data_5782 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 5782 _Entry.Title ; 1H chemical shift assignment for the truncated form of the human beta2-microglobulin lacking of the first 3 residues ; _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 Paolo Viglino . . . . 5782 2 Alessandra Corazza . . . . 5782 3 Fabio Pettirossi . . . . 5782 4 Giuliana Verdone . . . . 5782 5 Gennaro Esposito . . . . 5782 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 2 5782 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 716 5782 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 . 5782 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' 5782 BMRB 5783 'DN3 beta2-microglobulin (R3A mutant and with the first 3 residues)' 5782 BMRB 5784 'DN3 beta2-microglobulin (H31Y mutant and with the first 3 residues)' 5782 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 5782 _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 . . . . 5782 1 2 Fabio Pettirossi . . . . 5782 1 3 Paolo Viglino . . . . 5782 1 4 Giuliana Verdone . . . . 5782 1 5 Julian Garcia . . . . 5782 1 6 Pascal Dumy . . . . 5782 1 7 Sofia Giorgetti . . . . 5782 1 8 Palma Mangione . . . . 5782 1 9 Alessia Andreola . . . . 5782 1 10 Monica Stoppini . . . . 5782 1 11 Vittorio Bellotti . . . . 5782 1 12 Gennaro Esposito . . . . 5782 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID amyloidosis 5782 1 beta2-microglobulin 5782 1 stop_ save_ save_ref_1 _Citation.Sf_category citations _Citation.Sf_framecode ref_1 _Citation.Entry_ID 5782 _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. . . . 5782 2 2 Alessandra Corazza A. . . . 5782 2 3 Paolo Viglino P. . . . 5782 2 4 Fabio Pettirossi F. . . . 5782 2 5 Sofia Giorgetti S. . . . 5782 2 6 Palma Mangione P. . . . 5782 2 7 Alessia Andreola A. . . . 5782 2 8 Monica Stoppini M. . . . 5782 2 9 Vittorio Bellotti V. . . . 5782 2 10 Gennaro Esposito G. . . . 5782 2 stop_ save_ save_ref_2 _Citation.Sf_category citations _Citation.Sf_framecode ref_2 _Citation.Entry_ID 5782 _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. . . . 5782 3 2 R Michelutti R. . . . 5782 3 3 G Verdone G. . . . 5782 3 4 P Viglino P. . . . 5782 3 5 H Hernandez H. . . . 5782 3 6 C.V. Robinson C. V. . . 5782 3 7 A Amoresano A. . . . 5782 3 8 F 'Dal Piaz' F. . . . 5782 3 9 M Monti M. . . . 5782 3 10 P Pucci P. . . . 5782 3 11 P Mangione P. . . . 5782 3 12 M Stoppini M. . . . 5782 3 13 G Merlini G. . . . 5782 3 14 G Ferri G. . . . 5782 3 15 V Bellotti V. . . . 5782 3 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_DN3beta2-m _Assembly.Sf_category assembly _Assembly.Sf_framecode system_DN3beta2-m _Assembly.Entry_ID 5782 _Assembly.ID 1 _Assembly.Name DN3beta2-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 5782 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 DN3beta2-microglobulin 1 $D3Nbeta2-m . . . native . . . . . 5782 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 23 23 SG . 1 . 1 CYS 78 78 SG . . . . . . . . . . . . 5782 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID DN3beta2-m abbreviation 5782 1 DN3beta2-microglobulin system 5782 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_D3Nbeta2-m _Entity.Sf_category entity _Entity.Sf_framecode D3Nbeta2-m _Entity.Entry_ID 5782 _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 ; MTPKIQVYSRHPAENGKSNF LNCYVSGFHPSDIEVDLLKN GERIEKVEHSDLSFSKDWSF YLLYYTEFTPTEKDEYACRV NHVTLSQPKIVKWDRDM ; _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 97 _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 D3Nbeta2-m abbreviation 5782 1 D3Nbeta2-microglobulin variant 5782 1 beta2-microglobulin common 5782 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 . 5782 1 2 . THR . 5782 1 3 . PRO . 5782 1 4 . LYS . 5782 1 5 . ILE . 5782 1 6 . GLN . 5782 1 7 . VAL . 5782 1 8 . TYR . 5782 1 9 . SER . 5782 1 10 . ARG . 5782 1 11 . HIS . 5782 1 12 . PRO . 5782 1 13 . ALA . 5782 1 14 . GLU . 5782 1 15 . ASN . 5782 1 16 . GLY . 5782 1 17 . LYS . 5782 1 18 . SER . 5782 1 19 . ASN . 5782 1 20 . PHE . 5782 1 21 . LEU . 5782 1 22 . ASN . 5782 1 23 . CYS . 5782 1 24 . TYR . 5782 1 25 . VAL . 5782 1 26 . SER . 5782 1 27 . GLY . 5782 1 28 . PHE . 5782 1 29 . HIS . 5782 1 30 . PRO . 5782 1 31 . SER . 5782 1 32 . ASP . 5782 1 33 . ILE . 5782 1 34 . GLU . 5782 1 35 . VAL . 5782 1 36 . ASP . 5782 1 37 . LEU . 5782 1 38 . LEU . 5782 1 39 . LYS . 5782 1 40 . ASN . 5782 1 41 . GLY . 5782 1 42 . GLU . 5782 1 43 . ARG . 5782 1 44 . ILE . 5782 1 45 . GLU . 5782 1 46 . LYS . 5782 1 47 . VAL . 5782 1 48 . GLU . 5782 1 49 . HIS . 5782 1 50 . SER . 5782 1 51 . ASP . 5782 1 52 . LEU . 5782 1 53 . SER . 5782 1 54 . PHE . 5782 1 55 . SER . 5782 1 56 . LYS . 5782 1 57 . ASP . 5782 1 58 . TRP . 5782 1 59 . SER . 5782 1 60 . PHE . 5782 1 61 . TYR . 5782 1 62 . LEU . 5782 1 63 . LEU . 5782 1 64 . TYR . 5782 1 65 . TYR . 5782 1 66 . THR . 5782 1 67 . GLU . 5782 1 68 . PHE . 5782 1 69 . THR . 5782 1 70 . PRO . 5782 1 71 . THR . 5782 1 72 . GLU . 5782 1 73 . LYS . 5782 1 74 . ASP . 5782 1 75 . GLU . 5782 1 76 . TYR . 5782 1 77 . ALA . 5782 1 78 . CYS . 5782 1 79 . ARG . 5782 1 80 . VAL . 5782 1 81 . ASN . 5782 1 82 . HIS . 5782 1 83 . VAL . 5782 1 84 . THR . 5782 1 85 . LEU . 5782 1 86 . SER . 5782 1 87 . GLN . 5782 1 88 . PRO . 5782 1 89 . LYS . 5782 1 90 . ILE . 5782 1 91 . VAL . 5782 1 92 . LYS . 5782 1 93 . TRP . 5782 1 94 . ASP . 5782 1 95 . ARG . 5782 1 96 . ASP . 5782 1 97 . MET . 5782 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 5782 1 . THR 2 2 5782 1 . PRO 3 3 5782 1 . LYS 4 4 5782 1 . ILE 5 5 5782 1 . GLN 6 6 5782 1 . VAL 7 7 5782 1 . TYR 8 8 5782 1 . SER 9 9 5782 1 . ARG 10 10 5782 1 . HIS 11 11 5782 1 . PRO 12 12 5782 1 . ALA 13 13 5782 1 . GLU 14 14 5782 1 . ASN 15 15 5782 1 . GLY 16 16 5782 1 . LYS 17 17 5782 1 . SER 18 18 5782 1 . ASN 19 19 5782 1 . PHE 20 20 5782 1 . LEU 21 21 5782 1 . ASN 22 22 5782 1 . CYS 23 23 5782 1 . TYR 24 24 5782 1 . VAL 25 25 5782 1 . SER 26 26 5782 1 . GLY 27 27 5782 1 . PHE 28 28 5782 1 . HIS 29 29 5782 1 . PRO 30 30 5782 1 . SER 31 31 5782 1 . ASP 32 32 5782 1 . ILE 33 33 5782 1 . GLU 34 34 5782 1 . VAL 35 35 5782 1 . ASP 36 36 5782 1 . LEU 37 37 5782 1 . LEU 38 38 5782 1 . LYS 39 39 5782 1 . ASN 40 40 5782 1 . GLY 41 41 5782 1 . GLU 42 42 5782 1 . ARG 43 43 5782 1 . ILE 44 44 5782 1 . GLU 45 45 5782 1 . LYS 46 46 5782 1 . VAL 47 47 5782 1 . GLU 48 48 5782 1 . HIS 49 49 5782 1 . SER 50 50 5782 1 . ASP 51 51 5782 1 . LEU 52 52 5782 1 . SER 53 53 5782 1 . PHE 54 54 5782 1 . SER 55 55 5782 1 . LYS 56 56 5782 1 . ASP 57 57 5782 1 . TRP 58 58 5782 1 . SER 59 59 5782 1 . PHE 60 60 5782 1 . TYR 61 61 5782 1 . LEU 62 62 5782 1 . LEU 63 63 5782 1 . TYR 64 64 5782 1 . TYR 65 65 5782 1 . THR 66 66 5782 1 . GLU 67 67 5782 1 . PHE 68 68 5782 1 . THR 69 69 5782 1 . PRO 70 70 5782 1 . THR 71 71 5782 1 . GLU 72 72 5782 1 . LYS 73 73 5782 1 . ASP 74 74 5782 1 . GLU 75 75 5782 1 . TYR 76 76 5782 1 . ALA 77 77 5782 1 . CYS 78 78 5782 1 . ARG 79 79 5782 1 . VAL 80 80 5782 1 . ASN 81 81 5782 1 . HIS 82 82 5782 1 . VAL 83 83 5782 1 . THR 84 84 5782 1 . LEU 85 85 5782 1 . SER 86 86 5782 1 . GLN 87 87 5782 1 . PRO 88 88 5782 1 . LYS 89 89 5782 1 . ILE 90 90 5782 1 . VAL 91 91 5782 1 . LYS 92 92 5782 1 . TRP 93 93 5782 1 . ASP 94 94 5782 1 . ARG 95 95 5782 1 . ASP 96 96 5782 1 . MET 97 97 5782 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 5782 _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 $D3Nbeta2-m . 9606 . . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . . . . . . . . . . . . . 5782 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 5782 _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 $D3Nbeta2-m . 'recombinant technology' 'Escherichia coli' 'E. coli' . . Escherichia coli . . . . . . . . . . 5782 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 5782 _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 $D3Nbeta2-m . . 0.86 . . mM . . . . 5782 1 2 'sodium phosphate' . . . . . . . 70 . . mM . . . . 5782 1 3 'sodium chloride' . . . . . . . 100 . . mM . . . . 5782 1 4 H2O . . . . . . . 100 . . % . . . . 5782 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 5782 _Sample.ID 2 _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 $D3Nbeta2-m . . 0.7 . . mM . . . . 5782 2 2 'sodium phosphate' . . . . . . . 70 . . mM . . . . 5782 2 3 'sodium chloride' . . . . . . . 100 . . mM . . . . 5782 2 4 D2O . . . . . . . 95 . . % . . . . 5782 2 5 H2O . . . . . . . 5 . . % . . . . 5782 2 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 5782 _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 5782 1 temperature 310 0.1 K 5782 1 stop_ save_ ############################ # Computer software used # ############################ save_FELIX _Software.Sf_category software _Software.Sf_framecode FELIX _Software.Entry_ID 5782 _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 5782 _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 5782 _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 . . . 5782 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 5782 _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' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5782 1 2 '1H-1H NOESY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5782 1 3 '1H-1H DQF-COSY' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 5782 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 5782 _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 . . . . . 5782 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 5782 _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 'Principal conformational species (75%).' _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' . . . 5782 1 2 '1H-1H NOESY' . . . 5782 1 3 '1H-1H DQF-COSY' . . . 5782 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 1 1 MET HA H 1 3.977 0.02 . 1 . . . . . . . . . 5782 1 2 . 1 1 1 1 MET HB2 H 1 2.157 0.02 . 2 . . . . . . . . . 5782 1 3 . 1 1 1 1 MET HB3 H 1 2.053 0.02 . 2 . . . . . . . . . 5782 1 4 . 1 1 1 1 MET HG2 H 1 2.745 0.02 . 2 . . . . . . . . . 5782 1 5 . 1 1 1 1 MET HG3 H 1 2.524 0.02 . 2 . . . . . . . . . 5782 1 6 . 1 1 2 2 THR HA H 1 5.007 0.02 . 1 . . . . . . . . . 5782 1 7 . 1 1 2 2 THR HB H 1 4.135 0.02 . 1 . . . . . . . . . 5782 1 8 . 1 1 2 2 THR HG21 H 1 1.348 0.02 . 1 . . . . . . . . . 5782 1 9 . 1 1 2 2 THR HG22 H 1 1.348 0.02 . 1 . . . . . . . . . 5782 1 10 . 1 1 2 2 THR HG23 H 1 1.348 0.02 . 1 . . . . . . . . . 5782 1 11 . 1 1 3 3 PRO HA H 1 4.393 0.02 . 1 . . . . . . . . . 5782 1 12 . 1 1 3 3 PRO HB2 H 1 1.507 0.02 . 1 . . . . . . . . . 5782 1 13 . 1 1 3 3 PRO HD2 H 1 3.588 0.02 . 2 . . . . . . . . . 5782 1 14 . 1 1 3 3 PRO HD3 H 1 3.448 0.02 . 2 . . . . . . . . . 5782 1 15 . 1 1 3 3 PRO HG2 H 1 1.679 0.02 . 2 . . . . . . . . . 5782 1 16 . 1 1 3 3 PRO HG3 H 1 1.205 0.02 . 2 . . . . . . . . . 5782 1 17 . 1 1 4 4 LYS H H 1 9.168 0.02 . 1 . . . . . . . . . 5782 1 18 . 1 1 4 4 LYS HA H 1 4.516 0.02 . 1 . . . . . . . . . 5782 1 19 . 1 1 4 4 LYS HB2 H 1 1.785 0.02 . 2 . . . . . . . . . 5782 1 20 . 1 1 4 4 LYS HB3 H 1 1.523 0.02 . 2 . . . . . . . . . 5782 1 21 . 1 1 4 4 LYS HG2 H 1 1.635 0.02 . 2 . . . . . . . . . 5782 1 22 . 1 1 4 4 LYS HG3 H 1 1.444 0.02 . 2 . . . . . . . . . 5782 1 23 . 1 1 5 5 ILE H H 1 8.446 0.02 . 1 . . . . . . . . . 5782 1 24 . 1 1 5 5 ILE HA H 1 4.886 0.02 . 1 . . . . . . . . . 5782 1 25 . 1 1 5 5 ILE HB H 1 1.695 0.02 . 1 . . . . . . . . . 5782 1 26 . 1 1 5 5 ILE HD11 H 1 0.655 0.02 . 1 . . . . . . . . . 5782 1 27 . 1 1 5 5 ILE HD12 H 1 0.655 0.02 . 1 . . . . . . . . . 5782 1 28 . 1 1 5 5 ILE HD13 H 1 0.655 0.02 . 1 . . . . . . . . . 5782 1 29 . 1 1 5 5 ILE HG12 H 1 1.426 0.02 . 1 . . . . . . . . . 5782 1 30 . 1 1 5 5 ILE HG21 H 1 0.783 0.02 . 1 . . . . . . . . . 5782 1 31 . 1 1 5 5 ILE HG22 H 1 0.783 0.02 . 1 . . . . . . . . . 5782 1 32 . 1 1 5 5 ILE HG23 H 1 0.783 0.02 . 1 . . . . . . . . . 5782 1 33 . 1 1 6 6 GLN H H 1 9.144 0.02 . 1 . . . . . . . . . 5782 1 34 . 1 1 6 6 GLN HA H 1 4.946 0.02 . 1 . . . . . . . . . 5782 1 35 . 1 1 6 6 GLN HB2 H 1 2.348 0.02 . 2 . . . . . . . . . 5782 1 36 . 1 1 6 6 GLN HB3 H 1 2.189 0.02 . 2 . . . . . . . . . 5782 1 37 . 1 1 6 6 GLN HE21 H 1 7.492 0.02 . 2 . . . . . . . . . 5782 1 38 . 1 1 6 6 GLN HE22 H 1 6.818 0.02 . 2 . . . . . . . . . 5782 1 39 . 1 1 6 6 GLN HG2 H 1 2.414 0.02 . 1 . . . . . . . . . 5782 1 40 . 1 1 7 7 VAL H H 1 9.006 0.02 . 1 . . . . . . . . . 5782 1 41 . 1 1 7 7 VAL HA H 1 5.360 0.02 . 1 . . . . . . . . . 5782 1 42 . 1 1 7 7 VAL HB H 1 2.043 0.02 . 1 . . . . . . . . . 5782 1 43 . 1 1 7 7 VAL HG11 H 1 0.983 0.02 . 2 . . . . . . . . . 5782 1 44 . 1 1 7 7 VAL HG12 H 1 0.983 0.02 . 2 . . . . . . . . . 5782 1 45 . 1 1 7 7 VAL HG13 H 1 0.983 0.02 . 2 . . . . . . . . . 5782 1 46 . 1 1 7 7 VAL HG21 H 1 0.925 0.02 . 2 . . . . . . . . . 5782 1 47 . 1 1 7 7 VAL HG22 H 1 0.925 0.02 . 2 . . . . . . . . . 5782 1 48 . 1 1 7 7 VAL HG23 H 1 0.925 0.02 . 2 . . . . . . . . . 5782 1 49 . 1 1 8 8 TYR H H 1 8.468 0.02 . 1 . . . . . . . . . 5782 1 50 . 1 1 8 8 TYR HA H 1 5.320 0.02 . 1 . . . . . . . . . 5782 1 51 . 1 1 8 8 TYR HB2 H 1 3.413 0.02 . 2 . . . . . . . . . 5782 1 52 . 1 1 8 8 TYR HB3 H 1 3.183 0.02 . 2 . . . . . . . . . 5782 1 53 . 1 1 8 8 TYR HD1 H 1 6.818 0.02 . 1 . . . . . . . . . 5782 1 54 . 1 1 8 8 TYR HE1 H 1 6.566 0.02 . 1 . . . . . . . . . 5782 1 55 . 1 1 9 9 SER H H 1 9.327 0.02 . 1 . . . . . . . . . 5782 1 56 . 1 1 9 9 SER HA H 1 5.299 0.02 . 1 . . . . . . . . . 5782 1 57 . 1 1 9 9 SER HB2 H 1 4.426 0.02 . 2 . . . . . . . . . 5782 1 58 . 1 1 9 9 SER HB3 H 1 3.675 0.02 . 2 . . . . . . . . . 5782 1 59 . 1 1 10 10 ARG H H 1 8.855 0.02 . 1 . . . . . . . . . 5782 1 60 . 1 1 10 10 ARG HA H 1 3.940 0.02 . 1 . . . . . . . . . 5782 1 61 . 1 1 10 10 ARG HB2 H 1 1.941 0.02 . 2 . . . . . . . . . 5782 1 62 . 1 1 10 10 ARG HB3 H 1 1.754 0.02 . 2 . . . . . . . . . 5782 1 63 . 1 1 10 10 ARG HD2 H 1 3.065 0.02 . 2 . . . . . . . . . 5782 1 64 . 1 1 10 10 ARG HD3 H 1 2.797 0.02 . 2 . . . . . . . . . 5782 1 65 . 1 1 10 10 ARG HG2 H 1 1.432 0.02 . 1 . . . . . . . . . 5782 1 66 . 1 1 11 11 HIS H H 1 8.326 0.02 . 1 . . . . . . . . . 5782 1 67 . 1 1 11 11 HIS HA H 1 5.344 0.02 . 1 . . . . . . . . . 5782 1 68 . 1 1 11 11 HIS HB2 H 1 3.262 0.02 . 2 . . . . . . . . . 5782 1 69 . 1 1 11 11 HIS HB3 H 1 2.921 0.02 . 2 . . . . . . . . . 5782 1 70 . 1 1 11 11 HIS HD2 H 1 7.090 0.02 . 1 . . . . . . . . . 5782 1 71 . 1 1 11 11 HIS HE1 H 1 7.879 0.02 . 1 . . . . . . . . . 5782 1 72 . 1 1 12 12 PRO HA H 1 4.534 0.02 . 1 . . . . . . . . . 5782 1 73 . 1 1 12 12 PRO HB2 H 1 2.438 0.02 . 2 . . . . . . . . . 5782 1 74 . 1 1 12 12 PRO HB3 H 1 1.954 0.02 . 2 . . . . . . . . . 5782 1 75 . 1 1 12 12 PRO HD2 H 1 4.064 0.02 . 2 . . . . . . . . . 5782 1 76 . 1 1 12 12 PRO HD3 H 1 3.797 0.02 . 2 . . . . . . . . . 5782 1 77 . 1 1 12 12 PRO HG2 H 1 2.232 0.02 . 2 . . . . . . . . . 5782 1 78 . 1 1 12 12 PRO HG3 H 1 2.079 0.02 . 2 . . . . . . . . . 5782 1 79 . 1 1 13 13 ALA H H 1 8.979 0.02 . 1 . . . . . . . . . 5782 1 80 . 1 1 13 13 ALA HA H 1 4.113 0.02 . 1 . . . . . . . . . 5782 1 81 . 1 1 13 13 ALA HB1 H 1 1.699 0.02 . 1 . . . . . . . . . 5782 1 82 . 1 1 13 13 ALA HB2 H 1 1.699 0.02 . 1 . . . . . . . . . 5782 1 83 . 1 1 13 13 ALA HB3 H 1 1.699 0.02 . 1 . . . . . . . . . 5782 1 84 . 1 1 14 14 GLU H H 1 8.845 0.02 . 1 . . . . . . . . . 5782 1 85 . 1 1 14 14 GLU HA H 1 4.414 0.02 . 1 . . . . . . . . . 5782 1 86 . 1 1 14 14 GLU HB2 H 1 1.871 0.02 . 1 . . . . . . . . . 5782 1 87 . 1 1 14 14 GLU HG2 H 1 2.167 0.02 . 1 . . . . . . . . . 5782 1 88 . 1 1 15 15 ASN HA H 1 4.505 0.02 . 1 . . . . . . . . . 5782 1 89 . 1 1 15 15 ASN HB2 H 1 2.787 0.02 . 2 . . . . . . . . . 5782 1 90 . 1 1 15 15 ASN HB3 H 1 2.697 0.02 . 2 . . . . . . . . . 5782 1 91 . 1 1 15 15 ASN HD21 H 1 7.539 0.02 . 2 . . . . . . . . . 5782 1 92 . 1 1 15 15 ASN HD22 H 1 7.099 0.02 . 2 . . . . . . . . . 5782 1 93 . 1 1 16 16 GLY H H 1 8.834 0.02 . 1 . . . . . . . . . 5782 1 94 . 1 1 16 16 GLY HA2 H 1 4.198 0.02 . 2 . . . . . . . . . 5782 1 95 . 1 1 16 16 GLY HA3 H 1 3.536 0.02 . 2 . . . . . . . . . 5782 1 96 . 1 1 17 17 LYS H H 1 7.834 0.02 . 1 . . . . . . . . . 5782 1 97 . 1 1 17 17 LYS HA H 1 4.674 0.02 . 1 . . . . . . . . . 5782 1 98 . 1 1 17 17 LYS HB2 H 1 1.835 0.02 . 2 . . . . . . . . . 5782 1 99 . 1 1 17 17 LYS HB3 H 1 1.762 0.02 . 2 . . . . . . . . . 5782 1 100 . 1 1 17 17 LYS HD2 H 1 1.655 0.02 . 2 . . . . . . . . . 5782 1 101 . 1 1 17 17 LYS HD3 H 1 1.598 0.02 . 2 . . . . . . . . . 5782 1 102 . 1 1 17 17 LYS HE2 H 1 2.954 0.02 . 1 . . . . . . . . . 5782 1 103 . 1 1 17 17 LYS HG2 H 1 1.386 0.02 . 2 . . . . . . . . . 5782 1 104 . 1 1 17 17 LYS HG3 H 1 1.311 0.02 . 2 . . . . . . . . . 5782 1 105 . 1 1 18 18 SER H H 1 8.338 0.02 . 1 . . . . . . . . . 5782 1 106 . 1 1 18 18 SER HA H 1 4.268 0.02 . 1 . . . . . . . . . 5782 1 107 . 1 1 18 18 SER HB2 H 1 3.748 0.02 . 1 . . . . . . . . . 5782 1 108 . 1 1 19 19 ASN H H 1 8.887 0.02 . 1 . . . . . . . . . 5782 1 109 . 1 1 19 19 ASN HA H 1 4.878 0.02 . 1 . . . . . . . . . 5782 1 110 . 1 1 19 19 ASN HB2 H 1 2.765 0.02 . 2 . . . . . . . . . 5782 1 111 . 1 1 19 19 ASN HB3 H 1 2.555 0.02 . 2 . . . . . . . . . 5782 1 112 . 1 1 19 19 ASN HD21 H 1 7.765 0.02 . 2 . . . . . . . . . 5782 1 113 . 1 1 19 19 ASN HD22 H 1 7.445 0.02 . 2 . . . . . . . . . 5782 1 114 . 1 1 20 20 PHE H H 1 10.321 0.02 . 1 . . . . . . . . . 5782 1 115 . 1 1 20 20 PHE HA H 1 5.439 0.02 . 1 . . . . . . . . . 5782 1 116 . 1 1 20 20 PHE HB2 H 1 2.683 0.02 . 2 . . . . . . . . . 5782 1 117 . 1 1 20 20 PHE HB3 H 1 2.629 0.02 . 2 . . . . . . . . . 5782 1 118 . 1 1 20 20 PHE HD1 H 1 7.017 0.02 . 1 . . . . . . . . . 5782 1 119 . 1 1 20 20 PHE HE1 H 1 7.411 0.02 . 1 . . . . . . . . . 5782 1 120 . 1 1 20 20 PHE HZ H 1 7.340 0.02 . 1 . . . . . . . . . 5782 1 121 . 1 1 21 21 LEU H H 1 8.971 0.02 . 1 . . . . . . . . . 5782 1 122 . 1 1 21 21 LEU HA H 1 3.699 0.02 . 1 . . . . . . . . . 5782 1 123 . 1 1 21 21 LEU HB2 H 1 0.823 0.02 . 2 . . . . . . . . . 5782 1 124 . 1 1 21 21 LEU HB3 H 1 0.811 0.02 . 2 . . . . . . . . . 5782 1 125 . 1 1 21 21 LEU HD11 H 1 0.016 0.02 . 2 . . . . . . . . . 5782 1 126 . 1 1 21 21 LEU HD12 H 1 0.016 0.02 . 2 . . . . . . . . . 5782 1 127 . 1 1 21 21 LEU HD13 H 1 0.016 0.02 . 2 . . . . . . . . . 5782 1 128 . 1 1 21 21 LEU HD21 H 1 0.565 0.02 . 2 . . . . . . . . . 5782 1 129 . 1 1 21 21 LEU HD22 H 1 0.565 0.02 . 2 . . . . . . . . . 5782 1 130 . 1 1 21 21 LEU HD23 H 1 0.565 0.02 . 2 . . . . . . . . . 5782 1 131 . 1 1 21 21 LEU HG H 1 0.672 0.02 . 1 . . . . . . . . . 5782 1 132 . 1 1 22 22 ASN H H 1 8.200 0.02 . 1 . . . . . . . . . 5782 1 133 . 1 1 22 22 ASN HA H 1 5.388 0.02 . 1 . . . . . . . . . 5782 1 134 . 1 1 22 22 ASN HB2 H 1 1.854 0.02 . 2 . . . . . . . . . 5782 1 135 . 1 1 22 22 ASN HB3 H 1 1.470 0.02 . 2 . . . . . . . . . 5782 1 136 . 1 1 22 22 ASN HD21 H 1 5.730 0.02 . 2 . . . . . . . . . 5782 1 137 . 1 1 22 22 ASN HD22 H 1 5.560 0.02 . 2 . . . . . . . . . 5782 1 138 . 1 1 23 23 CYS H H 1 9.630 0.02 . 1 . . . . . . . . . 5782 1 139 . 1 1 23 23 CYS HA H 1 5.185 0.02 . 1 . . . . . . . . . 5782 1 140 . 1 1 23 23 CYS HB2 H 1 3.282 0.02 . 2 . . . . . . . . . 5782 1 141 . 1 1 23 23 CYS HB3 H 1 2.555 0.02 . 2 . . . . . . . . . 5782 1 142 . 1 1 24 24 TYR H H 1 9.669 0.02 . 1 . . . . . . . . . 5782 1 143 . 1 1 24 24 TYR HA H 1 5.425 0.02 . 1 . . . . . . . . . 5782 1 144 . 1 1 24 24 TYR HB2 H 1 3.187 0.02 . 1 . . . . . . . . . 5782 1 145 . 1 1 24 24 TYR HD1 H 1 7.153 0.02 . 1 . . . . . . . . . 5782 1 146 . 1 1 24 24 TYR HE1 H 1 6.577 0.02 . 1 . . . . . . . . . 5782 1 147 . 1 1 25 25 VAL H H 1 8.803 0.02 . 1 . . . . . . . . . 5782 1 148 . 1 1 25 25 VAL HA H 1 5.204 0.02 . 1 . . . . . . . . . 5782 1 149 . 1 1 25 25 VAL HB H 1 1.914 0.02 . 1 . . . . . . . . . 5782 1 150 . 1 1 25 25 VAL HG11 H 1 0.904 0.02 . 2 . . . . . . . . . 5782 1 151 . 1 1 25 25 VAL HG12 H 1 0.904 0.02 . 2 . . . . . . . . . 5782 1 152 . 1 1 25 25 VAL HG13 H 1 0.904 0.02 . 2 . . . . . . . . . 5782 1 153 . 1 1 25 25 VAL HG21 H 1 0.793 0.02 . 2 . . . . . . . . . 5782 1 154 . 1 1 25 25 VAL HG22 H 1 0.793 0.02 . 2 . . . . . . . . . 5782 1 155 . 1 1 25 25 VAL HG23 H 1 0.793 0.02 . 2 . . . . . . . . . 5782 1 156 . 1 1 26 26 SER H H 1 8.959 0.02 . 1 . . . . . . . . . 5782 1 157 . 1 1 26 26 SER HA H 1 5.718 0.02 . 1 . . . . . . . . . 5782 1 158 . 1 1 26 26 SER HB2 H 1 3.859 0.02 . 2 . . . . . . . . . 5782 1 159 . 1 1 26 26 SER HB3 H 1 3.472 0.02 . 2 . . . . . . . . . 5782 1 160 . 1 1 27 27 GLY H H 1 8.362 0.02 . 1 . . . . . . . . . 5782 1 161 . 1 1 27 27 GLY HA2 H 1 4.112 0.02 . 2 . . . . . . . . . 5782 1 162 . 1 1 27 27 GLY HA3 H 1 3.887 0.02 . 2 . . . . . . . . . 5782 1 163 . 1 1 28 28 PHE H H 1 7.170 0.02 . 1 . . . . . . . . . 5782 1 164 . 1 1 28 28 PHE HA H 1 4.971 0.02 . 1 . . . . . . . . . 5782 1 165 . 1 1 28 28 PHE HB2 H 1 2.269 0.02 . 2 . . . . . . . . . 5782 1 166 . 1 1 28 28 PHE HB3 H 1 1.962 0.02 . 2 . . . . . . . . . 5782 1 167 . 1 1 28 28 PHE HD1 H 1 6.961 0.02 . 1 . . . . . . . . . 5782 1 168 . 1 1 28 28 PHE HE1 H 1 7.248 0.02 . 1 . . . . . . . . . 5782 1 169 . 1 1 28 28 PHE HZ H 1 6.861 0.02 . 1 . . . . . . . . . 5782 1 170 . 1 1 29 29 HIS H H 1 8.262 0.02 . 1 . . . . . . . . . 5782 1 171 . 1 1 29 29 HIS HA H 1 4.528 0.02 . 1 . . . . . . . . . 5782 1 172 . 1 1 29 29 HIS HB2 H 1 3.314 0.02 . 2 . . . . . . . . . 5782 1 173 . 1 1 29 29 HIS HB3 H 1 3.114 0.02 . 2 . . . . . . . . . 5782 1 174 . 1 1 29 29 HIS HD2 H 1 7.074 0.02 . 1 . . . . . . . . . 5782 1 175 . 1 1 29 29 HIS HE1 H 1 7.849 0.02 . 1 . . . . . . . . . 5782 1 176 . 1 1 30 30 PRO HA H 1 3.962 0.02 . 1 . . . . . . . . . 5782 1 177 . 1 1 30 30 PRO HB2 H 1 2.248 0.02 . 2 . . . . . . . . . 5782 1 178 . 1 1 30 30 PRO HB3 H 1 2.013 0.02 . 2 . . . . . . . . . 5782 1 179 . 1 1 30 30 PRO HD2 H 1 3.744 0.02 . 2 . . . . . . . . . 5782 1 180 . 1 1 30 30 PRO HD3 H 1 3.644 0.02 . 2 . . . . . . . . . 5782 1 181 . 1 1 30 30 PRO HG2 H 1 1.817 0.02 . 1 . . . . . . . . . 5782 1 182 . 1 1 31 31 SER H H 1 8.262 0.02 . 1 . . . . . . . . . 5782 1 183 . 1 1 31 31 SER HA H 1 3.621 0.02 . 1 . . . . . . . . . 5782 1 184 . 1 1 31 31 SER HB2 H 1 3.314 0.02 . 2 . . . . . . . . . 5782 1 185 . 1 1 31 31 SER HB3 H 1 1.895 0.02 . 2 . . . . . . . . . 5782 1 186 . 1 1 32 32 ASP H H 1 7.211 0.02 . 1 . . . . . . . . . 5782 1 187 . 1 1 32 32 ASP HA H 1 4.428 0.02 . 1 . . . . . . . . . 5782 1 188 . 1 1 32 32 ASP HB2 H 1 2.414 0.02 . 2 . . . . . . . . . 5782 1 189 . 1 1 32 32 ASP HB3 H 1 2.351 0.02 . 2 . . . . . . . . . 5782 1 190 . 1 1 33 33 ILE H H 1 7.956 0.02 . 1 . . . . . . . . . 5782 1 191 . 1 1 33 33 ILE HA H 1 4.512 0.02 . 1 . . . . . . . . . 5782 1 192 . 1 1 33 33 ILE HB H 1 1.406 0.02 . 1 . . . . . . . . . 5782 1 193 . 1 1 33 33 ILE HD11 H 1 0.444 0.02 . 1 . . . . . . . . . 5782 1 194 . 1 1 33 33 ILE HD12 H 1 0.444 0.02 . 1 . . . . . . . . . 5782 1 195 . 1 1 33 33 ILE HD13 H 1 0.444 0.02 . 1 . . . . . . . . . 5782 1 196 . 1 1 33 33 ILE HG12 H 1 1.462 0.02 . 2 . . . . . . . . . 5782 1 197 . 1 1 33 33 ILE HG13 H 1 0.694 0.02 . 2 . . . . . . . . . 5782 1 198 . 1 1 33 33 ILE HG21 H 1 0.571 0.02 . 1 . . . . . . . . . 5782 1 199 . 1 1 33 33 ILE HG22 H 1 0.571 0.02 . 1 . . . . . . . . . 5782 1 200 . 1 1 33 33 ILE HG23 H 1 0.571 0.02 . 1 . . . . . . . . . 5782 1 201 . 1 1 34 34 GLU H H 1 7.963 0.02 . 1 . . . . . . . . . 5782 1 202 . 1 1 34 34 GLU HA H 1 4.588 0.02 . 1 . . . . . . . . . 5782 1 203 . 1 1 34 34 GLU HB2 H 1 1.939 0.02 . 2 . . . . . . . . . 5782 1 204 . 1 1 34 34 GLU HB3 H 1 1.785 0.02 . 2 . . . . . . . . . 5782 1 205 . 1 1 34 34 GLU HG2 H 1 2.111 0.02 . 2 . . . . . . . . . 5782 1 206 . 1 1 34 34 GLU HG3 H 1 2.077 0.02 . 2 . . . . . . . . . 5782 1 207 . 1 1 35 35 VAL H H 1 7.929 0.02 . 1 . . . . . . . . . 5782 1 208 . 1 1 35 35 VAL HA H 1 4.674 0.02 . 1 . . . . . . . . . 5782 1 209 . 1 1 35 35 VAL HB H 1 0.450 0.02 . 1 . . . . . . . . . 5782 1 210 . 1 1 35 35 VAL HG11 H 1 0.490 0.02 . 2 . . . . . . . . . 5782 1 211 . 1 1 35 35 VAL HG12 H 1 0.490 0.02 . 2 . . . . . . . . . 5782 1 212 . 1 1 35 35 VAL HG13 H 1 0.490 0.02 . 2 . . . . . . . . . 5782 1 213 . 1 1 35 35 VAL HG21 H 1 0.249 0.02 . 2 . . . . . . . . . 5782 1 214 . 1 1 35 35 VAL HG22 H 1 0.249 0.02 . 2 . . . . . . . . . 5782 1 215 . 1 1 35 35 VAL HG23 H 1 0.249 0.02 . 2 . . . . . . . . . 5782 1 216 . 1 1 36 36 ASP H H 1 8.866 0.02 . 1 . . . . . . . . . 5782 1 217 . 1 1 36 36 ASP HA H 1 4.947 0.02 . 1 . . . . . . . . . 5782 1 218 . 1 1 36 36 ASP HB2 H 1 2.404 0.02 . 2 . . . . . . . . . 5782 1 219 . 1 1 36 36 ASP HB3 H 1 2.206 0.02 . 2 . . . . . . . . . 5782 1 220 . 1 1 37 37 LEU H H 1 9.027 0.02 . 1 . . . . . . . . . 5782 1 221 . 1 1 37 37 LEU HA H 1 5.013 0.02 . 1 . . . . . . . . . 5782 1 222 . 1 1 37 37 LEU HB2 H 1 1.635 0.02 . 2 . . . . . . . . . 5782 1 223 . 1 1 37 37 LEU HB3 H 1 1.239 0.02 . 2 . . . . . . . . . 5782 1 224 . 1 1 37 37 LEU HD11 H 1 0.748 0.02 . 1 . . . . . . . . . 5782 1 225 . 1 1 37 37 LEU HD12 H 1 0.748 0.02 . 1 . . . . . . . . . 5782 1 226 . 1 1 37 37 LEU HD13 H 1 0.748 0.02 . 1 . . . . . . . . . 5782 1 227 . 1 1 37 37 LEU HG H 1 1.597 0.02 . 1 . . . . . . . . . 5782 1 228 . 1 1 38 38 LEU H H 1 8.969 0.02 . 1 . . . . . . . . . 5782 1 229 . 1 1 38 38 LEU HA H 1 5.006 0.02 . 1 . . . . . . . . . 5782 1 230 . 1 1 38 38 LEU HB2 H 1 1.577 0.02 . 2 . . . . . . . . . 5782 1 231 . 1 1 38 38 LEU HB3 H 1 0.829 0.02 . 2 . . . . . . . . . 5782 1 232 . 1 1 38 38 LEU HD11 H 1 0.602 0.02 . 2 . . . . . . . . . 5782 1 233 . 1 1 38 38 LEU HD12 H 1 0.602 0.02 . 2 . . . . . . . . . 5782 1 234 . 1 1 38 38 LEU HD13 H 1 0.602 0.02 . 2 . . . . . . . . . 5782 1 235 . 1 1 38 38 LEU HD21 H 1 0.406 0.02 . 2 . . . . . . . . . 5782 1 236 . 1 1 38 38 LEU HD22 H 1 0.406 0.02 . 2 . . . . . . . . . 5782 1 237 . 1 1 38 38 LEU HD23 H 1 0.406 0.02 . 2 . . . . . . . . . 5782 1 238 . 1 1 38 38 LEU HG H 1 1.207 0.02 . 1 . . . . . . . . . 5782 1 239 . 1 1 39 39 LYS H H 1 8.845 0.02 . 1 . . . . . . . . . 5782 1 240 . 1 1 39 39 LYS HA H 1 4.414 0.02 . 1 . . . . . . . . . 5782 1 241 . 1 1 39 39 LYS HB2 H 1 1.752 0.02 . 2 . . . . . . . . . 5782 1 242 . 1 1 39 39 LYS HB3 H 1 1.457 0.02 . 2 . . . . . . . . . 5782 1 243 . 1 1 39 39 LYS HD2 H 1 1.774 0.02 . 2 . . . . . . . . . 5782 1 244 . 1 1 39 39 LYS HD3 H 1 1.578 0.02 . 2 . . . . . . . . . 5782 1 245 . 1 1 39 39 LYS HE2 H 1 2.845 0.02 . 1 . . . . . . . . . 5782 1 246 . 1 1 39 39 LYS HG2 H 1 0.555 0.02 . 2 . . . . . . . . . 5782 1 247 . 1 1 39 39 LYS HG3 H 1 0.831 0.02 . 2 . . . . . . . . . 5782 1 248 . 1 1 40 40 ASN H H 1 9.731 0.02 . 1 . . . . . . . . . 5782 1 249 . 1 1 40 40 ASN HA H 1 4.363 0.02 . 1 . . . . . . . . . 5782 1 250 . 1 1 40 40 ASN HB2 H 1 2.859 0.02 . 2 . . . . . . . . . 5782 1 251 . 1 1 40 40 ASN HB3 H 1 2.909 0.02 . 2 . . . . . . . . . 5782 1 252 . 1 1 40 40 ASN HD21 H 1 7.980 0.02 . 2 . . . . . . . . . 5782 1 253 . 1 1 40 40 ASN HD22 H 1 7.730 0.02 . 2 . . . . . . . . . 5782 1 254 . 1 1 41 41 GLY H H 1 8.791 0.02 . 1 . . . . . . . . . 5782 1 255 . 1 1 41 41 GLY HA2 H 1 4.198 0.02 . 2 . . . . . . . . . 5782 1 256 . 1 1 41 41 GLY HA3 H 1 3.333 0.02 . 2 . . . . . . . . . 5782 1 257 . 1 1 42 42 GLU H H 1 7.832 0.02 . 1 . . . . . . . . . 5782 1 258 . 1 1 42 42 GLU HA H 1 4.582 0.02 . 1 . . . . . . . . . 5782 1 259 . 1 1 42 42 GLU HB2 H 1 2.060 0.02 . 2 . . . . . . . . . 5782 1 260 . 1 1 42 42 GLU HB3 H 1 1.963 0.02 . 2 . . . . . . . . . 5782 1 261 . 1 1 42 42 GLU HG2 H 1 2.287 0.02 . 2 . . . . . . . . . 5782 1 262 . 1 1 42 42 GLU HG3 H 1 2.177 0.02 . 2 . . . . . . . . . 5782 1 263 . 1 1 43 43 ARG H H 1 8.651 0.02 . 1 . . . . . . . . . 5782 1 264 . 1 1 43 43 ARG HA H 1 4.181 0.02 . 1 . . . . . . . . . 5782 1 265 . 1 1 43 43 ARG HB2 H 1 1.639 0.02 . 1 . . . . . . . . . 5782 1 266 . 1 1 43 43 ARG HD2 H 1 3.139 0.02 . 2 . . . . . . . . . 5782 1 267 . 1 1 43 43 ARG HD3 H 1 3.083 0.02 . 2 . . . . . . . . . 5782 1 268 . 1 1 43 43 ARG HG2 H 1 1.544 0.02 . 2 . . . . . . . . . 5782 1 269 . 1 1 43 43 ARG HG3 H 1 1.345 0.02 . 2 . . . . . . . . . 5782 1 270 . 1 1 44 44 ILE H H 1 8.793 0.02 . 1 . . . . . . . . . 5782 1 271 . 1 1 44 44 ILE HA H 1 4.000 0.02 . 1 . . . . . . . . . 5782 1 272 . 1 1 44 44 ILE HB H 1 1.547 0.02 . 1 . . . . . . . . . 5782 1 273 . 1 1 44 44 ILE HD11 H 1 0.903 0.02 . 1 . . . . . . . . . 5782 1 274 . 1 1 44 44 ILE HD12 H 1 0.903 0.02 . 1 . . . . . . . . . 5782 1 275 . 1 1 44 44 ILE HD13 H 1 0.903 0.02 . 1 . . . . . . . . . 5782 1 276 . 1 1 44 44 ILE HG12 H 1 1.702 0.02 . 2 . . . . . . . . . 5782 1 277 . 1 1 44 44 ILE HG13 H 1 1.038 0.02 . 2 . . . . . . . . . 5782 1 278 . 1 1 44 44 ILE HG21 H 1 0.983 0.02 . 1 . . . . . . . . . 5782 1 279 . 1 1 44 44 ILE HG22 H 1 0.983 0.02 . 1 . . . . . . . . . 5782 1 280 . 1 1 44 44 ILE HG23 H 1 0.983 0.02 . 1 . . . . . . . . . 5782 1 281 . 1 1 45 45 GLU H H 1 8.491 0.02 . 1 . . . . . . . . . 5782 1 282 . 1 1 45 45 GLU HA H 1 4.181 0.02 . 1 . . . . . . . . . 5782 1 283 . 1 1 45 45 GLU HB2 H 1 2.109 0.02 . 2 . . . . . . . . . 5782 1 284 . 1 1 45 45 GLU HB3 H 1 2.031 0.02 . 2 . . . . . . . . . 5782 1 285 . 1 1 45 45 GLU HG2 H 1 2.374 0.02 . 2 . . . . . . . . . 5782 1 286 . 1 1 45 45 GLU HG3 H 1 2.251 0.02 . 2 . . . . . . . . . 5782 1 287 . 1 1 46 46 LYS H H 1 7.923 0.02 . 1 . . . . . . . . . 5782 1 288 . 1 1 46 46 LYS HA H 1 4.512 0.02 . 1 . . . . . . . . . 5782 1 289 . 1 1 46 46 LYS HB2 H 1 1.943 0.02 . 2 . . . . . . . . . 5782 1 290 . 1 1 46 46 LYS HB3 H 1 1.785 0.02 . 2 . . . . . . . . . 5782 1 291 . 1 1 46 46 LYS HE2 H 1 3.040 0.02 . 1 . . . . . . . . . 5782 1 292 . 1 1 46 46 LYS HG2 H 1 1.445 0.02 . 2 . . . . . . . . . 5782 1 293 . 1 1 46 46 LYS HG3 H 1 1.407 0.02 . 2 . . . . . . . . . 5782 1 294 . 1 1 47 47 VAL H H 1 7.829 0.02 . 1 . . . . . . . . . 5782 1 295 . 1 1 47 47 VAL HA H 1 4.398 0.02 . 1 . . . . . . . . . 5782 1 296 . 1 1 47 47 VAL HB H 1 2.115 0.02 . 1 . . . . . . . . . 5782 1 297 . 1 1 47 47 VAL HG11 H 1 1.099 0.02 . 2 . . . . . . . . . 5782 1 298 . 1 1 47 47 VAL HG12 H 1 1.099 0.02 . 2 . . . . . . . . . 5782 1 299 . 1 1 47 47 VAL HG13 H 1 1.099 0.02 . 2 . . . . . . . . . 5782 1 300 . 1 1 47 47 VAL HG21 H 1 1.028 0.02 . 2 . . . . . . . . . 5782 1 301 . 1 1 47 47 VAL HG22 H 1 1.028 0.02 . 2 . . . . . . . . . 5782 1 302 . 1 1 47 47 VAL HG23 H 1 1.028 0.02 . 2 . . . . . . . . . 5782 1 303 . 1 1 48 48 GLU H H 1 8.441 0.02 . 1 . . . . . . . . . 5782 1 304 . 1 1 48 48 GLU HA H 1 4.492 0.02 . 1 . . . . . . . . . 5782 1 305 . 1 1 48 48 GLU HB2 H 1 1.589 0.02 . 2 . . . . . . . . . 5782 1 306 . 1 1 48 48 GLU HB3 H 1 0.755 0.02 . 2 . . . . . . . . . 5782 1 307 . 1 1 48 48 GLU HG2 H 1 2.075 0.02 . 1 . . . . . . . . . 5782 1 308 . 1 1 49 49 HIS H H 1 8.126 0.02 . 1 . . . . . . . . . 5782 1 309 . 1 1 49 49 HIS HA H 1 5.494 0.02 . 1 . . . . . . . . . 5782 1 310 . 1 1 49 49 HIS HB2 H 1 2.462 0.02 . 2 . . . . . . . . . 5782 1 311 . 1 1 49 49 HIS HB3 H 1 1.985 0.02 . 2 . . . . . . . . . 5782 1 312 . 1 1 49 49 HIS HD2 H 1 7.017 0.02 . 1 . . . . . . . . . 5782 1 313 . 1 1 49 49 HIS HE1 H 1 8.503 0.02 . 1 . . . . . . . . . 5782 1 314 . 1 1 50 50 SER H H 1 9.114 0.02 . 1 . . . . . . . . . 5782 1 315 . 1 1 50 50 SER HA H 1 4.662 0.02 . 1 . . . . . . . . . 5782 1 316 . 1 1 50 50 SER HB2 H 1 4.469 0.02 . 2 . . . . . . . . . 5782 1 317 . 1 1 50 50 SER HB3 H 1 4.099 0.02 . 2 . . . . . . . . . 5782 1 318 . 1 1 51 51 ASP HA H 1 4.808 0.02 . 1 . . . . . . . . . 5782 1 319 . 1 1 51 51 ASP HB2 H 1 2.754 0.02 . 2 . . . . . . . . . 5782 1 320 . 1 1 51 51 ASP HB3 H 1 2.579 0.02 . 2 . . . . . . . . . 5782 1 321 . 1 1 52 52 LEU HA H 1 4.318 0.02 . 1 . . . . . . . . . 5782 1 322 . 1 1 52 52 LEU HB2 H 1 1.809 0.02 . 1 . . . . . . . . . 5782 1 323 . 1 1 52 52 LEU HD11 H 1 1.054 0.02 . 2 . . . . . . . . . 5782 1 324 . 1 1 52 52 LEU HD12 H 1 1.054 0.02 . 2 . . . . . . . . . 5782 1 325 . 1 1 52 52 LEU HD13 H 1 1.054 0.02 . 2 . . . . . . . . . 5782 1 326 . 1 1 52 52 LEU HD21 H 1 0.871 0.02 . 2 . . . . . . . . . 5782 1 327 . 1 1 52 52 LEU HD22 H 1 0.871 0.02 . 2 . . . . . . . . . 5782 1 328 . 1 1 52 52 LEU HD23 H 1 0.871 0.02 . 2 . . . . . . . . . 5782 1 329 . 1 1 52 52 LEU HG H 1 1.659 0.02 . 1 . . . . . . . . . 5782 1 330 . 1 1 53 53 SER H H 1 8.033 0.02 . 1 . . . . . . . . . 5782 1 331 . 1 1 53 53 SER HA H 1 4.767 0.02 . 1 . . . . . . . . . 5782 1 332 . 1 1 53 53 SER HB2 H 1 3.421 0.02 . 2 . . . . . . . . . 5782 1 333 . 1 1 53 53 SER HB3 H 1 2.741 0.02 . 2 . . . . . . . . . 5782 1 334 . 1 1 54 54 PHE H H 1 8.158 0.02 . 1 . . . . . . . . . 5782 1 335 . 1 1 54 54 PHE HA H 1 5.047 0.02 . 1 . . . . . . . . . 5782 1 336 . 1 1 54 54 PHE HB2 H 1 2.680 0.02 . 1 . . . . . . . . . 5782 1 337 . 1 1 54 54 PHE HD1 H 1 6.346 0.02 . 1 . . . . . . . . . 5782 1 338 . 1 1 54 54 PHE HE1 H 1 7.004 0.02 . 1 . . . . . . . . . 5782 1 339 . 1 1 54 54 PHE HZ H 1 7.099 0.02 . 1 . . . . . . . . . 5782 1 340 . 1 1 55 55 SER H H 1 8.217 0.02 . 1 . . . . . . . . . 5782 1 341 . 1 1 55 55 SER HA H 1 4.537 0.02 . 1 . . . . . . . . . 5782 1 342 . 1 1 55 55 SER HB2 H 1 3.913 0.02 . 2 . . . . . . . . . 5782 1 343 . 1 1 55 55 SER HB3 H 1 3.653 0.02 . 2 . . . . . . . . . 5782 1 344 . 1 1 56 56 LYS HA H 1 3.828 0.02 . 1 . . . . . . . . . 5782 1 345 . 1 1 56 56 LYS HB2 H 1 1.742 0.02 . 1 . . . . . . . . . 5782 1 346 . 1 1 56 56 LYS HD2 H 1 1.646 0.02 . 1 . . . . . . . . . 5782 1 347 . 1 1 56 56 LYS HE2 H 1 2.978 0.02 . 1 . . . . . . . . . 5782 1 348 . 1 1 56 56 LYS HG2 H 1 1.397 0.02 . 1 . . . . . . . . . 5782 1 349 . 1 1 57 57 ASP H H 1 7.693 0.02 . 1 . . . . . . . . . 5782 1 350 . 1 1 57 57 ASP HA H 1 4.366 0.02 . 1 . . . . . . . . . 5782 1 351 . 1 1 57 57 ASP HB2 H 1 2.278 0.02 . 1 . . . . . . . . . 5782 1 352 . 1 1 58 58 TRP H H 1 7.285 0.02 . 1 . . . . . . . . . 5782 1 353 . 1 1 58 58 TRP HA H 1 4.655 0.02 . 1 . . . . . . . . . 5782 1 354 . 1 1 58 58 TRP HB2 H 1 3.039 0.02 . 2 . . . . . . . . . 5782 1 355 . 1 1 58 58 TRP HB3 H 1 3.180 0.02 . 2 . . . . . . . . . 5782 1 356 . 1 1 58 58 TRP HD1 H 1 6.875 0.02 . 1 . . . . . . . . . 5782 1 357 . 1 1 58 58 TRP HE1 H 1 9.641 0.02 . 1 . . . . . . . . . 5782 1 358 . 1 1 58 58 TRP HE3 H 1 6.968 0.02 . 1 . . . . . . . . . 5782 1 359 . 1 1 58 58 TRP HH2 H 1 7.094 0.02 . 1 . . . . . . . . . 5782 1 360 . 1 1 58 58 TRP HZ2 H 1 7.341 0.02 . 1 . . . . . . . . . 5782 1 361 . 1 1 58 58 TRP HZ3 H 1 6.852 0.02 . 1 . . . . . . . . . 5782 1 362 . 1 1 59 59 SER H H 1 7.601 0.02 . 1 . . . . . . . . . 5782 1 363 . 1 1 59 59 SER HA H 1 3.878 0.02 . 1 . . . . . . . . . 5782 1 364 . 1 1 59 59 SER HB2 H 1 3.776 0.02 . 2 . . . . . . . . . 5782 1 365 . 1 1 59 59 SER HB3 H 1 3.725 0.02 . 2 . . . . . . . . . 5782 1 366 . 1 1 60 60 PHE H H 1 7.708 0.02 . 1 . . . . . . . . . 5782 1 367 . 1 1 60 60 PHE HA H 1 5.252 0.02 . 1 . . . . . . . . . 5782 1 368 . 1 1 60 60 PHE HB2 H 1 2.488 0.02 . 2 . . . . . . . . . 5782 1 369 . 1 1 60 60 PHE HB3 H 1 1.793 0.02 . 2 . . . . . . . . . 5782 1 370 . 1 1 60 60 PHE HD1 H 1 7.396 0.02 . 1 . . . . . . . . . 5782 1 371 . 1 1 60 60 PHE HE1 H 1 7.271 0.02 . 1 . . . . . . . . . 5782 1 372 . 1 1 60 60 PHE HZ H 1 7.138 0.02 . 1 . . . . . . . . . 5782 1 373 . 1 1 61 61 TYR H H 1 8.237 0.02 . 1 . . . . . . . . . 5782 1 374 . 1 1 61 61 TYR HA H 1 5.552 0.02 . 1 . . . . . . . . . 5782 1 375 . 1 1 61 61 TYR HB2 H 1 2.995 0.02 . 2 . . . . . . . . . 5782 1 376 . 1 1 61 61 TYR HB3 H 1 2.817 0.02 . 2 . . . . . . . . . 5782 1 377 . 1 1 61 61 TYR HD1 H 1 6.989 0.02 . 1 . . . . . . . . . 5782 1 378 . 1 1 61 61 TYR HE1 H 1 6.649 0.02 . 1 . . . . . . . . . 5782 1 379 . 1 1 62 62 LEU H H 1 9.093 0.02 . 1 . . . . . . . . . 5782 1 380 . 1 1 62 62 LEU HA H 1 4.637 0.02 . 1 . . . . . . . . . 5782 1 381 . 1 1 62 62 LEU HB2 H 1 1.969 0.02 . 2 . . . . . . . . . 5782 1 382 . 1 1 62 62 LEU HB3 H 1 1.757 0.02 . 2 . . . . . . . . . 5782 1 383 . 1 1 62 62 LEU HD11 H 1 1.007 0.02 . 2 . . . . . . . . . 5782 1 384 . 1 1 62 62 LEU HD12 H 1 1.007 0.02 . 2 . . . . . . . . . 5782 1 385 . 1 1 62 62 LEU HD13 H 1 1.007 0.02 . 2 . . . . . . . . . 5782 1 386 . 1 1 62 62 LEU HD21 H 1 0.967 0.02 . 2 . . . . . . . . . 5782 1 387 . 1 1 62 62 LEU HD22 H 1 0.967 0.02 . 2 . . . . . . . . . 5782 1 388 . 1 1 62 62 LEU HD23 H 1 0.967 0.02 . 2 . . . . . . . . . 5782 1 389 . 1 1 63 63 LEU H H 1 8.128 0.02 . 1 . . . . . . . . . 5782 1 390 . 1 1 63 63 LEU HA H 1 5.480 0.02 . 1 . . . . . . . . . 5782 1 391 . 1 1 63 63 LEU HB2 H 1 1.987 0.02 . 2 . . . . . . . . . 5782 1 392 . 1 1 63 63 LEU HB3 H 1 1.573 0.02 . 2 . . . . . . . . . 5782 1 393 . 1 1 63 63 LEU HD11 H 1 1.033 0.02 . 2 . . . . . . . . . 5782 1 394 . 1 1 63 63 LEU HD12 H 1 1.033 0.02 . 2 . . . . . . . . . 5782 1 395 . 1 1 63 63 LEU HD13 H 1 1.033 0.02 . 2 . . . . . . . . . 5782 1 396 . 1 1 63 63 LEU HD21 H 1 0.840 0.02 . 2 . . . . . . . . . 5782 1 397 . 1 1 63 63 LEU HD22 H 1 0.840 0.02 . 2 . . . . . . . . . 5782 1 398 . 1 1 63 63 LEU HD23 H 1 0.840 0.02 . 2 . . . . . . . . . 5782 1 399 . 1 1 64 64 TYR H H 1 9.137 0.02 . 1 . . . . . . . . . 5782 1 400 . 1 1 64 64 TYR HA H 1 5.353 0.02 . 1 . . . . . . . . . 5782 1 401 . 1 1 64 64 TYR HB2 H 1 3.044 0.02 . 2 . . . . . . . . . 5782 1 402 . 1 1 64 64 TYR HB3 H 1 2.665 0.02 . 2 . . . . . . . . . 5782 1 403 . 1 1 64 64 TYR HD1 H 1 6.993 0.02 . 1 . . . . . . . . . 5782 1 404 . 1 1 64 64 TYR HE1 H 1 6.690 0.02 . 1 . . . . . . . . . 5782 1 405 . 1 1 65 65 TYR H H 1 8.921 0.02 . 1 . . . . . . . . . 5782 1 406 . 1 1 65 65 TYR HA H 1 5.981 0.02 . 1 . . . . . . . . . 5782 1 407 . 1 1 65 65 TYR HB2 H 1 3.223 0.02 . 2 . . . . . . . . . 5782 1 408 . 1 1 65 65 TYR HB3 H 1 2.658 0.02 . 2 . . . . . . . . . 5782 1 409 . 1 1 65 65 TYR HD1 H 1 6.699 0.02 . 1 . . . . . . . . . 5782 1 410 . 1 1 65 65 TYR HE1 H 1 6.547 0.02 . 1 . . . . . . . . . 5782 1 411 . 1 1 66 66 THR H H 1 8.294 0.02 . 1 . . . . . . . . . 5782 1 412 . 1 1 66 66 THR HA H 1 4.869 0.02 . 1 . . . . . . . . . 5782 1 413 . 1 1 66 66 THR HB H 1 4.120 0.02 . 1 . . . . . . . . . 5782 1 414 . 1 1 66 66 THR HG21 H 1 0.959 0.02 . 1 . . . . . . . . . 5782 1 415 . 1 1 66 66 THR HG22 H 1 0.959 0.02 . 1 . . . . . . . . . 5782 1 416 . 1 1 66 66 THR HG23 H 1 0.959 0.02 . 1 . . . . . . . . . 5782 1 417 . 1 1 67 67 GLU H H 1 8.477 0.02 . 1 . . . . . . . . . 5782 1 418 . 1 1 67 67 GLU HA H 1 4.329 0.02 . 1 . . . . . . . . . 5782 1 419 . 1 1 67 67 GLU HB2 H 1 1.838 0.02 . 2 . . . . . . . . . 5782 1 420 . 1 1 67 67 GLU HB3 H 1 1.697 0.02 . 2 . . . . . . . . . 5782 1 421 . 1 1 67 67 GLU HG2 H 1 1.893 0.02 . 1 . . . . . . . . . 5782 1 422 . 1 1 68 68 PHE H H 1 8.750 0.02 . 1 . . . . . . . . . 5782 1 423 . 1 1 68 68 PHE HA H 1 4.845 0.02 . 1 . . . . . . . . . 5782 1 424 . 1 1 68 68 PHE HB2 H 1 2.794 0.02 . 2 . . . . . . . . . 5782 1 425 . 1 1 68 68 PHE HB3 H 1 2.704 0.02 . 2 . . . . . . . . . 5782 1 426 . 1 1 68 68 PHE HD1 H 1 6.208 0.02 . 1 . . . . . . . . . 5782 1 427 . 1 1 68 68 PHE HZ H 1 5.744 0.02 . 1 . . . . . . . . . 5782 1 428 . 1 1 69 69 THR H H 1 8.194 0.02 . 1 . . . . . . . . . 5782 1 429 . 1 1 69 69 THR HA H 1 4.472 0.02 . 1 . . . . . . . . . 5782 1 430 . 1 1 69 69 THR HB H 1 3.881 0.02 . 1 . . . . . . . . . 5782 1 431 . 1 1 69 69 THR HG21 H 1 0.865 0.02 . 1 . . . . . . . . . 5782 1 432 . 1 1 69 69 THR HG22 H 1 0.865 0.02 . 1 . . . . . . . . . 5782 1 433 . 1 1 69 69 THR HG23 H 1 0.865 0.02 . 1 . . . . . . . . . 5782 1 434 . 1 1 70 70 PRO HA H 1 4.579 0.02 . 1 . . . . . . . . . 5782 1 435 . 1 1 70 70 PRO HB2 H 1 2.389 0.02 . 2 . . . . . . . . . 5782 1 436 . 1 1 70 70 PRO HB3 H 1 1.988 0.02 . 2 . . . . . . . . . 5782 1 437 . 1 1 70 70 PRO HD2 H 1 3.977 0.02 . 2 . . . . . . . . . 5782 1 438 . 1 1 70 70 PRO HD3 H 1 2.204 0.02 . 2 . . . . . . . . . 5782 1 439 . 1 1 70 70 PRO HG2 H 1 1.413 0.02 . 1 . . . . . . . . . 5782 1 440 . 1 1 71 71 THR H H 1 8.060 0.02 . 1 . . . . . . . . . 5782 1 441 . 1 1 71 71 THR HA H 1 4.690 0.02 . 1 . . . . . . . . . 5782 1 442 . 1 1 71 71 THR HB H 1 4.538 0.02 . 1 . . . . . . . . . 5782 1 443 . 1 1 71 71 THR HG21 H 1 1.325 0.02 . 1 . . . . . . . . . 5782 1 444 . 1 1 71 71 THR HG22 H 1 1.325 0.02 . 1 . . . . . . . . . 5782 1 445 . 1 1 71 71 THR HG23 H 1 1.325 0.02 . 1 . . . . . . . . . 5782 1 446 . 1 1 72 72 GLU H H 1 9.087 0.02 . 1 . . . . . . . . . 5782 1 447 . 1 1 72 72 GLU HA H 1 4.224 0.02 . 1 . . . . . . . . . 5782 1 448 . 1 1 72 72 GLU HB2 H 1 2.289 0.02 . 2 . . . . . . . . . 5782 1 449 . 1 1 72 72 GLU HB3 H 1 2.079 0.02 . 2 . . . . . . . . . 5782 1 450 . 1 1 72 72 GLU HG2 H 1 2.327 0.02 . 1 . . . . . . . . . 5782 1 451 . 1 1 73 73 LYS H H 1 7.799 0.02 . 1 . . . . . . . . . 5782 1 452 . 1 1 73 73 LYS HA H 1 4.467 0.02 . 1 . . . . . . . . . 5782 1 453 . 1 1 73 73 LYS HB2 H 1 1.873 0.02 . 2 . . . . . . . . . 5782 1 454 . 1 1 73 73 LYS HB3 H 1 1.786 0.02 . 2 . . . . . . . . . 5782 1 455 . 1 1 73 73 LYS HD2 H 1 1.693 0.02 . 1 . . . . . . . . . 5782 1 456 . 1 1 73 73 LYS HE2 H 1 3.000 0.02 . 1 . . . . . . . . . 5782 1 457 . 1 1 73 73 LYS HG2 H 1 1.400 0.02 . 1 . . . . . . . . . 5782 1 458 . 1 1 74 74 ASP H H 1 7.121 0.02 . 1 . . . . . . . . . 5782 1 459 . 1 1 74 74 ASP HA H 1 5.130 0.02 . 1 . . . . . . . . . 5782 1 460 . 1 1 74 74 ASP HB2 H 1 2.818 0.02 . 2 . . . . . . . . . 5782 1 461 . 1 1 74 74 ASP HB3 H 1 2.165 0.02 . 2 . . . . . . . . . 5782 1 462 . 1 1 75 75 GLU H H 1 8.604 0.02 . 1 . . . . . . . . . 5782 1 463 . 1 1 75 75 GLU HA H 1 4.813 0.02 . 1 . . . . . . . . . 5782 1 464 . 1 1 75 75 GLU HB2 H 1 2.109 0.02 . 2 . . . . . . . . . 5782 1 465 . 1 1 75 75 GLU HB3 H 1 2.016 0.02 . 2 . . . . . . . . . 5782 1 466 . 1 1 75 75 GLU HG2 H 1 2.378 0.02 . 1 . . . . . . . . . 5782 1 467 . 1 1 76 76 TYR H H 1 9.458 0.02 . 1 . . . . . . . . . 5782 1 468 . 1 1 76 76 TYR HA H 1 5.615 0.02 . 1 . . . . . . . . . 5782 1 469 . 1 1 76 76 TYR HB2 H 1 2.731 0.02 . 2 . . . . . . . . . 5782 1 470 . 1 1 76 76 TYR HB3 H 1 2.834 0.02 . 2 . . . . . . . . . 5782 1 471 . 1 1 76 76 TYR HD1 H 1 7.102 0.02 . 1 . . . . . . . . . 5782 1 472 . 1 1 76 76 TYR HE1 H 1 6.897 0.02 . 1 . . . . . . . . . 5782 1 473 . 1 1 77 77 ALA H H 1 8.790 0.02 . 1 . . . . . . . . . 5782 1 474 . 1 1 77 77 ALA HA H 1 5.060 0.02 . 1 . . . . . . . . . 5782 1 475 . 1 1 77 77 ALA HB1 H 1 1.211 0.02 . 1 . . . . . . . . . 5782 1 476 . 1 1 77 77 ALA HB2 H 1 1.211 0.02 . 1 . . . . . . . . . 5782 1 477 . 1 1 77 77 ALA HB3 H 1 1.211 0.02 . 1 . . . . . . . . . 5782 1 478 . 1 1 78 78 CYS H H 1 9.109 0.02 . 1 . . . . . . . . . 5782 1 479 . 1 1 78 78 CYS HA H 1 5.123 0.02 . 1 . . . . . . . . . 5782 1 480 . 1 1 78 78 CYS HB2 H 1 3.052 0.02 . 2 . . . . . . . . . 5782 1 481 . 1 1 78 78 CYS HB3 H 1 2.630 0.02 . 2 . . . . . . . . . 5782 1 482 . 1 1 79 79 ARG H H 1 9.400 0.02 . 1 . . . . . . . . . 5782 1 483 . 1 1 79 79 ARG HA H 1 5.390 0.02 . 1 . . . . . . . . . 5782 1 484 . 1 1 79 79 ARG HB2 H 1 1.798 0.02 . 2 . . . . . . . . . 5782 1 485 . 1 1 79 79 ARG HB3 H 1 1.186 0.02 . 2 . . . . . . . . . 5782 1 486 . 1 1 79 79 ARG HD2 H 1 3.081 0.02 . 2 . . . . . . . . . 5782 1 487 . 1 1 79 79 ARG HD3 H 1 2.925 0.02 . 2 . . . . . . . . . 5782 1 488 . 1 1 79 79 ARG HE H 1 7.088 0.02 . 1 . . . . . . . . . 5782 1 489 . 1 1 79 79 ARG HG2 H 1 1.328 0.02 . 2 . . . . . . . . . 5782 1 490 . 1 1 79 79 ARG HG3 H 1 1.235 0.02 . 2 . . . . . . . . . 5782 1 491 . 1 1 80 80 VAL H H 1 9.044 0.02 . 1 . . . . . . . . . 5782 1 492 . 1 1 80 80 VAL HA H 1 4.918 0.02 . 1 . . . . . . . . . 5782 1 493 . 1 1 80 80 VAL HB H 1 1.683 0.02 . 1 . . . . . . . . . 5782 1 494 . 1 1 80 80 VAL HG11 H 1 0.814 0.02 . 2 . . . . . . . . . 5782 1 495 . 1 1 80 80 VAL HG12 H 1 0.814 0.02 . 2 . . . . . . . . . 5782 1 496 . 1 1 80 80 VAL HG13 H 1 0.814 0.02 . 2 . . . . . . . . . 5782 1 497 . 1 1 80 80 VAL HG21 H 1 0.608 0.02 . 2 . . . . . . . . . 5782 1 498 . 1 1 80 80 VAL HG22 H 1 0.608 0.02 . 2 . . . . . . . . . 5782 1 499 . 1 1 80 80 VAL HG23 H 1 0.608 0.02 . 2 . . . . . . . . . 5782 1 500 . 1 1 81 81 ASN H H 1 9.019 0.02 . 1 . . . . . . . . . 5782 1 501 . 1 1 81 81 ASN HA H 1 5.180 0.02 . 1 . . . . . . . . . 5782 1 502 . 1 1 81 81 ASN HB2 H 1 2.826 0.02 . 2 . . . . . . . . . 5782 1 503 . 1 1 81 81 ASN HB3 H 1 2.385 0.02 . 2 . . . . . . . . . 5782 1 504 . 1 1 81 81 ASN HD21 H 1 7.430 0.02 . 2 . . . . . . . . . 5782 1 505 . 1 1 81 81 ASN HD22 H 1 6.649 0.02 . 2 . . . . . . . . . 5782 1 506 . 1 1 82 82 HIS H H 1 7.756 0.02 . 1 . . . . . . . . . 5782 1 507 . 1 1 82 82 HIS HA H 1 4.584 0.02 . 1 . . . . . . . . . 5782 1 508 . 1 1 82 82 HIS HB2 H 1 2.889 0.02 . 2 . . . . . . . . . 5782 1 509 . 1 1 82 82 HIS HB3 H 1 2.451 0.02 . 2 . . . . . . . . . 5782 1 510 . 1 1 82 82 HIS HD2 H 1 7.512 0.02 . 1 . . . . . . . . . 5782 1 511 . 1 1 82 82 HIS HE1 H 1 8.157 0.02 . 1 . . . . . . . . . 5782 1 512 . 1 1 83 83 VAL H H 1 7.920 0.02 . 1 . . . . . . . . . 5782 1 513 . 1 1 83 83 VAL HA H 1 4.020 0.02 . 1 . . . . . . . . . 5782 1 514 . 1 1 83 83 VAL HB H 1 2.017 0.02 . 1 . . . . . . . . . 5782 1 515 . 1 1 83 83 VAL HG11 H 1 0.888 0.02 . 2 . . . . . . . . . 5782 1 516 . 1 1 83 83 VAL HG12 H 1 0.888 0.02 . 2 . . . . . . . . . 5782 1 517 . 1 1 83 83 VAL HG13 H 1 0.888 0.02 . 2 . . . . . . . . . 5782 1 518 . 1 1 83 83 VAL HG21 H 1 0.691 0.02 . 2 . . . . . . . . . 5782 1 519 . 1 1 83 83 VAL HG22 H 1 0.691 0.02 . 2 . . . . . . . . . 5782 1 520 . 1 1 83 83 VAL HG23 H 1 0.691 0.02 . 2 . . . . . . . . . 5782 1 521 . 1 1 84 84 THR H H 1 7.835 0.02 . 1 . . . . . . . . . 5782 1 522 . 1 1 84 84 THR HA H 1 4.257 0.02 . 1 . . . . . . . . . 5782 1 523 . 1 1 84 84 THR HB H 1 4.535 0.02 . 1 . . . . . . . . . 5782 1 524 . 1 1 84 84 THR HG21 H 1 1.596 0.02 . 1 . . . . . . . . . 5782 1 525 . 1 1 84 84 THR HG22 H 1 1.596 0.02 . 1 . . . . . . . . . 5782 1 526 . 1 1 84 84 THR HG23 H 1 1.596 0.02 . 1 . . . . . . . . . 5782 1 527 . 1 1 85 85 LEU H H 1 8.025 0.02 . 1 . . . . . . . . . 5782 1 528 . 1 1 85 85 LEU HA H 1 4.752 0.02 . 1 . . . . . . . . . 5782 1 529 . 1 1 85 85 LEU HB2 H 1 2.068 0.02 . 2 . . . . . . . . . 5782 1 530 . 1 1 85 85 LEU HB3 H 1 1.851 0.02 . 2 . . . . . . . . . 5782 1 531 . 1 1 85 85 LEU HD11 H 1 1.017 0.02 . 1 . . . . . . . . . 5782 1 532 . 1 1 85 85 LEU HD12 H 1 1.017 0.02 . 1 . . . . . . . . . 5782 1 533 . 1 1 85 85 LEU HD13 H 1 1.017 0.02 . 1 . . . . . . . . . 5782 1 534 . 1 1 85 85 LEU HG H 1 1.759 0.02 . 1 . . . . . . . . . 5782 1 535 . 1 1 86 86 SER HA H 1 4.270 0.02 . 1 . . . . . . . . . 5782 1 536 . 1 1 86 86 SER HB2 H 1 4.004 0.02 . 2 . . . . . . . . . 5782 1 537 . 1 1 86 86 SER HB3 H 1 3.969 0.02 . 2 . . . . . . . . . 5782 1 538 . 1 1 87 87 GLN H H 1 7.543 0.02 . 1 . . . . . . . . . 5782 1 539 . 1 1 87 87 GLN HA H 1 4.763 0.02 . 1 . . . . . . . . . 5782 1 540 . 1 1 87 87 GLN HB2 H 1 2.319 0.02 . 2 . . . . . . . . . 5782 1 541 . 1 1 87 87 GLN HB3 H 1 2.175 0.02 . 2 . . . . . . . . . 5782 1 542 . 1 1 87 87 GLN HG2 H 1 2.269 0.02 . 1 . . . . . . . . . 5782 1 543 . 1 1 87 87 GLN HE22 H 1 6.818 0.02 . 2 . . . . . . . . . 5782 1 544 . 1 1 87 87 GLN HE21 H 1 7.492 0.02 . 2 . . . . . . . . . 5782 1 545 . 1 1 88 88 PRO HA H 1 4.475 0.02 . 1 . . . . . . . . . 5782 1 546 . 1 1 88 88 PRO HB2 H 1 1.859 0.02 . 2 . . . . . . . . . 5782 1 547 . 1 1 88 88 PRO HB3 H 1 1.512 0.02 . 2 . . . . . . . . . 5782 1 548 . 1 1 88 88 PRO HD2 H 1 3.745 0.02 . 2 . . . . . . . . . 5782 1 549 . 1 1 88 88 PRO HD3 H 1 3.543 0.02 . 2 . . . . . . . . . 5782 1 550 . 1 1 88 88 PRO HG2 H 1 2.003 0.02 . 2 . . . . . . . . . 5782 1 551 . 1 1 88 88 PRO HG3 H 1 1.783 0.02 . 2 . . . . . . . . . 5782 1 552 . 1 1 89 89 LYS H H 1 8.706 0.02 . 1 . . . . . . . . . 5782 1 553 . 1 1 89 89 LYS HA H 1 4.556 0.02 . 1 . . . . . . . . . 5782 1 554 . 1 1 89 89 LYS HB2 H 1 1.746 0.02 . 2 . . . . . . . . . 5782 1 555 . 1 1 89 89 LYS HB3 H 1 1.663 0.02 . 2 . . . . . . . . . 5782 1 556 . 1 1 89 89 LYS HG2 H 1 1.441 0.02 . 2 . . . . . . . . . 5782 1 557 . 1 1 89 89 LYS HG3 H 1 1.366 0.02 . 2 . . . . . . . . . 5782 1 558 . 1 1 90 90 ILE H H 1 8.482 0.02 . 1 . . . . . . . . . 5782 1 559 . 1 1 90 90 ILE HA H 1 4.819 0.02 . 1 . . . . . . . . . 5782 1 560 . 1 1 90 90 ILE HB H 1 1.705 0.02 . 1 . . . . . . . . . 5782 1 561 . 1 1 90 90 ILE HD11 H 1 0.755 0.02 . 1 . . . . . . . . . 5782 1 562 . 1 1 90 90 ILE HD12 H 1 0.755 0.02 . 1 . . . . . . . . . 5782 1 563 . 1 1 90 90 ILE HD13 H 1 0.755 0.02 . 1 . . . . . . . . . 5782 1 564 . 1 1 90 90 ILE HG12 H 1 1.428 0.02 . 1 . . . . . . . . . 5782 1 565 . 1 1 90 90 ILE HG21 H 1 0.632 0.02 . 1 . . . . . . . . . 5782 1 566 . 1 1 90 90 ILE HG22 H 1 0.632 0.02 . 1 . . . . . . . . . 5782 1 567 . 1 1 90 90 ILE HG23 H 1 0.632 0.02 . 1 . . . . . . . . . 5782 1 568 . 1 1 91 91 VAL H H 1 9.034 0.02 . 1 . . . . . . . . . 5782 1 569 . 1 1 91 91 VAL HA H 1 4.336 0.02 . 1 . . . . . . . . . 5782 1 570 . 1 1 91 91 VAL HB H 1 1.894 0.02 . 1 . . . . . . . . . 5782 1 571 . 1 1 91 91 VAL HG11 H 1 1.049 0.02 . 2 . . . . . . . . . 5782 1 572 . 1 1 91 91 VAL HG12 H 1 1.049 0.02 . 2 . . . . . . . . . 5782 1 573 . 1 1 91 91 VAL HG13 H 1 1.049 0.02 . 2 . . . . . . . . . 5782 1 574 . 1 1 91 91 VAL HG21 H 1 0.937 0.02 . 2 . . . . . . . . . 5782 1 575 . 1 1 91 91 VAL HG22 H 1 0.937 0.02 . 2 . . . . . . . . . 5782 1 576 . 1 1 91 91 VAL HG23 H 1 0.937 0.02 . 2 . . . . . . . . . 5782 1 577 . 1 1 92 92 LYS H H 1 8.763 0.02 . 1 . . . . . . . . . 5782 1 578 . 1 1 92 92 LYS HA H 1 4.472 0.02 . 1 . . . . . . . . . 5782 1 579 . 1 1 92 92 LYS HB2 H 1 1.861 0.02 . 1 . . . . . . . . . 5782 1 580 . 1 1 92 92 LYS HE2 H 1 3.008 0.02 . 1 . . . . . . . . . 5782 1 581 . 1 1 92 92 LYS HG2 H 1 1.565 0.02 . 2 . . . . . . . . . 5782 1 582 . 1 1 92 92 LYS HG3 H 1 1.443 0.02 . 2 . . . . . . . . . 5782 1 583 . 1 1 93 93 TRP H H 1 8.700 0.02 . 1 . . . . . . . . . 5782 1 584 . 1 1 93 93 TRP HA H 1 4.665 0.02 . 1 . . . . . . . . . 5782 1 585 . 1 1 93 93 TRP HB2 H 1 3.515 0.02 . 2 . . . . . . . . . 5782 1 586 . 1 1 93 93 TRP HB3 H 1 2.621 0.02 . 2 . . . . . . . . . 5782 1 587 . 1 1 93 93 TRP HD1 H 1 7.131 0.02 . 1 . . . . . . . . . 5782 1 588 . 1 1 93 93 TRP HE1 H 1 10.472 0.02 . 1 . . . . . . . . . 5782 1 589 . 1 1 93 93 TRP HE3 H 1 7.980 0.02 . 1 . . . . . . . . . 5782 1 590 . 1 1 93 93 TRP HH2 H 1 6.983 0.02 . 1 . . . . . . . . . 5782 1 591 . 1 1 93 93 TRP HZ2 H 1 7.640 0.02 . 1 . . . . . . . . . 5782 1 592 . 1 1 93 93 TRP HZ3 H 1 7.478 0.02 . 1 . . . . . . . . . 5782 1 593 . 1 1 94 94 ASP H H 1 8.432 0.02 . 1 . . . . . . . . . 5782 1 594 . 1 1 94 94 ASP HA H 1 4.492 0.02 . 1 . . . . . . . . . 5782 1 595 . 1 1 94 94 ASP HB2 H 1 2.760 0.02 . 2 . . . . . . . . . 5782 1 596 . 1 1 94 94 ASP HB3 H 1 2.472 0.02 . 2 . . . . . . . . . 5782 1 597 . 1 1 95 95 ARG H H 1 7.410 0.02 . 1 . . . . . . . . . 5782 1 598 . 1 1 95 95 ARG HA H 1 3.388 0.02 . 1 . . . . . . . . . 5782 1 599 . 1 1 95 95 ARG HB2 H 1 1.423 0.02 . 2 . . . . . . . . . 5782 1 600 . 1 1 95 95 ARG HB3 H 1 1.149 0.02 . 2 . . . . . . . . . 5782 1 601 . 1 1 95 95 ARG HD2 H 1 2.953 0.02 . 1 . . . . . . . . . 5782 1 602 . 1 1 95 95 ARG HG3 H 1 0.946 0.02 . 1 . . . . . . . . . 5782 1 603 . 1 1 96 96 ASP H H 1 8.192 0.02 . 1 . . . . . . . . . 5782 1 604 . 1 1 96 96 ASP HA H 1 4.663 0.02 . 1 . . . . . . . . . 5782 1 605 . 1 1 96 96 ASP HB2 H 1 2.783 0.02 . 2 . . . . . . . . . 5782 1 606 . 1 1 96 96 ASP HB3 H 1 2.611 0.02 . 2 . . . . . . . . . 5782 1 607 . 1 1 97 97 MET H H 1 7.586 0.02 . 1 . . . . . . . . . 5782 1 608 . 1 1 97 97 MET HA H 1 4.294 0.02 . 1 . . . . . . . . . 5782 1 609 . 1 1 97 97 MET HB2 H 1 2.172 0.02 . 2 . . . . . . . . . 5782 1 610 . 1 1 97 97 MET HB3 H 1 2.027 0.02 . 2 . . . . . . . . . 5782 1 611 . 1 1 97 97 MET HG2 H 1 2.172 0.02 . 2 . . . . . . . . . 5782 1 612 . 1 1 97 97 MET HG3 H 1 2.542 0.02 . 2 . . . . . . . . . 5782 1 stop_ save_ save_shift_set_2 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode shift_set_2 _Assigned_chem_shift_list.Entry_ID 5782 _Assigned_chem_shift_list.ID 2 _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 ; For several residues a second chemical shift is observed, indicating a minor conformational species (25%). ; _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' . . . 5782 2 2 '1H-1H NOESY' . . . 5782 2 3 '1H-1H DQF-COSY' . . . 5782 2 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 5 5 ILE H H 1 8.344 0.02 . 1 . . . . . . . . . 5782 2 2 . 1 1 5 5 ILE HA H 1 4.848 0.02 . 1 . . . . . . . . . 5782 2 3 . 1 1 5 5 ILE HB H 1 1.656 0.02 . 1 . . . . . . . . . 5782 2 4 . 1 1 6 6 GLN H H 1 9.205 0.02 . 1 . . . . . . . . . 5782 2 5 . 1 1 6 6 GLN HA H 1 4.942 0.02 . 1 . . . . . . . . . 5782 2 6 . 1 1 6 6 GLN HB2 H 1 2.348 0.02 . 2 . . . . . . . . . 5782 2 7 . 1 1 6 6 GLN HB3 H 1 2.214 0.02 . 2 . . . . . . . . . 5782 2 8 . 1 1 7 7 VAL H H 1 8.872 0.02 . 1 . . . . . . . . . 5782 2 9 . 1 1 7 7 VAL HA H 1 5.396 0.02 . 1 . . . . . . . . . 5782 2 10 . 1 1 7 7 VAL HB H 1 1.975 0.02 . 1 . . . . . . . . . 5782 2 11 . 1 1 7 7 VAL HG11 H 1 0.886 0.02 . 2 . . . . . . . . . 5782 2 12 . 1 1 7 7 VAL HG12 H 1 0.886 0.02 . 2 . . . . . . . . . 5782 2 13 . 1 1 7 7 VAL HG13 H 1 0.886 0.02 . 2 . . . . . . . . . 5782 2 14 . 1 1 7 7 VAL HG21 H 1 0.951 0.02 . 2 . . . . . . . . . 5782 2 15 . 1 1 7 7 VAL HG22 H 1 0.951 0.02 . 2 . . . . . . . . . 5782 2 16 . 1 1 7 7 VAL HG23 H 1 0.951 0.02 . 2 . . . . . . . . . 5782 2 17 . 1 1 8 8 TYR H H 1 8.595 0.02 . 1 . . . . . . . . . 5782 2 18 . 1 1 8 8 TYR HA H 1 5.299 0.02 . 1 . . . . . . . . . 5782 2 19 . 1 1 20 20 PHE H H 1 10.362 0.02 . 1 . . . . . . . . . 5782 2 20 . 1 1 20 20 PHE HA H 1 5.434 0.02 . 1 . . . . . . . . . 5782 2 21 . 1 1 20 20 PHE HB2 H 1 2.658 0.02 . 1 . . . . . . . . . 5782 2 22 . 1 1 20 20 PHE HD1 H 1 7.017 0.02 . 1 . . . . . . . . . 5782 2 23 . 1 1 23 23 CYS H H 1 9.622 0.02 . 1 . . . . . . . . . 5782 2 24 . 1 1 24 24 TYR H H 1 9.586 0.02 . 1 . . . . . . . . . 5782 2 25 . 1 1 24 24 TYR HA H 1 5.403 0.02 . 1 . . . . . . . . . 5782 2 26 . 1 1 24 24 TYR HB2 H 1 3.018 0.02 . 1 . . . . . . . . . 5782 2 27 . 1 1 35 35 VAL H H 1 8.140 0.02 . 1 . . . . . . . . . 5782 2 28 . 1 1 35 35 VAL HA H 1 4.793 0.02 . 1 . . . . . . . . . 5782 2 29 . 1 1 35 35 VAL HB H 1 0.617 0.02 . 1 . . . . . . . . . 5782 2 30 . 1 1 35 35 VAL HG11 H 1 0.451 0.02 . 2 . . . . . . . . . 5782 2 31 . 1 1 35 35 VAL HG12 H 1 0.451 0.02 . 2 . . . . . . . . . 5782 2 32 . 1 1 35 35 VAL HG13 H 1 0.451 0.02 . 2 . . . . . . . . . 5782 2 33 . 1 1 35 35 VAL HG21 H 1 0.200 0.02 . 2 . . . . . . . . . 5782 2 34 . 1 1 35 35 VAL HG22 H 1 0.200 0.02 . 2 . . . . . . . . . 5782 2 35 . 1 1 35 35 VAL HG23 H 1 0.200 0.02 . 2 . . . . . . . . . 5782 2 36 . 1 1 36 36 ASP H H 1 8.909 0.02 . 1 . . . . . . . . . 5782 2 37 . 1 1 36 36 ASP HA H 1 5.032 0.02 . 1 . . . . . . . . . 5782 2 38 . 1 1 36 36 ASP HB2 H 1 2.183 0.02 . 1 . . . . . . . . . 5782 2 39 . 1 1 47 47 VAL H H 1 7.939 0.02 . 1 . . . . . . . . . 5782 2 40 . 1 1 47 47 VAL HA H 1 4.507 0.02 . 1 . . . . . . . . . 5782 2 41 . 1 1 47 47 VAL HB H 1 2.053 0.02 . 1 . . . . . . . . . 5782 2 42 . 1 1 47 47 VAL HG11 H 1 1.070 0.02 . 2 . . . . . . . . . 5782 2 43 . 1 1 47 47 VAL HG12 H 1 1.070 0.02 . 2 . . . . . . . . . 5782 2 44 . 1 1 47 47 VAL HG13 H 1 1.070 0.02 . 2 . . . . . . . . . 5782 2 45 . 1 1 47 47 VAL HG21 H 1 0.986 0.02 . 2 . . . . . . . . . 5782 2 46 . 1 1 47 47 VAL HG22 H 1 0.986 0.02 . 2 . . . . . . . . . 5782 2 47 . 1 1 47 47 VAL HG23 H 1 0.986 0.02 . 2 . . . . . . . . . 5782 2 48 . 1 1 48 48 GLU H H 1 8.532 0.02 . 1 . . . . . . . . . 5782 2 49 . 1 1 48 48 GLU HA H 1 4.507 0.02 . 1 . . . . . . . . . 5782 2 50 . 1 1 48 48 GLU HB2 H 1 1.581 0.02 . 2 . . . . . . . . . 5782 2 51 . 1 1 48 48 GLU HB3 H 1 0.713 0.02 . 2 . . . . . . . . . 5782 2 52 . 1 1 53 53 SER H H 1 8.079 0.02 . 1 . . . . . . . . . 5782 2 53 . 1 1 53 53 SER HA H 1 4.709 0.02 . 1 . . . . . . . . . 5782 2 54 . 1 1 53 53 SER HB3 H 1 2.674 0.02 . 1 . . . . . . . . . 5782 2 55 . 1 1 64 64 TYR H H 1 9.067 0.02 . 1 . . . . . . . . . 5782 2 56 . 1 1 64 64 TYR HA H 1 5.345 0.02 . 1 . . . . . . . . . 5782 2 57 . 1 1 64 64 TYR HB2 H 1 2.840 0.02 . 2 . . . . . . . . . 5782 2 58 . 1 1 64 64 TYR HB3 H 1 2.642 0.02 . 2 . . . . . . . . . 5782 2 59 . 1 1 65 65 TYR H H 1 8.967 0.02 . 1 . . . . . . . . . 5782 2 60 . 1 1 65 65 TYR HA H 1 6.056 0.02 . 1 . . . . . . . . . 5782 2 61 . 1 1 65 65 TYR HB2 H 1 3.046 0.02 . 2 . . . . . . . . . 5782 2 62 . 1 1 65 65 TYR HB3 H 1 2.735 0.02 . 2 . . . . . . . . . 5782 2 63 . 1 1 67 67 GLU H H 1 8.466 0.02 . 1 . . . . . . . . . 5782 2 64 . 1 1 67 67 GLU HA H 1 4.361 0.02 . 1 . . . . . . . . . 5782 2 65 . 1 1 67 67 GLU HB2 H 1 1.857 0.02 . 1 . . . . . . . . . 5782 2 66 . 1 1 76 76 TYR H H 1 9.447 0.02 . 1 . . . . . . . . . 5782 2 67 . 1 1 76 76 TYR HA H 1 5.686 0.02 . 1 . . . . . . . . . 5782 2 68 . 1 1 76 76 TYR HB2 H 1 2.824 0.02 . 2 . . . . . . . . . 5782 2 69 . 1 1 76 76 TYR HB3 H 1 2.752 0.02 . 2 . . . . . . . . . 5782 2 70 . 1 1 77 77 ALA H H 1 8.790 0.02 . 1 . . . . . . . . . 5782 2 71 . 1 1 77 77 ALA HA H 1 5.059 0.02 . 1 . . . . . . . . . 5782 2 72 . 1 1 77 77 ALA HB1 H 1 1.218 0.02 . 1 . . . . . . . . . 5782 2 73 . 1 1 77 77 ALA HB2 H 1 1.218 0.02 . 1 . . . . . . . . . 5782 2 74 . 1 1 77 77 ALA HB3 H 1 1.218 0.02 . 1 . . . . . . . . . 5782 2 75 . 1 1 79 79 ARG H H 1 9.363 0.02 . 1 . . . . . . . . . 5782 2 76 . 1 1 79 79 ARG HA H 1 5.379 0.02 . 1 . . . . . . . . . 5782 2 77 . 1 1 79 79 ARG HB2 H 1 1.830 0.02 . 2 . . . . . . . . . 5782 2 78 . 1 1 79 79 ARG HB3 H 1 1.174 0.02 . 2 . . . . . . . . . 5782 2 79 . 1 1 81 81 ASN H H 1 8.931 0.02 . 1 . . . . . . . . . 5782 2 80 . 1 1 81 81 ASN HA H 1 5.167 0.02 . 1 . . . . . . . . . 5782 2 81 . 1 1 81 81 ASN HB2 H 1 2.810 0.02 . 2 . . . . . . . . . 5782 2 82 . 1 1 81 81 ASN HB3 H 1 2.413 0.02 . 2 . . . . . . . . . 5782 2 83 . 1 1 82 82 HIS H H 1 7.790 0.02 . 1 . . . . . . . . . 5782 2 84 . 1 1 82 82 HIS HA H 1 4.588 0.02 . 1 . . . . . . . . . 5782 2 85 . 1 1 83 83 VAL H H 1 7.950 0.02 . 1 . . . . . . . . . 5782 2 86 . 1 1 87 87 GLN H H 1 7.527 0.02 . 1 . . . . . . . . . 5782 2 87 . 1 1 87 87 GLN HA H 1 4.798 0.02 . 1 . . . . . . . . . 5782 2 88 . 1 1 89 89 LYS H H 1 8.563 0.02 . 1 . . . . . . . . . 5782 2 89 . 1 1 89 89 LYS HA H 1 4.556 0.02 . 1 . . . . . . . . . 5782 2 90 . 1 1 89 89 LYS HB2 H 1 1.742 0.02 . 1 . . . . . . . . . 5782 2 91 . 1 1 89 89 LYS HG2 H 1 1.440 0.02 . 1 . . . . . . . . . 5782 2 92 . 1 1 91 91 VAL H H 1 8.987 0.02 . 1 . . . . . . . . . 5782 2 93 . 1 1 91 91 VAL HA H 1 4.294 0.02 . 1 . . . . . . . . . 5782 2 94 . 1 1 91 91 VAL HB H 1 1.885 0.02 . 1 . . . . . . . . . 5782 2 95 . 1 1 91 91 VAL HG11 H 1 1.024 0.02 . 1 . . . . . . . . . 5782 2 96 . 1 1 91 91 VAL HG12 H 1 1.024 0.02 . 1 . . . . . . . . . 5782 2 97 . 1 1 91 91 VAL HG13 H 1 1.024 0.02 . 1 . . . . . . . . . 5782 2 98 . 1 1 94 94 ASP H H 1 8.506 0.02 . 1 . . . . . . . . . 5782 2 99 . 1 1 94 94 ASP HA H 1 4.521 0.02 . 1 . . . . . . . . . 5782 2 100 . 1 1 94 94 ASP HB2 H 1 2.779 0.02 . 2 . . . . . . . . . 5782 2 101 . 1 1 94 94 ASP HB3 H 1 2.491 0.02 . 2 . . . . . . . . . 5782 2 102 . 1 1 95 95 ARG H H 1 7.442 0.02 . 1 . . . . . . . . . 5782 2 103 . 1 1 95 95 ARG HA H 1 3.407 0.02 . 1 . . . . . . . . . 5782 2 104 . 1 1 95 95 ARG HB3 H 1 1.147 0.02 . 1 . . . . . . . . . 5782 2 stop_ save_