data_6656 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 6656 _Entry.Title ; 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 ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2005-06-06 _Entry.Accession_date 2005-06-06 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version . _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 M. Chavez . Isabel . 6656 2 Cecilia Andreu . . . 6656 3 Paloma Vidal . . . 6656 4 Felix Freire . . . 6656 5 Nuria Aboitiz . . . 6656 6 Patrick Groves . . . 6656 7 Juan Asensio . L. . 6656 8 Gregorio Asensio . . . 6656 9 Michiro Muraki . . . 6656 10 F. Canada . Javier . 6656 11 Jesus Jimenez-Barbero . . . 6656 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 6656 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 142 6656 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 2 . . 2008-07-31 2005-06-06 update BMRB 'updating non-standard residues' 6656 1 . . 2005-12-22 2005-06-06 original author 'Original release' 6656 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 6591 AcAMP2F18Pff/Y20Pff 6656 BMRB 6637 'AcAMP2F18Nalb mutant' 6656 BMRB 6639 'AcAMP2F18W mutant' 6656 BMRB 6647 AcAMP2F18Wb 6656 BMRB 6657 'AcAMP2F18Nal mutant' 6656 PDB 1ZNT 'BMRB Entry Tracking System' 6656 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 6656 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 16220560 _Citation.Full_citation . _Citation.Title ; 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 ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Chem. Eur. J.' _Citation.Journal_name_full . _Citation.Journal_volume 11 _Citation.Journal_issue 23 _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 7060 _Citation.Page_last 7074 _Citation.Year 2005 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 M. Chavez . Isabel . 6656 1 2 Cecilia Andreu . . . 6656 1 3 Paloma Vidal . . . 6656 1 4 Nuria Aboitiz . . . 6656 1 5 Felix Freire . . . 6656 1 6 Patrick Groves . . . 6656 1 7 Juan Asensio . L. . 6656 1 8 Gregorio Asensio . . . 6656 1 9 Michiro Muraki . . . 6656 1 10 F. Canada . Javier . 6656 1 11 Jesus Jimenez-Barbero . . . 6656 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID AcAMP2 6656 1 'carbohydrate binding' 6656 1 Chitin 6656 1 hevein 6656 1 'Molecular Dynamics' 6656 1 'molecular recognition' 6656 1 NMR 6656 1 protein 6656 1 stop_ save_ save_reference-1 _Citation.Sf_category citations _Citation.Sf_framecode reference-1 _Citation.Entry_ID 6656 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 8627629 _Citation.Full_citation ; 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. ; _Citation.Title 'H NMR study of the solution structure of Ac-AMP2, a sugar binding antimicrobial protein isolated from Amaranthus caudatus.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full 'Journal of molecular biology' _Citation.Journal_volume 258 _Citation.Journal_issue 2 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0022-2836 _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 322 _Citation.Page_last 333 _Citation.Year 1996 _Citation.Details ; 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. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 'J. C.' Martins J. C. . 6656 2 2 D. Maes D. . . 6656 2 3 R. Loris R. . . 6656 2 4 'H. A.' Pepermans H. A. . 6656 2 5 L. Wyns L. . . 6656 2 6 R. Willem R. . . 6656 2 7 P. Verheyden P. . . 6656 2 stop_ save_ save_reference-2 _Citation.Sf_category citations _Citation.Sf_framecode reference-2 _Citation.Entry_ID 6656 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 12144516 _Citation.Full_citation ; 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. ; _Citation.Title 'The importance of CH/pi interactions to the function of carbohydrate binding proteins.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Protein Pept. Lett.' _Citation.Journal_name_full 'Protein and peptide letters' _Citation.Journal_volume 9 _Citation.Journal_issue 3 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0929-8665 _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 195 _Citation.Page_last 209 _Citation.Year 2002 _Citation.Details ; 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. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Michiro Muraki M. . . 6656 3 stop_ save_ save_reference-3 _Citation.Sf_category citations _Citation.Sf_framecode reference-3 _Citation.Entry_ID 6656 _Citation.ID 4 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 15368576 _Citation.Full_citation ; 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. ; _Citation.Title '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.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Chembiochem _Citation.Journal_name_full 'Chembiochem : a European journal of chemical biology' _Citation.Journal_volume 5 _Citation.Journal_issue 9 _Citation.Journal_ASTM . _Citation.Journal_ISSN 1439-4227 _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 1245 _Citation.Page_last 1255 _Citation.Year 2004 _Citation.Details ; 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. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Nuria Aboitiz N. . . 6656 4 2 Miquel Vila-Perello M. . . 6656 4 3 Patrick Groves P. . . 6656 4 4 'Juan Luis' Asensio J. L. . 6656 4 5 David Andreu D. . . 6656 4 6 'Francisco Javier' Canada F. J. . 6656 4 7 Jesus Jimenez-Barbero J. . . 6656 4 stop_ save_ save_reference-4 _Citation.Sf_category citations _Citation.Sf_framecode reference-4 _Citation.Entry_ID 6656 _Citation.ID 5 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10842338 _Citation.Full_citation ; 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. ; _Citation.Title '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.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Proteins _Citation.Journal_name_full Proteins _Citation.Journal_volume 40 _Citation.Journal_issue 2 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0887-3585 _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 218 _Citation.Page_last 236 _Citation.Year 2000 _Citation.Details ; 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. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 'J. L.' Asensio J. L. . 6656 5 2 'H. C.' Siebert H. C. . 6656 5 3 'C. W.' 'von Der Lieth' C. W. . 6656 5 4 J. Laynez J. . . 6656 5 5 M. Bruix M. . . 6656 5 6 'U. M.' Soedjanaamadja U. M. . 6656 5 7 'J. J.' Beintema J. J. . 6656 5 8 'F. J.' Canada F. J. . 6656 5 9 'H. J.' Gabius H. J. . 6656 5 10 J. Jimenez-Barbero J. . . 6656 5 stop_ save_ save_reference-5 _Citation.Sf_category citations _Citation.Sf_framecode reference-5 _Citation.Entry_ID 6656 _Citation.ID 6 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10903932 _Citation.Full_citation ; 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. ; _Citation.Title 'Structural basis for chitin recognition by defense proteins: GlcNAc residues are bound in a multivalent fashion by extended binding sites in hevein domains.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'Chem. Biol.' _Citation.Journal_name_full 'Chemistry & biology' _Citation.Journal_volume 7 _Citation.Journal_issue 7 _Citation.Journal_ASTM . _Citation.Journal_ISSN 1074-5521 _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 529 _Citation.Page_last 543 _Citation.Year 2000 _Citation.Details ; 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. ; loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 'J. L.' Asensio J. L. . 6656 6 2 'F. J.' Canada F. J. . 6656 6 3 'H. C.' Siebert H. C. . 6656 6 4 J. Laynez J. . . 6656 6 5 A. Poveda A. . . 6656 6 6 'P. M.' Nieto P. M. . 6656 6 7 'U. M.' Soedjanaamadja U. M. . 6656 6 8 'H. J.' Gabius H. J. . 6656 6 9 J. Jimenez-Barbero J. . . 6656 6 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_AcAMP2F18Pff_F20Pfff _Assembly.Sf_category assembly _Assembly.Sf_framecode system_AcAMP2F18Pff_F20Pfff _Assembly.Entry_ID 6656 _Assembly.ID 1 _Assembly.Name 'AcAMP2F18Pff/F20Pfff mutant' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state 'all disulfide bound' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 6656 1 stop_ loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 AcAMP2F18Pff/F20Pfff 1 $AcAMP2F18Pff_F20Pfff . . . native . . . . . 6656 1 stop_ loop_ _Bond.ID _Bond.Type _Bond.Value_order _Bond.Assembly_atom_ID_1 _Bond.Entity_assembly_ID_1 _Bond.Entity_assembly_name_1 _Bond.Entity_ID_1 _Bond.Comp_ID_1 _Bond.Comp_index_ID_1 _Bond.Seq_ID_1 _Bond.Atom_ID_1 _Bond.Assembly_atom_ID_2 _Bond.Entity_assembly_ID_2 _Bond.Entity_assembly_name_2 _Bond.Entity_ID_2 _Bond.Comp_ID_2 _Bond.Comp_index_ID_2 _Bond.Seq_ID_2 _Bond.Atom_ID_2 _Bond.Auth_entity_assembly_ID_1 _Bond.Auth_entity_assembly_name_1 _Bond.Auth_seq_ID_1 _Bond.Auth_comp_ID_1 _Bond.Auth_atom_ID_1 _Bond.Auth_entity_assembly_ID_2 _Bond.Auth_entity_assembly_name_2 _Bond.Auth_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 disulfide single . 1 . 1 CYS 4 4 SG . 1 . 1 CYS 15 15 SG . . . . . . . . . . 6656 1 2 disulfide single . 1 . 1 CYS 9 9 SG . 1 . 1 CYS 21 21 SG . . . . . . . . . . 6656 1 3 disulfide single . 1 . 1 CYS 14 14 SG . 1 . 1 CYS 28 28 SG . . . . . . . . . . 6656 1 stop_ loop_ _Assembly_db_link.Author_supplied _Assembly_db_link.Database_code _Assembly_db_link.Accession_code _Assembly_db_link.Entry_mol_code _Assembly_db_link.Entry_mol_name _Assembly_db_link.Entry_experimental_method _Assembly_db_link.Entry_structure_resolution _Assembly_db_link.Entry_relation_type _Assembly_db_link.Entry_details _Assembly_db_link.Entry_ID _Assembly_db_link.Assembly_ID . PDB 1MMC . . . . . ; Residues Phe18 and Tyr20 have been mutated to 4-fluorophenylalanine in the molecule studied here ; 6656 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID AcAMP2F18Pff/F20Pfff abbreviation 6656 1 'AcAMP2F18Pff/F20Pfff mutant' system 6656 1 stop_ loop_ _Assembly_bio_function.Biological_function _Assembly_bio_function.Entry_ID _Assembly_bio_function.Assembly_ID 'chitin binding lectin' 6656 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_AcAMP2F18Pff_F20Pfff _Entity.Sf_category entity _Entity.Sf_framecode AcAMP2F18Pff_F20Pfff _Entity.Entry_ID 6656 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name AcAMP2 _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; VGECVRGRCPSGMCCSQXGX CGKGPKYCGR ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 30 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'all disulfide bound' _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 3209 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details ; The secondary structure of this protein presents beta-sheet on residues over residues 13 to 23. This protein is a hevein domain, and has high homology with AcAMP2 antimicrobial peptide. Carbohydrate binding site involves residues S16, F18FF, F20FF and Y27. ; _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-28 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 6591 . AcAMP2F18Pff/Y20Pff . . . . . 100.00 30 100.00 100.00 1.34e-08 . . . . 6656 1 2 no PDB 1ZNT . "18 Nmr Structures Of Acamp2-Like Peptide With Non Natural Fluoroaromatic Residue (Acamp2f18pffY20PFF) COMPLEX WITH N,N,N- Triac" . . . . . 100.00 31 100.00 100.00 1.35e-08 . . . . 6656 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID AcAMP2 common 6656 1 AcAMP2F18Pff/Y20Pfff abbreviation 6656 1 'AcAMP2F18Pff/Y20Pfff mutant' variant 6656 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . VAL . 6656 1 2 . GLY . 6656 1 3 . GLU . 6656 1 4 . CYS . 6656 1 5 . VAL . 6656 1 6 . ARG . 6656 1 7 . GLY . 6656 1 8 . ARG . 6656 1 9 . CYS . 6656 1 10 . PRO . 6656 1 11 . SER . 6656 1 12 . GLY . 6656 1 13 . MET . 6656 1 14 . CYS . 6656 1 15 . CYS . 6656 1 16 . SER . 6656 1 17 . GLN . 6656 1 18 . PFF . 6656 1 19 . GLY . 6656 1 20 . PFF . 6656 1 21 . CYS . 6656 1 22 . GLY . 6656 1 23 . LYS . 6656 1 24 . GLY . 6656 1 25 . PRO . 6656 1 26 . LYS . 6656 1 27 . TYR . 6656 1 28 . CYS . 6656 1 29 . GLY . 6656 1 30 . ARG . 6656 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . VAL 1 1 6656 1 . GLY 2 2 6656 1 . GLU 3 3 6656 1 . CYS 4 4 6656 1 . VAL 5 5 6656 1 . ARG 6 6 6656 1 . GLY 7 7 6656 1 . ARG 8 8 6656 1 . CYS 9 9 6656 1 . PRO 10 10 6656 1 . SER 11 11 6656 1 . GLY 12 12 6656 1 . MET 13 13 6656 1 . CYS 14 14 6656 1 . CYS 15 15 6656 1 . SER 16 16 6656 1 . GLN 17 17 6656 1 . PFF 18 18 6656 1 . GLY 19 19 6656 1 . PFF 20 20 6656 1 . CYS 21 21 6656 1 . GLY 22 22 6656 1 . LYS 23 23 6656 1 . GLY 24 24 6656 1 . PRO 25 25 6656 1 . LYS 26 26 6656 1 . TYR 27 27 6656 1 . CYS 28 28 6656 1 . GLY 29 29 6656 1 . ARG 30 30 6656 1 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 6656 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Subvariant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Cellular_location _Entity_natural_src.Fragment _Entity_natural_src.Fraction _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Plasmid_details _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Dev_stage _Entity_natural_src.Details _Entity_natural_src.Citation_ID _Entity_natural_src.Citation_label _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $AcAMP2F18Pff_F20Pfff . 3567 organism . 'Amaranthus caudatus' 'inca wheat' . . Eukaryota Viridiplantae Amaranthus caudatus . . . . seed . . . . . . . . . . . . . . . . 6656 1 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Entity_experimental_src_list.Sf_category experimental_source _Entity_experimental_src_list.Sf_framecode experimental_source _Entity_experimental_src_list.Entry_ID 6656 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_subvariant _Entity_experimental_src.Host_org_organ _Entity_experimental_src.Host_org_tissue _Entity_experimental_src.Host_org_tissue_fraction _Entity_experimental_src.Host_org_cell_line _Entity_experimental_src.Host_org_cell_type _Entity_experimental_src.Host_org_cellular_location _Entity_experimental_src.Host_org_organelle _Entity_experimental_src.Host_org_gene _Entity_experimental_src.Host_org_culture_collection _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Host_org_dev_stage _Entity_experimental_src.Details _Entity_experimental_src.Citation_ID _Entity_experimental_src.Citation_label _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $AcAMP2F18Pff_F20Pfff . 'chemical synthesis' . . . . . . . . . . . . . . . . . . . . . . . . . . ; The residues Phe18 and Tyr20 of the native AcAMP2 were changed to 4-fluorophenylalanine. The aminoacids were manually assembled by solid phase synthesis using Fmoc chemistry according to satandard protocols. ; . . 6656 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_PFF _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_PFF _Chem_comp.Entry_ID 6656 _Chem_comp.ID PFF _Chem_comp.Provenance . _Chem_comp.Name 4-FLUORO-L-PHENYLALANINE _Chem_comp.Type 'L-peptide linking' _Chem_comp.BMRB_code . _Chem_comp.PDB_code PFF _Chem_comp.Ambiguous_flag no _Chem_comp.Initial_date 2003-07-30 _Chem_comp.Modified_date 2011-06-04 _Chem_comp.Release_status REL _Chem_comp.Replaced_by . _Chem_comp.Replaces . _Chem_comp.One_letter_code F _Chem_comp.Three_letter_code PFF _Chem_comp.Number_atoms_all . _Chem_comp.Number_atoms_nh . _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code . _Chem_comp.Mon_nstd_flag . _Chem_comp.Mon_nstd_class . _Chem_comp.Mon_nstd_details . _Chem_comp.Mon_nstd_parent . _Chem_comp.Mon_nstd_parent_comp_ID PHE _Chem_comp.Std_deriv_one_letter_code . _Chem_comp.Std_deriv_three_letter_code . _Chem_comp.Std_deriv_BMRB_code . _Chem_comp.Std_deriv_PDB_code . _Chem_comp.Std_deriv_chem_comp_name . _Chem_comp.Synonyms . _Chem_comp.Formal_charge 0 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic yes _Chem_comp.Formula 'C9 H10 F N O2' _Chem_comp.Formula_weight 183.180 _Chem_comp.Formula_mono_iso_wt_nat . _Chem_comp.Formula_mono_iso_wt_13C . _Chem_comp.Formula_mono_iso_wt_15N . _Chem_comp.Formula_mono_iso_wt_13C_15N . _Chem_comp.Image_file_name . _Chem_comp.Image_file_format . _Chem_comp.Topo_file_name . _Chem_comp.Topo_file_format . _Chem_comp.Struct_file_name . _Chem_comp.Struct_file_format . _Chem_comp.Stereochem_param_file_name . _Chem_comp.Stereochem_param_file_format . _Chem_comp.Model_details . _Chem_comp.Model_erf . _Chem_comp.Model_source . _Chem_comp.Model_coordinates_details . _Chem_comp.Model_coordinates_missing_flag yes _Chem_comp.Ideal_coordinates_details . _Chem_comp.Ideal_coordinates_missing_flag no _Chem_comp.Model_coordinates_db_code . _Chem_comp.Processing_site PDBE _Chem_comp.Vendor . _Chem_comp.Vendor_product_code . _Chem_comp.Details ; Information obtained from PDB's Chemical Component Dictionary at http://wwpdb-remediation.rutgers.edu/downloads.html Downloaded on Mon Aug 8 14:18:20 2011 ; _Chem_comp.DB_query_date . _Chem_comp.DB_last_query_revised_last_date . loop_ _Chem_comp_descriptor.Descriptor _Chem_comp_descriptor.Type _Chem_comp_descriptor.Program _Chem_comp_descriptor.Program_version _Chem_comp_descriptor.Entry_ID _Chem_comp_descriptor.Comp_ID c1cc(ccc1CC(C(=O)O)N)F SMILES 'OpenEye OEToolkits' 1.5.0 6656 PFF c1cc(ccc1C[C@@H](C(=O)O)N)F SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 6656 PFF Fc1ccc(cc1)CC(C(=O)O)N SMILES ACDLabs 10.04 6656 PFF InChI=1S/C9H10FNO2/c10-7-3-1-6(2-4-7)5-8(11)9(12)13/h1-4,8H,5,11H2,(H,12,13)/t8-/m0/s1 InChI InChI 1.03 6656 PFF N[C@@H](Cc1ccc(F)cc1)C(O)=O SMILES_CANONICAL CACTVS 3.341 6656 PFF N[CH](Cc1ccc(F)cc1)C(O)=O SMILES CACTVS 3.341 6656 PFF XWHHYOYVRVGJJY-QMMMGPOBSA-N InChIKey InChI 1.03 6656 PFF stop_ loop_ _Chem_comp_identifier.Identifier _Chem_comp_identifier.Type _Chem_comp_identifier.Program _Chem_comp_identifier.Program_version _Chem_comp_identifier.Entry_ID _Chem_comp_identifier.Comp_ID '(2S)-2-amino-3-(4-fluorophenyl)propanoic acid' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 6656 PFF 4-fluoro-L-phenylalanine 'SYSTEMATIC NAME' ACDLabs 10.04 6656 PFF stop_ loop_ _Chem_comp_atom.Atom_ID _Chem_comp_atom.BMRB_code _Chem_comp_atom.PDB_atom_ID _Chem_comp_atom.Alt_atom_ID _Chem_comp_atom.Auth_atom_ID _Chem_comp_atom.Type_symbol _Chem_comp_atom.Isotope_number _Chem_comp_atom.Chirality _Chem_comp_atom.Stereo_config _Chem_comp_atom.Charge _Chem_comp_atom.Partial_charge _Chem_comp_atom.Oxidation_number _Chem_comp_atom.Unpaired_electron_number _Chem_comp_atom.Align _Chem_comp_atom.Aromatic_flag _Chem_comp_atom.Leaving_atom_flag _Chem_comp_atom.Substruct_code _Chem_comp_atom.Ionizable _Chem_comp_atom.Drawing_2D_coord_x _Chem_comp_atom.Drawing_2D_coord_y _Chem_comp_atom.Model_Cartn_x _Chem_comp_atom.Model_Cartn_x_esd _Chem_comp_atom.Model_Cartn_y _Chem_comp_atom.Model_Cartn_y_esd _Chem_comp_atom.Model_Cartn_z _Chem_comp_atom.Model_Cartn_z_esd _Chem_comp_atom.Model_Cartn_x_ideal _Chem_comp_atom.Model_Cartn_y_ideal _Chem_comp_atom.Model_Cartn_z_ideal _Chem_comp_atom.PDBX_ordinal _Chem_comp_atom.Details _Chem_comp_atom.Entry_ID _Chem_comp_atom.Comp_ID N . N . . N . . N 0 . . . . no no . . . . 46.465 . 27.890 . 1.389 . -0.040 -1.210 0.053 1 . 6656 PFF CA . CA . . C . . S 0 . . . . no no . . . . 47.091 . 29.119 . 0.910 . 1.172 -1.709 0.652 2 . 6656 PFF C . C . . C . . N 0 . . . . no no . . . . 48.578 . 29.095 . 1.054 . 1.083 -3.207 0.905 3 . 6656 PFF O . O . . O . . N 0 . . . . no no . . . . 49.223 . 30.130 . 1.065 . 0.040 -3.770 1.222 4 . 6656 PFF OXT . OXT . . O . . N 0 . . . . no yes . . . . . . . . . . 2.247 -3.882 0.744 5 . 6656 PFF CB . CB . . C . . N 0 . . . . no no . . . . 46.628 . 30.322 . 1.695 . 1.484 -0.975 1.962 6 . 6656 PFF CG . CG . . C . . N 0 . . . . yes no . . . . 45.398 . 31.033 . 1.284 . 2.940 -1.060 2.353 7 . 6656 PFF CD1 . CD1 . . C . . N 0 . . . . yes no . . . . 44.257 . 30.753 . 2.015 . 3.369 -2.109 3.149 8 . 6656 PFF CD2 . CD2 . . C . . N 0 . . . . yes no . . . . 45.270 . 31.304 . -0.071 . 3.820 -0.086 1.907 9 . 6656 PFF CE1 . CE1 . . C . . N 0 . . . . yes no . . . . 43.027 . 30.643 . 1.380 . 4.715 -2.188 3.510 10 . 6656 PFF CE2 . CE2 . . C . . N 0 . . . . yes no . . . . 44.037 . 31.227 . -0.706 . 5.166 -0.165 2.268 11 . 6656 PFF CZ . CZ . . C . . N 0 . . . . yes no . . . . 42.906 . 30.905 . 0.023 . 5.613 -1.216 3.069 12 . 6656 PFF F . F . . F . . N 0 . . . . no no . . . . 41.702 . 30.837 . -0.574 . 6.904 -1.291 3.415 13 . 6656 PFF H . H . . H . . N 0 . . . . no no . . . . 45.440 . 27.989 . 1.351 . -0.102 -1.155 -0.950 14 . 6656 PFF H2 . H2 . . H . . N 0 . . . . no yes . . . . 46.757 . 27.102 . 0.794 . -0.715 -0.741 0.634 15 . 6656 PFF HA . HA . . H . . N 0 . . . . no no . . . . 46.800 . 29.187 . -0.149 . 1.965 -1.558 -0.089 16 . 6656 PFF HXT . HXT . . H . . N 0 . . . . no yes . . . . 0.945 . -0.015 . 0.091 . 2.188 -4.848 0.901 17 . 6656 PFF HB2 . HB2 . . H . . N 0 . . . . no no . . . . 46.472 . 29.987 . 2.731 . 1.215 0.087 1.879 18 . 6656 PFF HB3 . HB3 . . H . . N 0 . . . . no no . . . . 47.423 . 31.063 . 1.523 . 0.859 -1.368 2.775 19 . 6656 PFF HD1 . HD1 . . H . . N 0 . . . . no no . . . . 44.322 . 30.622 . 3.066 . 2.677 -2.871 3.497 20 . 6656 PFF HD2 . HD2 . . H . . N 0 . . . . no no . . . . 46.129 . 31.575 . -0.632 . 3.481 0.736 1.283 21 . 6656 PFF HE1 . HE1 . . H . . N 0 . . . . no no . . . . 42.171 . 30.356 . 1.938 . 5.063 -3.006 4.134 22 . 6656 PFF HE2 . HE2 . . H . . N 0 . . . . no no . . . . 43.963 . 31.415 . -1.748 . 5.865 0.592 1.925 23 . 6656 PFF stop_ loop_ _Chem_comp_bond.ID _Chem_comp_bond.Type _Chem_comp_bond.Value_order _Chem_comp_bond.Atom_ID_1 _Chem_comp_bond.Atom_ID_2 _Chem_comp_bond.Aromatic_flag _Chem_comp_bond.Stereo_config _Chem_comp_bond.Ordinal _Chem_comp_bond.Details _Chem_comp_bond.Entry_ID _Chem_comp_bond.Comp_ID 1 . SING N CA no N 1 . 6656 PFF 2 . SING N H no N 2 . 6656 PFF 3 . SING N H2 no N 3 . 6656 PFF 4 . SING CA C no N 4 . 6656 PFF 5 . SING CA CB no N 5 . 6656 PFF 6 . SING CA HA no N 6 . 6656 PFF 7 . DOUB C O no N 7 . 6656 PFF 8 . SING C OXT no N 8 . 6656 PFF 9 . SING OXT HXT no N 9 . 6656 PFF 10 . SING CB CG no N 10 . 6656 PFF 11 . SING CB HB2 no N 11 . 6656 PFF 12 . SING CB HB3 no N 12 . 6656 PFF 13 . DOUB CG CD1 yes N 13 . 6656 PFF 14 . SING CG CD2 yes N 14 . 6656 PFF 15 . SING CD1 CE1 yes N 15 . 6656 PFF 16 . SING CD1 HD1 no N 16 . 6656 PFF 17 . DOUB CD2 CE2 yes N 17 . 6656 PFF 18 . SING CD2 HD2 no N 18 . 6656 PFF 19 . DOUB CE1 CZ yes N 19 . 6656 PFF 20 . SING CE1 HE1 no N 20 . 6656 PFF 21 . SING CE2 CZ yes N 21 . 6656 PFF 22 . SING CE2 HE2 no N 22 . 6656 PFF 23 . SING CZ F no N 23 . 6656 PFF stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample-1 _Sample.Sf_category sample _Sample.Sf_framecode sample-1 _Sample.Entry_ID 6656 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 AcAMP2 . . . 1 $AcAMP2F18Pff_F20Pfff . . 2.0 . . mM . . . . 6656 1 2 H2O . . . . . . . 90 . . % . . . . 6656 1 3 D2O . . . . . . . 10 . . % . . . . 6656 1 stop_ save_ ####################### # Sample conditions # ####################### save_conditions-1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode conditions-1 _Sample_condition_list.Entry_ID 6656 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID 'ionic strength' 0.15 0.02 M 6656 1 pH 5.6 0.2 pH 6656 1 temperature 298 0.2 K 6656 1 stop_ save_ ############################ # Computer software used # ############################ save_XWINNMR _Software.Sf_category software _Software.Sf_framecode XWINNMR _Software.Entry_ID 6656 _Software.ID 1 _Software.Name xwinnmr _Software.Version 3.2 _Software.Details 'The software performs acquisition and processing of NMR experiments' loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'Data collection' 6656 1 stop_ save_ save_XEASY _Software.Sf_category software _Software.Sf_framecode XEASY _Software.Entry_ID 6656 _Software.ID 2 _Software.Name XEASY _Software.Version 1.3.13 _Software.Details ; 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. This program helps visualization and assignment of 2D NMR spectra. ; loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'Data analysis' 6656 2 stop_ save_ save_DYANA _Software.Sf_category software _Software.Sf_framecode DYANA _Software.Entry_ID 6656 _Software.ID 3 _Software.Name DYANA _Software.Version 1.5 _Software.Details ; 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. This program yields a collection of protein structures that fit the 1H-1H distance constraints experimentally obtained. ; loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'Structure solution' 6656 3 stop_ save_ save_AMBER _Software.Sf_category software _Software.Sf_framecode AMBER _Software.Entry_ID 6656 _Software.ID 4 _Software.Name AMBER _Software.Version 5.0 _Software.Details ; Pearlman D. A., Case D. A., Caldwell J. W., Cheatham T. E., DeBolt S., Ross W. S., Ferguson D., Seibel G. L., and Kollman P. A. (1995) Comp. Phys. Commun. 91, 1-41. AMBER, a package of computer programs for applying molecular mechanics, normal mode analysis, molecular dynamics and free energy calculations to simulate the structural and energetic properties of molecules." The programs used from this package perform molecular dynamics calculations on protein structures. They also convert dyana-format pdb files into amber-format pdb files. ; loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'Structure refinement' 6656 4 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer _NMR_spectrometer.Entry_ID 6656 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model AMX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 500 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 6656 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 NMR_spectrometer Bruker AMX . 500 . . . 6656 1 stop_ save_ ############################# # NMR applied experiments # ############################# save_experiment_list _Experiment_list.Sf_category experiment_list _Experiment_list.Sf_framecode experiment_list _Experiment_list.Entry_ID 6656 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 TOCSY . . . . . . . . . . . 1 $sample-1 . . . 1 $conditions-1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 6656 1 2 NOESY . . . . . . . . . . . 1 $sample-1 . . . 1 $conditions-1 . . . 1 $NMR_spectrometer . . . . . . . . . . . . . . . . 6656 1 stop_ save_ save_NMR_applied_experiment _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_applied_experiment _NMR_spec_expt.Entry_ID 6656 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name . _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_1 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_1 _NMR_spec_expt.Entry_ID 6656 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name TOCSY _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_2 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_2 _NMR_spec_expt.Entry_ID 6656 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name NOESY _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID 1 _NMR_spec_expt.NMR_spectrometer_label $NMR_spectrometer _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 6656 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.0 . . . . . . . . . 6656 1 H 2 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.153506088 . . . . . . . . . 6656 1 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_AcAMP2F18Pff_Y20Pfff_shifts _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode AcAMP2F18Pff_Y20Pfff_shifts _Assigned_chem_shift_list.Entry_ID 6656 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $conditions-1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details ; The atom HA2 of GLY22 shows up at 1.828; due the proximity to the aromatic system of the residue 27 ; _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID . . 1 $sample-1 . 6656 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 1 1 VAL HA H 1 3.831 0.004 . 1 . . . . . . . . 6656 1 2 . 1 1 1 1 VAL HB H 1 2.143 0.007 . 1 . . . . . . . . 6656 1 3 . 1 1 1 1 VAL HG11 H 1 0.989 0.005 . 2 . . . . . . . . 6656 1 4 . 1 1 1 1 VAL HG12 H 1 0.989 0.005 . 2 . . . . . . . . 6656 1 5 . 1 1 1 1 VAL HG13 H 1 0.989 0.005 . 2 . . . . . . . . 6656 1 6 . 1 1 1 1 VAL HG21 H 1 1.038 0.02 . 2 . . . . . . . . 6656 1 7 . 1 1 1 1 VAL HG22 H 1 1.038 0.02 . 2 . . . . . . . . 6656 1 8 . 1 1 1 1 VAL HG23 H 1 1.038 0.02 . 2 . . . . . . . . 6656 1 9 . 1 1 2 2 GLY H H 1 8.969 0.02 . 1 . . . . . . . . 6656 1 10 . 1 1 2 2 GLY HA2 H 1 3.836 0.001 . 2 . . . . . . . . 6656 1 11 . 1 1 2 2 GLY HA3 H 1 4.224 0.012 . 2 . . . . . . . . 6656 1 12 . 1 1 3 3 GLU H H 1 9.095 0.003 . 1 . . . . . . . . 6656 1 13 . 1 1 3 3 GLU HA H 1 4.255 0.006 . 1 . . . . . . . . 6656 1 14 . 1 1 3 3 GLU HB2 H 1 1.902 0.005 . 2 . . . . . . . . 6656 1 15 . 1 1 3 3 GLU HB3 H 1 1.952 0.008 . 2 . . . . . . . . 6656 1 16 . 1 1 3 3 GLU HG2 H 1 2.362 0.007 . 2 . . . . . . . . 6656 1 17 . 1 1 4 4 CYS H H 1 7.654 0.001 . 1 . . . . . . . . 6656 1 18 . 1 1 4 4 CYS HA H 1 4.420 0.005 . 1 . . . . . . . . 6656 1 19 . 1 1 4 4 CYS HB2 H 1 2.770 0.005 . 2 . . . . . . . . 6656 1 20 . 1 1 4 4 CYS HB3 H 1 3.080 0.004 . 2 . . . . . . . . 6656 1 21 . 1 1 5 5 VAL H H 1 8.398 0.002 . 1 . . . . . . . . 6656 1 22 . 1 1 5 5 VAL HA H 1 4.069 0.003 . 1 . . . . . . . . 6656 1 23 . 1 1 5 5 VAL HB H 1 1.868 0.015 . 1 . . . . . . . . 6656 1 24 . 1 1 5 5 VAL HG11 H 1 0.841 0.007 . 2 . . . . . . . . 6656 1 25 . 1 1 5 5 VAL HG12 H 1 0.841 0.007 . 2 . . . . . . . . 6656 1 26 . 1 1 5 5 VAL HG13 H 1 0.841 0.007 . 2 . . . . . . . . 6656 1 27 . 1 1 6 6 ARG H H 1 9.381 0.003 . 1 . . . . . . . . 6656 1 28 . 1 1 6 6 ARG HA H 1 3.828 0.003 . 1 . . . . . . . . 6656 1 29 . 1 1 6 6 ARG HB2 H 1 1.807 0.008 . 2 . . . . . . . . 6656 1 30 . 1 1 6 6 ARG HB3 H 1 1.885 0.006 . 2 . . . . . . . . 6656 1 31 . 1 1 6 6 ARG HG2 H 1 1.557 0.008 . 2 . . . . . . . . 6656 1 32 . 1 1 6 6 ARG HD2 H 1 3.196 0.007 . 2 . . . . . . . . 6656 1 33 . 1 1 6 6 ARG HE H 1 7.145 0.001 . 1 . . . . . . . . 6656 1 34 . 1 1 7 7 GLY H H 1 8.277 0.002 . 1 . . . . . . . . 6656 1 35 . 1 1 7 7 GLY HA2 H 1 3.679 0.02 . 2 . . . . . . . . 6656 1 36 . 1 1 7 7 GLY HA3 H 1 4.064 0.001 . 2 . . . . . . . . 6656 1 37 . 1 1 8 8 ARG H H 1 7.837 0.004 . 1 . . . . . . . . 6656 1 38 . 1 1 8 8 ARG HA H 1 4.631 0.006 . 1 . . . . . . . . 6656 1 39 . 1 1 8 8 ARG HB2 H 1 1.807 0.006 . 2 . . . . . . . . 6656 1 40 . 1 1 8 8 ARG HB3 H 1 1.857 0.001 . 2 . . . . . . . . 6656 1 41 . 1 1 8 8 ARG HG2 H 1 1.538 0.006 . 2 . . . . . . . . 6656 1 42 . 1 1 8 8 ARG HG3 H 1 1.630 0.004 . 2 . . . . . . . . 6656 1 43 . 1 1 8 8 ARG HD2 H 1 3.143 0.002 . 2 . . . . . . . . 6656 1 44 . 1 1 8 8 ARG HH21 H 1 6.781 0.001 . 2 . . . . . . . . 6656 1 45 . 1 1 8 8 ARG HH22 H 1 7.339 0.001 . 2 . . . . . . . . 6656 1 46 . 1 1 9 9 CYS H H 1 8.608 0.005 . 1 . . . . . . . . 6656 1 47 . 1 1 9 9 CYS HA H 1 5.190 0.003 . 1 . . . . . . . . 6656 1 48 . 1 1 9 9 CYS HB2 H 1 2.225 0.007 . 2 . . . . . . . . 6656 1 49 . 1 1 9 9 CYS HB3 H 1 2.813 0.010 . 2 . . . . . . . . 6656 1 50 . 1 1 10 10 PRO HA H 1 4.405 0.003 . 1 . . . . . . . . 6656 1 51 . 1 1 10 10 PRO HB2 H 1 1.672 0.009 . 2 . . . . . . . . 6656 1 52 . 1 1 10 10 PRO HB3 H 1 2.340 0.006 . 2 . . . . . . . . 6656 1 53 . 1 1 10 10 PRO HG2 H 1 1.911 0.005 . 2 . . . . . . . . 6656 1 54 . 1 1 10 10 PRO HG3 H 1 1.960 0.007 . 2 . . . . . . . . 6656 1 55 . 1 1 10 10 PRO HD2 H 1 3.433 0.007 . 2 . . . . . . . . 6656 1 56 . 1 1 10 10 PRO HD3 H 1 3.916 0.004 . 2 . . . . . . . . 6656 1 57 . 1 1 11 11 SER H H 1 8.278 0.002 . 1 . . . . . . . . 6656 1 58 . 1 1 11 11 SER HA H 1 4.105 0.004 . 1 . . . . . . . . 6656 1 59 . 1 1 11 11 SER HB2 H 1 3.677 0.02 . 2 . . . . . . . . 6656 1 60 . 1 1 12 12 GLY H H 1 8.876 0.002 . 1 . . . . . . . . 6656 1 61 . 1 1 12 12 GLY HA2 H 1 3.627 0.004 . 2 . . . . . . . . 6656 1 62 . 1 1 12 12 GLY HA3 H 1 4.188 0.02 . 2 . . . . . . . . 6656 1 63 . 1 1 13 13 MET H H 1 7.907 0.002 . 1 . . . . . . . . 6656 1 64 . 1 1 13 13 MET HA H 1 4.637 0.009 . 1 . . . . . . . . 6656 1 65 . 1 1 13 13 MET HB2 H 1 1.717 0.006 . 2 . . . . . . . . 6656 1 66 . 1 1 13 13 MET HB3 H 1 1.985 0.006 . 2 . . . . . . . . 6656 1 67 . 1 1 13 13 MET HG2 H 1 2.287 0.006 . 2 . . . . . . . . 6656 1 68 . 1 1 14 14 CYS H H 1 9.212 0.005 . 1 . . . . . . . . 6656 1 69 . 1 1 14 14 CYS HA H 1 4.568 0.007 . 1 . . . . . . . . 6656 1 70 . 1 1 14 14 CYS HB2 H 1 2.360 0.004 . 2 . . . . . . . . 6656 1 71 . 1 1 14 14 CYS HB3 H 1 3.801 0.001 . 2 . . . . . . . . 6656 1 72 . 1 1 15 15 CYS H H 1 8.769 0.003 . 1 . . . . . . . . 6656 1 73 . 1 1 15 15 CYS HA H 1 4.727 0.02 . 1 . . . . . . . . 6656 1 74 . 1 1 15 15 CYS HB2 H 1 2.879 0.002 . 2 . . . . . . . . 6656 1 75 . 1 1 16 16 SER HA H 1 4.893 0.001 . 1 . . . . . . . . 6656 1 76 . 1 1 16 16 SER HB2 H 1 4.376 0.004 . 2 . . . . . . . . 6656 1 77 . 1 1 17 17 GLN H H 1 9.133 0.003 . 1 . . . . . . . . 6656 1 78 . 1 1 17 17 GLN HA H 1 4.027 0.008 . 1 . . . . . . . . 6656 1 79 . 1 1 17 17 GLN HB2 H 1 1.655 0.002 . 2 . . . . . . . . 6656 1 80 . 1 1 17 17 GLN HB3 H 1 1.811 0.006 . 2 . . . . . . . . 6656 1 81 . 1 1 17 17 GLN HG3 H 1 1.573 0.004 . 2 . . . . . . . . 6656 1 82 . 1 1 17 17 GLN HE21 H 1 7.041 0.007 . 2 . . . . . . . . 6656 1 83 . 1 1 17 17 GLN HE22 H 1 7.588 0.02 . 2 . . . . . . . . 6656 1 84 . 1 1 18 18 PFF H H 1 7.489 0.007 . 1 . . . . . . . . 6656 1 85 . 1 1 18 18 PFF HA H 1 4.714 0.02 . 1 . . . . . . . . 6656 1 86 . 1 1 18 18 PFF HB2 H 1 2.791 0.003 . 2 . . . . . . . . 6656 1 87 . 1 1 18 18 PFF HB3 H 1 3.614 0.006 . 2 . . . . . . . . 6656 1 88 . 1 1 18 18 PFF HD1 H 1 7.254 0.002 . 3 . . . . . . . . 6656 1 89 . 1 1 18 18 PFF HE1 H 1 7.048 0.02 . 3 . . . . . . . . 6656 1 90 . 1 1 19 19 GLY H H 1 7.850 0.001 . 1 . . . . . . . . 6656 1 91 . 1 1 19 19 GLY HA2 H 1 3.530 0.002 . 2 . . . . . . . . 6656 1 92 . 1 1 19 19 GLY HA3 H 1 3.925 0.005 . 2 . . . . . . . . 6656 1 93 . 1 1 20 20 PFF H H 1 7.517 0.006 . 1 . . . . . . . . 6656 1 94 . 1 1 20 20 PFF HA H 1 5.064 0.007 . 1 . . . . . . . . 6656 1 95 . 1 1 20 20 PFF HB2 H 1 2.884 0.006 . 2 . . . . . . . . 6656 1 96 . 1 1 20 20 PFF HB3 H 1 3.342 0.006 . 2 . . . . . . . . 6656 1 97 . 1 1 20 20 PFF HD1 H 1 7.035 0.004 . 3 . . . . . . . . 6656 1 98 . 1 1 20 20 PFF HE1 H 1 6.680 0.005 . 3 . . . . . . . . 6656 1 99 . 1 1 21 21 CYS H H 1 8.919 0.004 . 1 . . . . . . . . 6656 1 100 . 1 1 21 21 CYS HA H 1 5.503 0.002 . 1 . . . . . . . . 6656 1 101 . 1 1 21 21 CYS HB2 H 1 2.799 0.02 . 2 . . . . . . . . 6656 1 102 . 1 1 22 22 GLY H H 1 8.422 0.004 . 1 . . . . . . . . 6656 1 103 . 1 1 22 22 GLY HA2 H 1 1.828 0.003 . 2 . . . . . . . . 6656 1 104 . 1 1 22 22 GLY HA3 H 1 3.611 0.005 . 2 . . . . . . . . 6656 1 105 . 1 1 23 23 LYS H H 1 8.034 0.004 . 1 . . . . . . . . 6656 1 106 . 1 1 23 23 LYS HA H 1 4.899 0.005 . 1 . . . . . . . . 6656 1 107 . 1 1 23 23 LYS HB2 H 1 1.621 0.008 . 2 . . . . . . . . 6656 1 108 . 1 1 23 23 LYS HB3 H 1 1.825 0.006 . 2 . . . . . . . . 6656 1 109 . 1 1 23 23 LYS HG2 H 1 1.309 0.007 . 2 . . . . . . . . 6656 1 110 . 1 1 23 23 LYS HG3 H 1 1.403 0.004 . 2 . . . . . . . . 6656 1 111 . 1 1 23 23 LYS HD2 H 1 1.697 0.02 . 2 . . . . . . . . 6656 1 112 . 1 1 23 23 LYS HE2 H 1 2.850 0.02 . 2 . . . . . . . . 6656 1 113 . 1 1 24 24 GLY H H 1 8.347 0.003 . 1 . . . . . . . . 6656 1 114 . 1 1 24 24 GLY HA2 H 1 3.917 0.002 . 2 . . . . . . . . 6656 1 115 . 1 1 24 24 GLY HA3 H 1 4.538 0.005 . 2 . . . . . . . . 6656 1 116 . 1 1 25 25 PRO HA H 1 4.251 0.005 . 1 . . . . . . . . 6656 1 117 . 1 1 25 25 PRO HB2 H 1 1.908 0.003 . 2 . . . . . . . . 6656 1 118 . 1 1 25 25 PRO HG2 H 1 2.021 0.005 . 2 . . . . . . . . 6656 1 119 . 1 1 25 25 PRO HG3 H 1 2.272 0.004 . 2 . . . . . . . . 6656 1 120 . 1 1 25 25 PRO HD2 H 1 3.606 0.001 . 2 . . . . . . . . 6656 1 121 . 1 1 25 25 PRO HD3 H 1 3.809 0.006 . 2 . . . . . . . . 6656 1 122 . 1 1 26 26 LYS H H 1 8.780 0.002 . 1 . . . . . . . . 6656 1 123 . 1 1 26 26 LYS HA H 1 3.976 0.004 . 1 . . . . . . . . 6656 1 124 . 1 1 26 26 LYS HB2 H 1 1.544 0.011 . 2 . . . . . . . . 6656 1 125 . 1 1 26 26 LYS HB3 H 1 1.744 0.005 . 2 . . . . . . . . 6656 1 126 . 1 1 26 26 LYS HG2 H 1 1.075 0.007 . 2 . . . . . . . . 6656 1 127 . 1 1 26 26 LYS HG3 H 1 1.343 0.004 . 2 . . . . . . . . 6656 1 128 . 1 1 27 27 TYR H H 1 7.609 0.002 . 1 . . . . . . . . 6656 1 129 . 1 1 27 27 TYR HA H 1 4.084 0.004 . 1 . . . . . . . . 6656 1 130 . 1 1 27 27 TYR HB2 H 1 2.476 0.006 . 2 . . . . . . . . 6656 1 131 . 1 1 27 27 TYR HB3 H 1 2.931 0.004 . 2 . . . . . . . . 6656 1 132 . 1 1 27 27 TYR HD1 H 1 7.143 0.002 . 3 . . . . . . . . 6656 1 133 . 1 1 27 27 TYR HE1 H 1 6.683 0.007 . 3 . . . . . . . . 6656 1 134 . 1 1 28 28 CYS H H 1 8.465 0.001 . 1 . . . . . . . . 6656 1 135 . 1 1 28 28 CYS HA H 1 4.519 0.009 . 1 . . . . . . . . 6656 1 136 . 1 1 28 28 CYS HB2 H 1 2.712 0.007 . 2 . . . . . . . . 6656 1 137 . 1 1 28 28 CYS HB3 H 1 3.205 0.006 . 2 . . . . . . . . 6656 1 138 . 1 1 29 29 GLY H H 1 7.975 0.002 . 1 . . . . . . . . 6656 1 139 . 1 1 29 29 GLY HA2 H 1 3.973 0.010 . 2 . . . . . . . . 6656 1 140 . 1 1 30 30 ARG H H 1 8.273 0.002 . 1 . . . . . . . . 6656 1 141 . 1 1 30 30 ARG HA H 1 4.261 0.008 . 1 . . . . . . . . 6656 1 142 . 1 1 30 30 ARG HB2 H 1 1.682 0.002 . 2 . . . . . . . . 6656 1 143 . 1 1 30 30 ARG HB3 H 1 1.838 0.004 . 2 . . . . . . . . 6656 1 144 . 1 1 30 30 ARG HG2 H 1 1.547 0.003 . 2 . . . . . . . . 6656 1 145 . 1 1 30 30 ARG HD2 H 1 3.147 0.004 . 2 . . . . . . . . 6656 1 146 . 1 1 30 30 ARG HE H 1 7.145 0.001 . 1 . . . . . . . . 6656 1 147 . 1 1 30 30 ARG HH21 H 1 7.011 0.02 . 1 . . . . . . . . 6656 1 148 . 1 1 30 30 ARG HH22 H 1 7.011 0.02 . 1 . . . . . . . . 6656 1 stop_ save_