data_5784 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5784 _Entry.Title ; 1H assignment of a human variant of beta2-microglobulin where His 31 was replaced by a Tyr ; _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 Fabio Pettirossi . . . . 5784 2 Alessandra Corazza . . . . 5784 3 Paolo Viglino . . . . 5784 4 Giuliana Verdone . . . . 5784 5 Gennaro Esposito . . . . 5784 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 5784 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 541 5784 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 . 5784 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' 5784 BMRB 5782 'DN3 beta2-microglobulin (without the first 3 residue)' 5784 BMRB 5783 'DN3 beta2-microglobulin (R3A mutant with the first 3 residue)' 5784 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5784 _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 . . . . 5784 1 2 Fabio Pettirossi . . . . 5784 1 3 Paolo Viglino . . . . 5784 1 4 Giuliana Verdone . . . . 5784 1 5 Julian Garcia . . . . 5784 1 6 Pascal Dumy . . . . 5784 1 7 Sofia Giorgetti . . . . 5784 1 8 Palma Mangione . . . . 5784 1 9 Alessia Andreola . . . . 5784 1 10 Monica Stoppini . . . . 5784 1 11 Vittorio Bellotti . . . . 5784 1 12 Gennaro Esposito . . . . 5784 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID amyloidosis 5784 1 beta2-microglobulin 5784 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 5784 _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. . . . 5784 2 2 Alessandra Corazza A. . . . 5784 2 3 Paolo Viglino P. . . . 5784 2 4 Fabio Pettirossi F. . . . 5784 2 5 Sofia Giorgetti S. . . . 5784 2 6 Palma Mangione P. . . . 5784 2 7 Alessia Andreola A. . . . 5784 2 8 Monica Stoppini M. . . . 5784 2 9 Vittorio Bellotti V. . . . 5784 2 10 Gennaro Esposito G. . . . 5784 2 stop_ save_ save_ref_2 _Citation.Sf_category citations _Citation.Sf_framecode ref_2 _Citation.Entry_ID 5784 _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. . . . 5784 3 2 R Michelutti R. . . . 5784 3 3 G Verdone G. . . . 5784 3 4 P Viglino P. . . . 5784 3 5 H Hernandez H. . . . 5784 3 6 C.V. Robinson C. V. . . 5784 3 7 A Amoresano A. . . . 5784 3 8 F 'Dal Piaz' F. . . . 5784 3 9 M Monti M. . . . 5784 3 10 P Pucci P. . . . 5784 3 11 P Mangione P. . . . 5784 3 12 M Stoppini M. . . . 5784 3 13 G Merlini G. . . . 5784 3 14 G Ferri G. . . . 5784 3 15 V Bellotti V. . . . 5784 3 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_H31Yb2-m _Assembly.Sf_category assembly _Assembly.Sf_framecode system_H31Yb2-m _Assembly.Entry_ID 5784 _Assembly.ID 1 _Assembly.Name His31Tyrbeta2-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 5784 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 H31Ybeta2-microglobulin 1 $H31Ybeta2-m . . . native . . . . . 5784 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 . . . . . . . . . . . . 5784 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID H31Yb2-m abbreviation 5784 1 His31Tyrbeta2-microglobulin system 5784 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_H31Ybeta2-m _Entity.Sf_category entity _Entity.Sf_framecode H31Ybeta2-m _Entity.Entry_ID 5784 _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 ; MIQRTPKIQVYSRHPAENGK SNFLNCYVSGFYPSDIEVDL 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 . _Entity.DB_query_revised_last_date . loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID H31Ybeta2-m abbreviation 5784 1 H31Ybeta2-microglobulin variant 5784 1 beta2-microglobulin common 5784 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 0 MET . 5784 1 2 1 ILE . 5784 1 3 2 GLN . 5784 1 4 3 ARG . 5784 1 5 4 THR . 5784 1 6 5 PRO . 5784 1 7 6 LYS . 5784 1 8 7 ILE . 5784 1 9 8 GLN . 5784 1 10 9 VAL . 5784 1 11 10 TYR . 5784 1 12 11 SER . 5784 1 13 12 ARG . 5784 1 14 13 HIS . 5784 1 15 14 PRO . 5784 1 16 15 ALA . 5784 1 17 16 GLU . 5784 1 18 17 ASN . 5784 1 19 18 GLY . 5784 1 20 19 LYS . 5784 1 21 20 SER . 5784 1 22 21 ASN . 5784 1 23 22 PHE . 5784 1 24 23 LEU . 5784 1 25 24 ASN . 5784 1 26 25 CYS . 5784 1 27 26 TYR . 5784 1 28 27 VAL . 5784 1 29 28 SER . 5784 1 30 29 GLY . 5784 1 31 30 PHE . 5784 1 32 31 TYR . 5784 1 33 32 PRO . 5784 1 34 33 SER . 5784 1 35 34 ASP . 5784 1 36 35 ILE . 5784 1 37 36 GLU . 5784 1 38 37 VAL . 5784 1 39 38 ASP . 5784 1 40 39 LEU . 5784 1 41 40 LEU . 5784 1 42 41 LYS . 5784 1 43 42 ASN . 5784 1 44 43 GLY . 5784 1 45 44 GLU . 5784 1 46 45 ARG . 5784 1 47 46 ILE . 5784 1 48 47 GLU . 5784 1 49 48 LYS . 5784 1 50 49 VAL . 5784 1 51 50 GLU . 5784 1 52 51 HIS . 5784 1 53 52 SER . 5784 1 54 53 ASP . 5784 1 55 54 LEU . 5784 1 56 55 SER . 5784 1 57 56 PHE . 5784 1 58 57 SER . 5784 1 59 58 LYS . 5784 1 60 59 ASP . 5784 1 61 60 TRP . 5784 1 62 61 SER . 5784 1 63 62 PHE . 5784 1 64 63 TYR . 5784 1 65 64 LEU . 5784 1 66 65 LEU . 5784 1 67 66 TYR . 5784 1 68 67 TYR . 5784 1 69 68 THR . 5784 1 70 69 GLU . 5784 1 71 70 PHE . 5784 1 72 71 THR . 5784 1 73 72 PRO . 5784 1 74 73 THR . 5784 1 75 74 GLU . 5784 1 76 75 LYS . 5784 1 77 76 ASP . 5784 1 78 77 GLU . 5784 1 79 78 TYR . 5784 1 80 79 ALA . 5784 1 81 80 CYS . 5784 1 82 81 ARG . 5784 1 83 82 VAL . 5784 1 84 83 ASN . 5784 1 85 84 HIS . 5784 1 86 85 VAL . 5784 1 87 86 THR . 5784 1 88 87 LEU . 5784 1 89 88 SER . 5784 1 90 89 GLN . 5784 1 91 90 PRO . 5784 1 92 91 LYS . 5784 1 93 92 ILE . 5784 1 94 93 VAL . 5784 1 95 94 LYS . 5784 1 96 95 TRP . 5784 1 97 96 ASP . 5784 1 98 97 ARG . 5784 1 99 98 ASP . 5784 1 100 99 MET . 5784 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 5784 1 . ILE 2 2 5784 1 . GLN 3 3 5784 1 . ARG 4 4 5784 1 . THR 5 5 5784 1 . PRO 6 6 5784 1 . LYS 7 7 5784 1 . ILE 8 8 5784 1 . GLN 9 9 5784 1 . VAL 10 10 5784 1 . TYR 11 11 5784 1 . SER 12 12 5784 1 . ARG 13 13 5784 1 . HIS 14 14 5784 1 . PRO 15 15 5784 1 . ALA 16 16 5784 1 . GLU 17 17 5784 1 . ASN 18 18 5784 1 . GLY 19 19 5784 1 . LYS 20 20 5784 1 . SER 21 21 5784 1 . ASN 22 22 5784 1 . PHE 23 23 5784 1 . LEU 24 24 5784 1 . ASN 25 25 5784 1 . CYS 26 26 5784 1 . TYR 27 27 5784 1 . VAL 28 28 5784 1 . SER 29 29 5784 1 . GLY 30 30 5784 1 . PHE 31 31 5784 1 . TYR 32 32 5784 1 . PRO 33 33 5784 1 . SER 34 34 5784 1 . ASP 35 35 5784 1 . ILE 36 36 5784 1 . GLU 37 37 5784 1 . VAL 38 38 5784 1 . ASP 39 39 5784 1 . LEU 40 40 5784 1 . LEU 41 41 5784 1 . LYS 42 42 5784 1 . ASN 43 43 5784 1 . GLY 44 44 5784 1 . GLU 45 45 5784 1 . ARG 46 46 5784 1 . ILE 47 47 5784 1 . GLU 48 48 5784 1 . LYS 49 49 5784 1 . VAL 50 50 5784 1 . GLU 51 51 5784 1 . HIS 52 52 5784 1 . SER 53 53 5784 1 . ASP 54 54 5784 1 . LEU 55 55 5784 1 . SER 56 56 5784 1 . PHE 57 57 5784 1 . SER 58 58 5784 1 . LYS 59 59 5784 1 . ASP 60 60 5784 1 . TRP 61 61 5784 1 . SER 62 62 5784 1 . PHE 63 63 5784 1 . TYR 64 64 5784 1 . LEU 65 65 5784 1 . LEU 66 66 5784 1 . TYR 67 67 5784 1 . TYR 68 68 5784 1 . THR 69 69 5784 1 . GLU 70 70 5784 1 . PHE 71 71 5784 1 . THR 72 72 5784 1 . PRO 73 73 5784 1 . THR 74 74 5784 1 . GLU 75 75 5784 1 . LYS 76 76 5784 1 . ASP 77 77 5784 1 . GLU 78 78 5784 1 . TYR 79 79 5784 1 . ALA 80 80 5784 1 . CYS 81 81 5784 1 . ARG 82 82 5784 1 . VAL 83 83 5784 1 . ASN 84 84 5784 1 . HIS 85 85 5784 1 . VAL 86 86 5784 1 . THR 87 87 5784 1 . LEU 88 88 5784 1 . SER 89 89 5784 1 . GLN 90 90 5784 1 . PRO 91 91 5784 1 . LYS 92 92 5784 1 . ILE 93 93 5784 1 . VAL 94 94 5784 1 . LYS 95 95 5784 1 . TRP 96 96 5784 1 . ASP 97 97 5784 1 . ARG 98 98 5784 1 . ASP 99 99 5784 1 . MET 100 100 5784 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 5784 _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 $H31Ybeta2-m . 9606 . . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . 5784 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 5784 _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 $H31Ybeta2-m . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli . . . . . . . . . . 5784 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5784 _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 $H31Ybeta2-m . . 0.8 . . mM . . . . 5784 1 2 'sodium phosphate' . . . . . . . 70 . . mM . . . . 5784 1 3 'sodium chloride' . . . . . . . 100 . . mM . . . . 5784 1 4 H2O . . . . . . . 100 . . % . . . . 5784 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 5784 _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 5784 1 temperature 303 0.1 K 5784 1 stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Software.Sf_category software _Software.Sf_framecode FELIX _Software.Entry_ID 5784 _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 5784 _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 5784 _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 . . . 5784 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 5784 _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' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5784 1 2 '1H-1H NOESY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5784 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 5784 _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 . . . . . 5784 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 5784 _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 . 5784 1 2 '1H-1H NOESY' 1 $sample_1 . 5784 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 4 4 ARG H H 1 9.338 0.02 . 1 . . . . . . . . . 5784 1 2 . 1 1 4 4 ARG HA H 1 4.858 0.02 . 1 . . . . . . . . . 5784 1 3 . 1 1 4 4 ARG HB3 H 1 2.250 0.02 . 1 . . . . . . . . . 5784 1 4 . 1 1 4 4 ARG HD2 H 1 3.151 0.02 . 1 . . . . . . . . . 5784 1 5 . 1 1 4 4 ARG HG2 H 1 1.755 0.02 . 1 . . . . . . . . . 5784 1 6 . 1 1 5 5 THR H H 1 8.390 0.02 . 1 . . . . . . . . . 5784 1 7 . 1 1 5 5 THR HA H 1 5.004 0.02 . 1 . . . . . . . . . 5784 1 8 . 1 1 5 5 THR HB H 1 4.079 0.02 . 1 . . . . . . . . . 5784 1 9 . 1 1 5 5 THR HG21 H 1 1.311 0.02 . 1 . . . . . . . . . 5784 1 10 . 1 1 5 5 THR HG22 H 1 1.311 0.02 . 1 . . . . . . . . . 5784 1 11 . 1 1 5 5 THR HG23 H 1 1.311 0.02 . 1 . . . . . . . . . 5784 1 12 . 1 1 6 6 PRO HA H 1 4.391 0.02 . 1 . . . . . . . . . 5784 1 13 . 1 1 6 6 PRO HB2 H 1 1.509 0.02 . 1 . . . . . . . . . 5784 1 14 . 1 1 6 6 PRO HD2 H 1 3.622 0.02 . 2 . . . . . . . . . 5784 1 15 . 1 1 6 6 PRO HD3 H 1 3.076 0.02 . 2 . . . . . . . . . 5784 1 16 . 1 1 6 6 PRO HG2 H 1 1.105 0.02 . 2 . . . . . . . . . 5784 1 17 . 1 1 6 6 PRO HG3 H 1 1.641 0.02 . 2 . . . . . . . . . 5784 1 18 . 1 1 7 7 LYS H H 1 9.199 0.02 . 1 . . . . . . . . . 5784 1 19 . 1 1 7 7 LYS HA H 1 4.491 0.02 . 1 . . . . . . . . . 5784 1 20 . 1 1 7 7 LYS HB2 H 1 1.768 0.02 . 2 . . . . . . . . . 5784 1 21 . 1 1 7 7 LYS HB3 H 1 1.509 0.02 . 2 . . . . . . . . . 5784 1 22 . 1 1 7 7 LYS HG2 H 1 1.408 0.02 . 1 . . . . . . . . . 5784 1 23 . 1 1 8 8 ILE H H 1 8.382 0.02 . 1 . . . . . . . . . 5784 1 24 . 1 1 8 8 ILE HA H 1 4.731 0.02 . 1 . . . . . . . . . 5784 1 25 . 1 1 8 8 ILE HB H 1 1.634 0.02 . 1 . . . . . . . . . 5784 1 26 . 1 1 8 8 ILE HG12 H 1 1.309 0.02 . 1 . . . . . . . . . 5784 1 27 . 1 1 8 8 ILE HG21 H 1 0.756 0.02 . 1 . . . . . . . . . 5784 1 28 . 1 1 8 8 ILE HG22 H 1 0.756 0.02 . 1 . . . . . . . . . 5784 1 29 . 1 1 8 8 ILE HG23 H 1 0.756 0.02 . 1 . . . . . . . . . 5784 1 30 . 1 1 9 9 GLN H H 1 9.028 0.02 . 1 . . . . . . . . . 5784 1 31 . 1 1 9 9 GLN HA H 1 4.923 0.02 . 1 . . . . . . . . . 5784 1 32 . 1 1 9 9 GLN HB2 H 1 2.190 0.02 . 2 . . . . . . . . . 5784 1 33 . 1 1 9 9 GLN HB3 H 1 2.349 0.02 . 2 . . . . . . . . . 5784 1 34 . 1 1 9 9 GLN HE21 H 1 7.490 0.02 . 2 . . . . . . . . . 5784 1 35 . 1 1 9 9 GLN HE22 H 1 6.793 0.02 . 2 . . . . . . . . . 5784 1 36 . 1 1 9 9 GLN HG2 H 1 2.426 0.02 . 1 . . . . . . . . . 5784 1 37 . 1 1 10 10 VAL H H 1 9.046 0.02 . 1 . . . . . . . . . 5784 1 38 . 1 1 10 10 VAL HA H 1 5.324 0.02 . 1 . . . . . . . . . 5784 1 39 . 1 1 10 10 VAL HB H 1 2.021 0.02 . 1 . . . . . . . . . 5784 1 40 . 1 1 10 10 VAL HG11 H 1 0.907 0.02 . 2 . . . . . . . . . 5784 1 41 . 1 1 10 10 VAL HG12 H 1 0.907 0.02 . 2 . . . . . . . . . 5784 1 42 . 1 1 10 10 VAL HG13 H 1 0.907 0.02 . 2 . . . . . . . . . 5784 1 43 . 1 1 10 10 VAL HG21 H 1 0.964 0.02 . 2 . . . . . . . . . 5784 1 44 . 1 1 10 10 VAL HG22 H 1 0.964 0.02 . 2 . . . . . . . . . 5784 1 45 . 1 1 10 10 VAL HG23 H 1 0.964 0.02 . 2 . . . . . . . . . 5784 1 46 . 1 1 11 11 TYR H H 1 8.452 0.02 . 1 . . . . . . . . . 5784 1 47 . 1 1 11 11 TYR HA H 1 5.304 0.02 . 1 . . . . . . . . . 5784 1 48 . 1 1 11 11 TYR HB2 H 1 3.391 0.02 . 2 . . . . . . . . . 5784 1 49 . 1 1 11 11 TYR HB3 H 1 3.098 0.02 . 2 . . . . . . . . . 5784 1 50 . 1 1 11 11 TYR HD1 H 1 6.795 0.02 . 1 . . . . . . . . . 5784 1 51 . 1 1 11 11 TYR HE1 H 1 6.578 0.02 . 1 . . . . . . . . . 5784 1 52 . 1 1 12 12 SER H H 1 9.326 0.02 . 1 . . . . . . . . . 5784 1 53 . 1 1 12 12 SER HA H 1 5.319 0.02 . 1 . . . . . . . . . 5784 1 54 . 1 1 12 12 SER HB2 H 1 3.666 0.02 . 2 . . . . . . . . . 5784 1 55 . 1 1 12 12 SER HB3 H 1 4.438 0.02 . 2 . . . . . . . . . 5784 1 56 . 1 1 13 13 ARG H H 1 8.837 0.02 . 1 . . . . . . . . . 5784 1 57 . 1 1 13 13 ARG HA H 1 3.923 0.02 . 1 . . . . . . . . . 5784 1 58 . 1 1 13 13 ARG HB2 H 1 1.981 0.02 . 2 . . . . . . . . . 5784 1 59 . 1 1 13 13 ARG HB3 H 1 1.726 0.02 . 2 . . . . . . . . . 5784 1 60 . 1 1 13 13 ARG HG2 H 1 1.380 0.02 . 1 . . . . . . . . . 5784 1 61 . 1 1 14 14 HIS H H 1 8.309 0.02 . 1 . . . . . . . . . 5784 1 62 . 1 1 14 14 HIS HA H 1 5.333 0.02 . 1 . . . . . . . . . 5784 1 63 . 1 1 14 14 HIS HB2 H 1 3.232 0.02 . 2 . . . . . . . . . 5784 1 64 . 1 1 14 14 HIS HB3 H 1 2.891 0.02 . 2 . . . . . . . . . 5784 1 65 . 1 1 14 14 HIS HD2 H 1 7.063 0.02 . 1 . . . . . . . . . 5784 1 66 . 1 1 14 14 HIS HE1 H 1 7.841 0.02 . 1 . . . . . . . . . 5784 1 67 . 1 1 15 15 PRO HA H 1 4.505 0.02 . 1 . . . . . . . . . 5784 1 68 . 1 1 15 15 PRO HB2 H 1 1.922 0.02 . 2 . . . . . . . . . 5784 1 69 . 1 1 15 15 PRO HB3 H 1 2.424 0.02 . 2 . . . . . . . . . 5784 1 70 . 1 1 15 15 PRO HD2 H 1 4.069 0.02 . 2 . . . . . . . . . 5784 1 71 . 1 1 15 15 PRO HD3 H 1 3.805 0.02 . 2 . . . . . . . . . 5784 1 72 . 1 1 15 15 PRO HG2 H 1 2.066 0.02 . 2 . . . . . . . . . 5784 1 73 . 1 1 15 15 PRO HG3 H 1 2.239 0.02 . 2 . . . . . . . . . 5784 1 74 . 1 1 16 16 ALA H H 1 9.026 0.02 . 1 . . . . . . . . . 5784 1 75 . 1 1 16 16 ALA HA H 1 4.102 0.02 . 1 . . . . . . . . . 5784 1 76 . 1 1 16 16 ALA HB1 H 1 1.672 0.02 . 1 . . . . . . . . . 5784 1 77 . 1 1 16 16 ALA HB2 H 1 1.672 0.02 . 1 . . . . . . . . . 5784 1 78 . 1 1 16 16 ALA HB3 H 1 1.672 0.02 . 1 . . . . . . . . . 5784 1 79 . 1 1 17 17 GLU H H 1 8.860 0.02 . 1 . . . . . . . . . 5784 1 80 . 1 1 17 17 GLU HA H 1 4.388 0.02 . 1 . . . . . . . . . 5784 1 81 . 1 1 17 17 GLU HB2 H 1 1.847 0.02 . 1 . . . . . . . . . 5784 1 82 . 1 1 17 17 GLU HG2 H 1 2.142 0.02 . 1 . . . . . . . . . 5784 1 83 . 1 1 18 18 ASN H H 1 8.774 0.02 . 1 . . . . . . . . . 5784 1 84 . 1 1 18 18 ASN HA H 1 4.471 0.02 . 1 . . . . . . . . . 5784 1 85 . 1 1 18 18 ASN HB2 H 1 2.754 0.02 . 2 . . . . . . . . . 5784 1 86 . 1 1 18 18 ASN HB3 H 1 2.675 0.02 . 2 . . . . . . . . . 5784 1 87 . 1 1 18 18 ASN HD21 H 1 7.528 0.02 . 2 . . . . . . . . . 5784 1 88 . 1 1 18 18 ASN HD22 H 1 7.117 0.02 . 2 . . . . . . . . . 5784 1 89 . 1 1 19 19 GLY H H 1 8.819 0.02 . 1 . . . . . . . . . 5784 1 90 . 1 1 19 19 GLY HA2 H 1 4.174 0.02 . 2 . . . . . . . . . 5784 1 91 . 1 1 19 19 GLY HA3 H 1 3.514 0.02 . 2 . . . . . . . . . 5784 1 92 . 1 1 20 20 LYS H H 1 7.839 0.02 . 1 . . . . . . . . . 5784 1 93 . 1 1 20 20 LYS HA H 1 4.642 0.02 . 1 . . . . . . . . . 5784 1 94 . 1 1 20 20 LYS HB2 H 1 1.823 0.02 . 2 . . . . . . . . . 5784 1 95 . 1 1 20 20 LYS HB3 H 1 1.760 0.02 . 2 . . . . . . . . . 5784 1 96 . 1 1 20 20 LYS HD2 H 1 1.570 0.02 . 1 . . . . . . . . . 5784 1 97 . 1 1 20 20 LYS HE2 H 1 2.913 0.02 . 1 . . . . . . . . . 5784 1 98 . 1 1 20 20 LYS HG2 H 1 1.295 0.02 . 1 . . . . . . . . . 5784 1 99 . 1 1 21 21 SER H H 1 8.354 0.02 . 1 . . . . . . . . . 5784 1 100 . 1 1 21 21 SER HA H 1 4.244 0.02 . 1 . . . . . . . . . 5784 1 101 . 1 1 21 21 SER HB2 H 1 3.731 0.02 . 1 . . . . . . . . . 5784 1 102 . 1 1 22 22 ASN H H 1 8.893 0.02 . 1 . . . . . . . . . 5784 1 103 . 1 1 22 22 ASN HA H 1 4.883 0.02 . 1 . . . . . . . . . 5784 1 104 . 1 1 22 22 ASN HB2 H 1 2.536 0.02 . 2 . . . . . . . . . 5784 1 105 . 1 1 22 22 ASN HB3 H 1 2.720 0.02 . 2 . . . . . . . . . 5784 1 106 . 1 1 23 23 PHE H H 1 10.331 0.02 . 1 . . . . . . . . . 5784 1 107 . 1 1 23 23 PHE HA H 1 5.418 0.02 . 1 . . . . . . . . . 5784 1 108 . 1 1 23 23 PHE HB2 H 1 2.673 0.02 . 2 . . . . . . . . . 5784 1 109 . 1 1 23 23 PHE HB3 H 1 2.625 0.02 . 2 . . . . . . . . . 5784 1 110 . 1 1 23 23 PHE HD1 H 1 6.999 0.02 . 1 . . . . . . . . . 5784 1 111 . 1 1 23 23 PHE HE1 H 1 7.323 0.02 . 1 . . . . . . . . . 5784 1 112 . 1 1 23 23 PHE HZ H 1 7.390 0.02 . 1 . . . . . . . . . 5784 1 113 . 1 1 24 24 LEU H H 1 8.979 0.02 . 1 . . . . . . . . . 5784 1 114 . 1 1 24 24 LEU HA H 1 3.683 0.02 . 1 . . . . . . . . . 5784 1 115 . 1 1 24 24 LEU HB2 H 1 0.798 0.02 . 2 . . . . . . . . . 5784 1 116 . 1 1 24 24 LEU HB3 H 1 -0.823 0.02 . 2 . . . . . . . . . 5784 1 117 . 1 1 24 24 LEU HD11 H 1 -0.002 0.02 . 2 . . . . . . . . . 5784 1 118 . 1 1 24 24 LEU HD12 H 1 -0.002 0.02 . 2 . . . . . . . . . 5784 1 119 . 1 1 24 24 LEU HD13 H 1 -0.002 0.02 . 2 . . . . . . . . . 5784 1 120 . 1 1 24 24 LEU HD21 H 1 -0.566 0.02 . 2 . . . . . . . . . 5784 1 121 . 1 1 24 24 LEU HD22 H 1 -0.566 0.02 . 2 . . . . . . . . . 5784 1 122 . 1 1 24 24 LEU HD23 H 1 -0.566 0.02 . 2 . . . . . . . . . 5784 1 123 . 1 1 24 24 LEU HG H 1 0.653 0.02 . 1 . . . . . . . . . 5784 1 124 . 1 1 25 25 ASN H H 1 8.191 0.02 . 1 . . . . . . . . . 5784 1 125 . 1 1 25 25 ASN HA H 1 5.365 0.02 . 1 . . . . . . . . . 5784 1 126 . 1 1 25 25 ASN HB2 H 1 1.825 0.02 . 2 . . . . . . . . . 5784 1 127 . 1 1 25 25 ASN HB3 H 1 1.388 0.02 . 2 . . . . . . . . . 5784 1 128 . 1 1 26 26 CYS H H 1 9.626 0.02 . 1 . . . . . . . . . 5784 1 129 . 1 1 26 26 CYS HA H 1 5.112 0.02 . 1 . . . . . . . . . 5784 1 130 . 1 1 26 26 CYS HB2 H 1 2.521 0.02 . 2 . . . . . . . . . 5784 1 131 . 1 1 26 26 CYS HB3 H 1 3.266 0.02 . 2 . . . . . . . . . 5784 1 132 . 1 1 27 27 TYR H H 1 9.659 0.02 . 1 . . . . . . . . . 5784 1 133 . 1 1 27 27 TYR HA H 1 5.399 0.02 . 1 . . . . . . . . . 5784 1 134 . 1 1 27 27 TYR HB2 H 1 3.215 0.02 . 1 . . . . . . . . . 5784 1 135 . 1 1 27 27 TYR HD1 H 1 7.178 0.02 . 1 . . . . . . . . . 5784 1 136 . 1 1 27 27 TYR HE1 H 1 6.636 0.02 . 1 . . . . . . . . . 5784 1 137 . 1 1 28 28 VAL H H 1 8.810 0.02 . 1 . . . . . . . . . 5784 1 138 . 1 1 28 28 VAL HA H 1 5.125 0.02 . 1 . . . . . . . . . 5784 1 139 . 1 1 28 28 VAL HB H 1 1.922 0.02 . 1 . . . . . . . . . 5784 1 140 . 1 1 28 28 VAL HG11 H 1 0.732 0.02 . 2 . . . . . . . . . 5784 1 141 . 1 1 28 28 VAL HG12 H 1 0.732 0.02 . 2 . . . . . . . . . 5784 1 142 . 1 1 28 28 VAL HG13 H 1 0.732 0.02 . 2 . . . . . . . . . 5784 1 143 . 1 1 28 28 VAL HG21 H 1 0.891 0.02 . 2 . . . . . . . . . 5784 1 144 . 1 1 28 28 VAL HG22 H 1 0.891 0.02 . 2 . . . . . . . . . 5784 1 145 . 1 1 28 28 VAL HG23 H 1 0.891 0.02 . 2 . . . . . . . . . 5784 1 146 . 1 1 29 29 SER H H 1 8.987 0.02 . 1 . . . . . . . . . 5784 1 147 . 1 1 29 29 SER HA H 1 5.655 0.02 . 1 . . . . . . . . . 5784 1 148 . 1 1 29 29 SER HB2 H 1 3.810 0.02 . 2 . . . . . . . . . 5784 1 149 . 1 1 29 29 SER HB3 H 1 3.359 0.02 . 2 . . . . . . . . . 5784 1 150 . 1 1 36 36 ILE H H 1 7.943 0.02 . 1 . . . . . . . . . 5784 1 151 . 1 1 36 36 ILE HA H 1 4.559 0.02 . 1 . . . . . . . . . 5784 1 152 . 1 1 36 36 ILE HB H 1 1.349 0.02 . 1 . . . . . . . . . 5784 1 153 . 1 1 36 36 ILE HD11 H 1 -0.527 0.02 . 1 . . . . . . . . . 5784 1 154 . 1 1 36 36 ILE HD12 H 1 -0.527 0.02 . 1 . . . . . . . . . 5784 1 155 . 1 1 36 36 ILE HD13 H 1 -0.527 0.02 . 1 . . . . . . . . . 5784 1 156 . 1 1 36 36 ILE HG13 H 1 0.633 0.02 . 2 . . . . . . . . . 5784 1 157 . 1 1 36 36 ILE HG12 H 1 1.489 0.02 . 2 . . . . . . . . . 5784 1 158 . 1 1 36 36 ILE HG21 H 1 0.578 0.02 . 1 . . . . . . . . . 5784 1 159 . 1 1 36 36 ILE HG22 H 1 0.578 0.02 . 1 . . . . . . . . . 5784 1 160 . 1 1 36 36 ILE HG23 H 1 0.578 0.02 . 1 . . . . . . . . . 5784 1 161 . 1 1 37 37 GLU H H 1 8.015 0.02 . 1 . . . . . . . . . 5784 1 162 . 1 1 37 37 GLU HA H 1 4.563 0.02 . 1 . . . . . . . . . 5784 1 163 . 1 1 37 37 GLU HB2 H 1 1.897 0.02 . 2 . . . . . . . . . 5784 1 164 . 1 1 37 37 GLU HB3 H 1 1.708 0.02 . 2 . . . . . . . . . 5784 1 165 . 1 1 37 37 GLU HG3 H 1 2.032 0.02 . 1 . . . . . . . . . 5784 1 166 . 1 1 38 38 VAL H H 1 7.962 0.02 . 1 . . . . . . . . . 5784 1 167 . 1 1 38 38 VAL HA H 1 4.623 0.02 . 1 . . . . . . . . . 5784 1 168 . 1 1 38 38 VAL HB H 1 0.435 0.02 . 1 . . . . . . . . . 5784 1 169 . 1 1 38 38 VAL HG11 H 1 0.228 0.02 . 2 . . . . . . . . . 5784 1 170 . 1 1 38 38 VAL HG12 H 1 0.228 0.02 . 2 . . . . . . . . . 5784 1 171 . 1 1 38 38 VAL HG13 H 1 0.228 0.02 . 2 . . . . . . . . . 5784 1 172 . 1 1 38 38 VAL HG21 H 1 0.480 0.02 . 2 . . . . . . . . . 5784 1 173 . 1 1 38 38 VAL HG22 H 1 0.480 0.02 . 2 . . . . . . . . . 5784 1 174 . 1 1 38 38 VAL HG23 H 1 0.480 0.02 . 2 . . . . . . . . . 5784 1 175 . 1 1 39 39 ASP H H 1 8.833 0.02 . 1 . . . . . . . . . 5784 1 176 . 1 1 39 39 ASP HA H 1 4.930 0.02 . 1 . . . . . . . . . 5784 1 177 . 1 1 39 39 ASP HB2 H 1 2.365 0.02 . 2 . . . . . . . . . 5784 1 178 . 1 1 39 39 ASP HB3 H 1 2.161 0.02 . 2 . . . . . . . . . 5784 1 179 . 1 1 40 40 LEU H H 1 9.041 0.02 . 1 . . . . . . . . . 5784 1 180 . 1 1 40 40 LEU HA H 1 4.988 0.02 . 1 . . . . . . . . . 5784 1 181 . 1 1 40 40 LEU HB2 H 1 1.669 0.02 . 2 . . . . . . . . . 5784 1 182 . 1 1 40 40 LEU HB3 H 1 1.200 0.02 . 2 . . . . . . . . . 5784 1 183 . 1 1 40 40 LEU HD11 H 1 0.731 0.02 . 1 . . . . . . . . . 5784 1 184 . 1 1 40 40 LEU HD12 H 1 0.731 0.02 . 1 . . . . . . . . . 5784 1 185 . 1 1 40 40 LEU HD13 H 1 0.731 0.02 . 1 . . . . . . . . . 5784 1 186 . 1 1 41 41 LEU H H 1 8.969 0.02 . 1 . . . . . . . . . 5784 1 187 . 1 1 41 41 LEU HA H 1 4.981 0.02 . 1 . . . . . . . . . 5784 1 188 . 1 1 41 41 LEU HB2 H 1 1.558 0.02 . 2 . . . . . . . . . 5784 1 189 . 1 1 41 41 LEU HB3 H 1 0.798 0.02 . 2 . . . . . . . . . 5784 1 190 . 1 1 41 41 LEU HD11 H 1 0.377 0.02 . 2 . . . . . . . . . 5784 1 191 . 1 1 41 41 LEU HD12 H 1 0.377 0.02 . 2 . . . . . . . . . 5784 1 192 . 1 1 41 41 LEU HD13 H 1 0.377 0.02 . 2 . . . . . . . . . 5784 1 193 . 1 1 41 41 LEU HD21 H 1 0.577 0.02 . 2 . . . . . . . . . 5784 1 194 . 1 1 41 41 LEU HD22 H 1 0.577 0.02 . 2 . . . . . . . . . 5784 1 195 . 1 1 41 41 LEU HD23 H 1 0.577 0.02 . 2 . . . . . . . . . 5784 1 196 . 1 1 41 41 LEU HG H 1 1.191 0.02 . 1 . . . . . . . . . 5784 1 197 . 1 1 42 42 LYS H H 1 8.819 0.02 . 1 . . . . . . . . . 5784 1 198 . 1 1 42 42 LYS HA H 1 4.404 0.02 . 1 . . . . . . . . . 5784 1 199 . 1 1 42 42 LYS HB2 H 1 1.717 0.02 . 2 . . . . . . . . . 5784 1 200 . 1 1 42 42 LYS HG2 H 1 0.574 0.02 . 2 . . . . . . . . . 5784 1 201 . 1 1 43 43 ASN H H 1 9.721 0.02 . 1 . . . . . . . . . 5784 1 202 . 1 1 43 43 ASN HA H 1 4.339 0.02 . 1 . . . . . . . . . 5784 1 203 . 1 1 43 43 ASN HB2 H 1 2.861 0.02 . 2 . . . . . . . . . 5784 1 204 . 1 1 43 43 ASN HB3 H 1 2.919 0.02 . 2 . . . . . . . . . 5784 1 205 . 1 1 43 43 ASN HD21 H 1 7.704 0.02 . 2 . . . . . . . . . 5784 1 206 . 1 1 43 43 ASN HD22 H 1 7.969 0.02 . 2 . . . . . . . . . 5784 1 207 . 1 1 44 44 GLY H H 1 8.797 0.02 . 1 . . . . . . . . . 5784 1 208 . 1 1 44 44 GLY HA2 H 1 3.302 0.02 . 2 . . . . . . . . . 5784 1 209 . 1 1 44 44 GLY HA3 H 1 4.151 0.02 . 2 . . . . . . . . . 5784 1 210 . 1 1 45 45 GLU H H 1 7.806 0.02 . 1 . . . . . . . . . 5784 1 211 . 1 1 45 45 GLU HA H 1 4.563 0.02 . 1 . . . . . . . . . 5784 1 212 . 1 1 45 45 GLU HB2 H 1 1.931 0.02 . 2 . . . . . . . . . 5784 1 213 . 1 1 45 45 GLU HB3 H 1 2.018 0.02 . 2 . . . . . . . . . 5784 1 214 . 1 1 45 45 GLU HG2 H 1 2.150 0.02 . 2 . . . . . . . . . 5784 1 215 . 1 1 45 45 GLU HG3 H 1 2.276 0.02 . 2 . . . . . . . . . 5784 1 216 . 1 1 46 46 ARG H H 1 8.654 0.02 . 1 . . . . . . . . . 5784 1 217 . 1 1 46 46 ARG HA H 1 4.150 0.02 . 1 . . . . . . . . . 5784 1 218 . 1 1 46 46 ARG HB2 H 1 1.607 0.02 . 1 . . . . . . . . . 5784 1 219 . 1 1 46 46 ARG HD2 H 1 3.103 0.02 . 1 . . . . . . . . . 5784 1 220 . 1 1 46 46 ARG HD3 H 1 3.057 0.02 . 1 . . . . . . . . . 5784 1 221 . 1 1 46 46 ARG HG2 H 1 1.528 0.02 . 2 . . . . . . . . . 5784 1 222 . 1 1 46 46 ARG HG3 H 1 1.320 0.02 . 2 . . . . . . . . . 5784 1 223 . 1 1 47 47 ILE H H 1 8.795 0.02 . 1 . . . . . . . . . 5784 1 224 . 1 1 47 47 ILE HA H 1 3.966 0.02 . 1 . . . . . . . . . 5784 1 225 . 1 1 47 47 ILE HB H 1 1.518 0.02 . 1 . . . . . . . . . 5784 1 226 . 1 1 47 47 ILE HD11 H 1 0.837 0.02 . 1 . . . . . . . . . 5784 1 227 . 1 1 47 47 ILE HD12 H 1 0.837 0.02 . 1 . . . . . . . . . 5784 1 228 . 1 1 47 47 ILE HD13 H 1 0.837 0.02 . 1 . . . . . . . . . 5784 1 229 . 1 1 47 47 ILE HG13 H 1 1.052 0.02 . 2 . . . . . . . . . 5784 1 230 . 1 1 47 47 ILE HG12 H 1 1.689 0.02 . 2 . . . . . . . . . 5784 1 231 . 1 1 47 47 ILE HG21 H 1 0.946 0.02 . 1 . . . . . . . . . 5784 1 232 . 1 1 47 47 ILE HG22 H 1 0.946 0.02 . 1 . . . . . . . . . 5784 1 233 . 1 1 47 47 ILE HG23 H 1 0.946 0.02 . 1 . . . . . . . . . 5784 1 234 . 1 1 48 48 GLU H H 1 8.482 0.02 . 1 . . . . . . . . . 5784 1 235 . 1 1 48 48 GLU HA H 1 4.163 0.02 . 1 . . . . . . . . . 5784 1 236 . 1 1 48 48 GLU HB2 H 1 2.073 0.02 . 2 . . . . . . . . . 5784 1 237 . 1 1 48 48 GLU HB3 H 1 1.997 0.02 . 2 . . . . . . . . . 5784 1 238 . 1 1 48 48 GLU HG2 H 1 2.221 0.02 . 2 . . . . . . . . . 5784 1 239 . 1 1 48 48 GLU HG3 H 1 2.355 0.02 . 2 . . . . . . . . . 5784 1 240 . 1 1 49 49 LYS H H 1 7.960 0.02 . 1 . . . . . . . . . 5784 1 241 . 1 1 49 49 LYS HA H 1 4.508 0.02 . 1 . . . . . . . . . 5784 1 242 . 1 1 49 49 LYS HB2 H 1 1.927 0.02 . 2 . . . . . . . . . 5784 1 243 . 1 1 49 49 LYS HB3 H 1 1.767 0.02 . 2 . . . . . . . . . 5784 1 244 . 1 1 49 49 LYS HE2 H 1 3.119 0.02 . 2 . . . . . . . . . 5784 1 245 . 1 1 49 49 LYS HE3 H 1 3.022 0.02 . 2 . . . . . . . . . 5784 1 246 . 1 1 49 49 LYS HG2 H 1 1.377 0.02 . 2 . . . . . . . . . 5784 1 247 . 1 1 49 49 LYS HG3 H 1 1.439 0.02 . 2 . . . . . . . . . 5784 1 248 . 1 1 50 50 VAL H H 1 7.804 0.02 . 1 . . . . . . . . . 5784 1 249 . 1 1 50 50 VAL HA H 1 4.395 0.02 . 1 . . . . . . . . . 5784 1 250 . 1 1 50 50 VAL HB H 1 2.099 0.02 . 1 . . . . . . . . . 5784 1 251 . 1 1 50 50 VAL HG11 H 1 1.011 0.02 . 2 . . . . . . . . . 5784 1 252 . 1 1 50 50 VAL HG12 H 1 1.011 0.02 . 2 . . . . . . . . . 5784 1 253 . 1 1 50 50 VAL HG13 H 1 1.011 0.02 . 2 . . . . . . . . . 5784 1 254 . 1 1 50 50 VAL HG21 H 1 1.071 0.02 . 2 . . . . . . . . . 5784 1 255 . 1 1 50 50 VAL HG22 H 1 1.071 0.02 . 2 . . . . . . . . . 5784 1 256 . 1 1 50 50 VAL HG23 H 1 1.071 0.02 . 2 . . . . . . . . . 5784 1 257 . 1 1 51 51 GLU H H 1 8.428 0.02 . 1 . . . . . . . . . 5784 1 258 . 1 1 51 51 GLU HA H 1 4.462 0.02 . 1 . . . . . . . . . 5784 1 259 . 1 1 51 51 GLU HB2 H 1 0.735 0.02 . 2 . . . . . . . . . 5784 1 260 . 1 1 51 51 GLU HB3 H 1 1.547 0.02 . 2 . . . . . . . . . 5784 1 261 . 1 1 51 51 GLU HG2 H 1 2.049 0.02 . 1 . . . . . . . . . 5784 1 262 . 1 1 52 52 HIS H H 1 8.087 0.02 . 1 . . . . . . . . . 5784 1 263 . 1 1 52 52 HIS HA H 1 5.479 0.02 . 1 . . . . . . . . . 5784 1 264 . 1 1 52 52 HIS HB2 H 1 2.417 0.02 . 2 . . . . . . . . . 5784 1 265 . 1 1 52 52 HIS HB3 H 1 1.956 0.02 . 2 . . . . . . . . . 5784 1 266 . 1 1 52 52 HIS HD2 H 1 6.972 0.02 . 1 . . . . . . . . . 5784 1 267 . 1 1 52 52 HIS HE1 H 1 8.474 0.02 . 1 . . . . . . . . . 5784 1 268 . 1 1 53 53 SER H H 1 9.142 0.02 . 1 . . . . . . . . . 5784 1 269 . 1 1 53 53 SER HA H 1 4.671 0.02 . 1 . . . . . . . . . 5784 1 270 . 1 1 53 53 SER HB2 H 1 4.483 0.02 . 2 . . . . . . . . . 5784 1 271 . 1 1 53 53 SER HB3 H 1 4.083 0.02 . 2 . . . . . . . . . 5784 1 272 . 1 1 54 54 ASP H H 1 8.679 0.02 . 1 . . . . . . . . . 5784 1 273 . 1 1 54 54 ASP HA H 1 4.786 0.02 . 1 . . . . . . . . . 5784 1 274 . 1 1 54 54 ASP HB2 H 1 2.715 0.02 . 2 . . . . . . . . . 5784 1 275 . 1 1 54 54 ASP HB3 H 1 2.567 0.02 . 2 . . . . . . . . . 5784 1 276 . 1 1 55 55 LEU H H 1 8.721 0.02 . 1 . . . . . . . . . 5784 1 277 . 1 1 55 55 LEU HA H 1 4.338 0.02 . 1 . . . . . . . . . 5784 1 278 . 1 1 55 55 LEU HB2 H 1 1.843 0.02 . 1 . . . . . . . . . 5784 1 279 . 1 1 55 55 LEU HD11 H 1 1.058 0.02 . 2 . . . . . . . . . 5784 1 280 . 1 1 55 55 LEU HD12 H 1 1.058 0.02 . 2 . . . . . . . . . 5784 1 281 . 1 1 55 55 LEU HD13 H 1 1.058 0.02 . 2 . . . . . . . . . 5784 1 282 . 1 1 55 55 LEU HD21 H 1 0.937 0.02 . 2 . . . . . . . . . 5784 1 283 . 1 1 55 55 LEU HD22 H 1 0.937 0.02 . 2 . . . . . . . . . 5784 1 284 . 1 1 55 55 LEU HD23 H 1 0.937 0.02 . 2 . . . . . . . . . 5784 1 285 . 1 1 55 55 LEU HG H 1 1.672 0.02 . 1 . . . . . . . . . 5784 1 286 . 1 1 56 56 SER H H 1 8.103 0.02 . 1 . . . . . . . . . 5784 1 287 . 1 1 56 56 SER HA H 1 4.798 0.02 . 1 . . . . . . . . . 5784 1 288 . 1 1 56 56 SER HB2 H 1 3.390 0.02 . 2 . . . . . . . . . 5784 1 289 . 1 1 56 56 SER HB3 H 1 2.685 0.02 . 2 . . . . . . . . . 5784 1 290 . 1 1 57 57 PHE H H 1 8.183 0.02 . 1 . . . . . . . . . 5784 1 291 . 1 1 57 57 PHE HA H 1 4.990 0.02 . 1 . . . . . . . . . 5784 1 292 . 1 1 57 57 PHE HB2 H 1 2.591 0.02 . 1 . . . . . . . . . 5784 1 293 . 1 1 57 57 PHE HD1 H 1 6.303 0.02 . 1 . . . . . . . . . 5784 1 294 . 1 1 57 57 PHE HE1 H 1 6.879 0.02 . 1 . . . . . . . . . 5784 1 295 . 1 1 57 57 PHE HZ H 1 6.818 0.02 . 1 . . . . . . . . . 5784 1 296 . 1 1 59 59 LYS HA H 1 3.747 0.02 . 1 . . . . . . . . . 5784 1 297 . 1 1 59 59 LYS HB2 H 1 1.714 0.02 . 1 . . . . . . . . . 5784 1 298 . 1 1 59 59 LYS HD2 H 1 1.615 0.02 . 1 . . . . . . . . . 5784 1 299 . 1 1 59 59 LYS HE2 H 1 2.948 0.02 . 1 . . . . . . . . . 5784 1 300 . 1 1 59 59 LYS HG2 H 1 1.374 0.02 . 1 . . . . . . . . . 5784 1 301 . 1 1 60 60 ASP H H 1 7.655 0.02 . 1 . . . . . . . . . 5784 1 302 . 1 1 60 60 ASP HA H 1 4.347 0.02 . 1 . . . . . . . . . 5784 1 303 . 1 1 60 60 ASP HB2 H 1 2.294 0.02 . 1 . . . . . . . . . 5784 1 304 . 1 1 63 63 PHE HA H 1 5.322 0.02 . 1 . . . . . . . . . 5784 1 305 . 1 1 63 63 PHE HB2 H 1 2.413 0.02 . 2 . . . . . . . . . 5784 1 306 . 1 1 63 63 PHE HB3 H 1 1.524 0.02 . 2 . . . . . . . . . 5784 1 307 . 1 1 63 63 PHE HD1 H 1 7.305 0.02 . 1 . . . . . . . . . 5784 1 308 . 1 1 63 63 PHE HE1 H 1 7.215 0.02 . 1 . . . . . . . . . 5784 1 309 . 1 1 64 64 TYR H H 1 8.226 0.02 . 1 . . . . . . . . . 5784 1 310 . 1 1 64 64 TYR HA H 1 5.513 0.02 . 1 . . . . . . . . . 5784 1 311 . 1 1 64 64 TYR HB2 H 1 3.034 0.02 . 2 . . . . . . . . . 5784 1 312 . 1 1 64 64 TYR HB3 H 1 2.834 0.02 . 2 . . . . . . . . . 5784 1 313 . 1 1 64 64 TYR HD1 H 1 7.039 0.02 . 1 . . . . . . . . . 5784 1 314 . 1 1 64 64 TYR HE1 H 1 6.640 0.02 . 1 . . . . . . . . . 5784 1 315 . 1 1 65 65 LEU H H 1 9.174 0.02 . 1 . . . . . . . . . 5784 1 316 . 1 1 65 65 LEU HA H 1 4.632 0.02 . 1 . . . . . . . . . 5784 1 317 . 1 1 65 65 LEU HB2 H 1 2.026 0.02 . 1 . . . . . . . . . 5784 1 318 . 1 1 65 65 LEU HD11 H 1 1.049 0.02 . 2 . . . . . . . . . 5784 1 319 . 1 1 65 65 LEU HD12 H 1 1.049 0.02 . 2 . . . . . . . . . 5784 1 320 . 1 1 65 65 LEU HD13 H 1 1.049 0.02 . 2 . . . . . . . . . 5784 1 321 . 1 1 65 65 LEU HD21 H 1 0.954 0.02 . 2 . . . . . . . . . 5784 1 322 . 1 1 65 65 LEU HD22 H 1 0.954 0.02 . 2 . . . . . . . . . 5784 1 323 . 1 1 65 65 LEU HD23 H 1 0.954 0.02 . 2 . . . . . . . . . 5784 1 324 . 1 1 65 65 LEU HG H 1 1.771 0.02 . 1 . . . . . . . . . 5784 1 325 . 1 1 66 66 LEU H H 1 8.136 0.02 . 1 . . . . . . . . . 5784 1 326 . 1 1 66 66 LEU HA H 1 5.461 0.02 . 1 . . . . . . . . . 5784 1 327 . 1 1 66 66 LEU HB3 H 1 1.957 0.02 . 1 . . . . . . . . . 5784 1 328 . 1 1 66 66 LEU HD11 H 1 1.047 0.02 . 2 . . . . . . . . . 5784 1 329 . 1 1 66 66 LEU HD12 H 1 1.047 0.02 . 2 . . . . . . . . . 5784 1 330 . 1 1 66 66 LEU HD13 H 1 1.047 0.02 . 2 . . . . . . . . . 5784 1 331 . 1 1 66 66 LEU HD21 H 1 0.783 0.02 . 2 . . . . . . . . . 5784 1 332 . 1 1 66 66 LEU HD22 H 1 0.783 0.02 . 2 . . . . . . . . . 5784 1 333 . 1 1 66 66 LEU HD23 H 1 0.783 0.02 . 2 . . . . . . . . . 5784 1 334 . 1 1 66 66 LEU HG H 1 1.569 0.02 . 1 . . . . . . . . . 5784 1 335 . 1 1 67 67 TYR H H 1 9.097 0.02 . 1 . . . . . . . . . 5784 1 336 . 1 1 67 67 TYR HA H 1 5.346 0.02 . 1 . . . . . . . . . 5784 1 337 . 1 1 67 67 TYR HB2 H 1 2.662 0.02 . 2 . . . . . . . . . 5784 1 338 . 1 1 67 67 TYR HB3 H 1 3.036 0.02 . 2 . . . . . . . . . 5784 1 339 . 1 1 67 67 TYR HD1 H 1 6.968 0.02 . 1 . . . . . . . . . 5784 1 340 . 1 1 67 67 TYR HE1 H 1 6.643 0.02 . 1 . . . . . . . . . 5784 1 341 . 1 1 68 68 TYR H H 1 8.919 0.02 . 1 . . . . . . . . . 5784 1 342 . 1 1 68 68 TYR HA H 1 5.940 0.02 . 1 . . . . . . . . . 5784 1 343 . 1 1 68 68 TYR HB2 H 1 2.648 0.02 . 2 . . . . . . . . . 5784 1 344 . 1 1 68 68 TYR HB3 H 1 3.217 0.02 . 2 . . . . . . . . . 5784 1 345 . 1 1 68 68 TYR HD1 H 1 6.678 0.02 . 1 . . . . . . . . . 5784 1 346 . 1 1 68 68 TYR HE1 H 1 6.529 0.02 . 1 . . . . . . . . . 5784 1 347 . 1 1 69 69 THR H H 1 8.299 0.02 . 1 . . . . . . . . . 5784 1 348 . 1 1 69 69 THR HA H 1 4.844 0.02 . 1 . . . . . . . . . 5784 1 349 . 1 1 69 69 THR HB H 1 4.099 0.02 . 1 . . . . . . . . . 5784 1 350 . 1 1 69 69 THR HG21 H 1 0.930 0.02 . 1 . . . . . . . . . 5784 1 351 . 1 1 69 69 THR HG22 H 1 0.930 0.02 . 1 . . . . . . . . . 5784 1 352 . 1 1 69 69 THR HG23 H 1 0.930 0.02 . 1 . . . . . . . . . 5784 1 353 . 1 1 70 70 GLU H H 1 8.481 0.02 . 1 . . . . . . . . . 5784 1 354 . 1 1 70 70 GLU HA H 1 4.289 0.02 . 1 . . . . . . . . . 5784 1 355 . 1 1 70 70 GLU HB2 H 1 1.810 0.02 . 2 . . . . . . . . . 5784 1 356 . 1 1 70 70 GLU HB3 H 1 1.695 0.02 . 2 . . . . . . . . . 5784 1 357 . 1 1 70 70 GLU HG2 H 1 1.868 0.02 . 1 . . . . . . . . . 5784 1 358 . 1 1 71 71 PHE H H 1 8.736 0.02 . 1 . . . . . . . . . 5784 1 359 . 1 1 71 71 PHE HA H 1 4.818 0.02 . 1 . . . . . . . . . 5784 1 360 . 1 1 71 71 PHE HB2 H 1 2.788 0.02 . 2 . . . . . . . . . 5784 1 361 . 1 1 71 71 PHE HB3 H 1 2.687 0.02 . 2 . . . . . . . . . 5784 1 362 . 1 1 71 71 PHE HD1 H 1 6.187 0.02 . 1 . . . . . . . . . 5784 1 363 . 1 1 71 71 PHE HZ H 1 5.694 0.02 . 1 . . . . . . . . . 5784 1 364 . 1 1 72 72 THR H H 1 8.213 0.02 . 1 . . . . . . . . . 5784 1 365 . 1 1 72 72 THR HA H 1 4.456 0.02 . 1 . . . . . . . . . 5784 1 366 . 1 1 72 72 THR HB H 1 3.857 0.02 . 1 . . . . . . . . . 5784 1 367 . 1 1 72 72 THR HG21 H 1 0.842 0.02 . 1 . . . . . . . . . 5784 1 368 . 1 1 72 72 THR HG22 H 1 0.842 0.02 . 1 . . . . . . . . . 5784 1 369 . 1 1 72 72 THR HG23 H 1 0.842 0.02 . 1 . . . . . . . . . 5784 1 370 . 1 1 73 73 PRO HA H 1 4.571 0.02 . 1 . . . . . . . . . 5784 1 371 . 1 1 73 73 PRO HB2 H 1 2.131 0.02 . 2 . . . . . . . . . 5784 1 372 . 1 1 73 73 PRO HB3 H 1 2.388 0.02 . 2 . . . . . . . . . 5784 1 373 . 1 1 73 73 PRO HD2 H 1 2.216 0.02 . 2 . . . . . . . . . 5784 1 374 . 1 1 73 73 PRO HD3 H 1 3.958 0.02 . 2 . . . . . . . . . 5784 1 375 . 1 1 73 73 PRO HG2 H 1 1.978 0.02 . 2 . . . . . . . . . 5784 1 376 . 1 1 73 73 PRO HG3 H 1 1.400 0.02 . 2 . . . . . . . . . 5784 1 377 . 1 1 74 74 THR H H 1 8.041 0.02 . 1 . . . . . . . . . 5784 1 378 . 1 1 74 74 THR HA H 1 4.663 0.02 . 1 . . . . . . . . . 5784 1 379 . 1 1 74 74 THR HB H 1 4.528 0.02 . 1 . . . . . . . . . 5784 1 380 . 1 1 74 74 THR HG21 H 1 1.306 0.02 . 1 . . . . . . . . . 5784 1 381 . 1 1 74 74 THR HG22 H 1 1.306 0.02 . 1 . . . . . . . . . 5784 1 382 . 1 1 74 74 THR HG23 H 1 1.306 0.02 . 1 . . . . . . . . . 5784 1 383 . 1 1 75 75 GLU H H 1 9.070 0.02 . 1 . . . . . . . . . 5784 1 384 . 1 1 75 75 GLU HA H 1 4.192 0.02 . 1 . . . . . . . . . 5784 1 385 . 1 1 75 75 GLU HB2 H 1 2.057 0.02 . 1 . . . . . . . . . 5784 1 386 . 1 1 75 75 GLU HG2 H 1 2.260 0.02 . 2 . . . . . . . . . 5784 1 387 . 1 1 75 75 GLU HG3 H 1 2.326 0.02 . 2 . . . . . . . . . 5784 1 388 . 1 1 76 76 LYS H H 1 7.789 0.02 . 1 . . . . . . . . . 5784 1 389 . 1 1 76 76 LYS HA H 1 4.434 0.02 . 1 . . . . . . . . . 5784 1 390 . 1 1 76 76 LYS HB2 H 1 1.851 0.02 . 2 . . . . . . . . . 5784 1 391 . 1 1 76 76 LYS HB3 H 1 1.761 0.02 . 2 . . . . . . . . . 5784 1 392 . 1 1 76 76 LYS HD2 H 1 1.647 0.02 . 1 . . . . . . . . . 5784 1 393 . 1 1 76 76 LYS HE2 H 1 2.968 0.02 . 1 . . . . . . . . . 5784 1 394 . 1 1 76 76 LYS HG2 H 1 1.381 0.02 . 1 . . . . . . . . . 5784 1 395 . 1 1 77 77 ASP H H 1 7.105 0.02 . 1 . . . . . . . . . 5784 1 396 . 1 1 77 77 ASP HA H 1 5.111 0.02 . 1 . . . . . . . . . 5784 1 397 . 1 1 77 77 ASP HB2 H 1 2.801 0.02 . 2 . . . . . . . . . 5784 1 398 . 1 1 77 77 ASP HB3 H 1 2.141 0.02 . 2 . . . . . . . . . 5784 1 399 . 1 1 78 78 GLU H H 1 8.595 0.02 . 1 . . . . . . . . . 5784 1 400 . 1 1 78 78 GLU HA H 1 4.786 0.02 . 1 . . . . . . . . . 5784 1 401 . 1 1 78 78 GLU HB2 H 1 1.968 0.02 . 2 . . . . . . . . . 5784 1 402 . 1 1 78 78 GLU HB3 H 1 2.066 0.02 . 2 . . . . . . . . . 5784 1 403 . 1 1 78 78 GLU HG3 H 1 2.354 0.02 . 1 . . . . . . . . . 5784 1 404 . 1 1 79 79 TYR H H 1 9.476 0.02 . 1 . . . . . . . . . 5784 1 405 . 1 1 79 79 TYR HA H 1 5.589 0.02 . 1 . . . . . . . . . 5784 1 406 . 1 1 79 79 TYR HB2 H 1 2.810 0.02 . 2 . . . . . . . . . 5784 1 407 . 1 1 79 79 TYR HB3 H 1 2.715 0.02 . 2 . . . . . . . . . 5784 1 408 . 1 1 79 79 TYR HD1 H 1 7.072 0.02 . 1 . . . . . . . . . 5784 1 409 . 1 1 79 79 TYR HE1 H 1 6.874 0.02 . 1 . . . . . . . . . 5784 1 410 . 1 1 80 80 ALA H H 1 8.781 0.02 . 1 . . . . . . . . . 5784 1 411 . 1 1 80 80 ALA HA H 1 5.027 0.02 . 1 . . . . . . . . . 5784 1 412 . 1 1 80 80 ALA HB1 H 1 1.184 0.02 . 1 . . . . . . . . . 5784 1 413 . 1 1 80 80 ALA HB2 H 1 1.184 0.02 . 1 . . . . . . . . . 5784 1 414 . 1 1 80 80 ALA HB3 H 1 1.184 0.02 . 1 . . . . . . . . . 5784 1 415 . 1 1 81 81 CYS H H 1 9.096 0.02 . 1 . . . . . . . . . 5784 1 416 . 1 1 81 81 CYS HA H 1 5.105 0.02 . 1 . . . . . . . . . 5784 1 417 . 1 1 81 81 CYS HB2 H 1 2.613 0.02 . 2 . . . . . . . . . 5784 1 418 . 1 1 81 81 CYS HB3 H 1 3.036 0.02 . 2 . . . . . . . . . 5784 1 419 . 1 1 82 82 ARG H H 1 9.386 0.02 . 1 . . . . . . . . . 5784 1 420 . 1 1 82 82 ARG HA H 1 5.375 0.02 . 1 . . . . . . . . . 5784 1 421 . 1 1 82 82 ARG HB2 H 1 1.784 0.02 . 2 . . . . . . . . . 5784 1 422 . 1 1 82 82 ARG HB3 H 1 1.171 0.02 . 2 . . . . . . . . . 5784 1 423 . 1 1 83 83 VAL H H 1 9.013 0.02 . 1 . . . . . . . . . 5784 1 424 . 1 1 83 83 VAL HA H 1 4.960 0.02 . 1 . . . . . . . . . 5784 1 425 . 1 1 83 83 VAL HB H 1 1.665 0.02 . 1 . . . . . . . . . 5784 1 426 . 1 1 83 83 VAL HG11 H 1 0.576 0.02 . 2 . . . . . . . . . 5784 1 427 . 1 1 83 83 VAL HG12 H 1 0.576 0.02 . 2 . . . . . . . . . 5784 1 428 . 1 1 83 83 VAL HG13 H 1 0.576 0.02 . 2 . . . . . . . . . 5784 1 429 . 1 1 83 83 VAL HG21 H 1 0.787 0.02 . 2 . . . . . . . . . 5784 1 430 . 1 1 83 83 VAL HG22 H 1 0.787 0.02 . 2 . . . . . . . . . 5784 1 431 . 1 1 83 83 VAL HG23 H 1 0.787 0.02 . 2 . . . . . . . . . 5784 1 432 . 1 1 84 84 ASN H H 1 8.998 0.02 . 1 . . . . . . . . . 5784 1 433 . 1 1 84 84 ASN HA H 1 5.170 0.02 . 1 . . . . . . . . . 5784 1 434 . 1 1 84 84 ASN HB2 H 1 2.795 0.02 . 2 . . . . . . . . . 5784 1 435 . 1 1 84 84 ASN HB3 H 1 2.368 0.02 . 2 . . . . . . . . . 5784 1 436 . 1 1 84 84 ASN HD21 H 1 7.378 0.02 . 2 . . . . . . . . . 5784 1 437 . 1 1 84 84 ASN HD22 H 1 6.610 0.02 . 2 . . . . . . . . . 5784 1 438 . 1 1 85 85 HIS H H 1 7.723 0.02 . 1 . . . . . . . . . 5784 1 439 . 1 1 85 85 HIS HA H 1 4.531 0.02 . 1 . . . . . . . . . 5784 1 440 . 1 1 85 85 HIS HB2 H 1 2.878 0.02 . 2 . . . . . . . . . 5784 1 441 . 1 1 85 85 HIS HB3 H 1 2.382 0.02 . 2 . . . . . . . . . 5784 1 442 . 1 1 85 85 HIS HD2 H 1 7.517 0.02 . 1 . . . . . . . . . 5784 1 443 . 1 1 85 85 HIS HE1 H 1 8.017 0.02 . 1 . . . . . . . . . 5784 1 444 . 1 1 86 86 VAL H H 1 8.023 0.02 . 1 . . . . . . . . . 5784 1 445 . 1 1 86 86 VAL HA H 1 3.959 0.02 . 1 . . . . . . . . . 5784 1 446 . 1 1 86 86 VAL HB H 1 1.917 0.02 . 1 . . . . . . . . . 5784 1 447 . 1 1 86 86 VAL HG11 H 1 0.529 0.02 . 2 . . . . . . . . . 5784 1 448 . 1 1 86 86 VAL HG12 H 1 0.529 0.02 . 2 . . . . . . . . . 5784 1 449 . 1 1 86 86 VAL HG13 H 1 0.529 0.02 . 2 . . . . . . . . . 5784 1 450 . 1 1 86 86 VAL HG21 H 1 0.836 0.02 . 2 . . . . . . . . . 5784 1 451 . 1 1 86 86 VAL HG22 H 1 0.836 0.02 . 2 . . . . . . . . . 5784 1 452 . 1 1 86 86 VAL HG23 H 1 0.836 0.02 . 2 . . . . . . . . . 5784 1 453 . 1 1 87 87 THR H H 1 7.528 0.02 . 1 . . . . . . . . . 5784 1 454 . 1 1 87 87 THR HA H 1 4.122 0.02 . 1 . . . . . . . . . 5784 1 455 . 1 1 87 87 THR HB H 1 4.480 0.02 . 1 . . . . . . . . . 5784 1 456 . 1 1 87 87 THR HG1 H 1 7.653 0.02 . 1 . . . . . . . . . 5784 1 457 . 1 1 87 87 THR HG21 H 1 1.441 0.02 . 1 . . . . . . . . . 5784 1 458 . 1 1 87 87 THR HG22 H 1 1.441 0.02 . 1 . . . . . . . . . 5784 1 459 . 1 1 87 87 THR HG23 H 1 1.441 0.02 . 1 . . . . . . . . . 5784 1 460 . 1 1 88 88 LEU H H 1 8.013 0.02 . 1 . . . . . . . . . 5784 1 461 . 1 1 88 88 LEU HA H 1 4.739 0.02 . 1 . . . . . . . . . 5784 1 462 . 1 1 88 88 LEU HB2 H 1 2.010 0.02 . 1 . . . . . . . . . 5784 1 463 . 1 1 88 88 LEU HD11 H 1 0.933 0.02 . 1 . . . . . . . . . 5784 1 464 . 1 1 88 88 LEU HD12 H 1 0.933 0.02 . 1 . . . . . . . . . 5784 1 465 . 1 1 88 88 LEU HD13 H 1 0.933 0.02 . 1 . . . . . . . . . 5784 1 466 . 1 1 88 88 LEU HG H 1 1.695 0.02 . 1 . . . . . . . . . 5784 1 467 . 1 1 89 89 SER HA H 1 4.233 0.02 . 1 . . . . . . . . . 5784 1 468 . 1 1 89 89 SER HB2 H 1 3.951 0.02 . 1 . . . . . . . . . 5784 1 469 . 1 1 90 90 GLN H H 1 7.525 0.02 . 1 . . . . . . . . . 5784 1 470 . 1 1 90 90 GLN HA H 1 4.723 0.02 . 1 . . . . . . . . . 5784 1 471 . 1 1 90 90 GLN HB2 H 1 2.143 0.02 . 2 . . . . . . . . . 5784 1 472 . 1 1 90 90 GLN HB3 H 1 1.871 0.02 . 2 . . . . . . . . . 5784 1 473 . 1 1 90 90 GLN HG2 H 1 2.269 0.02 . 2 . . . . . . . . . 5784 1 474 . 1 1 90 90 GLN HG3 H 1 2.013 0.02 . 2 . . . . . . . . . 5784 1 475 . 1 1 91 91 PRO HA H 1 4.478 0.02 . 1 . . . . . . . . . 5784 1 476 . 1 1 91 91 PRO HB2 H 1 1.859 0.02 . 2 . . . . . . . . . 5784 1 477 . 1 1 91 91 PRO HB3 H 1 1.437 0.02 . 2 . . . . . . . . . 5784 1 478 . 1 1 91 91 PRO HD2 H 1 3.715 0.02 . 2 . . . . . . . . . 5784 1 479 . 1 1 91 91 PRO HD3 H 1 3.502 0.02 . 2 . . . . . . . . . 5784 1 480 . 1 1 91 91 PRO HG2 H 1 1.980 0.02 . 2 . . . . . . . . . 5784 1 481 . 1 1 91 91 PRO HG3 H 1 1.772 0.02 . 2 . . . . . . . . . 5784 1 482 . 1 1 92 92 LYS H H 1 8.715 0.02 . 1 . . . . . . . . . 5784 1 483 . 1 1 92 92 LYS HA H 1 4.500 0.02 . 1 . . . . . . . . . 5784 1 484 . 1 1 92 92 LYS HB2 H 1 1.699 0.02 . 2 . . . . . . . . . 5784 1 485 . 1 1 92 92 LYS HB3 H 1 1.620 0.02 . 2 . . . . . . . . . 5784 1 486 . 1 1 92 92 LYS HG2 H 1 1.396 0.02 . 2 . . . . . . . . . 5784 1 487 . 1 1 92 92 LYS HG3 H 1 1.305 0.02 . 2 . . . . . . . . . 5784 1 488 . 1 1 93 93 ILE H H 1 8.482 0.02 . 1 . . . . . . . . . 5784 1 489 . 1 1 93 93 ILE HA H 1 4.782 0.02 . 1 . . . . . . . . . 5784 1 490 . 1 1 93 93 ILE HB H 1 1.681 0.02 . 1 . . . . . . . . . 5784 1 491 . 1 1 93 93 ILE HG21 H 1 0.601 0.02 . 1 . . . . . . . . . 5784 1 492 . 1 1 93 93 ILE HG22 H 1 0.601 0.02 . 1 . . . . . . . . . 5784 1 493 . 1 1 93 93 ILE HG23 H 1 0.601 0.02 . 1 . . . . . . . . . 5784 1 494 . 1 1 93 93 ILE HD11 H 1 0.731 0.02 . 1 . . . . . . . . . 5784 1 495 . 1 1 93 93 ILE HD12 H 1 0.731 0.02 . 1 . . . . . . . . . 5784 1 496 . 1 1 93 93 ILE HD13 H 1 0.731 0.02 . 1 . . . . . . . . . 5784 1 497 . 1 1 93 93 ILE HG12 H 1 1.404 0.02 . 1 . . . . . . . . . 5784 1 498 . 1 1 94 94 VAL H H 1 9.039 0.02 . 1 . . . . . . . . . 5784 1 499 . 1 1 94 94 VAL HA H 1 4.305 0.02 . 1 . . . . . . . . . 5784 1 500 . 1 1 94 94 VAL HB H 1 1.865 0.02 . 1 . . . . . . . . . 5784 1 501 . 1 1 94 94 VAL HG11 H 1 0.907 0.02 . 2 . . . . . . . . . 5784 1 502 . 1 1 94 94 VAL HG12 H 1 0.907 0.02 . 2 . . . . . . . . . 5784 1 503 . 1 1 94 94 VAL HG13 H 1 0.907 0.02 . 2 . . . . . . . . . 5784 1 504 . 1 1 94 94 VAL HG21 H 1 1.022 0.02 . 2 . . . . . . . . . 5784 1 505 . 1 1 94 94 VAL HG22 H 1 1.022 0.02 . 2 . . . . . . . . . 5784 1 506 . 1 1 94 94 VAL HG23 H 1 1.022 0.02 . 2 . . . . . . . . . 5784 1 507 . 1 1 95 95 LYS H H 1 8.784 0.02 . 1 . . . . . . . . . 5784 1 508 . 1 1 95 95 LYS HA H 1 4.435 0.02 . 1 . . . . . . . . . 5784 1 509 . 1 1 95 95 LYS HB2 H 1 1.821 0.02 . 2 . . . . . . . . . 5784 1 510 . 1 1 95 95 LYS HG2 H 1 1.514 0.02 . 2 . . . . . . . . . 5784 1 511 . 1 1 95 95 LYS HG3 H 1 1.431 0.02 . 2 . . . . . . . . . 5784 1 512 . 1 1 96 96 TRP H H 1 8.679 0.02 . 1 . . . . . . . . . 5784 1 513 . 1 1 96 96 TRP HA H 1 4.608 0.02 . 1 . . . . . . . . . 5784 1 514 . 1 1 96 96 TRP HB2 H 1 3.468 0.02 . 2 . . . . . . . . . 5784 1 515 . 1 1 96 96 TRP HB3 H 1 2.596 0.02 . 2 . . . . . . . . . 5784 1 516 . 1 1 96 96 TRP HD1 H 1 7.105 0.02 . 1 . . . . . . . . . 5784 1 517 . 1 1 96 96 TRP HE1 H 1 10.388 0.02 . 1 . . . . . . . . . 5784 1 518 . 1 1 96 96 TRP HE3 H 1 7.963 0.02 . 1 . . . . . . . . . 5784 1 519 . 1 1 96 96 TRP HH2 H 1 6.952 0.02 . 1 . . . . . . . . . 5784 1 520 . 1 1 96 96 TRP HZ2 H 1 7.621 0.02 . 1 . . . . . . . . . 5784 1 521 . 1 1 96 96 TRP HZ3 H 1 7.459 0.02 . 1 . . . . . . . . . 5784 1 522 . 1 1 97 97 ASP H H 1 8.381 0.02 . 1 . . . . . . . . . 5784 1 523 . 1 1 97 97 ASP HA H 1 4.462 0.02 . 1 . . . . . . . . . 5784 1 524 . 1 1 97 97 ASP HB2 H 1 2.437 0.02 . 2 . . . . . . . . . 5784 1 525 . 1 1 97 97 ASP HB3 H 1 2.723 0.02 . 2 . . . . . . . . . 5784 1 526 . 1 1 98 98 ARG H H 1 7.450 0.02 . 1 . . . . . . . . . 5784 1 527 . 1 1 98 98 ARG HA H 1 3.371 0.02 . 1 . . . . . . . . . 5784 1 528 . 1 1 98 98 ARG HB2 H 1 1.378 0.02 . 2 . . . . . . . . . 5784 1 529 . 1 1 98 98 ARG HB3 H 1 1.121 0.02 . 2 . . . . . . . . . 5784 1 530 . 1 1 98 98 ARG HD2 H 1 2.941 0.02 . 1 . . . . . . . . . 5784 1 531 . 1 1 98 98 ARG HG2 H 1 0.946 0.02 . 1 . . . . . . . . . 5784 1 532 . 1 1 99 99 ASP H H 1 8.177 0.02 . 1 . . . . . . . . . 5784 1 533 . 1 1 99 99 ASP HA H 1 4.618 0.02 . 1 . . . . . . . . . 5784 1 534 . 1 1 99 99 ASP HB2 H 1 2.748 0.02 . 2 . . . . . . . . . 5784 1 535 . 1 1 99 99 ASP HB3 H 1 2.577 0.02 . 2 . . . . . . . . . 5784 1 536 . 1 1 100 100 MET H H 1 7.583 0.02 . 1 . . . . . . . . . 5784 1 537 . 1 1 100 100 MET HA H 1 4.263 0.02 . 1 . . . . . . . . . 5784 1 538 . 1 1 100 100 MET HB2 H 1 2.127 0.02 . 2 . . . . . . . . . 5784 1 539 . 1 1 100 100 MET HB3 H 1 1.991 0.02 . 2 . . . . . . . . . 5784 1 540 . 1 1 100 100 MET HG2 H 1 2.511 0.02 . 2 . . . . . . . . . 5784 1 541 . 1 1 100 100 MET HG3 H 1 2.552 0.02 . 2 . . . . . . . . . 5784 1 stop_ save_