data_5783 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5783 _Entry.Title ; 1H chemical shift assignments for a mutant of human beta2-microglobulin where ARG 3 is replaced by Ala ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2003-04-24 _Entry.Accession_date 2003-04-24 _Entry.Last_release_date 2003-04-24 _Entry.Original_release_date 2003-04-24 _Entry.Origination author _Entry.Format_name . _Entry.NMR_STAR_version 3.2.0.16 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Source_data_format . _Entry.Source_data_format_version . _Entry.Generated_software_name . _Entry.Generated_software_version . _Entry.Generated_software_ID . _Entry.Generated_software_label . _Entry.Generated_date . _Entry.DOI . _Entry.UUID . _Entry.Related_coordinate_file_name . _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.ORCID _Entry_author.Entry_ID 1 Alessandra Corazza . . . . 5783 2 Fabio Pettirossi . . . . 5783 3 Giuliana Verdone . . . . 5783 4 Paolo Viglino . . . . 5783 5 Gennaro Esposito . . . . 5783 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5783 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 587 5783 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 1 . . 2004-02-12 . original BMRB . 5783 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 5169 'beta2-microglobulin with the first 3 residues' 5783 BMRB 5782 'DN3 beta2-microglobulin without the first 3 residues' 5783 BMRB 5784 'DN3 beta2-microglobulin (H31Y mutant and with the first 3 residues)' 5783 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5783 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 14660575 _Citation.Full_citation . _Citation.Title ; Properties of some variants of human beta2-microglobulin and amyloidogenesis ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biol. Chem.' _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _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 . _Citation.Page_last . _Citation.Year . _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.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Alessandra Corazza . . . . 5783 1 2 Fabio Pettirossi . . . . 5783 1 3 Paolo Viglino . . . . 5783 1 4 Giuliana Verdone . . . . 5783 1 5 Julian Garcia . . . . 5783 1 6 Pascal Dumy . . . . 5783 1 7 Sofia Giorgetti . . . . 5783 1 8 Palma Mangione . . . . 5783 1 9 Alessia Andreola . . . . 5783 1 10 Monica Stoppini . . . . 5783 1 11 Vittorio Bellotti . . . . 5783 1 12 Gennaro Esposito . . . . 5783 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID amyloidosis 5783 1 beta2-microglobulin 5783 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 5783 _Citation.ID 2 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 11847272 _Citation.Full_citation ; 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 _Citation.Journal_abbrev 'Protein Sci.' _Citation.Journal_name_full 'Protein science : a publication of the Protein Society' _Citation.Journal_volume 11 _Citation.Journal_issue 3 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0961-8368 _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 487 _Citation.Page_last 499 _Citation.Year 2002 _Citation.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. ; 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.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Giuliana Verdone G. . . . 5783 2 2 Alessandra Corazza A. . . . 5783 2 3 Paolo Viglino P. . . . 5783 2 4 Fabio Pettirossi F. . . . 5783 2 5 Sofia Giorgetti S. . . . 5783 2 6 Palma Mangione P. . . . 5783 2 7 Alessia Andreola A. . . . 5783 2 8 Monica Stoppini M. . . . 5783 2 9 Vittorio Bellotti V. . . . 5783 2 10 Gennaro Esposito G. . . . 5783 2 stop_ save_ save_ref_2 _Citation.Sf_category citations _Citation.Sf_framecode ref_2 _Citation.Entry_ID 5783 _Citation.ID 3 _Citation.Class 'reference citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 10850793 _Citation.Full_citation ; 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 _Citation.Journal_abbrev 'Protein Sci.' _Citation.Journal_name_full 'Protein science : a publication of the Protein Society' _Citation.Journal_volume 9 _Citation.Journal_issue 5 _Citation.Journal_ASTM . _Citation.Journal_ISSN 0961-8368 _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 831 _Citation.Page_last 845 _Citation.Year 2000 _Citation.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. ; 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.ORCID _Citation_author.Entry_ID _Citation_author.Citation_ID 1 G Esposito G. . . . 5783 3 2 R Michelutti R. . . . 5783 3 3 G Verdone G. . . . 5783 3 4 P Viglino P. . . . 5783 3 5 H Hernandez H. . . . 5783 3 6 C.V. Robinson C. V. . . 5783 3 7 A Amoresano A. . . . 5783 3 8 F 'Dal Piaz' F. . . . 5783 3 9 M Monti M. . . . 5783 3 10 P Pucci P. . . . 5783 3 11 P Mangione P. . . . 5783 3 12 M Stoppini M. . . . 5783 3 13 G Merlini G. . . . 5783 3 14 G Ferri G. . . . 5783 3 15 V Bellotti V. . . . 5783 3 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_R3Abeta2-m _Assembly.Sf_category assembly _Assembly.Sf_framecode system_R3Abeta2-m _Assembly.Entry_ID 5783 _Assembly.ID 1 _Assembly.Name 'Arg3Ala beta2-microglobulin' _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 5783 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 R3Abeta2-microglobulin 1 $R3Abeta2-m . . . native . . . . . 5783 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_asym_ID_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_asym_ID_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 26 26 SG . 1 . 1 CYS 81 81 SG . . . . . . . . . . . . 5783 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'Arg3Ala beta2-microglobulin' system 5783 1 R3Abeta2-m abbreviation 5783 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_R3Abeta2-m _Entity.Sf_category entity _Entity.Sf_framecode R3Abeta2-m _Entity.Entry_ID 5783 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name beta2-microglobulin _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 ; MIQATPKIQVYSRHPAENGK SNFLNCYVSGFHPSDIEVDL LKNGERIEKVEHSDLSFSKD WSFYLLYYTEFTPTEKDEYA CRVNHVTLSQPKIVKWDRDM ; _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 100 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'all disulfide bound' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date 2008-08-19 _Entity.DB_query_revised_last_date 2008-08-19 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 . . BMRB 15480 . w60g-b2m . . . . . 100.00 100 98.00 98.00 5.49e-52 . . . . 5783 1 . . BMRB 3078 . microglobulin . . . . . 99.00 99 98.99 98.99 2.72e-52 . . . . 5783 1 . . BMRB 3079 . microglobulin . . . . . 99.00 99 98.99 98.99 2.72e-52 . . . . 5783 1 . . BMRB 5169 . beta2-microglobulin . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . BMRB 5782 . beta2-microglobulin . . . . . 96.00 97 100.00 100.00 3.01e-51 . . . . 5783 1 . . BMRB 5784 . beta2-microglobulin . . . . . 100.00 100 98.00 99.00 1.81e-52 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . PDB 1A6Z . 'Hfe (Human) Hemochromatosis Protein' . . . . . 99.00 99 98.99 98.99 2.72e-52 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . PDB 1B0G . 'Class I Histocompatibility Antigen (Hla-A2.1)BETA 2- MicroglobulinPEPTIDE P1049 COMPLEX' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . PDB 1C16 . 'Crystal Structure Analysis Of The GammaDELTA T CELL LIGAND T22' . . . . . 99.00 99 98.99 98.99 2.72e-52 . . . . 5783 1 . . PDB 1CE6 . 'Mhc Class I H-2db Complexed With A Sendai Virus Nucleoprotein Peptide' . . . . . 99.00 108 98.99 98.99 2.86e-52 . . . . 5783 1 . . 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 . . . . 5783 1 . . PDB 1DE4 . 'Hemochromatosis Protein Hfe Complexed With Transferrin Receptor' . . . . . 99.00 99 98.99 98.99 2.72e-52 . . . . 5783 1 . . PDB 1DUY . 'Crystal Structure Of Hla-A0201OCTAMERIC TAX PEPTIDE Complex' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . PDB 1EXU . 'Crystal Structure Of The Human Mhc-Related Fc Receptor' . . . . . 99.00 99 98.99 98.99 2.72e-52 . . . . 5783 1 . . PDB 1GZP . 'Cd1b In Complex With Gm2 Ganglioside' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . PDB 1GZQ . 'Cd1b In Complex With Phophatidylinositol' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . PDB 1HLA . 'Structure Of The Human Class I Histocompatibility Antigen, Hla-A2' . . . . . 97.00 97 98.97 98.97 6.60e-51 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . PDB 1I4F . 'Crystal Structure Of Hla-A0201MAGE-A4-Peptide Complex' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . PDB 1I7R . 'Crystal Structure Of Class I Mhc A2 In Complex With Peptide P1058' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . PDB 1JGD . 'Hla-B2709 Bound To Deca-Peptide S10r' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . PDB 1JGE . 'Hla-B2705 Bound To Nona-Peptide M9' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . 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 . . . . 5783 1 . . PDB 1JNJ . 'Nmr Solution Structure Of The Human Beta2-Microglobulin' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . PDB 1K5N . 'Hla-B2709 Bound To Nona-Peptide M9' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . PDB 1KPR . 'The Human Non-Classical Major Histocompatibility Complex Molecule Hla-E' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . PDB 1KTL . 'The Human Non-Classical Major Histocompatibility Complex Molecule Hla-E' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . PDB 1LDS . 'Crystal Structure Of Monomeric Human Beta-2-Microglobulin' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . PDB 1LP9 . 'Xenoreactive Complex Ahiii 12.2 Tcr Bound To P1049HLA-A2.1' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . PDB 1M05 . 'Hla B8 In Complex With An Epstein Barr Virus Determinant' . . . . . 99.00 99 98.99 98.99 2.72e-52 . . . . 5783 1 . . PDB 1M6O . 'Crystal Structure Of Hla B4402 In Complex With Hla Dpa0201 Peptide' . . . . . 99.00 99 98.99 98.99 2.72e-52 . . . . 5783 1 . . PDB 1MHE . 'The Human Non-Classical Major Histocompatibility Complex Molecule Hla-E' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . PDB 1OGA . 'A Structural Basis For Immunodominant Human T-Cell Receptor Recognition.' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . 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 . . . . 5783 1 . . PDB 1ONQ . 'Crystal Structure Of Cd1a In Complex With A Sulfatide' . . . . . 99.00 99 98.99 98.99 2.72e-52 . . . . 5783 1 . . 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 . . . . 5783 1 . . PDB 1PY4 . 'Beta2 Microglobulin Mutant H31y Displays Hints For Amyloid Formations' . . . . . 100.00 100 98.00 99.00 1.81e-52 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . PDB 1QLF . 'Mhc Class I H-2db Complexed With Glycopeptide K3g' . . . . . 99.00 99 98.99 98.99 2.72e-52 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . PDB 1R3H . 'Crystal Structure Of T10' . . . . . 99.00 99 98.99 98.99 2.72e-52 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . PDB 1SYS . 'Crystal Structure Of Hla, B4403, And Peptide Eeptvikky' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . PDB 1SYV . 'Hla-B4405 Complexed To The Dominant Self Ligand Eefgraygf' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . PDB 1UQS . 'The Crystal Structure Of Human Cd1b With A Bound Bacterial Glycolipid' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . PDB 1W72 . 'Crystal Structure Of Hla-A1:mage-A1 In Complex With Fab-Hyb3' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . PDB 1X7Q . 'Crystal Structure Of Hla-A1101 With Sars Nucleocapsid Peptide' . . . . . 99.00 99 98.99 98.99 2.72e-52 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . PDB 1XZ0 . 'Crystal Structure Of Cd1a In Complex With A Synthetic Mycobactin Lipopeptide' . . . . . 99.00 99 98.99 98.99 2.72e-52 . . . . 5783 1 . . PDB 1YDP . '1.9a Crystal Structure Of Hla-G' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . PDB 1YPZ . 'Immune Receptor' . . . . . 99.00 102 98.99 98.99 2.59e-52 . . . . 5783 1 . . PDB 1ZHK . 'Crystal Structure Of Hla-B3501 Presenting 13-Mer Ebv Antigen Lpeplpqgqltay' . . . . . 99.00 99 98.99 98.99 2.72e-52 . . . . 5783 1 . . PDB 1ZHL . 'Crystal Structure Of Hla-B3508 Presenting 13-Mer Ebv Antigen Lpeplpqgqltay' . . . . . 99.00 99 98.99 98.99 2.72e-52 . . . . 5783 1 . . PDB 1ZS8 . 'Crystal Structure Of The Murine Mhc Class Ib Molecule M10.5' . . . . . 99.00 99 98.99 98.99 2.72e-52 . . . . 5783 1 . . PDB 1ZSD . 'Crystal Structure Of Hla-B3501 Presenting An 11-Mer Ebv Antigen Eplpqgqltay' . . . . . 99.00 99 98.99 98.99 2.72e-52 . . . . 5783 1 . . PDB 1ZT4 . 'The Crystal Structure Of Human Cd1d With And Without Alpha- Galactosylceramide' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . PDB 1ZVS . 'Crystal Structure Of The First Class Mhc Mamu And Tat-Tl8 Complex' . . . . . 99.00 99 98.99 98.99 2.72e-52 . . . . 5783 1 . . 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 . . . . 5783 1 . . PDB 2AK4 . 'Crystal Structure Of Sb27 Tcr In Complex With Hla-B3508- 13mer Peptide' . . . . . 99.00 99 98.99 98.99 2.72e-52 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . PDB 2BCK . 'Crystal Structure Of Hla-A2402 Complexed With A Telomerase Peptide' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . PDB 2BNQ . 'Structural And Kinetic Basis For Heightened Immunogenicity Of T Cell Vaccines' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . PDB 2BNR . 'Structural And Kinetic Basis For Heightened Immunogenicity Of T Cell Vaccines' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . PDB 2D31 . 'Crystal Structure Of Disulfide-Linked Hla-G Dimer' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . PDB 2D4F . 'The Crystal Structure Of Human Beta2-Microglobulin' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . PDB 2DYP . 'Crystal Structure Of Lilrb2(Lir2ILT4CD85D) COMPLEXED WITH Hla-G' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . PDB 2ESV . 'Structure Of The Hla-E-VmaprtlilKK50.4 TCR COMPLEX' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . PDB 2F8O . 'A Native To Amyloidogenic Transition Regulated By A Backbone Trigger' . . . . . 100.00 100 98.00 98.00 2.09e-52 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . PDB 2H26 . 'Human Cd1b In Complex With Endogenous Phosphatidylcholine And Spacer' . . . . . 99.00 99 98.99 98.99 2.72e-52 . . . . 5783 1 . . 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 . . . . 5783 1 . . PDB 2HJK . 'Crystal Structure Of Hla-B5703 And Hiv-1 Peptide' . . . . . 99.00 99 98.99 98.99 2.72e-52 . . . . 5783 1 . . PDB 2HJL . 'Crystal Structure Of Hla-B5703 And Hiv-1 Peptide' . . . . . 99.00 99 98.99 98.99 2.72e-52 . . . . 5783 1 . . PDB 2HLA . 'Specificity Pockets For The Side Chains Of Peptide Antigens In Hla-Aw68' . . . . . 99.00 99 98.99 98.99 2.72e-52 . . . . 5783 1 . . PDB 2HN7 . 'Hla-A1101 In Complex With Hbv Peptide Homologue' . . . . . 99.00 99 98.99 98.99 2.72e-52 . . . . 5783 1 . . PDB 2J8U . 'Large Cdr3a Loop Alteration As A Function Of Mhc Mutation.' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . PDB 2JCC . 'Ah3 Recognition Of Mutant Hla-A2 W167a' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . PDB 2NW3 . 'Crystal Structure Of Hla-B3508 Presenting Ebv Peptide Eplpqgqltay At 1.7a' . . . . . 99.00 99 98.99 98.99 2.72e-52 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . PDB 2RFX . 'Crystal Structure Of Hla-B5701, Presenting The Self Peptide, Lsspvtksf' . . . . . 99.00 99 98.99 98.99 2.72e-52 . . . . 5783 1 . . PDB 2UWE . 'Large Cdr3a Loop Alteration As A Function Of Mhc Mutation' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . PDB 2V2W . 'T Cell Cross-Reactivity And Conformational Changes During Tcr Engagement' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . PDB 2V2X . 'T Cell Cross-Reactivity And Conformational Changes During Tcr Engagement.' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . PDB 2VB5 . 'Solution Structure Of W60g Mutant Of Human Beta2- Microglobulin' . . . . . 100.00 100 98.00 98.00 5.49e-52 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . PDB 2YXF . 'The High Resolution Crystal Structure Of Beta2- Microglobulin Under Physiological Conditions' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . PDB 2Z9T . 'Crystal Structure Of The Human Beta-2 Microglobulin Mutant W60g' . . . . . 100.00 100 98.00 98.00 5.49e-52 . . . . 5783 1 . . PDB 3B3I . 'Citrullination-Dependent Differential Presentation Of A Self-Peptide By Hla-B27 Subtypes' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . 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 . . . . 5783 1 . . PDB 3BZE . 'The Human Non-Classical Major Histocompatibility Complex Molecule Hla-E' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . PDB 3BZF . 'The Human Non-Classical Major Histocompatibility Complex Molecule Hla-E' . . . . . 96.00 97 100.00 100.00 3.19e-51 . . . . 5783 1 . . 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 . . . . 5783 1 . . PDB 3CDG . 'Human Cd94NKG2A IN COMPLEX WITH HLA-E' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . PDB 3CII . 'Structure Of Nkg2aCD94 BOUND TO HLA-E' . . . . . 100.00 100 99.00 99.00 3.90e-53 . . . . 5783 1 . . 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 . . . . 5783 1 . . PDB 3HLA . 'Specificity Pockets For The Side Chains Of Peptide Antigens In Hla-Aw68' . . . . . 99.00 99 98.99 98.99 2.72e-52 . . . . 5783 1 . . DBJ BAA35182 . 'beta 2-microglobulin [Homo sapiens]' . . . . . 99.00 119 98.99 98.99 3.47e-53 . . . . 5783 1 . . DBJ BAG38125 . 'unnamed protein product [Homo sapiens]' . . . . . 99.00 119 98.99 98.99 3.47e-53 . . . . 5783 1 . . EMBL CAA23830 . 'beta-2 microglobulin [Homo sapiens]' . . . . . 99.00 110 98.99 98.99 9.36e-53 . . . . 5783 1 . . EMBL CAH92078 . 'hypothetical protein [Pongo abelii]' . . . . . 99.00 119 98.99 98.99 3.47e-53 . . . . 5783 1 . . GenBank AAA87972 . beta-2-microglobulin . . . . . 99.00 119 98.99 98.99 3.47e-53 . . . . 5783 1 . . GenBank AAA88008 . beta-2-microglobulin . . . . . 99.00 119 98.99 98.99 3.47e-53 . . . . 5783 1 . . GenBank AAB25312 . 'beta 2-microglobulin [Homo sapiens]' . . . . . 75.00 101 98.67 98.67 8.65e-38 . . . . 5783 1 . . 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 . . . . 5783 1 . . GenBank AAD48083 . 'beta-2 microglobulin [Homo sapiens]' . . . . . 99.00 119 98.99 98.99 3.47e-53 . . . . 5783 1 . . REF NP_001009066 . 'beta-2-microglobulin [Pan troglodytes]' . . . . . 99.00 119 98.99 98.99 3.47e-53 . . . . 5783 1 . . REF NP_004039 . 'beta-2-microglobulin precursor [Homo sapiens]' . . . . . 99.00 119 98.99 98.99 3.47e-53 . . . . 5783 1 . . SWISS-PROT P16213 . 'Beta-2-microglobulin precursor' . . . . . 99.00 119 98.99 98.99 3.47e-53 . . . . 5783 1 . . 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 . . . . 5783 1 . . SWISS-PROT P61770 . 'Beta-2-microglobulin precursor' . . . . . 99.00 119 98.99 98.99 3.47e-53 . . . . 5783 1 . . SWISS-PROT P61771 . 'Beta-2-microglobulin precursor' . . . . . 99.00 119 98.99 98.99 3.47e-53 . . . . 5783 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID R3Abeta2-m abbreviation 5783 1 R3Abeta2-microglobulin variant 5783 1 beta2-microglobulin common 5783 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 . MET . 5783 1 2 . ILE . 5783 1 3 . GLN . 5783 1 4 . ALA . 5783 1 5 . THR . 5783 1 6 . PRO . 5783 1 7 . LYS . 5783 1 8 . ILE . 5783 1 9 . GLN . 5783 1 10 . VAL . 5783 1 11 . TYR . 5783 1 12 . SER . 5783 1 13 . ARG . 5783 1 14 . HIS . 5783 1 15 . PRO . 5783 1 16 . ALA . 5783 1 17 . GLU . 5783 1 18 . ASN . 5783 1 19 . GLY . 5783 1 20 . LYS . 5783 1 21 . SER . 5783 1 22 . ASN . 5783 1 23 . PHE . 5783 1 24 . LEU . 5783 1 25 . ASN . 5783 1 26 . CYS . 5783 1 27 . TYR . 5783 1 28 . VAL . 5783 1 29 . SER . 5783 1 30 . GLY . 5783 1 31 . PHE . 5783 1 32 . HIS . 5783 1 33 . PRO . 5783 1 34 . SER . 5783 1 35 . ASP . 5783 1 36 . ILE . 5783 1 37 . GLU . 5783 1 38 . VAL . 5783 1 39 . ASP . 5783 1 40 . LEU . 5783 1 41 . LEU . 5783 1 42 . LYS . 5783 1 43 . ASN . 5783 1 44 . GLY . 5783 1 45 . GLU . 5783 1 46 . ARG . 5783 1 47 . ILE . 5783 1 48 . GLU . 5783 1 49 . LYS . 5783 1 50 . VAL . 5783 1 51 . GLU . 5783 1 52 . HIS . 5783 1 53 . SER . 5783 1 54 . ASP . 5783 1 55 . LEU . 5783 1 56 . SER . 5783 1 57 . PHE . 5783 1 58 . SER . 5783 1 59 . LYS . 5783 1 60 . ASP . 5783 1 61 . TRP . 5783 1 62 . SER . 5783 1 63 . PHE . 5783 1 64 . TYR . 5783 1 65 . LEU . 5783 1 66 . LEU . 5783 1 67 . TYR . 5783 1 68 . TYR . 5783 1 69 . THR . 5783 1 70 . GLU . 5783 1 71 . PHE . 5783 1 72 . THR . 5783 1 73 . PRO . 5783 1 74 . THR . 5783 1 75 . GLU . 5783 1 76 . LYS . 5783 1 77 . ASP . 5783 1 78 . GLU . 5783 1 79 . TYR . 5783 1 80 . ALA . 5783 1 81 . CYS . 5783 1 82 . ARG . 5783 1 83 . VAL . 5783 1 84 . ASN . 5783 1 85 . HIS . 5783 1 86 . VAL . 5783 1 87 . THR . 5783 1 88 . LEU . 5783 1 89 . SER . 5783 1 90 . GLN . 5783 1 91 . PRO . 5783 1 92 . LYS . 5783 1 93 . ILE . 5783 1 94 . VAL . 5783 1 95 . LYS . 5783 1 96 . TRP . 5783 1 97 . ASP . 5783 1 98 . ARG . 5783 1 99 . ASP . 5783 1 100 . MET . 5783 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 . MET 1 1 5783 1 . ILE 2 2 5783 1 . GLN 3 3 5783 1 . ALA 4 4 5783 1 . THR 5 5 5783 1 . PRO 6 6 5783 1 . LYS 7 7 5783 1 . ILE 8 8 5783 1 . GLN 9 9 5783 1 . VAL 10 10 5783 1 . TYR 11 11 5783 1 . SER 12 12 5783 1 . ARG 13 13 5783 1 . HIS 14 14 5783 1 . PRO 15 15 5783 1 . ALA 16 16 5783 1 . GLU 17 17 5783 1 . ASN 18 18 5783 1 . GLY 19 19 5783 1 . LYS 20 20 5783 1 . SER 21 21 5783 1 . ASN 22 22 5783 1 . PHE 23 23 5783 1 . LEU 24 24 5783 1 . ASN 25 25 5783 1 . CYS 26 26 5783 1 . TYR 27 27 5783 1 . VAL 28 28 5783 1 . SER 29 29 5783 1 . GLY 30 30 5783 1 . PHE 31 31 5783 1 . HIS 32 32 5783 1 . PRO 33 33 5783 1 . SER 34 34 5783 1 . ASP 35 35 5783 1 . ILE 36 36 5783 1 . GLU 37 37 5783 1 . VAL 38 38 5783 1 . ASP 39 39 5783 1 . LEU 40 40 5783 1 . LEU 41 41 5783 1 . LYS 42 42 5783 1 . ASN 43 43 5783 1 . GLY 44 44 5783 1 . GLU 45 45 5783 1 . ARG 46 46 5783 1 . ILE 47 47 5783 1 . GLU 48 48 5783 1 . LYS 49 49 5783 1 . VAL 50 50 5783 1 . GLU 51 51 5783 1 . HIS 52 52 5783 1 . SER 53 53 5783 1 . ASP 54 54 5783 1 . LEU 55 55 5783 1 . SER 56 56 5783 1 . PHE 57 57 5783 1 . SER 58 58 5783 1 . LYS 59 59 5783 1 . ASP 60 60 5783 1 . TRP 61 61 5783 1 . SER 62 62 5783 1 . PHE 63 63 5783 1 . TYR 64 64 5783 1 . LEU 65 65 5783 1 . LEU 66 66 5783 1 . TYR 67 67 5783 1 . TYR 68 68 5783 1 . THR 69 69 5783 1 . GLU 70 70 5783 1 . PHE 71 71 5783 1 . THR 72 72 5783 1 . PRO 73 73 5783 1 . THR 74 74 5783 1 . GLU 75 75 5783 1 . LYS 76 76 5783 1 . ASP 77 77 5783 1 . GLU 78 78 5783 1 . TYR 79 79 5783 1 . ALA 80 80 5783 1 . CYS 81 81 5783 1 . ARG 82 82 5783 1 . VAL 83 83 5783 1 . ASN 84 84 5783 1 . HIS 85 85 5783 1 . VAL 86 86 5783 1 . THR 87 87 5783 1 . LEU 88 88 5783 1 . SER 89 89 5783 1 . GLN 90 90 5783 1 . PRO 91 91 5783 1 . LYS 92 92 5783 1 . ILE 93 93 5783 1 . VAL 94 94 5783 1 . LYS 95 95 5783 1 . TRP 96 96 5783 1 . ASP 97 97 5783 1 . ARG 98 98 5783 1 . ASP 99 99 5783 1 . MET 100 100 5783 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 5783 _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.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.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Details _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $R3Abeta2-m . 9606 . . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . 5783 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 5783 _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_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.Details _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $R3Abeta2-m . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli . . . . . . . . . . 5783 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5783 _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 beta2-microglobulin . . . 1 $R3Abeta2-m . . 0.7 . . mM . . . . 5783 1 2 'sodium phosphate' . . . . . . . 70 . . mM . . . . 5783 1 3 'sodium chloride' . . . . . . . 100 . . mM . . . . 5783 1 4 H2O . . . . . . . 100 . . % . . . . 5783 1 stop_ save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode Ex-cond_1 _Sample_condition_list.Entry_ID 5783 _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 pH 6.5 0.1 na 5783 1 temperature 310 0.1 K 5783 1 stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Software.Sf_category software _Software.Sf_framecode FELIX _Software.Entry_ID 5783 _Software.ID 1 _Software.Type . _Software.Name FELIX _Software.Version 2000 _Software.DOI . _Software.Details . 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 5783 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _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 5783 _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 Avance . 500 . . . 5783 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 5783 _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 '1H-1H TOCSY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5783 1 2 '1H-1H NOESY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5783 1 stop_ 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 5783 _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.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H 1 Dioxane 'methylene protons' . . . . ppm 3.53 internal direct 1.0 . . . . . 5783 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_shift_set_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode shift_set_1 _Assigned_chem_shift_list.Entry_ID 5783 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $Ex-cond_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 . _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 '1H-1H TOCSY' 1 $sample_1 . 5783 1 2 '1H-1H NOESY' 1 $sample_1 . 5783 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.Ambiguity_set_ID _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 2 2 ILE HA H 1 4.231 0.02 . 1 . . . . . . . . . 5783 1 2 . 1 1 2 2 ILE HB H 1 1.752 0.02 . 1 . . . . . . . . . 5783 1 3 . 1 1 2 2 ILE HG12 H 1 1.125 0.02 . 2 . . . . . . . . . 5783 1 4 . 1 1 2 2 ILE HG13 H 1 1.417 0.02 . 2 . . . . . . . . . 5783 1 5 . 1 1 2 2 ILE HG21 H 1 0.838 0.02 . 1 . . . . . . . . . 5783 1 6 . 1 1 2 2 ILE HG22 H 1 0.838 0.02 . 1 . . . . . . . . . 5783 1 7 . 1 1 2 2 ILE HG23 H 1 0.838 0.02 . 1 . . . . . . . . . 5783 1 8 . 1 1 3 3 GLN H H 1 8.276 0.02 . 1 . . . . . . . . . 5783 1 9 . 1 1 3 3 GLN HA H 1 4.583 0.02 . 1 . . . . . . . . . 5783 1 10 . 1 1 3 3 GLN HB2 H 1 2.058 0.02 . 2 . . . . . . . . . 5783 1 11 . 1 1 3 3 GLN HB3 H 1 2.136 0.02 . 2 . . . . . . . . . 5783 1 12 . 1 1 3 3 GLN HG2 H 1 2.471 0.02 . 2 . . . . . . . . . 5783 1 13 . 1 1 3 3 GLN HG3 H 1 2.595 0.02 . 2 . . . . . . . . . 5783 1 14 . 1 1 3 3 GLN HE21 H 1 6.735 0.02 . 2 . . . . . . . . . 5783 1 15 . 1 1 3 3 GLN HE22 H 1 7.431 0.02 . 2 . . . . . . . . . 5783 1 16 . 1 1 4 4 ALA H H 1 9.243 0.02 . 1 . . . . . . . . . 5783 1 17 . 1 1 4 4 ALA HA H 1 4.837 0.02 . 1 . . . . . . . . . 5783 1 18 . 1 1 4 4 ALA HB1 H 1 1.569 0.02 . 1 . . . . . . . . . 5783 1 19 . 1 1 4 4 ALA HB2 H 1 1.569 0.02 . 1 . . . . . . . . . 5783 1 20 . 1 1 4 4 ALA HB3 H 1 1.569 0.02 . 1 . . . . . . . . . 5783 1 21 . 1 1 5 5 THR H H 1 8.176 0.02 . 1 . . . . . . . . . 5783 1 22 . 1 1 5 5 THR HA H 1 4.992 0.02 . 1 . . . . . . . . . 5783 1 23 . 1 1 5 5 THR HB H 1 4.096 0.02 . 1 . . . . . . . . . 5783 1 24 . 1 1 5 5 THR HG21 H 1 1.313 0.02 . 1 . . . . . . . . . 5783 1 25 . 1 1 5 5 THR HG22 H 1 1.313 0.02 . 1 . . . . . . . . . 5783 1 26 . 1 1 5 5 THR HG23 H 1 1.313 0.02 . 1 . . . . . . . . . 5783 1 27 . 1 1 6 6 PRO HA H 1 4.395 0.02 . 1 . . . . . . . . . 5783 1 28 . 1 1 6 6 PRO HB2 H 1 1.539 0.02 . 2 . . . . . . . . . 5783 1 29 . 1 1 6 6 PRO HB3 H 1 1.679 0.02 . 2 . . . . . . . . . 5783 1 30 . 1 1 6 6 PRO HG2 H 1 1.150 0.02 . 1 . . . . . . . . . 5783 1 31 . 1 1 6 6 PRO HD2 H 1 3.164 0.02 . 2 . . . . . . . . . 5783 1 32 . 1 1 6 6 PRO HD3 H 1 3.611 0.02 . 2 . . . . . . . . . 5783 1 33 . 1 1 7 7 LYS H H 1 9.242 0.02 . 1 . . . . . . . . . 5783 1 34 . 1 1 7 7 LYS HA H 1 4.507 0.02 . 1 . . . . . . . . . 5783 1 35 . 1 1 7 7 LYS HB2 H 1 1.494 0.02 . 2 . . . . . . . . . 5783 1 36 . 1 1 7 7 LYS HB3 H 1 1.782 0.02 . 2 . . . . . . . . . 5783 1 37 . 1 1 8 8 ILE H H 1 8.398 0.02 . 1 . . . . . . . . . 5783 1 38 . 1 1 8 8 ILE HA H 1 4.798 0.02 . 1 . . . . . . . . . 5783 1 39 . 1 1 8 8 ILE HB H 1 1.641 0.02 . 1 . . . . . . . . . 5783 1 40 . 1 1 8 8 ILE HG21 H 1 0.779 0.02 . 1 . . . . . . . . . 5783 1 41 . 1 1 8 8 ILE HG22 H 1 0.779 0.02 . 1 . . . . . . . . . 5783 1 42 . 1 1 8 8 ILE HG23 H 1 0.779 0.02 . 1 . . . . . . . . . 5783 1 43 . 1 1 9 9 GLN H H 1 9.110 0.02 . 1 . . . . . . . . . 5783 1 44 . 1 1 9 9 GLN HA H 1 4.921 0.02 . 1 . . . . . . . . . 5783 1 45 . 1 1 9 9 GLN HB2 H 1 2.192 0.02 . 2 . . . . . . . . . 5783 1 46 . 1 1 9 9 GLN HB3 H 1 2.333 0.02 . 2 . . . . . . . . . 5783 1 47 . 1 1 9 9 GLN HG2 H 1 2.418 0.02 . 1 . . . . . . . . . 5783 1 48 . 1 1 10 10 VAL H H 1 9.022 0.02 . 1 . . . . . . . . . 5783 1 49 . 1 1 10 10 VAL HA H 1 5.339 0.02 . 1 . . . . . . . . . 5783 1 50 . 1 1 10 10 VAL HB H 1 2.032 0.02 . 1 . . . . . . . . . 5783 1 51 . 1 1 10 10 VAL HG11 H 1 0.916 0.02 . 2 . . . . . . . . . 5783 1 52 . 1 1 10 10 VAL HG12 H 1 0.916 0.02 . 2 . . . . . . . . . 5783 1 53 . 1 1 10 10 VAL HG13 H 1 0.916 0.02 . 2 . . . . . . . . . 5783 1 54 . 1 1 10 10 VAL HG21 H 1 0.975 0.02 . 2 . . . . . . . . . 5783 1 55 . 1 1 10 10 VAL HG22 H 1 0.975 0.02 . 2 . . . . . . . . . 5783 1 56 . 1 1 10 10 VAL HG23 H 1 0.975 0.02 . 2 . . . . . . . . . 5783 1 57 . 1 1 11 11 TYR H H 1 8.469 0.02 . 1 . . . . . . . . . 5783 1 58 . 1 1 11 11 TYR HA H 1 5.316 0.02 . 1 . . . . . . . . . 5783 1 59 . 1 1 11 11 TYR HB2 H 1 3.166 0.02 . 2 . . . . . . . . . 5783 1 60 . 1 1 11 11 TYR HB3 H 1 3.397 0.02 . 2 . . . . . . . . . 5783 1 61 . 1 1 11 11 TYR HD1 H 1 6.811 0.02 . 1 . . . . . . . . . 5783 1 62 . 1 1 11 11 TYR HE1 H 1 6.555 0.02 . 1 . . . . . . . . . 5783 1 63 . 1 1 12 12 SER H H 1 9.332 0.02 . 1 . . . . . . . . . 5783 1 64 . 1 1 12 12 SER HA H 1 5.310 0.02 . 1 . . . . . . . . . 5783 1 65 . 1 1 12 12 SER HB2 H 1 3.391 0.02 . 2 . . . . . . . . . 5783 1 66 . 1 1 12 12 SER HB3 H 1 4.647 0.02 . 2 . . . . . . . . . 5783 1 67 . 1 1 13 13 ARG H H 1 8.858 0.02 . 1 . . . . . . . . . 5783 1 68 . 1 1 13 13 ARG HA H 1 3.924 0.02 . 1 . . . . . . . . . 5783 1 69 . 1 1 13 13 ARG HB2 H 1 1.743 0.02 . 2 . . . . . . . . . 5783 1 70 . 1 1 13 13 ARG HB3 H 1 1.943 0.02 . 2 . . . . . . . . . 5783 1 71 . 1 1 13 13 ARG HG2 H 1 1.416 0.02 . 1 . . . . . . . . . 5783 1 72 . 1 1 14 14 HIS H H 1 8.314 0.02 . 1 . . . . . . . . . 5783 1 73 . 1 1 14 14 HIS HA H 1 5.341 0.02 . 1 . . . . . . . . . 5783 1 74 . 1 1 14 14 HIS HB2 H 1 2.909 0.02 . 2 . . . . . . . . . 5783 1 75 . 1 1 14 14 HIS HB3 H 1 3.251 0.02 . 2 . . . . . . . . . 5783 1 76 . 1 1 14 14 HIS HD2 H 1 7.069 0.02 . 1 . . . . . . . . . 5783 1 77 . 1 1 14 14 HIS HE1 H 1 7.848 0.02 . 1 . . . . . . . . . 5783 1 78 . 1 1 15 15 PRO HA H 1 4.524 0.02 . 1 . . . . . . . . . 5783 1 79 . 1 1 15 15 PRO HB2 H 1 1.960 0.02 . 2 . . . . . . . . . 5783 1 80 . 1 1 15 15 PRO HB3 H 1 2.426 0.02 . 2 . . . . . . . . . 5783 1 81 . 1 1 15 15 PRO HG2 H 1 2.081 0.02 . 2 . . . . . . . . . 5783 1 82 . 1 1 15 15 PRO HG3 H 1 2.227 0.02 . 2 . . . . . . . . . 5783 1 83 . 1 1 15 15 PRO HD2 H 1 3.799 0.02 . 2 . . . . . . . . . 5783 1 84 . 1 1 15 15 PRO HD3 H 1 4.067 0.02 . 2 . . . . . . . . . 5783 1 85 . 1 1 16 16 ALA H H 1 9.006 0.02 . 1 . . . . . . . . . 5783 1 86 . 1 1 16 16 ALA HA H 1 4.108 0.02 . 1 . . . . . . . . . 5783 1 87 . 1 1 16 16 ALA HB1 H 1 1.687 0.02 . 1 . . . . . . . . . 5783 1 88 . 1 1 16 16 ALA HB2 H 1 1.687 0.02 . 1 . . . . . . . . . 5783 1 89 . 1 1 16 16 ALA HB3 H 1 1.687 0.02 . 1 . . . . . . . . . 5783 1 90 . 1 1 17 17 GLU H H 1 8.871 0.02 . 1 . . . . . . . . . 5783 1 91 . 1 1 17 17 GLU HA H 1 4.402 0.02 . 1 . . . . . . . . . 5783 1 92 . 1 1 17 17 GLU HB2 H 1 1.860 0.02 . 2 . . . . . . . . . 5783 1 93 . 1 1 17 17 GLU HB3 H 1 2.169 0.02 . 2 . . . . . . . . . 5783 1 94 . 1 1 19 19 GLY H H 1 8.818 0.02 . 1 . . . . . . . . . 5783 1 95 . 1 1 19 19 GLY HA2 H 1 3.527 0.02 . 2 . . . . . . . . . 5783 1 96 . 1 1 19 19 GLY HA3 H 1 4.185 0.02 . 2 . . . . . . . . . 5783 1 97 . 1 1 20 20 LYS H H 1 7.846 0.02 . 1 . . . . . . . . . 5783 1 98 . 1 1 20 20 LYS HA H 1 4.674 0.02 . 1 . . . . . . . . . 5783 1 99 . 1 1 20 20 LYS HB2 H 1 1.752 0.02 . 2 . . . . . . . . . 5783 1 100 . 1 1 20 20 LYS HB3 H 1 1.823 0.02 . 2 . . . . . . . . . 5783 1 101 . 1 1 20 20 LYS HG2 H 1 1.291 0.02 . 2 . . . . . . . . . 5783 1 102 . 1 1 20 20 LYS HG3 H 1 1.339 0.02 . 2 . . . . . . . . . 5783 1 103 . 1 1 20 20 LYS HD2 H 1 1.644 0.02 . 1 . . . . . . . . . 5783 1 104 . 1 1 21 21 SER H H 1 8.356 0.02 . 1 . . . . . . . . . 5783 1 105 . 1 1 21 21 SER HA H 1 4.245 0.02 . 1 . . . . . . . . . 5783 1 106 . 1 1 21 21 SER HB2 H 1 3.738 0.02 . 1 . . . . . . . . . 5783 1 107 . 1 1 22 22 ASN H H 1 8.898 0.02 . 1 . . . . . . . . . 5783 1 108 . 1 1 22 22 ASN HA H 1 4.875 0.02 . 1 . . . . . . . . . 5783 1 109 . 1 1 22 22 ASN HB2 H 1 2.557 0.02 . 2 . . . . . . . . . 5783 1 110 . 1 1 22 22 ASN HB3 H 1 2.748 0.02 . 2 . . . . . . . . . 5783 1 111 . 1 1 22 22 ASN HD21 H 1 7.753 0.02 . 2 . . . . . . . . . 5783 1 112 . 1 1 22 22 ASN HD22 H 1 7.436 0.02 . 2 . . . . . . . . . 5783 1 113 . 1 1 23 23 PHE H H 1 10.341 0.02 . 1 . . . . . . . . . 5783 1 114 . 1 1 23 23 PHE HA H 1 5.435 0.02 . 1 . . . . . . . . . 5783 1 115 . 1 1 23 23 PHE HB2 H 1 2.633 0.02 . 2 . . . . . . . . . 5783 1 116 . 1 1 23 23 PHE HB3 H 1 2.684 0.02 . 2 . . . . . . . . . 5783 1 117 . 1 1 23 23 PHE HD1 H 1 6.995 0.02 . 1 . . . . . . . . . 5783 1 118 . 1 1 23 23 PHE HE1 H 1 7.401 0.02 . 1 . . . . . . . . . 5783 1 119 . 1 1 23 23 PHE HZ H 1 7.348 0.02 . 1 . . . . . . . . . 5783 1 120 . 1 1 24 24 LEU H H 1 8.975 0.02 . 1 . . . . . . . . . 5783 1 121 . 1 1 24 24 LEU HA H 1 3.688 0.02 . 1 . . . . . . . . . 5783 1 122 . 1 1 24 24 LEU HB2 H 1 -0.800 0.02 . 2 . . . . . . . . . 5783 1 123 . 1 1 24 24 LEU HB3 H 1 0.824 0.02 . 2 . . . . . . . . . 5783 1 124 . 1 1 24 24 LEU HG H 1 0.660 0.02 . 1 . . . . . . . . . 5783 1 125 . 1 1 24 24 LEU HD11 H 1 -0.564 0.02 . 2 . . . . . . . . . 5783 1 126 . 1 1 24 24 LEU HD12 H 1 -0.564 0.02 . 2 . . . . . . . . . 5783 1 127 . 1 1 24 24 LEU HD13 H 1 -0.564 0.02 . 2 . . . . . . . . . 5783 1 128 . 1 1 24 24 LEU HD21 H 1 0.012 0.02 . 2 . . . . . . . . . 5783 1 129 . 1 1 24 24 LEU HD22 H 1 0.012 0.02 . 2 . . . . . . . . . 5783 1 130 . 1 1 24 24 LEU HD23 H 1 0.012 0.02 . 2 . . . . . . . . . 5783 1 131 . 1 1 25 25 ASN H H 1 8.197 0.02 . 1 . . . . . . . . . 5783 1 132 . 1 1 25 25 ASN HA H 1 5.380 0.02 . 1 . . . . . . . . . 5783 1 133 . 1 1 25 25 ASN HB2 H 1 1.450 0.02 . 2 . . . . . . . . . 5783 1 134 . 1 1 25 25 ASN HB3 H 1 1.842 0.02 . 2 . . . . . . . . . 5783 1 135 . 1 1 25 25 ASN HD21 H 1 5.547 0.02 . 2 . . . . . . . . . 5783 1 136 . 1 1 25 25 ASN HD22 H 1 5.743 0.02 . 2 . . . . . . . . . 5783 1 137 . 1 1 26 26 CYS H H 1 9.611 0.02 . 1 . . . . . . . . . 5783 1 138 . 1 1 26 26 CYS HA H 1 5.149 0.02 . 1 . . . . . . . . . 5783 1 139 . 1 1 26 26 CYS HB2 H 1 2.539 0.02 . 2 . . . . . . . . . 5783 1 140 . 1 1 26 26 CYS HB3 H 1 3.276 0.02 . 2 . . . . . . . . . 5783 1 141 . 1 1 27 27 TYR H H 1 9.643 0.02 . 1 . . . . . . . . . 5783 1 142 . 1 1 27 27 TYR HA H 1 5.414 0.02 . 1 . . . . . . . . . 5783 1 143 . 1 1 27 27 TYR HB2 H 1 3.172 0.02 . 1 . . . . . . . . . 5783 1 144 . 1 1 27 27 TYR HD1 H 1 7.156 0.02 . 1 . . . . . . . . . 5783 1 145 . 1 1 27 27 TYR HE1 H 1 6.569 0.02 . 1 . . . . . . . . . 5783 1 146 . 1 1 28 28 VAL H H 1 8.794 0.02 . 1 . . . . . . . . . 5783 1 147 . 1 1 28 28 VAL HA H 1 5.198 0.02 . 1 . . . . . . . . . 5783 1 148 . 1 1 28 28 VAL HB H 1 1.901 0.02 . 1 . . . . . . . . . 5783 1 149 . 1 1 28 28 VAL HG11 H 1 0.765 0.02 . 2 . . . . . . . . . 5783 1 150 . 1 1 28 28 VAL HG12 H 1 0.765 0.02 . 2 . . . . . . . . . 5783 1 151 . 1 1 28 28 VAL HG13 H 1 0.765 0.02 . 2 . . . . . . . . . 5783 1 152 . 1 1 28 28 VAL HG21 H 1 0.896 0.02 . 2 . . . . . . . . . 5783 1 153 . 1 1 28 28 VAL HG22 H 1 0.896 0.02 . 2 . . . . . . . . . 5783 1 154 . 1 1 28 28 VAL HG23 H 1 0.896 0.02 . 2 . . . . . . . . . 5783 1 155 . 1 1 29 29 SER H H 1 8.964 0.02 . 1 . . . . . . . . . 5783 1 156 . 1 1 29 29 SER HA H 1 5.730 0.02 . 1 . . . . . . . . . 5783 1 157 . 1 1 29 29 SER HB2 H 1 3.447 0.02 . 2 . . . . . . . . . 5783 1 158 . 1 1 29 29 SER HB3 H 1 3.858 0.02 . 2 . . . . . . . . . 5783 1 159 . 1 1 30 30 GLY H H 1 8.327 0.02 . 1 . . . . . . . . . 5783 1 160 . 1 1 30 30 GLY HA2 H 1 3.852 0.02 . 2 . . . . . . . . . 5783 1 161 . 1 1 30 30 GLY HA3 H 1 4.106 0.02 . 2 . . . . . . . . . 5783 1 162 . 1 1 31 31 PHE H H 1 7.081 0.02 . 1 . . . . . . . . . 5783 1 163 . 1 1 31 31 PHE HA H 1 4.845 0.02 . 1 . . . . . . . . . 5783 1 164 . 1 1 31 31 PHE HB2 H 1 1.978 0.02 . 2 . . . . . . . . . 5783 1 165 . 1 1 31 31 PHE HB3 H 1 2.332 0.02 . 2 . . . . . . . . . 5783 1 166 . 1 1 31 31 PHE HD1 H 1 7.004 0.02 . 1 . . . . . . . . . 5783 1 167 . 1 1 31 31 PHE HE1 H 1 7.262 0.02 . 1 . . . . . . . . . 5783 1 168 . 1 1 31 31 PHE HZ H 1 6.982 0.02 . 1 . . . . . . . . . 5783 1 169 . 1 1 32 32 HIS H H 1 8.537 0.02 . 1 . . . . . . . . . 5783 1 170 . 1 1 32 32 HIS HA H 1 4.524 0.02 . 1 . . . . . . . . . 5783 1 171 . 1 1 32 32 HIS HB2 H 1 3.155 0.02 . 2 . . . . . . . . . 5783 1 172 . 1 1 32 32 HIS HB3 H 1 3.269 0.02 . 2 . . . . . . . . . 5783 1 173 . 1 1 32 32 HIS HD2 H 1 7.072 0.02 . 1 . . . . . . . . . 5783 1 174 . 1 1 32 32 HIS HE1 H 1 7.848 0.02 . 1 . . . . . . . . . 5783 1 175 . 1 1 33 33 PRO HA H 1 3.984 0.02 . 1 . . . . . . . . . 5783 1 176 . 1 1 33 33 PRO HB2 H 1 2.384 0.02 . 1 . . . . . . . . . 5783 1 177 . 1 1 33 33 PRO HG2 H 1 1.676 0.02 . 2 . . . . . . . . . 5783 1 178 . 1 1 33 33 PRO HG3 H 1 1.988 0.02 . 2 . . . . . . . . . 5783 1 179 . 1 1 33 33 PRO HD2 H 1 3.618 0.02 . 2 . . . . . . . . . 5783 1 180 . 1 1 33 33 PRO HD3 H 1 3.892 0.02 . 2 . . . . . . . . . 5783 1 181 . 1 1 34 34 SER H H 1 8.341 0.02 . 1 . . . . . . . . . 5783 1 182 . 1 1 34 34 SER HA H 1 3.634 0.02 . 1 . . . . . . . . . 5783 1 183 . 1 1 34 34 SER HB2 H 1 3.256 0.02 . 1 . . . . . . . . . 5783 1 184 . 1 1 35 35 ASP H H 1 7.164 0.02 . 1 . . . . . . . . . 5783 1 185 . 1 1 35 35 ASP HA H 1 4.410 0.02 . 1 . . . . . . . . . 5783 1 186 . 1 1 35 35 ASP HB2 H 1 2.342 0.02 . 2 . . . . . . . . . 5783 1 187 . 1 1 35 35 ASP HB3 H 1 2.398 0.02 . 2 . . . . . . . . . 5783 1 188 . 1 1 36 36 ILE H H 1 7.960 0.02 . 1 . . . . . . . . . 5783 1 189 . 1 1 36 36 ILE HA H 1 4.553 0.02 . 1 . . . . . . . . . 5783 1 190 . 1 1 36 36 ILE HB H 1 1.376 0.02 . 1 . . . . . . . . . 5783 1 191 . 1 1 36 36 ILE HG12 H 1 0.674 0.02 . 2 . . . . . . . . . 5783 1 192 . 1 1 36 36 ILE HG13 H 1 1.490 0.02 . 2 . . . . . . . . . 5783 1 193 . 1 1 36 36 ILE HG21 H 1 0.555 0.02 . 1 . . . . . . . . . 5783 1 194 . 1 1 36 36 ILE HG22 H 1 0.555 0.02 . 1 . . . . . . . . . 5783 1 195 . 1 1 36 36 ILE HG23 H 1 0.555 0.02 . 1 . . . . . . . . . 5783 1 196 . 1 1 36 36 ILE HD11 H 1 -0.492 0.02 . 1 . . . . . . . . . 5783 1 197 . 1 1 36 36 ILE HD12 H 1 -0.492 0.02 . 1 . . . . . . . . . 5783 1 198 . 1 1 36 36 ILE HD13 H 1 -0.492 0.02 . 1 . . . . . . . . . 5783 1 199 . 1 1 37 37 GLU H H 1 7.985 0.02 . 1 . . . . . . . . . 5783 1 200 . 1 1 37 37 GLU HA H 1 4.578 0.02 . 1 . . . . . . . . . 5783 1 201 . 1 1 37 37 GLU HB2 H 1 1.761 0.02 . 2 . . . . . . . . . 5783 1 202 . 1 1 37 37 GLU HB3 H 1 1.932 0.02 . 2 . . . . . . . . . 5783 1 203 . 1 1 37 37 GLU HG2 H 1 2.042 0.02 . 2 . . . . . . . . . 5783 1 204 . 1 1 37 37 GLU HG3 H 1 2.072 0.02 . 2 . . . . . . . . . 5783 1 205 . 1 1 38 38 VAL H H 1 7.951 0.02 . 1 . . . . . . . . . 5783 1 206 . 1 1 38 38 VAL HA H 1 4.627 0.02 . 1 . . . . . . . . . 5783 1 207 . 1 1 38 38 VAL HB H 1 0.418 0.02 . 1 . . . . . . . . . 5783 1 208 . 1 1 38 38 VAL HG11 H 1 0.241 0.02 . 2 . . . . . . . . . 5783 1 209 . 1 1 38 38 VAL HG12 H 1 0.241 0.02 . 2 . . . . . . . . . 5783 1 210 . 1 1 38 38 VAL HG13 H 1 0.241 0.02 . 2 . . . . . . . . . 5783 1 211 . 1 1 38 38 VAL HG21 H 1 0.474 0.02 . 2 . . . . . . . . . 5783 1 212 . 1 1 38 38 VAL HG22 H 1 0.474 0.02 . 2 . . . . . . . . . 5783 1 213 . 1 1 38 38 VAL HG23 H 1 0.474 0.02 . 2 . . . . . . . . . 5783 1 214 . 1 1 39 39 ASP H H 1 8.849 0.02 . 1 . . . . . . . . . 5783 1 215 . 1 1 39 39 ASP HA H 1 4.938 0.02 . 1 . . . . . . . . . 5783 1 216 . 1 1 39 39 ASP HB2 H 1 2.169 0.02 . 2 . . . . . . . . . 5783 1 217 . 1 1 39 39 ASP HB3 H 1 2.404 0.02 . 2 . . . . . . . . . 5783 1 218 . 1 1 40 40 LEU H H 1 9.034 0.02 . 1 . . . . . . . . . 5783 1 219 . 1 1 40 40 LEU HA H 1 4.986 0.02 . 1 . . . . . . . . . 5783 1 220 . 1 1 40 40 LEU HB2 H 1 1.226 0.02 . 2 . . . . . . . . . 5783 1 221 . 1 1 40 40 LEU HB3 H 1 1.651 0.02 . 2 . . . . . . . . . 5783 1 222 . 1 1 40 40 LEU HG H 1 1.605 0.02 . 1 . . . . . . . . . 5783 1 223 . 1 1 40 40 LEU HD11 H 1 0.734 0.02 . 1 . . . . . . . . . 5783 1 224 . 1 1 40 40 LEU HD12 H 1 0.734 0.02 . 1 . . . . . . . . . 5783 1 225 . 1 1 40 40 LEU HD13 H 1 0.734 0.02 . 1 . . . . . . . . . 5783 1 226 . 1 1 41 41 LEU H H 1 8.968 0.02 . 1 . . . . . . . . . 5783 1 227 . 1 1 41 41 LEU HA H 1 4.996 0.02 . 1 . . . . . . . . . 5783 1 228 . 1 1 41 41 LEU HB2 H 1 0.774 0.02 . 2 . . . . . . . . . 5783 1 229 . 1 1 41 41 LEU HB3 H 1 1.582 0.02 . 2 . . . . . . . . . 5783 1 230 . 1 1 41 41 LEU HG H 1 1.193 0.02 . 1 . . . . . . . . . 5783 1 231 . 1 1 41 41 LEU HD11 H 1 0.392 0.02 . 2 . . . . . . . . . 5783 1 232 . 1 1 41 41 LEU HD12 H 1 0.392 0.02 . 2 . . . . . . . . . 5783 1 233 . 1 1 41 41 LEU HD13 H 1 0.392 0.02 . 2 . . . . . . . . . 5783 1 234 . 1 1 41 41 LEU HD21 H 1 0.584 0.02 . 2 . . . . . . . . . 5783 1 235 . 1 1 41 41 LEU HD22 H 1 0.584 0.02 . 2 . . . . . . . . . 5783 1 236 . 1 1 41 41 LEU HD23 H 1 0.584 0.02 . 2 . . . . . . . . . 5783 1 237 . 1 1 42 42 LYS H H 1 8.835 0.02 . 1 . . . . . . . . . 5783 1 238 . 1 1 42 42 LYS HA H 1 4.410 0.02 . 1 . . . . . . . . . 5783 1 239 . 1 1 42 42 LYS HB2 H 1 1.455 0.02 . 2 . . . . . . . . . 5783 1 240 . 1 1 42 42 LYS HD2 H 1 1.737 0.02 . 2 . . . . . . . . . 5783 1 241 . 1 1 43 43 ASN H H 1 9.733 0.02 . 1 . . . . . . . . . 5783 1 242 . 1 1 43 43 ASN HA H 1 4.357 0.02 . 1 . . . . . . . . . 5783 1 243 . 1 1 43 43 ASN HB2 H 1 2.891 0.02 . 1 . . . . . . . . . 5783 1 244 . 1 1 44 44 GLY H H 1 8.803 0.02 . 1 . . . . . . . . . 5783 1 245 . 1 1 44 44 GLY HA2 H 1 3.322 0.02 . 2 . . . . . . . . . 5783 1 246 . 1 1 44 44 GLY HA3 H 1 4.161 0.02 . 2 . . . . . . . . . 5783 1 247 . 1 1 45 45 GLU H H 1 7.812 0.02 . 1 . . . . . . . . . 5783 1 248 . 1 1 45 45 GLU HA H 1 4.583 0.02 . 1 . . . . . . . . . 5783 1 249 . 1 1 45 45 GLU HB2 H 1 1.951 0.02 . 2 . . . . . . . . . 5783 1 250 . 1 1 45 45 GLU HB3 H 1 2.044 0.02 . 2 . . . . . . . . . 5783 1 251 . 1 1 45 45 GLU HG2 H 1 2.111 0.02 . 2 . . . . . . . . . 5783 1 252 . 1 1 45 45 GLU HG3 H 1 2.288 0.02 . 2 . . . . . . . . . 5783 1 253 . 1 1 46 46 ARG H H 1 8.669 0.02 . 1 . . . . . . . . . 5783 1 254 . 1 1 46 46 ARG HA H 1 4.168 0.02 . 1 . . . . . . . . . 5783 1 255 . 1 1 46 46 ARG HB2 H 1 1.628 0.02 . 1 . . . . . . . . . 5783 1 256 . 1 1 46 46 ARG HG2 H 1 1.325 0.02 . 2 . . . . . . . . . 5783 1 257 . 1 1 46 46 ARG HG3 H 1 1.538 0.02 . 2 . . . . . . . . . 5783 1 258 . 1 1 46 46 ARG HD2 H 1 3.070 0.02 . 2 . . . . . . . . . 5783 1 259 . 1 1 46 46 ARG HD3 H 1 3.145 0.02 . 2 . . . . . . . . . 5783 1 260 . 1 1 47 47 ILE H H 1 8.787 0.02 . 1 . . . . . . . . . 5783 1 261 . 1 1 47 47 ILE HA H 1 3.983 0.02 . 1 . . . . . . . . . 5783 1 262 . 1 1 47 47 ILE HB H 1 1.527 0.02 . 1 . . . . . . . . . 5783 1 263 . 1 1 47 47 ILE HG12 H 1 1.031 0.02 . 2 . . . . . . . . . 5783 1 264 . 1 1 47 47 ILE HG13 H 1 1.690 0.02 . 2 . . . . . . . . . 5783 1 265 . 1 1 47 47 ILE HG21 H 1 0.975 0.02 . 1 . . . . . . . . . 5783 1 266 . 1 1 47 47 ILE HG22 H 1 0.975 0.02 . 1 . . . . . . . . . 5783 1 267 . 1 1 47 47 ILE HG23 H 1 0.975 0.02 . 1 . . . . . . . . . 5783 1 268 . 1 1 47 47 ILE HD11 H 1 0.836 0.02 . 1 . . . . . . . . . 5783 1 269 . 1 1 47 47 ILE HD12 H 1 0.836 0.02 . 1 . . . . . . . . . 5783 1 270 . 1 1 47 47 ILE HD13 H 1 0.836 0.02 . 1 . . . . . . . . . 5783 1 271 . 1 1 48 48 GLU H H 1 8.496 0.02 . 1 . . . . . . . . . 5783 1 272 . 1 1 48 48 GLU HA H 1 4.177 0.02 . 1 . . . . . . . . . 5783 1 273 . 1 1 48 48 GLU HB2 H 1 2.023 0.02 . 2 . . . . . . . . . 5783 1 274 . 1 1 48 48 GLU HB3 H 1 2.113 0.02 . 2 . . . . . . . . . 5783 1 275 . 1 1 48 48 GLU HG2 H 1 2.241 0.02 . 2 . . . . . . . . . 5783 1 276 . 1 1 48 48 GLU HG3 H 1 2.368 0.02 . 2 . . . . . . . . . 5783 1 277 . 1 1 49 49 LYS H H 1 7.960 0.02 . 1 . . . . . . . . . 5783 1 278 . 1 1 49 49 LYS HA H 1 4.512 0.02 . 1 . . . . . . . . . 5783 1 279 . 1 1 49 49 LYS HB2 H 1 1.741 0.02 . 2 . . . . . . . . . 5783 1 280 . 1 1 49 49 LYS HB3 H 1 1.919 0.02 . 2 . . . . . . . . . 5783 1 281 . 1 1 49 49 LYS HG2 H 1 1.383 0.02 . 2 . . . . . . . . . 5783 1 282 . 1 1 49 49 LYS HG3 H 1 1.484 0.02 . 2 . . . . . . . . . 5783 1 283 . 1 1 50 50 VAL H H 1 7.812 0.02 . 1 . . . . . . . . . 5783 1 284 . 1 1 50 50 VAL HA H 1 4.385 0.02 . 1 . . . . . . . . . 5783 1 285 . 1 1 50 50 VAL HB H 1 2.111 0.02 . 1 . . . . . . . . . 5783 1 286 . 1 1 50 50 VAL HG11 H 1 1.022 0.02 . 2 . . . . . . . . . 5783 1 287 . 1 1 50 50 VAL HG12 H 1 1.022 0.02 . 2 . . . . . . . . . 5783 1 288 . 1 1 50 50 VAL HG13 H 1 1.022 0.02 . 2 . . . . . . . . . 5783 1 289 . 1 1 50 50 VAL HG21 H 1 1.092 0.02 . 2 . . . . . . . . . 5783 1 290 . 1 1 50 50 VAL HG22 H 1 1.092 0.02 . 2 . . . . . . . . . 5783 1 291 . 1 1 50 50 VAL HG23 H 1 1.092 0.02 . 2 . . . . . . . . . 5783 1 292 . 1 1 51 51 GLU H H 1 8.432 0.02 . 1 . . . . . . . . . 5783 1 293 . 1 1 51 51 GLU HA H 1 4.480 0.02 . 1 . . . . . . . . . 5783 1 294 . 1 1 51 51 GLU HB2 H 1 0.751 0.02 . 2 . . . . . . . . . 5783 1 295 . 1 1 51 51 GLU HB3 H 1 1.571 0.02 . 2 . . . . . . . . . 5783 1 296 . 1 1 51 51 GLU HG2 H 1 2.069 0.02 . 1 . . . . . . . . . 5783 1 297 . 1 1 52 52 HIS H H 1 8.105 0.02 . 1 . . . . . . . . . 5783 1 298 . 1 1 52 52 HIS HA H 1 5.481 0.02 . 1 . . . . . . . . . 5783 1 299 . 1 1 52 52 HIS HB2 H 1 1.984 0.02 . 2 . . . . . . . . . 5783 1 300 . 1 1 52 52 HIS HB3 H 1 2.429 0.02 . 2 . . . . . . . . . 5783 1 301 . 1 1 53 53 SER H H 1 9.110 0.02 . 1 . . . . . . . . . 5783 1 302 . 1 1 53 53 SER HA H 1 4.647 0.02 . 1 . . . . . . . . . 5783 1 303 . 1 1 53 53 SER HB2 H 1 4.089 0.02 . 2 . . . . . . . . . 5783 1 304 . 1 1 53 53 SER HB3 H 1 4.446 0.02 . 2 . . . . . . . . . 5783 1 305 . 1 1 54 54 ASP H H 1 8.704 0.02 . 1 . . . . . . . . . 5783 1 306 . 1 1 54 54 ASP HA H 1 4.807 0.02 . 1 . . . . . . . . . 5783 1 307 . 1 1 54 54 ASP HB2 H 1 2.580 0.02 . 2 . . . . . . . . . 5783 1 308 . 1 1 54 54 ASP HB3 H 1 2.742 0.02 . 2 . . . . . . . . . 5783 1 309 . 1 1 55 55 LEU H H 1 8.715 0.02 . 1 . . . . . . . . . 5783 1 310 . 1 1 55 55 LEU HA H 1 4.310 0.02 . 1 . . . . . . . . . 5783 1 311 . 1 1 55 55 LEU HB2 H 1 1.878 0.02 . 1 . . . . . . . . . 5783 1 312 . 1 1 55 55 LEU HG H 1 1.695 0.02 . 1 . . . . . . . . . 5783 1 313 . 1 1 55 55 LEU HD11 H 1 0.904 0.02 . 2 . . . . . . . . . 5783 1 314 . 1 1 55 55 LEU HD12 H 1 0.904 0.02 . 2 . . . . . . . . . 5783 1 315 . 1 1 55 55 LEU HD13 H 1 0.904 0.02 . 2 . . . . . . . . . 5783 1 316 . 1 1 55 55 LEU HD21 H 1 1.054 0.02 . 2 . . . . . . . . . 5783 1 317 . 1 1 55 55 LEU HD22 H 1 1.054 0.02 . 2 . . . . . . . . . 5783 1 318 . 1 1 55 55 LEU HD23 H 1 1.054 0.02 . 2 . . . . . . . . . 5783 1 319 . 1 1 56 56 SER H H 1 8.046 0.02 . 1 . . . . . . . . . 5783 1 320 . 1 1 56 56 SER HA H 1 4.764 0.02 . 1 . . . . . . . . . 5783 1 321 . 1 1 56 56 SER HB2 H 1 2.735 0.02 . 2 . . . . . . . . . 5783 1 322 . 1 1 56 56 SER HB3 H 1 3.412 0.02 . 2 . . . . . . . . . 5783 1 323 . 1 1 57 57 PHE H H 1 8.135 0.02 . 1 . . . . . . . . . 5783 1 324 . 1 1 57 57 PHE HA H 1 5.047 0.02 . 1 . . . . . . . . . 5783 1 325 . 1 1 57 57 PHE HB2 H 1 2.639 0.02 . 1 . . . . . . . . . 5783 1 326 . 1 1 57 57 PHE HD1 H 1 6.503 0.02 . 1 . . . . . . . . . 5783 1 327 . 1 1 57 57 PHE HE1 H 1 6.976 0.02 . 1 . . . . . . . . . 5783 1 328 . 1 1 58 58 SER H H 1 8.276 0.02 . 1 . . . . . . . . . 5783 1 329 . 1 1 58 58 SER HA H 1 4.583 0.02 . 1 . . . . . . . . . 5783 1 330 . 1 1 58 58 SER HB2 H 1 3.881 0.02 . 1 . . . . . . . . . 5783 1 331 . 1 1 59 59 LYS HA H 1 3.819 0.02 . 1 . . . . . . . . . 5783 1 332 . 1 1 59 59 LYS HB2 H 1 1.735 0.02 . 2 . . . . . . . . . 5783 1 333 . 1 1 59 59 LYS HG2 H 1 1.386 0.02 . 2 . . . . . . . . . 5783 1 334 . 1 1 59 59 LYS HD2 H 1 1.639 0.02 . 1 . . . . . . . . . 5783 1 335 . 1 1 59 59 LYS HE2 H 1 2.960 0.02 . 1 . . . . . . . . . 5783 1 336 . 1 1 60 60 ASP H H 1 7.678 0.02 . 1 . . . . . . . . . 5783 1 337 . 1 1 60 60 ASP HA H 1 4.341 0.02 . 1 . . . . . . . . . 5783 1 338 . 1 1 60 60 ASP HB2 H 1 2.250 0.02 . 1 . . . . . . . . . 5783 1 339 . 1 1 61 61 TRP H H 1 7.669 0.02 . 1 . . . . . . . . . 5783 1 340 . 1 1 61 61 TRP HA H 1 5.222 0.02 . 1 . . . . . . . . . 5783 1 341 . 1 1 61 61 TRP HB2 H 1 2.099 0.02 . 1 . . . . . . . . . 5783 1 342 . 1 1 61 61 TRP HD1 H 1 6.847 0.02 . 1 . . . . . . . . . 5783 1 343 . 1 1 61 61 TRP HE1 H 1 9.631 0.02 . 1 . . . . . . . . . 5783 1 344 . 1 1 61 61 TRP HZ2 H 1 7.317 0.02 . 1 . . . . . . . . . 5783 1 345 . 1 1 62 62 SER H H 1 7.574 0.02 . 1 . . . . . . . . . 5783 1 346 . 1 1 62 62 SER HA H 1 3.681 0.02 . 1 . . . . . . . . . 5783 1 347 . 1 1 62 62 SER HB2 H 1 3.743 0.02 . 2 . . . . . . . . . 5783 1 348 . 1 1 62 62 SER HB3 H 1 3.784 0.02 . 2 . . . . . . . . . 5783 1 349 . 1 1 63 63 PHE H H 1 8.125 0.02 . 1 . . . . . . . . . 5783 1 350 . 1 1 63 63 PHE HA H 1 5.467 0.02 . 1 . . . . . . . . . 5783 1 351 . 1 1 63 63 PHE HB2 H 1 1.573 0.02 . 2 . . . . . . . . . 5783 1 352 . 1 1 63 63 PHE HB3 H 1 1.984 0.02 . 2 . . . . . . . . . 5783 1 353 . 1 1 63 63 PHE HD1 H 1 6.982 0.02 . 1 . . . . . . . . . 5783 1 354 . 1 1 63 63 PHE HE1 H 1 7.169 0.02 . 1 . . . . . . . . . 5783 1 355 . 1 1 63 63 PHE HZ H 1 7.253 0.02 . 1 . . . . . . . . . 5783 1 356 . 1 1 64 64 TYR H H 1 8.264 0.02 . 1 . . . . . . . . . 5783 1 357 . 1 1 64 64 TYR HA H 1 5.533 0.02 . 1 . . . . . . . . . 5783 1 358 . 1 1 64 64 TYR HB2 H 1 2.804 0.02 . 2 . . . . . . . . . 5783 1 359 . 1 1 64 64 TYR HB3 H 1 3.037 0.02 . 2 . . . . . . . . . 5783 1 360 . 1 1 64 64 TYR HD1 H 1 7.050 0.02 . 1 . . . . . . . . . 5783 1 361 . 1 1 64 64 TYR HE1 H 1 6.662 0.02 . 1 . . . . . . . . . 5783 1 362 . 1 1 65 65 LEU H H 1 9.104 0.02 . 1 . . . . . . . . . 5783 1 363 . 1 1 65 65 LEU HA H 1 4.591 0.02 . 1 . . . . . . . . . 5783 1 364 . 1 1 65 65 LEU HB2 H 1 1.946 0.02 . 1 . . . . . . . . . 5783 1 365 . 1 1 65 65 LEU HG H 1 1.743 0.02 . 1 . . . . . . . . . 5783 1 366 . 1 1 65 65 LEU HD11 H 1 0.966 0.02 . 2 . . . . . . . . . 5783 1 367 . 1 1 65 65 LEU HD12 H 1 0.966 0.02 . 2 . . . . . . . . . 5783 1 368 . 1 1 65 65 LEU HD13 H 1 0.966 0.02 . 2 . . . . . . . . . 5783 1 369 . 1 1 65 65 LEU HD21 H 1 1.028 0.02 . 2 . . . . . . . . . 5783 1 370 . 1 1 65 65 LEU HD22 H 1 1.028 0.02 . 2 . . . . . . . . . 5783 1 371 . 1 1 65 65 LEU HD23 H 1 1.028 0.02 . 2 . . . . . . . . . 5783 1 372 . 1 1 66 66 LEU H H 1 8.129 0.02 . 1 . . . . . . . . . 5783 1 373 . 1 1 66 66 LEU HA H 1 5.472 0.02 . 1 . . . . . . . . . 5783 1 374 . 1 1 66 66 LEU HB2 H 1 1.978 0.02 . 1 . . . . . . . . . 5783 1 375 . 1 1 66 66 LEU HG H 1 1.567 0.02 . 1 . . . . . . . . . 5783 1 376 . 1 1 66 66 LEU HD11 H 1 0.803 0.02 . 2 . . . . . . . . . 5783 1 377 . 1 1 66 66 LEU HD12 H 1 0.803 0.02 . 2 . . . . . . . . . 5783 1 378 . 1 1 66 66 LEU HD13 H 1 0.803 0.02 . 2 . . . . . . . . . 5783 1 379 . 1 1 66 66 LEU HD21 H 1 1.030 0.02 . 2 . . . . . . . . . 5783 1 380 . 1 1 66 66 LEU HD22 H 1 1.030 0.02 . 2 . . . . . . . . . 5783 1 381 . 1 1 66 66 LEU HD23 H 1 1.030 0.02 . 2 . . . . . . . . . 5783 1 382 . 1 1 67 67 TYR H H 1 9.130 0.02 . 1 . . . . . . . . . 5783 1 383 . 1 1 67 67 TYR HA H 1 5.344 0.02 . 1 . . . . . . . . . 5783 1 384 . 1 1 67 67 TYR HB2 H 1 2.636 0.02 . 2 . . . . . . . . . 5783 1 385 . 1 1 67 67 TYR HB3 H 1 3.042 0.02 . 2 . . . . . . . . . 5783 1 386 . 1 1 67 67 TYR HD1 H 1 6.973 0.02 . 1 . . . . . . . . . 5783 1 387 . 1 1 67 67 TYR HE1 H 1 6.631 0.02 . 1 . . . . . . . . . 5783 1 388 . 1 1 68 68 TYR H H 1 8.931 0.02 . 1 . . . . . . . . . 5783 1 389 . 1 1 68 68 TYR HA H 1 5.973 0.02 . 1 . . . . . . . . . 5783 1 390 . 1 1 68 68 TYR HB2 H 1 2.650 0.02 . 2 . . . . . . . . . 5783 1 391 . 1 1 68 68 TYR HB3 H 1 3.199 0.02 . 2 . . . . . . . . . 5783 1 392 . 1 1 68 68 TYR HD1 H 1 6.691 0.02 . 1 . . . . . . . . . 5783 1 393 . 1 1 68 68 TYR HE1 H 1 6.544 0.02 . 1 . . . . . . . . . 5783 1 394 . 1 1 69 69 THR H H 1 8.288 0.02 . 1 . . . . . . . . . 5783 1 395 . 1 1 69 69 THR HA H 1 4.861 0.02 . 1 . . . . . . . . . 5783 1 396 . 1 1 69 69 THR HB H 1 4.108 0.02 . 1 . . . . . . . . . 5783 1 397 . 1 1 69 69 THR HG21 H 1 0.945 0.02 . 1 . . . . . . . . . 5783 1 398 . 1 1 69 69 THR HG22 H 1 0.945 0.02 . 1 . . . . . . . . . 5783 1 399 . 1 1 69 69 THR HG23 H 1 0.945 0.02 . 1 . . . . . . . . . 5783 1 400 . 1 1 70 70 GLU H H 1 8.491 0.02 . 1 . . . . . . . . . 5783 1 401 . 1 1 70 70 GLU HA H 1 4.314 0.02 . 1 . . . . . . . . . 5783 1 402 . 1 1 70 70 GLU HB2 H 1 1.701 0.02 . 2 . . . . . . . . . 5783 1 403 . 1 1 70 70 GLU HB3 H 1 1.827 0.02 . 2 . . . . . . . . . 5783 1 404 . 1 1 70 70 GLU HG2 H 1 1.880 0.02 . 1 . . . . . . . . . 5783 1 405 . 1 1 71 71 PHE H H 1 8.750 0.02 . 1 . . . . . . . . . 5783 1 406 . 1 1 71 71 PHE HA H 1 4.833 0.02 . 1 . . . . . . . . . 5783 1 407 . 1 1 71 71 PHE HB2 H 1 2.682 0.02 . 2 . . . . . . . . . 5783 1 408 . 1 1 71 71 PHE HB3 H 1 2.767 0.02 . 2 . . . . . . . . . 5783 1 409 . 1 1 71 71 PHE HD1 H 1 6.203 0.02 . 3 . . . . . . . . . 5783 1 410 . 1 1 71 71 PHE HZ H 1 5.718 0.02 . 1 . . . . . . . . . 5783 1 411 . 1 1 72 72 THR H H 1 8.201 0.02 . 1 . . . . . . . . . 5783 1 412 . 1 1 72 72 THR HA H 1 4.465 0.02 . 1 . . . . . . . . . 5783 1 413 . 1 1 72 72 THR HB H 1 3.870 0.02 . 1 . . . . . . . . . 5783 1 414 . 1 1 72 72 THR HG21 H 1 0.854 0.02 . 1 . . . . . . . . . 5783 1 415 . 1 1 72 72 THR HG22 H 1 0.854 0.02 . 1 . . . . . . . . . 5783 1 416 . 1 1 72 72 THR HG23 H 1 0.854 0.02 . 1 . . . . . . . . . 5783 1 417 . 1 1 73 73 PRO HA H 1 4.579 0.02 . 1 . . . . . . . . . 5783 1 418 . 1 1 73 73 PRO HB2 H 1 2.197 0.02 . 2 . . . . . . . . . 5783 1 419 . 1 1 73 73 PRO HB3 H 1 2.401 0.02 . 2 . . . . . . . . . 5783 1 420 . 1 1 73 73 PRO HG2 H 1 1.397 0.02 . 2 . . . . . . . . . 5783 1 421 . 1 1 73 73 PRO HG3 H 1 1.973 0.02 . 2 . . . . . . . . . 5783 1 422 . 1 1 73 73 PRO HD2 H 1 2.238 0.02 . 2 . . . . . . . . . 5783 1 423 . 1 1 73 73 PRO HD3 H 1 3.966 0.02 . 2 . . . . . . . . . 5783 1 424 . 1 1 74 74 THR H H 1 8.064 0.02 . 1 . . . . . . . . . 5783 1 425 . 1 1 74 74 THR HA H 1 4.675 0.02 . 1 . . . . . . . . . 5783 1 426 . 1 1 74 74 THR HB H 1 4.542 0.02 . 1 . . . . . . . . . 5783 1 427 . 1 1 74 74 THR HG21 H 1 1.315 0.02 . 1 . . . . . . . . . 5783 1 428 . 1 1 74 74 THR HG22 H 1 1.315 0.02 . 1 . . . . . . . . . 5783 1 429 . 1 1 74 74 THR HG23 H 1 1.315 0.02 . 1 . . . . . . . . . 5783 1 430 . 1 1 75 75 GLU H H 1 9.094 0.02 . 1 . . . . . . . . . 5783 1 431 . 1 1 75 75 GLU HA H 1 4.206 0.02 . 1 . . . . . . . . . 5783 1 432 . 1 1 75 75 GLU HB2 H 1 2.077 0.02 . 2 . . . . . . . . . 5783 1 433 . 1 1 75 75 GLU HG2 H 1 2.275 0.02 . 2 . . . . . . . . . 5783 1 434 . 1 1 75 75 GLU HG3 H 1 2.352 0.02 . 2 . . . . . . . . . 5783 1 435 . 1 1 76 76 LYS H H 1 7.799 0.02 . 1 . . . . . . . . . 5783 1 436 . 1 1 76 76 LYS HA H 1 4.458 0.02 . 1 . . . . . . . . . 5783 1 437 . 1 1 76 76 LYS HB2 H 1 1.783 0.02 . 2 . . . . . . . . . 5783 1 438 . 1 1 76 76 LYS HB3 H 1 1.865 0.02 . 2 . . . . . . . . . 5783 1 439 . 1 1 76 76 LYS HG2 H 1 1.409 0.02 . 2 . . . . . . . . . 5783 1 440 . 1 1 76 76 LYS HD2 H 1 1.679 0.02 . 2 . . . . . . . . . 5783 1 441 . 1 1 76 76 LYS HE2 H 1 2.986 0.02 . 2 . . . . . . . . . 5783 1 442 . 1 1 77 77 ASP H H 1 7.116 0.02 . 1 . . . . . . . . . 5783 1 443 . 1 1 77 77 ASP HA H 1 5.117 0.02 . 1 . . . . . . . . . 5783 1 444 . 1 1 77 77 ASP HB2 H 1 2.139 0.02 . 2 . . . . . . . . . 5783 1 445 . 1 1 77 77 ASP HB3 H 1 2.808 0.02 . 2 . . . . . . . . . 5783 1 446 . 1 1 78 78 GLU H H 1 8.598 0.02 . 1 . . . . . . . . . 5783 1 447 . 1 1 78 78 GLU HA H 1 4.797 0.02 . 1 . . . . . . . . . 5783 1 448 . 1 1 78 78 GLU HB2 H 1 1.989 0.02 . 2 . . . . . . . . . 5783 1 449 . 1 1 78 78 GLU HB3 H 1 2.081 0.02 . 2 . . . . . . . . . 5783 1 450 . 1 1 78 78 GLU HG2 H 1 2.368 0.02 . 2 . . . . . . . . . 5783 1 451 . 1 1 79 79 TYR H H 1 9.461 0.02 . 1 . . . . . . . . . 5783 1 452 . 1 1 79 79 TYR HA H 1 5.589 0.02 . 1 . . . . . . . . . 5783 1 453 . 1 1 79 79 TYR HB2 H 1 2.718 0.02 . 2 . . . . . . . . . 5783 1 454 . 1 1 79 79 TYR HB3 H 1 2.812 0.02 . 2 . . . . . . . . . 5783 1 455 . 1 1 79 79 TYR HD1 H 1 7.093 0.02 . 3 . . . . . . . . . 5783 1 456 . 1 1 79 79 TYR HE1 H 1 6.879 0.02 . 3 . . . . . . . . . 5783 1 457 . 1 1 80 80 ALA H H 1 8.791 0.02 . 1 . . . . . . . . . 5783 1 458 . 1 1 80 80 ALA HA H 1 5.038 0.02 . 1 . . . . . . . . . 5783 1 459 . 1 1 80 80 ALA HB1 H 1 1.191 0.02 . 1 . . . . . . . . . 5783 1 460 . 1 1 80 80 ALA HB2 H 1 1.191 0.02 . 1 . . . . . . . . . 5783 1 461 . 1 1 80 80 ALA HB3 H 1 1.191 0.02 . 1 . . . . . . . . . 5783 1 462 . 1 1 81 81 CYS H H 1 9.094 0.02 . 1 . . . . . . . . . 5783 1 463 . 1 1 81 81 CYS HA H 1 5.104 0.02 . 1 . . . . . . . . . 5783 1 464 . 1 1 81 81 CYS HB2 H 1 2.611 0.02 . 2 . . . . . . . . . 5783 1 465 . 1 1 81 81 CYS HB3 H 1 3.050 0.02 . 2 . . . . . . . . . 5783 1 466 . 1 1 82 82 ARG H H 1 9.407 0.02 . 1 . . . . . . . . . 5783 1 467 . 1 1 82 82 ARG HA H 1 5.391 0.02 . 1 . . . . . . . . . 5783 1 468 . 1 1 82 82 ARG HB2 H 1 1.184 0.02 . 2 . . . . . . . . . 5783 1 469 . 1 1 82 82 ARG HB3 H 1 1.789 0.02 . 2 . . . . . . . . . 5783 1 470 . 1 1 82 82 ARG HG2 H 1 1.266 0.02 . 2 . . . . . . . . . 5783 1 471 . 1 1 83 83 VAL H H 1 8.973 0.02 . 1 . . . . . . . . . 5783 1 472 . 1 1 83 83 VAL HA H 1 4.996 0.02 . 1 . . . . . . . . . 5783 1 473 . 1 1 83 83 VAL HB H 1 1.562 0.02 . 1 . . . . . . . . . 5783 1 474 . 1 1 83 83 VAL HG11 H 1 0.824 0.02 . 2 . . . . . . . . . 5783 1 475 . 1 1 83 83 VAL HG12 H 1 0.824 0.02 . 2 . . . . . . . . . 5783 1 476 . 1 1 83 83 VAL HG13 H 1 0.824 0.02 . 2 . . . . . . . . . 5783 1 477 . 1 1 83 83 VAL HG21 H 1 0.780 0.02 . 2 . . . . . . . . . 5783 1 478 . 1 1 83 83 VAL HG22 H 1 0.780 0.02 . 2 . . . . . . . . . 5783 1 479 . 1 1 83 83 VAL HG23 H 1 0.780 0.02 . 2 . . . . . . . . . 5783 1 480 . 1 1 84 84 ASN H H 1 9.013 0.02 . 1 . . . . . . . . . 5783 1 481 . 1 1 84 84 ASN HA H 1 5.187 0.02 . 1 . . . . . . . . . 5783 1 482 . 1 1 84 84 ASN HB2 H 1 2.387 0.02 . 2 . . . . . . . . . 5783 1 483 . 1 1 84 84 ASN HB3 H 1 2.806 0.02 . 2 . . . . . . . . . 5783 1 484 . 1 1 85 85 HIS H H 1 7.740 0.02 . 1 . . . . . . . . . 5783 1 485 . 1 1 85 85 HIS HA H 1 4.555 0.02 . 1 . . . . . . . . . 5783 1 486 . 1 1 85 85 HIS HB2 H 1 2.423 0.02 . 2 . . . . . . . . . 5783 1 487 . 1 1 85 85 HIS HB3 H 1 2.901 0.02 . 2 . . . . . . . . . 5783 1 488 . 1 1 85 85 HIS HD1 H 1 7.554 0.02 . 1 . . . . . . . . . 5783 1 489 . 1 1 85 85 HIS HE1 H 1 8.133 0.02 . 1 . . . . . . . . . 5783 1 490 . 1 1 86 86 VAL H H 1 7.986 0.02 . 1 . . . . . . . . . 5783 1 491 . 1 1 86 86 VAL HA H 1 3.976 0.02 . 1 . . . . . . . . . 5783 1 492 . 1 1 86 86 VAL HB H 1 1.929 0.02 . 1 . . . . . . . . . 5783 1 493 . 1 1 86 86 VAL HG11 H 1 0.620 0.02 . 2 . . . . . . . . . 5783 1 494 . 1 1 86 86 VAL HG12 H 1 0.620 0.02 . 2 . . . . . . . . . 5783 1 495 . 1 1 86 86 VAL HG13 H 1 0.620 0.02 . 2 . . . . . . . . . 5783 1 496 . 1 1 86 86 VAL HG21 H 1 0.855 0.02 . 2 . . . . . . . . . 5783 1 497 . 1 1 86 86 VAL HG22 H 1 0.855 0.02 . 2 . . . . . . . . . 5783 1 498 . 1 1 86 86 VAL HG23 H 1 0.855 0.02 . 2 . . . . . . . . . 5783 1 499 . 1 1 87 87 THR H H 1 7.587 0.02 . 1 . . . . . . . . . 5783 1 500 . 1 1 87 87 THR HA H 1 4.162 0.02 . 1 . . . . . . . . . 5783 1 501 . 1 1 87 87 THR HB H 1 4.492 0.02 . 1 . . . . . . . . . 5783 1 502 . 1 1 87 87 THR HG21 H 1 1.480 0.02 . 1 . . . . . . . . . 5783 1 503 . 1 1 87 87 THR HG22 H 1 1.480 0.02 . 1 . . . . . . . . . 5783 1 504 . 1 1 87 87 THR HG23 H 1 1.480 0.02 . 1 . . . . . . . . . 5783 1 505 . 1 1 88 88 LEU H H 1 8.034 0.02 . 1 . . . . . . . . . 5783 1 506 . 1 1 88 88 LEU HA H 1 4.757 0.02 . 1 . . . . . . . . . 5783 1 507 . 1 1 88 88 LEU HB2 H 1 1.837 0.02 . 2 . . . . . . . . . 5783 1 508 . 1 1 88 88 LEU HB3 H 1 2.033 0.02 . 2 . . . . . . . . . 5783 1 509 . 1 1 88 88 LEU HG H 1 1.713 0.02 . 1 . . . . . . . . . 5783 1 510 . 1 1 88 88 LEU HD11 H 1 0.968 0.02 . 2 . . . . . . . . . 5783 1 511 . 1 1 88 88 LEU HD12 H 1 0.968 0.02 . 2 . . . . . . . . . 5783 1 512 . 1 1 88 88 LEU HD13 H 1 0.968 0.02 . 2 . . . . . . . . . 5783 1 513 . 1 1 89 89 SER HA H 1 4.239 0.02 . 1 . . . . . . . . . 5783 1 514 . 1 1 89 89 SER HB2 H 1 3.952 0.02 . 2 . . . . . . . . . 5783 1 515 . 1 1 89 89 SER HB3 H 1 3.971 0.02 . 2 . . . . . . . . . 5783 1 516 . 1 1 90 90 GLN H H 1 7.531 0.02 . 1 . . . . . . . . . 5783 1 517 . 1 1 90 90 GLN HA H 1 4.733 0.02 . 1 . . . . . . . . . 5783 1 518 . 1 1 90 90 GLN HB2 H 1 1.884 0.02 . 2 . . . . . . . . . 5783 1 519 . 1 1 90 90 GLN HB3 H 1 2.141 0.02 . 2 . . . . . . . . . 5783 1 520 . 1 1 90 90 GLN HG2 H 1 2.291 0.02 . 2 . . . . . . . . . 5783 1 521 . 1 1 91 91 PRO HA H 1 4.491 0.02 . 1 . . . . . . . . . 5783 1 522 . 1 1 91 91 PRO HB2 H 1 1.493 0.02 . 2 . . . . . . . . . 5783 1 523 . 1 1 91 91 PRO HB3 H 1 1.838 0.02 . 2 . . . . . . . . . 5783 1 524 . 1 1 91 91 PRO HG2 H 1 1.768 0.02 . 2 . . . . . . . . . 5783 1 525 . 1 1 91 91 PRO HG3 H 1 1.995 0.02 . 2 . . . . . . . . . 5783 1 526 . 1 1 91 91 PRO HD2 H 1 3.522 0.02 . 2 . . . . . . . . . 5783 1 527 . 1 1 91 91 PRO HD3 H 1 3.729 0.02 . 2 . . . . . . . . . 5783 1 528 . 1 1 92 92 LYS H H 1 8.732 0.02 . 1 . . . . . . . . . 5783 1 529 . 1 1 92 92 LYS HA H 1 4.516 0.02 . 1 . . . . . . . . . 5783 1 530 . 1 1 92 92 LYS HB2 H 1 1.647 0.02 . 2 . . . . . . . . . 5783 1 531 . 1 1 92 92 LYS HB3 H 1 1.746 0.02 . 2 . . . . . . . . . 5783 1 532 . 1 1 92 92 LYS HG2 H 1 1.347 0.02 . 2 . . . . . . . . . 5783 1 533 . 1 1 92 92 LYS HG3 H 1 1.412 0.02 . 2 . . . . . . . . . 5783 1 534 . 1 1 93 93 ILE H H 1 8.499 0.02 . 1 . . . . . . . . . 5783 1 535 . 1 1 93 93 ILE HA H 1 4.789 0.02 . 1 . . . . . . . . . 5783 1 536 . 1 1 93 93 ILE HB H 1 1.701 0.02 . 1 . . . . . . . . . 5783 1 537 . 1 1 93 93 ILE HG12 H 1 1.414 0.02 . 2 . . . . . . . . . 5783 1 538 . 1 1 93 93 ILE HG21 H 1 0.616 0.02 . 1 . . . . . . . . . 5783 1 539 . 1 1 93 93 ILE HG22 H 1 0.616 0.02 . 1 . . . . . . . . . 5783 1 540 . 1 1 93 93 ILE HG23 H 1 0.616 0.02 . 1 . . . . . . . . . 5783 1 541 . 1 1 93 93 ILE HD11 H 1 0.742 0.02 . 1 . . . . . . . . . 5783 1 542 . 1 1 93 93 ILE HD12 H 1 0.742 0.02 . 1 . . . . . . . . . 5783 1 543 . 1 1 93 93 ILE HD13 H 1 0.742 0.02 . 1 . . . . . . . . . 5783 1 544 . 1 1 94 94 VAL H H 1 9.052 0.02 . 1 . . . . . . . . . 5783 1 545 . 1 1 94 94 VAL HA H 1 4.318 0.02 . 1 . . . . . . . . . 5783 1 546 . 1 1 94 94 VAL HB H 1 1.887 0.02 . 1 . . . . . . . . . 5783 1 547 . 1 1 94 94 VAL HG11 H 1 0.907 0.02 . 2 . . . . . . . . . 5783 1 548 . 1 1 94 94 VAL HG12 H 1 0.907 0.02 . 2 . . . . . . . . . 5783 1 549 . 1 1 94 94 VAL HG13 H 1 0.907 0.02 . 2 . . . . . . . . . 5783 1 550 . 1 1 94 94 VAL HG21 H 1 1.024 0.02 . 2 . . . . . . . . . 5783 1 551 . 1 1 94 94 VAL HG22 H 1 1.024 0.02 . 2 . . . . . . . . . 5783 1 552 . 1 1 94 94 VAL HG23 H 1 1.024 0.02 . 2 . . . . . . . . . 5783 1 553 . 1 1 95 95 LYS H H 1 8.790 0.02 . 1 . . . . . . . . . 5783 1 554 . 1 1 95 95 LYS HA H 1 4.445 0.02 . 1 . . . . . . . . . 5783 1 555 . 1 1 95 95 LYS HB2 H 1 1.838 0.02 . 2 . . . . . . . . . 5783 1 556 . 1 1 95 95 LYS HG2 H 1 1.438 0.02 . 2 . . . . . . . . . 5783 1 557 . 1 1 95 95 LYS HG3 H 1 1.534 0.02 . 2 . . . . . . . . . 5783 1 558 . 1 1 96 96 TRP H H 1 8.695 0.02 . 1 . . . . . . . . . 5783 1 559 . 1 1 96 96 TRP HA H 1 4.656 0.02 . 1 . . . . . . . . . 5783 1 560 . 1 1 96 96 TRP HB2 H 1 2.600 0.02 . 2 . . . . . . . . . 5783 1 561 . 1 1 96 96 TRP HB3 H 1 3.481 0.02 . 2 . . . . . . . . . 5783 1 562 . 1 1 96 96 TRP HD1 H 1 7.114 0.02 . 1 . . . . . . . . . 5783 1 563 . 1 1 96 96 TRP HE1 H 1 10.457 0.02 . 1 . . . . . . . . . 5783 1 564 . 1 1 96 96 TRP HE3 H 1 7.970 0.02 . 1 . . . . . . . . . 5783 1 565 . 1 1 96 96 TRP HZ2 H 1 7.633 0.02 . 1 . . . . . . . . . 5783 1 566 . 1 1 96 96 TRP HZ3 H 1 7.618 0.02 . 1 . . . . . . . . . 5783 1 567 . 1 1 96 96 TRP HH2 H 1 7.477 0.02 . 1 . . . . . . . . . 5783 1 568 . 1 1 97 97 ASP H H 1 8.432 0.02 . 1 . . . . . . . . . 5783 1 569 . 1 1 97 97 ASP HA H 1 4.480 0.02 . 1 . . . . . . . . . 5783 1 570 . 1 1 97 97 ASP HB2 H 1 2.458 0.02 . 2 . . . . . . . . . 5783 1 571 . 1 1 97 97 ASP HB3 H 1 2.754 0.02 . 2 . . . . . . . . . 5783 1 572 . 1 1 98 98 ARG H H 1 7.427 0.02 . 1 . . . . . . . . . 5783 1 573 . 1 1 98 98 ARG HA H 1 3.390 0.02 . 1 . . . . . . . . . 5783 1 574 . 1 1 98 98 ARG HB2 H 1 1.130 0.02 . 2 . . . . . . . . . 5783 1 575 . 1 1 98 98 ARG HB3 H 1 1.413 0.02 . 2 . . . . . . . . . 5783 1 576 . 1 1 98 98 ARG HG2 H 1 0.930 0.02 . 2 . . . . . . . . . 5783 1 577 . 1 1 98 98 ARG HD2 H 1 2.951 0.02 . 2 . . . . . . . . . 5783 1 578 . 1 1 99 99 ASP H H 1 8.195 0.02 . 1 . . . . . . . . . 5783 1 579 . 1 1 99 99 ASP HA H 1 4.649 0.02 . 1 . . . . . . . . . 5783 1 580 . 1 1 99 99 ASP HB2 H 1 2.598 0.02 . 2 . . . . . . . . . 5783 1 581 . 1 1 99 99 ASP HB3 H 1 2.775 0.02 . 2 . . . . . . . . . 5783 1 582 . 1 1 100 100 MET H H 1 7.587 0.02 . 1 . . . . . . . . . 5783 1 583 . 1 1 100 100 MET HA H 1 4.284 0.02 . 1 . . . . . . . . . 5783 1 584 . 1 1 100 100 MET HB2 H 1 2.027 0.02 . 2 . . . . . . . . . 5783 1 585 . 1 1 100 100 MET HB3 H 1 2.161 0.02 . 2 . . . . . . . . . 5783 1 586 . 1 1 100 100 MET HG2 H 1 2.539 0.02 . 2 . . . . . . . . . 5783 1 587 . 1 1 100 100 MET HG3 H 1 2.578 0.02 . 2 . . . . . . . . . 5783 1 stop_ save_