data_5783 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H chemical shift assignments for a mutant of human beta2-microglobulin where ARG 3 is replaced by Ala ; _BMRB_accession_number 5783 _BMRB_flat_file_name bmr5783.str _Entry_type original _Submission_date 2003-04-24 _Accession_date 2003-04-24 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Corazza Alessandra . . 2 Pettirossi Fabio . . 3 Verdone Giuliana . . 4 Viglino Paolo . . 5 Esposito Gennaro . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 503 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2004-02-12 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 5169 'beta2-microglobulin with the first 3 residues' 5782 'DN3 beta2-microglobulin without the first 3 residues' 5784 'DN3 beta2-microglobulin (H31Y mutant and with the first 3 residues)' stop_ _Original_release_date 2003-04-24 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Properties of some variants of human beta2-microglobulin and amyloidogenesis ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 14660575 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Corazza Alessandra . . 2 Pettirossi Fabio . . 3 Viglino Paolo . . 4 Verdone Giuliana . . 5 Garcia Julian . . 6 Dumy Pascal . . 7 Giorgetti Sofia . . 8 Mangione Palma . . 9 Andreola Alessia . . 10 Stoppini Monica . . 11 Bellotti Vittorio . . 12 Esposito Gennaro . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . loop_ _Keyword amyloidosis beta2-microglobulin stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _Citation_full ; 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. ; _Citation_title ; The solution structure of human beta2-microglobulin reveals the prodromes of its amyloid transition. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 11847272 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Verdone Giuliana . . 2 Corazza Alessandra . . 3 Viglino Paolo . . 4 Pettirossi Fabio . . 5 Giorgetti Sofia . . 6 Mangione Palma . . 7 Andreola Alessia . . 8 Stoppini Monica . . 9 Bellotti Vittorio . . 10 Esposito Gennaro . . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_name_full 'Protein science : a publication of the Protein Society' _Journal_volume 11 _Journal_issue 3 _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 . _Page_first 487 _Page_last 499 _Year 2002 _Details ; 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. ; save_ save_ref_2 _Saveframe_category citation _Citation_full ; 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. ; _Citation_title ; Removal of the N-terminal hexapeptide from human beta2-microglobulin facilitates protein aggregation and fibril formation. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 10850793 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Esposito G . . 2 Michelutti R . . 3 Verdone G . . 4 Viglino P . . 5 Hernandez H . . 6 Robinson C.V. V. . 7 Amoresano A . . 8 'Dal Piaz' F . . 9 Monti M . . 10 Pucci P . . 11 Mangione P . . 12 Stoppini M . . 13 Merlini G . . 14 Ferri G . . 15 Bellotti V . . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_name_full 'Protein science : a publication of the Protein Society' _Journal_volume 9 _Journal_issue 5 _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 . _Page_first 831 _Page_last 845 _Year 2000 _Details ; 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. ; save_ ################################## # Molecular system description # ################################## save_system_R3Abeta2-m _Saveframe_category molecular_system _Mol_system_name 'Arg3Ala beta2-microglobulin' _Abbreviation_common R3Abeta2-m _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label R3Abeta2-microglobulin $R3Abeta2-m stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_R3Abeta2-m _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common beta2-microglobulin _Name_variant R3Abeta2-microglobulin _Abbreviation_common R3Abeta2-m _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 100 _Mol_residue_sequence ; MIQATPKIQVYSRHPAENGK SNFLNCYVSGFHPSDIEVDL LKNGERIEKVEHSDLSFSKD WSFYLLYYTEFTPTEKDEYA CRVNHVTLSQPKIVKWDRDM ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ILE 3 GLN 4 ALA 5 THR 6 PRO 7 LYS 8 ILE 9 GLN 10 VAL 11 TYR 12 SER 13 ARG 14 HIS 15 PRO 16 ALA 17 GLU 18 ASN 19 GLY 20 LYS 21 SER 22 ASN 23 PHE 24 LEU 25 ASN 26 CYS 27 TYR 28 VAL 29 SER 30 GLY 31 PHE 32 HIS 33 PRO 34 SER 35 ASP 36 ILE 37 GLU 38 VAL 39 ASP 40 LEU 41 LEU 42 LYS 43 ASN 44 GLY 45 GLU 46 ARG 47 ILE 48 GLU 49 LYS 50 VAL 51 GLU 52 HIS 53 SER 54 ASP 55 LEU 56 SER 57 PHE 58 SER 59 LYS 60 ASP 61 TRP 62 SER 63 PHE 64 TYR 65 LEU 66 LEU 67 TYR 68 TYR 69 THR 70 GLU 71 PHE 72 THR 73 PRO 74 THR 75 GLU 76 LYS 77 ASP 78 GLU 79 TYR 80 ALA 81 CYS 82 ARG 83 VAL 84 ASN 85 HIS 86 VAL 87 THR 88 LEU 89 SER 90 GLN 91 PRO 92 LYS 93 ILE 94 VAL 95 LYS 96 TRP 97 ASP 98 ARG 99 ASP 100 MET stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 15480 w60g-b2m 100.00 100 98.00 98.00 5.49e-52 BMRB 3078 microglobulin 99.00 99 98.99 98.99 2.72e-52 BMRB 3079 microglobulin 99.00 99 98.99 98.99 2.72e-52 BMRB 5169 beta2-microglobulin 100.00 100 99.00 99.00 3.90e-53 BMRB 5782 beta2-microglobulin 96.00 97 100.00 100.00 3.01e-51 BMRB 5784 beta2-microglobulin 100.00 100 98.00 99.00 1.81e-52 PDB 1A1M 'Mhc Class I Molecule B5301 Complexed With Peptide Tpydinqml From Gag Protein Of Hiv2' 99.00 99 98.99 98.99 2.72e-52 PDB 1A1N 'Mhc Class I Molecule B3501 Complexed With Peptide Vplrpmty From The Nef Protein (75-82) Of Hiv1' 99.00 99 98.99 98.99 2.72e-52 PDB 1A1O 'Mhc Class I Molecule B5301 Complexed With Peptide Ls6 (Kpivqydnf) From The Malaria Parasite P. Falciparum' 99.00 99 98.99 98.99 2.72e-52 PDB 1A6Z 'Hfe (Human) Hemochromatosis Protein' 99.00 99 98.99 98.99 2.72e-52 PDB 1A9B 'Decamer-Like Conformation Of A Nano-Peptide Bound To Hla- B3501 Due To Nonstandard Positioning Of The C-Terminus' 100.00 100 99.00 99.00 3.90e-53 PDB 1A9E 'Decamer-Like Conformation Of A Nano-Peptide Bound To Hla- B3501 Due To Nonstandard Positioning Of The C-Terminus' 100.00 100 99.00 99.00 3.90e-53 PDB 1AGB 'Antagonist Hiv-1 Gag Peptides Induce Structural Changes In Hla B8-Hiv-1 Gag Peptide (Ggrkkykl-3r Mutation)' 99.00 99 98.99 98.99 2.72e-52 PDB 1AGC 'Antagonist Hiv-1 Gag Peptides Induce Structural Changes In Hla B8-Hiv-1 Gag Peptide (Ggkkkyql-7q Mutation)' 99.00 99 98.99 98.99 2.72e-52 PDB 1AGD 'Antagonist Hiv-1 Gag Peptides Induce Structural Changes In Hla B8-Hiv-1 Gag Peptide (Ggkkkykl-Index Peptide)' 99.00 99 98.99 98.99 2.72e-52 PDB 1AGE 'Antagonist Hiv-1 Gag Peptides Induce Structural Changes In Hla B8-Hiv-1 Gag Peptide (Ggkkkyrl-7r Mutation)' 99.00 99 98.99 98.99 2.72e-52 PDB 1AGF 'Antagonist Hiv-1 Gag Peptides Induce Structural Changes In Hla B8-Hiv-1 Gag Peptide (Ggkkrykl-5r Mutation)' 99.00 99 98.99 98.99 2.72e-52 PDB 1AKJ 'Complex Of The Human Mhc Class I Glycoprotein Hla-A2 And The T Cell Coreceptor Cd8' 99.00 99 98.99 98.99 2.72e-52 PDB 1B0G 'Class I Histocompatibility Antigen (Hla-A2.1)BETA 2- MicroglobulinPEPTIDE P1049 COMPLEX' 100.00 100 99.00 99.00 3.90e-53 PDB 1B0R 'Crystal Structure Of Hla-A0201 Complexed With A Peptide With The Carboxyl-Terminal Group Substituted By A Methyl Group' 100.00 100 99.00 99.00 3.90e-53 PDB 1BD2 'Complex Between Human T-Cell Receptor B7, Viral Peptide (Tax) And Mhc Class I Molecule Hla-A 0201' 100.00 100 99.00 99.00 3.90e-53 PDB 1C16 'Crystal Structure Analysis Of The GammaDELTA T CELL LIGAND T22' 99.00 99 98.99 98.99 2.72e-52 PDB 1CE6 'Mhc Class I H-2db Complexed With A Sendai Virus Nucleoprotein Peptide' 99.00 108 98.99 98.99 2.86e-52 PDB 1CG9 'Complex Recognition Of The Supertypic Bw6-Determinant On Hla-B And-C Molecules By The Monoclonal Antibody Sfr8-B6' 100.00 100 99.00 99.00 3.90e-53 PDB 1DE4 'Hemochromatosis Protein Hfe Complexed With Transferrin Receptor' 99.00 99 98.99 98.99 2.72e-52 PDB 1DUY 'Crystal Structure Of Hla-A0201OCTAMERIC TAX PEPTIDE Complex' 100.00 100 99.00 99.00 3.90e-53 PDB 1DUZ 'Human Class I Histocompatibility Antigen (Hla-A 0201) In Complex With A Nonameric Peptide From Htlv-1 Tax Protein' 100.00 100 99.00 99.00 3.90e-53 PDB 1E27 'Nonstandard Peptide Binding Of Hla-B5101 Complexed With Hiv Immunodominant Epitope Km1(Lppvvakei)' 99.00 99 98.99 98.99 2.72e-52 PDB 1E28 'Nonstandard Peptide Binding Of Hla-B5101 Complexed With Hiv Immunodominant Epitope Km2(Taftipsi)' 99.00 99 98.99 98.99 2.72e-52 PDB 1EEY 'Crystal Structure Determination Of Hla A2 Complexed To Peptide Gp2 With The Substitution (I2lV5LL9V)' 100.00 100 99.00 99.00 3.90e-53 PDB 1EEZ 'Crystal Structure Determination Of Hla-A2.1 Complexed To Gp2 Peptide Variant(I2lV5L)' 100.00 100 99.00 99.00 3.90e-53 PDB 1EFX 'Structure Of A Complex Between The Human Natural Killer Cell Receptor Kir2dl2 And A Class I Mhc Ligand Hla-Cw3' 100.00 100 99.00 99.00 3.90e-53 PDB 1EXU 'Crystal Structure Of The Human Mhc-Related Fc Receptor' 99.00 99 98.99 98.99 2.72e-52 PDB 1GZP 'Cd1b In Complex With Gm2 Ganglioside' 100.00 100 99.00 99.00 3.90e-53 PDB 1GZQ 'Cd1b In Complex With Phophatidylinositol' 100.00 100 99.00 99.00 3.90e-53 PDB 1HHG 'The Antigenic Identity Of Peptide(Slash)mhc Complexes: A Comparison Of The Conformation Of Five Peptides Presented By Hla-A2' 100.00 100 99.00 99.00 3.90e-53 PDB 1HHH 'The Antigenic Identity Of Peptide(Slash)mhc Complexes: A Comparison Of The Conformation Of Five Peptides Presented By Hla-A2' 100.00 100 99.00 99.00 3.90e-53 PDB 1HHI 'The Antigenic Identity Of Peptide(Slash)mhc Complexes: A Comparison Of The Conformation Of Five Peptides Presented By Hla-A2' 100.00 100 99.00 99.00 3.90e-53 PDB 1HHJ 'The Antigenic Identity Of Peptide(Slash)mhc Complexes: A Comparison Of The Conformation Of Five Peptides Presented By Hla-A2' 100.00 100 99.00 99.00 3.90e-53 PDB 1HHK 'The Antigenic Identity Of Peptide(Slash)mhc Complexes: A Comparison Of The Conformation Of Five Peptides Presented By Hla-A2' 100.00 100 99.00 99.00 3.90e-53 PDB 1HLA 'Structure Of The Human Class I Histocompatibility Antigen, Hla-A2' 97.00 97 98.97 98.97 6.60e-51 PDB 1HSA ; The Three-Dimensional Structure Of Hla-B27 At 2.1 Angstroms Resolution Suggests A General Mechanism For Tight Peptide Binding To Mhc ; 99.00 99 98.99 98.99 2.72e-52 PDB 1HSB 'Different Length Peptides Bind To Hla-Aw68 Similarly At Their Ends But Bulge Out In The Middle' 99.00 99 98.99 98.99 2.72e-52 PDB 1I1F 'Crystal Structure Of Human Class I Mhc (Hla-A2.1) Complexed With Beta 2-Microglobulin And Hiv-Rt Variant Peptide I1y' 100.00 100 99.00 99.00 3.90e-53 PDB 1I1Y 'Crystal Structure Of Human Class I Mhc (Hla-A2.1) Complexed With Beta 2-Microglobulin And Hiv-Rt Variant Peptide I1y' 100.00 100 99.00 99.00 3.90e-53 PDB 1I4F 'Crystal Structure Of Hla-A0201MAGE-A4-Peptide Complex' 100.00 100 99.00 99.00 3.90e-53 PDB 1I7R 'Crystal Structure Of Class I Mhc A2 In Complex With Peptide P1058' 100.00 100 99.00 99.00 3.90e-53 PDB 1I7T 'Crystal Structure Of Class I Mhc A2 In Complex With Peptide P1049-5v' 100.00 100 99.00 99.00 3.90e-53 PDB 1I7U 'Crystal Structure Of Class I Mhc A2 In Complex With Peptide P1049-6v' 100.00 100 99.00 99.00 3.90e-53 PDB 1IM3 'Crystal Structure Of The Human Cytomegalovirus Protein Us2 Bound To The Mhc Class I Molecule Hla-A2TAX' 100.00 100 99.00 99.00 3.90e-53 PDB 1IM9 'Crystal Structure Of The Human Natural Killer Cell Inhibitory Receptor Kir2dl1 Bound To Its Mhc Ligand Hla-Cw4' 100.00 100 99.00 99.00 3.90e-53 PDB 1JF1 'Crystal Structure Of Hla-A20201 In Complex With A Decameric Altered Peptide Ligand From The Mart-1MELAN-A' 100.00 100 99.00 99.00 3.90e-53 PDB 1JGD 'Hla-B2709 Bound To Deca-Peptide S10r' 100.00 100 99.00 99.00 3.90e-53 PDB 1JGE 'Hla-B2705 Bound To Nona-Peptide M9' 100.00 100 99.00 99.00 3.90e-53 PDB 1JHT 'Crystal Structure Of Hla-A20201 In Complex With A Nonameric Altered Peptide Ligand (Algigiltv) From The Mart- 1MELAN-A.' 100.00 100 99.00 99.00 3.90e-53 PDB 1JNJ 'Nmr Solution Structure Of The Human Beta2-Microglobulin' 100.00 100 99.00 99.00 3.90e-53 PDB 1K5N 'Hla-B2709 Bound To Nona-Peptide M9' 100.00 100 99.00 99.00 3.90e-53 PDB 1KPR 'The Human Non-Classical Major Histocompatibility Complex Molecule Hla-E' 100.00 100 99.00 99.00 3.90e-53 PDB 1KTL 'The Human Non-Classical Major Histocompatibility Complex Molecule Hla-E' 100.00 100 99.00 99.00 3.90e-53 PDB 1LDS 'Crystal Structure Of Monomeric Human Beta-2-Microglobulin' 100.00 100 99.00 99.00 3.90e-53 PDB 1LP9 'Xenoreactive Complex Ahiii 12.2 Tcr Bound To P1049HLA-A2.1' 100.00 100 99.00 99.00 3.90e-53 PDB 1M05 'Hla B8 In Complex With An Epstein Barr Virus Determinant' 99.00 99 98.99 98.99 2.72e-52 PDB 1M6O 'Crystal Structure Of Hla B4402 In Complex With Hla Dpa0201 Peptide' 99.00 99 98.99 98.99 2.72e-52 PDB 1MHE 'The Human Non-Classical Major Histocompatibility Complex Molecule Hla-E' 100.00 100 99.00 99.00 3.90e-53 PDB 1MI5 'The Crystal Structure Of Lc13 Tcr In Complex With Hlab8-Ebv Peptide Complex' 99.00 99 98.99 98.99 2.72e-52 PDB 1N2R 'A Natural Selected Dimorphism In Hla B44 Alters Self, Peptide Reportoire And T Cell Recognition.' 99.00 99 98.99 98.99 2.72e-52 PDB 1OF2 ; Crystal Structure Of Hla-B2709 Complexed With The Vasoactive Intestinal Peptide Type 1 Receptor (Vipr) Peptide (Residues 400-408) ; 100.00 100 99.00 99.00 3.90e-53 PDB 1OGA 'A Structural Basis For Immunodominant Human T-Cell Receptor Recognition.' 100.00 100 99.00 99.00 3.90e-53 PDB 1OGT ; Crystal Structure Of Hla-B2705 Complexed With The Vasoactive Intestinal Peptide Type 1 Receptor (Vipr) Peptide (Residues 400-408) ; 100.00 100 99.00 99.00 3.90e-53 PDB 1ONQ 'Crystal Structure Of Cd1a In Complex With A Sulfatide' 99.00 99 98.99 98.99 2.72e-52 PDB 1P7Q 'Crystal Structure Of Hla-A2 Bound To Lir-1, A Host And Viral Mhc Receptor' 99.00 99 98.99 98.99 2.72e-52 PDB 1PY4 'Beta2 Microglobulin Mutant H31y Displays Hints For Amyloid Formations' 100.00 100 98.00 99.00 1.81e-52 PDB 1Q94 ; Structures Of Hla-A1101 In Complex With Immunodominant Nonamer And Decamer Hiv-1 Epitopes Clearly Reveal The Presence Of A Middle Anchor Residue ; 100.00 100 99.00 99.00 3.90e-53 PDB 1QEW ; Human Class I Histocompatibility Antigen (Hla-A 0201) Complex With A Nonameric Peptide From Melanoma-Associated Antigen 3 (Residues 271-279) ; 100.00 100 99.00 99.00 3.90e-53 PDB 1QLF 'Mhc Class I H-2db Complexed With Glycopeptide K3g' 99.00 99 98.99 98.99 2.72e-52 PDB 1QR1 'Poor Binding Of A Her-2NEU EPITOPE (GP2) TO HLA-A2.1 Is Due To A Lack Of Interactions In The Center Of The Peptide' 100.00 100 99.00 99.00 3.90e-53 PDB 1QRN 'Crystal Structure Of Human A6 Tcr Complexed With Hla-A2 Bound To Altered Htlv-1 Tax Peptide P6a' 100.00 100 99.00 99.00 3.90e-53 PDB 1QSE 'Structure Of Human A6-Tcr Bound To Hla-A2 Complexed With Altered Htlv-1 Tax Peptide V7r' 100.00 100 99.00 99.00 3.90e-53 PDB 1QSF 'Structure Of A6-Tcr Bound To Hla-A2 Complexed With Altered Htlv-1 Tax Peptide Y8a' 100.00 100 99.00 99.00 3.90e-53 PDB 1QVO ; Structures Of Hla-A1101 In Complex With Immunodominant Nonamer And Decamer Hiv-1 Epitopes Clearly Reveal The Presence Of A Middle Anchor Residue ; 100.00 100 99.00 99.00 3.90e-53 PDB 1R3H 'Crystal Structure Of T10' 99.00 99 98.99 98.99 2.72e-52 PDB 1S8D 'Structural Basis For Degenerate Recognition Of Hiv Peptide Variants By Cytotoxic Lymphocyte, Variant Sl9-3a' 99.00 99 98.99 98.99 2.72e-52 PDB 1S9W 'Crystal Structure Analysis Of Ny-Eso-1 Epitope, Sllmwitqc, In Complex With Hla-A2' 100.00 100 99.00 99.00 3.90e-53 PDB 1S9X 'Crystal Structure Analysis Of Ny-Eso-1 Epitope Analogue, Sllmwitqa, In Complex With Hla-A2' 100.00 100 99.00 99.00 3.90e-53 PDB 1S9Y 'Crystal Structure Analysis Of Ny-Eso-1 Epitope Analogue, Sllmwitqs, In Complex With Hla-A2' 100.00 100 99.00 99.00 3.90e-53 PDB 1SYS 'Crystal Structure Of Hla, B4403, And Peptide Eeptvikky' 100.00 100 99.00 99.00 3.90e-53 PDB 1SYV 'Hla-B4405 Complexed To The Dominant Self Ligand Eefgraygf' 100.00 100 99.00 99.00 3.90e-53 PDB 1T1W 'Structural Basis For Degenerate Recognition Of Hiv Peptide Variants By Cytotoxic Lymphocyte, Variant Sl9-3f6i8v' 99.00 99 98.99 98.99 2.72e-52 PDB 1T1X 'Structural Basis For Degenerate Recognition Of Hiv Peptide Variants By Cytotoxic Lymphocyte, Variant Sl9-4l' 99.00 99 98.99 98.99 2.72e-52 PDB 1T1Y 'Structural Basis For Degenerate Recognition Of Hiv Peptide Variants By Cytotoxic Lymphocyte, Variant Sl9-5v' 99.00 99 98.99 98.99 2.72e-52 PDB 1T1Z 'Structural Basis For Degenerate Recognition Of Hiv Peptide Variants By Cytotoxic Lymphocyte, Variant Sl9-6a' 99.00 99 98.99 98.99 2.72e-52 PDB 1T20 'Structural Basis For Degenerate Recognition Of Hiv Peptide Variants By Cytotoxic Lymphocyte, Variant Sl9-6i' 99.00 99 98.99 98.99 2.72e-52 PDB 1T21 'Structural Basis For Degenerate Recognition Of Hiv Peptide Variants By Cytotoxic Lymphocyte, Variant Sl9, Monoclinic Crystal' 99.00 99 98.99 98.99 2.72e-52 PDB 1T22 'Structural Basis For Degenerate Recognition Of Hiv Peptide Variants By Cytotoxic Lymphocyte, Variant Sl9, Orthorhombic Crystal' 99.00 99 98.99 98.99 2.72e-52 PDB 1TMC ; The Htree-Dimensional Structure Of A Class I Major Histocompatibility Complex Molecule Missing The Alpha3 Domain Of The Heavy Chain ; 100.00 100 99.00 99.00 3.90e-53 PDB 1TVB 'Crystal Structure Of Melanoma Antigen Gp100(209-217) Bound To Human Class I Mhc Hla-A2' 100.00 100 99.00 99.00 3.90e-53 PDB 1TVH 'Crystal Structure Of Modified Melanoma Antigen Gp100(209- T2m) Bound To Human Class I Mhc Hla-A2' 100.00 100 99.00 99.00 3.90e-53 PDB 1UQS 'The Crystal Structure Of Human Cd1b With A Bound Bacterial Glycolipid' 100.00 100 99.00 99.00 3.90e-53 PDB 1UXS 'Crystal Structure Of Hla-B2705 Complexed With The Latent Membrane Protein 2 Peptide (Lmp2)of Epstein-Barr Virus' 100.00 100 99.00 99.00 3.90e-53 PDB 1UXW 'Crystal Structure Of Hla-B2709 Complexed With The Latent Membrane Protein 2 Peptide (Lmp2) Of Epstein-Barr Virus' 100.00 100 99.00 99.00 3.90e-53 PDB 1VGK 'The Crystal Structure Of Class I Major Histocompatibility Complex, H-2kd At 2.0 A Resolution' 99.00 99 98.99 98.99 2.72e-52 PDB 1W0V 'Crystal Structure Of Hla-B2705 Complexed With The Self- Peptide Tis From Egf-Response Factor 1' 100.00 100 99.00 99.00 3.90e-53 PDB 1W0W 'Crystal Structure Of Hla-B2709 Complexed With The Self- Peptide Tis From Egf-Response Factor 1' 100.00 100 99.00 99.00 3.90e-53 PDB 1W72 'Crystal Structure Of Hla-A1:mage-A1 In Complex With Fab-Hyb3' 100.00 100 99.00 99.00 3.90e-53 PDB 1X7Q 'Crystal Structure Of Hla-A1101 With Sars Nucleocapsid Peptide' 99.00 99 98.99 98.99 2.72e-52 PDB 1XH3 'Conformational Restraints And Flexibility Of 14-Meric Peptides In Complex With Hla-B3501' 99.00 99 98.99 98.99 2.72e-52 PDB 1XR8 'Crystal Structures Of Hla-B1501 In Complex With Peptides From Human Ubch6 And Epstein-Barr Virus Ebna-3' 99.00 99 98.99 98.99 2.72e-52 PDB 1XR9 'Crystal Structures Of Hla-B1501 In Complex With Peptides From Human Ubch6 And Epstein-Barr Virus Ebna-3' 99.00 99 98.99 98.99 2.72e-52 PDB 1XZ0 'Crystal Structure Of Cd1a In Complex With A Synthetic Mycobactin Lipopeptide' 99.00 99 98.99 98.99 2.72e-52 PDB 1YDP '1.9a Crystal Structure Of Hla-G' 100.00 100 99.00 99.00 3.90e-53 PDB 1YPZ 'Immune Receptor' 99.00 102 98.99 98.99 2.59e-52 PDB 1ZHK 'Crystal Structure Of Hla-B3501 Presenting 13-Mer Ebv Antigen Lpeplpqgqltay' 99.00 99 98.99 98.99 2.72e-52 PDB 1ZHL 'Crystal Structure Of Hla-B3508 Presenting 13-Mer Ebv Antigen Lpeplpqgqltay' 99.00 99 98.99 98.99 2.72e-52 PDB 1ZS8 'Crystal Structure Of The Murine Mhc Class Ib Molecule M10.5' 99.00 99 98.99 98.99 2.72e-52 PDB 1ZSD 'Crystal Structure Of Hla-B3501 Presenting An 11-Mer Ebv Antigen Eplpqgqltay' 99.00 99 98.99 98.99 2.72e-52 PDB 1ZT4 'The Crystal Structure Of Human Cd1d With And Without Alpha- Galactosylceramide' 100.00 100 99.00 99.00 3.90e-53 PDB 1ZVS 'Crystal Structure Of The First Class Mhc Mamu And Tat-Tl8 Complex' 99.00 99 98.99 98.99 2.72e-52 PDB 2A83 'Crystal Structure Of Hla-B2705 Complexed With The Glucagon Receptor (Gr) Peptide (Residues 412-420)' 100.00 100 99.00 99.00 3.90e-53 PDB 2AK4 'Crystal Structure Of Sb27 Tcr In Complex With Hla-B3508- 13mer Peptide' 99.00 99 98.99 98.99 2.72e-52 PDB 2AV1 'Crystal Structure Of Htlv-1 Tax Peptide Bound To Human Class I Mhc Hla-A2 With The E63q And K66a Mutations In The Heavy Chain.' 100.00 100 99.00 99.00 3.90e-53 PDB 2AV7 'Crystal Structure Of Htlv-1 Tax Peptide Bound To Human Class I Mhc Hla-A2 With The K66a Mutation In The Heavy Chain.' 100.00 100 99.00 99.00 3.90e-53 PDB 2AXF 'The Immunogenicity Of A Viral Cytotoxic T Cell Epitope Is Controlled By Its Mhc-Bound Conformation' 99.00 99 98.99 98.99 2.72e-52 PDB 2AXG 'The Immunogenicity Of A Viral Cytotoxic T Cell Epitope Is Controlled By Its Mhc-Bound Conformation' 99.00 99 98.99 98.99 2.72e-52 PDB 2BCK 'Crystal Structure Of Hla-A2402 Complexed With A Telomerase Peptide' 100.00 100 99.00 99.00 3.90e-53 PDB 2BNQ 'Structural And Kinetic Basis For Heightened Immunogenicity Of T Cell Vaccines' 100.00 100 99.00 99.00 3.90e-53 PDB 2BNR 'Structural And Kinetic Basis For Heightened Immunogenicity Of T Cell Vaccines' 100.00 100 99.00 99.00 3.90e-53 PDB 2BSR 'Crystal Structures And Kir3dl1 Recognition Of Three Immunodominant Viral Peptides Complexed To Hla-B2705' 100.00 100 99.00 99.00 3.90e-53 PDB 2BSS 'Crystal Structures And Kir3dl1 Recognition Of Three Immunodominant Viral Peptides Complexed To Hla-B2705' 100.00 100 99.00 99.00 3.90e-53 PDB 2BST 'Crystal Structures And Kir3dl1 Recognition Of Three Immunodominant Viral Peptides Complexed To Hla-B2705' 100.00 100 99.00 99.00 3.90e-53 PDB 2BVO ; Structures Of Three Hiv-1 Hla-B5703-Peptide Complexes And Identification Of Related Hlas Potentially Associated With Long-Term Non-Progression ; 100.00 100 99.00 99.00 3.90e-53 PDB 2BVP ; Structures Of Three Hiv-1 Hla-B5703-Peptide Complexes And Identification Of Related Hlas Potentially Associated With Long-Term Non-Progression ; 100.00 100 99.00 99.00 3.90e-53 PDB 2BVQ ; Structures Of Three Hiv-1 Hla-B5703-Peptide Complexes And Identification Of Related Hlas Potentially Associated With Long-Term Non-Progression ; 100.00 100 99.00 99.00 3.90e-53 PDB 2C7U 'Conflicting Selective Forces Affect Cd8 T-Cell Receptor Contact Sites In An Hla-A2 Immunodominant Hiv Epitope.' 100.00 100 99.00 99.00 3.90e-53 PDB 2CII 'The Crystal Structure Of H-2db Complexed With A Partial Peptide Epitope Suggests An Mhc Class I Assembly- Intermediate' 99.00 99 98.99 98.99 2.72e-52 PDB 2CIK ; Insights Into Crossreactivity In Human Allorecognition: The Structure Of Hla-B35011 Presenting An Epitope Derived From Cytochrome P450. ; 99.00 99 98.99 98.99 2.72e-52 PDB 2CLR 'Three Dimensional Structure Of A Peptide Extending Out One End Of A Class I Mhc Binding Site' 100.00 100 99.00 99.00 3.90e-53 PDB 2D31 'Crystal Structure Of Disulfide-Linked Hla-G Dimer' 100.00 100 99.00 99.00 3.90e-53 PDB 2D4F 'The Crystal Structure Of Human Beta2-Microglobulin' 100.00 100 99.00 99.00 3.90e-53 PDB 2DYP 'Crystal Structure Of Lilrb2(Lir2ILT4CD85D) COMPLEXED WITH Hla-G' 100.00 100 99.00 99.00 3.90e-53 PDB 2ESV 'Structure Of The Hla-E-VmaprtlilKK50.4 TCR COMPLEX' 100.00 100 99.00 99.00 3.90e-53 PDB 2F53 ; Directed Evolution Of Human T-Cell Receptor Cdr2 Residues By Phage Display Dramatically Enhances Affinity For Cognate Peptide-Mhc Without Apparent Cross-Reactivity ; 100.00 100 98.00 98.00 3.84e-52 PDB 2F74 'Murine Mhc Class I H-2db In Complex With Human B2- Microglobulin And Lcmv-Derived Immunodminant Peptide Gp33' 100.00 100 99.00 99.00 3.90e-53 PDB 2F8O 'A Native To Amyloidogenic Transition Regulated By A Backbone Trigger' 100.00 100 98.00 98.00 2.09e-52 PDB 2FYY 'The Role Of T Cell Receptor Alpha Genes In Directing Human Mhc Restriction' 99.00 99 98.99 98.99 2.72e-52 PDB 2FZ3 'The Role Of T Cell Receptor Alpha Genes In Directing Human Mhc Restriction' 99.00 99 98.99 98.99 2.72e-52 PDB 2GIT 'Human Class I Mhc Hla-A2 In Complex With The Modified Htlv- 1 Tax (Y5k-4-[3-Indolyl]-Butyric Acid) Peptide' 100.00 100 99.00 99.00 3.90e-53 PDB 2GJ6 'The Complex Between Tcr A6 And Human Class I Mhc Hla-A2 With The Modified Htlv-1 Tax (Y5k-4-[3-Indolyl]-Butyric Acid) Peptide' 100.00 100 99.00 99.00 3.90e-53 PDB 2GT9 'Human Class I Mhc Hla-A2 In Complex With The Decameric Melan-AMART-1(26-35) Peptide' 100.00 100 99.00 99.00 3.90e-53 PDB 2GTW 'Human Class I Mhc Hla-A2 In Complex With The Nonameric Melan-AMART-1(27-35) Peptide Having A27l Substitution' 100.00 100 99.00 99.00 3.90e-53 PDB 2GTZ 'Human Class I Mhc Hla-A2 In Complex With The Nonameric Melan-AMART-1(27-35) Peptide Having A28l Substitution' 100.00 100 99.00 99.00 3.90e-53 PDB 2GUO 'Human Class I Mhc Hla-A2 In Complex With The Native Nonameric Melan-AMART-1(27-35) Peptide' 100.00 100 99.00 99.00 3.90e-53 PDB 2H26 'Human Cd1b In Complex With Endogenous Phosphatidylcholine And Spacer' 99.00 99 98.99 98.99 2.72e-52 PDB 2H6P 'Crystal Structure Of Hla-B3501 Presenting The Human Cytochrome P450 Derived Peptide, Kpivvlhgy' 99.00 99 98.99 98.99 2.72e-52 PDB 2HJK 'Crystal Structure Of Hla-B5703 And Hiv-1 Peptide' 99.00 99 98.99 98.99 2.72e-52 PDB 2HJL 'Crystal Structure Of Hla-B5703 And Hiv-1 Peptide' 99.00 99 98.99 98.99 2.72e-52 PDB 2HLA 'Specificity Pockets For The Side Chains Of Peptide Antigens In Hla-Aw68' 99.00 99 98.99 98.99 2.72e-52 PDB 2HN7 'Hla-A1101 In Complex With Hbv Peptide Homologue' 99.00 99 98.99 98.99 2.72e-52 PDB 2J8U 'Large Cdr3a Loop Alteration As A Function Of Mhc Mutation.' 100.00 100 99.00 99.00 3.90e-53 PDB 2JCC 'Ah3 Recognition Of Mutant Hla-A2 W167a' 100.00 100 99.00 99.00 3.90e-53 PDB 2NW3 'Crystal Structure Of Hla-B3508 Presenting Ebv Peptide Eplpqgqltay At 1.7a' 99.00 99 98.99 98.99 2.72e-52 PDB 2NX5 'Crystal Structure Of Els4 Tcr Bound To Hla-B3508 Presenting Ebv Peptide Eplpqgqltay At 1.7a' 99.00 99 98.99 98.99 2.72e-52 PDB 2P5E 'Crystal Structures Of High Affinity Human T-Cell Receptors Bound To Pmhc Reveal Native Diagonal Binding Geometry' 100.00 100 98.00 98.00 3.84e-52 PDB 2P5W 'Crystal Structures Of High Affinity Human T-Cell Receptors Bound To Pmhc Reveal Native Diagonal Binding Geometry' 100.00 100 98.00 98.00 3.84e-52 PDB 2PO6 'Crystal Structure Of Cd1d-Lipid-Antigen Complexed With Beta- 2-Microglobulin, Nkt15 Alpha-Chain And Nkt15 Beta-Chain' 99.00 99 98.99 98.99 2.72e-52 PDB 2PYE ; Crystal Structures Of High Affinity Human T-Cell Receptors Bound To Pmhc Revealnative Diagonal Binding Geometry Tcr Clone C5c1 Complexed With Mhc ; 100.00 100 98.00 98.00 3.84e-52 PDB 2RFX 'Crystal Structure Of Hla-B5701, Presenting The Self Peptide, Lsspvtksf' 99.00 99 98.99 98.99 2.72e-52 PDB 2UWE 'Large Cdr3a Loop Alteration As A Function Of Mhc Mutation' 100.00 100 99.00 99.00 3.90e-53 PDB 2V2W 'T Cell Cross-Reactivity And Conformational Changes During Tcr Engagement' 100.00 100 99.00 99.00 3.90e-53 PDB 2V2X 'T Cell Cross-Reactivity And Conformational Changes During Tcr Engagement.' 100.00 100 99.00 99.00 3.90e-53 PDB 2VB5 'Solution Structure Of W60g Mutant Of Human Beta2- Microglobulin' 100.00 100 98.00 98.00 5.49e-52 PDB 2VLJ 'The Structural Dynamics And Energetics Of An Immunodominant T-Cell Receptor Are Programmed By Its Vbeta Domain' 100.00 100 99.00 99.00 3.90e-53 PDB 2VLK 'The Structural Dynamics And Energetics Of An Immunodominant T-Cell Receptor Are Programmed By Its Vbeta Domain' 100.00 100 99.00 99.00 3.90e-53 PDB 2VLL 'The Structural Dynamics And Energetics Of An Immunodominant T-Cell Receptor Are Programmed By Its Vbeta Domain' 100.00 100 99.00 99.00 3.90e-53 PDB 2VLR 'The Structural Dynamics And Energetics Of An Immunodominant T-Cell Receptor Are Programmed By Its Vbeta Domain' 100.00 100 99.00 99.00 3.90e-53 PDB 2YXF 'The High Resolution Crystal Structure Of Beta2- Microglobulin Under Physiological Conditions' 100.00 100 99.00 99.00 3.90e-53 PDB 2Z9T 'Crystal Structure Of The Human Beta-2 Microglobulin Mutant W60g' 100.00 100 98.00 98.00 5.49e-52 PDB 3B3I 'Citrullination-Dependent Differential Presentation Of A Self-Peptide By Hla-B27 Subtypes' 100.00 100 99.00 99.00 3.90e-53 PDB 3B6S ; Crystal Structure Of Hla-B2705 Complexed With The Citrullinated Vasoactive Intestinal Peptide Type 1 Receptor (Vipr) Peptide (Residues 400-408) ; 100.00 100 99.00 99.00 3.90e-53 PDB 3BW9 'Crystal Structure Of Hla B3508 In Complex With A Hcmv 12- Mer Peptide From The Pp65 Protein' 100.00 100 99.00 99.00 3.90e-53 PDB 3BWA 'Crystal Structure Of Hla B3508 In Complex With A Hcmv 8- Mer Peptide From The Pp65 Protein' 100.00 100 99.00 99.00 3.90e-53 PDB 3BZE 'The Human Non-Classical Major Histocompatibility Complex Molecule Hla-E' 100.00 100 99.00 99.00 3.90e-53 PDB 3BZF 'The Human Non-Classical Major Histocompatibility Complex Molecule Hla-E' 96.00 97 100.00 100.00 3.19e-51 PDB 3C9N ; Crystal Structure Of A Sars Corona Virus Derived Peptide Bound To The Human Major Histocompatibility Complex Class I Molecule Hla-B1501 ; 99.00 99 98.99 98.99 2.72e-52 PDB 3CDG 'Human Cd94NKG2A IN COMPLEX WITH HLA-E' 100.00 100 99.00 99.00 3.90e-53 PDB 3CII 'Structure Of Nkg2aCD94 BOUND TO HLA-E' 100.00 100 99.00 99.00 3.90e-53 PDB 3D2U 'Structure Of Ul18, A Peptide-Binding Viral Mhc Mimic, Bound To A Host Inhibitory Receptor' 99.00 99 98.99 98.99 2.72e-52 PDB 3HLA 'Specificity Pockets For The Side Chains Of Peptide Antigens In Hla-Aw68' 99.00 99 98.99 98.99 2.72e-52 DBJ BAA35182 'beta 2-microglobulin [Homo sapiens]' 99.00 119 98.99 98.99 3.47e-53 DBJ BAG38125 'unnamed protein product [Homo sapiens]' 99.00 119 98.99 98.99 3.47e-53 EMBL CAA23830 'beta-2 microglobulin [Homo sapiens]' 99.00 110 98.99 98.99 9.36e-53 EMBL CAH92078 'hypothetical protein [Pongo abelii]' 99.00 119 98.99 98.99 3.47e-53 GenBank AAA87972 beta-2-microglobulin 99.00 119 98.99 98.99 3.47e-53 GenBank AAA88008 beta-2-microglobulin 99.00 119 98.99 98.99 3.47e-53 GenBank AAB25312 'beta 2-microglobulin [Homo sapiens]' 75.00 101 98.67 98.67 8.65e-38 GenBank AAB35347 'pI 5.3 beta 2-microglobulin, BM [human, urine, chronic renal failure patient, Peptide, 98 aa]' 98.00 98 98.98 98.98 8.33e-52 GenBank AAD48083 'beta-2 microglobulin [Homo sapiens]' 99.00 119 98.99 98.99 3.47e-53 REF NP_001009066 'beta-2-microglobulin [Pan troglodytes]' 99.00 119 98.99 98.99 3.47e-53 REF NP_004039 'beta-2-microglobulin precursor [Homo sapiens]' 99.00 119 98.99 98.99 3.47e-53 SWISS-PROT P16213 'Beta-2-microglobulin precursor' 99.00 119 98.99 98.99 3.47e-53 SWISS-PROT P61769 'Beta-2-microglobulin precursor [Contains: Beta-2-microglobulin form pI 5.3]' 99.00 119 98.99 98.99 3.47e-53 SWISS-PROT P61770 'Beta-2-microglobulin precursor' 99.00 119 98.99 98.99 3.47e-53 SWISS-PROT P61771 'Beta-2-microglobulin precursor' 99.00 119 98.99 98.99 3.47e-53 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $R3Abeta2-m Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $R3Abeta2-m 'recombinant technology' 'E. coli' Escherichia coli . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $R3Abeta2-m 0.7 mM . 'sodium phosphate' 70 mM . 'sodium chloride' 100 mM . H2O 100 % . stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Saveframe_category software _Name FELIX _Version 2000 _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_1H-1H_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H TOCSY' _Sample_label . save_ save_1H-1H_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '1H-1H NOESY' _Sample_label . save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.5 0.1 na temperature 310 0.1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio Dioxane H 1 'methylene protons' ppm 3.53 internal direct . . . 1.0 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_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '1H-1H TOCSY' '1H-1H NOESY' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name R3Abeta2-microglobulin _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 2 ILE HA H 4.231 0.02 1 2 . 2 ILE HB H 1.752 0.02 1 3 . 2 ILE HG12 H 1.125 0.02 2 4 . 2 ILE HG13 H 1.417 0.02 2 5 . 2 ILE HG2 H 0.838 0.02 1 6 . 3 GLN H H 8.276 0.02 1 7 . 3 GLN HA H 4.583 0.02 1 8 . 3 GLN HB2 H 2.058 0.02 2 9 . 3 GLN HB3 H 2.136 0.02 2 10 . 3 GLN HG2 H 2.471 0.02 2 11 . 3 GLN HG3 H 2.595 0.02 2 12 . 3 GLN HE21 H 6.735 0.02 2 13 . 3 GLN HE22 H 7.431 0.02 2 14 . 4 ALA H H 9.243 0.02 1 15 . 4 ALA HA H 4.837 0.02 1 16 . 4 ALA HB H 1.569 0.02 1 17 . 5 THR H H 8.176 0.02 1 18 . 5 THR HA H 4.992 0.02 1 19 . 5 THR HB H 4.096 0.02 1 20 . 5 THR HG2 H 1.313 0.02 1 21 . 6 PRO HA H 4.395 0.02 1 22 . 6 PRO HB2 H 1.539 0.02 2 23 . 6 PRO HB3 H 1.679 0.02 2 24 . 6 PRO HG2 H 1.150 0.02 1 25 . 6 PRO HD2 H 3.164 0.02 2 26 . 6 PRO HD3 H 3.611 0.02 2 27 . 7 LYS H H 9.242 0.02 1 28 . 7 LYS HA H 4.507 0.02 1 29 . 7 LYS HB2 H 1.494 0.02 2 30 . 7 LYS HB3 H 1.782 0.02 2 31 . 8 ILE H H 8.398 0.02 1 32 . 8 ILE HA H 4.798 0.02 1 33 . 8 ILE HB H 1.641 0.02 1 34 . 8 ILE HG2 H 0.779 0.02 1 35 . 9 GLN H H 9.110 0.02 1 36 . 9 GLN HA H 4.921 0.02 1 37 . 9 GLN HB2 H 2.192 0.02 2 38 . 9 GLN HB3 H 2.333 0.02 2 39 . 9 GLN HG2 H 2.418 0.02 1 40 . 10 VAL H H 9.022 0.02 1 41 . 10 VAL HA H 5.339 0.02 1 42 . 10 VAL HB H 2.032 0.02 1 43 . 10 VAL HG1 H 0.916 0.02 2 44 . 10 VAL HG2 H 0.975 0.02 2 45 . 11 TYR H H 8.469 0.02 1 46 . 11 TYR HA H 5.316 0.02 1 47 . 11 TYR HB2 H 3.166 0.02 2 48 . 11 TYR HB3 H 3.397 0.02 2 49 . 11 TYR HD1 H 6.811 0.02 1 50 . 11 TYR HE1 H 6.555 0.02 1 51 . 12 SER H H 9.332 0.02 1 52 . 12 SER HA H 5.310 0.02 1 53 . 12 SER HB2 H 3.391 0.02 2 54 . 12 SER HB3 H 4.647 0.02 2 55 . 13 ARG H H 8.858 0.02 1 56 . 13 ARG HA H 3.924 0.02 1 57 . 13 ARG HB2 H 1.743 0.02 2 58 . 13 ARG HB3 H 1.943 0.02 2 59 . 13 ARG HG2 H 1.416 0.02 1 60 . 14 HIS H H 8.314 0.02 1 61 . 14 HIS HA H 5.341 0.02 1 62 . 14 HIS HB2 H 2.909 0.02 2 63 . 14 HIS HB3 H 3.251 0.02 2 64 . 14 HIS HD2 H 7.069 0.02 1 65 . 14 HIS HE1 H 7.848 0.02 1 66 . 15 PRO HA H 4.524 0.02 1 67 . 15 PRO HB2 H 1.960 0.02 2 68 . 15 PRO HB3 H 2.426 0.02 2 69 . 15 PRO HG2 H 2.081 0.02 2 70 . 15 PRO HG3 H 2.227 0.02 2 71 . 15 PRO HD2 H 3.799 0.02 2 72 . 15 PRO HD3 H 4.067 0.02 2 73 . 16 ALA H H 9.006 0.02 1 74 . 16 ALA HA H 4.108 0.02 1 75 . 16 ALA HB H 1.687 0.02 1 76 . 17 GLU H H 8.871 0.02 1 77 . 17 GLU HA H 4.402 0.02 1 78 . 17 GLU HB2 H 1.860 0.02 2 79 . 17 GLU HB3 H 2.169 0.02 2 80 . 19 GLY H H 8.818 0.02 1 81 . 19 GLY HA2 H 3.527 0.02 2 82 . 19 GLY HA3 H 4.185 0.02 2 83 . 20 LYS H H 7.846 0.02 1 84 . 20 LYS HA H 4.674 0.02 1 85 . 20 LYS HB2 H 1.752 0.02 2 86 . 20 LYS HB3 H 1.823 0.02 2 87 . 20 LYS HG2 H 1.291 0.02 2 88 . 20 LYS HG3 H 1.339 0.02 2 89 . 20 LYS HD2 H 1.644 0.02 1 90 . 21 SER H H 8.356 0.02 1 91 . 21 SER HA H 4.245 0.02 1 92 . 21 SER HB2 H 3.738 0.02 1 93 . 22 ASN H H 8.898 0.02 1 94 . 22 ASN HA H 4.875 0.02 1 95 . 22 ASN HB2 H 2.557 0.02 2 96 . 22 ASN HB3 H 2.748 0.02 2 97 . 22 ASN HD21 H 7.753 0.02 2 98 . 22 ASN HD22 H 7.436 0.02 2 99 . 23 PHE H H 10.341 0.02 1 100 . 23 PHE HA H 5.435 0.02 1 101 . 23 PHE HB2 H 2.633 0.02 2 102 . 23 PHE HB3 H 2.684 0.02 2 103 . 23 PHE HD1 H 6.995 0.02 1 104 . 23 PHE HE1 H 7.401 0.02 1 105 . 23 PHE HZ H 7.348 0.02 1 106 . 24 LEU H H 8.975 0.02 1 107 . 24 LEU HA H 3.688 0.02 1 108 . 24 LEU HB2 H -0.800 0.02 2 109 . 24 LEU HB3 H 0.824 0.02 2 110 . 24 LEU HG H 0.660 0.02 1 111 . 24 LEU HD1 H -0.564 0.02 2 112 . 24 LEU HD2 H 0.012 0.02 2 113 . 25 ASN H H 8.197 0.02 1 114 . 25 ASN HA H 5.380 0.02 1 115 . 25 ASN HB2 H 1.450 0.02 2 116 . 25 ASN HB3 H 1.842 0.02 2 117 . 25 ASN HD21 H 5.547 0.02 2 118 . 25 ASN HD22 H 5.743 0.02 2 119 . 26 CYS H H 9.611 0.02 1 120 . 26 CYS HA H 5.149 0.02 1 121 . 26 CYS HB2 H 2.539 0.02 2 122 . 26 CYS HB3 H 3.276 0.02 2 123 . 27 TYR H H 9.643 0.02 1 124 . 27 TYR HA H 5.414 0.02 1 125 . 27 TYR HB2 H 3.172 0.02 1 126 . 27 TYR HD1 H 7.156 0.02 1 127 . 27 TYR HE1 H 6.569 0.02 1 128 . 28 VAL H H 8.794 0.02 1 129 . 28 VAL HA H 5.198 0.02 1 130 . 28 VAL HB H 1.901 0.02 1 131 . 28 VAL HG1 H 0.765 0.02 2 132 . 28 VAL HG2 H 0.896 0.02 2 133 . 29 SER H H 8.964 0.02 1 134 . 29 SER HA H 5.730 0.02 1 135 . 29 SER HB2 H 3.447 0.02 2 136 . 29 SER HB3 H 3.858 0.02 2 137 . 30 GLY H H 8.327 0.02 1 138 . 30 GLY HA2 H 3.852 0.02 2 139 . 30 GLY HA3 H 4.106 0.02 2 140 . 31 PHE H H 7.081 0.02 1 141 . 31 PHE HA H 4.845 0.02 1 142 . 31 PHE HB2 H 1.978 0.02 2 143 . 31 PHE HB3 H 2.332 0.02 2 144 . 31 PHE HD1 H 7.004 0.02 1 145 . 31 PHE HE1 H 7.262 0.02 1 146 . 31 PHE HZ H 6.982 0.02 1 147 . 32 HIS H H 8.537 0.02 1 148 . 32 HIS HA H 4.524 0.02 1 149 . 32 HIS HB2 H 3.155 0.02 2 150 . 32 HIS HB3 H 3.269 0.02 2 151 . 32 HIS HD2 H 7.072 0.02 1 152 . 32 HIS HE1 H 7.848 0.02 1 153 . 33 PRO HA H 3.984 0.02 1 154 . 33 PRO HB2 H 2.384 0.02 1 155 . 33 PRO HG2 H 1.676 0.02 2 156 . 33 PRO HG3 H 1.988 0.02 2 157 . 33 PRO HD2 H 3.618 0.02 2 158 . 33 PRO HD3 H 3.892 0.02 2 159 . 34 SER H H 8.341 0.02 1 160 . 34 SER HA H 3.634 0.02 1 161 . 34 SER HB2 H 3.256 0.02 1 162 . 35 ASP H H 7.164 0.02 1 163 . 35 ASP HA H 4.410 0.02 1 164 . 35 ASP HB2 H 2.342 0.02 2 165 . 35 ASP HB3 H 2.398 0.02 2 166 . 36 ILE H H 7.960 0.02 1 167 . 36 ILE HA H 4.553 0.02 1 168 . 36 ILE HB H 1.376 0.02 1 169 . 36 ILE HG12 H 0.674 0.02 2 170 . 36 ILE HG13 H 1.490 0.02 2 171 . 36 ILE HG2 H 0.555 0.02 1 172 . 36 ILE HD1 H -0.492 0.02 1 173 . 37 GLU H H 7.985 0.02 1 174 . 37 GLU HA H 4.578 0.02 1 175 . 37 GLU HB2 H 1.761 0.02 2 176 . 37 GLU HB3 H 1.932 0.02 2 177 . 37 GLU HG2 H 2.042 0.02 2 178 . 37 GLU HG3 H 2.072 0.02 2 179 . 38 VAL H H 7.951 0.02 1 180 . 38 VAL HA H 4.627 0.02 1 181 . 38 VAL HB H 0.418 0.02 1 182 . 38 VAL HG1 H 0.241 0.02 2 183 . 38 VAL HG2 H 0.474 0.02 2 184 . 39 ASP H H 8.849 0.02 1 185 . 39 ASP HA H 4.938 0.02 1 186 . 39 ASP HB2 H 2.169 0.02 2 187 . 39 ASP HB3 H 2.404 0.02 2 188 . 40 LEU H H 9.034 0.02 1 189 . 40 LEU HA H 4.986 0.02 1 190 . 40 LEU HB2 H 1.226 0.02 2 191 . 40 LEU HB3 H 1.651 0.02 2 192 . 40 LEU HG H 1.605 0.02 1 193 . 40 LEU HD1 H 0.734 0.02 1 194 . 41 LEU H H 8.968 0.02 1 195 . 41 LEU HA H 4.996 0.02 1 196 . 41 LEU HB2 H 0.774 0.02 2 197 . 41 LEU HB3 H 1.582 0.02 2 198 . 41 LEU HG H 1.193 0.02 1 199 . 41 LEU HD1 H 0.392 0.02 2 200 . 41 LEU HD2 H 0.584 0.02 2 201 . 42 LYS H H 8.835 0.02 1 202 . 42 LYS HA H 4.410 0.02 1 203 . 42 LYS HB2 H 1.455 0.02 2 204 . 42 LYS HD2 H 1.737 0.02 2 205 . 43 ASN H H 9.733 0.02 1 206 . 43 ASN HA H 4.357 0.02 1 207 . 43 ASN HB2 H 2.891 0.02 1 208 . 44 GLY H H 8.803 0.02 1 209 . 44 GLY HA2 H 3.322 0.02 2 210 . 44 GLY HA3 H 4.161 0.02 2 211 . 45 GLU H H 7.812 0.02 1 212 . 45 GLU HA H 4.583 0.02 1 213 . 45 GLU HB2 H 1.951 0.02 2 214 . 45 GLU HB3 H 2.044 0.02 2 215 . 45 GLU HG2 H 2.111 0.02 2 216 . 45 GLU HG3 H 2.288 0.02 2 217 . 46 ARG H H 8.669 0.02 1 218 . 46 ARG HA H 4.168 0.02 1 219 . 46 ARG HB2 H 1.628 0.02 1 220 . 46 ARG HG2 H 1.325 0.02 2 221 . 46 ARG HG3 H 1.538 0.02 2 222 . 46 ARG HD2 H 3.070 0.02 2 223 . 46 ARG HD3 H 3.145 0.02 2 224 . 47 ILE H H 8.787 0.02 1 225 . 47 ILE HA H 3.983 0.02 1 226 . 47 ILE HB H 1.527 0.02 1 227 . 47 ILE HG12 H 1.031 0.02 2 228 . 47 ILE HG13 H 1.690 0.02 2 229 . 47 ILE HG2 H 0.975 0.02 1 230 . 47 ILE HD1 H 0.836 0.02 1 231 . 48 GLU H H 8.496 0.02 1 232 . 48 GLU HA H 4.177 0.02 1 233 . 48 GLU HB2 H 2.023 0.02 2 234 . 48 GLU HB3 H 2.113 0.02 2 235 . 48 GLU HG2 H 2.241 0.02 2 236 . 48 GLU HG3 H 2.368 0.02 2 237 . 49 LYS H H 7.960 0.02 1 238 . 49 LYS HA H 4.512 0.02 1 239 . 49 LYS HB2 H 1.741 0.02 2 240 . 49 LYS HB3 H 1.919 0.02 2 241 . 49 LYS HG2 H 1.383 0.02 2 242 . 49 LYS HG3 H 1.484 0.02 2 243 . 50 VAL H H 7.812 0.02 1 244 . 50 VAL HA H 4.385 0.02 1 245 . 50 VAL HB H 2.111 0.02 1 246 . 50 VAL HG1 H 1.022 0.02 2 247 . 50 VAL HG2 H 1.092 0.02 2 248 . 51 GLU H H 8.432 0.02 1 249 . 51 GLU HA H 4.480 0.02 1 250 . 51 GLU HB2 H 0.751 0.02 2 251 . 51 GLU HB3 H 1.571 0.02 2 252 . 51 GLU HG2 H 2.069 0.02 1 253 . 52 HIS H H 8.105 0.02 1 254 . 52 HIS HA H 5.481 0.02 1 255 . 52 HIS HB2 H 1.984 0.02 2 256 . 52 HIS HB3 H 2.429 0.02 2 257 . 53 SER H H 9.110 0.02 1 258 . 53 SER HA H 4.647 0.02 1 259 . 53 SER HB2 H 4.089 0.02 2 260 . 53 SER HB3 H 4.446 0.02 2 261 . 54 ASP H H 8.704 0.02 1 262 . 54 ASP HA H 4.807 0.02 1 263 . 54 ASP HB2 H 2.580 0.02 2 264 . 54 ASP HB3 H 2.742 0.02 2 265 . 55 LEU H H 8.715 0.02 1 266 . 55 LEU HA H 4.310 0.02 1 267 . 55 LEU HB2 H 1.878 0.02 1 268 . 55 LEU HG H 1.695 0.02 1 269 . 55 LEU HD1 H 0.904 0.02 2 270 . 55 LEU HD2 H 1.054 0.02 2 271 . 56 SER H H 8.046 0.02 1 272 . 56 SER HA H 4.764 0.02 1 273 . 56 SER HB2 H 2.735 0.02 2 274 . 56 SER HB3 H 3.412 0.02 2 275 . 57 PHE H H 8.135 0.02 1 276 . 57 PHE HA H 5.047 0.02 1 277 . 57 PHE HB2 H 2.639 0.02 1 278 . 57 PHE HD1 H 6.503 0.02 1 279 . 57 PHE HE1 H 6.976 0.02 1 280 . 58 SER H H 8.276 0.02 1 281 . 58 SER HA H 4.583 0.02 1 282 . 58 SER HB2 H 3.881 0.02 1 283 . 59 LYS HA H 3.819 0.02 1 284 . 59 LYS HB2 H 1.735 0.02 2 285 . 59 LYS HG2 H 1.386 0.02 2 286 . 59 LYS HD2 H 1.639 0.02 1 287 . 59 LYS HE2 H 2.960 0.02 1 288 . 60 ASP H H 7.678 0.02 1 289 . 60 ASP HA H 4.341 0.02 1 290 . 60 ASP HB2 H 2.250 0.02 1 291 . 61 TRP H H 7.669 0.02 1 292 . 61 TRP HA H 5.222 0.02 1 293 . 61 TRP HB2 H 2.099 0.02 1 294 . 61 TRP HD1 H 6.847 0.02 1 295 . 61 TRP HE1 H 9.631 0.02 1 296 . 61 TRP HZ2 H 7.317 0.02 1 297 . 62 SER H H 7.574 0.02 1 298 . 62 SER HA H 3.681 0.02 1 299 . 62 SER HB2 H 3.743 0.02 2 300 . 62 SER HB3 H 3.784 0.02 2 301 . 63 PHE H H 8.125 0.02 1 302 . 63 PHE HA H 5.467 0.02 1 303 . 63 PHE HB2 H 1.573 0.02 2 304 . 63 PHE HB3 H 1.984 0.02 2 305 . 63 PHE HD1 H 6.982 0.02 1 306 . 63 PHE HE1 H 7.169 0.02 1 307 . 63 PHE HZ H 7.253 0.02 1 308 . 64 TYR H H 8.264 0.02 1 309 . 64 TYR HA H 5.533 0.02 1 310 . 64 TYR HB2 H 2.804 0.02 2 311 . 64 TYR HB3 H 3.037 0.02 2 312 . 64 TYR HD1 H 7.050 0.02 1 313 . 64 TYR HE1 H 6.662 0.02 1 314 . 65 LEU H H 9.104 0.02 1 315 . 65 LEU HA H 4.591 0.02 1 316 . 65 LEU HB2 H 1.946 0.02 1 317 . 65 LEU HG H 1.743 0.02 1 318 . 65 LEU HD1 H 0.966 0.02 2 319 . 65 LEU HD2 H 1.028 0.02 2 320 . 66 LEU H H 8.129 0.02 1 321 . 66 LEU HA H 5.472 0.02 1 322 . 66 LEU HB2 H 1.978 0.02 1 323 . 66 LEU HG H 1.567 0.02 1 324 . 66 LEU HD1 H 0.803 0.02 2 325 . 66 LEU HD2 H 1.030 0.02 2 326 . 67 TYR H H 9.130 0.02 1 327 . 67 TYR HA H 5.344 0.02 1 328 . 67 TYR HB2 H 2.636 0.02 2 329 . 67 TYR HB3 H 3.042 0.02 2 330 . 67 TYR HD1 H 6.973 0.02 1 331 . 67 TYR HE1 H 6.631 0.02 1 332 . 68 TYR H H 8.931 0.02 1 333 . 68 TYR HA H 5.973 0.02 1 334 . 68 TYR HB2 H 2.650 0.02 2 335 . 68 TYR HB3 H 3.199 0.02 2 336 . 68 TYR HD1 H 6.691 0.02 1 337 . 68 TYR HE1 H 6.544 0.02 1 338 . 69 THR H H 8.288 0.02 1 339 . 69 THR HA H 4.861 0.02 1 340 . 69 THR HB H 4.108 0.02 1 341 . 69 THR HG2 H 0.945 0.02 1 342 . 70 GLU H H 8.491 0.02 1 343 . 70 GLU HA H 4.314 0.02 1 344 . 70 GLU HB2 H 1.701 0.02 2 345 . 70 GLU HB3 H 1.827 0.02 2 346 . 70 GLU HG2 H 1.880 0.02 1 347 . 71 PHE H H 8.750 0.02 1 348 . 71 PHE HA H 4.833 0.02 1 349 . 71 PHE HB2 H 2.682 0.02 2 350 . 71 PHE HB3 H 2.767 0.02 2 351 . 71 PHE HD1 H 6.203 0.02 3 352 . 71 PHE HZ H 5.718 0.02 1 353 . 72 THR H H 8.201 0.02 1 354 . 72 THR HA H 4.465 0.02 1 355 . 72 THR HB H 3.870 0.02 1 356 . 72 THR HG2 H 0.854 0.02 1 357 . 73 PRO HA H 4.579 0.02 1 358 . 73 PRO HB2 H 2.197 0.02 2 359 . 73 PRO HB3 H 2.401 0.02 2 360 . 73 PRO HG2 H 1.397 0.02 2 361 . 73 PRO HG3 H 1.973 0.02 2 362 . 73 PRO HD2 H 2.238 0.02 2 363 . 73 PRO HD3 H 3.966 0.02 2 364 . 74 THR H H 8.064 0.02 1 365 . 74 THR HA H 4.675 0.02 1 366 . 74 THR HB H 4.542 0.02 1 367 . 74 THR HG2 H 1.315 0.02 1 368 . 75 GLU H H 9.094 0.02 1 369 . 75 GLU HA H 4.206 0.02 1 370 . 75 GLU HB2 H 2.077 0.02 2 371 . 75 GLU HG2 H 2.275 0.02 2 372 . 75 GLU HG3 H 2.352 0.02 2 373 . 76 LYS H H 7.799 0.02 1 374 . 76 LYS HA H 4.458 0.02 1 375 . 76 LYS HB2 H 1.783 0.02 2 376 . 76 LYS HB3 H 1.865 0.02 2 377 . 76 LYS HG2 H 1.409 0.02 2 378 . 76 LYS HD2 H 1.679 0.02 2 379 . 76 LYS HE2 H 2.986 0.02 2 380 . 77 ASP H H 7.116 0.02 1 381 . 77 ASP HA H 5.117 0.02 1 382 . 77 ASP HB2 H 2.139 0.02 2 383 . 77 ASP HB3 H 2.808 0.02 2 384 . 78 GLU H H 8.598 0.02 1 385 . 78 GLU HA H 4.797 0.02 1 386 . 78 GLU HB2 H 1.989 0.02 2 387 . 78 GLU HB3 H 2.081 0.02 2 388 . 78 GLU HG2 H 2.368 0.02 2 389 . 79 TYR H H 9.461 0.02 1 390 . 79 TYR HA H 5.589 0.02 1 391 . 79 TYR HB2 H 2.718 0.02 2 392 . 79 TYR HB3 H 2.812 0.02 2 393 . 79 TYR HD1 H 7.093 0.02 3 394 . 79 TYR HE1 H 6.879 0.02 3 395 . 80 ALA H H 8.791 0.02 1 396 . 80 ALA HA H 5.038 0.02 1 397 . 80 ALA HB H 1.191 0.02 1 398 . 81 CYS H H 9.094 0.02 1 399 . 81 CYS HA H 5.104 0.02 1 400 . 81 CYS HB2 H 2.611 0.02 2 401 . 81 CYS HB3 H 3.050 0.02 2 402 . 82 ARG H H 9.407 0.02 1 403 . 82 ARG HA H 5.391 0.02 1 404 . 82 ARG HB2 H 1.184 0.02 2 405 . 82 ARG HB3 H 1.789 0.02 2 406 . 82 ARG HG2 H 1.266 0.02 2 407 . 83 VAL H H 8.973 0.02 1 408 . 83 VAL HA H 4.996 0.02 1 409 . 83 VAL HB H 1.562 0.02 1 410 . 83 VAL HG1 H 0.824 0.02 2 411 . 83 VAL HG2 H 0.780 0.02 2 412 . 84 ASN H H 9.013 0.02 1 413 . 84 ASN HA H 5.187 0.02 1 414 . 84 ASN HB2 H 2.387 0.02 2 415 . 84 ASN HB3 H 2.806 0.02 2 416 . 85 HIS H H 7.740 0.02 1 417 . 85 HIS HA H 4.555 0.02 1 418 . 85 HIS HB2 H 2.423 0.02 2 419 . 85 HIS HB3 H 2.901 0.02 2 420 . 85 HIS HD1 H 7.554 0.02 1 421 . 85 HIS HE1 H 8.133 0.02 1 422 . 86 VAL H H 7.986 0.02 1 423 . 86 VAL HA H 3.976 0.02 1 424 . 86 VAL HB H 1.929 0.02 1 425 . 86 VAL HG1 H 0.620 0.02 2 426 . 86 VAL HG2 H 0.855 0.02 2 427 . 87 THR H H 7.587 0.02 1 428 . 87 THR HA H 4.162 0.02 1 429 . 87 THR HB H 4.492 0.02 1 430 . 87 THR HG2 H 1.480 0.02 1 431 . 88 LEU H H 8.034 0.02 1 432 . 88 LEU HA H 4.757 0.02 1 433 . 88 LEU HB2 H 1.837 0.02 2 434 . 88 LEU HB3 H 2.033 0.02 2 435 . 88 LEU HG H 1.713 0.02 1 436 . 88 LEU HD1 H 0.968 0.02 2 437 . 89 SER HA H 4.239 0.02 1 438 . 89 SER HB2 H 3.952 0.02 2 439 . 89 SER HB3 H 3.971 0.02 2 440 . 90 GLN H H 7.531 0.02 1 441 . 90 GLN HA H 4.733 0.02 1 442 . 90 GLN HB2 H 1.884 0.02 2 443 . 90 GLN HB3 H 2.141 0.02 2 444 . 90 GLN HG2 H 2.291 0.02 2 445 . 91 PRO HA H 4.491 0.02 1 446 . 91 PRO HB2 H 1.493 0.02 2 447 . 91 PRO HB3 H 1.838 0.02 2 448 . 91 PRO HG2 H 1.768 0.02 2 449 . 91 PRO HG3 H 1.995 0.02 2 450 . 91 PRO HD2 H 3.522 0.02 2 451 . 91 PRO HD3 H 3.729 0.02 2 452 . 92 LYS H H 8.732 0.02 1 453 . 92 LYS HA H 4.516 0.02 1 454 . 92 LYS HB2 H 1.647 0.02 2 455 . 92 LYS HB3 H 1.746 0.02 2 456 . 92 LYS HG2 H 1.347 0.02 2 457 . 92 LYS HG3 H 1.412 0.02 2 458 . 93 ILE H H 8.499 0.02 1 459 . 93 ILE HA H 4.789 0.02 1 460 . 93 ILE HB H 1.701 0.02 1 461 . 93 ILE HG12 H 1.414 0.02 2 462 . 93 ILE HG2 H 0.616 0.02 1 463 . 93 ILE HD1 H 0.742 0.02 1 464 . 94 VAL H H 9.052 0.02 1 465 . 94 VAL HA H 4.318 0.02 1 466 . 94 VAL HB H 1.887 0.02 1 467 . 94 VAL HG1 H 0.907 0.02 2 468 . 94 VAL HG2 H 1.024 0.02 2 469 . 95 LYS H H 8.790 0.02 1 470 . 95 LYS HA H 4.445 0.02 1 471 . 95 LYS HB2 H 1.838 0.02 2 472 . 95 LYS HG2 H 1.438 0.02 2 473 . 95 LYS HG3 H 1.534 0.02 2 474 . 96 TRP H H 8.695 0.02 1 475 . 96 TRP HA H 4.656 0.02 1 476 . 96 TRP HB2 H 2.600 0.02 2 477 . 96 TRP HB3 H 3.481 0.02 2 478 . 96 TRP HD1 H 7.114 0.02 1 479 . 96 TRP HE1 H 10.457 0.02 1 480 . 96 TRP HE3 H 7.970 0.02 1 481 . 96 TRP HZ2 H 7.633 0.02 1 482 . 96 TRP HZ3 H 7.618 0.02 1 483 . 96 TRP HH2 H 7.477 0.02 1 484 . 97 ASP H H 8.432 0.02 1 485 . 97 ASP HA H 4.480 0.02 1 486 . 97 ASP HB2 H 2.458 0.02 2 487 . 97 ASP HB3 H 2.754 0.02 2 488 . 98 ARG H H 7.427 0.02 1 489 . 98 ARG HA H 3.390 0.02 1 490 . 98 ARG HB2 H 1.130 0.02 2 491 . 98 ARG HB3 H 1.413 0.02 2 492 . 98 ARG HG2 H 0.930 0.02 2 493 . 98 ARG HD2 H 2.951 0.02 2 494 . 99 ASP H H 8.195 0.02 1 495 . 99 ASP HA H 4.649 0.02 1 496 . 99 ASP HB2 H 2.598 0.02 2 497 . 99 ASP HB3 H 2.775 0.02 2 498 . 100 MET H H 7.587 0.02 1 499 . 100 MET HA H 4.284 0.02 1 500 . 100 MET HB2 H 2.027 0.02 2 501 . 100 MET HB3 H 2.161 0.02 2 502 . 100 MET HG2 H 2.539 0.02 2 503 . 100 MET HG3 H 2.578 0.02 2 stop_ save_