive inhibitor of cathepsin L,published,journal,FEBS Lett.,,576,3,,,,,,,,,,,,,,,,,,,,,,358,362,2004, citations,entry_citation,6190,241174,1,,entry citation,,,15181013,,,Solution structure of Cox11: A novel type of beta-immunoglobulin-like fold involved in CuB site formation of cytochrome c oxidase,published,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,2004, citations,entry_citation,6191,241194,1,,entry citation,,,15260479,,,Solution NMR structure and X-ray absorption analysis of the C-terminal zinc-binding domain of the SecA ATPase,published,journal,Biochemistry,,43,29,,,,,,,,,,,,,,,,,,,,,,9361,9371,2004, citations,entry_citation,6192,241218,1,,entry citation,,,,,,"1H, 13C, and 15N Chemical Shift Assignments for Omega-atracotoxin-Hv1a at pH 3.6",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,Ref_1,6192,241219,2,,reference citation,,,9228949,,"Fletcher JI, Smith R, O'Donoghue SI, Nilges M, Connor M, Howden ME, Christie MJ, King GF. The structure of a novel insecticidal neurotoxin, omega-atracotoxin-HV1, from the venom of an Australian funnel web spider. Nat Struct Biol. 1997 Jul;4(7):559-66.","The structure of a novel insecticidal neurotoxin, omega-atracotoxin-HV1, from the venom of an Australian funnel web spider.",published,journal,Nat. Struct. Biol.,Nature structural biology,4,7,,1072-8368,,,,,,,,,,,,,,,,,,,,559,566,1997,"A family of potent insecticidal toxins has recently been isolated from the venom of Australian funnel web spiders. Among these is the 37-residue peptide omega-atracotoxin-HV1 (omega-ACTX-HV1) from Hadronyche versuta. We have chemically synthesized and folded omega-ACTX-HV1, shown that it is neurotoxic, ascertained its disulphide bonding pattern, and determined its three-dimensional solution structure using NMR spectroscopy. The structure consists of a solvent-accessible beta-hairpin protruding from a disulphide-bonded globular core comprising four beta-turns. The three intramolecular disulphide bonds from a cystine knot motif similar to that seen in several other neurotoxic peptides. Despite limited sequence identity, omega-ACTX-HV1 displays significant structural homology with the omega-agatoxins and omega-conotoxins, both of which are vertebrate calcium channel antagonists; however, in contrast with these toxins, we show that omega-ACTX-HV1 inhibits insect, but not mammalian, voltage-gated calcium channel currents." citations,Ref_2,6192,241220,3,,reference citation,,,11313356,,"Tedford HW, Fletcher JI, King GF. Functional significance of the beta hairpin in the insecticidal neurotoxin omega-atracotoxin-Hv1a. J Biol Chem. 2001 Jul 13;276(28):26568-76.",Functional significance of the beta hairpin in the insecticidal neurotoxin omega-atracotoxin-Hv1a.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,276,28,,0021-9258,,,,,,,,,,,,,,,,,,,,26568,26576,2001,"omega-Atracotoxin-Hv1a is an insect-specific neurotoxin whose phylogenetic specificity derives from its ability to antagonize insect, but not vertebrate, voltage-gated calcium channels. In order to help understand its mechanism of action and to enhance its utility as a lead compound for insecticide development, we used a combination of protein engineering and site-directed mutagenesis to probe the toxin for key functional regions. First, we constructed a Hairpinless mutant in which the C-terminal beta-hairpin, which is highly conserved in this family of neurotoxins, was excised without affecting the fold of the residual disulfide-rich core of the toxin. The Hairpinless mutant was devoid of insecticidal activity, indicating the functional importance of the hairpin. We subsequently developed a highly efficient system for production of recombinant toxin and then probed the hairpin for key functional residues using alanine-scanning mutagenesis followed by a second round of mutagenesis based on initial ""hits"" from the alanine scan. This revealed that two spatially proximal residues, Asn(27) and Arg(35), form a contiguous molecular surface that is essential for toxin activity. We propose that this surface of the beta-hairpin is a key site for interaction of the toxin with insect calcium channels." citations,entry_citation,6193,241238,1,,entry citation,,,15452444,,,"Letter to the Editor: 1H, 15N and 13C Backbone and Side Chain Assignments of PSD-95 PDZ3 protein",published,journal,J. Biomol. NMR,,30,1,,,,,,,,,,,,,,,,,,,,,,111,112,2004, citations,entry_citation,6194,241253,1,,entry citation,,,,,,"1H, 13C, and 15N Chemical Shift Assignments for Omega-atracotoxin-Hv1a at pH 6.0",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6242,242217,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N sequence-specific resonance assignments of the two-domain thrombin inhibitor dipetalin",published,journal,J. Biomol. NMR,,30,3,,,,,,,,,,,,,,,,,,,,,,383,384,2004, citations,entry_citation,6243,242232,1,,entry citation,,,15364584,,,"Gated electron transfers and electron pathways in azurin: a NMR dynamic study at multiple fields and temperatures",published,journal,J. Mol. Biol.,,342,5,,,,,,,,,,,,,,,,,,,,,,1599,1611,2004, citations,entry_citation,6261,242662,1,,entry citation,,,16155203,,,"Structural characterization of Lyn-SH3 domain in complex with a herpesviral protein reveals an extended recognition motif that enhances binding affinity",published,journal,Protein Sci.,,14,10,,,,,,,,,,,,,,,,,,,,,,2487,2498,2005, citations,ref_1,6261,242663,2,,reference citation,,,,,"Johnson, B. A. and Blevins R. A. (1994) NMRView: A computer program for the visualization and analysis of NMR data, J. Biomol. NMR 4, 603-614.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6262,242688,1,,entry citation,,,15173166,,,"The structure and dynamics of tandem WW domains in a negative regulator of notch signaling, suppressor of deltex",published,journal,J. Biol. Chem.,,279,33,,,,,,,,,,,,,,,,,,,,,,34991,35000,2004, citations,Ref_1,6194,241254,2,,reference citation,,,9228949,,"Fletcher JI, Smith R, O'Donoghue SI, Nilges M, Connor M, Howden ME, Christie MJ, King GF. The structure of a novel insecticidal neurotoxin, omega-atracotoxin-HV1, from the venom of an Australian funnel web spider. Nat Struct Biol. 1997 Jul;4(7):559-66.","The structure of a novel insecticidal neurotoxin, omega-atracotoxin-HV1, from the venom of an Australian funnel web spider.",published,journal,Nat. Struct. Biol.,Nature structural biology,4,7,,1072-8368,,,,,,,,,,,,,,,,,,,,559,566,1997,"A family of potent insecticidal toxins has recently been isolated from the venom of Australian funnel web spiders. Among these is the 37-residue peptide omega-atracotoxin-HV1 (omega-ACTX-HV1) from Hadronyche versuta. We have chemically synthesized and folded omega-ACTX-HV1, shown that it is neurotoxic, ascertained its disulphide bonding pattern, and determined its three-dimensional solution structure using NMR spectroscopy. The structure consists of a solvent-accessible beta-hairpin protruding from a disulphide-bonded globular core comprising four beta-turns. The three intramolecular disulphide bonds from a cystine knot motif similar to that seen in several other neurotoxic peptides. Despite limited sequence identity, omega-ACTX-HV1 displays significant structural homology with the omega-agatoxins and omega-conotoxins, both of which are vertebrate calcium channel antagonists; however, in contrast with these toxins, we show that omega-ACTX-HV1 inhibits insect, but not mammalian, voltage-gated calcium channel currents." citations,Ref_2,6194,241255,3,,reference citation,,,11313356,,"Tedford HW, Fletcher JI, King GF. Functional significance of the beta hairpin in the insecticidal neurotoxin omega-atracotoxin-Hv1a. J Biol Chem. 2001 Jul 13;276(28):26568-76.",Functional significance of the beta hairpin in the insecticidal neurotoxin omega-atracotoxin-Hv1a.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,276,28,,0021-9258,,,,,,,,,,,,,,,,,,,,26568,26576,2001,"omega-Atracotoxin-Hv1a is an insect-specific neurotoxin whose phylogenetic specificity derives from its ability to antagonize insect, but not vertebrate, voltage-gated calcium channels. In order to help understand its mechanism of action and to enhance its utility as a lead compound for insecticide development, we used a combination of protein engineering and site-directed mutagenesis to probe the toxin for key functional regions. First, we constructed a Hairpinless mutant in which the C-terminal beta-hairpin, which is highly conserved in this family of neurotoxins, was excised without affecting the fold of the residual disulfide-rich core of the toxin. The Hairpinless mutant was devoid of insecticidal activity, indicating the functional importance of the hairpin. We subsequently developed a highly efficient system for production of recombinant toxin and then probed the hairpin for key functional residues using alanine-scanning mutagenesis followed by a second round of mutagenesis based on initial ""hits"" from the alanine scan. This revealed that two spatially proximal residues, Asn(27) and Arg(35), form a contiguous molecular surface that is essential for toxin activity. We propose that this surface of the beta-hairpin is a key site for interaction of the toxin with insect calcium channels." citations,entry_citation,6195,241272,1,,entry citation,,,15329414,,,A small CDC25 dual-specificity tyrosine-phosphatase isoform in Arabidopsis thaliana,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,,,,,,,,,,,,,,,,,,,,,,,,,,2004, citations,entry_citation,6196,241293,1,,entry citation,,,15329414,,,A small CDC25 dual-specificity tyrosine-phosphatase isoform in Arabidopsis thaliana,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,,,,,,,,,,,,,,,,,,,,,,,,,,2004, citations,entry_citation,6197,241314,1,,entry citation,,,,,,"1H, 15N and 13C assigned chemical shifts for the Myosin type I SH3 domain (Myo3) from saccharomyces cerevisiae",published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,,This data will only be published in BMRB. citations,entry_citation,6198,241335,1,,entry citation,,,15937903,,,NMR structure determination of the conserved hypothetical protein TM1816 from Thermotoga maritima,published,journal,Proteins,,60,3,,,,,,,,,,,,,,,,,,,,,,552,557,2005, citations,entry_citation,6199,241350,1,,entry citation,,,,,,"Structure of 5,10 methenyltetrahydrofolate synthetase from Aquifex aeolicus",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,62,241366,1,,entry citation,,,,,"LeMaster, David M., Richards, Frederic M., ""NMR Sequential Assignment of Escherichia coli Thioredoxin Utilizing Random Fractional Deuteriation,"" Biochemistry 27, 142-150 (1988).","NMR Sequential Assignment of Escherichia coli Thioredoxin Utilizing Random Fractional Deuteriation",published,journal,Biochemistry,,27,,,,,,,,,,,,,,,,,,,,,,,142,150,1988, citations,entry_citation,6200,241379,1,,entry citation,,,15225618,,,Determination of a high-precision NMR structure of the minicollagen cysteine rich domain from Hydra and characterization of its disulfide bond formation,published,journal,FEBS Lett.,,569,1,,,,,,,,,,,,,,,,,,,,,,112,116,2004, citations,entry_citation,6201,241394,1,,entry citation,,,15713084,,,"Design of a Calcium-Binding Protein with Desired Structure in a Cell Adhesion Molecule",published,journal,J. Am. Chem. Soc.,,127,7,,,,,,,,,,,,,,,,,,,,,,2085,2093,2005, citations,entry_citation,6202,241410,1,,entry citation,,,,,,"Letter to the Editor: Assignment of the 1H, 13C, and 15N resonances of the class II E2 conjugating enzyme, Ubc1",published,journal,J. Biomol NMR,,30,3,,,,,,,,,,,,,,,,,,,,,,369,370,2004, citations,entry_citation,6203,241435,1,,entry citation,,,,,,"How Insulin Binds: the B-Chain alpha-Helix Contacts the L1 beta -Helix of the Insulin Receptor.",published,journal,J. Mol. Biol.,,341,,,,,,,,,,,,,,,,,,,,,,,529,550,2004, citations,entry_citation,6204,241455,1,,entry citation,,,,,,"How Insulin Binds: the B-Chain alpha-Helix Contacts the L1 beta -Helix of the Insulin Receptor.",published,journal,J. Mol. Biol.,,341,,,,,,,,,,,,,,,,,,,,,,,529,550,2004, citations,entry_citation,6205,241478,1,,entry citation,,,,,,"How Insulin Binds: the B-Chain alpha-Helix Contacts the L1 beta -Helix of the Insulin Receptor.",published,journal,J. Mol. Biol.,,341,,,,,,,,,,,,,,,,,,,,,,,529,550,2004, citations,entry_citation,6207,241499,1,,entry citation,,,16027363,,,NMR data collection and analysis protocol for high-throughput protein structure determination,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,102,30,,,,,,,,,,,,,,,,,,,,,,10487,10492,2005, citations,entry_citation,6208,241513,1,,entry citation,,,,,,"1H, 13C and 15N Assigned Chemical Shifts for Diacylglycerol kinase alpha",in preparation,journal,J. Biomol. NMR,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation,6209,241537,1,,entry citation,,,,,,"Letter to the Editor: Solution Structure of a Calmodulin-Like Calcium-Binding Domain from Arabidopsis thaliana",published,journal,J. Biomol. NMR,,30,4,,,,,,,,,,,,,,,,,,,,,,451,456,2004, citations,entry_citation,6210,241559,1,,entry citation,,,,,,1H and 15N Assigned Chemical Shifts for HR2106,in preparation,journal,J. Biomol. NMR,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6211,241579,1,,entry citation,,,15362858,,,"NMR Solution Structure of ImB2, a Protein Conferring Immunity to Antimicrobial Activity of the Type IIa Bacteriocin, Carnobacteriocin B2",published,journal,Biochemistry,,43,37,,,,,,,,,,,,,,,,,,,,,,11740,11749,2004, citations,entry_citation,6263,242707,1,,entry citation,,,15691333,,,"Structural Determinants of Protein Stabilization by Solutes: The Important of the Hair-pin Loop in Rubredoxins",published,journal,FEBS J.,,272,4,,,,,,,,,,,,,,,,,,,,,,999,1011,2005, citations,ref_1,6211,241580,2,,reference citation,,,8520220,,"Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J. & Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes, J. Biomol. NMR. 6, 277-93.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref_2,6211,241581,3,,reference citation,,,,,"Johnson, B. A. & Blevins, R. A. (1994) NMR View - a Computer-Program for the Visualization and Analysis of NMR Data, J. Biomol. NMR. 4, 603-614.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6212,241610,1,,entry citation,,,15327958,,,"Solution structure of subunit f(6) from the peripheral stalk region of ATP synthase from bovine heart mitochondria",published,journal,J. Mol. Biol.,,342,2,,,,,,,,,,,,,,,,,,,,,,593,603,2004, citations,entry_citation,6214,241627,1,,entry citation,,,14872124,,,"Signal assignments and chemical-shift structural analysis of uniformly 13C, 15N-labeled peptide, mastoparan-X, by multidimensional solid-state NMR under magic-angle spinning",published,journal,J. Biomol. NMR,,28,4,,,,,,,,,,,,,,,,,,,,,,311,325,2004, citations,entry_citation,6216,241642,1,,entry citation,,,15234987,,,"A classic zinc finger from friend of GATA mediates an interaction with the coiled-coil of transforming acidic coiled-coil 3",published,journal,J. Biol. Chem.,,279,38,,,,,,,,,,,,,,,,,,,,,,39789,39797,2004, citations,entry_citation,6217,241667,1,,entry citation,,,15369808,,,"Antibiotic Activity and Structural Analysis of the Scorpion-derived Antimicrobial peptide IsCT and Its Analogs",published,journal,Biochem. Biophys. Res. Commun.,,323,2,,,,,,,,,,,,,,,,,,,,,,712,719,2004, citations,entry_citation,6218,241687,1,,entry citation,,,15369808,,,"Antibiotic Activity and Structural Analysis of the Scorpion-derived Antimicrobial peptide IsCT and Its Analogs",published,journal,Biochem. Biophys. Res. Commun.,,323,2,,,,,,,,,,,,,,,,,,,,,,712,719,2004, citations,entry_citation,6219,241706,1,,entry citation,,,15369808,,,"Antibiotic Activity and Structural Analysis of the Scorpion-derived Antimicrobial peptide IsCT and Its Analogs",published,journal,Biochem. Biophys. Res. Commun.,,323,2,,,,,,,,,,,,,,,,,,,,,,712,719,2004, citations,entry_citation,6220,241728,1,,entry citation,,,15369808,,,"Antibiotic Activity and Structural Analysis of the Scorpion-derived Antimicrobial peptide IsCT and Its Analogs",published,journal,Biochem. Biophys. Res. Commun.,,323,2,,,,,,,,,,,,,,,,,,,,,,712,719,2004, citations,entry_citation,6221,241750,1,,entry citation,,,15614636,,,"1H, 15N and 13C Chemical Shifts Assignments of the Resuscitation Promoting Factor domain of Rv1009 from Mycobacterium tuberculosis",published,journal,J. Biomol. NMR,,30,3,,,,,,,,,,,,,,,,,,,,,,373,374,2004, citations,entry_citation,6222,241764,1,,entry citation,,,,,,Solution Structure of Kurtoxin,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6223,241780,1,,entry citation,,,17091334,,,"Simultaneous NMR assignment of backbone and side chain amides in large proteins with IS-TROSY",published,journal,J. Biomol. NMR,,36,4,,,,,,,,,,,,,,,,,,,,,,205,214,2006, citations,entry_citation,6224,241797,1,,entry citation,,,,,,"Letter to the Editor: Assignment of the 1H, 15N and 13C resonances of SufA from Escherichia coli involved in Fe-S cluster biosynthesis",published,journal,J. Biomol. NMR,,30,3,,,,,,,,,,,,,,,,,,,,,,379,380,2004, citations,entry_citation,6225,241821,1,,entry citation,,,,,,"Letter to the Editor: 1H, 15N, and 13C Resonance Assignment of the Amino-terminal Domain of Tfb1 subunit of yeast TFIIH",published,journal,J. Biomol. NMR,,31,2,,,,,,,,,,,,,,,,,,,,,,173,174,2005, citations,entry_citation,6226,241854,1,,entry citation,,,15756471,,,"Letter to the Editor: 1H, 13C and 15N chemical shift assignment of the C-terminal 15 kDa domain of novel galactose-binding protein from the earth worm Lumbricus terrestris",published,journal,J. Biomol. NMR,,30,3,,,,,,,,,,,,,,,,,,,,,,377,378,2004, citations,entry_citation,6227,241870,1,,entry citation,,,15537753,,,"Native and non-native conformational preferences in the urea-unfolded state of barstar",published,journal,Protein Sci.,,13,,,,,,,,,,,,,,,,,,,,,,,3085,3091,2004, citations,ref_1,6227,241871,2,,reference citation,,,2146954,,"Nunez DJ, Davenport AP, Brown MJ. Abstract Atrial natriuretic factor mRNA and binding sites in the adrenal gland. Biochem J. 1990 Oct 15;271(2):555-8.",Atrial natriuretic factor mRNA and binding sites in the adrenal gland.,published,journal,Biochem. J.,The Biochemical journal,271,2,,0264-6021,,,,,,,,,,,,,,,,,,,,555,558,1990,"The factor inhibiting aldosterone secretion produced by the adrenal medulla may be atrial natriuretic factor (ANF), since the latter abolishes aldosterone release in response to a number of secretagogues, including angiotensin II and K+. In this study we have shown that cells in the adrenal medulla contain ANF mRNA and therefore have the potential to synthesize this peptide. The presence of binding sites for ANF predominantly in the adrenal zona glomerulosa suggests that, if ANF is synthesized in the medulla and transferred to the cortex, it may affect mineralocorticoid status." citations,entry_citation,6228,241893,1,,entry citation,,,15772072,,,"The solution structure of the FATC domain of the protein kinase TOR suggests a role for redox-dependent structural and cellular stability",published,journal,J. Biol. Chem.,,280,21,,,,,,,,,,,,,,,,,,,,,,20558,20564,2005, citations,entry_citation,6229,241908,1,,entry citation,,,15452445,,,"Letter to the Editor: TROSY-driven NMR backbone assignments of the 381-residue nucleotide-binding domain of the Thermus Thermophilus DnaK molecular chaperone.",published,journal,J. Biomol. NMR,,30,1,,,,,,,,,,,,,,,,,,,,,,113,114,2004, citations,ref_1,6229,241909,2,,reference citation,,,15452445,,"Letter to the Editor: TROSY-driven NMR backbone assignments of the 381-residue nucleotide-binding domain of the Thermus Thermophilus DnaK molecular chaperone. Revington, M., and Zuiderweg, E.R.P. J. Biol. NMR in press",TROSY-driven NMR backbone assignments of the 381-residue nucleotide-binding domain of the Thermus Thermophilus DnaK molecular chaperone.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,30,1,,0925-2738,,,,,,,,,,,,,,,,,,,,113,114,2004, citations,ref_2,6229,241910,3,,reference citation,,,15175340,,"NMR study of nucleotide-induced changes in the nucleotide binding domain of Thermus Thermophilus Hsp70 chaperone DnaK: Implications for the allosteric mechanism. Revington M, Holder TM, Zuiderweg ER. J Biol Chem. 2004 Jun 2 [Epub ahead of print]",NMR study of nucleotide-induced changes in the nucleotide binding domain of Thermus thermophilus Hsp70 chaperone DnaK: implications for the allosteric mechanism.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,279,32,,0021-9258,,,,,,,,,,,,,,,,,,,,33958,33967,2004,"We present an NMR investigation of the nucleotide-dependent conformational properties of a 44-kDa nucleotide binding domain (NBD) of an Hsp70 protein. Conformational changes driven by ATP binding and hydrolysis in the N-terminal NBD are believed to allosterically regulate substrate affinity in the C-terminal substrate binding domain. Several crystal structures of Hsc70 NBDs in different nucleotide states have, however, not shown significant structural differences. We have previously reported the NMR assignments of the backbone resonances of the NBD of the bacterial Hsp70 homologue Thermus thermophilus DnaK in the ADP-bound state. In this study we show, by assigning the NBD with the ATP/transition state analogue, ADP.AlFx, bound, that it closely mimics the ATP-bound state. Chemical shift difference mapping of the two nucleotide states identified differences in a cluster of residues at the interface between subdomains 1A and 1B. Further analysis of the spectra revealed that the ATP state exhibited a single conformation, whereas the ADP state was in slow conformational exchange between a form similar to the ATP state and another state unique to the ADP-bound form. A model is proposed of the allosteric mechanism based on the nucleotide state altering the balance of a dynamic equilibrium between the open and closed states. The observed chemical shift perturbations were concentrated in an area close to a previously described J-domain binding channel, confirming the importance of that region in the allosteric mechanism." citations,entry_citation,623,241935,1,,entry citation,,,,,"Price, William S., Mendz, George L., Martenson, Russell E., ""Conformation of a Heptadecapeptide Comprising the Segment Encephalitogenic in Rhesus Monkeys,"" Biochemistry 27, 8990-8999 (1988).","Conformation of a Heptadecapeptide Comprising the Segment Encephalitogenic in Rhesus Monkeys",published,journal,Biochemistry,,27,,,,,,,,,,,,,,,,,,,,,,,8990,8999,1988, citations,entry_citation,6230,241948,1,,entry citation,,,,,,"Solution 1H NMR study of the active site molecular structure and magnetic properties of the cyanomet complex of the isolated, tetrameric beta-chain from human adult hemoglobin",published,journal,Biochim. Biophys. Acta,,1701,1-2,,,,,,,,,,,,,,,,,,,,,,75,87,2004, citations,entry_citation,6231,241971,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N resonance assignments and secondary structure of human pancreatitis-associated protein (hPAP)",published,journal,J. Biomol. NMR,,30,3,,,,,,,,,,,,,,,,,,,,,,381,382,2004, citations,entry_citation,6232,241989,1,,entry citation,,,16826544,,,Solution structures of the putative anti-sigma-factor antagonist TM1442 from Thermotoga maritima in the free and phosphorylated states.,published,journal,Magn Reson Chem.,,44,,,,,,,,,,,,,,,,,,,,,,,S61,S70,2006, citations,citation1,6233,242009,1,,entry citation,,,,,,"Letter to the Editor: Chemical shift assignments of the (poly)ubiquitin-binding region of the proteasome subunit S5a",published,journal,J. Biomol. NMR,,30,2,,,,,,,,,,,,,,,,,,,,,,231,232,2004, citations,entry_citation,6234,242028,1,,entry citation,,,,,,"The integral membrane enzyme PagP alternates between two dynamically distinct states.",in press,journal,Proc. Natl. Acad. Sci. U. S. A.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6235,242042,1,,entry citation,,,15733924,,,Aare Neuronal SNARE Proteins Ca(2+) Sensors?,published,journal,J. Mol. Biol.,,347,1,,,,,,,,,,,,,,,,,,,,,,145,158,2005, citations,entry_citation,6236,242067,1,,entry citation,,,15274612,,,"Three-Dimensional Structure of an Independently Folded Extracellular Domain of Human Amyloid-beta Precursor Protein",published,journal,Biochemistry,,43,30,,,,,,,,,,,,,,,,,,,,,,9583,9588,2004, citations,entry_citation,6237,242087,1,,entry citation,,,16678128,,,"Solution conformation of a neuronal nicotinic acetylcholine receptor antagonist alpha-conotoxin OmIA that discriminates alpha3 vs. alpha6 nAChR subtypes",published,journal,Biochem. Biophys. Res. Commun.,,345,1,,,,,,,,,,,,,,,,,,,,,,248,254,2006, citations,entry_citation,6238,242109,1,,entry citation,,,15476823,,,ZZ Domain of CBP: an Unusual Zinc Finger Fold in a Protein Interaction Module,published,journal,J. Mol. Biol.,,343,4,,,,,,,,,,,,,,,,,,,,,,1081,1093,2004, citations,citation_1,6239,242144,1,,entry citation,,,15328609,,,"The Solution Structure of the VS Ribozyme Active Site Loop Reveals a Dynamic 'Hotspot'",published,journal,J. Mol. Biol.,,341,4,,,,,,,,,,,,,,,,,,,,,,935,949,2004, citations,entry_citation,6240,242161,1,,entry citation,,,,,,"Solution structure of At5g66040, a putative protein from Arabidopsis Thaliana",in preparation,journal,J. Biomol. NMR,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6241,242188,1,,entry citation,,,,,,"Letter to the Editor: Assignment of the 1H, 13C, and 15N resonances of the josephin domain of human ataxin-3",published,journal,J. Biomol. NMR,,30,4,,,,,,,,,,,,,,,,,,,,,,457,458,2004, citations,ref_1,6241,242189,2,,reference citation,,,12914917,,"Masino L, Musi V, Menon RP, Fusi P, Kelly G, Frenkiel TA, Trottier Y, Pastore A. Abstract Domain architecture of the polyglutamine protein ataxin-3: a globular domain followed by a flexible tail. FEBS Lett. 2003 Aug 14;549(1-3):21-5.",Domain architecture of the polyglutamine protein ataxin-3: a globular domain followed by a flexible tail.,published,journal,FEBS Lett.,FEBS letters,549,1-3,,0014-5793,,,,,,,,,,,,,,,,,,,,21,25,2003,"Anomalous expansion of a polyglutamine (polyQ) tract in the protein ataxin-3 causes spinocerebellar ataxia type 3, an autosomal dominant neurodegenerative disease. Very little is known about the structure and the function of ataxin-3, although this information would undoubtedly help to understand why the expanded protein forms insoluble nuclear aggregates and causes neuronal cell death. With the aim of establishing the domain architecture of ataxin-3 and the role of the polyQ tract within the protein context, we have studied the human and murine orthologues using a combination of techniques, which range from limited proteolysis to circular dichroism (CD) and nuclear magnetic resonance (NMR) spectroscopies. The two protein sequences share a highly conserved N-terminus and differ only in the length of the glutamine repeats and in the C-terminus. Our data conclusively indicate that ataxin-3 is composed by a structured N-terminal domain, followed by a flexible tail. Moreover, [(15)N]glutamine selectively labelled samples allowed us to have a direct insight by NMR into the structure of the polyQ region." citations,ref_2,6241,242190,3,,reference citation,,,12196134,,"Masino L, Pastore A. Abstract Glutamine repeats: structural hypotheses and neurodegeneration. Biochem Soc Trans. 2002 Aug;30(4):548-51. Review.",Glutamine repeats: structural hypotheses and neurodegeneration.,published,journal,Biochem. Soc. Trans.,Biochemical Society transactions,30,4,,0300-5127,,,,,,,,,,,,,,,,,,,,548,551,2002,"A growing number of neurodegenerative diseases are caused by expansion of CAG trinucleotide repeats coding for polyglutamine. The presence of intranuclear inclusions in the affected neuronal cells has suggested a mechanism for pathogenesis based on protein misfolding and aggregation. Detailed understanding of these phenomena is therefore crucial in order to rationalize different phases of the diseases. In the past decade, a few studies have focused on the structural properties of polyglutamine and on the molecular bases of the aggregation process. Most of these studies have been performed on polyglutamine peptides and protein models. Only one report is currently available on the characterization of a full-length polyglutamine protein. The structural hypotheses resulting from these studies are reviewed here." citations,ref-1,6243,242233,2,,reference citation,,,8520220,,"Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. Abstract NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR. 1995 Nov;6(3):277-93.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref-2,6243,242234,3,,reference citation,,,,,"Orekhov, V. Y., Nolde, D. E., Golovanov, A. P., Korzhnev, D. M., Arseniev, A. S. Processing of heteronuclear NMR relaxation data with the new software DASHA. Applied Magnetic Resonance 9(4): 581-588. (1995).",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref-3,6243,242235,4,,reference citation,,,11775742,,"Korzhneva DM, Ibraghimov IV, Billeter M, Orekhov VY. Abstract MUNIN: application of three-way decomposition to the analysis of heteronuclear NMR relaxation data. J Biomol NMR. 2001 Nov;21(3):263-8.",MUNIN: application of three-way decomposition to the analysis of heteronuclear NMR relaxation data.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,21,3,,0925-2738,,,,,,,,,,,,,,,,,,,,263,268,2001,"MUNIN (Multidimensional NMR Spectra Interpretation), a recently introduced approach exploiting the mathematical concept of three-way decomposition, is proposed for separation and quantitative relaxation measurements of strongly overlapped resonances in sets of heteronuclear two-dimensional spectra that result from typical relaxation experiments. The approach is general and may also be applied to sets of two-dimensional spectra with arbitrary modulation along the third dimension (e.g., J-coupling, diffusion). Here, the method is applied for the analysis of 15N rotating frame relaxation data." citations,entry_citation,6244,242277,1,,entry citation,,,,,,"Novel all alpha-helical fold for gene target gi3844938 from Mycoplasma genitalium",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6245,242308,1,,entry citation,,,15522230,,,"NMR structure of the glucose-dependent insulinotropic polypeptide fragment, GIP(1-30)amide",published,journal,Biochem. Biophys. Res. Commun.,,325,1,,,,,,,,,,,,,,,,,,,,,,281,286,2004, citations,entry_citation,6246,242332,1,,entry citation,,,15271353,,,"Structural transitions as determinants of the action of the calcium-dependent antibiotic daptomycin",published,journal,Chem. Biol.,,11,7,,,,,,,,,,,,,,,,,,,,,,949,957,2004, citations,entry_citation,6247,242360,1,,entry citation,,,15978837,,,Refolding and purification of recombinant OsNifU1A domain II that was expressed by Escherichia coli.,published,journal,Protein Expr. Purif.,,43,2,,,,,,,,,,,,,,,,,,,,,,149,156,2005, citations,entry_citation,6248,242380,1,,entry citation,,,,,,NMR Structure of a Complex Between MDM2 and a Small Molecule Inhibitor,published,journal,J. Biomol. NMR,,30,2,,,,,,,,,,,,,,,,,,,,,,163,173,2004, citations,citation_1,6249,242404,1,,entry citation,,,,,,"Letter to the Editor: 1H, 15N and 13C Backbone resonance assignments of the 37 kDA surface antigen protein Bd37 from Babesia divergens.",published,journal,J. Biomol. NMR,,31,1,,,,,,,,,,,,,,,,,,,,,,67,68,2005, citations,entry_citation,6250,242419,1,,entry citation,,,12850150,,,"Native-like partially folded conformations and folding process revealed in the N-terminal large fragments of staphylococcal nuclease: a study by NMR spectroscopy",published,journal,J. Mol. Biol.,,330,4,,,,,,,,,,,,,,,,,,,,,,821,837,2003, citations,entry_citation,6251,242438,1,,entry citation,,,12850150,,,"Native-like partially folded conformations and folding process revealed in the N-terminal large fragments of staphylococcal nuclease: a study by NMR spectroscopy",published,journal,J. Mol. Biol.,,330,4,,,,,,,,,,,,,,,,,,,,,,821,837,2003, citations,entry_citation,6252,242459,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C, 15N Resonance Assignments of the EscJ Protein, a Structural Component of the Type III Secretion System of Enteropathogenic E. coli (EPEC)",published,journal,J. Biomol. NMR,,30,3,,,,,,,,,,,,,,,,,,,,,,387,388,2004, citations,entry_citation,6253,242487,1,,entry citation,,,,,,"Letter to the Editor: 1H, 15N and 13C resonance assignment of human gamma S- crystallin, a 21-kDa eye-lens protein",published,journal,J. Biomol. NMR,,30,3,,,,,,,,,,,,,,,,,,,,,,385,386,2004, citations,citation,6254,242513,1,,entry citation,,,15606769,,,"Solution structure of the active-centre mutant I14A of the histidine-containing phosphocarrier protein from Staphylococcus carnosus",published,journal,Eur. J. Biochem.,,271,23-24,,,,,,,,,,,,,,,,,,,,,,4815,4824,2004, citations,ref_1,6254,242514,2,,reference citation,,,,,"Gorler Adrian, Hengstenberg Wolfgang, Kravanja M., Beneicke W., Maurer Till, Kalbitzer ""Hans Robert"" Appl. Magn. Reson. 1999 17, 465-480",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_2,6254,242515,3,,reference citation,,,10794411,,"Kalbitzer HR, Gorler A, Li H, Dubovskii PV, Hengstenberg W, Kowolik C, Yamada H, Akasaka K. Protein Sci. 693-703 Protein Sci. 2000 Apr;9(4):693-703.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6255,242537,1,,entry citation,,,,,,Solution Structure of Ribosomal Protein L16 from Thermus thermophilus HB8,published,journal,J. Mol. Biol.,,344,5,,,,,,,,,,,,,,,,,,,,,,1369,1383,2004, citations,entry_citation,6256,242566,1,,entry citation,,,,,,"NMR solution structure of Thermotoga maritima protein TM1509 reveals a Zn-metalloprotease-like tertiary structure",published,journal,J. Struct. Funct. Genomics,,6,1,,,,,,,,,,,,,,,,,,,,,,51,62,2005, citations,entry_citation,6257,242592,1,,entry citation,,,15557279,,,"Alzheimer's Abeta40 Studied by NMR at Low pH Reveals That DSS Binds and Promotes beta-ball Oligomerization",published,journal,J. Biol. Chem.,,280,5,,,,,,,,,,,,,,,,,,,,,,3675,3685,2004, citations,entry_citation,6258,242607,1,,entry citation,,,15701516,,,"Solution Structure of the E.coli TolA C-terminal Domain Reveals Conformational Changes upon Binding to the Phage g3p N-terminal Domain",published,journal,J. Mol. Biol.,,346,4,,,,,,,,,,,,,,,,,,,,,,1047,1057,2005, citations,citation_1,6259,242623,1,,entry citation,,,16963640,,,"NMR structure of the enzyme GatB of the galactitol-specific phosphoenolpyruvate-dependent phosphotransferase system and its interaction with GatA.",published,journal,Protein Sci.,,15,10,,,,,,,,,,,,,,,,,,,,,,2435,2441,2006, citations,entry_citation,6265,242748,1,,entry citation,,,15231834,,,Structure and Biochemical Function of a Prototypical Arabidopsis U-box Domain,published,journal,J. Biol. Chem.,,279,38,,,,,,,,,,,,,,,,,,,,,,40053,40061,2004, citations,entry_citation,6266,242779,1,,entry citation,,,15476398,,,Solution structure of the apo and copper(I)-loaded human metallochaperone HAH1,published,journal,Biochemistry,,43,41,,,,,,,,,,,,,,,,,,,,,,13046,13053,2004, citations,entry_citation,6267,242811,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N resonance assignments of the phosphorylated enzyme IIB of the mannitol-specific phosphoenolpyruvate-dependent phosphotransferase system of Escherichia coli",published,journal,J. Biomol. NMR,,30,4,,,,,,,,,,,,,,,,,,,,,,461,462,2004, citations,entry_citation,6268,242836,1,,entry citation,,,15641773,,,CBP/p300 TAZ1 domain forms a structured scaffold for ligand binding,published,journal,Biochemistry,,44,2,,,,,,,,,,,,,,,,,,,,,,490,497,2005, citations,entry_citation,6269,242855,1,,entry citation,,,15459548,,,"Letters to the Editor: NMR assignment of the chicken prion protein fragments chPrP(128-242) and chPrP(25-242)",published,journal,J. Biomol. NMR,,30,1,,,,,,,,,,,,,,,,,,,,,,97,97,2004, citations,ref_1,6269,242856,2,,reference citation,,,1715573,,"Harris DA, Falls DL, Johnson FA, Fischbach GD. Related Articles, Links Free in PMC A prion-like protein from chicken brain copurifies with an acetylcholine receptor-inducing activity. Proc Natl Acad Sci U S A. 1991 Sep 1;88(17):7664-8.",A prion-like protein from chicken brain copurifies with an acetylcholine receptor-inducing activity.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,88,17,,0027-8424,,,,,,,,,,,,,,,,,,,,7664,7668,1991,"The mammalian prion protein (PrPC) is a cellular protein of unknown function, an altered isoform of which (PrPSc) is a component of the infectious particle (prion) thought to be responsible for spongiform encephalopathies in humans and animals. We report here the isolation of a cDNA that encodes a chicken protein that is homologous to PrPC. This chicken prion-like protein (ch-PrLP) is identical to the mouse PrP at 33% of its amino acid positions, including an uninterrupted stretch of 24 identical residues, and it displays the same structural domains. In addition, ch-PrLP, like its mammalian counterpart, is attached to the cell surface by a glycosyl-phosphatidylinositol anchor. We find that ch-PrLP is the major protein in preparations of an acetylcholine receptor-inducing activity that has been purified greater than 10(6)-fold from brain on the basis of its ability to stimulate synthesis of nicotinic receptors by cultured myotubes. The ch-PrLP gene is expressed in the spinal cord and brain as early as embryonic day 6; and in the spinal cord, the protein appears to be concentrated in motor neurons. Our results therefore raise the possibility that prion proteins serve normally to regulate the chemoreceptor number at the neuromuscular junction and perhaps in the central nervous system as well." citations,ref_2,6269,242857,3,,reference citation,,,9280298,,"Riek R, Hornemann S, Wider G, Glockshuber R, Wuthrich K. Related Articles, Links Abstract NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231). FEBS Lett. 1997 Aug 18;413(2):282-8.","NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231).",published,journal,FEBS Lett.,FEBS letters,413,2,,0014-5793,,,,,,,,,,,,,,,,,,,,282,288,1997,"The recombinant murine prion protein, mPrP(23-231), was expressed in E. coli with uniform 15N-labeling. NMR experiments showed that the previously determined globular three-dimensional structure of the C-terminal domain mPrP(121-231) is preserved in the intact protein, and that the N-terminal polypeptide segment 23-120 is flexibly disordered. This structural information is based on nearly complete sequence-specific assignments for the backbone amide nitrogens, amide protons and alpha-protols of the polypeptide segment of residues 121-231 in mPrP(23-231). Coincidence of corresponding sequential and medium-range nuclear Overhauser effects (NOE) showed that the helical secondary structures previously identified in mPrP(121-231) are also present in mPrP(23-231), and near-identity of corresponding amide nitrogen and amide proton chemical shifts indicates that the three-dimensional fold of mPrP(121-231) is also preserved in the intact protein. The linewidths in heteronuclear 1H-15N correlation spectra and 15N[1H]-NOEs showed that the well structured residues 126-230 have correlation times of several nanoseconds, as is typical for small globular proteins, whereas correlation times shorter than 1 nanosecond were observed for all residues of mPrP(23-231) outside of this domain." citations,entry_citation,6270,242872,1,,entry citation,,,15459548,,,"Letters to the Editor: NMR assignment of the chicken prion protein fragments chPrP(128-242) and chPrP(25-242)",published,journal,J. Biomol. NMR,,30,1,,,,,,,,,,,,,,,,,,,,,,97,97,2004, citations,ref_1,6270,242873,2,,reference citation,,,1715573,,"Harris DA, Falls DL, Johnson FA, Fischbach GD. Related Articles, Links Free in PMC A prion-like protein from chicken brain copurifies with an acetylcholine receptor-inducing activity. Proc Natl Acad Sci U S A. 1991 Sep 1;88(17):7664-8.",A prion-like protein from chicken brain copurifies with an acetylcholine receptor-inducing activity.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,88,17,,0027-8424,,,,,,,,,,,,,,,,,,,,7664,7668,1991,"The mammalian prion protein (PrPC) is a cellular protein of unknown function, an altered isoform of which (PrPSc) is a component of the infectious particle (prion) thought to be responsible for spongiform encephalopathies in humans and animals. We report here the isolation of a cDNA that encodes a chicken protein that is homologous to PrPC. This chicken prion-like protein (ch-PrLP) is identical to the mouse PrP at 33% of its amino acid positions, including an uninterrupted stretch of 24 identical residues, and it displays the same structural domains. In addition, ch-PrLP, like its mammalian counterpart, is attached to the cell surface by a glycosyl-phosphatidylinositol anchor. We find that ch-PrLP is the major protein in preparations of an acetylcholine receptor-inducing activity that has been purified greater than 10(6)-fold from brain on the basis of its ability to stimulate synthesis of nicotinic receptors by cultured myotubes. The ch-PrLP gene is expressed in the spinal cord and brain as early as embryonic day 6; and in the spinal cord, the protein appears to be concentrated in motor neurons. Our results therefore raise the possibility that prion proteins serve normally to regulate the chemoreceptor number at the neuromuscular junction and perhaps in the central nervous system as well." citations,entry_citation,6282,243153,1,,entry citation,,,15459548,,,"Letters to the Editor: NMR assignment of the turtle prion protein fragments tPrP(121-225)",published,journal,J. Biomol. NMR,,30,1,,,,,,,,,,,,,,,,,,,,,,97,97,2004, citations,entry_citation,6283,243168,1,,entry citation,,,,,,Letter to the Editor: NMR Structure of Human Coactosin-Like Protein,published,journal,J. Biomol. NMR,,30,3,,,,,,,,,,,,,,,,,,,,,,353,356,2004, citations,entry_citation,6284,243192,1,,entry citation,,,15649896,,,"Crystal and solution structures of the helicase-binding domain of Escherichia coli primase",published,journal,J. Biol. Chem.,,280,12,,,,,,,,,,,,,,,,,,,,,,11495,11504,2005, citations,entry_citation,6285,243209,1,,entry citation,,,15642262,,,"A vinculin binding domain from the talin rod unfolds to form a complex with the vinculin head",published,journal,Structure,,13,1,,,,,,,,,,,,,,,,,,,,,,65,74,2005, citations,ref_2,6270,242874,3,,reference citation,,,9280298,,"Riek R, Hornemann S, Wider G, Glockshuber R, Wuthrich K. Related Articles, Links Abstract NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231). FEBS Lett. 1997 Aug 18;413(2):282-8.","NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231).",published,journal,FEBS Lett.,FEBS letters,413,2,,0014-5793,,,,,,,,,,,,,,,,,,,,282,288,1997,"The recombinant murine prion protein, mPrP(23-231), was expressed in E. coli with uniform 15N-labeling. NMR experiments showed that the previously determined globular three-dimensional structure of the C-terminal domain mPrP(121-231) is preserved in the intact protein, and that the N-terminal polypeptide segment 23-120 is flexibly disordered. This structural information is based on nearly complete sequence-specific assignments for the backbone amide nitrogens, amide protons and alpha-protols of the polypeptide segment of residues 121-231 in mPrP(23-231). Coincidence of corresponding sequential and medium-range nuclear Overhauser effects (NOE) showed that the helical secondary structures previously identified in mPrP(121-231) are also present in mPrP(23-231), and near-identity of corresponding amide nitrogen and amide proton chemical shifts indicates that the three-dimensional fold of mPrP(121-231) is also preserved in the intact protein. The linewidths in heteronuclear 1H-15N correlation spectra and 15N[1H]-NOEs showed that the well structured residues 126-230 have correlation times of several nanoseconds, as is typical for small globular proteins, whereas correlation times shorter than 1 nanosecond were observed for all residues of mPrP(23-231) outside of this domain." citations,citation,6271,242889,1,,entry citation,,,17363368,,,"Molecular insights into quorum sensing in the human pathogen Pseudomonas aeruginosa from the structure of the virulence regulator LasR bound to its autoinducer",published,journal,J. Biol. Chem.,,282,18,,,,,,,,,,,,,,,,,,,,,,13592,13600,2007, citations,entry_citation,6272,242904,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C AND 15N NMR Assignments of MTH0776 from Methanobacterium thermoautotrophicum",published,journal,J. Biomol. NMR,,30,4,,,,,,,,,,,,,,,,,,,,,,459,460,2004, citations,ref_citation,6272,242905,2,,reference citation,,,,,,Solution Structure of MTH0776 from Methanobacterium Thermoautotrophicum,,journal,J. Biomol. NMR,,33,1,,,,,,,,,,,,,,,,,,,,,,51,56,2005, citations,entry_citation,6273,242932,1,,entry citation,,,16530466,,,"Spectroscopic and structural impact of a stem base-pair change in DNA hairpins: GTTC-ACA-GAAC versus GTAC-ACA-GTAC.",published,journal,Spectrochim. Acta. A. Mol. Biomol. Spectrosc.,,65,1,,,,,,,,,,,,,,,,,,,,,,84,94,2006, citations,entry_citation,6274,242951,1,,entry citation,,,16530466,,,"Spectroscopic and structural impact of a stem base-pair change in DNA hairpins: GTTC-ACA-GAAC versus GTAC-ACA-GTAC.",published,journal,Spectrochim. Acta. A. Mol. Biomol. Spectrosc.,,65,1,,,,,,,,,,,,,,,,,,,,,,84,94,2006, citations,entry_citation,6275,242969,1,,entry citation,,,,,,NMR assignment of the six zinc fingers of MTF-1 in the free and DNA bound states,published,journal,J. Biomol. NMR,,31,1,,,,,,,,,,,,,,,,,,,,,,94,94,2005, citations,Original_cloning_of_MTF-1,6275,242970,2,,reference citation,,,8467794,,"Radtke, F., Heuchel, R., Georgiev, O., Hergersberg, M., Gariglio, M., Dembic, Z., and Schaffner, W. (1993). Cloned transcription factor MTF-1 activates the mouse metallothionein I promoter. EMBO J., 12, 1355-1362.",Cloned transcription factor MTF-1 activates the mouse metallothionein I promoter.,published,journal,EMBO J.,The EMBO journal,12,4,,0261-4189,,,,,,,,,,,,,,,,,,,,1355,1362,1993,"Metallothioneins (MTs) are small cysteine-rich proteins whose structure is conserved from fungi to man. MTs strongly bind heavy metals, notably zinc, copper and cadmium. Upon exposure of cells to heavy metal and other adverse treatments, MT gene transcription is strongly enhanced. Metal induction is mediated by several copies of a 15 bp consensus sequence (metal-responsive element, MRE) present in the promoter region of MT genes. We and others have demonstrated the presence of an MRE-binding factor in HeLa cell nuclear extracts. We found that this factor, termed MTF-1 (MRE-binding transcription factor) is inactivated/reactivated in vitro by zinc withdrawal/addition. Here we report that the amounts of MTF-1-DNA complexes are elevated several-fold in zinc-treated cells, as measured by bandshift assay. We have also cloned the cDNA of mouse MTF-1, a 72.5 kDa protein. MTF-1 contains six zinc fingers and separate transcriptional activation domains with high contents of acidic and proline residues. Ectopic expression of MTF-1 in primate or rodent cells strongly enhances transcription of a reporter gene that is driven by four consensus MREd sites, or by the complete mouse MT-I promoter, even at normal zinc levels." citations,entry_citation,6276,243000,1,,entry citation,,,,,,NMR assignment of the six zinc fingers of MTF-1 in the free and DNA-bound states,published,journal,J. Biomol. NMR,,31,1,,,,,,,,,,,,,,,,,,,,,,94,94,2005, citations,Original_cloning_of_MTF-1,6276,243001,2,,reference citation,,,8467794,,"Radtke, F., Heuchel, R., Georgiev, O., Hergersberg, M., Gariglio, M., Dembic, Z., and Schaffner, W. (1993). Cloned transcription factor MTF-1 activates the mouse metallothionein I promoter. EMBO J., 12, 1355-1362.",Cloned transcription factor MTF-1 activates the mouse metallothionein I promoter.,published,journal,EMBO J.,The EMBO journal,12,4,,0261-4189,,,,,,,,,,,,,,,,,,,,1355,1362,1993,"Metallothioneins (MTs) are small cysteine-rich proteins whose structure is conserved from fungi to man. MTs strongly bind heavy metals, notably zinc, copper and cadmium. Upon exposure of cells to heavy metal and other adverse treatments, MT gene transcription is strongly enhanced. Metal induction is mediated by several copies of a 15 bp consensus sequence (metal-responsive element, MRE) present in the promoter region of MT genes. We and others have demonstrated the presence of an MRE-binding factor in HeLa cell nuclear extracts. We found that this factor, termed MTF-1 (MRE-binding transcription factor) is inactivated/reactivated in vitro by zinc withdrawal/addition. Here we report that the amounts of MTF-1-DNA complexes are elevated several-fold in zinc-treated cells, as measured by bandshift assay. We have also cloned the cDNA of mouse MTF-1, a 72.5 kDa protein. MTF-1 contains six zinc fingers and separate transcriptional activation domains with high contents of acidic and proline residues. Ectopic expression of MTF-1 in primate or rodent cells strongly enhances transcription of a reporter gene that is driven by four consensus MREd sites, or by the complete mouse MT-I promoter, even at normal zinc levels." citations,entry_citation,6277,243026,1,,entry citation,,,15522302,,,Solution structure of the ubiquitin-conjugating enzyme UbcH5B,published,journal,J. Mol. Biol.,,344,2,,,,,,,,,,,,,,,,,,,,,,513,526,2004, citations,entry_citation,6278,243045,1,,entry citation,,,11879635,,,Sly1 Binds to Golgi and ER Syntaxins via a Conserved N-Terminal Peptide Motif,published,journal,Dev. Cell,,2,,,,,,,,,,,,,,,,,,,,,,,295,305,2002, citations,entry_citation,6279,243063,1,,entry citation,,,,,,"Letter to Editor: 1H, 13C and 15N resonance assignments and secondary structure of the murine angiogenin 4",published,journal,J. Biomol. NMR,,31,2,,,,,,,,,,,,,,,,,,,,,,175,176,2005, citations,entry_citation,6280,243097,1,,entry citation,,,,,,"Letter to the Editor: Resonance assignments of the double-stranded RNA-binding of adenosine deaminase acting on RNA 2 (ADAR2)",published,journal,J. Biomol. NMR,,31,1,,,,,,,,,,,,,,,,,,,,,,71,72,2005, citations,entry_citation,6286,243222,1,,entry citation,,,15837933,,,"From The Cover: Structural insights into the interaction and activation of histone deacetylase 3 by nuclear receptor corepressors.",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,102,17,,,,,,,,,,,,,,,,,,,,,,6009,6014,2005, citations,entry_citation,6287,243238,1,,entry citation,,,,,,Diversity in structure and function of the Ets family pointed domains,in press,journal,J. Mol. Biol.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6288,243265,1,,entry citation,,,15606783,,,"Solution structure of long neurotoxin NTX-1 from the venom of Naja naja oxiana by 2D-NMR spectroscopy",published,journal,Eur. J. Biochem.,,271,23-24,,,,,,,,,,,,,,,,,,,,,,4950,4957,2004, citations,entry_citation,6289,243284,1,,entry citation,,,15488768,,,NMR structure of the C-terminal domain of SecA in the free state.,published,journal,Biochim. Biophys. Acta,Biochimica et biophysica acta,1702,2,,,,,,,,,,,,,,,,,,,,,,163,171,2004, citations,entry_citation,6290,243311,1,,entry citation,,,15511227,,,Solution Structure of Cu Metallothionein from the fungus Neurospora crassa,published,journal,Eur. J. Biochem.,,271,21,,,,,,,,,,,,,,,,,,,,,,4213,4221,2004, citations,entry_citation,6291,243327,1,,entry citation,,,,,,"Solution structure of hypothetical membrane protein ta0354 from Thermoplasma acidophilum",published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,2005, citations,entry_citation,6292,243356,1,,entry citation,,,15803404,,,"Letter to the Editor: 1H, 15N and 13C assignments of the alkaline proteinase inhibitor APRin from Pseudomonas aeruginosa",published,journal,J. Biomol. NMR,,31,3,,,,,,,,,,,,,,,,,,,,,,265,266,2005, citations,entry_citation,6293,243383,1,,entry citation,,,,,,1H Assigned Chemical Shifts for FMBP-1 tandem repeat 2 in 30% (v/v) TFE solution,published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,2005, citations,entry_citation,6294,243401,1,,entry citation,,,,,,1H Assigned Chemical Shifts for FMBP-1 tandem repeat 4 in 30% (v/v) TFE solution,published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,2005, citations,entry_citation,6295,243419,1,,entry citation,,,15379538,,,"NMR structure of the flavin domain from soluble methane monooxygenase reductase from Methylococcus capsulatus (Bath)",published,journal,Biochemistry,,43,38,,,,,,,,,,,,,,,,,,,,,,11983,11991,2004, citations,entry_citation,6296,243457,1,,entry citation,,,,,,1H Assigned Chemical Shifts for FMBP-1 tandem repeat 3 in 30% (v/v) TFE solution,published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,2005, citations,entry_citation,6297,243475,1,,entry citation,,,15273307,,,Solution structure of the RWD domain of the mouse GCN2 protein,published,journal,Protein Sci.,,13,8,,,,,,,,,,,,,,,,,,,,,,2089,2100,2004, citations,entry_citation,6298,243505,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N Resonance Assignments of the Conserved Core of hAsf1 A",published,journal,J. Biomol. NMR,,29,3,,,,,,,,,,,,,,,,,,,,,,413,414,2004, citations,citation,6298,243506,2,,reference citation,,,15840725,,,Structural basis for the interaction of Asf1 with histone H3 and its functional implications.,,,Proc. Natl. Acad. Sci. U. S. A.,,102,,,,,,,,,,,,,,,,,,,,,,,5975,5980,2005, citations,entry_citation,6299,243525,1,,entry citation,,,15466413,,,"Solution Structure and Dynamics of a Prototypical Chordin-like Cysteine-rich Repeat (von Willebrand Factor Type C Module) from Collagen IIA",published,journal,J. Biol. Chem.,,279,51,,,,,,,,,,,,,,,,,,,,,,53857,53866,2004, citations,entry_citation,63,243541,1,,entry citation,,,,,"Wemmer, David, Kumar, N. Vasant, Metrione, Robert M., Lazdunski, Michel, Drobny, Gary P., Kallenbach, Neville R., ""NMR Analysis and Sequence of Toxin II from the Sea Anemone Radianthus paumotensis,"" Biochemistry 25, 6842-6849 (1986).","NMR Analysis and Sequence of Toxin II from the Sea Anemone Radianthus paumotensis",published,journal,Biochemistry,,25,,,,,,,,,,,,,,,,,,,,,,,6842,6849,1986, citations,entry_citation,630,243554,1,,entry citation,,,,,"Moore, Geoffrey R., Williams, Robert J. P., ""The Stability of Ferricytochrome c Temperature Dependence of Its NMR Spectrum,"" Eur. J. Biochem. 103, 523-532 (1980).",The Stability of Ferricytochrome c Temperature Dependence of Its NMR Spectrum,published,journal,Eur. J. Biochem.,,103,,,,,,,,,,,,,,,,,,,,,,,523,532,1980, citations,entry_citation,6300,243570,1,,entry citation,,,16644733,,,"Regulation of RhoGEF activity by intramolecular and intermolecular SH3 domain interactions",published,journal,J. Biol. Chem.,,281,27,,,,,,,,,,,,,,,,,,,,,,18774,18786,2006, citations,entry_citation,6301,243590,1,,entry citation,,,15449933,,,"Inverse electrostatic effect: electrostatic repulsion in the unfolded state stabilizes a leucine zipper",published,journal,Biochemistry,,43,39,,,,,,,,,,,,,,,,,,,,,,12436,12447,2004, citations,entry_citation,6302,243618,1,,entry citation,,,15700297,,,Artificial diiron proteins: From structure to function,published,journal,Biopolymers,,80,2-3,,,,,,,,,,,,,,,,,,,,,,264,278,2005, citations,entry_citation,6303,243639,1,,entry citation,,,15700297,,,Artificial diiron proteins: From structure to function,published,journal,Biopolymers,,80,2-3,,,,,,,,,,,,,,,,,,,,,,264,278,2005, citations,entry_citation,6304,243660,1,,entry citation,,,15355965,,,Structural and Dynamic Independence of Isopeptide-linked RanGAP1 and SUMO-1,published,journal,J. Biol. Chem.,,279,47,,,,,,,,,,,,,,,,,,,,,,49131,49137,2004, citations,entry_citation,6305,243679,1,,entry citation,,,15355965,,,Structural and Dynamic Independence of Isopeptide-linked RanGAP1 and SUMO-1,published,journal,J. Biol. Chem.,,279,47,,,,,,,,,,,,,,,,,,,,,,49131,49137,2004, citations,entry_citation,6306,243700,1,,entry citation,,,15355965,,,"Structural and Dynamic Independence of Isopeptide-linked RanGAP1 and SUMO-1",published,journal,J. Biol. Chem.,,279,47,,,,,,,,,,,,,,,,,,,,,,49131,49137,2004, citations,entry_citation,6307,243715,1,,entry citation,,,15498650,,,"d(G3T4G4) forms unusual dimeric G-quadruplex structure with the same general fold in the presence of K+, Na+ or NH4+ ions",published,journal,Bioorg. Med. Chem.,,12,22,,,,,,,,,,,,,,,,,,,,,,5735,5744,2004, citations,entry_citation,6308,243736,1,,entry citation,,,,,,NMR Assignment of the N-terminal Domain a of the Glycoprotein Chaperone ERp57,published,journal,J. Biomol. NMR,,33,2,,,,,,,,,,,,,,,,,,,,,,136,136,2005, citations,entry_citation,6309,243752,1,,entry citation,,,16647096,,,Structure of the envelope protein domain III of Omsk hemorrhagic fever virus,published,journal,Virology,,351,1,,,,,,,,,,,,,,,,,,,,,,188,195,2006, citations,entry_citation,6310,243765,1,,entry citation,,,,,,"Letter to the Editor: Backbone and side chain assignments of human Peptidylprolyl Isomerase Like 1 (hPPIL1)",published,journal,J. Biomol. NMR,,31,2,,,,,,,,,,,,,,,,,,,,,,179,180,2005, citations,entry_citation,6311,243778,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N assignments of the 25 kDa SPRY domain-containing SOCS box protein 2 (SSB-2)",published,journal,J. Biomol. NMR,,31,1,,,,,,,,,,,,,,,,,,,,,,69,70,2005, citations,entry_citation,6312,243804,1,,entry citation,,,19636813,,,NMR assignment of the Rhodobacter sphaeroides fasciclin-1 domain protein (Fdp),published,journal,Biomol. NMR Assignments,,1,1,,,,,,,,,,,,,,,,,,,,,,11,12,2007, citations,entry_citation,6313,243822,1,,entry citation,,,,,,"Letter to the Editor: Assignments for the Bombyx mori pheromone-binding protein fragment BmPBP(1-128) at pH 6.5",published,journal,J. Biomol. NMR,,31,1,,,,,,,,,,,,,,,,,,,,,,65,65,2005, citations,entry_citation,6336,244286,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C, and 15N resonance assignments of the 17 kDa Ap4A hydrolase from Homo sapiens in the presence and absence of ATP",published,journal,J. Biomol. NMR,,31,2,,,,,,,,,,,,,,,,,,,,,,181,182,2005, citations,ref_3,6313,243823,2,,reference citation,,,12522306,,"Herrmann T, Guntert P, Wuthrich K. J Biomol NMR. 2002 Nov;24(3):171-89.",Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,24,3,,0925-2738,,,,,,,,,,,,,,,,,,,,171,189,2002,"Novel algorithms are presented for automated NOESY peak picking and NOE signal identification in homonuclear 2D and heteronuclear-resolved 3D [(1)H,(1)H]-NOESY spectra during de novo protein structure determination by NMR, which have been implemented in the new software ATNOS (automated NOESY peak picking). The input for ATNOS consists of the amino acid sequence of the protein, chemical shift lists from the sequence-specific resonance assignment, and one or several 2D or 3D NOESY spectra. In the present implementation, ATNOS performs multiple cycles of NOE peak identification in concert with automated NOE assignment with the software CANDID and protein structure calculation with the program DYANA. In the second and subsequent cycles, the intermediate protein structures are used as an additional guide for the interpretation of the NOESY spectra. By incorporating the analysis of the raw NMR data into the process of automated de novo protein NMR structure determination, ATNOS enables direct feedback between the protein structure, the NOE assignments and the experimental NOESY spectra. The main elements of the algorithms for NOESY spectral analysis are techniques for local baseline correction and evaluation of local noise level amplitudes, automated determination of spectrum-specific threshold parameters, the use of symmetry relations, and the inclusion of the chemical shift information and the intermediate protein structures in the process of distinguishing between NOE peaks and artifacts. The ATNOS procedure has been validated with experimental NMR data sets of three proteins, for which high-quality NMR structures had previously been obtained by interactive interpretation of the NOESY spectra. The ATNOS-based structures coincide closely with those obtained with interactive peak picking. Overall, we present the algorithms used in this paper as a further important step towards objective and efficient de novo protein structure determination by NMR." citations,ref_4,6313,243824,3,,reference citation,,,12051947,,"Herrmann T, Guntert P, Wuthrich K. J Mol Biol. 2002 May 24;319(1):209-27.",Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA.,published,journal,J. Mol. Biol.,Journal of molecular biology,319,1,,0022-2836,,,,,,,,,,,,,,,,,,,,209,227,2002,"Combined automated NOE assignment and structure determination module (CANDID) is a new software for efficient NMR structure determination of proteins by automated assignment of the NOESY spectra. CANDID uses an iterative approach with multiple cycles of NOE cross-peak assignment and protein structure calculation using the fast DYANA torsion angle dynamics algorithm, so that the result from each CANDID cycle consists of exhaustive, possibly ambiguous NOE cross-peak assignments in all available spectra and a three-dimensional protein structure represented by a bundle of conformers. The input for the first CANDID cycle consists of the amino acid sequence, the chemical shift list from the sequence-specific resonance assignment, and listings of the cross-peak positions and volumes in one or several two, three or four-dimensional NOESY spectra. The input for the second and subsequent CANDID cycles contains the three-dimensional protein structure from the previous cycle, in addition to the complete input used for the first cycle. CANDID includes two new elements that make it robust with respect to the presence of artifacts in the input data, i.e. network-anchoring and constraint-combination, which have a key role in de novo protein structure determinations for the successful generation of the correct polypeptide fold by the first CANDID cycle. Network-anchoring makes use of the fact that any network of correct NOE cross-peak assignments forms a self-consistent set; the initial, chemical shift-based assignments for each individual NOE cross-peak are therefore weighted by the extent to which they can be embedded into the network formed by all other NOE cross-peak assignments. Constraint-combination reduces the deleterious impact of artifact NOE upper distance constraints in the input for a protein structure calculation by combining the assignments for two or several peaks into a single upper limit distance constraint, which lowers the probability that the presence of an artifact peak will influence the outcome of the structure calculation. CANDID test calculations were performed with NMR data sets of four proteins for which high-quality structures had previously been solved by interactive protocols, and they yielded comparable results to these reference structure determinations with regard to both the residual constraint violations, and the precision and accuracy of the atomic coordinates. The CANDID approach has further been validated by de novo NMR structure determinations of four additional proteins. The experience gained in these calculations shows that once nearly complete sequence-specific resonance assignments are available, the automated CANDID approach results in greatly enhanced efficiency of the NOESY spectral analysis. The fact that the correct fold is obtained in cycle 1 of a de novo structure calculation is the single most important advance achieved with CANDID, when compared with previously proposed automated NOESY assignment methods that do not use network-anchoring and constraint-combination." citations,ref_5,6313,243825,4,,reference citation,,,9367762,,"Guntert P, Mumenthaler C, Wuthrich K. J Mol Biol. 1997 Oct 17;273(1):283-98.",Torsion angle dynamics for NMR structure calculation with the new program DYANA.,published,journal,J. Mol. Biol.,Journal of molecular biology,273,1,,0022-2836,,,,,,,,,,,,,,,,,,,,283,298,1997,"The new program DYANA (DYnamics Algorithm for Nmr Applications) for efficient calculation of three-dimensional protein and nucleic acid structures from distance constraints and torsion angle constraints collected by nuclear magnetic resonance (NMR) experiments performs simulated annealing by molecular dynamics in torsion angle space and uses a fast recursive algorithm to integrate the equations of motions. Torsion angle dynamics can be more efficient than molecular dynamics in Cartesian coordinate space because of the reduced number of degrees of freedom and the concomitant absence of high-frequency bond and angle vibrations, which allows for the use of longer time-steps and/or higher temperatures in the structure calculation. It also represents a significant advance over the variable target function method in torsion angle space with the REDAC strategy used by the predecessor program DIANA. DYANA computation times per accepted conformer in the ""bundle"" used to represent the NMR structure compare favorably with those of other presently available structure calculation algorithms, and are of the order of 160 seconds for a protein of 165 amino acid residues when using a DEC Alpha 8400 5/300 computer. Test calculations starting from conformers with random torsion angle values further showed that DYANA is capable of efficient calculation of high-quality protein structures with up to 400 amino acid residues, and of nucleic acid structures." citations,entry_citation,6314,243843,1,,entry citation,,,,,,"Letter to the Editor: NMR assignments of the cold-shock protein ribosome-binding factor A (RbfA) from Thermotoga maritima",published,journal,J. Biomol. NMR,,31,1,,,,,,,,,,,,,,,,,,,,,,73,74,2005, citations,entry_citation,6315,243868,1,,entry citation,,,15751947,,,"NMR structural study of TcUBP1, a single RRM domain protein from Trypanosoma cruzi: contribution of a beta hairpin to RNA binding",published,journal,Biochemistry,,44,10,,,,,,,,,,,,,,,,,,,,,,3708,3717,2005, citations,entry_citation,6317,243881,1,,entry citation,,,15359276,,,"Structure and DNA-binding properties of the cytolysin regulator CylR2 from Enterococcus faecalis",published,journal,EMBO J.,,23,18,,,,,,,,,,,,,,,,,,,,,,3632,3642,2004, citations,entry_citation,6318,243894,1,,entry citation,,,15987893,,,Solution structure of thioredoxin h1 from Arabidopsis thaliana,published,journal,Protein Sci.,,14,8,,,,,,,,,,,,,,,,,,,,,,2195,2200,2005, citations,ref_1,6318,243895,2,,reference citation,,,8520220,,"Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A. Abstract NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR. 1995 Nov;6(3):277-93.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,ref_2,6318,243896,3,,reference citation,,,,,"Bartels, C., Xia, T.-H., Billeter, M., Guntert, P. and Wuthrich, K. (1995) J. Biomol. NMR, 6, 1-10.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_3,6318,243897,4,,reference citation,,,,,"Bartels, C., Guntert, P., Billeter, M. and Wuthrich, K. (1997) J. Comp. Chem. 18, 139-149.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation,6336,244287,2,,reference citation,,,15596429,,,Structure and substrate-binding mechanism of human AP4A hydrolase,,journal,J. Biol. Chem.,,280,9,,,,,,,,,,,,,,,,,,,,,,8471,8481,2005, citations,entry_citation,6337,244305,1,,entry citation,,,,,,Solution structure of Ubiquitin like protein from Mus musculus,in preparation,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6338,244326,1,,entry citation,,,17128971,,,"Structure of Arabidopsis thaliana At1g77540 Protein, a Minimal Acetyltransferase from the COG2388 Family",published,journal,Biochemistry,,45,48,,,,,,,,,,,,,,,,,,,,,,14325,14336,2006, citations,entry_citation,6339,244346,1,,entry citation,,,,,,Solution structure of AT1g01470 from Arabidopsis Thaliana,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,LEA protein citations,entry_citation,6340,244367,1,,entry citation,,,,,,Solution structure of AT3g03773 from Arabidopsis Thaliana,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,p23 domain citations,ref_4,6318,243898,5,,reference citation,,,10212987,,"Cornilescu G, Delaglio F, Bax A. Abstract Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J Biomol NMR. 1999 Mar;13(3):289-302.",Protein backbone angle restraints from searching a database for chemical shift and sequence homology.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,13,3,,0925-2738,,,,,,,,,,,,,,,,,,,,289,302,1999,"Chemical shifts of backbone atoms in proteins are exquisitely sensitive to local conformation, and homologous proteins show quite similar patterns of secondary chemical shifts. The inverse of this relation is used to search a database for triplets of adjacent residues with secondary chemical shifts and sequence similarity which provide the best match to the query triplet of interest. The database contains 13C alpha, 13C beta, 13C', 1H alpha and 15N chemical shifts for 20 proteins for which a high resolution X-ray structure is available. The computer program TALOS was developed to search this database for strings of residues with chemical shift and residue type homology. The relative importance of the weighting factors attached to the secondary chemical shifts of the five types of resonances relative to that of sequence similarity was optimized empirically. TALOS yields the 10 triplets which have the closest similarity in secondary chemical shift and amino acid sequence to those of the query sequence. If the central residues in these 10 triplets exhibit similar phi and psi backbone angles, their averages can reliably be used as angular restraints for the protein whose structure is being studied. Tests carried out for proteins of known structure indicate that the root-mean-square difference (rmsd) between the output of TALOS and the X-ray derived backbone angles is about 15 degrees. Approximately 3% of the predictions made by TALOS are found to be in error." citations,ref_5,6318,243899,6,,reference citation,,,12051947,,"Herrmann T, Guntert P, Wuthrich K. Abstract Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J Mol Biol. 2002 May 24;319(1):209-27.",Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA.,published,journal,J. Mol. Biol.,Journal of molecular biology,319,1,,0022-2836,,,,,,,,,,,,,,,,,,,,209,227,2002,"Combined automated NOE assignment and structure determination module (CANDID) is a new software for efficient NMR structure determination of proteins by automated assignment of the NOESY spectra. CANDID uses an iterative approach with multiple cycles of NOE cross-peak assignment and protein structure calculation using the fast DYANA torsion angle dynamics algorithm, so that the result from each CANDID cycle consists of exhaustive, possibly ambiguous NOE cross-peak assignments in all available spectra and a three-dimensional protein structure represented by a bundle of conformers. The input for the first CANDID cycle consists of the amino acid sequence, the chemical shift list from the sequence-specific resonance assignment, and listings of the cross-peak positions and volumes in one or several two, three or four-dimensional NOESY spectra. The input for the second and subsequent CANDID cycles contains the three-dimensional protein structure from the previous cycle, in addition to the complete input used for the first cycle. CANDID includes two new elements that make it robust with respect to the presence of artifacts in the input data, i.e. network-anchoring and constraint-combination, which have a key role in de novo protein structure determinations for the successful generation of the correct polypeptide fold by the first CANDID cycle. Network-anchoring makes use of the fact that any network of correct NOE cross-peak assignments forms a self-consistent set; the initial, chemical shift-based assignments for each individual NOE cross-peak are therefore weighted by the extent to which they can be embedded into the network formed by all other NOE cross-peak assignments. Constraint-combination reduces the deleterious impact of artifact NOE upper distance constraints in the input for a protein structure calculation by combining the assignments for two or several peaks into a single upper limit distance constraint, which lowers the probability that the presence of an artifact peak will influence the outcome of the structure calculation. CANDID test calculations were performed with NMR data sets of four proteins for which high-quality structures had previously been solved by interactive protocols, and they yielded comparable results to these reference structure determinations with regard to both the residual constraint violations, and the precision and accuracy of the atomic coordinates. The CANDID approach has further been validated by de novo NMR structure determinations of four additional proteins. The experience gained in these calculations shows that once nearly complete sequence-specific resonance assignments are available, the automated CANDID approach results in greatly enhanced efficiency of the NOESY spectral analysis. The fact that the correct fold is obtained in cycle 1 of a de novo structure calculation is the single most important advance achieved with CANDID, when compared with previously proposed automated NOESY assignment methods that do not use network-anchoring and constraint-combination." citations,ref_6,6318,243900,7,,reference citation,,,12565051,,"Schwieters CD, Kuszewski JJ, Tjandra N, Marius Clore G. Abstract The Xplor-NIH NMR molecular structure determination package. J Magn Reson. 2003 Jan;160(1):65-73.",The Xplor-NIH NMR molecular structure determination package.,published,journal,J. Magn. Reson.,"Journal of magnetic resonance (San Diego, Calif. : 1997)",160,1,,1090-7807,,,,,,,,,,,,,,,,,,,,65,73,2003,"We announce the availability of the Xplor-NIH software package for NMR biomolecular structure determination. This package consists of the pre-existing XPLOR program, along with many NMR-specific extensions developed at the NIH. In addition to many features which have been developed over the last 20 years, the Xplor-NIH package contains an interface with a new programmatic framework written in C++. This interface currently supports the general purpose scripting languages Python and TCL, enabling rapid development of new tools, such as new potential energy terms and new optimization methods. Support for these scripting languages also facilitates interaction with existing external programs for structure analysis, structure manipulation, visualization, and spectral analysis." citations,entry_citation,6319,243932,1,,entry citation,,,,,,"Letter to the Editor: NMR assignments of the DNA-bound human Csx/Nkx2.5 homeodomain and NK2-specific domain",published,journal,J. Biomol. NMR,,31,1,,,,,,,,,,,,,,,,,,,,,,75,76,2005, citations,entry_citation,6320,243947,1,,entry citation,,,15543154,,,"U2-U6 RNA folding reveals a group II intron-like domain and a four-helix junction",published,journal,Nat. Struct. Mol. Biol.,,11,12,,,,,,,,,,,,,,,,,,,,,,1237,1242,2004, citations,entry_citation,6321,243972,1,,entry citation,,,16004868,,,"The solution structure of a transient photoreceptor intermediate: delta25 photoactive yellow protein.",published,journal,"Structure (Cambridge, MA, U. S.)",,13,7,,,,,,,,,,,,,,,,,,,,,,953,962,2005, citations,entry_citation,6322,243986,1,,entry citation,,,16004868,,,"The solution structure of a transient photoreceptor intermediate: delta25 photoactive yellow protein.",published,journal,"Structure (Cambridge, MA, U. S.)",,13,7,,,,,,,,,,,,,,,,,,,,,,953,962,2005, citations,entry_citation,6324,244012,1,,entry citation,,,15608123,,,"A novel member of the YchN-like fold: solution structure of the hypothetical protein Tm0979 from Thermotoga maritima",published,journal,Protein Sci.,,14,1,,,,,,,,,,,,,,,,,,,,,,216,223,2005, citations,entry_citation,6325,244038,1,,entry citation,,,15698569,,,"Assessment of the robustness of a serendipitous zinc-binding fold: mutagenesis and protein grafting",published,journal,Structure,,13,2,,,,,,,,,,,,,,,,,,,,,,257,266,2005, citations,entry_citation,6326,244061,1,,entry citation,,,15698569,,,"Assessment of the robustness of a serendipitous zinc-binding fold: mutagenesis and protein grafting",published,journal,Structure,,13,2,,,,,,,,,,,,,,,,,,,,,,257,266,2005, citations,entry_citation,6327,244083,1,,entry citation,,,15698569,,,"Assessment of the robustness of a serendipitous zinc-binding fold: mutagenesis and protein grafting",published,journal,Structure,,13,2,,,,,,,,,,,,,,,,,,,,,,257,266,2005, citations,entry_citation,6328,244105,1,,entry citation,,,15698569,,,"Assessment of the robustness of a serendipitous zinc-binding fold: mutagenesis and protein grafting",published,journal,Structure,,13,2,,,,,,,,,,,,,,,,,,,,,,257,266,2005, citations,entry_citation,6329,244128,1,,entry citation,,,15698569,,,"Assessment of the robustness of a serendipitous zinc-binding fold: mutagenesis and protein grafting",published,journal,Structure,,13,2,,,,,,,,,,,,,,,,,,,,,,257,266,2005, citations,entry_citation,6330,244152,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C, and 15N resonance assignments of the 17 kDa Ap4A hydrolase from Homo sapiens in the presence and absence of ATP",published,journal,J. Biomol. NMR,,31,2,,,,,,,,,,,,,,,,,,,,,,181,182,2005, citations,citation,6330,244153,2,,reference citation,,,15596429,,,Structure and substrate-binding mechanism of human AP4A hydrolase,,journal,J. Biol. Chem.,,280,9,,,,,,,,,,,,,,,,,,,,,,8471,8481,2005, citations,entry_citation,6331,244169,1,,entry citation,,,,,,"Letter to the Editor: NMR assignment of the SH2 domain from the human feline sarcoma oncogene FES",published,journal,J. Biomol. NMR,,30,4,,,,,,,,,,,,,,,,,,,,,,463,464,2004, citations,entry_citation,6332,244198,1,,entry citation,,,,,,"Letter to the Editor: Assignment of the 1H, 13C and 15N resonances of Mlc1p from Saccharomyces cerevisiae",published,journal,J. Biomol. NMR,,31,4,,,,,,,,,,,,,,,,,,,,,,367,368,2005, citations,entry_citation,6333,244224,1,,entry citation,,,,,,"Resonance assignment of ABA-1A, from Ascaris suum nematode polyprotein allergen",published,journal,J. Biomol. NMR,,32,2,,,,,,,,,,,,,,,,,,,,,,176,176,2005, citations,entry_citation,6334,244246,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C, 15N backbone and sidechain resonance assignment of Mip(77-213) the PPIase domain of the Legionella pneumophila Mip protein",published,journal,J. Biomol. NMR,,31,1,,,,,,,,,,,,,,,,,,,,,,77,78,2005, citations,entry_citation,6335,244270,1,,entry citation,,,15328602,,,The zinc-dependent redox switch domain of the chaperone Hsp33 has a novel fold,published,journal,J. Mol. Biol.,,341,4,,,,,,,,,,,,,,,,,,,,,,893,899,2004, citations,entry_citation,6341,244388,1,,entry citation,,,,,,"Solution structure of At3g04780.1, an Arabidopsis ortholog of the C-terminal domain of human thioredoxin-like protein",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6342,244410,1,,entry citation,,,15628841,,,Solution structure of human survivin and its binding interface with Smac/Diablo,published,journal,Biochemistry,,44,1,,,,,,,,,,,,,,,,,,,,,,11,17,2005, citations,entry_citation,6343,244432,1,,entry citation,,,,,,Chemical shift assignments of PA1324 (21-170),published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6344,244450,1,,entry citation,,,,,,"Solution NMR Structure of Human protein HSPCO34. Northeast Structural Genomics Target HR1958.",published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,2004, citations,entry_citation,6345,244469,1,,entry citation,,,16202234,,,"Solution Structure of YKR049C, a Putative Redox Protein from Saccharomyces cerevisiae.",published,journal,J. Biochem. Mol. Biol.,,38,5,,,,,,,,,,,,,,,,,,,,,,550,554,2005, citations,entry_citation,6346,244494,1,,entry citation,,,15929008,,,"Letter to the Editor: 1H, 15N and 13C Resonance assignments and secondary structure determination reveal that the minimal Rac1 GTPase binding domain of plexin-B1 has a ubiquitin fold",published,journal,J. Biomol. NMR,,31,4,,,,,,,,,,,,,,,,,,,,,,369,370,2005, citations,ref_1,6346,244495,2,,reference citation,,,11035813,,"Vikis HG, Li W, He Z, Guan KL. Proc Natl Acad Sci U S A. 2000 Nov 7;97(23):12457-62.",The semaphorin receptor plexin-B1 specifically interacts with active Rac in a ligand-dependent manner.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,97,23,,0027-8424,,,,,,,,,,,,,,,,,,,,12457,12462,2000,"Semaphorin molecules serve as axon guidance signals that regulate the navigation of neuronal growth cones. Semaphorins have also been implicated in other biological processes, including the immune response. Plexins, acting either alone or in complex with neuropilins, have recently been identified as functional semaphorin receptors. However, the mechanisms of signal transduction by plexins remain largely unknown. We have demonstrated a direct interaction between plexin-B1 and activated Rac. Rac specifically interacts with the cytosolic domain of plexin-B1, but not with that of plexin-A3 or -C1. Neither RhoA nor Cdc42 interacts with plexin-B1, indicating that the Rac/plexin-B1 interaction is highly specific. The binding of GTP and the integrity of the Rac effector domain are required for the interaction with plexin-B1. Furthermore, we have identified that a Cdc42/Rac interactive binding (CRIB) motif in the cytosolic domain of plexin-B1 is essential for its interaction with active Rac. We have also observed that the semaphorin CD100, a ligand for plexin-B1, stimulates the interaction between plexin-B1 and active Rac. Our results support a model by which activated Rac plays a role in mediating semaphorin signals, resulting in reorganization of actin cytoskeletal structure." citations,entry_citation,6347,244526,1,,entry citation,,,15498765,,,"Evidence for domain-specific recognition of SK and Kv channels by MTX and HsTx1 scorpion toxins",published,journal,J. Biol. Chem.,,279,53,,,,,,,,,,,,,,,,,,,,,,55690,55696,2004, citations,entry_citation,6348,244543,1,,entry citation,,,15754054,,,"Residual backbone and side-chain 13C and 15N resonance assignments of the intrinsic transmembrane light-harvesting 2 protein complex by solid state Magic Angle Spinning NMR spectroscopy",published,journal,J. Biomol. NMR,,31,4,,,,,,,,,,,,,,,,,,,,,,279,293,2005, citations,entry_citation,6349,244562,1,,entry citation,,,15740753,,,"Solution Structures of the Core Light-harvesting alpha and beta Polypeptides from Rhodospirillum rubrum: Implications for the Pigment-Protein and Protein-Protein Interactions",published,journal,J. Mol. Biol.,,347,2,,,,,,,,,,,,,,,,,,,,,,465,477,2005, citations,entry_citation,6350,244584,1,,entry citation,,,15740753,,,"Solution Structures of the Core Light-harvesting alpha and beta Polypeptides from Rhodospirillum rubrum: Implications for the Pigment-Protein and Protein-Protein Interactions",published,journal,J. Mol. Biol.,,347,2,,,,,,,,,,,,,,,,,,,,,,465,477,2005, citations,entry_citation,6351,244606,1,,entry citation,,,,,,A concept for rapid protein structure determination using Solid-state NMR,published,journal,"Angew. Chem., Int. Ed.",,44,14,,,,,,,,,,,,,,,,,,,,,,2089,2092,2005, citations,entry_citation,6352,244620,1,,entry citation,,,15792796,,,"Isolation and structural characterization of epilancin 15X, a novel lantibiotic from a clinical strain of Staphylococcus epidermidis",published,journal,FEBS Lett.,,579,9,,,,,,,,,,,,,,,,,,,,,,1917,1922,2005, citations,ref_1,6352,244621,2,,reference citation,,,12056898,,"Hsu ST, Breukink E, de Kruijff B, Kaptein R, Bonvin AM, van Nuland NA. Mapping the targeted membrane pore formation mechanism by solution NMR: the nisin Z and lipid II interaction in SDS micelles. Biochemistry. 2002 Jun 18;41(24):7670-6.",Mapping the targeted membrane pore formation mechanism by solution NMR: the nisin Z and lipid II interaction in SDS micelles.,published,journal,Biochemistry,Biochemistry,41,24,,0006-2960,,,,,,,,,,,,,,,,,,,,7670,7676,2002,"Nisin is an example of type-A lantibiotics that contain cyclic lanthionine rings and unusual dehydrated amino acids. Among the numerous pore-forming antimicrobial peptides, type-A lantibiotics form an unique family of post-translationally modified peptides. Via the recognition of cell wall precursor lipid II, nisin has the capacity to form pores against Gram-positive bacteria with an extremely high activity in the nanomolar (nM) range. Here we report a high-resolution NMR spectroscopy study of nisin/lipid II interactions in SDS micelles as a model membrane system in order to elucidate the mechanism of molecular recognition at residue level. The binding to lipid II was studied through (15)N-(1)H HSQC titration, backbone amide proton temperature coefficient analysis, and heteronuclear (15)N[(1)H]-NOE relaxation dynamics experiments. Upon the addition of lipid II, significant changes were monitored in the N-terminal part of nisin. An extremely low amide proton temperature coefficient (Delta delta/Delta T) was found for the amide proton of Ala3 (> -0.1 ppb/K) in the complex form. This suggests tight hydrogen bonding and/or isolation from the bulk solvent for this residue. Large chemical shift perturbations were also observed in the first two rings. In contrast, the C-terminal part of nisin was almost unaffected. This part of the molecule remains flexible and solvent-exposed. On the basis of our results, a multistep pore-forming mechanism is proposed. The N-terminal part of nisin first binds to lipid II, and a subsequent structural rearrangement takes place. The C-terminal part of nisin is possibly responsible for the activation of the pore formation. In light of the emerging antibiotic resistance problems, an understanding of the specific recognition mechanism of nisin with lipid II at the residue specific level may therefore aid in the development of novel antibiotics." citations,ref_2,6352,244622,3,,reference citation,,,12562773,,"Hsu ST, Breukink E, Bierbaum G, Sahl HG, de Kruijff B, Kaptein R, van Nuland NA, Bonvin AM. Free Full Text NMR study of mersacidin and lipid II interaction in dodecylphosphocholine micelles. Conformational changes are a key to antimicrobial activity. J Biol Chem. 2003 Apr 11;278(15):13110-7. Epub 2003 Jan 31.",NMR study of mersacidin and lipid II interaction in dodecylphosphocholine micelles. Conformational changes are a key to antimicrobial activity.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,278,15,,0021-9258,,,,,,,,,,,,,,,,,,,,13110,13117,2003,"Mersacidin belongs to the type B lantibiotics (lanthionine-containing antibiotics) that contain post-translationally modified amino acids and cyclic ring structures. It targets the cell wall precursor lipid II and thereby inhibits cell wall synthesis. In light of the emerging antibiotics resistance problem, the understanding of the antibacterial activity on a structural basis provides a key to circumvent this issue. Here we present solution NMR studies of mersacidin-lipid II interaction in dodecylphosphocholine (DPC) micelles. Distinct solution structures of mersacidin were determined in three different states: in water/methanol solution and in DPC micelles with and without lipid II. The structures in various sample conditions reveal remarkable conformational changes in which the junction between Ala-12 and Abu-13 (where Abu is aminobutyric acid) effectively serves as the hinge for the opening and closure of the ring structures. The DPC micelle-bound form resembles the previously determined NMR and x-ray crystal structures of mersacidin in pure methanol but substantially deviates from the other two states in our current report. The structural changes delineate the large chemical shift perturbations observed during the course of a two-step (15)N-(1)H heteronuclear single quantum coherence titration. They also modulate the surface charge distribution of mersacidin suggesting that electrostatics play a central role in the mersacidin-lipid II interaction. The observed conformational adaptability of mersacidin might be a general feature of lipid II-interacting antibiotics/peptides." citations,citation_1,6376,245173,1,,entry citation,,,,,,"Letter to the Editor: Complete resonance assignments of the C-terminal domain from MIC1: A micronemal protein from Toxoplasma gondii",published,journal,J. Biomol. NMR,,31,2,,,,,,,,,,,,,,,,,,,,,,177,178,2005, citations,entry_citation,6377,245189,1,,entry citation,,,15647367,,,"Prion protein NMR structures of cats, dogs, pigs, and sheep",published,journal,Proc. Natl. Acad. Sci. U.S.A.,,102,3,,,,,,,,,,,,,,,,,,,,,,640,645,2005, citations,entry_citation,6378,245204,1,,entry citation,,,15647367,,,"Prion protein NMR structures of cats, dogs, pigs, and sheep",published,journal,Proc. Natl. Acad. Sci. U.S.A.,,102,3,,,,,,,,,,,,,,,,,,,,,,640,645,2005, citations,ref_3,6352,244623,4,,reference citation,,,15361862,,"Hsu ST, Breukink E, Tischenko E, Lutters MA, De Kruijff B, Kaptein R, Bonvin AM, Van Nuland NA. The nisin-lipid II complex reveals a pyrophosphate cage that provides a blueprint for novel antibiotics. Nat Struct Mol Biol. 2004 Oct;11(10):963-7. Epub 2004 Sep 12.",The nisin-lipid II complex reveals a pyrophosphate cage that provides a blueprint for novel antibiotics.,published,journal,Nat. Struct. Mol. Biol.,Nature structural & molecular biology,11,10,,1545-9993,,,,,,,,,,,,,,,,,,,,963,967,2004,"The emerging antibiotics-resistance problem has underlined the urgent need for novel antimicrobial agents. Lantibiotics (lanthionine-containing antibiotics) are promising candidates to alleviate this problem. Nisin, a member of this family, has a unique pore-forming activity against bacteria. It binds to lipid II, the essential precursor of cell wall synthesis. As a result, the membrane permeabilization activity of nisin is increased by three orders of magnitude. Here we report the solution structure of the complex of nisin and lipid II. The structure shows a novel lipid II-binding motif in which the pyrophosphate moiety of lipid II is primarily coordinated by the N-terminal backbone amides of nisin via intermolecular hydrogen bonds. This cage structure provides a rationale for the conservation of the lanthionine rings among several lipid II-binding lantibiotics. The structure of the pyrophosphate cage offers a template for structure-based design of novel antibiotics." citations,entry_citation,6353,244645,1,,entry citation,,,,,,"Letter to the Editor: 1H, 15N and 13C resonance assignments of the BRCT Region of the large subunit of human Replication Factor C",published,journal,J. Biomol. NMR,,31,2,,,,,,,,,,,,,,,,,,,,,,183,184,2005, citations,entry_citation,6354,244660,1,,entry citation,,,17762867,,,Solution structure of NECAP1 protein,published,journal,EMBO J.,,26,18,,,,,,,,,,,,,,,,,,,,,,4066,4077,2007, citations,entry_citation,6355,244678,1,,entry citation,,,,,,"Solution Structure Of The Staphylococcus Epidermis Protein SE0936. Northest Strucutral Genomics Consortium Target SeR8.",submitted,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6356,244707,1,,entry citation,,,15610019,,,"Yeast frataxin solution structure, iron binding and ferrochelatase interaction",published,journal,Biochemistry,,43,51,,,,,,,,,,,,,,,,,,,,,,16254,16262,2004, citations,entry_citation,6357,244736,1,,entry citation,,,,,,Backbone Resonance Assignments of Wild-Type TEM-1 Beta-lactamase from E. coli,published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,2004, citations,ref1,6357,244737,2,,reference citation,,,15213455,,"1H, 13C and 15N backbone resonance assignments for TEM-1, a 28.9 kDa beta-lactamase from E. coli. J Biomol NMR. 2004 Jul;29(3):433-4.","1H, 13C and 15N backbone resonance assignments for TEM-1, a 28.9 kDa beta-lactamase from E. coli.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,29,3,,0925-2738,,,,,,,,,,,,,,,,,,,,433,434,2004, citations,entry_citation,6358,244762,1,,entry citation,,,,,,"Letter to the Editor: NMR structure note - Solution structure of a bacterial BolA-like protein XC975 from a plant pathogen Xanthomonas Campestris pv. campestris",published,journal,J. Biomol. NMR,,31,2,,,,,,,,,,,,,,,,,,,,,,167,172,2005, citations,entry_citation,6359,244798,1,,entry citation,,,16329120,,,"Solution structure of YggX: A prokaryotic protein involved in Fe(II) trafficking.",published,journal,Proteins,,62,3,,,,,,,,,,,,,,,,,,,,,,578,586,2005, citations,entry_citation,6360,244812,1,,entry citation,,,15850378,,,"The micelle-bound structure of an antimicrobial peptide derived from the alpha-chain of bovine hemoglobin isolated from the tick Boophilus microplus.",published,journal,Biochemistry,,44,17,,,,,,,,,,,,,,,,,,,,,,6440,6451,2005, citations,entry_citation,6361,244834,1,,entry citation,,,,,,"Letter to the Editor: NMR resonance assignments for the DNA-supercoiling domain of the human protein DEK",published,journal,J. Biomol. NMR,,31,1,,,,,,,,,,,,,,,,,,,,,,65,65,2005, citations,entry_citation,6362,244857,1,,entry citation,,,15522305,,,"Solution NMR structure of the iron-sulfur cluster assembly protein U (IscU) with zinc bound at the active site",published,journal,J. Mol. Biol.,,344,2,,,,,,,,,,,,,,,,,,,,,,567,583,2004, citations,entry_citation,6363,244889,1,,entry citation,,,16027363,,,NMR data collection and analysis protocol for high-throughput protein structure determination,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,102,30,,,,,,,,,,,,,,,,,,,,,,10487,10492,2005, citations,entry_citation,6364,244905,1,,entry citation,,,16027363,,,NMR data collection and analysis protocol for high-throughput protein structure determination,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,102,30,,,,,,,,,,,,,,,,,,,,,,10487,10492,2005, citations,entry_citation,6365,244924,1,,entry citation,,,16027363,,,NMR data collection and analysis protocol for high-throughput protein structure determination,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,102,30,,,,,,,,,,,,,,,,,,,,,,10487,10492,2005, citations,entry_citation,6366,244938,1,,entry citation,,,16281282,,,"NMR structure of protein yqbG from Bacillus subtilis reveals a novel alpha-helical protein fold",published,journal,Proteins,,62,1,,,,,,,,,,,,,,,,,,,,,,288,291,2006, citations,entry_citation,6367,244960,1,,entry citation,,,16027363,,,NMR data collection and analysis protocol for high-throughput protein structure determination,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,102,30,,,,,,,,,,,,,,,,,,,,,,10487,10492,2005, citations,entry_citation,6368,244982,1,,entry citation,,,16027363,,,NMR data collection and analysis protocol for high-throughput protein structure determination,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,102,30,,,,,,,,,,,,,,,,,,,,,,10487,10492,2005, citations,entry_citation,6369,245001,1,,entry citation,,,16027363,,,NMR data collection and analysis protocol for high-throughput protein structure determination,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,102,30,,,,,,,,,,,,,,,,,,,,,,10487,10492,2005, citations,entry_citation,6370,245019,1,,entry citation,,,15726634,,,"Solution structure of APETx1 from the sea anemone Anthopleura elegantissima: a new fold for an HERG toxin.",published,journal,Proteins,,59,2,,,,,,,,,,,,,,,,,,,,,,380,386,2005, citations,entry_citation,6371,245035,1,,entry citation,,,,,,"Letters to the Editor: 1H, 13C, and 15N resonance assignments of SAP18",published,journal,J. Biomol. NMR,,31,3,,,,,,,,,,,,,,,,,,,,,,259,259,2005, citations,entry_citation,6372,245063,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N resonance assignments of the N-terminal Domain of the SARS CoV Nucleocapsid Protein",published,journal,J. Biomol. NMR,,31,1,,,,,,,,,,,,,,,,,,,,,,79,80,2005, citations,entry_citation,6373,245093,1,,entry citation,,,15929009,,,"Letter to the Editor: Backbone chemical shift assignments of the LexA catalytic domain in its active conformation.",published,journal,J. Biomol. NMR,,31,4,,,,,,,,,,,,,,,,,,,,,,371,372,2005, citations,entry_citation,6374,245113,1,,entry citation,,,15649886,,,"NMR structure of the first PHD finger of autoimmune regulator protein (AIRE1). Insights into autoimmune polyendocrinopathy-candidiasis-ectodermal dystrophy (APECED) disease",published,journal,J. Biol. Chem.,,280,12,,,,,,,,,,,,,,,,,,,,,,11505,11512,2005, citations,entry_citation,6375,245138,1,,entry citation,,,15644214,,,"The solution structure of the C-terminal domain of TonB and interation studies with TonB box peptides.",published,journal,J. Mol. Biol.,,345,5,,,,,,,,,,,,,,,,,,,,,,1185,1197,2005, citations,citation,6469,247127,1,,entry citation,,,,,,Solution Structure of the HMG-box domain in the SSRP1 subunit of FACT,published,journal,J. Biomol. NMR,,32,1,,,,,,,,,,,,,,,,,,,,,,83,88,2005, citations,entry_citation,6379,245217,1,,entry citation,,,15929010,,,"Letter to the Editor: Backbone and side chain 1H, 13C and 15N assignments for Escherichia coli SdiA1-171, the autoinducer-binding domain of a quorum sensing protein",published,journal,J. Biomol. NMR,,31,4,,,,,,,,,,,,,,,,,,,,,,373,374,2005, citations,entry_citation,6380,245240,1,,entry citation,,,15647367,,,"Prion protein NMR structures of cats, dogs, pigs, and sheep",published,journal,Proc. Natl. Acad. Sci. U.S.A.,,102,3,,,,,,,,,,,,,,,,,,,,,,640,645,2005, citations,entry_citation,6381,245253,1,,entry citation,,,15647367,,,"Prion protein NMR structures of cats, dogs, pigs, and sheep",published,journal,Proc. Natl. Acad. Sci. U.S.A.,,102,3,,,,,,,,,,,,,,,,,,,,,,640,645,2005, citations,citation,6382,245266,1,,entry citation,,,,,,NMR assignment of the Xenopus leavis prion protein fragment xlPrP(98-226),published,journal,J. Biomol. NMR,,31,3,,,,,,,,,,,,,,,,,,,,,,260,260,2005, citations,entry_citation,6383,245280,1,,entry citation,,,,,,Prion protein NMR structures of the elk and of mouse/elk hybrids,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,102,3,,,,,,,,,,,,,,,,,,,,,,646,650,2005, citations,entry_citation,6384,245293,1,,entry citation,,,15542592,,,"Structures of APRIL-receptor complexes: like BCMA, TACI employs only a single cysteine-rich domain for high-affinity ligand binding",published,journal,J. Biol. Chem.,,280,8,,,,,,,,,,,,,,,,,,,,,,7218,7227,2005, citations,entry_citation,6385,245312,1,,entry citation,,,15573383,,,"Structure and dynamics of the human pleckstrin DEP domain: distinct molecular features of a novel DEP domain subfamily.",published,journal,Proteins,,58,2,,,,,,,,,,,,,,,,,,,,,,354,366,2005, citations,entry_citation,6386,245341,1,,entry citation,,,16008348,,,"Structural and Functional Study of an Anemonia Elastase Inhibitor, a ""Nonclassical"" Kazal-Type Inhibitor from Anemonia sulcata.",published,journal,Biochemistry,,44,28,,,,,,,,,,,,,,,,,,,,,,9626,9636,2005, citations,entry_citation,6387,245358,1,,entry citation,,,16008348,,,"Structural and Functional Study of an Anemonia Elastase Inhibitor, a ""Nonclassical"" Kazal-Type Inhibitor from Anemonia sulcata.",published,journal,Biochemistry,,44,28,,,,,,,,,,,,,,,,,,,,,,9626,9636,2005, citations,entry_citation,6388,245375,1,,entry citation,,,15699044,,,"Solution structure of synthetic penaeidin-4 with structural and functional comparisons to penaeidin-3",published,journal,J. Biol. Chem.,,280,16,,,,,,,,,,,,,,,,,,,,,,16009,16018,2005, citations,entry_citation,6389,245395,1,,entry citation,,,15971207,,,"Increasing the Molecular Contacts between Maurotoxin and Kv1.2 Channel Augments Ligand Affinity",published,journal,Proteins,,60,3,,,,,,,,,,,,,,,,,,,,,,401,411,2005, citations,entry_citation,6390,245409,1,,entry citation,,,,,,"NMR assignment of the R-module from the Azotobacter vinelandii mannuronan C5-epimerase AlgE4",published,journal,J. Biomol. NMR,,31,3,,,,,,,,,,,,,,,,,,,,,,259,259,2005, citations,entry_citation,6391,245426,1,,entry citation,,,,,,"1H, 13C, and 15N assignments of MMP-12, a key protease implicated in lung tissue remodeling",published,journal,J. Biomol. NMR,,31,3,,,,,,,,,,,,,,,,,,,,,,260,260,2005, citations,entry_citation,6392,245458,1,,entry citation,,,15718240,,,"Towards a Structure for a TSG-6{middle dot}Hyaluronan Complex by Modeling and NMR Spectroscopy: INSIGHTS INTO OTHER MEMBERS OF THE LINK MODULE SUPERFAMILY.",published,journal,J. Biol. Chem.,,280,18,,,,,,,,,,,,,,,,,,,,,,18189,18201,2005, citations,entry_citation,6393,245480,1,,entry citation,,,15718240,,,"Towards a structure for a hyaluronan-TSG-6 complex by modeling and NMR spectroscopy: Insights into other members of the link module superfamily",published,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,Citation_1,6395,245503,1,,entry citation,,,15803402,,,"Letter to the Editor: Backbone and side-chain 1H, 15N, and 13C assignments for the beta domain of the bacterial cell division protein DivIB",published,journal,J. Biomol. NMR,,31,3,,,,,,,,,,,,,,,,,,,,,,261,262,2005, citations,entry_citation,6396,245535,1,,entry citation,,,16289575,,,"Solution structure of isoform 1 of Roadblock/LC7, a light chain in the dynein complex",published,journal,J. Mol. Biol.,,354,5,,,,,,,,,,,,,,,,,,,,,,1043,1051,2005, citations,entry_citation,6398,245550,1,,entry citation,,,16287076,,,"Structure, conformational stability, and enzymatic properties of acylphosphatase from the hyperthermophile Sulfolobus solfataricus",published,journal,Proteins,,62,1,,,,,,,,,,,,,,,,,,,,,,64,79,2006, citations,citation_1,6399,245572,1,,entry citation,,,,,,"1H, 13C and 15N resonance assignments of the backbone and methyl groups of the 24 kDa tetratricopeptide repeat domain in p67phox",published,journal,J. Biomol. NMR,,32,2,,,,,,,,,,,,,,,,,,,,,,176,176,2005, citations,entry_citation,64,245600,1,,entry citation,,,,,"Koyama, Satoshi, Kobayashi, Yuji, Norioka, Shigemi, Kyogoku, Yoshimasa, Ikenaka, Tokuji, ""Conformational Studies by 1H Nuclear Magnetic Resonance of the Trypsin-Chymotrypsin Inhibitor B-III from Peanuts and Its Enzymatically Modified Derivative,"" Biochemistry 25, 8076-8082 (1986).","Conformational Studies by 1H Nuclear Magnetic Resonance of the Trypsin-Chymotrypsin Inhibitor B-III from Peanuts and Its Enzymatically Modified Derivative",published,journal,Biochemistry,,25,,,,,,,,,,,,,,,,,,,,,,,8076,8082,1986, citations,entry_citation,6400,245613,1,,entry citation,,,,,,"Letter to the Editor: Assignment of 1H, 13C, and 15N resonances of WT matrix protein and its R55F mutant from Mason-Pfizer monkey virus",published,journal,J. Biomol. NMR,,31,4,,,,,,,,,,,,,,,,,,,,,,381,382,2005, citations,entry_citation,6401,245638,1,,entry citation,,,,,,"Letter to the Editor: Assignment of 1H, 13C, and 15N resonances of WT matrix protein and its R55F mutant from Mason-Pfizer monkey virus",published,journal,J. Biomol. NMR,,31,4,,,,,,,,,,,,,,,,,,,,,,381,382,2005, citations,entry_citation,6402,245664,1,,entry citation,,,15866937,,,"Solution structure of the carbon storage regulator protein CsrA from Escherichia coli",published,journal,J. Bacteriol.,,187,10,,,,,,,,,,,,,,,,,,,,,,3496,3501,2005, citations,entry_citation,6403,245677,1,,entry citation,,,,,,"Prion protein NMR structures of cat, dog, pig, and sheep",in press,journal,Proc. Natl. Acad. Sci. U.S.A.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6404,245692,1,,entry citation,,,,,,Backbone assignment of PCF11 CTD binding domain,published,journal,J. Biomol. NMR,,31,4,,,,,,,,,,,,,,,,,,,,,,363,363,2005, citations,entry_citation,6405,245712,1,,entry citation,,,15929006,,,"Letter to the Editor: 1H, 13C and 15N resonance assignments of the first cadherin domain of Cadherin-related neuronal receptor (CNR)/protocadherin alpha.",published,journal,J. Biomol. NMR,,31,4,,,,,,,,,,,,,,,,,,,,,,365,366,2005, citations,entry_citation,6406,245728,1,,entry citation,,,,,,"Letter to the Editor: Backbone and side chain resonance assignments of a TRAV14-3 mouse T cell receptor domain",published,journal,J. Biomol. NMR,,31,3,,,,,,,,,,,,,,,,,,,,,,271,272,2005, citations,entry_citation,6407,245766,1,,entry citation,,,,,,"1H and 15N resonance assignment, secondary structure and dynamic behaviour of the C-terminal domain of human papillomavirus Oncoprotein E6",published,journal,J. Biomol. NMR,,31,2,,,,,,,,,,,,,,,,,,,,,,129,141,2005, citations,entry_citation,6408,245786,1,,entry citation,,,16055450,,,"The six zinc fingers of metal-responsive element binding transcription factor-1 form stable and quasi-ordered structures with relatively small differences in zinc affinities.",published,journal,J. Biol. Chem.,,280,31,,,,,,,,,,,,,,,,,,,,,,28529,28540,2005, citations,reference_1,6408,245787,2,,reference citation,,,8467794,,"Radtke, F., Heuchel, R., Georgiev, O., Hergersberg, M., Gariglio, M., Dembic, Z., and Schaffner, W. (1993). Cloned transcription factor MTF-1 activates the mouse metallothionein I promoter. EMBO J., 12, 1355-1362.",Cloned transcription factor MTF-1 activates the mouse metallothionein I promoter.,published,journal,EMBO J.,The EMBO journal,12,4,,0261-4189,,,,,,,,,,,,,,,,,,,,1355,1362,1993,"Metallothioneins (MTs) are small cysteine-rich proteins whose structure is conserved from fungi to man. MTs strongly bind heavy metals, notably zinc, copper and cadmium. Upon exposure of cells to heavy metal and other adverse treatments, MT gene transcription is strongly enhanced. Metal induction is mediated by several copies of a 15 bp consensus sequence (metal-responsive element, MRE) present in the promoter region of MT genes. We and others have demonstrated the presence of an MRE-binding factor in HeLa cell nuclear extracts. We found that this factor, termed MTF-1 (MRE-binding transcription factor) is inactivated/reactivated in vitro by zinc withdrawal/addition. Here we report that the amounts of MTF-1-DNA complexes are elevated several-fold in zinc-treated cells, as measured by bandshift assay. We have also cloned the cDNA of mouse MTF-1, a 72.5 kDa protein. MTF-1 contains six zinc fingers and separate transcriptional activation domains with high contents of acidic and proline residues. Ectopic expression of MTF-1 in primate or rodent cells strongly enhances transcription of a reporter gene that is driven by four consensus MREd sites, or by the complete mouse MT-I promoter, even at normal zinc levels." citations,entry_citation,6409,245809,1,,entry citation,,,16055450,,,"The six zinc fingers of metal-responsive element binding transcription factor-1 form stable and quasi-ordered structures with relatively small differences in zinc affinities.",published,journal,J. Biol. Chem.,,280,31,,,,,,,,,,,,,,,,,,,,,,28529,28540,2005, citations,reference_1,6409,245810,2,,reference citation,,,8467794,,"Radtke, F., Heuchel, R., Georgiev, O., Hergersberg, M., Gariglio, M., Dembic, Z., and Schaffner, W. (1993). Cloned transcription factor MTF-1 activates the mouse metallothionein I promoter. EMBO J., 12, 1355-1362.",Cloned transcription factor MTF-1 activates the mouse metallothionein I promoter.,published,journal,EMBO J.,The EMBO journal,12,4,,0261-4189,,,,,,,,,,,,,,,,,,,,1355,1362,1993,"Metallothioneins (MTs) are small cysteine-rich proteins whose structure is conserved from fungi to man. MTs strongly bind heavy metals, notably zinc, copper and cadmium. Upon exposure of cells to heavy metal and other adverse treatments, MT gene transcription is strongly enhanced. Metal induction is mediated by several copies of a 15 bp consensus sequence (metal-responsive element, MRE) present in the promoter region of MT genes. We and others have demonstrated the presence of an MRE-binding factor in HeLa cell nuclear extracts. We found that this factor, termed MTF-1 (MRE-binding transcription factor) is inactivated/reactivated in vitro by zinc withdrawal/addition. Here we report that the amounts of MTF-1-DNA complexes are elevated several-fold in zinc-treated cells, as measured by bandshift assay. We have also cloned the cDNA of mouse MTF-1, a 72.5 kDa protein. MTF-1 contains six zinc fingers and separate transcriptional activation domains with high contents of acidic and proline residues. Ectopic expression of MTF-1 in primate or rodent cells strongly enhances transcription of a reporter gene that is driven by four consensus MREd sites, or by the complete mouse MT-I promoter, even at normal zinc levels." citations,entry_citation,6410,245832,1,,entry citation,,,,,,"Letter to the Editor: 1H, 15N, and 13C resonance assignments of reduced glutaredoxin C1 from Populus tremula x tremuloides",published,journal,J. Biomol. NMR,,31,3,,,,,,,,,,,,,,,,,,,,,,263,264,2005, citations,entry_citation,6411,245868,1,,entry citation,,,15850378,,,"The micelle-bound structure of an antimicrobial peptide derived from the alpha-chain of bovine hemoglobin isolated from the tick Boophilus microplus.",published,journal,Biochemistry,,44,17,,,,,,,,,,,,,,,,,,,,,,6440,6451,2005, citations,ref_1,6411,245869,2,,reference citation,,,8520220,,"Delaglio, F.; Grzesiek, S.; Vuister, G. W.; Zhu, G.; Pfeifer, J.; Bax, A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 1995, 6, 277-293; Johnson, B.; Blevins, R. A. NMRView: A computer program for the visualization and analysis of NMR data. J. Biomol. NMR 1994, 4, 603-614.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,entry_citation,6412,245885,1,,entry citation,,,15850378,,,"The micelle-bound structure of an antimicrobial peptide derived from the alpha-chain of bovine hemoglobin isolated from the tick Boophilus microplus.",published,journal,Biochemistry,,44,17,,,,,,,,,,,,,,,,,,,,,,6440,6451,2005, citations,entry_citation,6438,246438,1,,entry citation,,,,,,"1H, 13C and 15N Chemical Shift Assignments of the C-Terminal, 133-Residue Pseudo-Receiver Domain of Circadian Input Kinase (CikA) in Synechococcus elongatus",published,journal,J. Biomol. NMR,,32,,,,,,,,,,,,,,,,,,,,,,,259,259,2005, citations,citation_1,6439,246469,1,,entry citation,,,,,,"Letter to the Editor: 1H, 15N and 13C backbone and side-chain assignments of the rice phytochrome B PAS1 domain and backbone assignments of the PAS1-PAS2 domain",published,journal,J. Biomol. NMR,,31,3,,,,,,,,,,,,,,,,,,,,,,269,270,2005, citations,entry_citation,644,246497,1,,entry citation,,,,,"Torchia, Dennis A., Sparks, Steven W., Young, Paul E., Bax, Ad, ""Proline Assignments and Identification of the Cis K116/P117 Peptide Bond in Liganded Staphylococcal Nuclease Using Isotope Edited 2D NMR Spectroscopy,"" J. Am. Chem. Soc. 111, 8315-8317 (1989).","Proline Assignments and Identification of the Cis K116/P117 Peptide Bond in Liganded Staphylococcal Nuclease Using Isotope Edited 2D NMR Spectroscopy",published,journal,J. Am. Chem. Soc.,,111,,,,,,,,,,,,,,,,,,,,,,,8315,8317,1989, citations,citation_1,6440,246510,1,,entry citation,,,,,,"Letter to the Editor: 1H, 15N and 13C backbone and side-chain assignments of the rice phytochrome B PAS1 domain and backbone assignments of the PAS1-PAS2 domain",published,journal,J. Biomol. NMR,,31,3,,,,,,,,,,,,,,,,,,,,,,269,270,2005, citations,ref_1,6412,245886,2,,reference citation,,,8520220,,"Delaglio, F.; Grzesiek, S.; Vuister, G. W.; Zhu, G.; Pfeifer, J.; Bax, A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 1995, 6, 277-293; Johnson, B.; Blevins, R. A. NMRView: A computer program for the visualization and analysis of NMR data. J. Biomol. NMR 1994, 4, 603-614.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,entry_citation,6413,245906,1,,entry citation,,,15850378,,,"The micelle-bound structure of an antimicrobial peptide derived from the alpha-chain of bovine hemoglobin isolated from the tick Boophilus microplus.",published,journal,Biochemistry,,44,17,,,,,,,,,,,,,,,,,,,,,,6440,6451,2005, citations,ref_1,6413,245907,2,,reference citation,,,8520220,,"Delaglio, F.; Grzesiek, S.; Vuister, G. W.; Zhu, G.; Pfeifer, J.; Bax, A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 1995, 6, 277-293; Johnson, B.; Blevins, R. A. NMRView: A computer program for the visualization and analysis of NMR data. J. Biomol. NMR 1994, 4, 603-614.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,entry_citation,6414,245926,1,,entry citation,,,15850378,,,"The micelle-bound structure of an antimicrobial peptide derived from the alpha-chain of bovine hemoglobin isolated from the tick Boophilus microplus.",published,journal,Biochemistry,,44,17,,,,,,,,,,,,,,,,,,,,,,6440,6451,2005, citations,ref_1,6414,245927,2,,reference citation,,,8520220,,"Delaglio, F.; Grzesiek, S.; Vuister, G. W.; Zhu, G.; Pfeifer, J.; Bax, A. NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 1995, 6, 277-293; Johnson, B.; Blevins, R. A. NMRView: A computer program for the visualization and analysis of NMR data. J. Biomol. NMR 1994, 4, 603-614.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,entry_citation,6415,245947,1,,entry citation,,,15157100,,,"NMR Characterization of Three-Disulfide Variants of Lysozyme, C64A/C80A, C76A/C94A, and C30A/C115A -A Marginally Stable State in Folded Proteins",published,journal,Biochemistry,,43,21,,,,,,,,,,,,,,,,,,,,,,6663,6669,2004, citations,ref_1,6415,245948,2,,reference citation,,,10395829,,"van den Berg B, Chung EW, Robinson CV, Dobson CM. Characterisation of the dominant oxidative folding intermediate of hen lysozyme. J Mol Biol. 1999 Jul 16;290(3):781-96.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,ref_2,6415,245949,3,,reference citation,,,11841203,,"Noda Y, Yokota A, Horii D, Tominaga T, Tanisaka Y, Tachibana H, Segawa S. NMR structural study of two-disulfide variant of hen lysozyme: 2SS[6-127, 30-115]--a disulfide intermediate with a partly unfolded structure. Biochemistry. 2002 Feb 19;41(7):2130-9.",,,,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6416,245970,1,,entry citation,,,,,,"Backbone 1H, 13C, and 15N resonance assignments of a 56 kDa E. coli nickel binding protein NikA",published,journal,J. Biomol. NMR,,32,2,,,,,,,,,,,,,,,,,,,,,,177,177,2005, citations,citation_1,6441,246531,1,,entry citation,,,16429482,,,"Orexin-A is composed of a highly conserved C-terminal and a specific, hydrophilic N-terminal region, revealing the structural basis of specific recognition by the orexin-1 receptor.",published,journal,J. Pept. Sci.,,12,7,,,,,,,,,,,,,,,,,,,,,,443,454,2006, citations,ref_1,6416,245971,2,,reference citation,,,12960164,,"Heddle J, Scott DJ, Unzai S, Park SY, Tame JR. Crystal structures of the liganded and unliganded nickel-binding protein NikA from Escherichia coli. J Biol Chem. 2003 Dec 12;278(50):50322-9. Epub 2003 Sep 05.",Crystal structures of the liganded and unliganded nickel-binding protein NikA from Escherichia coli.,published,journal,J. Biol. Chem.,The Journal of biological chemistry,278,50,,0021-9258,,,,,,,,,,,,,,,,,,,,50322,50329,2003,"Bacteria have evolved a number of tightly controlled import and export systems to maintain intracellular levels of the essential but potentially toxic metal nickel. Nickel homeostasis systems include the dedicated nickel uptake system nik found in Escherichia coli, a member of the ABC family of transporters, that involves a periplasmic nickel-binding protein, NikA. This is the initial nickel receptor and mediator of the chemotactic response away from nickel. We have solved the crystal structure of NikA protein in the presence and absence of nickel, showing that it behaves as a ""classical"" periplasmic binding protein. In contrast to other binding proteins, however, the ligand remains accessible to the solvent and is not completely enclosed. No direct bonds are formed between the metal cation and the protein. The nickel binding site is apolar, quite unlike any previously characterized protein nickel binding site. Despite relatively weak binding, NikA is specific for nickel. Using isothermal titration calorimetry, the dissociation constant for nickel was found to be approximately 10 microm and that for cobalt was approximately 20 times higher." citations,entry_citation,6418,246021,1,,entry citation,,,,,,"Letter to the Editor: Backbone 1H, 13C and 15N resonance assignments for the Mg2+ -bound form of the Ca2+ -binding photoprotein aequorin",published,journal,J. Biomol. NMR,,31,4,,,,,,,,,,,,,,,,,,,,,,375,376,2005, citations,entry_citation,6419,246053,1,,entry citation,,,15557330,,,"Structure of the C-terminal Domain from Trypanosoma brucei Variant Surface Glycoprotein MITat1.2",published,journal,J. Biol. Chem.,,280,8,,,,,,,,,,,,,,,,,,,,,,7228,7235,2005, citations,entry_citation,6420,246071,1,,entry citation,,,15227539,,,"NMR structure determination and calcium binding effects of lipopeptide antibiotic daptomycin.",published,journal,Org. Biomol. Chem.,,2,13,,,,,,,,,,,,,,,,,,,,,,1872,1878,2004, citations,entry_citation,6421,246094,1,,entry citation,,,15658866,,,"Somatostatin receptor 1 selective analogues: 4. Three-dimensional consensus structure by NMR.",published,journal,J. Med. Chem.,,48,2,,,,,,,,,,,,,,,,,,,,,,523,533,2005, citations,entry_citation,6422,246111,1,,entry citation,,,15658866,,,"Somatostatin receptor 1 selective analogues: 4. Three-dimensional consensus structure by NMR",published,journal,J. Med. Chem.,,48,2,,,,,,,,,,,,,,,,,,,,,,523,533,2005, citations,entry_citation,6423,246128,1,,entry citation,,,15658866,,,"Somatostatin receptor 1 selective analogues: 4. Three-dimensional consensus structure by NMR",published,journal,J. Med. Chem.,,48,2,,,,,,,,,,,,,,,,,,,,,,523,533,2005, citations,entry_citation,6424,246146,1,,entry citation,,,15658866,,,"Somatostatin receptor 1 selective analogues: 4. Three-dimensional consensus structure by NMR",published,journal,J. Med. Chem.,,48,2,,,,,,,,,,,,,,,,,,,,,,523,533,2005, citations,entry_citation,6425,246162,1,,entry citation,,,15658866,,,"Somatostatin receptor 1 selective analogues: 4. Three-dimensional consensus structure by NMR",published,journal,J. Med. Chem.,,48,2,,,,,,,,,,,,,,,,,,,,,,523,533,2005, citations,entry_citation,6426,246179,1,,entry citation,,,15658866,,,"Somatostatin receptor 1 selective analogues: 4. Three-dimensional consensus structure by NMR",published,journal,J. Med. Chem.,,48,2,,,,,,,,,,,,,,,,,,,,,,523,533,2005, citations,entry_citation,6427,246196,1,,entry citation,,,15697223,,,Solution structure of a recombinant type I sculpin antifreeze protein.,published,journal,Biochemistry,,44,6,,,,,,,,,,,,,,,,,,,,,,1980,1988,2005, citations,ref_1,6427,246197,2,,reference citation,,,11940576,,"Fairley K, Westman BJ, Pham LH, Haymet AD, Harding MM, Mackay JP. Type I shorthorn sculpin antifreeze protein: recombinant synthesis, solution conformation, and ice growth inhibition studies. J Biol Chem. 2002 Jul 5;277(27):24073-80. Epub 2002 Apr 08.","Type I shorthorn sculpin antifreeze protein: recombinant synthesis, solution conformation, and ice growth inhibition studies.",published,journal,J. Biol. Chem.,The Journal of biological chemistry,277,27,,0021-9258,,,,,,,,,,,,,,,,,,,,24073,24080,2002,"A number of structurally diverse classes of ""antifreeze"" proteins that allow fish to survive in sub-zero ice-laden waters have been isolated from the blood plasma of cold water teleosts. However, despite receiving a great deal of attention, the one or more mechanisms through which these proteins act are not fully understood. In this report we have synthesized a type I antifreeze polypeptide (AFP) from the shorthorn sculpin Myoxocephalus scorpius using recombinant methods. Construction of a synthetic gene with optimized codon usage and expression as a glutathione S-transferase fusion protein followed by purification yielded milligram amounts of polypeptide with two extra residues appended to the N terminus. Circular dichroism and NMR experiments, including residual dipolar coupling measurements on a 15N-labeled recombinant polypeptide, show that the polypeptides are alpha-helical with the first four residues being more flexible than the remainder of the sequence. Both the recombinant and synthetic polypeptides modify ice growth, forming facetted crystals just below the freezing point, but display negligible thermal hysteresis. Acetylation of Lys-10, Lys-20, and Lys-21 as well as the N terminus of the recombinant polypeptide gave a derivative that displays both thermal hysteresis (0.4 degrees C at 15 mg/ml) and ice crystal faceting. These results confirm that the N terminus of wild-type polypeptide is functionally important and support our previously proposed mechanism for all type I proteins, in which the hydrophobic face is oriented toward the ice at the ice/water interface." citations,entry_citation,6428,246231,1,,entry citation,,,15772309,,,"Probing the pH-dependent structural features of alpha-KTx12.1 a potassium channel blocker from the scorpion Tityus serrulatus",published,journal,Protein Sci.,,14,4,,,,,,,,,,,,,,,,,,,,,,1025,1038,2005, citations,entry_citation_1,6429,246250,1,,entry citation,,,16460010,,,"Analysis of ligand binding and protein dynamics of human retinoid x receptor alpha ligand-binding domain by nuclear magnetic resonance.",published,journal,Biochemistry,,45,6,,,,,,,,,,,,,,,,,,,,,,1629,1639,2006, citations,Citation_2,6429,246251,2,,reference citation,,,7760929,,,Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha,,journal,Nature,,375,6530,,,,,,,,,,,,,,,,,,,,,,377,382,1995, citations,Citation_3,6429,246252,3,,reference citation,,,10835357,,,"Crystal structure of the human RXRalpha ligand-binding domain bound to its natural ligand: 9-cis retinoic acid",,journal,EMBO J.,,19,11,,,,,,,,,,,,,,,,,,,,,,2592,2601,2000, citations,Citation_4,6429,246253,4,,reference citation,,,10764590,,,"Ligand-induced Stabilization of PPARgamma Monitored by NMR Spectroscopy: Implications for Nuclear Receptor Activation",,journal,J. Mol. Biol.,,298,2,,,,,,,,,,,,,,,,,,,,,,187,194,2000, citations,entry_citation,6430,246276,1,,entry citation,,,,,,"An interlocked dimeric parallel-stranded DNA quadruplex: a potent inhibitor of HIV-1 integrase",published,journal,Proc. Natl. Acad. Sci. U.S.A.,,102,3,,,,,,,,,,,,,,,,,,,,,,634,639,2005, citations,entry_citation,6431,246305,1,,entry citation,,,16041487,,,"Letter to the Editor: 1H, 13C and 15N assignments for the II-III loop region of the skeletal dyhydropyridine receptor",published,journal,J. Biomol. NMR,,32,1,,,,,,,,,,,,,,,,,,,,,,89,90,2005, citations,entry_citation,6432,246330,1,,entry citation,,,,,,"NMR solution Structure of a partially diordered protein from Arabdopsis Thaliana At2g23090",in preparation,journal,J. Biomol. NMR,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6433,246355,1,,entry citation,,,15929013,,,"Letter to the Editor: Sequence specific 1HN, 13C and 15N resonance assignments of a novel calcium-binding protein from Entamoeba histolytica.",published,journal,J. Biomol. NMR,,31,4,,,,,,,,,,,,,,,,,,,,,,379,380,2005, citations,entry_citation,6434,246377,1,,entry citation,,,,,,"Letter to the Editor: NMR assignment of the gpU tail protein from lambda bacteriophage",published,journal,J. Biomol. NMR,,32,1,,,,,,,,,,,,,,,,,,,,,,91,92,2005, citations,entry_citation,6436,246395,1,,entry citation,,,,,,"1H,15N, and 13C resonance assignments of a natively unfolded protein XC4149 from the plant pathogen XCC 17",submitted,journal,J. Biomol. NMR,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6437,246418,1,,entry citation,,,15687491,,,Structural Origin of Endotoxin Neutralization and Antimicrobial Activity of a Lactoferrin-based Peptide.,published,journal,J. Biol. Chem.,,280,17,,,,,,,,,,,,,,,,,,,,,,16955,16961,2005, citations,citation_1,6442,246549,1,,entry citation,,,16211497,,,"1H, 13C, and 15N Sequence-specific Resonance Assignment and Secondary Structure of Plasmodium falciparum Thioredoxin",published,journal,J. Biomol. NMR,,32,4,,,,,,,,,,,,,,,,,,,,,,340,340,2005, citations,Original_cloning_of_MTF-1,6445,246612,2,,reference citation,,,8467794,,"Radtke, F., Heuchel, R., Georgiev, O., Hergersberg, M., Gariglio, M., Dembic, Z., and Schaffner, W. (1993). Cloned transcription factor MTF-1 activates the mouse metallothionein I promoter. EMBO J., 12, 1355-1362.",Cloned transcription factor MTF-1 activates the mouse metallothionein I promoter.,published,journal,EMBO J.,The EMBO journal,12,4,,0261-4189,,,,,,,,,,,,,,,,,,,,1355,1362,1993,"Metallothioneins (MTs) are small cysteine-rich proteins whose structure is conserved from fungi to man. MTs strongly bind heavy metals, notably zinc, copper and cadmium. Upon exposure of cells to heavy metal and other adverse treatments, MT gene transcription is strongly enhanced. Metal induction is mediated by several copies of a 15 bp consensus sequence (metal-responsive element, MRE) present in the promoter region of MT genes. We and others have demonstrated the presence of an MRE-binding factor in HeLa cell nuclear extracts. We found that this factor, termed MTF-1 (MRE-binding transcription factor) is inactivated/reactivated in vitro by zinc withdrawal/addition. Here we report that the amounts of MTF-1-DNA complexes are elevated several-fold in zinc-treated cells, as measured by bandshift assay. We have also cloned the cDNA of mouse MTF-1, a 72.5 kDa protein. MTF-1 contains six zinc fingers and separate transcriptional activation domains with high contents of acidic and proline residues. Ectopic expression of MTF-1 in primate or rodent cells strongly enhances transcription of a reporter gene that is driven by four consensus MREd sites, or by the complete mouse MT-I promoter, even at normal zinc levels." citations,entry_citation,6446,246636,1,,entry citation,,,15677483,,,The Na+/H+ Exchanger isoform 1,published,journal,J. Biol. Chem.,,280,18,,,,,,,,,,,,,,,,,,,,,,17863,17872,2005, citations,entry_citation,6447,246660,1,,entry citation,,,16373071,,,Solution Structure of a Two-repeat Fragment of Major Vault Protein.,published,journal,J. Mol. Biol.,,356,2,,,,,,,,,,,,,,,,,,,,,,444,452,2006, citations,entry_citation,6448,246680,1,,entry citation,,,,,,"1H, 13C, and 15N Resonance Assignments for Escherichia coli ytfP, a Member of the Broadly Conserved UPF0131 Protein Domain Family",published,journal,J. Biomol. NMR,,33,3,,,,,,,,,,,,,,,,,,,,,,197,197,2005, citations,entry_citation_1,6449,246726,1,,entry citation,,,16460010,,,"Analysis of ligand binding and protein dynamics of human retinoid x receptor alpha ligand-binding domain by nuclear magnetic resonance",published,journal,Biochemistry,,45,6,,,,,,,,,,,,,,,,,,,,,,1629,1639,2006, citations,Citation_2,6449,246727,2,,reference citation,,,7760929,,,Crystal structure of the ligand-binding domain of the human nuclear receptor RXR-alpha,,journal,Nature,,375,6530,,,,,,,,,,,,,,,,,,,,,,377,382,1995, citations,Citation_3,6449,246728,3,,reference citation,,,10835357,,,"Crystal structure of the human RXRalpha ligand-binding domain bound to its natural ligand: 9-cis retinoic acid",,journal,EMBO J.,,19,11,,,,,,,,,,,,,,,,,,,,,,2592,2601,2000, citations,Citation_4,6449,246729,4,,reference citation,,,10764590,,,"Ligand-induced Stabilization of PPARgamma Monitored by NMR Spectroscopy: Implications for Nuclear Receptor Activation",,journal,J. Mol. Biol.,,298,2,,,,,,,,,,,,,,,,,,,,,,187,194,2000, citations,entry_citation,645,246754,1,,entry citation,,,,,"Falk, Karl-Erik, Jovall, Per-Ake, Angstrom, Jonas, ""N.m.r. and e.p.r. characterization of [4-carboxy-2,6-dinitrophenyllysine]cytochromes c,"" Biochem. J. 193, 1021-1024 (1981).","N.m.r. and e.p.r. characterization of [4-carboxy-2,6-dinitrophenyllysine]cytochromes c",published,journal,Biochem. J.,,193,,,,,,,,,,,,,,,,,,,,,,,1021,1024,1981, citations,entry_citation,6451,246770,1,,entry citation,,,15929012,,,"Letter to the Editor: Backbone resonance assigment of the homodimeric, 35 kDa chaperone CesT from enteropathogenic Escherichia coli",published,journal,J. Biomol. NMR,,31,4,,,,,,,,,,,,,,,,,,,,,,377,378,2005, citations,entry_citation,6452,246786,1,,entry citation,,,,,,"1H, 13C and 15N resonance assignments of the PDZ domain of CLP-36",in preparation,journal,J. Biomol. NMR,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6453,246809,1,,entry citation,,,15883188,,,The solution structure of the oxidative stress-related protein YggX from Escherichia coli.,published,journal,Protein Sci.,,14,,,,,,,,,,,,,,,,,,,,,,,1673,1678,2005, citations,entry_citation,6454,246836,1,,entry citation,,,15929010,,,"Letter to the Editor: Backbone and side chain 1H, 13C and 15N assignments for Escherichia coli SdiA1-171, the autoinducer-binding domain of a quorum sensing protein",published,journal,J. Biomol. NMR,,31,4,,,,,,,,,,,,,,,,,,,,,,373,374,2005, citations,entry_citation_1,6455,246852,1,,entry citation,,,16569017,,,"Three-dimensional structure of the water-insoluble protein crambin in dodecylphosphocholine micelles and its minimal solvent-exposed surface",published,journal,J. Am. Chem. Soc.,,128,13,,,,,,,,,,,,,,,,,,,,,,4398,4404,2006, citations,entry_citation,6456,246867,1,,entry citation,,,16155203,,,"Structural characterization of Lyn-SH3 domain in complex with a herpesviral protein reveals an extended recognition motif that enhances binding affinity",published,journal,Protein Sci.,,14,10,,,,,,,,,,,,,,,,,,,,,,2487,2498,2005, citations,entry_citation,6457,246896,1,,entry citation,,,,,,Validation of Protein Structure from Anisotropic Carbonyl Chemical Shifts in a Dilute Liquid Crystalline Phase,published,journal,J. Am. Chem. Soc.,,120,,,,,,,,,,,,,,,,,,,,,,,6836,6837,1998, citations,entry_citation,6458,246910,1,,entry citation,,,2827748,,,"Two-Dimensional 1H NMR Study of Human Ubiquitin: A Main Chain Directed Assignment and Structure Analysis",published,journal,Biochemistry,,26,23,,,,,,,,,,,,,,,,,,,,,,7272,7281,1987, citations,entry_citation,6459,246924,1,,entry citation,,,15971201,,,"Phosphorylation of either Ser16 or Thr30 does not disrupt the structure of the Itch E3 ubiquitin ligase third WW domain",published,journal,Proteins,,60,3,,,,,,,,,,,,,,,,,,,,,,558,560,2005, citations,entry_citation,6460,246955,1,,entry citation,,,15929004,,,"Letter to the Editor: NMR assignments of a low molecular weight protein tyrosine phosphatase (PTPase) from Bacillus subtilis",published,journal,J. Biomol. NMR,,31,4,,,,,,,,,,,,,,,,,,,,,,363,363,2005, citations,entry_citation,6462,246981,1,,entry citation,,,15635665,,,"Structural studies and model membrane interactions of two peptides derived from bovine lactoferricin.",published,journal,J. Pept. Sci.,,11,7,,,,,,,,,,,,,,,,,,,,,,379,389,2004, citations,entry_citation,6463,246998,1,,entry citation,,,15635665,,,"Structural studies and model membrane interactions of two peptides derived from bovine lactoferricin.",published,journal,J. Pept. Sci.,,11,7,,,,,,,,,,,,,,,,,,,,,,379,289,2004, citations,entry_citation,6464,247013,1,,entry citation,,,16081658,,,Structure of the B3 domain from Arabidopsis thaliana protein At1g16640.,published,journal,Protein Sci.,,14,,,,,,,,,,,,,,,,,,,,,,,2478,2483,2005, citations,entry_citation,6465,247036,1,,entry citation,,,,,,"NMR assignment of the periplasmic domain of peptidoglycan-associated lipoprotein (Pal) from Haemophilus influenzae",published,journal,J. Biomol. NMR,,32,1,,,,,,,,,,,,,,,,,,,,,,93,93,2005, citations,entry_citation,6466,247063,1,,entry citation,,,8634254,,,"Internal Dynamics of Human Ubiquitin Revealed by 13C-Relaxation Studies of Randomly Fractionally Labeled Protein",published,journal,Biochemistry,,35,19,,,,,,,,,,,,,,,,,,,,,,6116,6125,1996, citations,entry_citation,6467,247093,1,,entry citation,,,15987885,,,"Solution structure of APETx2, a specific peptide inhibitor of ASIC3 proton-gated channels",published,journal,Protein Sci.,,14,8,,,,,,,,,,,,,,,,,,,,,,2003,2010,2005, citations,entry_citation,6470,247150,1,,entry citation,,,,,,Rotational Diffusion Anisotropy of Human Ubiquitin from 15N NMR Relaxation,published,journal,J. Am. Chem. Soc.,,117,50,,,,,,,,,,,,,,,,,,,,,,12562,12566,1995, citations,entry_citation,6473,247169,1,,entry citation,,,15752694,,,Compact molten globule-like state of hUBF HMG Box1 at extremely low pH,published,journal,Biochim Biophys Acta,,1748,1,,,,,,,,,,,,,,,,,,,,,,66,73,2005, citations,entry_citation,6474,247182,1,,entry citation,,,16042389,,,"PhosphoThr Peptide Binding Globally Rigidifies Much of the FHA Domain from Arabidopsis Receptor Kinase-Associated Protein Phosphatase",published,journal,Biochemistry,,44,30,,,,,,,,,,,,,,,,,,,,,,10119,10134,2005, citations,citation_1,6475,247206,1,,entry citation,,,15740741,,,"Structure of a Mannan-specific Family 35 Carbohydrate-Binding Module: Evidence for Significant Conformational Changes upon Ligand Binding",published,journal,J. Mol. Biol.,,347,2,,,,,,,,,,,,,,,,,,,,,,287,296,2005, citations,entry_citation,6476,247232,1,,entry citation,,,15878177,,,"Engineering the structural stability and functional properties of the GI domain into the intrinsically unfolded GII domain of the yeast linker histone Hho1p.",published,journal,J. Mol. Biol.,,349,3,,,,,,,,,,,,,,,,,,,,,,608,620,2005, citations,entry_citation,6477,247255,1,,entry citation,,,15749017,,,"Structure of the human telomerase RNA pseudoknot reveals conserved tertiary interactions essential for function.",published,journal,Mol. Cell,,17,,,,,,,,,,,,,,,,,,,,,,,671,682,2005, citations,entry_citation,6478,247293,1,,entry citation,,,15939023,,,"AbrB-like Transcription Factors Assume a Swapped Hairpin Fold that Is Evolutionarily Related to Double-Psi beta Barrels",published,journal,Structure (Camb),,13,6,,,,,,,,,,,,,,,,,,,,,,919,928,2005, citations,entry_citation,6479,247310,1,,entry citation,,,15733914,,,"The structure of the excisionase (Xis) protein from conjugative transposon Tn916 provides insights into the regulation of heterobivalent tyrosine recombinases",published,journal,J. Mol. Biol.,,374,1,,,,,,,,,,,,,,,,,,,,,,11,25,2005, citations,citation_one,6479,247311,2,,reference citation,,,8589602,,"Wishart, D. S., Bigam, C. G., Yao, J., Abildgaard, F., Dyson, H. J., Oldfield, E., Markley, J. L., and Sykes, B. D. J. Biomol. NMR 6, 135-140 (1995).","1H, 13C and 15N chemical shift referencing in biomolecular NMR.",published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,2,,0925-2738,,,,,,,,,,,,,,,,,,,,135,140,1995,"A considerable degree of variability exists in the way that 1H, 13C and 15N chemical shifts are reported and referenced for biomolecules. In this article we explore some of the reasons for this situation and propose guidelines for future chemical shift referencing and for conversion from many common 1H, 13C and 15N chemical shift standards, now used in biomolecular NMR, to those proposed here." citations,entry_citation,6480,247347,1,,entry citation,,,16083905,,,"An Atomic-level Investigation of the Disease-causing A629P Mutant of the Menkes Protein, ATP7A.",published,journal,J. Mol. Biol.,,352,2,,,,,,,,,,,,,,,,,,,,,,409,417,2005, citations,entry_citation,6481,247376,1,,entry citation,,,16083905,,,"An Atomic-level Investigation of the Disease-causing A629P Mutant of the Menkes Protein, ATP7A.",published,journal,J. Mol. Biol.,,352,2,,,,,,,,,,,,,,,,,,,,,,409,417,2005, citations,entry_citation,6482,247403,1,,entry citation,,,16083905,,,"An Atomic-level Investigation of the Disease-causing A629P Mutant of the Menkes Protein, ATP7A.",published,journal,J. Mol. Biol.,,352,2,,,,,,,,,,,,,,,,,,,,,,409,417,2005, citations,entry_citation,6483,247432,1,,entry citation,,,16083905,,,"An Atomic-level Investigation of the Disease-causing A629P Mutant of the Menkes Protein, ATP7A.",published,journal,J. Mol. Biol.,,352,2,,,,,,,,,,,,,,,,,,,,,,409,417,2005, citations,citation,6484,247459,1,,entry citation,,,,,,Resonance Assignments for Mouse S100A13,published,journal,J. Biomol. NMR,,32,3,,,,,,,,,,,,,,,,,,,,,,257,257,2005, citations,entry_citation,6485,247490,1,,entry citation,,,15840813,,,A novel RNA pentaloop fold involved in targeting ADAR2,published,journal,RNA,,11,5,,,,,,,,,,,,,,,,,,,,,,592,597,2005, citations,entry_citation,6488,247509,1,,entry citation,,,,,,"Reparametrization of the Karplus Relation for 3J(HA-N) and 3J(HN-C') in Peptides from Uniformly 13C/15N-Enriched Human Ubiquitin",published,journal,J. Am. Chem. Soc.,,117,10,,,,,,,,,,,,,,,,,,,,,,1810,1813,1995, citations,citation_1,6489,247522,1,,entry citation,,,16497328,,,"A New Solution Structure of ATP Synthase Subunit c from Thermophilic Bacillus PS3, Suggesting a Local Conformational Change for H(+)-Translocation",published,journal,J. Mol. Biol.,,,,,,,,,,,,,,,,,,,,,,,,,,,2006, citations,entry_citation,6493,247551,1,,entry citation,,,,,,"Letter to the Editor: 1H, 13C and 15N resonance assignments of URNdesign, a computationally redesigned RRM protein",submitted,journal,J. Biomol. NMR,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,main_citation,6494,247566,1,,entry citation,,,15865424,,,"Investigation of Ligand Binding and Protein Dynamics in Bacillus subtilis Chorismate Mutase by Transverse Relaxation Optimized Spectroscopy-Nuclear Magnetic Resonance",published,journal,Biochemistry,,44,18,,,,,,,,,,,,,,,,,,,,,,6788,6799,2005, citations,main_citation,6495,247593,1,,entry citation,,,15865424,,,"Investigation of Ligand Binding and Protein Dynamics in Bacillus subtilis Chorismate Mutase by Transverse Relaxation Optimized Spectroscopy-Nuclear Magnetic Resonance",published,journal,Biochemistry,,44,18,,,,,,,,,,,,,,,,,,,,,,6788,6799,2005, citations,main_citation,6496,247618,1,,entry citation,,,15865424,,,"Investigation of Ligand Binding and Protein Dynamics in Bacillus subtilis Chorismate Mutase by Transverse Relaxation Optimized Spectroscopy-Nuclear Magnetic Resonance",published,journal,Biochemistry,,44,18,,,,,,,,,,,,,,,,,,,,,,6788,6799,2005, citations,entry_citation,6498,247637,1,,entry citation,,,15996101,,,"The Modular Structure of SIP Facilitates Its Role in Stabilizing Multiprotein Assemblies(,).",published,journal,Biochemistry,,44,27,,,,,,,,,,,,,,,,,,,,,,9462,9471,2005, citations,entry_citation,6499,247661,1,,entry citation,,,15840728,,,"A folding-dependent mechanism of antimicrobial peptide resistance to degradation unveiled by solution structure of distinctin.",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,65,247680,1,,entry citation,,,,,"Arseniev, Alexander S., Wider, Gerhard, Joubert, Francois J., Wuthrich, Kurt, ""Assignment of the 1H Nuclear Magnetic Resonance Spectrum of the Trypsin Inhibitor E from Dendroaspis polylepis polylepis Two-dimensional Nuclear Magnetic Resonance at 500MHz,"" J. Mol. Biol. 159, 323-351 (1982).","Assignment of the 1H Nuclear Magnetic Resonance Spectrum of the Trypsin Inhibitor E from Dendroaspis polylepis polylepis Two-dimensional Nuclear Magnetic Resonance at 500MHz",published,journal,J. Mol. Biol.,,159,,,,,,,,,,,,,,,,,,,,,,,323,351,1982, citations,entry_citation,6500,247693,1,,entry citation,,,15996101,,,"The Modular Structure of SIP Facilitates Its Role in Stabilizing Multiprotein Assemblies",published,journal,Biochemistry,,44,27,,,,,,,,,,,,,,,,,,,,,,9462,9471,2005, citations,entry_citation,6501,247712,1,,entry citation,,,,,,Backbone dynamics of SARS-CoV Nsp9 by NMR spectroscopy,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,6502,247725,1,,entry citation,,,,,,Resonance assignments for the DNA binding domain of ERCC-1/XPF heterodimer,published,journal,J. Biomol. NMR,,32,2,,,,,,,,,,,,,,,,,,,,,,175,175,2005, citations,entry_citation,6503,247736,1,,entry citation,,,16211495,,,"NMR Assignment of the Apo and Peptide-bound SH2 Domain from the Rous Sarcoma Viral Protein Src",published,journal,J. Biomol. NMR,,32,4,,,,,,,,,,,,,,,,,,,,,,339,339,2005, citations,1,6504,247768,1,,entry citation,,,,,,NMR solution structures of crambin determined in a mixed organic/aqueous solvent and in detergent micelles: effect of lipid chains on protein compactness and stability,submitted,journal,Proc. Natl. Acad. Sci. U.S.A.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6505,247781,1,,entry citation,,,17496898,,,Microgram-scale protein structure determination by NMR,published,journal,Nature Methods,,4,6,,,,,,,,,,,,,,,,,,,,,,491,493,2007, citations,ref-2,6505,247782,2,,reference citation,,,8520220,,"Delaglio F., Grzesiek S., Vuister G.W., Zhu G., Pfeifer J., Bax A. J. Biomol. NMR. (1995) 6, 277-293.",NMRPipe: a multidimensional spectral processing system based on UNIX pipes.,published,journal,J. Biomol. NMR,Journal of biomolecular NMR,6,3,,0925-2738,,,,,,,,,,,,,,,,,,,,277,293,1995,"The NMRPipe system is a UNIX software environment of processing, graphics, and analysis tools designed to meet current routine and research-oriented multidimensional processing requirements, and to anticipate and accommodate future demands and developments. The system is based on UNIX pipes, which allow programs running simultaneously to exchange streams of data under user control. In an NMRPipe processing scheme, a stream of spectral data flows through a pipeline of processing programs, each of which performs one component of the overall scheme, such as Fourier transformation or linear prediction. Complete multidimensional processing schemes are constructed as simple UNIX shell scripts. The processing modules themselves maintain and exploit accurate records of data sizes, detection modes, and calibration information in all dimensions, so that schemes can be constructed without the need to explicitly define or anticipate data sizes or storage details of real and imaginary channels during processing. The asynchronous pipeline scheme provides other substantial advantages, including high flexibility, favorable processing speeds, choice of both all-in-memory and disk-bound processing, easy adaptation to different data formats, simpler software development and maintenance, and the ability to distribute processing tasks on multi-CPU computers and computer networks." citations,entry_citation,6506,247820,1,,entry citation,,,15833744,,,"Conkunitzin-S1 Is the First Member of a New Kunitz-type Neurotoxin Family: STRUCTURAL AND FUNCTIONAL CHARACTERIZATION.",published,journal,J. Biol. Chem.,,280,25,,,,,,,,,,,,,,,,,,,,,,23766,23770,2005, citations,entry_citation,6507,247842,1,,entry citation,,,15724976,,,Selective small molecules blocking HIV-1 Tat and coactivator PCAF association.,published,journal,J. Am. Chem. Soc.,,127,8,,,,,,,,,,,,,,,,,,,,,,2376,2377,2005, citations,entry_citation,6508,247866,1,,entry citation,,,15724976,,,Selective small molecules blocking HIV-1 Tat and coactivator PCAF association,submitted,journal,J. Am. Chem. Soc.,,127(8),,,,,,,,,,,,,,,,,,,,,,,2376,2377,2005, citations,entry_citation,6509,247888,1,,entry citation,,,16123125,,,"A loop 2 cytidine-stem 1 minor groove interaction as a positive determinant for pseudoknot-stimulated -1 ribosomal frameshifting.",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,102,36,,,,,,,,,,,,,,,,,,,,,,12694,12699,2005, citations,entry_citation,6510,247913,1,,entry citation,,,15964019,,,"Structure and Inter-domain Interactions of Domain II from the Blood-stage Malarial Protein, Apical Membrane Antigen 1",published,journal,J. Mol. Biol.,,350,4,,,,,,,,,,,,,,,,,,,,,,641,656,2005, citations,entry_citation,6511,247930,1,,entry citation,,,,,,"Structure, epitope mapping and docking simulation of a gibberellin mimic peptide recognized by an anti-gibberellin A4 antibody 4-B8(8)/E9",published,journal,FEBS J.,,272,19,,,,,,,,,,,,,,,,,,,,,,4938,4948,2005, citations,entry_citation,6512,247947,1,,entry citation,,,,,,NMR assignment of the vaccinia virus envelope protein A27L,published,journal,J. Biomol. NMR,,32,2,,,,,,,,,,,,,,,,,,,,,,178,178,2005, citations,entry_citation,6513,247971,1,,entry citation,,,16188992,,,Structural genomics of the SARS coronavirus: NMR structure of the protein nsp7,published,journal,J. Virol.,,79,20,,,,,,,,,,,,,,,,,,,,,,12905,12913,2005, citations,entry_citation,6514,247995,1,,entry citation,,,,,,Solution NMR Structure of Pseudomonas Aeruginosa PA4608. Northeast Structural Genomics Target PaT7.,in preparation,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6515,248009,1,,entry citation,,,,,,,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6516,248033,1,,entry citation,,,16132833,,,NMR Assignment of the Holo-ACP from Malaria Parasite Plasmodium Falciparum,published,journal,J. Biomol. NMR,,32,3,,,,,,,,,,,,,,,,,,,,,,260,260,2005, citations,cited_references_within_the_entry_1,6516,248034,2,,reference citation,,,,,,"Solution Structure and Backbone Dynamics of the Holo Form of the Frenolicin Acyl Carrier Protein",published,journal,Biochemistry,,42,16,,,,,,,,,,,,,,,,,,,,,,4648,4657,2003, citations,reference_cited_withih_the_entry_2,6516,248035,3,,reference citation,,,,,,"Heteronuclear multidimensional NMR experiments for the structure determination of proteins in solution employing pulsed field gradients",published,journal,Prog. Nucl. Magn. Reson. Spectrosc.,,34,,,,,,,,,,,,,,,,,,,,,,,93,158,1999, citations,entry_citation,6517,248051,1,,entry citation,,,,,,NMR structure of Pseudomonas aeruginosa protein PA4738,in preparation,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6518,248065,1,,entry citation,,,,,,"H,C,N Chemical Shift Assignments of A. vinosum DsrC",in preparation,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation_2,6518,248066,2,,reference citation,,,15687204,,,"Novel genes of the dsr gene cluster and evidence for close interaction of Dsr proteins during sulfur oxidation in the phototrophic sulfur bacterium Allochromatium vinosum",published,journal,J. Bacteriol.,,187,4,,,,,,,,,,,,,,,,,,,,,,1392,1404,2005, citations,entry_citation_3,6518,248067,3,,reference citation,,,9695921,,,"Sirohaem sulfite reductase and other proteins encoded by genes at the dsr locus of Chromatium vinosum are involved in the oxidation of intracellular sulfur",published,journal,"Microbiology (Reading, U. K.)",,144,7,,,,,,,,,,,,,,,,,,,,,,1881,1894,1998, citations,entry_citation,6519,248081,1,,entry citation,,,15937283,,,"Solution structure and backbone dynamics of Calsensin, an invertebrate neuronal calcium-binding protein.",published,journal,Protein Sci.,,14,7,,,,,,,,,,,,,,,,,,,,,,1894,1901,2005, citations,entry_citation,6520,248096,1,,entry citation,,,,,,"The solution structure of the recombinant elicitor protein PcF from the oomycete pathogen P. cactorum displays a helix-loop-helix fold and reveals calcium binding ability",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,Phytophthora_cactorum,6520,248097,2,,reference citation,,,12943233,,"PcF protein from Phytophthora cactorum and its recombinant homologue elicit phenylalanine ammonia lyase activation in tomato. Cell Mol Life Sci. 2003 Jul;60(7):1470-6.",PcF protein from Phytophthora cactorum and its recombinant homologue elicit phenylalanine ammonia lyase activation in tomato.,published,journal,Cell. Mol. Life Sci.,,60,7,,,,,,,,,,,,,,,,,,,,,,1470,1476,2003, citations,citation_1,6521,248110,1,,entry citation,,,16260757,,,"Disruption of an intermonomer salt bridge in the p53 tetramerization domain results in an increased propensity to form amyloid fibrils.",published,journal,Protein Sci.,,14,12,,,,,,,,,,,,,,,,,,,,,,2993,3003,2005, citations,entry_citation,6522,248129,1,,entry citation,,,16260757,,,"Disruption of an intermonomer salt bridge in the p53 tetramerization domain results in an increased propensity to form amyloid fibrils.",published,journal,Protein Sci.,,14,12,,,,,,,,,,,,,,,,,,,,,,2993,3003,2005, citations,citation,6524,248146,1,,entry citation,,,,,,A complete backbone assignment of the apolipoprotein E LDL receptor binding domain,published,journal,J. Biomol. NMR,,32,2,,,,,,,,,,,,,,,,,,,,,,177,177,2005, citations,entry_citation,6525,248168,1,,entry citation,,,16544327,,,"Solution structure of the plant defensin VrD1 from mung bean and its possible role in insecticidal activity against bruchids",published,journal,Proteins,,63,4,,,,,,,,,,,,,,,,,,,,,,777,786,2006, citations,entry_citation,6526,248182,1,,entry citation,,,15811367,,,Solution structure and backbone dynamics of the KH-QUA2 region of the Xenopus STAR/GSG Quaking protein.,published,journal,J. Mol. Biol.,,348,2,,,,,,,,,,,,,,,,,,,,,,265,279,2005, citations,entry_citation,6527,248195,1,,entry citation,,,16083906,,,Structure and Dynamics of the Homodimeric Dynein Light Chain km23.,published,journal,J. Mol. Biol.,,352,2,,,,,,,,,,,,,,,,,,,,,,338,354,2005, citations,citation_1,6528,248211,1,,entry citation,,,,,,NMR assignment of the R2 domain of pneumococcal choline binding protein A (CbpA),published,journal,J. Biomol. NMR,,31,1,,,,,,,,,,,,,,,,,,,,,,93,93,2005, citations,entry_citation,6529,248230,1,,entry citation,,,,,,Complete Assignment and Secondary Structure of the Brazil Nut Allergen Ber e 1,published,journal,J. Biomol. NMR,,32,4,,,,,,,,,,,,,,,,,,,,,,336,336,2005, citations,entry_citation,653,248255,1,,entry citation,,,,,"Sawada, Shintaro, Akutsu, Hideo, Ogasahara, Kyoko, Yutani, Katsuhide, ""Assignment of tyrosine resonances in the 1H-NMR spectrum of tryptophan synthase alpha-subunit Monitoring conformational changes due to substitutions at position 49,"" Eur. J. Biochem. 189, 667-673 (1990).","Assignment of tyrosine resonances in the 1H-NMR spectrum of tryptophan synthase alpha-subunit Monitoring conformational changes due to substitutions at position 49",published,journal,Eur. J. Biochem.,,189,,,,,,,,,,,,,,,,,,,,,,,667,673,1990, citations,entry_citation,6530,248268,1,,entry citation,,,16177782,,,Evolutionary information for specifying a protein fold,published,journal,Nature,,437,7058,,,,,,,,,,,,,,,,,,,,,,512,518,2005, citations,entry_citation,6531,248292,1,,entry citation,,,16145699,,,Structural interplay between calcium(II) and copper(II) binding to S100A13 protein.,published,journal,Angew. Chem. Int. Ed. Engl.,,44,39,,,,,,,,,,,,,,,,,,,,,,6341,6344,2005, citations,entry_citation,6532,248312,1,,entry citation,,,16145699,,,Structural interplay between calcium(II) and copper(II) binding to S100A13 protein,published,journal,Angew. Chem. Int. Ed. Engl.,,44,39,,,,,,,,,,,,,,,,,,,,,,6341,6344,2005, citations,entry_citation,6533,248330,1,,entry citation,,,,,,"Characterization of the bacterial nucleoid protein STPA: Structure, self-association and interaction with H-NS",published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation_1,6533,248331,2,,reference citation,,,1480493,,,"Nucleotide sequence of a newly-identified Escherichia coli gene, stpA, encoding an H-NS-like protein.",published,journal,Nucleic Acids Res.,,20,24,,,,,,,,,,,,,,,,,,,,,,6735,6735,1992, citations,citation_2,6533,248332,3,,reference citation,,,8520220,,,NMRPipe: a multidimensional spectral processing system based on UNIX pipes,published,journal,J. Biomol. NMR,,6,3,,,,,,,,,,,,,,,,,,,,,,277,293,1995, citations,citation_3,6533,248333,4,,reference citation,,,8142349,,,Solution structure and dynamics of ras p21.GDP determined by heteronuclear three- and four-dimensional NMR spectroscopy.,published,journal,Biochemistry,,,,,,,,,,,,,,,,,,,,,,,,,3515,3531,1994, citations,entry_citation,6535,248349,1,,entry citation,,,15793585,,,Insights into hRPA32 C-terminal domain-mediated assembly of the simian virus 40 replisome.,published,journal,Nat. Struct. Mol. Biol.,,12,4,,,,,,,,,,,,,,,,,,,,,,332,339,2005, citations,citation_1,6536,248366,1,,entry citation,,,,,,NMR assignment of the reduced and oxidized forms of the human ADAP hSH3-1 domain,published,journal,J. Biomol. NMR,,32,1,,,,,,,,,,,,,,,,,,,,,,94,94,2005, citations,Citation_1,6537,248381,1,,entry citation,,,16407992,,,Small-molecule ligand induces nucleotide flipping in (CAG)(n) trinucleotide repeats.,published,journal,Nat. Chem. Biol.,,1,1,,,,,,,,,,,,,,,,,,,,,,39,43,2005, citations,entry_citation,6538,248396,1,,entry citation,,,,,,"NMR Structure of the Natural Killer Cell Receptor 2B4 (CD244): Implications for Ligand Recognition",published,journal,Biochemistry.,,44,17,,,,,,,,,,,,,,,,,,,,,,6416,6423,2005, citations,citation_1,6539,248410,1,,entry citation,,,,,,NMR assignment of the reduced and oxidized forms of the human ADAP hSH3-1 domain,published,journal,J. Biomol. NMR,,32,1,,,,,,,,,,,,,,,,,,,,,,94,94,2005, citations,entry_citation,6540,248429,1,,entry citation,,,,,,NMR Assignments of the Winged-Helix Domain of Human Werner Syndrome Protein,published,journal,J. Biomol. NMR,,32,3,,,,,,,,,,,,,,,,,,,,,,261,261,2005, citations,references_1,6540,248430,2,,reference citation,,,8602509,,"Yu CE, Oshima J, Fu YH, Wijsman EM, Hisama F, Alisch R, Matthews S, Nakura J, Miki T, Ouais S, Martin GM, Mulligan J, Schellenberg GD. Positional cloning of the Werner's syndrome gene. Science. 1996 Apr 12;272(5259):258-62.",Positional cloning of the Werner's syndrome gene.,published,journal,Science,"Science (New York, N.Y.)",272,5259,,0036-8075,,,,,,,,,,,,,,,,,,,,258,262,1996,"Werner's syndrome (WS) is an inherited disease with clinical symptoms resembling premature aging. Early susceptibility to a number of major age-related diseases is a key feature of this disorder. The gene responsible for WS (known as WRN) was identified by positional cloning. The predicted protein is 1432 amino acids in length and shows significant similarity to DNA helicases. Four mutations in WS patients were identified. Two of the mutations are splice-junction mutations, with the predicted result being the exclusion of exons from the final messenger RNA. One of the these mutations, which results in a frameshift and a predicted truncated protein, was found in the homozygous state in 60 percent of Japanese WS patients examined. The other two mutations are nonsense mutations. The identification of a mutated putative helicase as the gene product of the WS gene suggests that defective DNA metabolism is involved in the complex process of aging in WS patients." citations,entry_citation,6551,248571,1,,entry citation,,,16338413,,,"The Structure of the Human ERCC1/XPF Interaction Domains Reveals a Complementary Role for the Two Proteins in Nucleotide Excision Repair",published,journal,"Structure (Cambridge, MA, U. S.)",,13,12,,,,,,,,,,,,,,,,,,,,,,1849,1858,2005, citations,entry_citation,6552,248598,1,,entry citation,,,15793003,,,"A protein folding pathway with multiple folding intermediates at atomic resolution",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,102,,,,,,,,,,,,,,,,,,,,,,,5026,5031,2005, citations,entry_citation,6553,248625,1,,entry citation,,,14580191,,,"Specific non-native hydrophobic interactions in a hidden folding intermediate: implications for protein folding",published,journal,Biochemistry,,42,43,,,,,,,,,,,,,,,,,,,,,,12461,12465,2003, citations,entry_citation,6554,248652,1,,entry citation,,,16444756,,,"The alpha-to-beta Conformational Transition of Alzheimer's Abeta-(1-42) Peptide in Aqueous Media is Reversible: A Step by Step Conformational Analysis Suggests the Location of beta Conformation Seeding.",published,journal,Chembiochem.,,7,2,,,,,,,,,,,,,,,,,,,,,,257,267,2006, citations,references_2,6540,248431,3,,reference citation,,,12803543,,"Bachrati CZ, Hickson ID. RecQ helicases: suppressors of tumorigenesis and premature aging. Biochem J. 2003 Sep 15;374(Pt 3):577-606.",RecQ helicases: suppressors of tumorigenesis and premature aging.,published,journal,Biochem. J.,The Biochemical journal,374,Pt 3,,1470-8728,,,,,,,,,,,,,,,,,,,,577,606,2003,"The RecQ helicases represent a subfamily of DNA helicases that are highly conserved in evolution. Loss of RecQ helicase function leads to a breakdown in the maintenance of genome integrity, in particular hyper-recombination. Germ-line defects in three of the five known human RecQ helicases give rise to defined genetic disorders associated with cancer predisposition and/or premature aging. These are Bloom's syndrome, Werner's syndrome and Rothmund-Thomson syndrome, which are caused by defects in the genes BLM, WRN and RECQ4 respectively. Here we review the properties of RecQ helicases in organisms from bacteria to humans, with an emphasis on the biochemical functions of these enzymes and the range of protein partners that they operate with. We will discuss models in which RecQ helicases are required to protect against replication fork demise, either through prevention of fork breakdown or restoration of productive DNA synthesis." citations,references_3,6540,248432,4,,reference citation,,,9397680,,"Morozov V, Mushegian AR, Koonin EV, Bork P. A putative nucleic acid-binding domain in Bloom's and Werner's syndrome helicases. Trends Biochem Sci. 1997 Nov;22(11):417-8.",A putative nucleic acid-binding domain in Bloom's and Werner's syndrome helicases.,published,journal,Trends Biochem. Sci.,Trends in biochemical sciences,22,11,,0968-0004,,,,,,,,,,,,,,,,,,,,417,418,1997, citations,references_4,6540,248433,5,,reference citation,,,15217989,,"Bennett RJ, Keck JL. Structure and function of RecQ DNA helicases. Crit Rev Biochem Mol Biol. 2004 Mar-Apr;39(2):79-97.",Structure and function of RecQ DNA helicases.,published,journal,Crit. Rev. Biochem. Mol. Biol.,Critical reviews in biochemistry and molecular biology,39,2,,1040-9238,,,,,,,,,,,,,,,,,,,,79,97,,"RecQ family helicases play important roles in coordinating genome maintenance pathways in living cells. In the absence of functional RecQ proteins, cells exhibit a variety of phenotypes, including increased mitotic recombination, elevated chromosome missegregation, hypersensitivity to DNA-damaging agents, and defects in meiosis. Mutations in three of the five human RecQ family members give rise to genetic disorders associated with a predisposition to cancer and premature aging, highlighting the importance of RecQ proteins and their cellular activities for human health. Current evidence suggests that RecQ proteins act at multiple steps in DNA replication, including stabilization of replication forks and removal of DNA recombination intermediates, in order to maintain genome integrity. The cellular basis of RecQ helicase function may be explained through interactions with multiple components of the DNA replication and recombination machinery. This review focuses on biochemical and structural aspects of the RecQ helicases and how these features relate to their known cellular function, specifically in preventing excessive recombination." citations,references_5,6540,248434,6,,reference citation,,,15610765,,"Lee JW, Harrigan J, Opresko PL, Bohr VA. Pathways and functions of the Werner syndrome protein. Mech Ageing Dev. 2005 Jan;126(1):79-86.",Pathways and functions of the Werner syndrome protein.,published,journal,Mech. Ageing Dev.,Mechanisms of ageing and development,126,1,,0047-6374,,,,,,,,,,,,,,,,,,,,79,86,2005,"Mutations in human WRN (also known as RECQ3) gene give rise to a rare autosomal recessive genetic disorder, Werner syndrome (WS). WS is a premature aging disease characterized by predisposition to cancer and early onset of symptoms related to normal aging including osteoporosis, ocular cataracts, graying and loss of hair, diabetes mellitus, arteriosclerosis, and atherosclerosis. This review focuses on the functional role of Werner protein (WRN) in guarding the genetic stability of cells, particularly by playing an integral role in the base excision repair, and at the telomere ends. Furthermore, in-depth biochemical investigations have significantly advanced our understanding of WRN protein regarding its binding partners and the site of protein-protein interaction. The mapping analysis of protein interaction sites in WRN for most of its binding partners have revealed a common site of protein-protein interaction in the RecQ conserved (RQC) region of WRN." citations,references_6,6540,248435,7,,reference citation,,,9683536,,"Gray MD, Wang L, Youssoufian H, Martin GM, Oshima J. Werner helicase is localized to transcriptionally active nucleoli of cycling cells. Exp Cell Res. 1998 Aug 1;242(2):487-94.",Werner helicase is localized to transcriptionally active nucleoli of cycling cells.,published,journal,Exp. Cell Res.,Experimental cell research,242,2,,0014-4827,,,,,,,,,,,,,,,,,,,,487,494,1998,"Mutations at the Werner helicase locus (WRN) are responsible for the Werner syndrome (WS), a ""caricature of aging."" We have localized the Werner protein (WRNp) to the nucleoli of replicating mammalian cells, where its appearance is associated with transcriptional activity. A dramatic reduction of the nucleolar signal and of [3H]uridine incorporation occurred when cultures were made quiescent or were exposed to 4-nitroquinoline-1-oxide (4NQO), to which WS cells are particularly susceptible. Total cellular levels of WRNp, however, did not change, and virtually all WRNp was in the nuclear fractions, consistent with translocation to the nucleoplasm and/or masking of the epitopes. The 4NQO-induced altered state of WRNp was prevented by Na3VO4, but not by okadaic acid, suggesting that WRNp localization/function is partially regulated by kinases/phosphatases for Tyr substrates on WRNp or interacting proteins. The repression of rDNA transcription by 4NQO was not reversed by Na3VO4. We suggest that physiological states and genotoxic agents modulate the interaction of WRNp with rDNA, consistent with a role of WRNp in rDNA transcription." citations,entry_citation,6541,248474,1,,entry citation,,,16511487,,,Optimal isotope labelling for NMR protein structure determinations,published,journal,Nature,,440,7080,,,,,,,,,,,,,,,,,,,,,,52,57,2006, citations,reference_citation,6541,248475,2,,reference citation,,,15754057,,,Efficient production of isotopically labeled proteins by cell-free synthesis: A practical protocol,published,journal,J. Biomol. NMR,,30,3,,,,,,,,,,,,,,,,,,,,,,311,325,2004, citations,entry_citation,6542,248489,1,,entry citation,,,,,,"Main chain 1H, 13C, and 15N resonance assignments of the 42-kDa enzyme arginine kinase",published,journal,J. Biomol. NMR,,32,2,,,,,,,,,,,,,,,,,,,,,,178,178,2005, citations,entry_citation,6543,248502,1,,entry citation,,,15927637,,,Soultion structure and thermodynamic investigation of the HIV-1 frameshift inducing element,published,journal,J. Mol. Biol.,,349,5,,,,,,,,,,,,,,,,,,,,,,1011,1023,2005, citations,entry_citation,6546,248520,1,,entry citation,,,16132835,,,GFT NMR based resonance assignment for the 21 kDa human protein UFC1,published,journal,J. Biomol. NMR,,32,3,,,,,,,,,,,,,,,,,,,,,,261,261,2005, citations,entry_citation,6547,248536,1,,entry citation,,,,,,"structure-function relationships of the polyhistidine-rich peptide LAH4 in micellar environments; pH dependent mode of antibiotic action & DNA transfection",in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6549,248558,1,,entry citation,,,16132831,,,"Sequential Backbone Assignment of Peroxisome Proliferator-Activated Receptor-g Ligand Binding Domain",published,journal,J. Biomol. NMR,,32,3,,,,,,,,,,,,,,,,,,,,,,259,259,2005, citations,entry_citation,6555,248672,1,,entry citation,,,18021800,,,"Biochemical and Structural Characterization of a Novel Family of Cystathionine beta-Synthase Domain Proteins Fused to a Zn Ribbon-Like Domain",published,journal,J. Mol. Biol.,,375,1,,,,,,,,,,,,,,,,,,,,,,301,315,2008, citations,entry_citation,6556,248693,1,,entry citation,,,16083422,,,"The N-terminal 26-residue fragment of human programmed cell death 5 protein can form a stable alpha-helix having unique electrostatic potential character",published,journal,Biochem. J.,,392,,,,,,,,,,,,,,,,,,,,,,,47,54,2005, citations,entry_citation,6557,248719,1,,entry citation,,,16872688,,,"Solution conformation of an immunodominant epitope in the hepatitis B virus preS2 surface antigen",published,journal,Antiviral Res.,,72,3,,,,,,,,,,,,,,,,,,,,,,207,215,2006, citations,entry_citation,6558,248741,1,,entry citation,,,15811376,,,Structural basis for APPTPPPLPP peptide recognition by the FBP11WW1 domain,published,journal,J. Mol. Biol.,,348,2,,,,,,,,,,,,,,,,,,,,,,399,408,2005, citations,entry_citation,6559,248766,1,,entry citation,,,15811376,,,Structural basis for APPTPPPLPP peptide recognition by the FBP11WW1 domain,published,journal,J. Mol. Biol.,,348,2,,,,,,,,,,,,,,,,,,,,,,399,408,2005, citations,entry_citation,6560,248794,1,,entry citation,,,14580191,,,"Specific non-native hydrophobic interactions in a hidden folding intermediate: implications for protein folding",published,journal,Biochemistry,,42,43,,,,,,,,,,,,,,,,,,,,,,12461,12465,2003, citations,entry_citation,6561,248818,1,,entry citation,,,15805109,,,"Structure and mode of action of the membrane-permeabilizing antimicrobial peptide pheromone plantaricin A",published,journal,J. Biol. Chem.,,280,24,,,,,,,,,,,,,,,,,,,,,,22945,22950,2005, citations,entry_citation,6562,248837,1,,entry citation,,,15814817,,,"A novel cGUUAg tetraloop structure with a conserved yYNMGg-type backbone conformation from cloverleaf 1 of bovine enterovirus 1 RNA",published,journal,Nucleic Acids Res.,,33,6,,,,,,,,,,,,,,,,,,,,,,2003,2011,2005, citations,entry_citation,6563,248879,1,,entry citation,,,16192272,,,Solution structures and backbone dynamics of arsenate reductase from Bacillus subtilis: Reversible conformational switch associates with arsenate reduction.,published,journal,J. Biol. Chem.,,280,47,,,,,,,,,,,,,,,,,,,,,,39601,39608,2005, citations,citation_1,6564,248892,1,,entry citation,,,,,,"Structure of the F(1)-binding Domain of the Stator of Bovine F(1)F(o)-ATPase and How it Binds an alpha-Subunit.",published,journal,J. Mol. Biol.,,351,4,,,,,,,,,,,,,,,,,,,,,,824,838,2005, citations,citation_1,6565,248910,1,,entry citation,,,16132826,,,NMR Assignment of the Barnacle Cement Protein Mrcp-20k,published,journal,J. Biomol. NMR,,32,3,,,,,,,,,,,,,,,,,,,,,,257,257,2005, citations,entry_citation,6566,248926,1,,entry citation,,,15159535,,,Structural basis for the attachment of a paramyxoviral polymerase to its template,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,101,22,,,,,,,,,,,,,,,,,,,,,,8301,8306,2004, citations,entry_citation,6567,248941,1,,entry citation,,,15159535,,,Structural basis for the attachment of a paramyxoviral polymerase to its template,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,101,22,,,,,,,,,,,,,,,,,,,,,,8301,8306,2004, citations,entry_citation,6568,248957,1,,entry citation,,,15159535,,,Structural basis for the attachment of a paramyxoviral polymerase to its template,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,101,22,,,,,,,,,,,,,,,,,,,,,,8301,8306,2004, citations,entry_citation,6569,248972,1,,entry citation,,,15159535,,,Structural basis for the attachment of a paramyxoviral polymerase to its template,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,101,22,,,,,,,,,,,,,,,,,,,,,,8301,8306,2004, citations,entry_citation,6570,248988,1,,entry citation,,,16211486,,,"NMR Assignment Reveals an alpha-Helical Fold for the F-Actin Binding Domain of Human Bcr-Abl/c-Abl",published,journal,J. Biomol. NMR,,32,4,,,,,,,,,,,,,,,,,,,,,,335,335,2005, citations,entry_citation,6571,249020,1,,entry citation,,,16199579,,,"Nuclear Magnetic Resonance Solution Structure of the Escherichia coli DNA Polymerase III {theta} Subunit.",published,journal,J. Bacteriol.,,187,20,,,,,,,,,,,,,,,,,,,,,,7081,7089,2005, citations,citation_1,6572,249038,1,,entry citation,,,16460012,,,"Redox Interaction of Cytochrome c(3) with [NiFe] Hydrogenase from Desulfovibrio vulgaris Miyazaki F.",published,journal,Biochemistry,,45,6,,,,,,,,,,,,,,,,,,,,,,1653,1662,2006, citations,entry_citation,6573,249053,1,,entry citation,,,16174732,,,Structure and ESCRT-III protein interactions of the MIT domain of human VPS4A.,published,journal,Proc. Natl. Acad. Sci. U. S. A.,,102,39,,,,,,,,,,,,,,,,,,,,,,13813,13818,2005, citations,entry_citation,6574,249072,1,,entry citation,,,,,,,submitted,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6575,249102,1,,entry citation,,,15764601,,,Structural Insight into the Binding Diversity between the Tyr-phosphorylated Human EphrinBs and Nck2 SH2 Domain.,published,journal,J. Biol. Chem.,,280,19,,,,,,,,,,,,,,,,,,,,,,19205,19212,2005, citations,Crotamine_structure_and_disulfide_bonds,6576,249113,1,,entry citation,,,,,,"Automated NMR structure determination and disulfide bond identification of the myotoxin crotamine from Crotalus durissus terrificus",published,journal,Toxicon,,,,,,,,,,,,,,,,,,,,,,,,,,,2005, citations,citation_1,6577,249133,1,,entry citation,,,16081655,,,Solution structure of the C1-subdomain of Bacillus stearothermophilus translation initiation factor IF2.,published,journal,Protein Sci.,,14,9,,,,,,,,,,,,,,,,,,,,,,2461,2468,2005, citations,entry_citation,6578,249174,1,,entry citation,,,16132832,,,"1H, 13C and 15N Resonance Assignments of a Bcl-xL/Bad Peptide Complex",published,journal,J. Biomol. NMR,,32,3,,,,,,,,,,,,,,,,,,,,,,260,260,2005, citations,entry_citation,6579,249188,1,,entry citation,,,15840573,,,"A structural model for the membrane-bound form of the juxtamembrane domain of the epidermal growth factor receptor.",published,journal,J. Biol. Chem.,,280,25,,,,,,,,,,,,,,,,,,,,,,24043,24052,2005, citations,entry_citation,6580,249206,1,,entry citation,,,16302975,,,"Secondary structure assignment of mouse SOCS3 by NMR defines the domain boundaries and identifies an unstructured insertion in the SH2 domain.",published,journal,FEBS J.,,272,23,,,,,,,,,,,,,,,,,,,,,,6120,6130,2005, citations,entry_citation,6581,249225,1,,entry citation,,,17141806,,,"Solution structure of a Hck SH3 Domain Ligand Complex Reveals Novel Interaction Modes",published,journal,J. Mol. Biol.,,365,5,,,,,,,,,,,,,,,,,,,,,,1517,1532,2007, citations,entry_citation,6582,249260,1,,entry citation,,,16211489,,,Sequential Resonance Assignment of the Human BMP Type II Receptor Extracellular Domain,published,journal,J. Biomol. NMR,,32,4,,,,,,,,,,,,,,,,,,,,,,336,336,2005, citations,entry_citation,6583,249281,1,,entry citation,,,16169012,,,"The Three-dimensional Solution Structure of Ca(2+)-bound S100A1 as Determined by NMR Spectroscopy",published,journal,J. Mol. Biol.,,353,2,,,,,,,,,,,,,,,,,,,,,,410,426,2005, citations,entry_citation,6584,249297,1,,entry citation,,,16211490,,,"Backbone NMR Assignment of the Human E2 Ubiquitin Conjugating Enzyme UbcH5alpha (F72K,F82S) Double Mutant",published,journal,J. Biomol. NMR,,32,4,,,,,,,,,,,,,,,,,,,,,,338,338,2005, citations,entry_citation,6604,249698,1,,entry citation,,,16211495,,,"NMR Assignment of the Apo and Peptide-bound SH2 Domain from the Rous Sarcoma Viral Protein Src",published,journal,J. Biomol. NMR,,32,4,,,,,,,,,,,,,,,,,,,,,,339,339,2005, citations,entry_citation,6744,252320,1,,entry citation,,,16456705,,,"1H, 13C and 15N Resonance Assignments of the C-terminal Domain of RP2",published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,9,9,2006, citations,ref_1,6584,249298,2,,reference citation,,,8090726,,"Scheffner M, Huibregtse JM, Howley PM. Free in PMC Identification of a human ubiquitin-conjugating enzyme that mediates the E6-AP-dependent ubiquitination of p53. Proc Natl Acad Sci U S A. 1994 Sep 13;91(19):8797-801.",Identification of a human ubiquitin-conjugating enzyme that mediates the E6-AP-dependent ubiquitination of p53.,published,journal,Proc. Natl. Acad. Sci. U.S.A.,Proceedings of the National Academy of Sciences of the United States of America,91,19,,0027-8424,,,,,,,,,,,,,,,,,,,,8797,8801,1994,"The E6 protein of the oncogenic human papillomavirus types 16 and 18 facilitates the rapid degradation of the tumor-suppressor protein p53 via the ubiquitin-dependent proteolytic pathway. The E6 protein binds to a cellular protein of 100 kDa termed E6-AP. The complex of E6 and E6-AP specifically interacts with p53 and induces the ubiquitination of p53 in a reaction which requires the ubiquitin-activating enzyme (E1) and a cellular fraction thought to contain a mammalian ubiquitin-conjugating enzyme (E2). This mammalian E2 activity could be replaced with bacterially expressed UBC8 from Arabidopsis thaliana, which belongs to a subfamily of E2s including yeast UBC4 and UBC5 which are highly conserved at the amino acid level. In this paper we describe the cloning of a human cDNA encoding a human E2 that we have designated UbcH5 and that is related to Arabidopsis UBC8 and the other members of this subfamily. We demonstrate that UbcH5 can function in the E6/E6-AP-induced ubiquitination of p53." citations,entry_citation,6585,249318,1,,entry citation,,,,,,"1H, 15N and 13C Resonance Assignments of the Putative Bet v 1 Family Protein At1g24000.1 from Arabidopsis Thaliana",published,journal,J. Biomol. NMR,,32,4,,,,,,,,,,,,,,,,,,,,,,335,335,2005, citations,entry_citation,6586,249341,1,,entry citation,,,16132836,,,"1H, 13C and 15N Backbone Resonance Assignment of the Hsp90 Binding Domain of Human Cdc37",published,journal,J. Biomol. NMR,,32,3,,,,,,,,,,,,,,,,,,,,,,262,262,2005, citations,entry_citation,6587,249368,1,,entry citation,,,12062424,,"Okon M, Frank PG, Marcel YL, Cushley RJ. Heteronuclear NMR studies of human serum apolipoprotein A-I. Part I. Secondary structure in lipid-mimetic solution. FEBS Lett. 517 (2002) 139-143","Heteronuclear NMR studies of human serum apolipoprotein A-I. Part I. Secondary structure in lipid-mimetic solution",published,journal,FEBS Lett.,,517,1-3,,,,,,,,,,,,,,,,,,,,,,139,143,2002, citations,entry_citation,6588,249381,1,,entry citation,,,11163364,,"Okon M, Frank PG, Marcel YL, Cushley RJ. Secondary structure of human lipoprotein A-I(1-186) in lipid-mimetic solution. FEBS Lett. 487 (2001) 390-396",Secondary structure of human lipoprotein A-I(1-186) in lipid-mimetic solution,published,journal,FEBS Lett.,,487,3,,,,,,,,,,,,,,,,,,,,,,390,396,2001, citations,entry_citation,6589,249392,1,,entry citation,,,16183644,,,Three-dimensional solution structures of the chromodomains of cpSRP43,published,journal,J. Biol. Chem.,,280,50,,,,,,,,,,,,,,,,,,,,,,41465,41471,2005, citations,entry_citation,6590,249406,1,,entry citation,,,,,,"1H, 15N, and 13C Chemical Shift Assignments of the Human Sulfiredoxin (hSrx)",published,journal,J. Biomol. NMR,,32,4,,,,,,,,,,,,,,,,,,,,,,339,339,2005, citations,entry_citation,6591,249429,1,,entry citation,,,16220560,,,"On the Importance of Carbohydrate-Aromatic Interactions for the Molecular Recognition of Oligosaccharides by Proteins: NMR Studies of the Structure and Binding Affinity of AcAMP2-Like Peptides with Non-Natural Napthyl and Fluoroaromatic Residues.",published,journal,Chem. Eur. J.,,11,23,,,,,,,,,,,,,,,,,,,,,,7060,7074,2005, citations,reference-1,6591,249430,2,,reference citation,,,8627629,,"Martins JC, Maes D, Loris R, Pepermans HA, Wyns L, Willem R, Verheyden H NMR study of the solution structure of Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus. J Mol Biol. 1996 May 3;258(2):322-33.","H NMR study of the solution structure of Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus.",published,journal,J. Mol. Biol.,Journal of molecular biology,258,2,,0022-2836,,,,,,,,,,,,,,,,,,,,322,333,1996,"The conformation in water of antimicrobial protein 2 from Amaranthus caudatus (Ac-AMP2) was determined using 1H NMR, DIANA and restrained molecular modeling. Ac-AMP2 is a 30 amino acid residue, lectin-like protein that specifically binds to chitin, a polymer of beta-1,4-N-acetyl-D-glucosamine. After sequence specific resonance assignments, a total of 198 distance restraints were collected from 2D NOESY buildup spectra at 500 MHz at pH 2, supplemented by a 2D NOESY spectrum at 600 MHz. The location of the three previously unassigned disulfide bridges was determined from preliminary DIANA structures, using a statistical analysis of intercystinyl distances. The solution structure of Ac-AMP2 is presented as a set of 26 DIANA structures, further refined by restrained molecular dynamics using a simulated annealing protocol in the AMBER force field, with a backbone r.m.s.d. for the well defined Glu3-Cys28 segment of 0.69(+/-0.12) angstroms. The main structural element is an antiparallel beta-sheet from Met13 to Lys23 including a betaI-turn over Gln17-Phel8 with a beta bulge at Gly19. In addition, a beta'I turn over Arg6-Gly7, a beta'III turn over Ser11-Gly12 and a helical turn from Gly24 to Cys28 are identified. This structure is very similar to the equivalent regions of the X-ray structure of wheat germ agglutinin and the NMR structure of hevein." citations,reference-2,6591,249431,3,,reference citation,,,12144516,,"Muraki M. The importance of CH/pi interactions to the function of carbohydrate binding proteins. Protein Pept Lett. 2002 Jun;9(3):195-209.",The importance of CH/pi interactions to the function of carbohydrate binding proteins.,published,journal,Protein Pept. Lett.,Protein and peptide letters,9,3,,0929-8665,,,,,,,,,,,,,,,,,,,,195,209,2002,"It is suggested that the interactions between the hydrophobic C-H groups of carbohydrate residues and the pi-electron systems of aromatic amino-acid residues play an important role in the ligand-recognition function of carbohydrate-binding proteins. This review focuses on our recent structural and functional studies of human lysozyme and hevein-domain type lectins (wheat-germ agglutinin and Ac-AMP2) aimed at understanding how CH/pi interactions are involved in the actual binding events." citations,entry_citation,660,249613,1,,entry citation,,,,,"van Mierlo, Carlo P.M., Muller, Franz, Vervoort, Jacques, ""Secondary and tertiary structure characteristics of Megasphaera elsdenii flavodoxin in the reduced state as determined by two-dimensional 1H NMR,"" Eur. J. Biochem. 189, 589-600 (1990).","Secondary and tertiary structure characteristics of Megasphaera elsdenii flavodoxin in the reduced state as determined by two-dimensional 1H NMR",published,journal,Eur. J. Biochem.,,189,,,,,,,,,,,,,,,,,,,,,,,589,600,1990, citations,entry_citation,6600,249626,1,,entry citation,,,16699181,,,"Identification and solution structures of a single-domain biotin/lipoyl attachment protein from bacillus subtilis",published,journal,J. Biol. Chem.,,281,29,,,,,,,,,,,,,,,,,,,,,,20598,20607,2006, citations,entry_citation,6601,249646,1,,entry citation,,,16516208,,,"NMR solution structure and characterization of substrate binding site of the PPIase domain of PrsA protein from Bacillus subtilis",published,journal,FEBS Lett.,,580,7,,,,,,,,,,,,,,,,,,,,,,1822,1826,2006, citations,Citation_1,6602,249662,1,,entry citation,,,16222566,,,"Backbone 1H, 13C, and 15N Resonance Assignment of the 46 kDa Dimeric GAF A Domain of Phosphodiesterase 5",published,journal,J. Biomol. NMR,,33,1,,,,,,,,,,,,,,,,,,,,,,75,75,2005, citations,reference-3,6591,249432,4,,reference citation,,,15368576,,"Aboitiz N, Vila-Perello M, Groves P, Asensio JL, Andreu D, Canada FJ, Jimenez-Barbero J. NMR and modeling studies of protein-carbohydrate interactions: synthesis, three-dimensional structure, and recognition properties of a minimum hevein domain with binding affinity for chitooligosaccharides. Chembiochem. 2004 Sep 6;5(9):1245-55.","NMR and modeling studies of protein-carbohydrate interactions: synthesis, three-dimensional structure, and recognition properties of a minimum hevein domain with binding affinity for chitooligosaccharides.",published,journal,Chembiochem,Chembiochem : a European journal of chemical biology,5,9,,1439-4227,,,,,,,,,,,,,,,,,,,,1245,1255,2004,"HEV32, a 32-residue, truncated hevein lacking eleven C-terminal amino acids, was synthesized by solid-phase methodology and correctly folded with three cysteine bridge pairs. The affinities of HEV32 for small chitin fragments--in the forms of N,N',N""-triacetylchitotriose ((GlcNAc)3) (millimolar) and N,N',N"",N""',N"""",N""""'-hexaacetylchitohexaose ((GlcNAc)6) (micromolar)--as measured by NMR and fluorescence methods, are comparable with those of native hevein. The HEV32 ligand-binding process is enthalpy driven, while entropy opposes binding. The NMR structure of ligand-bound HEV32 in aqueous solution was determined to be highly similar to the NMR structure of ligand-bound hevein. Solvated molecular-dynamics simulations were performed in order to monitor the changes in side-chain conformation of the binding site of HEV32 and hevein upon interaction with ligands. The calculations suggest that the Trp21 side-chain orientation of HEV32 in the free form differs from that in the bound state; this agrees with fluorescence and thermodynamic data. HEV32 provides a simple molecular model for studying protein-carbohydrate interactions and for understanding the physiological relevance of small native hevein domains lacking C-terminal residues." citations,reference-4,6591,249433,5,,reference citation,,,10842338,,"Asensio JL, Siebert HC, von Der Lieth CW, Laynez J, Bruix M, Soedjanaamadja UM, Beintema JJ, Canada FJ, Gabius HJ, Jimenez-Barbero J. NMR investigations of protein-carbohydrate interactions: studies on the relevance of Trp/Tyr variations in lectin binding sites as deduced from titration microcalorimetry and NMR studies on hevein domains. Determination of the NMR structure of the complex between pseudohevein and N,N',N""-triacetylchitotriose. Proteins. 2000 Aug 1;40(2):218-36.","NMR investigations of protein-carbohydrate interactions: studies on the relevance of Trp/Tyr variations in lectin binding sites as deduced from titration microcalorimetry and NMR studies on hevein domains. Determination of the NMR structure of the complex between pseudohevein and N,N',N""-triacetylchitotriose.",published,journal,Proteins,Proteins,40,2,,0887-3585,,,,,,,,,,,,,,,,,,,,218,236,2000,"Model studies on lectins and their interactions with carbohydrate ligands in solution are essential to gain insights into the driving forces for complex formation and to optimize programs for computer simulations. The specific interaction of pseudohevein with N,N', N""-triacetylchitotriose has been analyzed by (1)H-NMR spectroscopy. Because of its small size, with a chain length of 45 amino acids, this lectin is a prime target to solution-structure determination by NOESY NMR experiments in water. The NMR-analysis was extended to assessment of the topology of the complex between pseudohevein and N, N',N""-triacetylchitotriose. NOESY experiments in water solution provided 342 protein proton-proton distance constraints. Binding of the ligand did not affect the pattern of the protein nuclear Overhauser effect signal noticeably, what would otherwise be indicative of a ligand-induced conformational change. The average backbone (residues 3-41) RMSD of the 20 refined structures was 1.14 A, whereas the heavy atom RMSD was 2.18 A. Two different orientations of the trisaccharide within the pseudohevein binding site are suggested, furnishing an explanation in structural terms for the lectin's capacity to target chitin. In both cases, hydrogen bonds and van der Waals contacts confer stability to the complexes. This conclusion is corroborated by the thermodynamic parameters of binding determined by NMR and isothermal titration calorimetry. The association process was enthalpically driven. In relation to hevein, the Trp/Tyr-substitution in the binding pocket has only a small effect on the free energy of binding in contrast to engineered galectin-1 and a mammalian C-type lectin. A comparison of the three-dimensional structure of pseudohevein in solution to those reported for wheat germ agglutinin (WGA) in the solid state and for hevein and WGA-B in solution has been performed, providing a data source about structural variability of the hevein domains. The experimentally derived structures and the values of the solvent accessibilities for several key residues have also been compared with conformations obtained by molecular dynamics simulations, pointing to the necessity to further refine the programs to enhance their predictive reliability and, thus, underscoring the importance of this kind of combined analysis in model systems." citations,reference-5,6591,249434,6,,reference citation,,,10903932,,"Asensio JL, Canada FJ, Siebert HC, Laynez J, Poveda A, Nieto PM, Soedjanaamadja UM, Gabius HJ, Jimenez-Barbero J. Structural basis for chitin recognition by defense proteins: GlcNAc residues are bound in a multivalent fashion by extended binding sites in hevein domains. Chem Biol. 2000 Jul;7(7):529-43.",Structural basis for chitin recognition by defense proteins: GlcNAc residues are bound in a multivalent fashion by extended binding sites in hevein domains.,published,journal,Chem. Biol.,Chemistry & biology,7,7,,1074-5521,,,,,,,,,,,,,,,,,,,,529,543,2000,"BACKGROUND: Many plants respond to pathogenic attack by producing defense proteins that are capable of reversible binding to chitin, a polysaccharide present in the cell wall of fungi and the exoskeleton of insects. Most of these chitin-binding proteins include a common structural motif of 30 to 43 residues organized around a conserved four-disulfide core, known as the 'hevein domain' or 'chitin-binding' motif. Although a number of structural and thermodynamic studies on hevein-type domains have been reported, these studies do not clarify how chitin recognition is achieved. RESULTS: The specific interaction of hevein with several (GlcNAc)(n) oligomers has been studied using nuclear magnetic resonance (NMR), analytical ultracentrifugation and isothermal titration microcalorimetry (ITC). The data demonstrate that hevein binds (GlcNAc)(2-4) in 1:1 stoichiometry with millimolar affinity. In contrast, for (GlcNAc)(5), a significant increase in binding affinity is observed. Analytical ultracentrifugation studies on the hevein-(GlcNAc)(5,8) interaction allowed detection of protein-carbohydrate complexes with a ratio of 2:1 in solution. NMR structural studies on the hevein-(GlcNAc)(5) complex showed the existence of an extended binding site with at least five GlcNAc units directly involved in protein-sugar contacts. CONCLUSIONS: The first detailed structural model for the hevein-chitin complex is presented on the basis of the analysis of NMR data. The resulting model, in combination with ITC and analytical ultracentrifugation data, conclusively shows that recognition of chitin by hevein domains is a dynamic process, which is not exclusively restricted to the binding of the nonreducing end of the polymer as previously thought. This allows chitin to bind with high affinity to a variable number of protein molecules, depending on the polysaccharide chain length. The biological process is multivalent." citations,reference-6,6591,249435,7,,reference citation,,,10877847,,"Muraki M, Morii H, Harata K. Chemically prepared hevein domains: effect of C-terminal truncation and the mutagenesis of aromatic residues on the affinity for chitin. Protein Eng. 2000 Jun;13(6):385-9.",Chemically prepared hevein domains: effect of C-terminal truncation and the mutagenesis of aromatic residues on the affinity for chitin.,published,journal,Protein Eng.,Protein engineering,13,6,,0269-2139,,,,,,,,,,,,,,,,,,,,385,389,2000,"Chemically prepared hevein domains (HDs), N-terminal domain of an antifungal protein from Nicotiana tabacum (CBP20-N) and an antimicrobial peptide from Amaranthus caudatus (Ac-AMP2), were examined for their affinity for chitin, a beta-1,4-linked polymer of N-acetylglucosamine. An intact binding domain, CBP20-N, showed a higher affinity than a C-terminal truncated domain, Ac-AMP2. The formation of a pyroglutamate residue from N-terminal Gln of CBP20-N increased the affinity. The single replacement of any aromatic residue of Ac-AMP2 with Ala resulted in a significant reduction in affinity, suggesting the importance of the complete set of three aromatic residues in the ligand binding site. The mutations of Phe18 of Ac-AMP2 to the residues with larger aromatic rings, i.e. Trp, beta-(1-naphthyl)alanine or beta-(2-naphthyl)alanine, enhanced the affinity, whereas the mutation of Tyr20 to Trp reduced the affinity. The affinity of an HD for chitin might be improved by adjusting the size and substituent group of stacking aromatic rings." citations,entry_citation,6592,249459,1,,entry citation,,,16183644,,,Three-dimensional solution structures of the chromodomains of cpSRP43,published,journal,J. Biol. Chem.,,280,50,,,,,,,,,,,,,,,,,,,,,,41465,41471,2005, citations,entry_citation,6593,249473,1,,entry citation,,,16183644,,,Three-dimensional solution structures of the chromodomains of cpSRP43,published,journal,J. Biol. Chem.,,280,50,,,,,,,,,,,,,,,,,,,,,,41465,41471,2005, citations,entry_citation,6594,249487,1,,entry citation,,,,,,A high-resolution solution structure of a trypanosomatid FYVE domain,published,journal,Protein Sci.,,16,11,,,,,,,,,,,,,,,,,,,,,,2552,2559,2007, citations,entry_citation,6596,249513,1,,entry citation,,,15824119,,,"Isolation and characterisation of novel cyclotides from Viola hederaceae: solution structure and anti-HIV activity of vhl-1, a leaf-specific-expressed cyclotide",published,journal,J. Biol. Chem.,,280,23,,,,,,,,,,,,,,,,,,,,,,22395,22405,2005, citations,entry_citation,6597,249530,1,,entry citation,,,16181639,,,"Structural Basis of ARNT PAS-B Dimerization: Use of a Common Beta-sheet Interface for Hetero- and Homodimerization.",published,journal,J. Mol. Biol.,,353,3,,,,,,,,,,,,,,,,,,,,,,664,677,2005, citations,entry_citation,6598,249559,1,,entry citation,,,16388591,,,"NMR Solution Structure of the Peptide Fragment 1-30, Derived from Unprocessed Mouse Doppel Protein, in DHPC Micelles",published,journal,Biochemistry,,45,1,,,,,,,,,,,,,,,,,,,,,,159,166,2006, citations,entry_citation,6599,249576,1,,entry citation,,,16699181,,,"Identification and solution structures of a single-domain biotin/lipoyl attachment protein from bacillus subtilis",published,journal,J. Biol. Chem.,,281,29,,,,,,,,,,,,,,,,,,,,,,20598,20607,2006, citations,entry_citation,66,249600,1,,entry citation,,,,,"Keller, Regula M., Baumann, Rudolf, Hunziker-Kwik, Eng-Hiang, Joubert, Francois J., Wuthrich, Kurt, ""Assignment of the 1H Nuclear Magnetic Resonance Spectrum of the Trypsin Inhibitor Homologue K from Dendroaspis polylepis polylepis. Two-dimensional Nuclear Magnetic Resonance at 360 and 500 MHz.,"" J. Mol. Biol. 163, 623-646 (1983).","Assignment of the 1H Nuclear Magnetic Resonance Spectrum of the Trypsin Inhibitor Homologue K from Dendroaspis polylepis polylepis. Two-dimensional Nuclear Magnetic Resonance at 360 and 500 MHz.",published,journal,J. Mol. Biol.,,163,,,,,,,,,,,,,,,,,,,,,,,623,646,1983, citations,entry_citation,6603,249686,1,,entry citation,,,,,,NMR Assignment of New Thioredoxin-like Protein YkuV from Bacillus subtilis,published,journal,J. Biomol. NMR,,32,3,,,,,,,,,,,,,,,,,,,,,,258,258,2005, citations,citation_1,7050,257512,1,,entry citation,,,,,,"Solution structure of growth-blocking peptide of the cabbage armyworm, Mamestra brassicae",published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citation,6605,249716,1,,entry citation,,,16209950,,,"A Methylation-Dependent Electrostatic Switch Controls DNA Repair and Transcriptional Activation by E. coli Ada",published,journal,Mol Cell,,20,1,,,,,,,,,,,,,,,,,,,,,,117,129,2005, citations,entry_citation,6606,249740,1,,entry citation,,,16222565,,,NMR Assignment of the DNA Binding Domain A of RPA from S. cerevisiae,published,journal,J. Biomol. NMR,,33,1,,,,,,,,,,,,,,,,,,,,,,75,75,2005, citations,citation,6607,249756,1,,entry citation,,,16222563,,,"1H, 13C and 15N Resonance Assignments of the AT-Rich Interaction Domain (ARID) of Jumonji",published,journal,J. Biomol. NMR,,33,1,,,,,,,,,,,,,,,,,,,,,,74,74,2005, citations,entry_citation,6608,249770,1,,entry citation,,,16300399,,,"Solution structure and interaction of the antimicrobial polyphemusins with lipid membranes",published,journal,Biochemistry,,44,47,,,,,,,,,,,,,,,,,,,,,,15504,15513,2005, citations,entry_citation,6609,249783,1,,entry citation,,,15987890,,,"Solution structure of the ubiquitin-like domain of human DC-UbP from dendritic cells.",published,journal,Protein Sci.,,14,8,,,,,,,,,,,,,,,,,,,,,,2044,2050,2005, citations,entry_citation,661,249805,1,,entry citation,,,,,"Ribeiro, A.A., Wemmer, David, Bray, R.C., Jardetzky, Oleg, ""A Folded Structure for the Lac-Repressor Headpiece,"" Biochem. Biophys. Res. Commun. 99 (2), 668-674 (1981).",A Folded Structure for the Lac-Repressor Headpiece,published,journal,Biochem. Biophys. Res. Commun.,,99,2,,,,,,,,,,,,,,,,,,,,,,668,674,1981, citations,citation_1,6610,249818,1,,entry citation,,,16211491,,,"1H, 15N and 13C Resonance Assignments of a Protein Involved in the Autophagy Process, At4g21980.1 from Arabidopsis thaliana",published,journal,J. Biomol. NMR,,32,4,,,,,,,,,,,,,,,,,,,,,,337,337,2005, citations,entry_citation,6611,249831,1,,entry citation,,,,,,"1H, 13C, and 15N chemical shift assignments of the receiver domain of NtrC4 from Aquifex aeolicus",submitted,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6612,249848,1,,entry citation,,,15953616,,,"Structure of free MDM2 N-terminal domain reveals conformational adjustments that accompany p53-binding.",published,journal,J. Mol. Biol.,,350,3,,,,,,,,,,,,,,,,,,,,,,587,598,2005, citations,entry_citation,6613,249865,1,,entry citation,,,16415022,,,"Structure and dynamics of coxsackievirus B4 2A proteinase, an enzyme involved in the etiology of heart disease",published,journal,J. Virol.,,80,3,,,,,,,,,,,,,,,,,,,,,,1451,1462,2006, citations,entry_citation,6615,249888,1,,entry citation,,,19636865,,,"(1)H, (13)C and (15)N resonance assignments of alpha-domain for Bacillus subtilis Lon protease",published,journal,Biomol. NMR Assignments,,1,2,,,,,,,,,,,,,,,,,,,,,,201,203,2007, citations,citations,6616,249902,1,,entry citation,,,16460023,,,"Lytic Activity and Structural Differences of Amphipathic Peptides Derived from Trialysin",published,journal,Biochemistry,,45,6,,,,,,,,,,,,,,,,,,,,,,1765,1774,2006, citations,entry_citation,6617,249919,1,,entry citation,,,16211490,,,"Backbone NMR Assignment of the C-terminal Haemopexin-like Domain (HPLD) of Human Matrix Metalloproteinase MMP-13",published,journal,J. Biomol. NMR,,32,4,,,,,,,,,,,,,,,,,,,,,,337,337,2005, citations,reference_citation,6617,249920,2,,reference citation,,,8969305,,,"The helping hand of collagenase-3 (MMP-13): 2.7 A crystal structure of its C-terminal haemopexin-like domain",published,journal,J. Mol. Biol.,,264,3,,,,,,,,,,,,,,,,,,,,,,556,566,1996, citations,citations,6618,249936,1,,entry citation,,,16460023,,,"Lytic Activity and Structural Differences of Amphipathic Peptides Derived from Trialysin",published,journal,Biochemistry,,45,6,,,,,,,,,,,,,,,,,,,,,,1765,1774,2006, citations,citations,6619,249954,1,,entry citation,,,16460023,,,"Lytic Activity and Structural Differences of Amphipathic Peptides Derived from Trialysin",published,journal,Biochemistry,,45,6,,,,,,,,,,,,,,,,,,,,,,1765,1774,2006, citations,entry_citation,662,249971,1,,entry citation,,,,,"Seigneuret, Michel, Neumann, Jean-Michel, Levy, Daniel, Rigaud, Jean-Louis, ""High-Resolution 13C-NMR Study of the Topography and Dynamics of Methionine Residues in Detergent-Solubilized Bacteriorhodopsin,"" Biochemistry 30, 3885-3892 (1991).","High-Resolution 13C-NMR Study of the Topography and Dynamics of Methionine Residues in Detergent-Solubilized Bacteriorhodopsin",published,journal,Biochemistry,,30,,,,,,,,,,,,,,,,,,,,,,,3885,3892,1991, citations,entry_citation,6620,249985,1,,entry citation,,,16905545,,,The first structure from the soul/HBP family of heme binding proteins: Murine P22HBP.,published,journal,J. Biol. Chem,,281,42,,,,,,,,,,,,,,,,,,,,,,31553,31561,2006, citations,reference,6620,249986,2,,reference citation,,,16211492,,Journal of Biomolecular NMR,"1H, 15N and 13C Resonance Assignments of the Heme-binding Protein Murine p22HBP",published,journal,J. Biomol. NMR,,32,4,,,,,,,,,,,,,,,,,,,,,,338,338,2005, citations,entry_citation,6621,250017,1,,entry citation,,,16132828,,,"1H, 15N, and 13C Resonance Assignments of Human Interleukin-2",published,journal,J. Biomol. NMR,,32,3,,,,,,,,,,,,,,,,,,,,,,258,258,2005, citations,entry_citation,6622,250031,1,,entry citation,,,,,,"Heterologous expression of hen egg white lysozyme and resonance assignment of tryptophan side chains in its non-native states",published,journal,J. Biomol. NMR,,33,2,,,,,,,,,,,,,,,,,,,,,,95,104,2005, citations,citation_1,6623,250046,1,,entry citation,,,16098208,,,Solution Structure of Human Proinsulin C-Peptide,published,journal,FEBS J.,,272,16,,,,,,,,,,,,,,,,,,,,,,4284,4293,2005, citations,entry_citation,6624,250063,1,,entry citation,,,16258837,,,"Backbone 1H, 13C, and 15N Resonance Assignments for the two 13 kD Ras Associating Domains (RA1 and RA2) from Phospholipase C(epsilon)",published,journal,J. Biomol. NMR,,33,2,,,,,,,,,,,,,,,,,,,,,,138,138,2005, citations,entry_citation,6625,250080,1,,entry citation,,,19636872,,,"(1)H, (13)C, and (15)N resonance assignments of human phosphohistidine phosphatase 1 (PHPT1)",published,journal,Biomol. NMR Assignments,,1,2,,,,,,,,,,,,,,,,,,,,,,229,231,2007, citations,entry_citation,6626,250093,1,,entry citation,,,,,,"1H, 13C and 15N Resonance Assignments of the Cytosolic Domain of Tom20 from Arabidopsis thaliana",published,journal,J. Biomol. NMR,,33,3,,,,,,,,,,,,,,,,,,,,,,198,198,2005, citations,entry_citation,6627,250124,1,,entry citation,,,16817894,,,Conformation and mode of membrane interaction in cyclotides,published,journal,FEBS J.,,273,12,,,,,,,,,,,,,,,,,,,,,,2658,2672,2006, citations,citation_1,6628,250143,1,,entry citation,,,15933069,,,Specificity and mechanism of the histone methyltransferase Pr-Set7,published,journal,Genes Dev.,,19,12,,,,,,,,,,,,,,,,,,,,,,1444,1454,2005, citations,entry_citation,6629,250156,1,,entry citation,,,15920478,,,"Structural basis of chaperone-subunit complex recognition by type 1 pilus assembly platform FimD",published,journal,EMBO J.,,24,12,,,,,,,,,,,,,,,,,,,,,,2075,2086,2005, citations,entry_citation,6631,250173,1,,entry citation,,,,,,Solution structure of a human ubiquitin-like domain in SF3A1,submitted,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6633,250193,1,,entry citation,,,15907937,,,Structure of the RNA Signal Essential for Translational Frameshifting in HIV-1,published,journal,J. Mol. Biol.,,349,5,,,,,,,,,,,,,,,,,,,,,,1024,1035,2005, citations,entry_citation,6634,250223,1,,entry citation,,,16527248,,,"Solution structures of tetrahaem ferricytochrome c(3) from Desulfovibrio vulgaris (Hildenborough) and its K45Q mutant: The molecular basis of cooperativity",published,journal,Biochim. Biophys. Acta.,,1757,2,,,,,,,,,,,,,,,,,,,,,,143,153,2006, citations,citation_1,6634,250224,2,,reference citation,,,9724528,,"Ligia M. Saraiva, Carlos A. Salgueiro, Patricia N. da Costa, Ana C. Messias, Jean LeGall, Walter M. A. M. van Dongen and Antonio V. Xavier (1998) Biochemistry, 37, 12160-12165, ""Replacement of Lysine 45 by uncharged residues modulates the redox-Bohr effect in tetraheme cytochrome c3 of Desulfovibrio vulgaris (Hildenborough)"".",Replacement of lysine 45 by uncharged residues modulates the redox-Bohr effect in tetraheme cytochrome c3 of Desulfovibrio vulgaris (Hildenborough).,published,journal,Biochemistry,Biochemistry,37,35,,0006-2960,,,,,,,,,,,,,,,,,,,,12160,12165,1998,"The structural basis for the pH dependence of the redox potential in the tetrahemic Desulfovibrio vulgaris (Hildenborough) cytochrome c3 was investigated by site-directed mutagenesis of charged residues in the vicinity of heme I. Mutation of lysine 45, located in the neighborhood of the propionates of heme I, by uncharged residues, namely threonine, glutamine and leucine, was performed. The replacement of a conserved charged residue, aspartate 7, present in the N-terminal region and near heme I was also attempted. The analysis of the redox interactions as well as the redox-Bohr behavior of the mutated cytochromes c3 allowed the conclusion that residue 45 has a functional role in the control of the pKa of the propionate groups of heme I and confirms the involvement of this residue in the redox-Bohr effect." citations,entry_citation,6635,250247,1,,entry citation,,,16258837,,,"Backbone 1H, 13C, and 15N Resonance Assignments for the two 13 kD Ras Associating Domains (RA1 and RA2) from Phospholipase C(epsilon)",published,journal,J. Biomol. NMR,,33,2,,,,,,,,,,,,,,,,,,,,,,138,138,2005, citations,entry_citation,6636,250267,1,,entry citation,,,,,,"Solution structure of PcFK1, a spider peptide active against Plasmodium falciparum.",published,journal,Protein Sci.,,,,,,,,,,,,,,,,,,,,,,,,,,,2006, citations,entry_citation,6637,250286,1,,entry citation,,,16220560,,,"On the Importance of Carbohydrate-Aromatic Interactions for the Molecular Recognition of Oligosaccharides by Proteins: NMR Studies of the Structure and Binding Affinity of AcAMP2-Like Peptides with Non-Natural Napthyl and Fluoroaromatic Residues.",published,journal,Chem. Eur. J.,,11,23,,,,,,,,,,,,,,,,,,,,,,7060,7074,2005, citations,reference-1,6637,250287,2,,reference citation,,,8627629,,"Martins JC, Maes D, Loris R, Pepermans HA, Wyns L, Willem R, Verheyden P. H NMR study of the solution structure of Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus. J Mol Biol. 1996 May 3;258(2):322-33.","H NMR study of the solution structure of Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus.",published,journal,J. Mol. Biol.,Journal of molecular biology,258,2,,0022-2836,,,,,,,,,,,,,,,,,,,,322,333,1996,"The conformation in water of antimicrobial protein 2 from Amaranthus caudatus (Ac-AMP2) was determined using 1H NMR, DIANA and restrained molecular modeling. Ac-AMP2 is a 30 amino acid residue, lectin-like protein that specifically binds to chitin, a polymer of beta-1,4-N-acetyl-D-glucosamine. After sequence specific resonance assignments, a total of 198 distance restraints were collected from 2D NOESY buildup spectra at 500 MHz at pH 2, supplemented by a 2D NOESY spectrum at 600 MHz. The location of the three previously unassigned disulfide bridges was determined from preliminary DIANA structures, using a statistical analysis of intercystinyl distances. The solution structure of Ac-AMP2 is presented as a set of 26 DIANA structures, further refined by restrained molecular dynamics using a simulated annealing protocol in the AMBER force field, with a backbone r.m.s.d. for the well defined Glu3-Cys28 segment of 0.69(+/-0.12) angstroms. The main structural element is an antiparallel beta-sheet from Met13 to Lys23 including a betaI-turn over Gln17-Phel8 with a beta bulge at Gly19. In addition, a beta'I turn over Arg6-Gly7, a beta'III turn over Ser11-Gly12 and a helical turn from Gly24 to Cys28 are identified. This structure is very similar to the equivalent regions of the X-ray structure of wheat germ agglutinin and the NMR structure of hevein." citations,reference-2,6637,250288,3,,reference citation,,,12144516,,"Muraki M. The importance of CH/pi interactions to the function of carbohydrate binding proteins. Protein Pept Lett. 2002 Jun;9(3):195-209.",The importance of CH/pi interactions to the function of carbohydrate binding proteins.,published,journal,Protein Pept. Lett.,Protein and peptide letters,9,3,,0929-8665,,,,,,,,,,,,,,,,,,,,195,209,2002,"It is suggested that the interactions between the hydrophobic C-H groups of carbohydrate residues and the pi-electron systems of aromatic amino-acid residues play an important role in the ligand-recognition function of carbohydrate-binding proteins. This review focuses on our recent structural and functional studies of human lysozyme and hevein-domain type lectins (wheat-germ agglutinin and Ac-AMP2) aimed at understanding how CH/pi interactions are involved in the actual binding events." citations,reference-3,6637,250289,4,,reference citation,,,15368576,,"Aboitiz N, Vila-Perello M, Groves P, Asensio JL, Andreu D, Canada FJ, Jimenez-Barbero J. NMR and modeling studies of protein-carbohydrate interactions: synthesis, three-dimensional structure, and recognition properties of a minimum hevein domain with binding affinity for chitooligosaccharides. Chembiochem. 2004 Sep 6;5(9):1245-55.","NMR and modeling studies of protein-carbohydrate interactions: synthesis, three-dimensional structure, and recognition properties of a minimum hevein domain with binding affinity for chitooligosaccharides.",published,journal,Chembiochem,Chembiochem : a European journal of chemical biology,5,9,,1439-4227,,,,,,,,,,,,,,,,,,,,1245,1255,2004,"HEV32, a 32-residue, truncated hevein lacking eleven C-terminal amino acids, was synthesized by solid-phase methodology and correctly folded with three cysteine bridge pairs. The affinities of HEV32 for small chitin fragments--in the forms of N,N',N""-triacetylchitotriose ((GlcNAc)3) (millimolar) and N,N',N"",N""',N"""",N""""'-hexaacetylchitohexaose ((GlcNAc)6) (micromolar)--as measured by NMR and fluorescence methods, are comparable with those of native hevein. The HEV32 ligand-binding process is enthalpy driven, while entropy opposes binding. The NMR structure of ligand-bound HEV32 in aqueous solution was determined to be highly similar to the NMR structure of ligand-bound hevein. Solvated molecular-dynamics simulations were performed in order to monitor the changes in side-chain conformation of the binding site of HEV32 and hevein upon interaction with ligands. The calculations suggest that the Trp21 side-chain orientation of HEV32 in the free form differs from that in the bound state; this agrees with fluorescence and thermodynamic data. HEV32 provides a simple molecular model for studying protein-carbohydrate interactions and for understanding the physiological relevance of small native hevein domains lacking C-terminal residues." citations,ref_nmrview,6651,250583,1,,reference citation,,,,,"Johnson, B. A., and Blevins, R.A. (1994), Journal of Biomolecular NMR, 4:603-614.",NMRView: A computer program for the visualization and analysis of NMR data,published,journal,J. Biomol. NMR,,4,5,,,,,,,,,,,,,,,,,,,,,,603,614,1994, citations,nmrpipe_ref,6651,250584,2,,reference citation,,,,,,NMRPipe: A multidimensional spectral processong system based on UNIX pipes,published,journal,J. Biomol. NMR,,6,3,,,,,,,,,,,,,,,,,,,,,,277,293,1995, citations,entry_citation,6651,250585,3,,entry citation,,,16170802,,,Model peptides mimic the structure and function of the N-terminus of the pore-forming toxin sticholysin II,published,journal,Biopolymers,,84,2,,,,,,,,,,,,,,,,,,,,,,169,180,2006, citations,reference-4,6637,250290,5,,reference citation,,,10842338,,"Asensio JL, Siebert HC, von Der Lieth CW, Laynez J, Bruix M, Soedjanaamadja UM, Beintema JJ, Canada FJ, Gabius HJ, Jimenez-Barbero J. NMR investigations of protein-carbohydrate interactions: studies on the relevance of Trp/Tyr variations in lectin binding sites as deduced from titration microcalorimetry and NMR studies on hevein domains. Determination of the NMR structure of the complex between pseudohevein and N,N',N""-triacetylchitotriose. Proteins. 2000 Aug 1;40(2):218-36.","NMR investigations of protein-carbohydrate interactions: studies on the relevance of Trp/Tyr variations in lectin binding sites as deduced from titration microcalorimetry and NMR studies on hevein domains. Determination of the NMR structure of the complex between pseudohevein and N,N',N""-triacetylchitotriose.",published,journal,Proteins,Proteins,40,2,,0887-3585,,,,,,,,,,,,,,,,,,,,218,236,2000,"Model studies on lectins and their interactions with carbohydrate ligands in solution are essential to gain insights into the driving forces for complex formation and to optimize programs for computer simulations. The specific interaction of pseudohevein with N,N', N""-triacetylchitotriose has been analyzed by (1)H-NMR spectroscopy. Because of its small size, with a chain length of 45 amino acids, this lectin is a prime target to solution-structure determination by NOESY NMR experiments in water. The NMR-analysis was extended to assessment of the topology of the complex between pseudohevein and N, N',N""-triacetylchitotriose. NOESY experiments in water solution provided 342 protein proton-proton distance constraints. Binding of the ligand did not affect the pattern of the protein nuclear Overhauser effect signal noticeably, what would otherwise be indicative of a ligand-induced conformational change. The average backbone (residues 3-41) RMSD of the 20 refined structures was 1.14 A, whereas the heavy atom RMSD was 2.18 A. Two different orientations of the trisaccharide within the pseudohevein binding site are suggested, furnishing an explanation in structural terms for the lectin's capacity to target chitin. In both cases, hydrogen bonds and van der Waals contacts confer stability to the complexes. This conclusion is corroborated by the thermodynamic parameters of binding determined by NMR and isothermal titration calorimetry. The association process was enthalpically driven. In relation to hevein, the Trp/Tyr-substitution in the binding pocket has only a small effect on the free energy of binding in contrast to engineered galectin-1 and a mammalian C-type lectin. A comparison of the three-dimensional structure of pseudohevein in solution to those reported for wheat germ agglutinin (WGA) in the solid state and for hevein and WGA-B in solution has been performed, providing a data source about structural variability of the hevein domains. The experimentally derived structures and the values of the solvent accessibilities for several key residues have also been compared with conformations obtained by molecular dynamics simulations, pointing to the necessity to further refine the programs to enhance their predictive reliability and, thus, underscoring the importance of this kind of combined analysis in model systems." citations,reference-5,6637,250291,6,,reference citation,,,10903932,,"Asensio JL, Canada FJ, Siebert HC, Laynez J, Poveda A, Nieto PM, Soedjanaamadja UM, Gabius HJ, Jimenez-Barbero J. Structural basis for chitin recognition by defense proteins: GlcNAc residues are bound in a multivalent fashion by extended binding sites in hevein domains. Chem Biol. 2000 Jul;7(7):529-43.",Structural basis for chitin recognition by defense proteins: GlcNAc residues are bound in a multivalent fashion by extended binding sites in hevein domains.,published,journal,Chem. Biol.,Chemistry & biology,7,7,,1074-5521,,,,,,,,,,,,,,,,,,,,529,543,2000,"BACKGROUND: Many plants respond to pathogenic attack by producing defense proteins that are capable of reversible binding to chitin, a polysaccharide present in the cell wall of fungi and the exoskeleton of insects. Most of these chitin-binding proteins include a common structural motif of 30 to 43 residues organized around a conserved four-disulfide core, known as the 'hevein domain' or 'chitin-binding' motif. Although a number of structural and thermodynamic studies on hevein-type domains have been reported, these studies do not clarify how chitin recognition is achieved. RESULTS: The specific interaction of hevein with several (GlcNAc)(n) oligomers has been studied using nuclear magnetic resonance (NMR), analytical ultracentrifugation and isothermal titration microcalorimetry (ITC). The data demonstrate that hevein binds (GlcNAc)(2-4) in 1:1 stoichiometry with millimolar affinity. In contrast, for (GlcNAc)(5), a significant increase in binding affinity is observed. Analytical ultracentrifugation studies on the hevein-(GlcNAc)(5,8) interaction allowed detection of protein-carbohydrate complexes with a ratio of 2:1 in solution. NMR structural studies on the hevein-(GlcNAc)(5) complex showed the existence of an extended binding site with at least five GlcNAc units directly involved in protein-sugar contacts. CONCLUSIONS: The first detailed structural model for the hevein-chitin complex is presented on the basis of the analysis of NMR data. The resulting model, in combination with ITC and analytical ultracentrifugation data, conclusively shows that recognition of chitin by hevein domains is a dynamic process, which is not exclusively restricted to the binding of the nonreducing end of the polymer as previously thought. This allows chitin to bind with high affinity to a variable number of protein molecules, depending on the polysaccharide chain length. The biological process is multivalent." citations,entry_citation,6638,250311,1,,entry citation,,,15802216,,,"Expression and characterization of N-terminal domain of Epstein-Barr Virus latent membrane protein 2A in Escherichia coli",published,journal,Protein Expr. Purf.,,41,1,,,,,,,,,,,,,,,,,,,,,,9,17,2005, citations,entry_citation,6639,250325,1,,entry citation,,,16220560,,,"On the Importance of Carbohydrate-Aromatic Interactions for the Molecular Recognition of Oligosaccharides by Proteins: NMR Studies of the Structure and Binding Affinity of AcAMP2-Like Peptides with Non-Natural Napthyl and Fluoroaromatic Residues.",published,journal,Chem. Eur. J.,,11,23,,,,,,,,,,,,,,,,,,,,,,7060,7074,2005, citations,reference-1,6639,250326,2,,reference citation,,,8627629,,"Martins JC, Maes D, Loris R, Pepermans HA, Wyns L, Willem R, Verheyden P. H NMR study of the solution structure of Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus. J Mol Biol. 1996 May 3;258(2):322-33.","H NMR study of the solution structure of Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus.",published,journal,J. Mol. Biol.,Journal of molecular biology,258,2,,0022-2836,,,,,,,,,,,,,,,,,,,,322,333,1996,"The conformation in water of antimicrobial protein 2 from Amaranthus caudatus (Ac-AMP2) was determined using 1H NMR, DIANA and restrained molecular modeling. Ac-AMP2 is a 30 amino acid residue, lectin-like protein that specifically binds to chitin, a polymer of beta-1,4-N-acetyl-D-glucosamine. After sequence specific resonance assignments, a total of 198 distance restraints were collected from 2D NOESY buildup spectra at 500 MHz at pH 2, supplemented by a 2D NOESY spectrum at 600 MHz. The location of the three previously unassigned disulfide bridges was determined from preliminary DIANA structures, using a statistical analysis of intercystinyl distances. The solution structure of Ac-AMP2 is presented as a set of 26 DIANA structures, further refined by restrained molecular dynamics using a simulated annealing protocol in the AMBER force field, with a backbone r.m.s.d. for the well defined Glu3-Cys28 segment of 0.69(+/-0.12) angstroms. The main structural element is an antiparallel beta-sheet from Met13 to Lys23 including a betaI-turn over Gln17-Phel8 with a beta bulge at Gly19. In addition, a beta'I turn over Arg6-Gly7, a beta'III turn over Ser11-Gly12 and a helical turn from Gly24 to Cys28 are identified. This structure is very similar to the equivalent regions of the X-ray structure of wheat germ agglutinin and the NMR structure of hevein." citations,reference-2,6639,250327,3,,reference citation,,,12144516,,"Muraki M. The importance of CH/pi interactions to the function of carbohydrate binding proteins. Protein Pept Lett. 2002 Jun;9(3):195-209.",The importance of CH/pi interactions to the function of carbohydrate binding proteins.,published,journal,Protein Pept. Lett.,Protein and peptide letters,9,3,,0929-8665,,,,,,,,,,,,,,,,,,,,195,209,2002,"It is suggested that the interactions between the hydrophobic C-H groups of carbohydrate residues and the pi-electron systems of aromatic amino-acid residues play an important role in the ligand-recognition function of carbohydrate-binding proteins. This review focuses on our recent structural and functional studies of human lysozyme and hevein-domain type lectins (wheat-germ agglutinin and Ac-AMP2) aimed at understanding how CH/pi interactions are involved in the actual binding events." citations,reference-3,6639,250328,4,,reference citation,,,15368576,,"Aboitiz N, Vila-Perello M, Groves P, Asensio JL, Andreu D, Canada FJ, Jimenez-Barbero J. NMR and modeling studies of protein-carbohydrate interactions: synthesis, three-dimensional structure, and recognition properties of a minimum hevein domain with binding affinity for chitooligosaccharides. Chembiochem. 2004 Sep 6;5(9):1245-55.","NMR and modeling studies of protein-carbohydrate interactions: synthesis, three-dimensional structure, and recognition properties of a minimum hevein domain with binding affinity for chitooligosaccharides.",published,journal,Chembiochem,Chembiochem : a European journal of chemical biology,5,9,,1439-4227,,,,,,,,,,,,,,,,,,,,1245,1255,2004,"HEV32, a 32-residue, truncated hevein lacking eleven C-terminal amino acids, was synthesized by solid-phase methodology and correctly folded with three cysteine bridge pairs. The affinities of HEV32 for small chitin fragments--in the forms of N,N',N""-triacetylchitotriose ((GlcNAc)3) (millimolar) and N,N',N"",N""',N"""",N""""'-hexaacetylchitohexaose ((GlcNAc)6) (micromolar)--as measured by NMR and fluorescence methods, are comparable with those of native hevein. The HEV32 ligand-binding process is enthalpy driven, while entropy opposes binding. The NMR structure of ligand-bound HEV32 in aqueous solution was determined to be highly similar to the NMR structure of ligand-bound hevein. Solvated molecular-dynamics simulations were performed in order to monitor the changes in side-chain conformation of the binding site of HEV32 and hevein upon interaction with ligands. The calculations suggest that the Trp21 side-chain orientation of HEV32 in the free form differs from that in the bound state; this agrees with fluorescence and thermodynamic data. HEV32 provides a simple molecular model for studying protein-carbohydrate interactions and for understanding the physiological relevance of small native hevein domains lacking C-terminal residues." citations,entry_citation,6652,250606,1,,entry citation,,,16002091,,,"RNA Helical Packing in Solution: NMR Structure of a 30kDa GAAA Tetraloop-Receptor Complex.",published,journal,J. Mol. Biol.,,351,2,,,,,,,,,,,,,,,,,,,,,,371,382,2005, citations,Reference_1,6653,250626,1,,reference citation,,,,,,"Zap1p, a metalloregulatory protein involved in zinc-responsive transcriptional regulation in Saccharomyces cerevisiae.",published,journal,Mol. Cell,,17,9,,,,,,,,,,,,,,,,,,,,,,5044,5052,1997, citations,entry_citation,6653,250627,2,,entry citation,,,16483601,,,"Solution Structure of a Zap1 Zinc-responsive Domain Provides Insights into Metalloregulatory Transcriptional Repression in Saccharomyces cerevisiae.",published,journal,J. Mol. Biol.,,357,4,,,,,,,,,,,,,,,,,,,,,,1167,1183,2006, citations,reference-4,6639,250329,5,,reference citation,,,10842338,,"Asensio JL, Siebert HC, von Der Lieth CW, Laynez J, Bruix M, Soedjanaamadja UM, Beintema JJ, Canada FJ, Gabius HJ, Jimenez-Barbero J. NMR investigations of protein-carbohydrate interactions: studies on the relevance of Trp/Tyr variations in lectin binding sites as deduced from titration microcalorimetry and NMR studies on hevein domains. Determination of the NMR structure of the complex between pseudohevein and N,N',N""-triacetylchitotriose. Proteins. 2000 Aug 1;40(2):218-36.","NMR investigations of protein-carbohydrate interactions: studies on the relevance of Trp/Tyr variations in lectin binding sites as deduced from titration microcalorimetry and NMR studies on hevein domains. Determination of the NMR structure of the complex between pseudohevein and N,N',N""-triacetylchitotriose.",published,journal,Proteins,Proteins,40,2,,0887-3585,,,,,,,,,,,,,,,,,,,,218,236,2000,"Model studies on lectins and their interactions with carbohydrate ligands in solution are essential to gain insights into the driving forces for complex formation and to optimize programs for computer simulations. The specific interaction of pseudohevein with N,N', N""-triacetylchitotriose has been analyzed by (1)H-NMR spectroscopy. Because of its small size, with a chain length of 45 amino acids, this lectin is a prime target to solution-structure determination by NOESY NMR experiments in water. The NMR-analysis was extended to assessment of the topology of the complex between pseudohevein and N, N',N""-triacetylchitotriose. NOESY experiments in water solution provided 342 protein proton-proton distance constraints. Binding of the ligand did not affect the pattern of the protein nuclear Overhauser effect signal noticeably, what would otherwise be indicative of a ligand-induced conformational change. The average backbone (residues 3-41) RMSD of the 20 refined structures was 1.14 A, whereas the heavy atom RMSD was 2.18 A. Two different orientations of the trisaccharide within the pseudohevein binding site are suggested, furnishing an explanation in structural terms for the lectin's capacity to target chitin. In both cases, hydrogen bonds and van der Waals contacts confer stability to the complexes. This conclusion is corroborated by the thermodynamic parameters of binding determined by NMR and isothermal titration calorimetry. The association process was enthalpically driven. In relation to hevein, the Trp/Tyr-substitution in the binding pocket has only a small effect on the free energy of binding in contrast to engineered galectin-1 and a mammalian C-type lectin. A comparison of the three-dimensional structure of pseudohevein in solution to those reported for wheat germ agglutinin (WGA) in the solid state and for hevein and WGA-B in solution has been performed, providing a data source about structural variability of the hevein domains. The experimentally derived structures and the values of the solvent accessibilities for several key residues have also been compared with conformations obtained by molecular dynamics simulations, pointing to the necessity to further refine the programs to enhance their predictive reliability and, thus, underscoring the importance of this kind of combined analysis in model systems." citations,reference-5,6639,250330,6,,reference citation,,,10903932,,"Asensio JL, Canada FJ, Siebert HC, Laynez J, Poveda A, Nieto PM, Soedjanaamadja UM, Gabius HJ, Jimenez-Barbero J. Structural basis for chitin recognition by defense proteins: GlcNAc residues are bound in a multivalent fashion by extended binding sites in hevein domains. Chem Biol. 2000 Jul;7(7):529-43.",Structural basis for chitin recognition by defense proteins: GlcNAc residues are bound in a multivalent fashion by extended binding sites in hevein domains.,published,journal,Chem. Biol.,Chemistry & biology,7,7,,1074-5521,,,,,,,,,,,,,,,,,,,,529,543,2000,"BACKGROUND: Many plants respond to pathogenic attack by producing defense proteins that are capable of reversible binding to chitin, a polysaccharide present in the cell wall of fungi and the exoskeleton of insects. Most of these chitin-binding proteins include a common structural motif of 30 to 43 residues organized around a conserved four-disulfide core, known as the 'hevein domain' or 'chitin-binding' motif. Although a number of structural and thermodynamic studies on hevein-type domains have been reported, these studies do not clarify how chitin recognition is achieved. RESULTS: The specific interaction of hevein with several (GlcNAc)(n) oligomers has been studied using nuclear magnetic resonance (NMR), analytical ultracentrifugation and isothermal titration microcalorimetry (ITC). The data demonstrate that hevein binds (GlcNAc)(2-4) in 1:1 stoichiometry with millimolar affinity. In contrast, for (GlcNAc)(5), a significant increase in binding affinity is observed. Analytical ultracentrifugation studies on the hevein-(GlcNAc)(5,8) interaction allowed detection of protein-carbohydrate complexes with a ratio of 2:1 in solution. NMR structural studies on the hevein-(GlcNAc)(5) complex showed the existence of an extended binding site with at least five GlcNAc units directly involved in protein-sugar contacts. CONCLUSIONS: The first detailed structural model for the hevein-chitin complex is presented on the basis of the analysis of NMR data. The resulting model, in combination with ITC and analytical ultracentrifugation data, conclusively shows that recognition of chitin by hevein domains is a dynamic process, which is not exclusively restricted to the binding of the nonreducing end of the polymer as previously thought. This allows chitin to bind with high affinity to a variable number of protein molecules, depending on the polysaccharide chain length. The biological process is multivalent." citations,entry_citation,664,250350,1,,entry citation,,,,,"Williams, Glyn, Moore, Geoffrey R., Porteous, Rod, Robinson, Martin N., Soffe, Nick, Williams, Robert J. P., ""Solution Structure of Mitochondrial Cytochrome c I. H1 Nuclear Magnetic Resonance of Ferricytochrome c,"" J. Mol. Biol. 183, 409-428 (1985).","Solution Structure of Mitochondrial Cytochrome c I. H1 Nuclear Magnetic Resonance of Ferricytochrome c",published,journal,J. Mol. Biol.,,183,,,,,,,,,,,,,,,,,,,,,,,409,428,1985, citations,entry_citation,6640,250366,1,,entry citation,,,,,,NMR Assignment of the Novel Helicobacter pylori Protein JHP1348,published,journal,J. Biomol. NMR,,32,3,,,,,,,,,,,,,,,,,,,,,,262,262,2005, citations,citation_1,6642,250398,1,,entry citation,,,16439356,,,"NMR dynamic studies suggest that allosteric activation regulates ligand binding in chicken liver bile acid binding protein",published,journal,J. Biol. Chem.,,281,14,,,,,,,,,,,,,,,,,,,,,,9697,9709,2006, citations,entry_citation,6643,250410,1,,entry citation,,,16045928,,,Solution Structure of Human Prolactin,published,journal,J. Mol. Biol.,,351,4,,,,,,,,,,,,,,,,,,,,,,810,823,2005, citations,citation_1,6644,250423,1,,entry citation,,,16222564,,,"1H, 13C, and 15N NMR Assignments for AlgH, a Putative Transcriptional Regulator from Pseudomonas Aeruginosa",published,journal,J. Biomol. NMR,,33,1,,,,,,,,,,,,,,,,,,,,,,74,74,2005, citations,entry_citation,6645,250437,1,,entry citation,,,16341756,,,"1H, 13C and 15N backbone and side chain resonance assignments of Haloferax volcanii DHFR1",published,journal,J. Biomol. NMR,,33,4,,,,,,,,,,,,,,,,,,,,,,281,281,2005, citations,entry_citation,6646,250450,1,,entry citation,,,16222562,,,"NMR Assignment of the Backbone Resonances of the Firefly Luciferase C-terminal 14.3 kDa Domain",published,journal,J. Biomol. NMR,,33,1,,,,,,,,,,,,,,,,,,,,,,73,73,2005, citations,entry_citation,6647,250464,1,,entry citation,,,16220560,,,"On the Importance of Carbohydrate-Aromatic Interactions for the Molecular Recognition of Oligosaccharides by Proteins: NMR Studies of the Structure and Binding Affinity of AcAMP2-Like Peptides with Non-Natural Napthyl and Fluoroaromatic Residues.",published,journal,Chem. Eur. J.,,11,23,,,,,,,,,,,,,,,,,,,,,,7060,7074,2005, citations,reference-1,6647,250465,2,,reference citation,,,8627629,,"Martins JC, Maes D, Loris R, Pepermans HA, Wyns L, Willem R, Verheyden P. H NMR study of the solution structure of Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus. J Mol Biol. 1996 May 3;258(2):322-33.","H NMR study of the solution structure of Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus.",published,journal,J. Mol. Biol.,Journal of molecular biology,258,2,,0022-2836,,,,,,,,,,,,,,,,,,,,322,333,1996,"The conformation in water of antimicrobial protein 2 from Amaranthus caudatus (Ac-AMP2) was determined using 1H NMR, DIANA and restrained molecular modeling. Ac-AMP2 is a 30 amino acid residue, lectin-like protein that specifically binds to chitin, a polymer of beta-1,4-N-acetyl-D-glucosamine. After sequence specific resonance assignments, a total of 198 distance restraints were collected from 2D NOESY buildup spectra at 500 MHz at pH 2, supplemented by a 2D NOESY spectrum at 600 MHz. The location of the three previously unassigned disulfide bridges was determined from preliminary DIANA structures, using a statistical analysis of intercystinyl distances. The solution structure of Ac-AMP2 is presented as a set of 26 DIANA structures, further refined by restrained molecular dynamics using a simulated annealing protocol in the AMBER force field, with a backbone r.m.s.d. for the well defined Glu3-Cys28 segment of 0.69(+/-0.12) angstroms. The main structural element is an antiparallel beta-sheet from Met13 to Lys23 including a betaI-turn over Gln17-Phel8 with a beta bulge at Gly19. In addition, a beta'I turn over Arg6-Gly7, a beta'III turn over Ser11-Gly12 and a helical turn from Gly24 to Cys28 are identified. This structure is very similar to the equivalent regions of the X-ray structure of wheat germ agglutinin and the NMR structure of hevein." citations,reference-2,6647,250466,3,,reference citation,,,12144516,,"Muraki M. The importance of CH/pi interactions to the function of carbohydrate binding proteins. Protein Pept Lett. 2002 Jun;9(3):195-209. Review.",The importance of CH/pi interactions to the function of carbohydrate binding proteins.,published,journal,Protein Pept. Lett.,Protein and peptide letters,9,3,,0929-8665,,,,,,,,,,,,,,,,,,,,195,209,2002,"It is suggested that the interactions between the hydrophobic C-H groups of carbohydrate residues and the pi-electron systems of aromatic amino-acid residues play an important role in the ligand-recognition function of carbohydrate-binding proteins. This review focuses on our recent structural and functional studies of human lysozyme and hevein-domain type lectins (wheat-germ agglutinin and Ac-AMP2) aimed at understanding how CH/pi interactions are involved in the actual binding events." citations,Reference_2,6653,250628,3,,reference citation,,,14517251,,,"Zinc fingers can act as Zn(II) sensors to regulate transcriptional activation domain function",published,journal,EMBO J.,,22,19,,,,,,,,,,,,,,,,,,,,,,5137,5146,2003, citations,Reference_3,6653,250629,4,,reference citation,,,,,,NMRView: A computer program for the visualization and analysis of NMR Data,published,journal,J. Biomol. NMR,,6,,,,,,,,,,,,,,,,,,,,,,,603,614,1994, citations,Reference_4,6653,250630,5,,reference citation,,,8520220,,,NMRPipe: a multidimensional spectral processing system based on UNIX pipes,published,journal,J. Biomol. NMR,,6,3,,,,,,,,,,,,,,,,,,,,,,277,293,1995, citations,entry_citation,6654,250650,1,,entry citation,,,,,,Solution structure of Jingzhaotoxin-VII,published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6655,250665,1,,entry citation,,,16051273,,,"Solution Structure of the N-terminal Zinc Fingers of the Xenopus laevis double-stranded RNA-binding Protein ZFa.",published,journal,J. Mol. Biol.,,351,4,,,,,,,,,,,,,,,,,,,,,,718,730,2005, citations,citation_1,7051,257527,1,,entry citation,,,,,,"Solution structure of growth-blocking peptide of the cabbage armyworm, Mamestra brassicae",published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,reference-3,6647,250467,4,,reference citation,,,15368576,,"Aboitiz N, Vila-Perello M, Groves P, Asensio JL, Andreu D, Canada FJ, Jimenez-Barbero J. NMR and modeling studies of protein-carbohydrate interactions: synthesis, three-dimensional structure, and recognition properties of a minimum hevein domain with binding affinity for chitooligosaccharides. Chembiochem. 2004 Sep 6;5(9):1245-55.","NMR and modeling studies of protein-carbohydrate interactions: synthesis, three-dimensional structure, and recognition properties of a minimum hevein domain with binding affinity for chitooligosaccharides.",published,journal,Chembiochem,Chembiochem : a European journal of chemical biology,5,9,,1439-4227,,,,,,,,,,,,,,,,,,,,1245,1255,2004,"HEV32, a 32-residue, truncated hevein lacking eleven C-terminal amino acids, was synthesized by solid-phase methodology and correctly folded with three cysteine bridge pairs. The affinities of HEV32 for small chitin fragments--in the forms of N,N',N""-triacetylchitotriose ((GlcNAc)3) (millimolar) and N,N',N"",N""',N"""",N""""'-hexaacetylchitohexaose ((GlcNAc)6) (micromolar)--as measured by NMR and fluorescence methods, are comparable with those of native hevein. The HEV32 ligand-binding process is enthalpy driven, while entropy opposes binding. The NMR structure of ligand-bound HEV32 in aqueous solution was determined to be highly similar to the NMR structure of ligand-bound hevein. Solvated molecular-dynamics simulations were performed in order to monitor the changes in side-chain conformation of the binding site of HEV32 and hevein upon interaction with ligands. The calculations suggest that the Trp21 side-chain orientation of HEV32 in the free form differs from that in the bound state; this agrees with fluorescence and thermodynamic data. HEV32 provides a simple molecular model for studying protein-carbohydrate interactions and for understanding the physiological relevance of small native hevein domains lacking C-terminal residues." citations,reference-4,6647,250468,5,,reference citation,,,10842338,,"Asensio JL, Siebert HC, von Der Lieth CW, Laynez J, Bruix M, Soedjanaamadja UM, Beintema JJ, Canada FJ, Gabius HJ, Jimenez-Barbero J. NMR investigations of protein-carbohydrate interactions: studies on the relevance of Trp/Tyr variations in lectin binding sites as deduced from titration microcalorimetry and NMR studies on hevein domains. Determination of the NMR structure of the complex between pseudohevein and N,N',N""-triacetylchitotriose. Proteins. 2000 Aug 1;40(2):218-36.","NMR investigations of protein-carbohydrate interactions: studies on the relevance of Trp/Tyr variations in lectin binding sites as deduced from titration microcalorimetry and NMR studies on hevein domains. Determination of the NMR structure of the complex between pseudohevein and N,N',N""-triacetylchitotriose.",published,journal,Proteins,Proteins,40,2,,0887-3585,,,,,,,,,,,,,,,,,,,,218,236,2000,"Model studies on lectins and their interactions with carbohydrate ligands in solution are essential to gain insights into the driving forces for complex formation and to optimize programs for computer simulations. The specific interaction of pseudohevein with N,N', N""-triacetylchitotriose has been analyzed by (1)H-NMR spectroscopy. Because of its small size, with a chain length of 45 amino acids, this lectin is a prime target to solution-structure determination by NOESY NMR experiments in water. The NMR-analysis was extended to assessment of the topology of the complex between pseudohevein and N, N',N""-triacetylchitotriose. NOESY experiments in water solution provided 342 protein proton-proton distance constraints. Binding of the ligand did not affect the pattern of the protein nuclear Overhauser effect signal noticeably, what would otherwise be indicative of a ligand-induced conformational change. The average backbone (residues 3-41) RMSD of the 20 refined structures was 1.14 A, whereas the heavy atom RMSD was 2.18 A. Two different orientations of the trisaccharide within the pseudohevein binding site are suggested, furnishing an explanation in structural terms for the lectin's capacity to target chitin. In both cases, hydrogen bonds and van der Waals contacts confer stability to the complexes. This conclusion is corroborated by the thermodynamic parameters of binding determined by NMR and isothermal titration calorimetry. The association process was enthalpically driven. In relation to hevein, the Trp/Tyr-substitution in the binding pocket has only a small effect on the free energy of binding in contrast to engineered galectin-1 and a mammalian C-type lectin. A comparison of the three-dimensional structure of pseudohevein in solution to those reported for wheat germ agglutinin (WGA) in the solid state and for hevein and WGA-B in solution has been performed, providing a data source about structural variability of the hevein domains. The experimentally derived structures and the values of the solvent accessibilities for several key residues have also been compared with conformations obtained by molecular dynamics simulations, pointing to the necessity to further refine the programs to enhance their predictive reliability and, thus, underscoring the importance of this kind of combined analysis in model systems." citations,reference-5,6647,250469,6,,reference citation,,,10903932,,"Asensio JL, Canada FJ, Siebert HC, Laynez J, Poveda A, Nieto PM, Soedjanaamadja UM, Gabius HJ, Jimenez-Barbero J. Structural basis for chitin recognition by defense proteins: GlcNAc residues are bound in a multivalent fashion by extended binding sites in hevein domains. Chem Biol. 2000 Jul;7(7):529-43.",Structural basis for chitin recognition by defense proteins: GlcNAc residues are bound in a multivalent fashion by extended binding sites in hevein domains.,published,journal,Chem. Biol.,Chemistry & biology,7,7,,1074-5521,,,,,,,,,,,,,,,,,,,,529,543,2000,"BACKGROUND: Many plants respond to pathogenic attack by producing defense proteins that are capable of reversible binding to chitin, a polysaccharide present in the cell wall of fungi and the exoskeleton of insects. Most of these chitin-binding proteins include a common structural motif of 30 to 43 residues organized around a conserved four-disulfide core, known as the 'hevein domain' or 'chitin-binding' motif. Although a number of structural and thermodynamic studies on hevein-type domains have been reported, these studies do not clarify how chitin recognition is achieved. RESULTS: The specific interaction of hevein with several (GlcNAc)(n) oligomers has been studied using nuclear magnetic resonance (NMR), analytical ultracentrifugation and isothermal titration microcalorimetry (ITC). The data demonstrate that hevein binds (GlcNAc)(2-4) in 1:1 stoichiometry with millimolar affinity. In contrast, for (GlcNAc)(5), a significant increase in binding affinity is observed. Analytical ultracentrifugation studies on the hevein-(GlcNAc)(5,8) interaction allowed detection of protein-carbohydrate complexes with a ratio of 2:1 in solution. NMR structural studies on the hevein-(GlcNAc)(5) complex showed the existence of an extended binding site with at least five GlcNAc units directly involved in protein-sugar contacts. CONCLUSIONS: The first detailed structural model for the hevein-chitin complex is presented on the basis of the analysis of NMR data. The resulting model, in combination with ITC and analytical ultracentrifugation data, conclusively shows that recognition of chitin by hevein domains is a dynamic process, which is not exclusively restricted to the binding of the nonreducing end of the polymer as previously thought. This allows chitin to bind with high affinity to a variable number of protein molecules, depending on the polysaccharide chain length. The biological process is multivalent." citations,reference-6,6647,250470,7,,reference citation,,,10877847,,"Muraki M, Morii H, Harata K. Chemically prepared hevein domains: effect of C-terminal truncation and the mutagenesis of aromatic residues on the affinity for chitin. Protein Eng. 2000 Jun;13(6):385-9.",Chemically prepared hevein domains: effect of C-terminal truncation and the mutagenesis of aromatic residues on the affinity for chitin.,published,journal,Protein Eng.,Protein engineering,13,6,,0269-2139,,,,,,,,,,,,,,,,,,,,385,389,2000,"Chemically prepared hevein domains (HDs), N-terminal domain of an antifungal protein from Nicotiana tabacum (CBP20-N) and an antimicrobial peptide from Amaranthus caudatus (Ac-AMP2), were examined for their affinity for chitin, a beta-1,4-linked polymer of N-acetylglucosamine. An intact binding domain, CBP20-N, showed a higher affinity than a C-terminal truncated domain, Ac-AMP2. The formation of a pyroglutamate residue from N-terminal Gln of CBP20-N increased the affinity. The single replacement of any aromatic residue of Ac-AMP2 with Ala resulted in a significant reduction in affinity, suggesting the importance of the complete set of three aromatic residues in the ligand binding site. The mutations of Phe18 of Ac-AMP2 to the residues with larger aromatic rings, i.e. Trp, beta-(1-naphthyl)alanine or beta-(2-naphthyl)alanine, enhanced the affinity, whereas the mutation of Tyr20 to Trp reduced the affinity. The affinity of an HD for chitin might be improved by adjusting the size and substituent group of stacking aromatic rings." citations,Reference_2,6648,250491,1,,reference citation,,,,,,"Zinc fingers can act as Zn(II) sensors to regulate transcriptional activation domain function",published,journal,EMBO J.,,22,19,,,,,,,,,,,,,,,,,,,,,,5137,5146,2003, citations,Reference_1,6648,250492,2,,reference citation,,,,,,"Zap1p, a metalloregulatory protein involved in zinc-responsive transcriptional regulation in Saccharomyces cerevisiae",published,journal,Mol. Cell,,17,9,,,,,,,,,,,,,,,,,,,,,,5044,5052,1997, citations,entry_citation,6648,250493,3,,entry citation,,,,,,"Solution Structure of a Zap1 Zinc-responsive Domain Provides Insights into Metalloregulatory Transcriptional Repression in Saccharomyces cerevisiae",published,journal,J. Mol. Biol.,,357,4,,,,,,,,,,,,,,,,,,,,,,1167,1183,2006, citations,Reference_3,6648,250494,4,,reference citation,,,,,,NMRView: A computer program for the visualization and analysis of NMR Data,published,journal,J. Biomol. NMR,,4,,,,,,,,,,,,,,,,,,,,,,,603,614,1994, citations,Reference_4,6648,250495,5,,reference citation,,,,,,NMRPipe: a multidimensional spectral processing system based on UNIX pipes,published,journal,J. Biomol. NMR,,6,,,,,,,,,,,,,,,,,,,,,,,277,293,1995, citations,entry_citation,6649,250522,1,,entry citation,,,16042392,,,"Solution structure of the peptidoglycan binding domain of Bacillus subtilis cell wall lytic enzyme CwlC: characterization of the sporulation-related repeats by NMR.",published,journal,Biochemistry,,44,30,,,,,,,,,,,,,,,,,,,,,,10153,10163,2005, citations,entry_citation,665,250542,1,,entry citation,,,,,"Williams, Glyn, Moore, Geoffrey R., Porteous, Rod, Robinson, Martin N., Soffe, Nick, Williams, Robert J. P., ""Solution Structure of Mitochondrial Cytochrome c I. H1 Nuclear Magnetic Resonance of Ferricytochrome c,"" J. Mol. Biol. 183, 409-428 (1985).","Solution Structure of Mitochondrial Cytochrome c I. H1 Nuclear Magnetic Resonance of Ferricytochrome c",published,journal,J. Mol. Biol.,,183,,,,,,,,,,,,,,,,,,,,,,,409,428,1985, citations,ref_nmrview,6650,250559,1,,reference citation,,,,,"Johnson, B. A., and Blevins, R.A. (1994), Journal of Biomolecular NMR, 4:603-614.",NMRView: A computer program for the visualization and analysis of NMR data,published,journal,J. Biomol. NMR,,4,5,,,,,,,,,,,,,,,,,,,,,,603,614,1994, citations,nmrpipe_ref,6650,250560,2,,reference citation,,,,,,NMRPipe: A multidimensional spectral processong system based on UNIX pipes,published,journal,J. Biomol. NMR,,6,3,,,,,,,,,,,,,,,,,,,,,,277,293,1995, citations,entry_citation,6650,250561,3,,entry citation,,,16170802,,,Model peptides mimic the structure and function of the N-terminus of the pore-forming toxin sticholysin II,published,journal,Biopolymers,,84,2,,,,,,,,,,,,,,,,,,,,,,169,180,2006, citations,entry_citation,6656,250703,1,,entry citation,,,16220560,,,"On the Importance of Carbohydrate-Aromatic Interactions for the Molecular Recognition of Chitooligosaccharides by Hevein Domains. NMR Studies of the Structure and Binding Affinity of AcAMP2-Like Peptides with non Natural Napthyl and Fluoroaromatic Residues",published,journal,Chem. Eur. J.,,11,23,,,,,,,,,,,,,,,,,,,,,,7060,7074,2005, citations,reference-1,6656,250704,2,,reference citation,,,8627629,,"Martins JC, Maes D, Loris R, Pepermans HA, Wyns L, Willem R, Verheyden P. H NMR study of the solution structure of Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus. J Mol Biol. 1996 May 3;258(2):322-33.","H NMR study of the solution structure of Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus.",published,journal,J. Mol. Biol.,Journal of molecular biology,258,2,,0022-2836,,,,,,,,,,,,,,,,,,,,322,333,1996,"The conformation in water of antimicrobial protein 2 from Amaranthus caudatus (Ac-AMP2) was determined using 1H NMR, DIANA and restrained molecular modeling. Ac-AMP2 is a 30 amino acid residue, lectin-like protein that specifically binds to chitin, a polymer of beta-1,4-N-acetyl-D-glucosamine. After sequence specific resonance assignments, a total of 198 distance restraints were collected from 2D NOESY buildup spectra at 500 MHz at pH 2, supplemented by a 2D NOESY spectrum at 600 MHz. The location of the three previously unassigned disulfide bridges was determined from preliminary DIANA structures, using a statistical analysis of intercystinyl distances. The solution structure of Ac-AMP2 is presented as a set of 26 DIANA structures, further refined by restrained molecular dynamics using a simulated annealing protocol in the AMBER force field, with a backbone r.m.s.d. for the well defined Glu3-Cys28 segment of 0.69(+/-0.12) angstroms. The main structural element is an antiparallel beta-sheet from Met13 to Lys23 including a betaI-turn over Gln17-Phel8 with a beta bulge at Gly19. In addition, a beta'I turn over Arg6-Gly7, a beta'III turn over Ser11-Gly12 and a helical turn from Gly24 to Cys28 are identified. This structure is very similar to the equivalent regions of the X-ray structure of wheat germ agglutinin and the NMR structure of hevein." citations,reference-2,6656,250705,3,,reference citation,,,12144516,,"Muraki M. The importance of CH/pi interactions to the function of carbohydrate binding proteins. Protein Pept Lett. 2002 Jun;9(3):195-209. Review.",The importance of CH/pi interactions to the function of carbohydrate binding proteins.,published,journal,Protein Pept. Lett.,Protein and peptide letters,9,3,,0929-8665,,,,,,,,,,,,,,,,,,,,195,209,2002,"It is suggested that the interactions between the hydrophobic C-H groups of carbohydrate residues and the pi-electron systems of aromatic amino-acid residues play an important role in the ligand-recognition function of carbohydrate-binding proteins. This review focuses on our recent structural and functional studies of human lysozyme and hevein-domain type lectins (wheat-germ agglutinin and Ac-AMP2) aimed at understanding how CH/pi interactions are involved in the actual binding events." citations,reference-3,6656,250706,4,,reference citation,,,15368576,,"Aboitiz N, Vila-Perello M, Groves P, Asensio JL, Andreu D, Canada FJ, Jimenez-Barbero J. NMR and modeling studies of protein-carbohydrate interactions: synthesis, three-dimensional structure, and recognition properties of a minimum hevein domain with binding affinity for chitooligosaccharides. Chembiochem. 2004 Sep 6;5(9):1245-55.","NMR and modeling studies of protein-carbohydrate interactions: synthesis, three-dimensional structure, and recognition properties of a minimum hevein domain with binding affinity for chitooligosaccharides.",published,journal,Chembiochem,Chembiochem : a European journal of chemical biology,5,9,,1439-4227,,,,,,,,,,,,,,,,,,,,1245,1255,2004,"HEV32, a 32-residue, truncated hevein lacking eleven C-terminal amino acids, was synthesized by solid-phase methodology and correctly folded with three cysteine bridge pairs. The affinities of HEV32 for small chitin fragments--in the forms of N,N',N""-triacetylchitotriose ((GlcNAc)3) (millimolar) and N,N',N"",N""',N"""",N""""'-hexaacetylchitohexaose ((GlcNAc)6) (micromolar)--as measured by NMR and fluorescence methods, are comparable with those of native hevein. The HEV32 ligand-binding process is enthalpy driven, while entropy opposes binding. The NMR structure of ligand-bound HEV32 in aqueous solution was determined to be highly similar to the NMR structure of ligand-bound hevein. Solvated molecular-dynamics simulations were performed in order to monitor the changes in side-chain conformation of the binding site of HEV32 and hevein upon interaction with ligands. The calculations suggest that the Trp21 side-chain orientation of HEV32 in the free form differs from that in the bound state; this agrees with fluorescence and thermodynamic data. HEV32 provides a simple molecular model for studying protein-carbohydrate interactions and for understanding the physiological relevance of small native hevein domains lacking C-terminal residues." citations,reference-4,6656,250707,5,,reference citation,,,10842338,,"Asensio JL, Siebert HC, von Der Lieth CW, Laynez J, Bruix M, Soedjanaamadja UM, Beintema JJ, Canada FJ, Gabius HJ, Jimenez-Barbero J. NMR investigations of protein-carbohydrate interactions: studies on the relevance of Trp/Tyr variations in lectin binding sites as deduced from titration microcalorimetry and NMR studies on hevein domains. Determination of the NMR structure of the complex between pseudohevein and N,N',N""-triacetylchitotriose. Proteins. 2000 Aug 1;40(2):218-36.","NMR investigations of protein-carbohydrate interactions: studies on the relevance of Trp/Tyr variations in lectin binding sites as deduced from titration microcalorimetry and NMR studies on hevein domains. Determination of the NMR structure of the complex between pseudohevein and N,N',N""-triacetylchitotriose.",published,journal,Proteins,Proteins,40,2,,0887-3585,,,,,,,,,,,,,,,,,,,,218,236,2000,"Model studies on lectins and their interactions with carbohydrate ligands in solution are essential to gain insights into the driving forces for complex formation and to optimize programs for computer simulations. The specific interaction of pseudohevein with N,N', N""-triacetylchitotriose has been analyzed by (1)H-NMR spectroscopy. Because of its small size, with a chain length of 45 amino acids, this lectin is a prime target to solution-structure determination by NOESY NMR experiments in water. The NMR-analysis was extended to assessment of the topology of the complex between pseudohevein and N, N',N""-triacetylchitotriose. NOESY experiments in water solution provided 342 protein proton-proton distance constraints. Binding of the ligand did not affect the pattern of the protein nuclear Overhauser effect signal noticeably, what would otherwise be indicative of a ligand-induced conformational change. The average backbone (residues 3-41) RMSD of the 20 refined structures was 1.14 A, whereas the heavy atom RMSD was 2.18 A. Two different orientations of the trisaccharide within the pseudohevein binding site are suggested, furnishing an explanation in structural terms for the lectin's capacity to target chitin. In both cases, hydrogen bonds and van der Waals contacts confer stability to the complexes. This conclusion is corroborated by the thermodynamic parameters of binding determined by NMR and isothermal titration calorimetry. The association process was enthalpically driven. In relation to hevein, the Trp/Tyr-substitution in the binding pocket has only a small effect on the free energy of binding in contrast to engineered galectin-1 and a mammalian C-type lectin. A comparison of the three-dimensional structure of pseudohevein in solution to those reported for wheat germ agglutinin (WGA) in the solid state and for hevein and WGA-B in solution has been performed, providing a data source about structural variability of the hevein domains. The experimentally derived structures and the values of the solvent accessibilities for several key residues have also been compared with conformations obtained by molecular dynamics simulations, pointing to the necessity to further refine the programs to enhance their predictive reliability and, thus, underscoring the importance of this kind of combined analysis in model systems." citations,reference-5,6656,250708,6,,reference citation,,,10903932,,"Asensio JL, Canada FJ, Siebert HC, Laynez J, Poveda A, Nieto PM, Soedjanaamadja UM, Gabius HJ, Jimenez-Barbero J. Structural basis for chitin recognition by defense proteins: GlcNAc residues are bound in a multivalent fashion by extended binding sites in hevein domains. Chem Biol. 2000 Jul;7(7):529-43.",Structural basis for chitin recognition by defense proteins: GlcNAc residues are bound in a multivalent fashion by extended binding sites in hevein domains.,published,journal,Chem. Biol.,Chemistry & biology,7,7,,1074-5521,,,,,,,,,,,,,,,,,,,,529,543,2000,"BACKGROUND: Many plants respond to pathogenic attack by producing defense proteins that are capable of reversible binding to chitin, a polysaccharide present in the cell wall of fungi and the exoskeleton of insects. Most of these chitin-binding proteins include a common structural motif of 30 to 43 residues organized around a conserved four-disulfide core, known as the 'hevein domain' or 'chitin-binding' motif. Although a number of structural and thermodynamic studies on hevein-type domains have been reported, these studies do not clarify how chitin recognition is achieved. RESULTS: The specific interaction of hevein with several (GlcNAc)(n) oligomers has been studied using nuclear magnetic resonance (NMR), analytical ultracentrifugation and isothermal titration microcalorimetry (ITC). The data demonstrate that hevein binds (GlcNAc)(2-4) in 1:1 stoichiometry with millimolar affinity. In contrast, for (GlcNAc)(5), a significant increase in binding affinity is observed. Analytical ultracentrifugation studies on the hevein-(GlcNAc)(5,8) interaction allowed detection of protein-carbohydrate complexes with a ratio of 2:1 in solution. NMR structural studies on the hevein-(GlcNAc)(5) complex showed the existence of an extended binding site with at least five GlcNAc units directly involved in protein-sugar contacts. CONCLUSIONS: The first detailed structural model for the hevein-chitin complex is presented on the basis of the analysis of NMR data. The resulting model, in combination with ITC and analytical ultracentrifugation data, conclusively shows that recognition of chitin by hevein domains is a dynamic process, which is not exclusively restricted to the binding of the nonreducing end of the polymer as previously thought. This allows chitin to bind with high affinity to a variable number of protein molecules, depending on the polysaccharide chain length. The biological process is multivalent." citations,entry_citation,6657,250729,1,,entry citation,,,16220560,,,"On the Importance of Carbohydrate-Aromatic Interactions for the Molecular Recognition of Chitooligosaccharides by Hevein Domains. NMR Studies of the Structure and Binding Affinity of AcAMP2-Like Peptides with non Natural Napthyl and Fluoroaromatic Residues",published,journal,Chem. Eur. J.,,11,23,,,,,,,,,,,,,,,,,,,,,,7060,7074,2005, citations,entry_citation,6662,250839,1,,entry citation,,,,,,"Changes in hydrogen-bond strengths explain reduction potentials in 10 rubredoxin variants.",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,11,102,,,,,,,,,,,,,,,,,,,,,,14581,14586,2005, citations,entry_citation,6663,250855,1,,entry citation,,,,,,"Changes in hydrogen-bond strengths explain reduction potentials in 10 rubredoxin variants.",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,11,102,,,,,,,,,,,,,,,,,,,,,,14581,14586,2005, citations,entry_citation,6664,250871,1,,entry citation,,,,,,"Changes in hydrogen-bond strengths explain reduction potentials in 10 rubredoxin variants.",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,11,102,,,,,,,,,,,,,,,,,,,,,,14581,14586,2005, citations,reference-1,6657,250730,2,,reference citation,,,8627629,,"Martins JC, Maes D, Loris R, Pepermans HA, Wyns L, Willem R, Verheyden P. H NMR study of the solution structure of Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus. J Mol Biol. 1996 May 3;258(2):322-33.","H NMR study of the solution structure of Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus.",published,journal,J. Mol. Biol.,Journal of molecular biology,258,2,,0022-2836,,,,,,,,,,,,,,,,,,,,322,333,1996,"The conformation in water of antimicrobial protein 2 from Amaranthus caudatus (Ac-AMP2) was determined using 1H NMR, DIANA and restrained molecular modeling. Ac-AMP2 is a 30 amino acid residue, lectin-like protein that specifically binds to chitin, a polymer of beta-1,4-N-acetyl-D-glucosamine. After sequence specific resonance assignments, a total of 198 distance restraints were collected from 2D NOESY buildup spectra at 500 MHz at pH 2, supplemented by a 2D NOESY spectrum at 600 MHz. The location of the three previously unassigned disulfide bridges was determined from preliminary DIANA structures, using a statistical analysis of intercystinyl distances. The solution structure of Ac-AMP2 is presented as a set of 26 DIANA structures, further refined by restrained molecular dynamics using a simulated annealing protocol in the AMBER force field, with a backbone r.m.s.d. for the well defined Glu3-Cys28 segment of 0.69(+/-0.12) angstroms. The main structural element is an antiparallel beta-sheet from Met13 to Lys23 including a betaI-turn over Gln17-Phel8 with a beta bulge at Gly19. In addition, a beta'I turn over Arg6-Gly7, a beta'III turn over Ser11-Gly12 and a helical turn from Gly24 to Cys28 are identified. This structure is very similar to the equivalent regions of the X-ray structure of wheat germ agglutinin and the NMR structure of hevein." citations,reference-2,6657,250731,3,,reference citation,,,12144516,,"Muraki M. The importance of CH/pi interactions to the function of carbohydrate binding proteins. Protein Pept Lett. 2002 Jun;9(3):195-209. Review.",The importance of CH/pi interactions to the function of carbohydrate binding proteins.,published,journal,Protein Pept. Lett.,Protein and peptide letters,9,3,,0929-8665,,,,,,,,,,,,,,,,,,,,195,209,2002,"It is suggested that the interactions between the hydrophobic C-H groups of carbohydrate residues and the pi-electron systems of aromatic amino-acid residues play an important role in the ligand-recognition function of carbohydrate-binding proteins. This review focuses on our recent structural and functional studies of human lysozyme and hevein-domain type lectins (wheat-germ agglutinin and Ac-AMP2) aimed at understanding how CH/pi interactions are involved in the actual binding events." citations,reference-3,6657,250732,4,,reference citation,,,15368576,,"Aboitiz N, Vila-Perello M, Groves P, Asensio JL, Andreu D, Canada FJ, Jimenez-Barbero J. NMR and modeling studies of protein-carbohydrate interactions: synthesis, three-dimensional structure, and recognition properties of a minimum hevein domain with binding affinity for chitooligosaccharides. Chembiochem. 2004 Sep 6;5(9):1245-55.","NMR and modeling studies of protein-carbohydrate interactions: synthesis, three-dimensional structure, and recognition properties of a minimum hevein domain with binding affinity for chitooligosaccharides.",published,journal,Chembiochem,Chembiochem : a European journal of chemical biology,5,9,,1439-4227,,,,,,,,,,,,,,,,,,,,1245,1255,2004,"HEV32, a 32-residue, truncated hevein lacking eleven C-terminal amino acids, was synthesized by solid-phase methodology and correctly folded with three cysteine bridge pairs. The affinities of HEV32 for small chitin fragments--in the forms of N,N',N""-triacetylchitotriose ((GlcNAc)3) (millimolar) and N,N',N"",N""',N"""",N""""'-hexaacetylchitohexaose ((GlcNAc)6) (micromolar)--as measured by NMR and fluorescence methods, are comparable with those of native hevein. The HEV32 ligand-binding process is enthalpy driven, while entropy opposes binding. The NMR structure of ligand-bound HEV32 in aqueous solution was determined to be highly similar to the NMR structure of ligand-bound hevein. Solvated molecular-dynamics simulations were performed in order to monitor the changes in side-chain conformation of the binding site of HEV32 and hevein upon interaction with ligands. The calculations suggest that the Trp21 side-chain orientation of HEV32 in the free form differs from that in the bound state; this agrees with fluorescence and thermodynamic data. HEV32 provides a simple molecular model for studying protein-carbohydrate interactions and for understanding the physiological relevance of small native hevein domains lacking C-terminal residues." citations,reference-4,6657,250733,5,,reference citation,,,10842338,,"Asensio JL, Siebert HC, von Der Lieth CW, Laynez J, Bruix M, Soedjanaamadja UM, Beintema JJ, Canada FJ, Gabius HJ, Jimenez-Barbero J. NMR investigations of protein-carbohydrate interactions: studies on the relevance of Trp/Tyr variations in lectin binding sites as deduced from titration microcalorimetry and NMR studies on hevein domains. Determination of the NMR structure of the complex between pseudohevein and N,N',N""-triacetylchitotriose. Proteins. 2000 Aug 1;40(2):218-36.","NMR investigations of protein-carbohydrate interactions: studies on the relevance of Trp/Tyr variations in lectin binding sites as deduced from titration microcalorimetry and NMR studies on hevein domains. Determination of the NMR structure of the complex between pseudohevein and N,N',N""-triacetylchitotriose.",published,journal,Proteins,Proteins,40,2,,0887-3585,,,,,,,,,,,,,,,,,,,,218,236,2000,"Model studies on lectins and their interactions with carbohydrate ligands in solution are essential to gain insights into the driving forces for complex formation and to optimize programs for computer simulations. The specific interaction of pseudohevein with N,N', N""-triacetylchitotriose has been analyzed by (1)H-NMR spectroscopy. Because of its small size, with a chain length of 45 amino acids, this lectin is a prime target to solution-structure determination by NOESY NMR experiments in water. The NMR-analysis was extended to assessment of the topology of the complex between pseudohevein and N, N',N""-triacetylchitotriose. NOESY experiments in water solution provided 342 protein proton-proton distance constraints. Binding of the ligand did not affect the pattern of the protein nuclear Overhauser effect signal noticeably, what would otherwise be indicative of a ligand-induced conformational change. The average backbone (residues 3-41) RMSD of the 20 refined structures was 1.14 A, whereas the heavy atom RMSD was 2.18 A. Two different orientations of the trisaccharide within the pseudohevein binding site are suggested, furnishing an explanation in structural terms for the lectin's capacity to target chitin. In both cases, hydrogen bonds and van der Waals contacts confer stability to the complexes. This conclusion is corroborated by the thermodynamic parameters of binding determined by NMR and isothermal titration calorimetry. The association process was enthalpically driven. In relation to hevein, the Trp/Tyr-substitution in the binding pocket has only a small effect on the free energy of binding in contrast to engineered galectin-1 and a mammalian C-type lectin. A comparison of the three-dimensional structure of pseudohevein in solution to those reported for wheat germ agglutinin (WGA) in the solid state and for hevein and WGA-B in solution has been performed, providing a data source about structural variability of the hevein domains. The experimentally derived structures and the values of the solvent accessibilities for several key residues have also been compared with conformations obtained by molecular dynamics simulations, pointing to the necessity to further refine the programs to enhance their predictive reliability and, thus, underscoring the importance of this kind of combined analysis in model systems." citations,reference-5,6657,250734,6,,reference citation,,,10903932,,"Asensio JL, Canada FJ, Siebert HC, Laynez J, Poveda A, Nieto PM, Soedjanaamadja UM, Gabius HJ, Jimenez-Barbero J. Structural basis for chitin recognition by defense proteins: GlcNAc residues are bound in a multivalent fashion by extended binding sites in hevein domains. Chem Biol. 2000 Jul;7(7):529-43.",Structural basis for chitin recognition by defense proteins: GlcNAc residues are bound in a multivalent fashion by extended binding sites in hevein domains.,published,journal,Chem. Biol.,Chemistry & biology,7,7,,1074-5521,,,,,,,,,,,,,,,,,,,,529,543,2000,"BACKGROUND: Many plants respond to pathogenic attack by producing defense proteins that are capable of reversible binding to chitin, a polysaccharide present in the cell wall of fungi and the exoskeleton of insects. Most of these chitin-binding proteins include a common structural motif of 30 to 43 residues organized around a conserved four-disulfide core, known as the 'hevein domain' or 'chitin-binding' motif. Although a number of structural and thermodynamic studies on hevein-type domains have been reported, these studies do not clarify how chitin recognition is achieved. RESULTS: The specific interaction of hevein with several (GlcNAc)(n) oligomers has been studied using nuclear magnetic resonance (NMR), analytical ultracentrifugation and isothermal titration microcalorimetry (ITC). The data demonstrate that hevein binds (GlcNAc)(2-4) in 1:1 stoichiometry with millimolar affinity. In contrast, for (GlcNAc)(5), a significant increase in binding affinity is observed. Analytical ultracentrifugation studies on the hevein-(GlcNAc)(5,8) interaction allowed detection of protein-carbohydrate complexes with a ratio of 2:1 in solution. NMR structural studies on the hevein-(GlcNAc)(5) complex showed the existence of an extended binding site with at least five GlcNAc units directly involved in protein-sugar contacts. CONCLUSIONS: The first detailed structural model for the hevein-chitin complex is presented on the basis of the analysis of NMR data. The resulting model, in combination with ITC and analytical ultracentrifugation data, conclusively shows that recognition of chitin by hevein domains is a dynamic process, which is not exclusively restricted to the binding of the nonreducing end of the polymer as previously thought. This allows chitin to bind with high affinity to a variable number of protein molecules, depending on the polysaccharide chain length. The biological process is multivalent." citations,entry_citation,6658,250752,1,,entry citation,,,,,,"1H, 15N and 13C Assignments of an Intramolecular Lhx3:ldb1 Complex",published,journal,J. Biomol. NMR,,33,3,,,,,,,,,,,,,,,,,,,,,,198,198,2005, citations,entry_citation,6659,250778,1,,entry citation,,,,,,"Changes in hydrogen-bond strengths explain reduction potentials in 10 rubredoxin variants.",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,11,102,,,,,,,,,,,,,,,,,,,,,,14581,14586,2005, citations,entry_citation,666,250793,1,,entry citation,,,,,"Williams, Glyn, Moore, Geoffrey R., Porteous, Rod, Robinson, Martin N., Soffe, Nick, Williams, Robert J. P., ""Solution Structure of Mitochondrial Cytochrome c I. H1 Nuclear Magnetic Resonance of Ferricytochrome c,"" J. Mol. Biol. 183, 409-428 (1985).","Solution Structure of Mitochondrial Cytochrome c I. H1 Nuclear Magnetic Resonance of Ferricytochrome c",published,journal,J. Mol. Biol.,,183,,,,,,,,,,,,,,,,,,,,,,,409,428,1985, citations,entry_citation,6660,250807,1,,entry citation,,,,,,"Changes in hydrogen-bond strengths explain reduction potentials in 10 rubredoxin variants.",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,11,102,,,,,,,,,,,,,,,,,,,,,,14581,14586,2005, citations,entry_citation,6661,250823,1,,entry citation,,,,,,"Changes in hydrogen-bond strengths explain reduction potentials in 10 rubredoxin variants.",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,11,102,,,,,,,,,,,,,,,,,,,,,,14581,14586,2005, citations,entry_citation,6665,250887,1,,entry citation,,,,,,"Changes in hydrogen-bond strengths explain reduction potentials in 10 rubredoxin variants.",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,11,102,,,,,,,,,,,,,,,,,,,,,,14581,14586,2005, citations,entry_citation,6666,250903,1,,entry citation,,,,,,"Changes in hydrogen-bond strengths explain reduction potentials in 10 rubredoxin variants.",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,11,102,,,,,,,,,,,,,,,,,,,,,,14581,14586,2005, citations,entry_citation,6667,250919,1,,entry citation,,,,,,"Changes in hydrogen-bond strengths explain reduction potentials in 10 rubredoxin variants.",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,11,102,,,,,,,,,,,,,,,,,,,,,,14581,14586,2005, citations,entry_citation,6668,250935,1,,entry citation,,,,,,"Changes in hydrogen-bond strengths explain reduction potentials in 10 rubredoxin variants.",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,11,102,,,,,,,,,,,,,,,,,,,,,,14581,14586,2005, citations,entry_citation,6669,250951,1,,entry citation,,,,,,"Changes in hydrogen-bond strengths explain reduction potentials in 10 rubredoxin variants.",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,11,102,,,,,,,,,,,,,,,,,,,,,,14581,14586,2005, citations,entry_citation,667,250966,1,,entry citation,,,,,"Williams, Glyn, Moore, Geoffrey R., Porteous, Rod, Robinson, Martin N., Soffe, Nick, Williams, Robert J. P., ""Solution Structure of Mitochondrial Cytochrome c I. H1 Nuclear Magnetic Resonance of Ferricytochrome c,"" J. Mol. Biol. 183, 409-428 (1985).","Solution Structure of Mitochondrial Cytochrome c I. H1 Nuclear Magnetic Resonance of Ferricytochrome c",published,journal,J. Mol. Biol.,,183,,,,,,,,,,,,,,,,,,,,,,,409,428,1985, citations,entry_citation,6670,250983,1,,entry citation,,,,,,"Changes in hydrogen-bond strengths explain reduction potentials in 10 rubredoxin variants.",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,11,102,,,,,,,,,,,,,,,,,,,,,,14581,14586,2005, citations,entry_citation,6671,250999,1,,entry citation,,,,,,"Changes in hydrogen-bond strengths explain reduction potentials in 10 rubredoxin variants.",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,11,102,,,,,,,,,,,,,,,,,,,,,,14581,14586,2005, citations,entry_citation,6672,251015,1,,entry citation,,,,,,"Changes in hydrogen-bond strengths explain reduction potentials in 10 rubredoxin variants.",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,11,102,,,,,,,,,,,,,,,,,,,,,,14581,14586,2005, citations,entry_citation,6673,251031,1,,entry citation,,,,,,"Changes in hydrogen-bond strengths explain reduction potentials in 10 rubredoxin variants.",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,11,102,,,,,,,,,,,,,,,,,,,,,,14581,14586,2005, citations,entry_citation,6674,251047,1,,entry citation,,,,,,"Changes in hydrogen-bond strengths explain reduction potentials in 10 rubredoxin variants.",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,11,102,,,,,,,,,,,,,,,,,,,,,,14581,14586,2005, citations,entry_citation,6675,251063,1,,entry citation,,,,,,"Changes in hydrogen-bond strengths explain reduction potentials in 10 rubredoxin variants.",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,11,102,,,,,,,,,,,,,,,,,,,,,,14581,14586,2005, citations,entry_citation,6676,251079,1,,entry citation,,,,,,"Changes in hydrogen-bond strengths explain reduction potentials in 10 rubredoxin variants.",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,11,102,,,,,,,,,,,,,,,,,,,,,,14581,14586,2005, citations,entry_citation,6677,251095,1,,entry citation,,,,,,"Changes in hydrogen-bond strengths explain reduction potentials in 10 rubredoxin variants.",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,11,102,,,,,,,,,,,,,,,,,,,,,,14581,14586,2005, citations,entry_citation,6678,251111,1,,entry citation,,,,,,"Changes in hydrogen-bond strengths explain reduction potentials in 10 rubredoxin variants.",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,11,102,,,,,,,,,,,,,,,,,,,,,,14581,14586,2005, citations,entry_citation,6679,251127,1,,entry citation,,,16245921,,,"Solution NMR structures of IgG binding domains with artificially evolved high levels of sequence identity but different folds",published,journal,Biochemistry,,44,43,,,,,,,,,,,,,,,,,,,,,,14055,14061,2005, citations,entry_citation,668,251142,1,,entry citation,,,,,"Williams, Glyn, Moore, Geoffrey R., Porteous, Rod, Robinson, Martin N., Soffe, Nick, Williams, Robert J. P., ""Solution Structure of Mitochondrial Cytochrome c I. H1 Nuclear Magnetic Resonance of Ferricytochrome c,"" J. Mol. Biol. 183, 409-428 (1985).","Solution Structure of Mitochondrial Cytochrome c I. H1 Nuclear Magnetic Resonance of Ferricytochrome c",published,journal,J. Mol. Biol.,,183,,,,,,,,,,,,,,,,,,,,,,,409,428,1985, citations,entry_citation,6680,251156,1,,entry citation,,,16245921,,,"Solution NMR structures of IgG binding domains with artificially evolved high levels of sequence identity but different folds",published,journal,Biochemistry,,44,43,,,,,,,,,,,,,,,,,,,,,,14055,14061,2005, citations,entry_citation,6681,251170,1,,entry citation,,,15522230,,,"NMR structure of the glucose-dependent insulinotropic polypeptide fragment, GIP(1-30)amide",published,journal,Biochem. Biophys. Res. Commun.,,325,1,,,,,,,,,,,,,,,,,,,,,,281,286,2005, citations,entry_citation,6682,251190,1,,entry citation,,,18287285,,,"The solution structure of ZNF593 from Homo sapiens reveals a zinc finger in a predominantly unstructured protein",published,journal,Protein Sci.,,17,3,,,,,,,,,,,,,,,,,,,,,,571,576,2008, citations,entry_citation,6683,251224,1,,entry citation,,,16703421,,,Backbone Resonance Assignment of Human Adult Hemoglobin in the Deoxy Form,published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,1,1,2006, citations,entry_citation,6685,251243,1,,entry citation,,,16258838,,,"Resonance Assignments of Escherichia Coli AlkB: A Key 2-oxoglutarate and Fe(II) Dependent Dioxygenase of the Adaptive DNA-repair Response",published,journal,J. Biomol. NMR,,33,2,,,,,,,,,,,,,,,,,,,,,,138,138,2005, citations,entry_citation,6686,251260,1,,entry citation,,,9305950,,,"Solution Structure of the Paramagnetic Complex of the N-Terminal Domain of Calmodulin with Two Ce3+ Ions by 1H NMR.",published,journal,Biochemistry,,36,39,,,,,,,,,,,,,,,,,,,,,,11605,11618,1997, citations,entry_citation,6687,251280,1,,entry citation,,,16411764,,,"The N-terminal domain of human centrin 2 has a closed structure, binds calcium with a very low affinity, and plays a role in the protein self-assembly",published,journal,Biochemistry,,45,3,,,,,,,,,,,,,,,,,,,,,,880,889,2006, citations,entry_citation,6688,251305,1,,entry citation,,,16222561,,,NMR Assignment of Protein Rv1980c from Mycobacterium Tuberculosis,published,journal,J. Biomol. NMR,,33,1,,,,,,,,,,,,,,,,,,,,,,73,73,2005, citations,citation_2,6688,251306,2,,reference citation,,,,,,NMRView: A computer program for the visualization and analysis of NMR Data,published,journal,J. Biomol. NMR,,6,,,,,,,,,,,,,,,,,,,,,,,603,614,1994, citations,citation_3,6688,251307,3,,reference citation,,,,,,NMRPipe: a multidimensional spectral processing system based on UNIX pipes,published,journal,J. Biomol. NMR,,6,,,,,,,,,,,,,,,,,,,,,,,277,293,1995, citations,citation_1,6689,251333,1,,entry citation,,,16411764,,,"The N-terminal domain of human centrin 2 has a closed structure, binds calcium with a very low affinity, and plays a role in the protein self-assembly",published,journal,Biochemistry,,45,3,,,,,,,,,,,,,,,,,,,,,,880,889,2006, citations,entry_citation,6690,251352,1,,entry citation,,,15990112,,,"Structural Basis of the Interaction Between P-element Somatic Inhibitor and U1-70k Essential for the Alternative Splicing of P-element Transposase",published,journal,J. Mol. Biol.,,351,1,,,,,,,,,,,,,,,,,,,,,,52,65,2005, citations,entry_citation,6691,251385,1,,entry citation,,,15990112,,,"Structural Basis of the Interaction Between P-element Somatic Inhibitor and U1-70k Essential for the Alternative Splicing of P-element Transposase.",published,journal,J. Mol. Biol.,,351,1,,,,,,,,,,,,,,,,,,,,,,52,65,2005, citations,entry_citation,6692,251415,1,,entry citation,,,16323221,,,"The Solution Structure of the AppA BLUF Domain: Insight into the Mechanism of Light-Induced Signaling",published,journal,Chem. Biochem.,,7,1,,,,,,,,,,,,,,,,,,,,,,187,193,2006, citations,entry_citation,6693,251432,1,,entry citation,,,16331425,,,"1H, 13C, and 15N Resonance Assignments for the Protein Coded by Gene Locus BB0938 of Bordetella bronchiseptica",published,journal,J. Biomol. NMR,,33,3,,,,,,,,,,,,,,,,,,,,,,197,197,2005, citations,citation_1,6695,251495,1,,entry citation,,,16060673,,"Biochemistry 2005, 44, 10644-10653; ""Identification of the N- and C-Terminal Substrate Binding Segments of Ferredoxin-NADP+ Reductase by NMR"" Masahiro Maeda, Young Ho Lee, Takahisa Ikegami, Kohsuke Tamura, Masaru Hoshino, Toshio Yamazaki, Masato Nakayama, Toshiharu Hase, and Yuji Goto","Identification of the N- and C-Terminal Substrate Binding Segments of Ferredoxin-NADP+ Reductase by NMR",published,journal,Biochemistry,,44,31,,,,,,,,,,,,,,,,,,,,,,10644,10653,2005, citations,entry_citation,6696,251514,1,,entry citation,,,16531226,,,"Conformational Diversity in the TPR Domain-Mediated Interaction of Protein Phosphatase 5 with Hsp90",published,journal,Structure,,14,3,,,,,,,,,,,,,,,,,,,,,,415,426,2006, citations,entry_citation,6698,251542,1,,entry citation,,,17883245,,,"A partially structured region of a largely unstructured protein, Plasmodium falciparum merozoite surface protein 2 (MSP2), forms amyloid-like fibrils",published,journal,J. 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NMR,,33,1,,,,,,,,,,,,,,,,,,,,,,76,76,2005, citations,entry_citation,6705,251605,1,,entry citation,,,16258835,,,"Backbone and Side-chains 1H, 13C and 15N NMR Assignment of Human beta-parvalbumin",published,journal,J. Biomol. NMR,,33,2,,,,,,,,,,,,,,,,,,,,,,137,137,2005, citations,entry_citation,6707,251621,1,,entry citation,,,12450379,,,"Calcium-induced conformational switching of Paramecium calmodulin provides evidence for domain coupling.",published,journal,Biochemistry,,41,48,,,,,,,,,,,,,,,,,,,,,,14158,14166,2002, citations,entry_citation,6709,251645,1,,entry citation,,,16424993,,,"1H, 13C and 15N Resonance Assignment of the N-terminal Domain of PilB from Neisseria Meningitidis.",published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,6,6,2006, citations,1,6710,251662,1,,entry citation,,,,,,NMR characterization of free and complexed p67phox and p40phox PB1 domains in solution,in preparation,journal,Eur. J. Biochem.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6711,251678,1,,entry citation,,,16211496,,,NMR Assignment of Human Ubiquitin Conjugating Enzyme Ubc7,published,journal,J. Biomol. NMR,,32,4,,,,,,,,,,,,,,,,,,,,,,340,340,2005, citations,reference_1,6711,251679,2,,reference citation,,,9048545,,"Cook, W.J., Martin, P.D., Edwards, B.F.P., Yamazaki, R.K., and Chau, V. (1997) Biochemistry, 36, 1621-1627.","Crystal structure of a class I ubiquitin conjugating enzyme (Ubc7) from Saccharomyces cerevisiae at 2.9 angstroms resolution.",published,journal,Biochemistry,,36,,,,,,,,,,,,,,,,,,,,,,,1621,1627,1997,X-ray crystal structure of yeast Ubc7 citations,entry_citation,6712,251695,1,,entry citation,,,16330538,,,"Human C4b-binding protein, structural basis for interaction with Streptococcal M protein, a major bacterial virulence factor",published,journal,J. Biol. 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Mol. Biol.,,366,1,,,,,,,,,,,,,,,,,,,,,,155,164,2007, citations,entry_citation,6861,254539,1,,entry citation,,,11266616,,,Solvation energetics and conformational change in EF-hand proteins,published,journal,Protein Sci.,,10,2,,,,,,,,,,,,,,,,,,,,,,301,312,2001, citations,entry_citation,6862,254554,1,,entry citation,,,11266616,,,Solvation energetics and conformational change in EF-hand proteins,published,journal,Protein Sci.,,10,2,,,,,,,,,,,,,,,,,,,,,,301,312,2001, citations,Mengovirus_Leader_polypeptide_fragment,6863,254571,1,,entry citation,,,11883190,,,"Leader Protein of Encephalomyocarditis Virus Binds Zinc, Is Phosphorylated during Viral Infection, and Affects the Efficiency of Genome Translation",published,journal,Virology,,290,2,,,,,,,,,,,,,,,,,,,,,,261,271,2001, citations,entry_citation,6864,254588,1,,entry citation,,,16601859,,,"Resonance Assignments of a Repeated Domain of the Egg Case Silk from Nephila Antipodiana",published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,17,17,2006, citations,entry_citation,6865,254602,1,,entry citation,,,16815922,,,The layered fold of the TSR domain of P. falciparum TRAP contains a heparin binding site,published,journal,Protein Sci.,,15,7,,,,,,,,,,,,,,,,,,,,,,1760,1768,2006, citations,entry_citation,6866,254623,1,,entry citation,,,17400918,,,Solution structure of human sorting nexin 22,published,journal,Protein Sci.,,16,5,,,,,,,,,,,,,,,,,,,,,,807,814,2007, citations,entry_citation,6867,254645,1,,entry citation,,,16331977,,,"Structure and Dynamics of Micelle-Associated Human Immunodeficiency Virus gp41 Fusion Domain",published,journal,Biochemistry,,44,49,,,,,,,,,,,,,,,,,,,,,,16167,16180,2005, citations,entry_citation,6868,254672,1,,entry citation,,,16260765,,,"Solution structure of the Escherichia coli protein ydhR: a putative mono-oxygenase",published,journal,Protein Sci.,,14,12,,,,,,,,,,,,,,,,,,,,,,3115,3120,2005, citations,entry_citation,6869,254694,1,,entry citation,,,17355988,,,"The unstructured C-terminus of the {tau} subunit of Escherichia coli DNA polymerase III holoenzyme is the site of interaction with the {alpha} subunit",published,journal,Nucleic Acids Res.,,35,9,,,,,,,,,,,,,,,,,,,,,,2813,2824,2007, citations,entry_citation,6870,254725,1,,entry citation,,,18191874,,,Probing the conformation and dynamics of allatostatin neuropeptides: a structural model for functional differences.,published,journal,Peptides,Peptides,29,3,,,,,,,,,,,,,,,,,,,,,,375,385,2008, citations,entry_citation,6872,254745,1,,entry citation,,,16207177,,,"Kalata B8, a novel antiviral circular protein, exhibits conformational flexibility in the cystine knot motif",published,journal,Biochem. J.,,393,Pt 3,,,,,,,,,,,,,,,,,,,,,,619,626,2006, citations,entry_citation,6873,254762,1,,entry citation,,,16642402,,,"New NMR Assignment 1H, 13C, and 15N Assignment of the Second PH Domain of Human Pleckstrin (234-350)",published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,21,21,2006,assignment note citations,citation_1,6873,254763,2,,reference citation,,,1569857,,Structure (Camb). 2005 Feb;13(2):277-86.,"Structure and phosphatidylinositol-(3,4)-bisphosphate binding of the C-terminal PH domain of human pleckstrin.",published,journal,Structure,,13,2,,,,,,,,,,,,,,,,,,,,,,277,286,2005,structure and pip binding citations,entry_citation,6874,254777,1,,entry citation,,,16540468,,,Structural Diversity in p160/CREB-binding Protein Coactivator Complexes,published,journal,J. Biol. Chem.,,281,21,,,,,,,,,,,,,,,,,,,,,,14787,14795,2006, citations,entry_citation,6875,254803,1,,entry citation,,,16995857,,,"Solution NMR structure of a human FGF-1 monomer, activated by a hexasaccharide heparin-analogue",published,journal,FEBS J.,,273,20,,,,,,,,,,,,,,,,,,,,,,4716,4727,2006, citations,reference-1,6875,254804,2,,reference citation,,,10819962,,"Lozano RM, Pineda-Lucena A, Gonzalez C, Angeles Jimenez M, Cuevas P, Redondo-Horcajo M, Sanz JM, Rico M, Gimenez-Gallego G. 1H NMR structural characterization of a nonmitogenic, vasodilatory, ischemia-protector and neuromodulatory acidic fibroblast growth factor. Biochemistry. 2000 May 2;39(17):4982-93.","1H NMR structural characterization of a nonmitogenic, vasodilatory, ischemia-protector and neuromodulatory acidic fibroblast growth factor",published,journal,Biochemistry,Biochemistry,39,17,,0006-2960,,,,,,,,,,,,,,,,,,,,4982,4993,2000,"A shortened genetically engineered form of acidic fibroblast growth factor (aFGF), that includes amino acids 28-154 of the full-length sequence (154 residues) plus Met in substitution of Leu27, does not induce cell division even though it is recognized by the cell membrane receptor, triggers the early mitogenic events, and retains the neuromodulatory, vasoactive, and cardio- and neuroprotective properties of the native full-length molecule. Taken together, these properties make this truncated aFGF a promising compound in the treatment of a wide assortment of neurological and cardiovascular pathologies where aFGF mitogenic activity is dispensable. Differences in biological activities between the shortened aFGF and the wild-type form have been attributed to lack of stability, and to the specific amino acid sequence missing at the N-terminus. Here we show that this shortened aFGF form has a three-dimensional structure even more stable than the wild-type protein at the mitogenic assay conditions; that this structure is similar to that of the wild type except at site 1 of interaction with the cell membrane receptor; that its lack of mitogenic activity cannot be attributed to the specific missing sequence; and that the vasodilatory activity of aFGF seems impaired by alterations of the three-dimensional structure of site 2 of interaction with the cell membrane receptor." citations,reference-2,6875,254805,3,,reference citation,,,15839662,,"Canales A, Angulo J, Ojeda R, Bruix M, Fayos R, Lozano R, Gimenez-Gallego G, Martin-Lomas M, Nieto PM, Jimenez-Barbero J. Conformational flexibility of a synthetic glycosylaminoglycan bound to a fibroblast growth factor. FGF-1 recognizes both the (1)C(4) and (2)S(O) conformations of a bioactive heparin-like hexasaccharide. J. Am. Chem. Soc. 2005 Apr 27;127(16):5778-9.","Conformational flexibility of a synthetic glycosylaminoglycan bound to a fibroblast growth factor. FGF-1 recognizes both the (1)C(4) and (2)S(O) conformations of a bioactive heparin-like hexasaccharide",published,journal,J. Am. Chem. Soc.,Journal of the American Chemical Society,127,16,,0002-7863,,,,,,,,,,,,,,,,,,,,5778,5779,2005,"The first direct NMR determination of the conformation of a conformationally flexible heparin-like hexasaccharide bound to a key receptor, FGF-1, is described. The determination has been based on the use of a 13C-labeled protein and a regular 12C sugar. FGF-1 recognizes several conformations of the iduronic moieties of the hexasaccharide. Therefore, this case is different than that described for the controversial recognition of heparin-like saccharides by AT-III, which seems to recognize just one conformation of the iduronic acid residues." citations,entry_citation,6876,254831,1,,entry citation,,,16680406,,,"1H, 15N and 13C assignments of the cysteine protease inhibitor Chagasin from Trypanosoma cruzi",published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,30,30,2006, citations,entry_citation,6877,254852,1,,entry citation,,,16716065,,,"Structural and Thermodynamic Basis for the Enhanced Transcriptional Control by the Human Papillomavirus Strain-16 E2 Protein",published,journal,Biochemistry,,45,21,,,,,,,,,,,,,,,,,,,,,,6551,6560,2006, citations,citation_1,6878,254869,1,,entry citation,,,16962559,,,"Structure and localization of an essential transmembrane segment of the proton translocation channel of yeast H+-V-ATPase",published,journal,Biochim. Biophys. Acta,,1768,2,,,,,,,,,,,,,,,,,,,,,,218,227,2007, citations,entry_citation,6879,254882,1,,entry citation,,,16460013,,,"NMR-Derived Dynamic Aspects of N-Type Inactivation of a Kv Channel Suggest a Transient Interaction with the T1 Domain",published,journal,Biochemistry,,45,6,,,,,,,,,,,,,,,,,,,,,,1663,1672,2006, citations,entry_citation,6880,254903,1,,entry citation,,,16623717,,,"Local binding with globally distributed changes in a small protease inhibitor upon enzyme binding",published,journal,FEBS J.,,273,8,,,,,,,,,,,,,,,,,,,,,,1831,1842,2006, citations,entry_citation,6881,254920,1,,entry citation,,,16623717,,,"Local binding with globally distributed changes in a small protease inhibitor upon enzyme binding",published,journal,FEBS J.,,273,8,,,,,,,,,,,,,,,,,,,,,,1831,1842,2006, citations,Interleukin-15_receptor,6882,254949,1,,entry citation,,,16377614,,,"The structure of the IL-15alpha-receptor and its implications for ligand binding",published,journal,J. Biol. Chem.,,281,10,,,,,,,,,,,,,,,,,,,,,,6642,6647,2006, citations,citation_1,6883,254972,1,,entry citation,,,16004872,,,Ufd1 exhibits the AAA-ATPase fold with two distinct ubiquitin interaction sites,published,journal,Structure,,13,7,,,,,,,,,,,,,,,,,,,,,,995,1005,2005, citations,entry_citation,6884,254988,1,,entry citation,,,,,,solution structure of Bacillus subtilis Acylphosphatase,in preparation,journal,J. Biol. Chem.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6885,255003,1,,entry citation,,,16609835,,,1H and 15N Resonance Assignment of the First Module of FGFR1,published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,28,28,2006, citations,entry_citation,6886,255017,1,,entry citation,,,,,,"NMR structures of the histidine-rich peptide LAH4 in micellar environments: membrane insertion, pH-dependent mode of antimicrobial action and DNA transfection",in preparation,journal,Biophysical J.,Biophysical Journal,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,Primary_publication,6888,255031,1,,entry citation,,,16568976,,,Synthetic ligands for apo-neocarzinostatin,published,journal,J. Am. Chem. Soc.,,128,13,,,,,,,,,,,,,,,,,,,,,,4204,4205,2006, citations,reference_citation,6888,255032,2,,reference citation,,,12269815,,,Solution structure of a novel chromoprotein derived from apo-neocarzinostatin and a synthetic chromophore.,published,journal,Biochemistry,,41,39,,,,,,,,,,,,,,,,,,,,,,11731,11739,2002, citations,entry_citation,6890,255052,1,,entry citation,,,16531238,,"Kanelis, V. Bruce, M.C., Skrynnikov, N.R., Rotin, D. and Forman-Kay, J.D.",Structural Determinants for High-Affinity Binding in a Nedd4 WW3* Domain-Comm PY Motif Complex,published,journal,Structure (Cambridge MA U.S.),,14,3,,,,,,,,,,,,,,,,,,,,,,543,553,2006, citations,entry_citation,6891,255088,1,,entry citation,,,15931669,,,"Solution structure of chi-conopeptide MrIA, a modulator of the human norepinephrine transporter",published,journal,Biopolymers,,80,6,,,,,,,,,,,,,,,,,,,,,,815,823,2005, citations,entry_citation,6892,255107,1,,entry citation,,,16478467,,,"Structure and influence on stability and activity of the N-terminal propeptide part of lung surfactant protein C",published,journal,FEBS J.,,273,5,,,,,,,,,,,,,,,,,,,,,,926,935,2006, citations,entry_citation,6893,255128,1,,entry citation,,,16475814,,,"Identification of an Ordered Compact Structure within the Recombinant Bovine Fibrinogen alphaC-Domain Fragment by NMR",published,journal,Biochemistry,,45,7,,,,,,,,,,,,,,,,,,,,,,2257,2266,2006, citations,entry_citation,6894,255143,1,,entry citation,,,,,,New insights into binding of the possible cancer target RalGDS,submitted,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6895,255162,1,,entry citation,,,16362037,,,"Molecular basis of RNA recognition by the human alternative splicing factor Fox-1.",published,journal,EMBO J.,,25,1,,,,,,,,,,,,,,,,,,,,,,163,173,2006, citations,entry_citation,6896,255193,1,,entry citation,,,16500898,,,"alpha -selenoconotoxins: A new class of potent alpha 7 neuronal nicotinic receptor antagonists",published,journal,J. Biol. Chem.,,281,20,,,,,,,,,,,,,,,,,,,,,,14136,14143,2006, citations,entry_citation,6897,255212,1,,entry citation,,,16500898,,,"alpha-selenoconotoxins: A new class of potent alpha 7 neuronal nicotinic receptor antagonists",published,journal,J. Biol. Chem.,,281,20,,,,,,,,,,,,,,,,,,,,,,14136,14143,2006, citations,entry_citation,6898,255230,1,,entry citation,,,16540201,,,NMR structure of the viral peptide linked to the genome (VPg) of poliovirus,published,journal,Peptides,,27,7,,,,,,,,,,,,,,,,,,,,,,1676,1684,2006, citations,entry_citation,6899,255251,1,,entry citation,,,16519900,,,"Role of Structural and Dynamical Plasticity in Sin3: The Free PAH2 Domain is a Folded Module in mSin3B",published,journal,J. Mol. Biol.,,358,2,,,,,,,,,,,,,,,,,,,,,,485,497,2006, citations,entry_citation,6900,255266,1,,entry citation,,,16518566,,,"NMR Assignment and Secondary Structure Determination of the C-terminal MA-3 Domain of the Tumour Suppressor Protein Pdcd4",published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,18,18,2006, citations,entry_citation,6901,255295,1,,entry citation,,,16298993,,,Solution structure of the human Ubiquitin Specific Protease 15 DUSP Domain,published,journal,J. Biol. Chem.,,281,8,,,,,,,,,,,,,,,,,,,,,,5026,5031,2006, citations,entry_citation,6902,255307,1,,entry citation,,,16604427,,,NMR Structure Note: Solution structure of the FK506-binding domain of human FKBP38,published,journal,J. Biomol. NMR,,34,3,,,,,,,,,,,,,,,,,,,,,,197,202,2006, citations,entry_citation,6903,255329,1,,entry citation,,,16607466,,,"NMR Assignment of M-crystallin: A Novel Ca(2+) Binding Protein of the betagamma-crystallin Superfamily from Methanosarcina acetivorans.",published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,32,32,2006, citations,entry_citation,6904,255345,1,,entry citation,,,16607466,,,"NMR Assignment of M-crystallin: A Novel Ca(2+) Binding Protein of the betagamma-crystallin Superfamily from Methanosarcina acetivorans.",published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,32,32,2006, citations,entry_citation,6905,255365,1,,entry citation,,,,,,"Solution Structure of a Zap1 Zinc-responsive Domain Provides Insights into Metalloregulatory Transcriptional Repression in Saccharomyces cerevisiae",published,journal,J. Mol. Biol.,,357,4,,,,,,,,,,,,,,,,,,,,,,1167,1183,2006, citations,entry_citation,6906,255381,1,,entry citation,,,16406070,,,"The solution structure of the native K50 Bicoid homeodomain bound to the consensus TAATCC DNA-binding site",published,journal,J. Mol. Biol.,,356,5,,,,,,,,,,,,,,,,,,,,,,1137,1151,2006, citations,entry_citation,6907,255397,1,,entry citation,,,17172296,,,"Folding stability and cooperativity of the three forms of 1-110 residues fragment of staphylococcal nuclease",published,journal,Biophys. J.,,92,6,,,,,,,,,,,,,,,,,,,,,,2090,2107,2007, citations,entry_citation,6908,255410,1,,entry citation,,,17172296,,,"Folding stability and cooperativity of the three forms of 1-110 residues fragment of staphylococcal nuclease",published,journal,Biophys. J.,,92,6,,,,,,,,,,,,,,,,,,,,,,2090,2107,2007, citations,citation_1,6909,255424,1,,entry citation,,,16413543,,,Solution structure and dynamics of human metallothionein-3 (MT-3),published,journal,FEBS Lett.,,580,3,,,,,,,,,,,,,,,,,,,,,,795,800,2006, citations,entry_citation,6910,255439,1,,entry citation,,,16601858,,,"1H, 13C and 15N Resonance Assignments of SMP-1: A Small Myristoylated Protein from Leishmania major",published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,26,26,2006, citations,citation_1,6911,255454,1,,entry citation,,,16636753,,,"13C, 15N and 1H Resonance Assignment of the PDZ1 domain of MAGI-1 using QUASI",published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,33,33,2006, citations,entry_citation,6912,255470,1,,entry citation,,,16609834,,,"1H, 13C and 15N Resonance Assignments for the Reduced Forms of Thioredoxin 1 and 2 from S. cerevisiae",published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,35,35,2006, citations,entry_citation,6913,255484,1,,entry citation,,,16609834,,,"1H, 13C and 15N Resonance Assignments for the Reduced Forms of Thioredoxin 1 and 2 from S. cerevisiae",published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,35,35,2006, citations,entry_citation,6914,255498,1,,entry citation,,,16868859,,,NMR assignment of the Wilson disease associated protein N-domain,published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,61,61,2006, citations,citation,6914,255499,2,,reference citation,,,16567646,,,"Solution structure of the N-domain of Wilson disease protein: Distinct nucleotide-binding environment and effects of disease mutations",published,journal,Proc. Natl. Acad. Sci. U. S. A.,,103,14,,,,,,,,,,,,,,,,,,,,,,5302,5307,2006, citations,ciration_1,6915,255515,1,,entry citation,,,,,,"Expression in Pichia pastoris and backbone dynamics of dendroaspin, a three finger toxin",in preparation,journal,Proteins,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6916,255531,1,,entry citation,,,16636661,,,"Solution structure of the partially folded high-risk human papilloma virus 45 oncoprotein E7",published,journal,Oncogene,,25,44,,,,,,,,,,,,,,,,,,,,,,5953,5959,2006, citations,citation_1,6917,255552,1,,entry citation,,,16418270,,,"Structure of Pfu Pop5, an archaeal RNase P protein",published,journal,Proc. Natl. Acad. Sci. U.S.A.,,103,4,,,,,,,,,,,,,,,,,,,,,,873,878,2006, citations,entry_citation,6918,255564,1,,entry citation,,,16317001,,,"Structure of the N-terminal Calcium Sensor Domain of Centrin Reveals the Biochemical Basis for Domain-Specific Function",published,journal,J. Biol. Chem.,,281,5,,,,,,,,,,,,,,,,,,,,,,2876,2881,2006, citations,entry_citation,6919,255580,1,,entry citation,,,16601860,,,NMR Assignment of Region 655-775 of Human MAN1,published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,2,2,2006, citations,entry_citation,6920,255596,1,,entry citation,,,16529770,,,"Solution Structure of the RBCC/TRIM B-box1 Domain of Human MID1: B-box with a RING",published,journal,J. Mol. Biol.,,358,2,,,,,,,,,,,,,,,,,,,,,,532,545,2006, citations,entry_citation,6921,255610,1,,entry citation,,,,,,"1H, 13C and 15N backbone resonances assignment of the hydrophilic domain of human cytochrome b5",in preparation,journal,J. Biomol. NMR,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6922,255625,1,,entry citation,,,16405996,,,Solution Structure of the Vts1 SAM Domain in the Presence of RNA,published,journal,J. Mol. Biol.,,356,5,,,,,,,,,,,,,,,,,,,,,,1065,1072,2006, citations,entry_citation,6923,255639,1,,entry citation,,,24145868,10.1038/srep02985,,Functional role of the flexible N-terminal extension of FKBP38 in catalysis,published,journal,Sci. Rep.,,3,2985,,,,,,,,,,,,,,,,,,,,,,,,2013, citations,reference_citation,6923,255640,2,,reference citation,,,16718587,,,"Backbone 1H, 13C, and 15N resonance assignments of the N-terminal domain of FKBP38 (FKBP38NTD)",published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,37,37,2006, citations,citation1,6924,255654,1,,reference citation,,,15369825,,,"Discrepin, a new peptide of the subfamily alpha-KTx15 irreversibly blocks K+-channels (IA currents) of cerebellum granular cells",published,journal,Arch. Biochem. Biophys.,,430,2,,,,,,,,,,,,,,,,,,,,,,256,263,2004, citations,citation2,6924,255655,2,,entry citation,,,16460026,,,"Solution Structure of Discrepin, a New K(+)-Channel Blocking Peptide from the alpha-KTx15 Subfamily(,).",published,journal,Biochemistry,,45,6,,,,,,,,,,,,,,,,,,,,,,1795,1804,2006, citations,citation_1,6925,255671,1,,entry citation,,,16413033,,,"Model for RNA binding and the catalytic site of the RNase Kid of the bacterial parD toxin-antitoxin system",published,journal,J. Mol. Biol.,,357,1,,,,,,,,,,,,,,,,,,,,,,115,126,2006, citations,entry_citation,6926,255683,1,,entry citation,,,17176085,,,Micelle-induced folding of spinach thylakoid soluble phosphoprotein of 9 kDa and its functional implications,published,journal,Biochemistry,,45,51,,,,,,,,,,,,,,,,,,,,,,15633,15643,2006, citations,citation_1,6927,255695,1,,entry citation,,,16607467,,,NMR assignment of the Spinophilin PDZ domain (493-602),published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,24,24,2006, citations,citation_1,6928,255708,1,,entry citation,,,16636755,,,"1H, 13C, and 15N NMR Assignment of the Rep Protein Nuclease Domain from the Porcine Circovirus PCV2",published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,25,25,2006, citations,entry_citation,6929,255726,1,,entry citation,,,,,,Solution NMR Structure of Nitrosomonas Europaea Protein Ne2328,in preparation,journal,Proteins: Struct. Funct. Genet.,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6930,255748,1,,entry citation,,,19727396,,,Structure and Novel Functional Mechanism of Drosophila SNF in Sex-Lethal Splicing,published,journal,PLoS One,,4,9,,,,,,,,,,,,,,,,,,,,,,6890,,2009, citations,citation_1,6932,255761,1,,entry citation,,,16460017,,,"Examination of the structure, stability, and catalytic potential in the engineered phosphoryl carrier domain of pyruvate phosphate dikinase.",published,journal,Biochemistry,,45,6,,,,,,,,,,,,,,,,,,,,,,1702,1711,2006, citations,citation_1,6933,255774,1,,entry citation,,,17279777,,,Structural basis for spinophilin-neurabin receptor interaction.,published,journal,Biochemistry.,,46,9,,,,,,,,,,,,,,,,,,,,,,2333,2344,2007, citations,entry_citation,6934,255793,1,,entry citation,,,16651264,,,"The solution structure of Escherichia coli Wzb reveals a novel substrate recognition mechanism of prokaryotic low molecular weight protein tyrosine phosphatases",published,journal,J. Biol. Chem.,,281,28,,,,,,,,,,,,,,,,,,,,,,19570,19577,2006, citations,entry_citation,6935,255807,1,,entry citation,,,16823035,,,"Comparative NMR study on the impact of point mutations on protein stability of Pseudomonas mendocina lipase",published,journal,Protein Sci.,,15,8,,,,,,,,,,,,,,,,,,,,,,1915,1927,2006, citations,entry_citation,6936,255822,1,,entry citation,,,16601857,,,"Resonance Assignments of the Complex between TraN and the C-terminal Domain of TraO from the Conjugative Plasmid pKM101",published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,31,31,2006, citations,entry_citation,6938,255841,1,,entry citation,,,16636754,,,"NMR Assignment of Region 51-160 of Human KIN17, a DNA and RNA-binding Protein",published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,29,29,2006, citations,citation_1,6939,255856,1,,entry citation,,,15808506,,"Saridakis V, Sheng Y, Sarkari F, Holowaty MN, Shire K, Nguyen T, Zhang RG, Liao J, Lee W, Edwards AM, Arrowsmith CH, Frappier L. Structure of the p53 binding domain of HAUSP/USP7 bound to Epstein-Barr nuclear antigen 1 implications for EBV-mediated immortalization. Mol Cell. 2005 Apr 1;18(1):25-36.","'1H,15N and 13C Assigned Chemical Shifts for USP7 in a complex with an EBNA1 peptide",published,journal,Mol. Cell,,18,1,,,,,,,,,,,,,,,,,,,,,,25,36,2005,The first and second authors contributed equally to this publication citations,citation_2,6939,255857,2,,reference citation,,,16474402,,"Sheng Y, Saridakis V, Sarkari F, Duan S, Wu T, Arrowsmith CH, Frappier L. Molecular Recognition of p53 and Mdm2 by USP7/ HAUSP.",Molecular recognition of p53 and MDM2 by USP7/HAUSP,published,journal,Nat. Struct. Biol.,,13,3,,,,,,,,,,,,,,,,,,,,,,285,291,2006, citations,entry_citation,6940,255874,1,,entry citation,,,16705359,,,"NMR Assignment of 2H, 13C and 15N Labeled Amino-Terminal Domain of Apo-Pantothenate Synthetase from E. coli",published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,38,38,2006, citations,citation_1,6941,255887,1,,entry citation,,,16446433,,,"Polyproline II conformation is one of many local conformational states and is not an overall conformation of unfolded peptides and proteins",published,journal,Proc. Natl. Acad. Sci. U.S.A.,,103,6,,,,,,,,,,,,,,,,,,,,,,1744,1749,2006, citations,citations_Myristoylated_NCS-1,6942,255902,1,,entry citation,,,16804767,,,"1H, 13C, and 15N chemical shift assignments of neuronal calcium sensor-1, a multi-functional calcium-binding protein",published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,48,48,2006, citations,entry_citation,6943,255916,1,,entry citation,,,16819588,,,"1H, 13C, and 15N Resonance Assignment of Bombyx mori Chemosensory Protein 1 (BmorCSP1).",published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,47,47,2006, citations,entry_citation,6944,255931,1,,entry citation,,,16738784,,,"Resonance assignment for the N-terminal region of the eukaryotic initiation factor 5 (eIF5)",published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,42,42,2006, citations,entry_citation,6945,255947,1,,entry citation,,,16906768,,,"Structure, dynamics, and stability variation in bacterial albumin binding modules: implications for species specificity",published,journal,Biochemistry,,45,33,,,,,,,,,,,,,,,,,,,,,,10102,10109,2006, citations,entry_citation,6946,255960,1,,entry citation,,,16968770,,,The nucleotide-binding site of bacterial translation initiation factor 2 (IF2) as a metabolic sensor,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,103,38,,,,,,,,,,,,,,,,,,,,,,13962,13967,2006, citations,citation_1,6947,255978,1,,entry citation,,,16690618,,,"Structural changes of E. coli Ferric uptake regulator during metal-dependent dimerization and activation explored by NMR and X-ray crystallography",published,journal,J. Biol. Chem.,,281,30,,,,,,,,,,,,,,,,,,,,,,21286,21295,2006, citations,citation_1,6948,255998,1,,entry citation,,,16690618,,,"Structural changes of E. coli Ferric uptake regulator during metal-dependent dimerization and activation explored by NMR and X-ray crystallography",published,journal,J. Biol. Chem.,,281,30,,,,,,,,,,,,,,,,,,,,,,21286,21295,2006, citations,entry_citation,6949,256012,1,,entry citation,,,16865416,,,NMR assignment of domain 2 of the receptor-associated protein,published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,54,54,2006, citations,entry_citation,695,256024,1,,entry citation,,,,,"Adjadj, Elisabeth, Mispelter, Joel, Quiniou, Eric, Dimicoli, Jean-Luc, Favaudon, Vincent, Lhoste, Jean-Marc, ""Proton NMR studies of apo-neocarzinostatin from Streptomyces carzinostaticus Sequence-specific assignment and secondary structure,"" Eur. J. Biochem. 190, 263-271 (1990).","Proton NMR studies of apo-neocarzinostatin from Streptomyces carzinostaticus Sequence-specific assignment and secondary structure",published,journal,Eur. J. Biochem.,,190,,,,,,,,,,,,,,,,,,,,,,,263,271,1990, citations,entry_citation,6950,256037,1,,entry citation,,,17016671,,,NMR assignment of domain 3 of the receptor-associated protein (RAP),published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,56,56,2006, citations,entry_citation,6951,256049,1,,entry citation,,,16819832,,,"A Novel Conotoxin Inhibitor of Kv1.6 Channel and nAChR Subtypes Defines a New Superfamily of Conotoxins",published,journal,Biochemistry,,45,27,,,,,,,,,,,,,,,,,,,,,,8331,8340,2006, citations,entry_citation,6952,256067,1,,entry citation,,,16488428,,,"Discovery and Characterization of a Linear Cyclotide from Viola odorata: Implications for the Processing of Circular Proteins",published,journal,J. Mol. Biol.,,357,5,,,,,,,,,,,,,,,,,,,,,,1522,1535,2006, citations,entry_citation,6953,256085,1,,entry citation,,,17415669,,,"1H, 13C and 15N resonance assignments of rabbit prion protein (91-228)",published,journal,J. Biomol. NMR,,38,2,,,,,,,,,,,,,,,,,,,,,,181,181,2007, citations,entry_citation,6954,256100,1,,entry citation,,,16407195,,,"Fusion peptide of influenza hemagglutinin requires a fixed angle boomerang structure for activity",published,journal,J. Biol. Chem.,,281,9,,,,,,,,,,,,,,,,,,,,,,5760,5770,2006, citations,entry_citation,6955,256114,1,,entry citation,,,16937244,,,The solution structure of the protein ydhA from Escherichia coli,published,journal,J. Biomol. NMR,,35,4,,,,,,,,,,,,,,,,,,,,,,295,300,2006, citations,entry_citation,6956,256132,1,,entry citation,,,16429155,,,RNA recognition by the Vts1p SAM domain,published,journal,Nat. Struct. Mol. Biol.,,13,2,,,,,,,,,,,,,,,,,,,,,,177,178,2006, citations,entry_citation,6957,256149,1,,entry citation,,,16950398,,,Structure of the SCAN domain from the tumor suppressor protein MZF1,published,journal,J. Mol. Biol.,,363,1,,,,,,,,,,,,,,,,,,,,,,137,147,2006, citations,entry_citation,6960,256170,1,,entry citation,,,16426974,,,"Target structure-based discovery of small molecules that block human p53 and CREB binding protein association",published,journal,Chem. Biol.,,13,1,,,,,,,,,,,,,,,,,,,,,,81,90,2006, citations,entry_citation,6962,256188,1,,entry citation,,,16618110,,,Solution Structures of Spinach Acyl Carrier Protein with Decanoate and Stearate,published,journal,Biochemistry,,45,16,,,,,,,,,,,,,,,,,,,,,,5217,5227,2006, citations,Production_paper,6962,256189,2,,reference citation,,,16325425,,,"Preparation of isotopically labeled spinach acyl-acyl carrier protein for NMR structural studies",published,journal,Prot. Expr. Purif.,,46,2,,,,,,,,,,,,,,,,,,,,,,446,455,2006, citations,entry_citation,6963,256212,1,,entry citation,,,16791741,,,Second Kunitz-type protease inhibitor domain of the human WFIKKN1 protein,published,journal,J. Biomol. NMR,,35,1,,,,,,,,,,,,,,,,,,,,,,73,78,2006, citations,entry_citation,6964,256226,1,,entry citation,,,,,,NMR structure of the Rpa2829 protein from Rhodopseudomonas palustris,published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6965,256241,1,,entry citation,,,16554303,,,"The electron transfer complex between cytochrome c552 and the CuA domain of the Thermus thermophilus ba3 oxidase - a combined NMR and computational approach",published,journal,J. Biol. Chem.,,281,20,,,,,,,,,,,,,,,,,,,,,,14503,14513,2006, citations,reference_1,6965,256242,2,,reference citation,,,8639488,,"Slutter CE, Sanders D, Wittung P, Malmstrom BG, Aasa R, Richards JH, Gray HB, Fee JA. Water-soluble, recombinant CuA-domain of the cytochrome ba3 subunit II from Thermus thermophilus. Biochemistry. 1996 Mar 19;35(11):3387-95.","Water-soluble, recombinant CuA-domain of the cytochrome ba3 subunit II from Thermus thermophilus.",published,journal,Biochemistry,Biochemistry,35,11,,0006-2960,,,,,,,,,,,,,,,,,,,,3387,3395,1996,"Recently, the genes of cytochrome ba3 from thermus thermophilus [Keightley, J.A., et al. (1995) J. Biol. Chem. 270, 20345-20358], a homolog of the heme-copper oxidase family, have been cloned. We report here expression of a truncated gene, encoding the copper A (CuA) domain of cytochrome ba3, that is regulated by a T7 RNA polymerase promoter in Escherichia coli. The CuA-containing domain is purified in high yields as a water-soluble, thermostable, purple-colored protein. Copper analysis by chemical assay, mass spectrometry, X-ray fluorescence, and EPR spin quantification show that this protein contains two copper ions bound in a mixed-valence state, indicating that the CuA site in cytochrome ba3, is a binuclear center. The absorption spectrum of the CuA site, free of the heme interference in cytochrome ba3, is similar to the spectra of other soluble fragments from the aa3-type oxidase of Parachccus denitrificans [Lappalainen, P., et al. (1993) J. Biol Chem. 268, 26416-26421] and the caa3-type oxidase of Bacillus subtilis [von Wachenfeldt, C. et al. (1994) FEBS Lett. 340, 109-113]. There are intense bands at 480 nm (3100 M(-1) cm(-1)) and 530 nm (3200 M(-1) cm(-1)), a band in the near -IR centered at 790 nm (1900 M(-1) cn(-1)), and a weaker band at 363 nm (1300M(-1) cm(-1)). The visible CD spectrum shows a positive-going band at 460 nm and a negative-going band at 527 nm, the opposite signs of which may result from the binuclear nature of the site. The secondary structure prediction from the far-UV CD spectrum indicates that this domain is predominantly beta-sheet, in agreement with the recent X-ray structure reported for the complete P. denitrificans cytochrome aa3 molecule [Iwata, S., et al. (1995) Nature 376, 660-669] and the engineered, purple CyoA protein [Wilmanns, M., et al. (1996) Proc. Natl Acad. Sci. U.S.A. 92, 11955-11959]. However, the thermostability of the fragment described here (Tm approximately 80 degrees C) and the stable binding of copper over a broad pH range (pH 3-9) suggest this protein may be uniquely suitable for detailed physical-chemical study." citations,entry_citation,6966,256262,1,,entry citation,,,16554303,,,"The electron transfer complex between cytochrome c552 and the CuA domain of the Thermus thermophilus ba3 oxidase - a combined NMR and computational approach",published,journal,J. Biol. Chem.,,281,20,,,,,,,,,,,,,,,,,,,,,,14503,14513,2006, citations,entry_citation,6967,256279,1,,entry citation,,,16554303,,,"The electron transfer complex between cytochrome c552 and the CuA domain of the Thermus thermophilus ba3 oxidase - a combined NMR and computational approach",published,journal,J. Biol. Chem.,,281,20,,,,,,,,,,,,,,,,,,,,,,14503,14513,2006, citations,entry_citation,6968,256297,1,,entry citation,,,16551093,,,Protonless NMR experiments for sequence-specific assignment of backbone nuclei in unfolded proteins,published,journal,J. Am. Chem. Soc.,,128,12,,,,,,,,,,,,,,,,,,,,,,3918,3919,2006, citations,reference_citation,6968,256298,2,,reference citation,,,22684679,,,Speeding up sequence specific assignment of IDPs,published,journal,J. Bimol. NMR,,53,4,,,,,,,,,,,,,,,,,,,,,,293,301,2012, citations,citation_1,6969,256312,1,,entry citation,,,16507566,,,Solution structure of the SARS-coronavirus HR2 domain in the prefusion state,published,journal,J. Biol. Chem.,,281,17,,,,,,,,,,,,,,,,,,,,,,11965,11971,2006, citations,citation1,6970,256325,1,,entry citation,,,16858624,,,"1H, 15N, 13C assignments for the activated form of the small Rho-GTPase Rac1",published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,51,51,2006, citations,citation_1,6971,256343,1,,entry citation,,,16819589,,,NMR Assignments of the b' and a' Domains of Thermophilic Fungal Protein Disulfide Isomerase,published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,44,44,2006, citations,citation_1,6972,256357,1,,entry citation,,,16819589,,,NMR Assignments of the b' and a' Domains of Thermophilic Fungal Protein Disulfide Isomerase,published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,44,44,2006, citations,entry_citation,6973,256371,1,,entry citation,,,16565516,,,Localization of sites of interaction between p23 and Hsp90 in solution,published,journal,J. Biol. Chem.,,281,20,,,,,,,,,,,,,,,,,,,,,,14457,14464,2006, citations,entry_citation,6974,256385,1,,entry citation,,,16565516,,,Localization of sites of interaction between p23 and Hsp90 in solution,published,journal,J. Biol. Chem.,,281,20,,,,,,,,,,,,,,,,,,,,,,14457,14464,2006, citations,entry_citation,6975,256399,1,,entry citation,,,,,,"An intramolecular G-quadruplex structure with mixed parallel/antiparallel G-strands formed in the human BCL-2 promoter region in solution",published,journal,J. Am. Chem. Soc.,,128,4,,,,,,,,,,,,,,,,,,,,,,1096,1098,2006, citations,entry_citation,6976,256410,1,,entry citation,,,,,,"Solution NMR structure of the UPF0346 protein yozE from Bacillus subtilis. Northeast Structural Genomics target SR391.",submitted,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6979,256430,1,,entry citation,,,,,,"An Alternating Sheared AA Pair and Elements of Stability for a Single Sheared Purine-Purine Pair Flanked by Sheared GA Pairs in RNA",published,journal,Biochemistry,,45,22,,,,,,,,,,,,,,,,,,,,,,6889,6903,2006, citations,entry_citation,6980,256451,1,,entry citation,,,,,,Solution Structure of Human Allograft Inflammatory Factor I,in preparation,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,6981,256467,1,,entry citation,,,16631790,,,"Solution Structure of Monomeric BsaL, the Type III Secretion Needle Protein of Burkholderia pseudomallei",published,journal,J. Mol. Biol.,,359,2,,,,,,,,,,,,,,,,,,,,,,322,330,2006, citations,entry_citation,6982,256479,1,,entry citation,,,17019685,,,"Solution structure of TA0895, a MoaD homologue from Thermoplasma acidophilum",published,journal,Proteins: Struct. Funct. Genet.,,65,4,,,,,,,,,,,,,,,,,,,,,,1055,1057,2006, citations,entry_citation,6983,256497,1,,entry citation,,,16584193,,,"Backbone NMR Assignments and H/D Exchange Studies on the Ferric Azide- and Cyanide-Inhibited Forms of Pseudomonas aeruginosa Heme Oxygenase",published,journal,Biochemistry,,45,14,,,,,,,,,,,,,,,,,,,,,,4578,4592,2006, citations,entry_citation,6984,256514,1,,entry citation,,,17016670,,,NMR assignment of the cAMP-binding domain A of the PKA regulatory subunit,published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,64,64,2006, citations,citation_1,6985,256530,1,,entry citation,,,16917728,,,NMR assignment of the Cyclin T-binding domain of human Hexim 1,published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,39,39,2006, citations,entry_citation,6986,256550,1,,entry citation,,,16705357,,,NMR assignment of the phosphotyrosine binding (PTB) domain of tensin,published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,40,40,2006, citations,entry_citation,6987,256566,1,,entry citation,,,16584193,,,"Backbone NMR Assignments and H/D Exchange Studies on the Ferric Azide- and Cyanide-Inhibited Forms of Pseudomonas aeruginosa Heme Oxygenase",published,journal,Biochemistry,,45,14,,,,,,,,,,,,,,,,,,,,,,4578,4592,2006, citations,entry_citation,6988,256584,1,,entry citation,,,16731964,,,"Solution structure of the ubiquitin-associated domain of human BMSC-UbP and its complex with ubiquitin",published,journal,Protein Sci.,,15,6,,,,,,,,,,,,,,,,,,,,,,1248,1259,2006, citations,citation_1,6989,256598,1,,entry citation,,,10476961,,,Placement of protein and RNA structures into a 5 A-resolution map of the 50S ribosomal subunit.,published,journal,Nature,,400,6747,,,,,,,,,,,,,,,,,,,,,,841,847,1999, citations,entry_citation,699,256614,1,,entry citation,,,,,"van de Ven, F. J. M., Hilbers, C. W., ""Sequential Resonance Assignments as a Basis for the Determination of a Three-dimensional Structure of Protein E-L30 of Escherichia coli,"" J. Mol. Biol. 192, 419-441 (1986).","Sequential Resonance Assignments as a Basis for the Determination of a Three-dimensional Structure of Protein E-L30 of Escherichia coli",published,journal,J. Mol. Biol.,,192,,,,,,,,,,,,,,,,,,,,,,,419,441,1986, citations,citation_1,6990,256628,1,,entry citation,,,10455173,,,"Purification, Characterization and Amino Acid Sequence of Cerato-platanin, a New Phytotoxic Protein from Ceratocystis fimbriata f. sp. platani.",published,journal,J. Biol. Chem.,,274,,,,,,,,,,,,,,,,,,,,,,,24959,24964,1999, citations,citation_2,6990,256629,2,,entry citation,,,16819587,,,"1H, 15N and 13C Resonance Assignments of Cerato-platanin, a Phytotoxic Protein from Ceratocystis fimbriata.",published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,50,50,2006, citations,citation_for_TFCD,6991,256644,1,,entry citation,,,20076769,,,Spectroscopic Characterization of Successive Phosphorylation of the Tissue Factor Cytoplasmic Region,published,journal,Open Spectrosc J.,The open spectroscopy journal,3,,,1874-3838,,,,,,,,,,,,,,,,,,,,58,64,2009, citations,entry_citation,6992,256660,1,,entry citation,,,16537437,,,Three-dimensional structure of the bacterial cell wall peptidoglycan,published,journal,Proc. Natl. Acad. Sci. U. S. A.,,103,12,,,,,,,,,,,,,,,,,,,,,,4404,4409,2006, citations,entry_citation,6993,256681,1,,entry citation,,,20076769,,,Spectroscopic Characterization of Successive Phosphorylation of the Tissue Factor Cytoplasmic Region,published,journal,Open Spectrosc J.,The open spectroscopy journal,3,,,1874-3838,,,,,,,,,,,,,,,,,,,,58,64,2009, citations,entry_citation,6995,256697,1,,entry citation,,,16968770,,,The nucleotide-binding site of bacterial translation initiation factor 2 (IF2) as a metabolic sensor,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,103,38,,,,,,,,,,,,,,,,,,,,,,13962,13967,2006, citations,entry_citation,6996,256717,1,,entry citation,,,20076769,,,Spectroscopic Characterization of Successive Phosphorylation of the Tissue Factor Cytoplasmic Region,published,journal,Open Spectrosc J.,The open spectroscopy journal,3,,,1874-3838,,,,,,,,,,,,,,,,,,,,58,64,2009, citations,entry_citation,6997,256733,1,,entry citation,,,16603186,,,"Structural Insights of the Specificity and Catalysis of a Viral Histone H3 Lysine 27 Methyltransferase.",published,journal,J. Mol. Biol.,,359,1,,,,,,,,,,,,,,,,,,,,,,86,89,2006, citations,entry_citation,6998,256752,1,,entry citation,,,20076769,,,Spectroscopic Characterization of Successive Phosphorylation of the Tissue Factor Cytoplasmic Region,published,journal,Open Spectrosc J.,The open spectroscopy journal,3,,,1874-3838,,,,,,,,,,,,,,,,,,,,58,64,2009, citations,entry_citation,6999,256768,1,,entry citation,,,16944275,,,"1H, 13C and 15N assignments of the KorA global transcriptional repressor protein from the low copy number IncP-1 plasmid, RK2",published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,71,71,2006, citations,entry_citation,7,256783,1,,entry citation,,,,,"Carver, John A., ""The conformation of bombesin in solution as determined by two-dimensional 1H-NMR techniques,"" Eur. J. Biochem. 168, 193-199 (1987).","The conformation of bombesin in solution as determined by two-dimensional 1H-NMR techniques",published,journal,Eur. J. Biochem.,,168,,,,,,,,,,,,,,,,,,,,,,,193,199,1987, citations,entry_citation,700,256796,1,,entry citation,,,,,"Coddington, Jan M., Barling, Peter M., ""Proton Nuclear Magnetic Resonance Studies of Intact Native Bovine Parathyroid Hormone,"" Mol. Endocrinol. 3 (4), 749-753 (1989).","Proton Nuclear Magnetic Resonance Studies of Intact Native Bovine Parathyroid Hormone",published,journal,Mol. Endocrinol.,,3,4,,,,,,,,,,,,,,,,,,,,,,749,753,1989, citations,entry_citation,7000,256809,1,,entry citation,,,16885468,,,Solution structure of the conserved hypothetical protein Rv2302 from the bacterium Mycobacterium tuberculosis,published,journal,J. Bacteriol.,,188,16,,,,,,,,,,,,,,,,,,,,,,5993,6001,2006, citations,Publi_1,7001,256823,1,,entry citation,,,16996060,,,"STD and TRNOESY NMR Studies for the Epitope Mapping of the Phosphorylation Motif of the oncogenic Protein beta-Catenin Recognized By a Selective Monoclonal Antibody",published,journal,FEBS Lett.,,580,22,,,,,,,,,,,,,,,,,,,,,,5411,5422,2006, citations,entry_citation,7002,256840,1,,entry citation,,,16563434,,,Structural Basis for Monoubiquitin Recognition by the Ede1 UBA Domain,published,journal,J. Mol. Biol.,,358,3,,,,,,,,,,,,,,,,,,,,,,713,724,2006, citations,entry_citation,7003,256851,1,,entry citation,,,16821127,,,NMR Backbone Assignment of the N-terminal Domain of Human HSP90,published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,52,52,2006, citations,entry_citation,7004,256863,1,,entry citation,,,,,,NMR structure of Rpa0253 from Rhodopseudomonas paulstris,published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,7005,256877,1,,entry citation,,,16819834,,,"The PP-Fold Solution Structure of Human Polypeptide YY and Human PYY3-36 As Determined by NMR",published,journal,Biochemistry,,45,27,,,,,,,,,,,,,,,,,,,,,,8350,8357,2006, citations,entry_citation,7006,256899,1,,entry citation,,,16819834,,,"The PP-Fold Solution Structure of Human Polypeptide YY and Human PYY3-36 As Determined by NMR(,).",published,journal,Biochemistry,,45,27,,,,,,,,,,,,,,,,,,,,,,8350,8357,2006, citations,entry_citation,7007,256921,1,,entry citation,,,16754964,,,"Solution structure of Arabidopsis thaliana protein At5g39720.1, a member of the AIG2-like protein family",published,journal,Acta Crystallograph Sect. F Struct. Biol. Cryst. Commun.,,62,Pt. 6,,,,,,,,,,,,,,,,,,,,,,490,493,2006, citations,entry_citation,7008,256943,1,,entry citation,,,16600866,,,"Ca(2+) regulation in the na(+)/ca(2+) exchanger involves two markedly different ca(2+) sensors",published,journal,Mol. Cell.,,22,1,,,,,,,,,,,,,,,,,,,,,,15,25,2006, citations,entry_citation,7009,256965,1,,entry citation,,,16600866,,,"Ca(2+) regulation in the na(+)/ca(2+) exchanger involves two markedly different ca(2+) sensors",published,journal,Mol. Cell.,,22,1,,,,,,,,,,,,,,,,,,,,,,15,25,2006, citations,entry_citation,7010,256987,1,,entry citation,,,17068840,,,"Synthesis, Solution Structure and Immune Recognition of an Epidermal Growth Factor-Like Domain from Plasmodium falciparum Merozoite Surface Protein-1",published,journal,ChemBioChem,,7,12,,,,,,,,,,,,,,,,,,,,,,1943,1950,2006, citations,entry_citation,7011,257006,1,,entry citation,,,16767771,,,"Two peptide fragments G55-I72 and K97-A109 from staphylococcal nuclease exhibit different behaviors in conformational preferences for helix formation",published,journal,Biopolymers,,83,3,,,,,,,,,,,,,,,,,,,,,,268,279,2006, citations,entry_citation,7012,257027,1,,entry citation,,,16767771,,,"Two peptide fragments G55-I72 and K97-A109 from staphylococcal nuclease exhibit different behaviors in conformational preferences for helix formation",published,journal,Biopolymers,,83,3,,,,,,,,,,,,,,,,,,,,,,268,279,2006, citations,citation_1,7013,257049,1,,entry citation,,,17223694,,,Heat-induced dimerization of Bcl-xL through alpha-helix swapping,published,journal,Biochemistry,,46,3,,,,,,,,,,,,,,,,,,,,,,734,740,2007, citations,citation_2,7013,257050,2,,reference citation,,,,,,Symmetric Bcl-xL protein dimerization by alpha-helix swapping,published,abstract,,,,,,,,,,,,,,,ANZMAG-2006,Murramarang National Park,New South Wales,Australia,2006-02-12,2006-02-16,O46,,,,,,,2006, citations,entry_citation,7014,257063,1,,entry citation,,,16821128,,,NMR assignment of the SARS-CoV protein nsp1,published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,46,46,2006,Letter to the Editor. citations,entry_citation,7015,257076,1,,entry citation,,,12450379,,,"Calcium-induced conformational switching of Paramecium calmodulin provides evidence for domain coupling.",published,journal,Biochemistry,,41,48,,,,,,,,,,,,,,,,,,,,,,14158,14166,2002, citations,entry_citation,7016,257101,1,,entry citation,,,9753463,,,Ca2+ binding and conformational changes in a calmodulin domain.,published,journal,Biochemistry,,37,39,,,,,,,,,,,,,,,,,,,,,,13744,13754,1998, citations,entry_citation,7017,257121,1,,entry citation,,,9753463,,,Ca2+ binding and conformational changes in a calmodulin domain.,published,journal,,,37,39,,,,,,,,,,,,,,,,,,,,,,13744,13754,1998, citations,entry_citation,7018,257139,1,,entry citation,,,14984199,,,"Spectroscopic characterization of the calmodulin-binding and autoinhibitory domains of calcium/calmodulin-dependent protein kinase I",published,journal,Arch. Biochem. Biophys.,,421,2,,,,,,,,,,,,,,,,,,,,,,192,206,2004, citations,entry_citation,7019,257157,1,,entry citation,,,16799860,,,NMR assignment of the protein nsp3a from SARS-CoV,published,journal,J. Biomol. NMR,,36,Suppl 5,,,,,,,,,,,,,,,,,,,,,,45,45,2006, citations,entry_citation,7020,257170,1,,entry citation,,,16632472,,,"Structural, biochemical, and dynamic characterizations of the hRPB8 subunit of human RNA polymerases",published,journal,J. Biol. Chem.,,281,26,,,,,,,,,,,,,,,,,,,,,,18216,18226,2006, citations,entry_citation,7021,257183,1,,entry citation,,,17014083,,,Domain Motions of the Mip Protein from Legionella pneumophila,published,journal,Biochemistry,,45,40,,,,,,,,,,,,,,,,,,,,,,12303,12311,2006, citations,entry_citation,7022,257210,1,,entry citation,,,16865415,,,"1H, 13C and 15N backbone resonance assignments of the DUF589 domain from human HSPC144 protein.",published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,57,57,2006, citations,entry_citation,7023,257234,1,,entry citation,,,16738786,,,"Assignment of 1H, 13C, and 15N resonances for the REF2-I mRNA export factor",published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,41,41,2006,The first and second authors contributed equally to this publication. citations,reference_1,7023,257235,2,,reference citation,,,15264823,,,A simple method for improving protein solubility and long-term stability.,published,journal,J. Am. Chem. Soc.,,126,29,,,,,,,,,,,,,,,,,,,,,,8933,8939,2004, citations,entry_citation,7024,257263,1,,entry citation,,,16804766,,,Resonance assignments of the 34 kD rabbitpox vCCI:human MIP-1beta complex,published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,49,49,2006, citations,citation1,7025,257288,1,,entry citation,,,17031525,,,"1H, 13C, and 15N Resonance Assignments of the VAP-A:OSBP Complex",published,journal,J. Biomol. NMR,,36,Suppl. 5,,,,,,,,,,,,,,,,,,,,,,69,69,2006, citations,entry_citation,7028,257304,1,,entry citation,,,8563635,,,"Role of the N-terminal region of the skeletal muscle myosin light chain kinase target sequence in its interaction with calmodulin",published,journal,Protein Sci.,,4,11,,,,,,,,,,,,,,,,,,,,,,2375,2382,1995, citations,entry_citation,7029,257319,1,,entry citation,,,8563635,,,"Role of the N-terminal region of the skeletal muscle myosin light chain kinase target sequence in its interaction with calmodulin",published,journal,Protein Sci.,,4,11,,,,,,,,,,,,,,,,,,,,,,2375,2382,1995, citations,entry_citation,7030,257334,1,,entry citation,,,8563635,,,"Role of the N-terminal region of the skeletal muscle myosin light chain kinase target sequence in its interaction with calmodulin",published,journal,Protein Sci.,,4,11,,,,,,,,,,,,,,,,,,,,,,2375,2382,1995, citations,entry_citation,7031,257349,1,,entry citation,,,8563635,,,"Role of the N-terminal region of the skeletal muscle myosin light chain kinase target sequence in its interaction with calmodulin",published,journal,Protein Sci.,,4,11,,,,,,,,,,,,,,,,,,,,,,2375,2382,1995, citations,BMRB_Chemical_Shifts_for_KIV8,7032,257364,1,,entry citation,,,17263558,,,"Nuclear magnetic resonance (NMR) solution structure, dynamics, and binding properties of the kringle IV type 8 module of apolipoprotein(a)",published,journal,Biochemistry,,46,7,,,,,,,,,,,,,,,,,,,,,,1732,1742,2007, citations,entry_citation,7033,257391,1,,entry citation,,,,,,"1H Assigned Chemical Shifts for eRF3a, and 1H, 13C, and 15N Assigned Chemical Shifts for PABC",in preparation,journal,J. 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Immun.,,75,1,,,,,,,,,,,,,,,,,,,,,,61,73,2007, citations,citation_1,7216,260324,1,,entry citation,,,,,,"Backbone 1H, 13C, and 15N Chemical Shift Assignments for yeast triosephosphate isomerase, TIM",in preparation,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,7218,260344,1,,entry citation,,,17043745,,,"(1)H, (13)C, and (15)N NMR assignment of the master Rep protein nuclease domain from the Nanovirus FBNYV",published,journal,J. Biomol. NMR,,38,2,,,,,,,,,,,,,,,,,,,,,,169,169,2007, citations,entry_citation,7219,260368,1,,entry citation,,,16893187,,"D. Duong Hau, Michael J. Lewis, Linda F. Saltibus, Landon Pastushok, Wei Xiao, and Leo Spyracopoulos. Structure and Interactions of the Ubiquitin-Conjugating Enzyme Variant Human Uev1: Implications fro Enzymatic Synthesis of Polyubiquitin Chains. Biochemistry, in the press, 2006.","Structure and interactions of the ubiquitin-conjugating enzyme variant human Uev1a: implications for enzymatic synthesis of polyubiquitin chains",published,journal,Biochemistry,,45,32,,,,,,,,,,,,,,,,,,,,,,9866,9877,2006, citations,entry_citation,7220,260410,1,,entry citation,,,17061024,,,NMR assignment of Human ephrinB2 ectodomain,published,journal,J. Biomol. NMR,,38,2,,,,,,,,,,,,,,,,,,,,,,171,171,2007, citations,entry_citation,7221,260431,1,,entry citation,,,17307731,,,Determining the molecular basis for the pH-dependent interaction between the Link module of human TSG-6 and hyaluronan,published,journal,J. Biol. Chem.,,282,17,,,,,,,,,,,,,,,,,,,,,,12976,12988,2007, citations,entry_citation,7223,260515,1,,entry citation,,,,,,"Solution NMR structure of the C-terminal domain of the interferon alpha-inducible ISG15 protein from Homo sapiens. Northeast Structural Genomics target HR2873B.",submitted,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,7224,260548,1,,entry citation,,,,,,"Solution NMR structure of Phage-like element PBSX protein xkdW, Northeast Structural Genomics Consortium Target SR355",submitted,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,7225,260572,1,,entry citation,,,18431750,,,Solution NMR structure of the SOS response protein YnzC from Bacillus subtilis,published,journal,Proteins,,72,1,,,,,,,,,,,,,,,,,,,,,,526,530,2008, citations,entry_citation,7226,260608,1,,entry citation,,,,,,"Solution NMR Structure of Conserved protein MTH1368, Northeast Structural Genomics Consortium Target TT821A",submitted,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,7227,260632,1,,entry citation,,,,,,"Solution NMR structure of hypothetical protein yppE: Northeast Structural Genomics Consortium Target SR213",submitted,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,7228,260659,1,,entry citation,,,,,,"Solution NMR structure of UPF0107 protein AF_0055, Northeast Structural Genomics Consortium Target GR101 (CASP Target)",submitted,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,7229,260683,1,,entry citation,,,16987528,,,"Structural Determinants Involved in the Regulation of CXCL14/BRAK Expression by the 26 S Proteasome",published,journal,J. Mol. Biol.,,363,4,,,,,,,,,,,,,,,,,,,,,,813,822,2006, citations,entry_citation,7230,260706,1,,entry citation,,,17002278,,,"The NMR Structure of an Internal Loop from 23S Ribosomal RNA Differs from Its Structure in Crystals of 50S Ribosomal Subunits",published,journal,Biochemistry,,45,39,,,,,,,,,,,,,,,,,,,,,,11776,11789,2006, citations,entry_citation,7231,260726,1,,entry citation,,,16905148,,,A novel haem-binding interface in the 22 kDa haem-binding protein p22HBP,published,journal,J. Mol. Biol.,,362,2,,,,,,,,,,,,,,,,,,,,,,287,297,2006, citations,entry_citation,7232,260748,1,,entry citation,,,16933352,,,"A Photoswitchable Miniprotein based on the Sequence of Avian Pancreatic Polypeptide",published,journal,Angew Chem. Int. Ed. Engl.,,45,38,,,,,,,,,,,,,,,,,,,,,,6297,6300,2006, citations,entry_citation,7233,260770,1,,entry citation,,,16933352,,,"A Photoswitchable Miniprotein Based on the Sequence of Avian Pancreatic Polypeptide",published,journal,Angew Chem. Int. Ed. Engl.,,45,38,,,,,,,,,,,,,,,,,,,,,,6297,6300,2006, citations,citation_1,7234,260799,1,,entry citation,,,16990434,,,A trojan horse transition state analogue generated by MgF3- formation in an enzyme active site,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,103,40,,,,,,,,,,,,,,,,,,,,,,14732,14737,2006,The first three authors contributed equally to this publication citations,citation_1,7235,260828,1,,entry citation,,,16990434,,,A trojan horse transition state analogue generated by MgF3- formation in an enzyme active site,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,103,40,,,,,,,,,,,,,,,,,,,,,,14732,14737,2006,The first three authors contributed equally to this publication citations,Citation_1,7236,260852,1,,entry citation,,,16981701,,,Backbone dynamics of TEM-1 determined by NMR: evidence for a highly ordered protein.,published,journal,Biochemistry,,45,38,,,,,,,,,,,,,,,,,,,,,,11414,11424,2006,The first and second authors contributed equally to this work. citations,Citation_1,7237,260872,1,,entry citation,,,16981701,,,Backbone dynamics of TEM-1 determined by NMR: evidence for a highly ordered protein.,published,journal,Biochemistry,,45,38,,,,,,,,,,,,,,,,,,,,,,11414,11424,2006,The first and second authors contributed equally to this work. citations,Citation_1,7238,260892,1,,entry citation,,,16981701,,,Backbone dynamics of TEM-1 determined by NMR: evidence for a highly ordered protein.,published,journal,Biochemistry,,45,38,,,,,,,,,,,,,,,,,,,,,,11414,11424,2006,The first and second authors contributed equally to this work. citations,Citation_1,7239,260912,1,,entry citation,,,16981701,,,Backbone dynamics of TEM-1 determined by NMR: evidence for a highly ordered protein.,published,journal,Biochemistry,,45,38,,,,,,,,,,,,,,,,,,,,,,11414,11424,2006,The first and second authors contributed equally to this work. citations,citation_1,7240,260931,1,,entry citation,,,17036161,,,Backbone Assignment of the 98kDa homotrimeric yeast PCNA ring,published,journal,J. Biomol. NMR,,38,2,,,,,,,,,,,,,,,,,,,,,,167,167,2006, citations,Citation_1,7241,260961,1,,entry citation,,,,,,"Structural Characterization of the Interface of the Subunits Chloroplast Signal Recognition Particle (cpSRP) ? Determination of the Three-Dimensional Solution Structure of the Chromo Domain 2 ? cpSRP54 Peptide Complex",in preparation,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,7242,260977,1,,entry citation,,,18004775,,,Human uroporphyrinogen III synthase: NMR-based mapping of the active site,published,journal,Proteins,,71,2,,,,,,,,,,,,,,,,,,,,,,855,873,2008, citations,entry_citation,7243,261004,1,,entry citation,,,16930619,,,Solution structures of human and porcine beta-microseminoprotein,published,journal,J. Mol. Biol.,,362,3,,,,,,,,,,,,,,,,,,,,,,502,515,2006, citations,entry_citation,7244,261024,1,,entry citation,,,17088319,,,"Sensitivity of secondary structure propensities to sequence differences between a- and g-synuclein: Implications for fibrillation",published,journal,Protein Sci.,,15,12,,,,,,,,,,,,,,,,,,,,,,2795,2804,2006, citations,entry_citation,7245,261039,1,,entry citation,,,16861220,,,"Structural and functional characterization of transmembrane segment VII of the Na+/H+ exchanger isoform 1.",published,journal,J. Biol. Chem.,,281,40,,,,,,,,,,,,,,,,,,,,,,29817,29829,2006,The first and second authors contributed equally to this publication. citations,entry_citation,7246,261060,1,,entry citation,,,10734220,,"Perez-Alvarado, G.C., Munnerlyn, A., Dyson, H.J., Grosschedl, R. and Wright, P.E. 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NMR Assignments,,1,1,,,,,,,,,,,,,,,,,,,,,,3,5,2007, citations,citation_2,7248,261111,2,,reference citation,,,12581519,,,Coaxing the LDL receptor family into the fold,published,journal,Cell,,112,3,,,,,,,,,,,,,,,,,,,,,,289,292,2003, citations,entry_citation,7249,261129,1,,entry citation,,,17122951,,,NMR assignment of the human spliceosomeal 15.5K protein,published,journal,J. Biomol. NMR,,38,2,,,,,,,,,,,,,,,,,,,,,,175,175,2007, citations,entry_citation,7250,261157,1,,entry citation,,,16840558,,,Structural Basis for targeting HIV-1 Gag proteins to the plasma membrane for virus assembly,published,journal,Proc. Natl. Acad. Sci. U.S.A.,,103,30,,,,,,,,,,,,,,,,,,,,,,11364,11369,2006, citations,entry_citation,7251,261176,1,,entry citation,,,18076077,,,Solvent-exposed residues located in the beta-sheet modulate the stability of the tetramerization domain of p53-A structural and combinatorial approach,published,journal,Proteins,,71,4,,,,,,,,,,,,,,,,,,,,,,1670,1685,2008, citations,entry_citation,7252,261194,1,,entry citation,,,18076077,,,Solvent-exposed residues located in the beta-sheet modulate the stability of the tetramerization domain of p53-A structural and combinatorial approach,published,journal,Proteins,,71,4,,,,,,,,,,,,,,,,,,,,,,1670,1685,2008, citations,entry_citation,7253,261212,1,,entry citation,,,18076077,,,Solvent-exposed residues located in the beta-sheet modulate the stability of the tetramerization domain of p53-A structural and combinatorial approach,published,journal,Proteins,,71,4,,,,,,,,,,,,,,,,,,,,,,1670,1685,2008, citations,entry_citation,7254,261230,1,,entry citation,,,18076077,,,Solvent-exposed residues located in the beta-sheet modulate the stability of the tetramerization domain of p53-A structural and combinatorial approach,published,journal,Proteins,,71,4,,,,,,,,,,,,,,,,,,,,,,1670,1685,2008, citations,entry_citation,7255,261248,1,,entry citation,,,18076077,,,Solvent-exposed residues located in the beta-sheet modulate the stability of the tetramerization domain of p53-A structural and combinatorial approach,published,journal,Proteins,,71,4,,,,,,,,,,,,,,,,,,,,,,1670,1685,2008, citations,entry_citation,7256,261265,1,,entry citation,,,,,,"NMR structure of protein Hydrogenase-1 operon protein hyaE from Escherichia coli: Northeast Structural Genomics Consortium Target ER415",submitted,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,7257,261291,1,,entry citation,,,17036044,,,"Molecular basis of RNA recognition and TAP binding by the SR proteins SRp20 and 9G8",published,journal,EMBO J.,,25,21,,,,,,,,,,,,,,,,,,,,,,5126,5137,2006, citations,entry_citation,7258,261312,1,,entry citation,,,17052982,,,"Structural characterization and oligomerization of PB1-F2, a pro-apoptotic influenza A virus protein",published,journal,J. Biol. Chem.,,282,1,,,,,,,,,,,,,,,,,,,,,,353,363,2006, citations,entry_citation,7259,261328,1,,entry citation,,,17915942,,,Solution Structure of Polymerase mu's BRCT Domain Reveals an Element Essential for Its Role in Nonhomologous End Joining.,published,journal,Biochemistry,,46,43,,,,,,,,,,,,,,,,,,,,,,12100,12110,2007, citations,entry_citation,7260,261348,1,,entry citation,,,,,,"Solution NMR structure of the YjcQ protein from Bacillus subtilis. Northeast Structural Genomics target SR346. (CASP Target)",submitted,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,7261,261387,1,,entry citation,,,,,,"Solution NMR structure of protein ykfF from Escherichia coli. Northeast Structural Genomics target ER397",submitted,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,7262,261419,1,,entry citation,,,17305365,,,"The N-Terminal Subdomain of Insulin-like Growth Factor (IGF) Binding Protein 6. Structure and Interaction with IGFs",published,journal,Biochemistry,,46,11,,,,,,,,,,,,,,,,,,,,,,3065,3074,2007, citations,entry_citation,7263,261440,1,,entry citation,,,17245526,,,Solution structure of the twelfth cysteine-rich ligand-binding repeat in rat megalin,published,journal,J. Biomol. NMR,,37,4,,,,,,,,,,,,,,,,,,,,,,321,328,2007, citations,entry_citation,7264,261459,1,,entry citation,,,17253772,,,"NMR spectroscopic characterization of a beta-(1,4)-glycosidase along its reaction pathway: stabilization upon formation of the glycosyl-enzyme intermediate.",published,journal,Biochemistry,,46,7,,,,,,,,,,,,,,,,,,,,,,1759,1770,2007, citations,entry_citation,7266,261481,1,,entry citation,,,,,,"Chemical shift assignments for protein NE1680 from Nitrosomonas europaea: Northeast Structural Genomics Consortium target NeT5",published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,7268,261506,1,,entry citation,,,17180550,,,"1H, 13C, and 15N chemical shift assignments for the N-terminal extracellular domain of T-cadherin",published,journal,J. Biomol. NMR,,38,2,,,,,,,,,,,,,,,,,,,,,,179,179,2007, citations,entry_citation,7269,261520,1,,entry citation,,,19636814,,,NMR assignment of backbone and side chain resonances for a dockerin-containing C-terminal fragment of the putative mu-toxin from Clostridium perfringens,published,journal,Biomol. NMR Assignments,,1,1,,,,,,,,,,,,,,,,,,,,,,13,15,2007, citations,entry_citation,7270,261534,1,,entry citation,,,19636812,,,NMR assignment of backbone and side chain resonances for a putative protein-protein interaction module from a family 84 glycoside hydrolase of Clostridium perfringens,published,journal,Biomol. NMR Assignments,,1,1,,,,,,,,,,,,,,,,,,,,,,7,9,2007, citations,entry_citation,7271,261547,1,,entry citation,,,17206469,,,"Backbone and side chain 1H, 13C, and 15N resonance assignments of AF2241 from Archaeoglobus fulgidus",published,journal,J. Biomol. NMR,,38,2,,,,,,,,,,,,,,,,,,,,,,183,183,2007, citations,entry_citation,7272,261571,1,,entry citation,,,17180548,,,Resonance assignment of the RGS domain of human RGS10,published,journal,J. Biomol. NMR,,38,2,,,,,,,,,,,,,,,,,,,,,,191,191,2007, citations,entry_citation,7273,261599,1,,entry citation,,,17481690,,,"Solution structure of Jingzhaotoxin-III, a peptide toxin inhibiting both Nav1.5 and Kv2.1 channels",published,journal,Toxicon,,50,1,,,,,,,,,,,,,,,,,,,,,,135,143,2007, citations,entry_citation,7274,261614,1,,entry citation,,,,,,"Solution NMR structure of the YdfO protein from Escherichia coli. Northeast Structural Genomics target ER251",submitted,journal,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,7276,261656,1,,entry citation,,,17206470,,,"Complete 1H, 13C and 15N resonance assignments of Blo t 5, a major mite allergen from Blomia tropicalis.",published,journal,J. Biomol. NMR,,38,2,,,,,,,,,,,,,,,,,,,,,,189,189,2006,Letter to the Editor in Journal of Biomolecular NMR. citations,entry_citation,7277,261703,1,,entry citation,,,17088323,,,An inserted Gly residue fine tunes dynamics between mesophilic and thermophilic ribonucleases H,published,journal,Protein Sci.,,15,12,,,,,,,,,,,,,,,,,,,,,,2697,2707,2006, citations,entry_citation,7278,261717,1,,entry citation,,,17088323,,,An inserted Gly residue fine tunes dynamics between mesophilc and thermophilic ribonucleases H,published,journal,Protein Sci.,,15,12,,,,,,,,,,,,,,,,,,,,,,2697,2707,2006, citations,entry_citation,7279,261731,1,,entry citation,,,17206468,,,NMR resonance assignments of the human high mobility group protein HMGA1.,published,journal,J. Biomol. NMR,,38,2,,,,,,,,,,,,,,,,,,,,,,185,185,2007, citations,entry_citation,7280,261747,1,,entry citation,,,18076052,,,Pressure-Induced Changes in the Solution Structure of the GB1 Domain of Protein G,published,journal,Proteins,,71,3,,,,,,,,,,,,,,,,,,,,,,1432,1440,2008, citations,entry_citation,7281,261761,1,,entry citation,,,17266124,,,"NMR structure of protein yjbR from Escherichia coli reveals 'double-wing' DNA binding motif.",published,journal,Proteins,,67,2,,,,,,,,,,,,,,,,,,,,,,501,504,2007, citations,entry_citation,7282,261783,1,,entry citation,,,18247449,,,Design of a bivalent peptide with two independent elements of secondary structure able to fold autonomously,published,journal,J. Pept. Sci.,,14,7,,,,,,,,,,,,,,,,,,,,,,845,854,2008, citations,entry_citation,7283,261798,1,,entry citation,,,18247449,,,Design of a bivalent peptide with two independent elements of secondary structure able to fold autonomously,published,journal,J. Pept. Sci.,,14,7,,,,,,,,,,,,,,,,,,,,,,845,854,2008, citations,entry_citation,7284,261812,1,,entry citation,,,18247449,,,Design of a bivalent peptide with two independent elements of secondary structure able to fold autonomously,published,journal,J. Pept. Sci.,,14,7,,,,,,,,,,,,,,,,,,,,,,845,854,2008, citations,entry_citation,7285,261827,1,,entry citation,,,17869267,,,Characterization of a double dockerin from the cellulosome of the anaerobic fungus Piromyces equi,published,journal,J. Mol. Biol.,,373,3,,,,,,,,,,,,,,,,,,,,,,612,622,2007, citations,entry_citation,7286,261853,1,,entry citation,,,17396237,,,"(1)H, (15)N and (13)C resonance assignments of CG7054, a new PEBP from Drosophila melanogaster",published,journal,J. Biomol. NMR,,38,2,,,,,,,,,,,,,,,,,,,,,,187,187,2007, citations,entry_citation,7287,261882,1,,entry citation,,,17498659,,,"Solution structure of BRD7 bromodomain and its interaction with acetylated peptides from histone H3 and H4.",published,journal,Biochem. Biophys. Res. Commun.,,358,2,,,,,,,,,,,,,,,,,,,,,,435,441,2007, citations,entry_citation,7288,261909,1,,entry citation,,,17412696,,,Unique dimeric structure of BNip3 transmembrane domain suggests membrane permeabilization as a cell death trigger.,published,journal,J. Biol. Chem.,,282,22,,,,,,,,,,,,,,,,,,,,,,16256,16266,2007, citations,entry_citation,7289,261932,1,,entry citation,,,17052982,,,"Structural characterization and oligomerization of PB1-F2, a pro-apoptotic influenza A virus protein",published,journal,J. Biol. Chem.,,282,1,,,,,,,,,,,,,,,,,,,,,,353,363,2006, citations,entry_citation,7290,261949,1,,entry citation,,,17052982,,,"Structural characterization and oligomerization of PB1-F2, a pro-apoptotic influenza A virus protein",published,journal,J. Biol. Chem.,,282,1,,,,,,,,,,,,,,,,,,,,,,353,363,2006, citations,entry_citation,7291,261966,1,,entry citation,,,17322536,,,Solution structure of the coxsackievirus and adenovirus receptor domain 2,published,journal,Protein Sci.,,16,3,,,,,,,,,,,,,,,,,,,,,,539,542,2007, citations,citation1,7292,261991,1,,entry citation,,,19636834,,,Backbone NMR assignment of the internal interaction site of ALP,published,journal,Biomol. NMR Assignments,,1,1,,,,,,,,,,,,,,,,,,,,,,85,87,2007, citations,1,7293,262011,1,,entry citation,,,17020884,,,Structural Basis for Calcium-induced Inhibition of Rhodopsin Kinase by Recoverin,published,journal,J. Biol. Chem.,,281,48,,,,,,,,,,,,,,,,,,,,,,37237,37245,2006, citations,1,7294,262033,1,,reference citation,,,10447689,,,NMR structure of active and inactive forms of the sterol-dependent antifungal antibiotic bacillomycin L,published,journal,Eur. J. Biochem.,,264,1,,,,,,,,,,,,,,,,,,,,,,200,210,1999,"After reexamination of the NMR spectra, the antibiotic studied in this paper (bacillomycin L) was found to be bacillomycin Lc instead (see the citation 2)." citations,2,7294,262034,2,,entry citation,,,17129757,,,"NMR structure determination of a synthetic analogue of bacillomycin Lc reveals the strategic role of L-Asn1 in the natural iturinic antibiotics",published,journal,Spectrochim. Acta A. Mol. Biomol. Spectrosc.,,67,5,,,,,,,,,,,,,,,,,,,,,,1374,1381,2007,"After reexamination of the NMR spectra (citation 2), the antibiotic presented here (bacillomycin L) was found to be bacillomycin Lc instead." citations,1,7295,262059,1,,entry citation,,,17129757,,,NMR structure determination of a synthetic analogue of bacillomycin Lc reveals the strategic role of L-Asn1 in the natural iturinic antibiotics.,published,journal,Spectrochemica Acta Part A,,67,5,,,,,,,,,,,,,,,,,,,,,,1374,1381,2006, citations,2,7295,262060,2,,reference citation,,,10447689,,,NMR structure of active and inactive forms of the sterol-dependent antifungal antibiotic bacillomycin L.,published,journal,Eur. J. Biochem.,,264,1,,,,,,,,,,,,,,,,,,,,,,200,210,1999,"After reexamination of the NMR spectra, the antibiotic studied in this paper (bacillomycin L) was finally found to be the bacillomycin Lc (see citation 1)" citations,entry_citation,7296,262084,1,,entry citation,,,17496029,,,"Solution conformation of the His-47 to Ala-47 mutant of Pseudomonas stutzeri ZoBell ferrocytochrome c-551.",published,journal,Biophys. J.,,93,5,,,,,,,,,,,,,,,,,,,,,,1700,1706,2007, citations,entry_citation,7297,262105,1,,entry citation,,,,,,Solution structure of RPA1320,published,BMRB only,,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,entry_citation,7298,262131,1,,entry citation,,,17512543,,,"Solution structure of the Ubp-M BUZ domain, a highly specific protein module that recognizes the C-terminal tail of free ubiquitin",published,journal,J. Mol. Biol.,,370,2,,,,,,,,,,,,,,,,,,,,,,290,302,2007, citations,entry_citation,7299,262156,1,,entry citation,,,17125258,,,Solution structure of mouse Cripto CFC domain and its inactive variant Trp107Ala,published,journal,J. Med. Chem.,,49,24,,,,,,,,,,,,,,,,,,,,,,7054,7062,2006, citations,entry_citation,7300,262174,1,,entry citation,,,17097678,,,Solution structure of the COMMD1 N-terminal domain,published,journal,J. Mol. Biol.,,365,3,,,,,,,,,,,,,,,,,,,,,,715,721,2007, citations,entry_citation,7301,262197,1,,entry citation,,,17415668,,,"Assignment of 1H, 13C, and 15N resonances for SF2 RNA recognition motif 2",published,journal,J. Biomol. NMR,,38,2,,,,,,,,,,,,,,,,,,,,,,193,193,2007, citations,entry_citation,7302,262220,1,,entry citation,,,15673616,,,Determinants of the Localization of Sorting Nexin 1,published,journal,Mol. Biol. Cell,,16,4,,,,,,,,,,,,,,,,,,,,,,2049,2057,2005,The first and second authors contributed equally to this publication. citations,entry_citation,7303,262235,1,,entry citation,,,19636819,,,"1H, 13C and 15N resonance assignments for proapoptotic protein Nix (residue 1 approximately 156) from Danio rerio",published,journal,Biomol. NMR Assignments,,1,1,,,,,,,,,,,,,,,,,,,,,,29,31,2007, citations,entry_citation,7304,262250,1,,entry citation,,,16930619,,,Solution structures of human and porcine beta-microseminoprotein,published,journal,J. Mol. Biol.,,362,3,,,,,,,,,,,,,,,,,,,,,,502,515,2006, citations,entry_citation,7305,262263,1,,entry citation,,,17407569,,,The high-resolution NMR structure of the R21A Spc-SH3:P41 complex: Understanding the determinants of binding affinity by comparison with Abl-SH3,published,journal,BMC Struct. 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Biol.,Journal of molecular biology,391,3,,,,,,,,,,,,,,,,,,,,,,518,535,2009, citations,entry_citation,7434,263961,1,,entry citation,,,,,,Structural insight into the recognition of PABPN1 by the flexible loops of a heavy chain antibody fragment,in preparation,journal,Not known,,,,,,,,,,,,,,,,,,,,,,,,,,,, citations,citations,7435,263977,1,,entry citation,,,21253573,,,Structural Basis for the Recognition of Cellular mRNA Export Factor REF by Herpes Viral Proteins HSV-1 ICP27 and HVS ORF57.,published,journal,PLoS Pathog.,PLoS pathogens,7,1,,,,,,,,,,,,,,,,,,,,,,e1001244,,2011, citations,entry_citation,749,263994,1,,entry citation,,,,,"Tsuda, Sakae, Hasegawa, Yasushi, Yoshida, Mikiharu, Yagi, Koichi, Hikichi, Kunio, ""Nuclear Magnetic Resonance Study on Rabbit Skeletal Troponin C: Calcium-Induced Conformational Change,"" Biochemistry 27, 4120-4126 (1988).","Nuclear Magnetic Resonance Study on Rabbit Skeletal Troponin C: Calcium-Induced Conformational Change",published,journal,Biochemistry,,27,,,,,,,,,,,,,,,,,,,,,,,4120,4126,1988, citations,entry_citation,750,264007,1,,entry citation,,,,,"Tsuda, Sakae, Hasegawa, Yasushi, Yoshida, Mikiharu, Yagi, Koichi, Hikichi, Kunio, ""Nuclear Magnetic Resonance Study on Rabbit Skeletal Troponin C: Calcium-Induced Conformational Change,"" Biochemistry 27, 4120-4126 (1988).","Nuclear Magnetic Resonance Study on Rabbit Skeletal Troponin C: Calcium-Induced Conformational Change",published,journal,Biochemistry,,27,,,,,,,,,,,,,,,,,,,,,,,4120,4126,1988, citations,entry_citation,753,264020,1,,entry citation,,,,,"Skelton, Nicholas J., Forsen, Sture, Chazin, Walter J., ""1H NMR Resonance Assignments, Secondary Structure, and Global Fold of Apo Bovine Calbindin D9k,"" Biochemistry 29, 5752-5761 (1990).","1H NMR Resonance Assignments, Secondary Structure, and Global Fold of Apo Bovine Calbindin D9k",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,5752,5761,1990, citations,entry_citation,754,264033,1,,entry citation,,,,,"Khan, Nikhat, Graslund, Astrid, Ehrenberg, Anders, Shriver, John, ""Sequence-Specific 1H NMR Assignments and Secondary Structure of Porcine Motilin,"" Biochemistry 29, 5743-5751 (1990).",Sequence-Specific 1H NMR Assignments and Secondary Structure of Porcine Motilin,published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,5743,5751,1990, citations,entry_citation,758,264046,1,,entry citation,,,,,"Chau, Mei-Hing, Cai, Meng Li, Timkovich, Russell, ""NMR Comparison of Prokaryotic and Eukaryotic Cytochromes c,"" Biochemistry 29, 5076-5087 (1990).",NMR Comparison of Prokaryotic and Eukaryotic Cytochromes c,published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,5076,5087,1990, citations,entry_citation,759,264061,1,,entry citation,,,,,"Chau, Mei-Hing, Cai, Meng Li, Timkovich, Russell, ""NMR Comparison of Prokaryotic and Eukaryotic Cytochromes c,"" Biochemistry 29, 5076-5087 (1990).",NMR Comparison of Prokaryotic and Eukaryotic Cytochromes c,published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,5076,5087,1990, citations,entry_citation,76,264076,1,,entry citation,,,,,"Boyd, Jonathan, Dobson, Christopher M., Redfield, Christina, ""Assignment of resonances in the 1H NMR spectrum of human lysozyme,"" Eur. J. Biochem. 153, 383-396 (1985).",Assignment of resonances in the 1H NMR spectrum of human lysozyme,published,journal,Eur. J. Biochem.,,153,,,,,,,,,,,,,,,,,,,,,,,383,396,1985, citations,entry_citation,760,264089,1,,entry citation,,,,,"Chau, Mei-Hing, Cai, Meng Li, Timkovich, Russell, ""NMR Comparison of Prokaryotic and Eukaryotic Cytochromes c,"" Biochemistry 29, 5076-5087 (1990).",NMR Comparison of Prokaryotic and Eukaryotic Cytochromes c,published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,5076,5087,1990, citations,entry_citation,761,264104,1,,entry citation,,,,,"Chau, Mei-Hing, Cai, Meng Li, Timkovich, Russell, ""NMR Comparison of Prokaryotic and Eukaryotic Cytochromes c,"" Biochemistry 29, 5076-5087 (1990).",NMR Comparison of Prokaryotic and Eukaryotic Cytochromes c,published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,5076,5087,1990, citations,entry_citation,779,264119,1,,entry citation,,,,,"Shimada, Ichio, Kato, Koichi, Saito, Kazuki, Kitada, Chieko, Fujino, Masahiko, Nakajima, Terumi, Arata, Yoji, ""A 1H-NMR Study of the Solution Conformation of Icaria chemotactic peptide and its [Lys7] analog: Effects on the physiological activity of a substitution of proline to lysine at position 7,"" Biochem. Biophys. Res. Commun. 168 (2), 596-603 (1990).","A 1H-NMR Study of the Solution Conformation of Icaria chemotactic peptide and its [Lys7] analog: Effects on the physiological activity of a substitution of proline to lysine at position 7",published,journal,Biochem. Biophys. Res. Commun.,,168,2,,,,,,,,,,,,,,,,,,,,,,596,603,1990, citations,entry_citation,780,264133,1,,entry citation,,,,,"Neuhaus, David, Nakaseko, Yukinobu, Nagai, Kiyoshi, Klug, Aaron, ""Sequence-specific [1H]NMR resonance assignments and secondary structure identification for 1- and 2-zinc finger constructs from SWI5 A hydrophobic core involving four invariant residues,"" FEBS Lett. 262 (2), 179-184 (1990).","Sequence-specific [1H]NMR resonance assignments and secondary structure identification for 1- and 2-zinc finger constructs from SWI5 A hydrophobic core involving four invariant residues",published,journal,FEBS Lett.,,262,2,,,,,,,,,,,,,,,,,,,,,,179,184,1990, citations,entry_citation,781,264146,1,,entry citation,,,,,"Neuhaus, David, Nakaseko, Yukinobu, Nagai, Kiyoshi, Klug, Aaron, ""Sequence-specific [1H]NMR resonance assignments and secondary structure identification for 1- and 2-zinc finger constructs from SWI5 A hydrophobic core involving four invariant residues,"" FEBS Lett. 262 (2), 179-184 (1990).","Sequence-specific [1H]NMR resonance assignments and secondary structure identification for 1- and 2-zinc finger constructs from SWI5 A hydrophobic core involving four invariant residues",published,journal,FEBS Lett.,,262,2,,,,,,,,,,,,,,,,,,,,,,179,184,1990, citations,entry_citation,79,264159,1,,entry citation,,,,,"Driscoll, Paul C., Hill, H. Allen O., Redfield, Christina, ""1H-NMR sequential assignments and cation-binding studies of spinach plastocyanin,"" Eur. J. Biochem. 170, 279-292 (1987).",1H-NMR sequential assignments and cation-binding studies of spinach plastocyanin,published,journal,Eur. J. Biochem.,,170,,,,,,,,,,,,,,,,,,,,,,,279,292,1987, citations,entry_citation,791,264172,1,,entry citation,,,,,"Davis, Donald G., ""Proton NMR Detection of Long-Range Heteronuclear Multiquantum Coherences in Proteins: The Complete Assignment of the Quaternary Aromatic 13C Shifts in Lysozyme,"" J. Am. Chem. Soc. 111, 5466-5468 (1989).","Proton NMR Detection of Long-Range Heteronuclear Multiquantum Coherences in Proteins: The Complete Assignment of the Quaternary Aromatic 13C Shifts in Lysozyme",published,journal,J. Am. Chem. Soc.,,111,,,,,,,,,,,,,,,,,,,,,,,5466,5468,1989, citations,entry_citation,8,264185,1,,entry citation,,,,,"Basus, Vladimir J., Billeter, Martin, Love, Robert A., Stroud, Robert M., Kuntz, Irwin D., ""Structural Studies of alpha-Bungarotoxin. 1. Sequence-Specific 1H NMR Resonance Assignments,"" Biochemistry 27, 2763-2771 (1988).","Structural Studies of alpha-Bungarotoxin. 1. Sequence-Specific 1H NMR Resonance Assignments",published,journal,Biochemistry,,27,,,,,,,,,,,,,,,,,,,,,,,2763,2771,1988, citations,entry_citation,80,264196,1,,entry citation,,,,,"Widmer, Hans, Wagner, Gerhard, Schweitz, Hugues, Lazdunski, Michel, Wuthrich, Kurt, ""The Secondary Structure of the Toxin ATX Ia from Anemonia sulcata in Aqueous Solution Determined on the Basis of Complete Sequence-specific 1H NMR Assignments,"" Eur. J. Biochem. 171, 177-192 (1988).","The Secondary Structure of the Toxin ATX Ia from Anemonia sulcata in Aqueous Solution Determined on the Basis of Complete Sequence-specific 1H NMR Assignments",published,journal,Eur. J. Biochem.,,171,,,,,,,,,,,,,,,,,,,,,,,177,192,1988, citations,entry_citation,81,264209,1,,entry citation,,,,,"Nygaard, Erik, Mendz, George L., Moore, Walter J., Martenson, Russell E., ""NMR of a Peptic Peptide Spanning the Triprolyl Sequence in Myelin Basic Protein,"" Biochemistry 23, 4003-4010 (1984).",NMR of a Peptic Peptide Spanning the Triprolyl Sequence in Myelin Basic Protein,published,journal,Biochemistry,,23,,,,,,,,,,,,,,,,,,,,,,,4003,4010,1984, citations,entry_citation,810,264222,1,,entry citation,,,,,"van de Ven, F. J. M., Lycksell, Per-Olof, van Kammen, Ab, Hilbers, C. W., ""Computer-aided assignment of the 1H-NMR spectrum of the viral-protein-genome-linked polypeptide from cowpea mosaic virus,"" Eur. J. Biochem. 190, 583-591 (1990).","Computer-aided assignment of the 1H-NMR spectrum of the viral-protein-genome-linked polypeptide from cowpea mosaic virus",published,journal,Eur. J. Biochem.,,190,,,,,,,,,,,,,,,,,,,,,,,583,591,1990, citations,entry_citation,811,264235,1,,entry citation,,,,,"Banci, Lucia, Bertini, Ivano, Cabelli, Diane, Hallewell, Robert A., Luchinat, Claudio, Viezzoli, Maria Silvia, ""Investigation of Copper-Zinc Superoxide Dismutase Ser-137 and Ala-137 Mutants,"" Inorg. Chem. 29, 2398-2403 (1990).",Investigation of Copper-Zinc Superoxide Dismutase Ser-137 and Ala-137 Mutants,published,journal,Inorg. Chem.,,29,,,,,,,,,,,,,,,,,,,,,,,2398,2403,1990, citations,entry_citation,812,264249,1,,entry citation,,,,,"Banci, Lucia, Bertini, Ivano, Cabelli, Diane, Hallewell, Robert A., Luchinat, Claudio, Viezzoli, Maria Silvia, ""Investigation of Copper-Zinc Superoxide Dismutase Ser-137 and Ala-137 Mutants,"" Inorg. Chem. 29, 2398-2403 (1990).",Investigation of Copper-Zinc Superoxide Dismutase Ser-137 and Ala-137 Mutants,published,journal,Inorg. Chem.,,29,,,,,,,,,,,,,,,,,,,,,,,2398,2403,1990, citations,entry_citation,813,264263,1,,entry citation,,,,,"Banci, Lucia, Bertini, Ivano, Cabelli, Diane, Hallewell, Robert A., Luchinat, Claudio, Viezzoli, Maria Silvia, ""Investigation of Copper-Zinc Superoxide Dismutase Ser-137 and Ala-137 Mutants,"" Inorg. Chem. 29, 2398-2403 (1990).",Investigation of Copper-Zinc Superoxide Dismutase Ser-137 and Ala-137 Mutants,published,journal,Inorg. Chem.,,29,,,,,,,,,,,,,,,,,,,,,,,2398,2403,1990, citations,entry_citation,814,264277,1,,entry citation,,,,,"Banci, Lucia, Bertini, Ivano, Cabelli, Diane, Hallewell, Robert A., Luchinat, Claudio, Viezzoli, Maria Silvia, ""Investigation of Copper-Zinc Superoxide Dismutase Ser-137 and Ala-137 Mutants,"" Inorg. Chem. 29, 2398-2403 (1990).",Investigation of Copper-Zinc Superoxide Dismutase Ser-137 and Ala-137 Mutants,published,journal,Inorg. Chem.,,29,,,,,,,,,,,,,,,,,,,,,,,2398,2403,1990, citations,entry_citation,821,264291,1,,entry citation,,,,,"Dugad, Laxmichand B., La Mar, Gerd N., Banci, Lucia, Bertini, Ivano, ""Identification of Localized Redox States in Plant-Type Two-Iron Ferredoxins Using the Nuclear Overhauser Effect,"" Biochemistry 29, 2263-2271 (1990).","Identification of Localized Redox States in Plant-Type Two-Iron Ferredoxins Using the Nuclear Overhauser Effect",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,2263,2271,1990, citations,entry_citation,822,264304,1,,entry citation,,,,,"Dugad, Laxmichand B., La Mar, Gerd N., Banci, Lucia, Bertini, Ivano, ""Identification of Localized Redox States in Plant-Type Two-Iron Ferredoxins Using the Nuclear Overhauser Effect,"" Biochemistry 29, 2263-2271 (1990).","Identification of Localized Redox States in Plant-Type Two-Iron Ferredoxins Using the Nuclear Overhauser Effect",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,2263,2271,1990, citations,entry_citation,823,264317,1,,entry citation,,,,,"Mabbutt, Bridget C., Wright, Peter E., ""Assignment of heme and distal amino acid resonances in the 1H-NMR spectra of the carbon monoxide and oxygen complexes of sperm whale myoglobin,"" Biochim. Biophys. Acta 832, 175-185 (1985).","Assignment of heme and distal amino acid resonances in the 1H-NMR spectra of the carbon monoxide and oxygen complexes of sperm whale myoglobin",published,journal,Biochim. Biophys. Acta,,832,,,,,,,,,,,,,,,,,,,,,,,175,185,1985, citations,entry_citation,824,264330,1,,entry citation,,,,,"Mabbutt, Bridget C., Wright, Peter E., ""Assignment of heme and distal amino acid resonances in the 1H-NMR spectra of the carbon monoxide and oxygen complexes of sperm whale myoglobin,"" Biochim. Biophys. Acta 832, 175-185 (1985).","Assignment of heme and distal amino acid resonances in the 1H-NMR spectra of the carbon monoxide and oxygen complexes of sperm whale myoglobin",published,journal,Biochim. Biophys. Acta,,832,,,,,,,,,,,,,,,,,,,,,,,175,185,1985, citations,entry_citation,846,264343,1,,entry citation,,,,,"Hincke, Maxwell T., Sykes, Brian D., Kay, Cyril M., ""Hydrogen-1 Nuclear Magnetic Resonance Investigation of Bovine Cardiac Troponin C. Comparison of Tyrosyl Assignments and Calcium-Induced Structural Changes to Those of Two Homologous Proteins, Rabbit Skeletal Troponin C and Bovine Brain Calm,"" Biochemistry 20, 3286-3294 (1981).","Hydrogen-1 Nuclear Magnetic Resonance Investigation of Bovine Cardiac Troponin C. Comparison of Tyrosyl Assignments and Calcium-Induced Structural Changes to Those of Two Homologous Proteins, Rabbit Skeletal Troponin C and Bovine Brain Calm",published,journal,Biochemistry,,20,,,,,,,,,,,,,,,,,,,,,,,3286,3294,1981, citations,entry_citation,848,264357,1,,entry citation,,,,,"Ribeiro, A.A., Wemmer, David, Bray, R.C., Wade-Jardetzky, N.G., Jardetzky, Oleg, ""High-Resolution Nuclear Magnetic Resonance Studies of the Lac Repressor. 1. Assignments of Tyrosine Resonances in the N-Terminal Headpiece,"" Biochemistry 20, 818-823 (1981).","High-Resolution Nuclear Magnetic Resonance Studies of the Lac Repressor. 1. Assignments of Tyrosine Resonances in the N-Terminal Headpiece",published,journal,Biochemistry,,20,,,,,,,,,,,,,,,,,,,,,,,818,823,1981, citations,entry_citation,849,264370,1,,entry citation,,,,,"Ribeiro, A.A., Wemmer, David, Bray, R.C., Wade-Jardetzky, N.G., Jardetzky, Oleg, ""High-Resolution Nuclear Magnetic Resonance Studies of the Lac Repressor. 2. Partial Analysis of the Aliphatic Region of the Lac Repressor Headpiece Spectrum,"" Biochemistry 20, 823-829 (1981).","High-Resolution Nuclear Magnetic Resonance Studies of the Lac Repressor. 2. Partial Analysis of the Aliphatic Region of the Lac Repressor Headpiece Spectrum",published,journal,Biochemistry,,20,,,,,,,,,,,,,,,,,,,,,,,823,829,1981, citations,entry_citation,86,264383,1,,entry citation,,,,,"Esposito, Gennaro, Carver, John A., Boyd, Jonathan, Campbell, Iain D., ""High-Resolution 1H NMR Study of the Solution Structure of Alamethicin,"" Biochemistry 26, 1043-1050 (1987).",High-Resolution 1H NMR Study of the Solution Structure of Alamethicin,published,journal,Biochemistry,,26,,,,,,,,,,,,,,,,,,,,,,,1043,1050,1987, citations,entry_citation,862,264398,1,,entry citation,,,,,"Hincke, Maxwell T., Sykes, Brian D., Kay, Cyril M., ""Hydrogen-1 Nuclear Magnetic Resonance Investigation of Bovine Cardiac Troponin C. Comparison of Tyrosyl Assignments and Calcium-Induced Structural Changes to Those of Two Homologous Proteins, Rabbit Skeletal Troponin C and Bovine Brain Calm,"" Biochemistry 20, 3286-3294 (1981).","Hydrogen-1 Nuclear Magnetic Resonance Investigation of Bovine Cardiac Troponin C. Comparison of Tyrosyl Assignments and Calcium-Induced Structural Changes to Those of Two Homologous Proteins, Rabbit Skeletal Troponin C and Bovine Brain Calm",published,journal,Biochemistry,,20,,,,,,,,,,,,,,,,,,,,,,,3286,3294,1981, citations,entry_citation,87,264412,1,,entry citation,,,,,"Carver, John A., ""The conformation of bombesin in solution as determined by two-dimensional 1H-NMR techniques,"" Eur. J. Biochem. 168, 193-199 (1987).","The conformation of bombesin in solution as determined by two-dimensional 1H-NMR techniques",published,journal,Eur. J. Biochem.,,168,,,,,,,,,,,,,,,,,,,,,,,193,199,1987, citations,entry_citation,877,264427,1,,entry citation,,,,,"Eakin, R.T., Morgan, L.O., Matwiyoff, N.A., ""Carbon-13 Nuclear-Magnetic-Resonance Spectroscopy of Whole Cells and of Cytochrome c from Neurospora crassa Grown with [S-Me-13C]Methionine,"" Biochem. J. 152, 529-535 (1975).","Carbon-13 Nuclear-Magnetic-Resonance Spectroscopy of Whole Cells and of Cytochrome c from Neurospora crassa Grown with [S-Me-13C]Methionine",published,journal,Biochem. J.,,152,,,,,,,,,,,,,,,,,,,,,,,529,535,1975, citations,entry_citation,878,264443,1,,entry citation,,,,,"Eakin, R.T., Morgan, L.O., Matwiyoff, N.A., ""Carbon-13 Nuclear-Magnetic-Resonance Spectroscopy of Whole Cells and of Cytochrome c from Neurospora crassa Grown with [S-Me-13C]Methionine,"" Biochem. J. 152, 529-535 (1975).","Carbon-13 Nuclear-Magnetic-Resonance Spectroscopy of Whole Cells and of Cytochrome c from Neurospora crassa Grown with [S-Me-13C]Methionine",published,journal,Biochem. J.,,152,,,,,,,,,,,,,,,,,,,,,,,529,535,1975, citations,entry_citation,88,264459,1,,entry citation,,,,,"Otting, Gottfried, Steinmetz, Wayne E., Bougis, Pierre E., Rochat, Herve, Wuthrich, Kurt, ""Sequence-specific 1H-NMR assignments and determination of the secondary structure in aqueous solution of the cardiotoxins CTXIIa and CTXIIb from Naja mossambica mossambica,"" Eur. J. Biochem. 168, 609-620 (1987).","Sequence-specific 1H-NMR assignments and determination of the secondary structure in aqueous solution of the cardiotoxins CTXIIa and CTXIIb from Naja mossambica mossambica",published,journal,Eur. J. Biochem.,,168,,,,,,,,,,,,,,,,,,,,,,,609,620,1987, citations,entry_citation,883,264472,1,,entry citation,,,,,"Bradbury, J. Howard, Ramesh, Vasudevan, Dodson, Guy, ""1H Nuclear Magnetic Resonance Study of the Histidine Residues of Insulin,"" J. Mol. Biol. 150, 609-613 (1981).",1H Nuclear Magnetic Resonance Study of the Histidine Residues of Insulin,published,journal,J. Mol. Biol.,,150,,,,,,,,,,,,,,,,,,,,,,,609,613,1981, citations,entry_citation,884,264485,1,,entry citation,,,,,"Bradbury, J. Howard, Ramesh, Vasudevan, Dodson, Guy, ""1H Nuclear Magnetic Resonance Study of the Histidine Residues of Insulin,"" J. Mol. Biol. 150, 609-613 (1981).",1H Nuclear Magnetic Resonance Study of the Histidine Residues of Insulin,published,journal,J. Mol. Biol.,,150,,,,,,,,,,,,,,,,,,,,,,,609,613,1981, citations,entry_citation,887,264498,1,,entry citation,,,,,"Anderson, D. Eric, Becktel, Wayne J., Dahlquist, Frederick W., ""pH-Induced Denaturation of Proteins: A Single Salt Bridge Contributes 3-5 kcal/mol to the Free Energy of Folding of T4 Lysozyme,"" Biochemistry 29, 2403-2408 (1990).","pH-Induced Denaturation of Proteins: A Single Salt Bridge Contributes 3-5 kcal/mol to the Free Energy of Folding of T4 Lysozyme",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,2403,2408,1990, citations,entry_citation,888,264511,1,,entry citation,,,,,"Anderson, D. Eric, Becktel, Wayne J., Dahlquist, Frederick W., ""pH-Induced Denaturation of Proteins: A Single Salt Bridge Contributes 3-5 kcal/mol to the Free Energy of Folding of T4 Lysozyme,"" Biochemistry 29, 2403-2408 (1990).","pH-Induced Denaturation of Proteins: A Single Salt Bridge Contributes 3-5 kcal/mol to the Free Energy of Folding of T4 Lysozyme",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,2403,2408,1990, citations,entry_citation,893,264525,1,,entry citation,,,,,"McDonald, George G., Cohn, Mildred, Noda, Lafayette, ""Proton Magnetic Resonance Spectra of Porcine Muscle Adenylate Kinase and Substrate Complexes,"" J. Biol. Chem. 250 (17), 6947-6954 (1975).","Proton Magnetic Resonance Spectra of Porcine Muscle Adenylate Kinase and Substrate Complexes",published,journal,J. Biol. Chem.,,250,17,,,,,,,,,,,,,,,,,,,,,,6947,6954,1975, citations,entry_citation,9,264538,1,,entry citation,,,,,"Clore, G. Marius, Gronenborn, Angela M., Nilges, Michael, Ryan, Clarence A., ""Three-Dimensional Structure of Potato Carboxypeptidase Inhibitor in Solution. A Study Using Nuclear Magnetic Resonance, Distance Geometry, and Restrained Molecular Dynamics,"" Biochemistry 26 (24), 8012-8023 (1987).","Three-Dimensional Structure of Potato Carboxypeptidase Inhibitor in Solution. A Study Using Nuclear Magnetic Resonance, Distance Geometry, and Restrained Molecular Dynamics",published,journal,Biochemistry,,26,24,,,,,,,,,,,,,,,,,,,,,,8012,8023,1987, citations,entry_citation,90,264550,1,,entry citation,,,,,"Lecomte, Juliette T.J., De Marco, A., Llinas, M., ""Analysis of the Methyl 1H-NMR Spectrum of Crambin, a Hydrophobic Protein,"" Biochim. Biophys. Acta 703, 223-230 (1982).","Analysis of the Methyl 1H-NMR Spectrum of Crambin, a Hydrophobic Protein",published,journal,Biochim. Biophys. Acta,,703,,,,,,,,,,,,,,,,,,,,,,,223,230,1982, citations,entry_citation,907,264563,1,,entry citation,,,,,"Oldfield, Eric, Allerhand, Adam, ""Studies of Individual Carbon Sites of Hemoglobins in Solution by Natural Abundance Carbon 13 Nuclear Magnetic Resonance Spectroscopy,"" J. Biol. Chem. 250 (16), 6403-6407 (1975).","Studies of Individual Carbon Sites of Hemoglobins in Solution by Natural Abundance Carbon 13 Nuclear Magnetic Resonance Spectroscopy",published,journal,J. Biol. Chem.,,250,16,,,,,,,,,,,,,,,,,,,,,,6403,6407,1975, citations,entry_citation,908,264576,1,,entry citation,,,,,"Oldfield, Eric, Allerhand, Adam, ""Studies of Individual Carbon Sites of Hemoglobins in Solution by Natural Abundance Carbon 13 Nuclear Magnetic Resonance Spectroscopy,"" J. Biol. Chem. 250 (16), 6403-6407 (1975).","Studies of Individual Carbon Sites of Hemoglobins in Solution by Natural Abundance Carbon 13 Nuclear Magnetic Resonance Spectroscopy",published,journal,J. Biol. Chem.,,250,16,,,,,,,,,,,,,,,,,,,,,,6403,6407,1975, citations,entry_citation,909,264589,1,,entry citation,,,,,"Oldfield, Eric, Allerhand, Adam, ""Studies of Individual Carbon Sites of Hemoglobins in Solution by Natural Abundance Carbon 13 Nuclear Magnetic Resonance Spectroscopy,"" J. Biol. Chem. 250 (16), 6403-6407 (1975).","Studies of Individual Carbon Sites of Hemoglobins in Solution by Natural Abundance Carbon 13 Nuclear Magnetic Resonance Spectroscopy",published,journal,J. Biol. Chem.,,250,16,,,,,,,,,,,,,,,,,,,,,,6403,6407,1975, citations,entry_citation,910,264602,1,,entry citation,,,,,"Oldfield, Eric, Allerhand, Adam, ""Studies of Individual Carbon Sites of Hemoglobins in Solution by Natural Abundance Carbon 13 Nuclear Magnetic Resonance Spectroscopy,"" J. Biol. Chem. 250 (16), 6403-6407 (1975).","Studies of Individual Carbon Sites of Hemoglobins in Solution by Natural Abundance Carbon 13 Nuclear Magnetic Resonance Spectroscopy",published,journal,J. Biol. Chem.,,250,16,,,,,,,,,,,,,,,,,,,,,,6403,6407,1975, citations,entry_citation,911,264615,1,,entry citation,,,,,"Oldfield, Eric, Allerhand, Adam, ""Studies of Individual Carbon Sites of Hemoglobins in Solution by Natural Abundance Carbon 13 Nuclear Magnetic Resonance Spectroscopy,"" J. Biol. Chem. 250 (16), 6403-6407 (1975).","Studies of Individual Carbon Sites of Hemoglobins in Solution by Natural Abundance Carbon 13 Nuclear Magnetic Resonance Spectroscopy",published,journal,J. Biol. Chem.,,250,16,,,,,,,,,,,,,,,,,,,,,,6403,6407,1975, citations,entry_citation,912,264628,1,,entry citation,,,,,"Oldfield, Eric, Allerhand, Adam, ""Studies of Individual Carbon Sites of Hemoglobins in Solution by Natural Abundance Carbon 13 Nuclear Magnetic Resonance Spectroscopy,"" J. Biol. Chem. 250 (16), 6403-6407 (1975).","Studies of Individual Carbon Sites of Hemoglobins in Solution by Natural Abundance Carbon 13 Nuclear Magnetic Resonance Spectroscopy",published,journal,J. Biol. Chem.,,250,16,,,,,,,,,,,,,,,,,,,,,,6403,6407,1975, citations,entry_citation,913,264641,1,,entry citation,,,,,"Oldfield, Eric, Allerhand, Adam, ""Studies of Individual Carbon Sites of Hemoglobins in Solution by Natural Abundance Carbon 13 Nuclear Magnetic Resonance Spectroscopy,"" J. Biol. Chem. 250 (16), 6403-6407 (1975).","Studies of Individual Carbon Sites of Hemoglobins in Solution by Natural Abundance Carbon 13 Nuclear Magnetic Resonance Spectroscopy",published,journal,J. Biol. Chem.,,250,16,,,,,,,,,,,,,,,,,,,,,,6403,6407,1975, citations,entry_citation,914,264654,1,,entry citation,,,,,"Oldfield, Eric, Allerhand, Adam, ""Studies of Individual Carbon Sites of Hemoglobins in Solution by Natural Abundance Carbon 13 Nuclear Magnetic Resonance Spectroscopy,"" J. Biol. Chem. 250 (16), 6403-6407 (1975).","Studies of Individual Carbon Sites of Hemoglobins in Solution by Natural Abundance Carbon 13 Nuclear Magnetic Resonance Spectroscopy",published,journal,J. Biol. Chem.,,250,16,,,,,,,,,,,,,,,,,,,,,,6403,6407,1975, citations,entry_citation,915,264667,1,,entry citation,,,,,"McIntosh, Lawrence P., Wand, A. Joshua, Lowry, David F., Redfield, Alfred G., Dahlquist, Frederick W., ""Assignment of the Backbone 1H and 15N NMR Resonances of Bacteriophage T4 Lysozyme,"" Biochemistry 29, 6341-6362 (1990).","Assignment of the Backbone 1H and 15N NMR Resonances of Bacteriophage T4 Lysozyme",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,6341,6362,1990, citations,entry_citation,916,264680,1,,entry citation,,,,,"Arrowsmith, Cheryl H., Pachter, R., Altman, R.B., Iyer, S.B., Jardetzky, Oleg, ""Sequence-Specific 1H NMR Assignments and Secondary Structure in Solution of Escherichia coli trp Repressor,"" Biochemistry 29, 6332-6341 (1990).","Sequence-Specific 1H NMR Assignments and Secondary Structure in Solution of Escherichia coli trp Repressor",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,6332,6341,1990, citations,entry_citation,918,264693,1,,entry citation,,,,,"Yan, Honggao, Shi, Zhengtao, Tsai, Ming-Daw, ""Mechanism of Adenylate Kinase. Structural and Functional Demonstration of Arginine-138 as a Key Catalytic Residue That Cannot Be Replaced by Lysine,"" Biochemistry 29, 6385-6392 (1990).","Mechanism of Adenylate Kinase. Structural and Functional Demonstration of Arginine-138 as a Key Catalytic Residue That Cannot Be Replaced by Lysine",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,6385,6392,1990, citations,entry_citation,919,264706,1,,entry citation,,,,,"Yan, Honggao, Shi, Zhengtao, Tsai, Ming-Daw, ""Mechanism of Adenylate Kinase. Structural and Functional Demonstration of Arginine-138 as a Key Catalytic Residue That Cannot Be Replaced by Lysine,"" Biochemistry 29, 6385-6392 (1990).","Mechanism of Adenylate Kinase. Structural and Functional Demonstration of Arginine-138 as a Key Catalytic Residue That Cannot Be Replaced by Lysine",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,6385,6392,1990, citations,entry_citation,920,264719,1,,entry citation,,,,,"Yan, Honggao, Shi, Zhengtao, Tsai, Ming-Daw, ""Mechanism of Adenylate Kinase. Structural and Functional Demonstration of Arginine-138 as a Key Catalytic Residue That Cannot Be Replaced by Lysine,"" Biochemistry 29, 6385-6392 (1990).","Mechanism of Adenylate Kinase. Structural and Functional Demonstration of Arginine-138 as a Key Catalytic Residue That Cannot Be Replaced by Lysine",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,6385,6392,1990, citations,entry_citation,922,264732,1,,entry citation,,,,,"Gao, Yuan, Boyd, Jonathan, Williams, Robert J. P., Pielak, Gary J., ""Assignment of Proton Resonances, Identification of Secondary Structural Elements, and Analysis of Backbone Chemical Shifts for the C102T Variant of Yeast Iso-1-cytochrome c and Horse Cytochrome c,"" Biochemistry 29, 6994-7003 (1990).","Assignment of Proton Resonances, Identification of Secondary Structural Elements, and Analysis of Backbone Chemical Shifts for the C102T Variant of Yeast Iso-1-cytochrome c and Horse Cytochrome c",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,6994,7003,1990, citations,entry_citation,923,264749,1,,entry citation,,,,,"Gao, Yuan, Boyd, Jonathan, Williams, Robert J. P., Pielak, Gary J., ""Assignment of Proton Resonances, Identification of Secondary Structural Elements, and Analysis of Backbone Chemical Shifts for the C102T Variant of Yeast Iso-1-cytochrome c and Horse Cytochrome c,"" Biochemistry 29, 6994-7003 (1990).","Assignment of Proton Resonances, Identification of Secondary Structural Elements, and Analysis of Backbone Chemical Shifts for the C102T Variant of Yeast Iso-1-cytochrome c and Horse Cytochrome c",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,6994,7003,1990, citations,entry_citation,932,264765,1,,entry citation,,,,,"Wittekind, Michael, Reizer, Jonathan, Klevit, Rachel E., ""Sequence-Specific 1H NMR Resonance Assignments of Bacillus subtilis HPr: Use of Spectra Obtained from Mutants To Resolve Spectral Overlap,"" Biochemistry 29, 7191-7200 (1990).","Sequence-Specific 1H NMR Resonance Assignments of Bacillus subtilis HPr: Use of Spectra Obtained from Mutants To Resolve Spectral Overlap",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,7191,7200,1990, citations,entry_citation,934,264778,1,,entry citation,,,,,"MacLachlan, Lesley K., Reid, David G., Carter, Nigel, ""A Proton Nuclear Magnetic Resonance and Molecular Modeling Study of Cardiac Troponin C Calcium Dependence and Aromatic Spectral Assignments,"" J. Biol. Chem. 265 (17), 9754-9763 (1990).","A Proton Nuclear Magnetic Resonance and Molecular Modeling Study of Cardiac Troponin C Calcium Dependence and Aromatic Spectral Assignments",published,journal,J. Biol. Chem.,,265,17,,,,,,,,,,,,,,,,,,,,,,9754,9763,1990, citations,entry_citation,936,264792,1,,entry citation,,,,,"Boelens, Rolf, Ganadu, Maria Luisa, Verheyden, Patricia, Kaptein, Robert, ""Two-dimensional NMR studies on des-pentapeptide-insulin Proton resonance assignments and secondary structure analysis,"" Eur. J. Biochem. 191, 147-153 (1990).","Two-dimensional NMR studies on des-pentapeptide-insulin Proton resonance assignments and secondary structure analysis",published,journal,Eur. J. Biochem.,,191,,,,,,,,,,,,,,,,,,,,,,,147,153,1990, citations,entry_citation,937,264805,1,,entry citation,,,,,"Boelens, Rolf, Ganadu, Maria Luisa, Verheyden, Patricia, Kaptein, Robert, ""Two-dimensional NMR studies on des-pentapeptide-insulin Proton resonance assignments and secondary structure analysis,"" Eur. J. Biochem. 191, 147-153 (1990).","Two-dimensional NMR studies on des-pentapeptide-insulin Proton resonance assignments and secondary structure analysis",published,journal,Eur. J. Biochem.,,191,,,,,,,,,,,,,,,,,,,,,,,147,153,1990, citations,entry_citation,939,264818,1,,entry citation,,,,,"Skelton, Nicholas J., Kordel, Johan, Forsen, Sture, Chazin, Walter J., ""Comparative Structural Analysis of the Calcium Free and Bound States of the Calcium Regulatory Protein Calbindin D9K,"" J. Mol. Biol. 213, 593-598 (1990).","Comparative Structural Analysis of the Calcium Free and Bound States of the Calcium Regulatory Protein Calbindin D9K",published,journal,J. Mol. Biol.,,213,,,,,,,,,,,,,,,,,,,,,,,593,598,1990, citations,entry_citation,94,264831,1,,entry citation,,,,,"Mayo, Kevin H., Burke, Carl, ""Structural and dynamical comparison of alpha, beta, and gamma forms of murine epidermal growth factor,"" Eur. J. Biochem. 169, 201-207 (1987).","Structural and dynamical comparison of alpha, beta, and gamma forms of murine epidermal growth factor",published,journal,Eur. J. Biochem.,,169,,,,,,,,,,,,,,,,,,,,,,,201,207,1987, citations,entry_citation,940,264844,1,,entry citation,,,,,"Skelton, Nicholas J., Kordel, Johan, Forsen, Sture, Chazin, Walter J., ""Comparative Structural Analysis of the Calcium Free and Bound States of the Calcium Regulatory Protein Calbindin D9K,"" J. Mol. Biol. 213, 593-598 (1990).","Comparative Structural Analysis of the Calcium Free and Bound States of the Calcium Regulatory Protein Calbindin D9K",published,journal,J. Mol. Biol.,,213,,,,,,,,,,,,,,,,,,,,,,,593,598,1990, citations,entry_citation,944,264857,1,,entry citation,,,,,"Stellwagen, E., Shulman, R.G., ""Nuclear Magnetic Resonances Study of Exchangeable Protons in Ferrocytochrome c,"" J. Mol. Biol. 75, 683-695 (1973).",Nuclear Magnetic Resonances Study of Exchangeable Protons in Ferrocytochrome c,published,journal,J. Mol. Biol.,,75,,,,,,,,,,,,,,,,,,,,,,,683,695,1973, citations,entry_citation,945,264873,1,,entry citation,,,,,"Stellwagen, E., Shulman, R.G., ""Nuclear Magnetic Resonances Study of Exchangeable Protons in Ferrocytochrome c,"" J. Mol. Biol. 75, 683-695 (1973).",Nuclear Magnetic Resonances Study of Exchangeable Protons in Ferrocytochrome c,published,journal,J. Mol. Biol.,,75,,,,,,,,,,,,,,,,,,,,,,,683,695,1973, citations,entry_citation,946,264886,1,,entry citation,,,,,"Oldfield, Eric, Allerhand, Adam, ""Cytochrome c. Observation of Numerous Single-Carbon Sites of the Reduced and Oxidized Species by Means of Natural-Abundance 13C Nuclear Magnetic Resonance Spectroscopy,"" Proc. Natl. Acad. Sci. U.S.A. 70 (12), 3531-3535 (1973).","Cytochrome c. Observation of Numerous Single-Carbon Sites of the Reduced and Oxidized Species by Means of Natural-Abundance 13C Nuclear Magnetic Resonance Spectroscopy",published,journal,Proc. Natl. Acad. Sci. U.S.A.,,70,12,,,,,,,,,,,,,,,,,,,,,,3531,3535,1973, citations,entry_citation,947,264902,1,,entry citation,,,,,"Oldfield, Eric, Allerhand, Adam, ""Cytochrome c. Observation of Numerous Single-Carbon Sites of the Reduced and Oxidized Species by Means of Natural-Abundance 13C Nuclear Magnetic Resonance Spectroscopy,"" Proc. Natl. Acad. Sci. U.S.A. 70 (12), 3531-3535 (1973).","Cytochrome c. Observation of Numerous Single-Carbon Sites of the Reduced and Oxidized Species by Means of Natural-Abundance 13C Nuclear Magnetic Resonance Spectroscopy",published,journal,Proc. Natl. Acad. Sci. U.S.A.,,70,12,,,,,,,,,,,,,,,,,,,,,,3531,3535,1973, citations,entry_citation,948,264918,1,,entry citation,,,,,"Dobson, Christopher M., Moore, Geoffrey R., Williams, Robert J. P., ""Assignment of aromatic amino acid pmr resonances of horse ferricytochrome c,"" FEBS Lett. 51 (1), 60-65 (1975).",Assignment of aromatic amino acid pmr resonances of horse ferricytochrome c,published,journal,FEBS Lett.,,51,1,,,,,,,,,,,,,,,,,,,,,,60,65,1975, citations,entry_citation,949,264934,1,,entry citation,,,,,"Dobson, Christopher M., Moore, Geoffrey R., Williams, Robert J. P., ""Assignment of aromatic amino acid pmr resonances of horse ferricytochrome c,"" FEBS Lett. 51 (1), 60-65 (1975).",Assignment of aromatic amino acid pmr resonances of horse ferricytochrome c,published,journal,FEBS Lett.,,51,1,,,,,,,,,,,,,,,,,,,,,,60,65,1975, citations,entry_citation,95,264950,1,,entry citation,,,,,"Mayo, Kevin H., Burke, Carl, ""Structural and dynamical comparison of alpha, beta, and gamma forms of murine epidermal growth factor,"" Eur. J. Biochem. 169, 201-207 (1987).","Structural and dynamical comparison of alpha, beta, and gamma forms of murine epidermal growth factor",published,journal,Eur. J. Biochem.,,169,,,,,,,,,,,,,,,,,,,,,,,201,207,1987, citations,citation_1,9500,264964,1,,entry citation,,,16061251,,,"Structural Basis for Ca(2+)-regulated Muscle Relaxation at Interaction Sites of Troponin with Actin and Tropomyosin",published,journal,J. Mol. Biol.,,352,1,JMOBAK,0022-2836,0353,,,,,,,,,,,,,,,,,,,178,201,2005, citations,entry_citation,956,264984,1,,entry citation,,,,,"Redfield, Alfred G., Gupta, Raj K., ""Pulsed NMR Study of the Structure of Cytochrome c,"" Cold Spring Harbor Symp. Quant. Biol. 36, 405-411 (1972).",Pulsed NMR Study of the Structure of Cytochrome c,published,journal,Cold Spring Harbor Symp. Quant. Biol.,,36,,,,,,,,,,,,,,,,,,,,,,,405,411,1972, citations,entry_citation,957,264997,1,,entry citation,,,,,"Redfield, Alfred G., Gupta, Raj K., ""Pulsed NMR Study of the Structure of Cytochrome c,"" Cold Spring Harbor Symp. Quant. Biol. 36, 405-411 (1972).",Pulsed NMR Study of the Structure of Cytochrome c,published,journal,Cold Spring Harbor Symp. Quant. Biol.,,36,,,,,,,,,,,,,,,,,,,,,,,405,411,1972, citations,entry_citation,96,265010,1,,entry citation,,,,,"Zuiderweg, Erik R. P., Kaptein, Robert, Wuthrich, Kurt, ""Sequence-specific resonance assignments in the 1H nuclear-magnetic-resonance spectrum of the Lac repressor DNA-binding domain 1-51 from Escherichia coli by two-dimensional spectroscopy,"" Eur. J. Biochem. 137, 279-292 (1983).","Sequence-specific resonance assignments in the 1H nuclear-magnetic-resonance spectrum of the Lac repressor DNA-binding domain 1-51 from Escherichia coli by two-dimensional spectroscopy",published,journal,Eur. J. Biochem.,,137,,,,,,,,,,,,,,,,,,,,,,,279,292,1983, citations,entry_citation,960,265022,1,,entry citation,,,,,"Robillard, G., Shulman, R.G., ""High Resolution Nuclear Magnetic Resonance Studies of the Active Site of Chymotrypsin II. Polarization of Histidine 57 by Substrate Analogues and Competitive Inhibitors,"" J. Mol. Biol. 86, 541-558 (1974).","High Resolution Nuclear Magnetic Resonance Studies of the Active Site of Chymotrypsin II. Polarization of Histidine 57 by Substrate Analogues and Competitive Inhibitors",published,journal,J. Mol. Biol.,,86,,,,,,,,,,,,,,,,,,,,,,,541,558,1974, citations,entry_citation,961,265035,1,,entry citation,,,,,"Robillard, G., Shulman, R.G., ""High Resolution Nuclear Magnetic Resonance Studies of the Active Site of Chymotrypsin II. Polarization of Histidine 57 by Substrate Analogues and Competitive Inhibitors,"" J. Mol. Biol. 86, 541-558 (1974).","High Resolution Nuclear Magnetic Resonance Studies of the Active Site of Chymotrypsin II. Polarization of Histidine 57 by Substrate Analogues and Competitive Inhibitors",published,journal,J. Mol. Biol.,,86,,,,,,,,,,,,,,,,,,,,,,,541,558,1974, citations,entry_citation,962,265048,1,,entry citation,,,,,"Robillard, G., Shulman, R.G., ""High Resolution Nuclear Magnetic Resonance Studies of the Active Site of Chymotrypsin II. Polarization of Histidine 57 by Substrate Analogues and Competitive Inhibitors,"" J. Mol. Biol. 86, 541-558 (1974).","High Resolution Nuclear Magnetic Resonance Studies of the Active Site of Chymotrypsin II. Polarization of Histidine 57 by Substrate Analogues and Competitive Inhibitors",published,journal,J. Mol. Biol.,,86,,,,,,,,,,,,,,,,,,,,,,,541,558,1974, citations,entry_citation,963,265061,1,,entry citation,,,,,"Robillard, G., Shulman, R.G., ""High Resolution Nuclear Magnetic Resonance Studies of the Active Site of Chymotrypsin II. Polarization of Histidine 57 by Substrate Analogues and Competitive Inhibitors,"" J. Mol. Biol. 86, 541-558 (1974).","High Resolution Nuclear Magnetic Resonance Studies of the Active Site of Chymotrypsin II. Polarization of Histidine 57 by Substrate Analogues and Competitive Inhibitors",published,journal,J. Mol. Biol.,,86,,,,,,,,,,,,,,,,,,,,,,,541,558,1974, citations,entry_citation,964,265074,1,,entry citation,,,,,"Robillard, G., Shulman, R.G., ""High Resolution Nuclear Magnetic Resonance Studies of the Active Site of Chymotrypsin II. Polarization of Histidine 57 by Substrate Analogues and Competitive Inhibitors,"" J. Mol. Biol. 86, 541-558 (1974).","High Resolution Nuclear Magnetic Resonance Studies of the Active Site of Chymotrypsin II. Polarization of Histidine 57 by Substrate Analogues and Competitive Inhibitors",published,journal,J. Mol. Biol.,,86,,,,,,,,,,,,,,,,,,,,,,,541,558,1974, citations,entry_citation,965,265087,1,,entry citation,,,,,"Robillard, G., Shulman, R.G., ""High Resolution Nuclear Magnetic Resonance Studies of the Active Site of Chymotrypsin II. Polarization of Histidine 57 by Substrate Analogues and Competitive Inhibitors,"" J. Mol. Biol. 86, 541-558 (1974).","High Resolution Nuclear Magnetic Resonance Studies of the Active Site of Chymotrypsin II. Polarization of Histidine 57 by Substrate Analogues and Competitive Inhibitors",published,journal,J. Mol. Biol.,,86,,,,,,,,,,,,,,,,,,,,,,,541,558,1974, citations,entry_citation,966,265100,1,,entry citation,,,,,"Robillard, G., Shulman, R.G., ""High Resolution Nuclear Magnetic Resonance Studies of the Active Site of Chymotrypsin II. Polarization of Histidine 57 by Substrate Analogues and Competitive Inhibitors,"" J. Mol. Biol. 86, 541-558 (1974).","High Resolution Nuclear Magnetic Resonance Studies of the Active Site of Chymotrypsin II. Polarization of Histidine 57 by Substrate Analogues and Competitive Inhibitors",published,journal,J. Mol. Biol.,,86,,,,,,,,,,,,,,,,,,,,,,,541,558,1974, citations,entry_citation,967,265113,1,,entry citation,,,,,"Robillard, G., Shulman, R.G., ""High Resolution Nuclear Magnetic Resonance Studies of the Active Site of Chymotrypsin II. Polarization of Histidine 57 by Substrate Analogues and Competitive Inhibitors,"" J. Mol. Biol. 86, 541-558 (1974).","High Resolution Nuclear Magnetic Resonance Studies of the Active Site of Chymotrypsin II. Polarization of Histidine 57 by Substrate Analogues and Competitive Inhibitors",published,journal,J. Mol. Biol.,,86,,,,,,,,,,,,,,,,,,,,,,,541,558,1974, citations,entry_citation,968,265126,1,,entry citation,,,,,"Timkovich, Russell, ""15N NMR Spectroscopy of Pseudomonas Cytochrome c-551,"" Biochemistry 29, 7773-7780 (1990).",15N NMR Spectroscopy of Pseudomonas Cytochrome c-551,published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,7773,7780,1990, citations,entry_citation,969,265141,1,,entry citation,,,,,"Timkovich, Russell, ""15N NMR Spectroscopy of Pseudomonas Cytochrome c-551,"" Biochemistry 29, 7773-7780 (1990).",15N NMR Spectroscopy of Pseudomonas Cytochrome c-551,published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,7773,7780,1990, citations,entry_citation,97,265156,1,,entry citation,,,,,"Worgotter, Erich, Wagner, Gerhard, Vasak, Milan, Kagi, Jeremias H.R., Wuthrich, Kurt, ""Sequence-specific 1H-NMR assignments in rat-liver metallothionein-2,"" Eur. J. Biochem. 167, 457-466 (1987).",Sequence-specific 1H-NMR assignments in rat-liver metallothionein-2,published,journal,Eur. J. Biochem.,,167,,,,,,,,,,,,,,,,,,,,,,,457,466,1987, citations,entry_citation,970,265170,1,,entry citation,,,,,"Timkovich, Russell, ""15N NMR Spectroscopy of Pseudomonas Cytochrome c-551,"" Biochemistry 29, 7773-7780 (1990).",15N NMR Spectroscopy of Pseudomonas Cytochrome c-551,published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,7773,7780,1990, citations,entry_citation,971,265186,1,,entry citation,,,,,"Timkovich, Russell, ""15N NMR Spectroscopy of Pseudomonas Cytochrome c-551,"" Biochemistry 29, 7773-7780 (1990).",15N NMR Spectroscopy of Pseudomonas Cytochrome c-551,published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,7773,7780,1990, citations,entry_citation,975,265201,1,,entry citation,,,,,"Bycroft, Mark, Sheppard, Richard N., Lau, Frankie Tat-Kwong, Fersht, Alan R., ""Sequential Assignment of the 1H Nuclear Magnetic Resonance Spectrum of Barnase,"" Biochemistry 29, 7425-7432 (1990).",Sequential Assignment of the 1H Nuclear Magnetic Resonance Spectrum of Barnase,published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,7425,7432,1990, citations,entry_citation,979,265214,1,,entry citation,,,,,"Vendrell, Josep, Wider, Gerhard, Aviles, Francesc X., Wuthrich, Kurt, ""Sequence Specific 1H NMR Assignments and Determination of the Secondary Structure for the Activation Domain Isolated from Pancreatic Procarboxypeptidase B,"" Biochemistry 29, 7515-7522 (1990).","Sequence Specific 1H NMR Assignments and Determination of the Secondary Structure for the Activation Domain Isolated from Pancreatic Procarboxypeptidase B",published,journal,Biochemistry,,29,,,,,,,,,,,,,,,,,,,,,,,7515,7522,1990, citations,entry_citation,994,265227,1,,entry citation,,,,,"Roy, Melinda, Lee, Robert W.-K., Kaarsholm, Niels C., Thogersen, Henning, Brange, Jens, Dunn, M.F., ""Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin,"" Biochim. Biophys. Acta 1053, 63-73 (1990).","Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin",published,journal,Biochim. Biophys. Acta,,1053,,,,,,,,,,,,,,,,,,,,,,,63,73,1990, citations,entry_citation,995,265240,1,,entry citation,,,,,"Roy, Melinda, Lee, Robert W.-K., Kaarsholm, Niels C., Thogersen, Henning, Brange, Jens, Dunn, M.F., ""Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin,"" Biochim. Biophys. Acta 1053, 63-73 (1990).","Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin",published,journal,Biochim. Biophys. Acta,,1053,,,,,,,,,,,,,,,,,,,,,,,63,73,1990, citations,entry_citation,996,265253,1,,entry citation,,,,,"Roy, Melinda, Lee, Robert W.-K., Kaarsholm, Niels C., Thogersen, Henning, Brange, Jens, Dunn, M.F., ""Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin,"" Biochim. Biophys. Acta 1053, 63-73 (1990).","Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin",published,journal,Biochim. Biophys. Acta,,1053,,,,,,,,,,,,,,,,,,,,,,,63,73,1990, citations,entry_citation,997,265266,1,,entry citation,,,,,"Roy, Melinda, Lee, Robert W.-K., Kaarsholm, Niels C., Thogersen, Henning, Brange, Jens, Dunn, M.F., ""Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin,"" Biochim. Biophys. Acta 1053, 63-73 (1990).","Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin",published,journal,Biochim. Biophys. Acta,,1053,,,,,,,,,,,,,,,,,,,,,,,63,73,1990, citations,entry_citation,998,265279,1,,entry citation,,,,,"Roy, Melinda, Lee, Robert W.-K., Kaarsholm, Niels C., Thogersen, Henning, Brange, Jens, Dunn, M.F., ""Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin,"" Biochim. Biophys. Acta 1053, 63-73 (1990).","Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin",published,journal,Biochim. Biophys. Acta,,1053,,,,,,,,,,,,,,,,,,,,,,,63,73,1990, citations,entry_citation,999,265292,1,,entry citation,,,,,"Roy, Melinda, Lee, Robert W.-K., Kaarsholm, Niels C., Thogersen, Henning, Brange, Jens, Dunn, M.F., ""Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin,"" Biochim. Biophys. Acta 1053, 63-73 (1990).","Sequence-specific 1H-NMR assignments for the aromatic region of several biologically active, monomeric insulins including native human insulin",published,journal,Biochim. Biophys. Acta,,1053,,,,,,,,,,,,,,,,,,,,,,,63,73,1990,