data_18387 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 18387 _Entry.Title ; Solution structure of a thiol:disulfide interchange protein from Bacteroides sp. ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2012-04-10 _Entry.Accession_date 2012-04-10 _Entry.Last_release_date 2012-05-21 _Entry.Original_release_date 2012-05-21 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype 'SOLUTION NMR' _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 R. Harris . . . 18387 2 A. Bandaranayake . D. . 18387 3 R. Banu . . . 18387 4 J. Bonanno . B. . 18387 5 D. Calarese . A. . 18387 6 A. Celikgil . . . 18387 7 S. Chamala . . . 18387 8 M. Chan . K. . 18387 9 R. Chaparro . . . 18387 10 B. Evans . . . 18387 11 S. Garforth . . . 18387 12 A. Gizzi . . . 18387 13 B. Hillerich . . . 18387 14 A. Kar . . . 18387 15 J. Lafleur . . . 18387 16 S. Lim . . . 18387 17 J. Love . . . 18387 18 B. Matikainen . . . 18387 19 H. Patel . . . 18387 20 R. Seidel . D. . 18387 21 B. Smith . . . 18387 22 M. Stead . . . 18387 23 M. Girvin . E. . 18387 24 S. Almo . C. . 18387 stop_ loop_ _SG_project.SG_project_ID _SG_project.Project_name _SG_project.Full_name_of_center _SG_project.Initial_of_center _SG_project.Entry_ID 1 'PSI, Protein Structure Initiative' 'New York Structural Genomics Research Consortium' . 18387 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID 'New York Structural Genomics Research Consortium' . 18387 'STRUCTURAL GENOMICS' . 18387 THIOREDOXIN-LIKE . 18387 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 18387 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 676 18387 '15N chemical shifts' 149 18387 '1H chemical shifts' 1036 18387 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 . . 2012-05-21 2012-04-10 original author . 18387 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 2LRN 'BMRB Entry Tracking System' 18387 TargetDB NYSGRC-011666 . 18387 stop_ save_ ############### # Citations # ############### save_citations _Citation.Sf_category citations _Citation.Sf_framecode citations _Citation.Entry_ID 18387 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title 'Solution structure of a thiol:disulfide interchange protein from Bacteroides sp.' _Citation.Status 'in preparation' _Citation.Type journal _Citation.Journal_abbrev 'To be published' _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.Entry_ID _Citation_author.Citation_ID 1 R. Harris . . . 18387 1 2 A. Bandaranayake . D. . 18387 1 3 R. Banu . . . 18387 1 4 J. Bonanno . B. . 18387 1 5 D. Calarese . A. . 18387 1 6 A. Celikgil . . . 18387 1 7 S. Chamala . . . 18387 1 8 M. Chan . K. . 18387 1 9 R. Chaparro . . . 18387 1 10 B. Evans . . . 18387 1 11 S. Garforth . . . 18387 1 12 A. Gizzi . . . 18387 1 13 B. Hillerich . . . 18387 1 14 A. Kar . . . 18387 1 15 J. Lafleur . . . 18387 1 16 S. Lim . . . 18387 1 17 J. Love . . . 18387 1 18 B. Matikainen . . . 18387 1 19 H. Patel . . . 18387 1 20 R. Seidel . D. . 18387 1 21 B. Smith . . . 18387 1 22 M. Stead . . . 18387 1 23 M. Girvin . E. . 18387 1 24 S. Almo . C. . 18387 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 18387 _Assembly.ID 1 _Assembly.Name 'thiol:disulfide interchange protein' _Assembly.BMRB_code . _Assembly.Number_of_components 1 _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 . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . 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 'thiol:disulfide interchange protein' 1 $thiol:disulfide_interchange_protein A . yes native no no . . . 18387 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_thiol:disulfide_interchange_protein _Entity.Sf_category entity _Entity.Sf_framecode thiol:disulfide_interchange_protein _Entity.Entry_ID 18387 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name thiol:disulfide_interchange_protein _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID A _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; MSLATGSVAPAITGIDLKGN SVSLNDFKGKYVLVDFWFAG CSWCRKETPYLLKTYNAFKD KGFTIYGVSTDRREEDWKKA IEEDKSYWNQVLLQKDDVKD VLESYCIVGFPHIILVDPEG KIVAKELRGDDLYNTVEKFV NGAKEGHHHHHH ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states no _Entity.Ambiguous_chem_comp_sites no _Entity.Nstd_monomer no _Entity.Nstd_chirality no _Entity.Nstd_linkage no _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 152 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state . _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 17364.814 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-25 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no PDB 2LRN . "Solution Structure Of A Thiol:disulfide Interchange Protein From Bacteroides Sp." . . . . . 100.00 152 100.00 100.00 2.70e-107 . . . . 18387 1 2 no PDB 4GRF . "Crystal Structure Of Thioredoxin Domain Of Thiol-Disulfide Oxidoreductase Bvu-2223 (Target Efi-501010) From Bacteroides Vulgatu" . . . . . 100.00 152 100.00 100.00 2.70e-107 . . . . 18387 1 3 no EMBL CDF17112 . "thiol-disulfide oxidoreductase [Bacteroides vulgatus CAG:6]" . . . . . 92.76 392 100.00 100.00 6.18e-97 . . . . 18387 1 4 no EMBL CUO45804 . "thiol-disulfide oxidoreductase [Bacteroides vulgatus]" . . . . . 92.76 392 100.00 100.00 6.74e-97 . . . . 18387 1 5 no EMBL CUP23578 . "thiol-disulfide oxidoreductase [Bacteroides vulgatus]" . . . . . 92.76 392 100.00 100.00 6.18e-97 . . . . 18387 1 6 no EMBL CUQ28905 . "thiol-disulfide oxidoreductase [Bacteroides vulgatus]" . . . . . 92.76 392 100.00 100.00 6.31e-97 . . . . 18387 1 7 no GB ABR39883 . "putative thiol-disulfide oxidoreductase [Bacteroides vulgatus ATCC 8482]" . . . . . 92.76 392 100.00 100.00 6.31e-97 . . . . 18387 1 8 no GB AII62327 . "thiol-disulfide oxidoreductase [Bacteroides dorei]" . . . . . 92.76 392 98.58 100.00 2.57e-95 . . . . 18387 1 9 no GB AII68254 . "thiol-disulfide oxidoreductase [Bacteroides dorei]" . . . . . 92.76 392 98.58 100.00 2.57e-95 . . . . 18387 1 10 no GB ALA74015 . "thiol-disulfide oxidoreductase [Bacteroides dorei]" . . . . . 92.76 392 98.58 100.00 2.57e-95 . . . . 18387 1 11 no GB ALK84387 . "Thiol-disulfide oxidoreductase resA [Bacteroides vulgatus]" . . . . . 92.76 392 100.00 100.00 6.31e-97 . . . . 18387 1 12 no REF WP_005839115 . "thiol-disulfide oxidoreductase [Bacteroides vulgatus]" . . . . . 92.76 392 100.00 100.00 6.31e-97 . . . . 18387 1 13 no REF WP_005848742 . "thiol-disulfide oxidoreductase [Bacteroides vulgatus]" . . . . . 92.76 392 100.00 100.00 6.18e-97 . . . . 18387 1 14 no REF WP_007844725 . "thiol-disulfide oxidoreductase [Bacteroides dorei]" . . . . . 92.76 392 98.58 100.00 3.09e-95 . . . . 18387 1 15 no REF WP_007845545 . "MULTISPECIES: thiol-disulfide oxidoreductase [Bacteroides]" . . . . . 92.76 392 98.58 100.00 2.57e-95 . . . . 18387 1 16 no REF WP_008668408 . "MULTISPECIES: thiol-disulfide oxidoreductase [Bacteroides]" . . . . . 92.76 392 100.00 100.00 6.18e-97 . . . . 18387 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 . 18387 1 2 . SER . 18387 1 3 . LEU . 18387 1 4 . ALA . 18387 1 5 . THR . 18387 1 6 . GLY . 18387 1 7 . SER . 18387 1 8 . VAL . 18387 1 9 . ALA . 18387 1 10 . PRO . 18387 1 11 . ALA . 18387 1 12 . ILE . 18387 1 13 . THR . 18387 1 14 . GLY . 18387 1 15 . ILE . 18387 1 16 . ASP . 18387 1 17 . LEU . 18387 1 18 . LYS . 18387 1 19 . GLY . 18387 1 20 . ASN . 18387 1 21 . SER . 18387 1 22 . VAL . 18387 1 23 . SER . 18387 1 24 . LEU . 18387 1 25 . ASN . 18387 1 26 . ASP . 18387 1 27 . PHE . 18387 1 28 . LYS . 18387 1 29 . GLY . 18387 1 30 . LYS . 18387 1 31 . TYR . 18387 1 32 . VAL . 18387 1 33 . LEU . 18387 1 34 . VAL . 18387 1 35 . ASP . 18387 1 36 . PHE . 18387 1 37 . TRP . 18387 1 38 . PHE . 18387 1 39 . ALA . 18387 1 40 . GLY . 18387 1 41 . CYS . 18387 1 42 . SER . 18387 1 43 . TRP . 18387 1 44 . CYS . 18387 1 45 . ARG . 18387 1 46 . LYS . 18387 1 47 . GLU . 18387 1 48 . THR . 18387 1 49 . PRO . 18387 1 50 . TYR . 18387 1 51 . LEU . 18387 1 52 . LEU . 18387 1 53 . LYS . 18387 1 54 . THR . 18387 1 55 . TYR . 18387 1 56 . ASN . 18387 1 57 . ALA . 18387 1 58 . PHE . 18387 1 59 . LYS . 18387 1 60 . ASP . 18387 1 61 . LYS . 18387 1 62 . GLY . 18387 1 63 . PHE . 18387 1 64 . THR . 18387 1 65 . ILE . 18387 1 66 . TYR . 18387 1 67 . GLY . 18387 1 68 . VAL . 18387 1 69 . SER . 18387 1 70 . THR . 18387 1 71 . ASP . 18387 1 72 . ARG . 18387 1 73 . ARG . 18387 1 74 . GLU . 18387 1 75 . GLU . 18387 1 76 . ASP . 18387 1 77 . TRP . 18387 1 78 . LYS . 18387 1 79 . LYS . 18387 1 80 . ALA . 18387 1 81 . ILE . 18387 1 82 . GLU . 18387 1 83 . GLU . 18387 1 84 . ASP . 18387 1 85 . LYS . 18387 1 86 . SER . 18387 1 87 . TYR . 18387 1 88 . TRP . 18387 1 89 . ASN . 18387 1 90 . GLN . 18387 1 91 . VAL . 18387 1 92 . LEU . 18387 1 93 . LEU . 18387 1 94 . GLN . 18387 1 95 . LYS . 18387 1 96 . ASP . 18387 1 97 . ASP . 18387 1 98 . VAL . 18387 1 99 . LYS . 18387 1 100 . ASP . 18387 1 101 . VAL . 18387 1 102 . LEU . 18387 1 103 . GLU . 18387 1 104 . SER . 18387 1 105 . TYR . 18387 1 106 . CYS . 18387 1 107 . ILE . 18387 1 108 . VAL . 18387 1 109 . GLY . 18387 1 110 . PHE . 18387 1 111 . PRO . 18387 1 112 . HIS . 18387 1 113 . ILE . 18387 1 114 . ILE . 18387 1 115 . LEU . 18387 1 116 . VAL . 18387 1 117 . ASP . 18387 1 118 . PRO . 18387 1 119 . GLU . 18387 1 120 . GLY . 18387 1 121 . LYS . 18387 1 122 . ILE . 18387 1 123 . VAL . 18387 1 124 . ALA . 18387 1 125 . LYS . 18387 1 126 . GLU . 18387 1 127 . LEU . 18387 1 128 . ARG . 18387 1 129 . GLY . 18387 1 130 . ASP . 18387 1 131 . ASP . 18387 1 132 . LEU . 18387 1 133 . TYR . 18387 1 134 . ASN . 18387 1 135 . THR . 18387 1 136 . VAL . 18387 1 137 . GLU . 18387 1 138 . LYS . 18387 1 139 . PHE . 18387 1 140 . VAL . 18387 1 141 . ASN . 18387 1 142 . GLY . 18387 1 143 . ALA . 18387 1 144 . LYS . 18387 1 145 . GLU . 18387 1 146 . GLY . 18387 1 147 . HIS . 18387 1 148 . HIS . 18387 1 149 . HIS . 18387 1 150 . HIS . 18387 1 151 . HIS . 18387 1 152 . HIS . 18387 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 18387 1 . SER 2 2 18387 1 . LEU 3 3 18387 1 . ALA 4 4 18387 1 . THR 5 5 18387 1 . GLY 6 6 18387 1 . SER 7 7 18387 1 . VAL 8 8 18387 1 . ALA 9 9 18387 1 . PRO 10 10 18387 1 . ALA 11 11 18387 1 . ILE 12 12 18387 1 . THR 13 13 18387 1 . GLY 14 14 18387 1 . ILE 15 15 18387 1 . ASP 16 16 18387 1 . LEU 17 17 18387 1 . LYS 18 18 18387 1 . GLY 19 19 18387 1 . ASN 20 20 18387 1 . SER 21 21 18387 1 . VAL 22 22 18387 1 . SER 23 23 18387 1 . LEU 24 24 18387 1 . ASN 25 25 18387 1 . ASP 26 26 18387 1 . PHE 27 27 18387 1 . LYS 28 28 18387 1 . GLY 29 29 18387 1 . LYS 30 30 18387 1 . TYR 31 31 18387 1 . VAL 32 32 18387 1 . LEU 33 33 18387 1 . VAL 34 34 18387 1 . ASP 35 35 18387 1 . PHE 36 36 18387 1 . TRP 37 37 18387 1 . PHE 38 38 18387 1 . ALA 39 39 18387 1 . GLY 40 40 18387 1 . CYS 41 41 18387 1 . SER 42 42 18387 1 . TRP 43 43 18387 1 . CYS 44 44 18387 1 . ARG 45 45 18387 1 . LYS 46 46 18387 1 . GLU 47 47 18387 1 . THR 48 48 18387 1 . PRO 49 49 18387 1 . TYR 50 50 18387 1 . LEU 51 51 18387 1 . LEU 52 52 18387 1 . LYS 53 53 18387 1 . THR 54 54 18387 1 . TYR 55 55 18387 1 . ASN 56 56 18387 1 . ALA 57 57 18387 1 . PHE 58 58 18387 1 . LYS 59 59 18387 1 . ASP 60 60 18387 1 . LYS 61 61 18387 1 . GLY 62 62 18387 1 . PHE 63 63 18387 1 . THR 64 64 18387 1 . ILE 65 65 18387 1 . TYR 66 66 18387 1 . GLY 67 67 18387 1 . VAL 68 68 18387 1 . SER 69 69 18387 1 . THR 70 70 18387 1 . ASP 71 71 18387 1 . ARG 72 72 18387 1 . ARG 73 73 18387 1 . GLU 74 74 18387 1 . GLU 75 75 18387 1 . ASP 76 76 18387 1 . TRP 77 77 18387 1 . LYS 78 78 18387 1 . LYS 79 79 18387 1 . ALA 80 80 18387 1 . ILE 81 81 18387 1 . GLU 82 82 18387 1 . GLU 83 83 18387 1 . ASP 84 84 18387 1 . LYS 85 85 18387 1 . SER 86 86 18387 1 . TYR 87 87 18387 1 . TRP 88 88 18387 1 . ASN 89 89 18387 1 . GLN 90 90 18387 1 . VAL 91 91 18387 1 . LEU 92 92 18387 1 . LEU 93 93 18387 1 . GLN 94 94 18387 1 . LYS 95 95 18387 1 . ASP 96 96 18387 1 . ASP 97 97 18387 1 . VAL 98 98 18387 1 . LYS 99 99 18387 1 . ASP 100 100 18387 1 . VAL 101 101 18387 1 . LEU 102 102 18387 1 . GLU 103 103 18387 1 . SER 104 104 18387 1 . TYR 105 105 18387 1 . CYS 106 106 18387 1 . ILE 107 107 18387 1 . VAL 108 108 18387 1 . GLY 109 109 18387 1 . PHE 110 110 18387 1 . PRO 111 111 18387 1 . HIS 112 112 18387 1 . ILE 113 113 18387 1 . ILE 114 114 18387 1 . LEU 115 115 18387 1 . VAL 116 116 18387 1 . ASP 117 117 18387 1 . PRO 118 118 18387 1 . GLU 119 119 18387 1 . GLY 120 120 18387 1 . LYS 121 121 18387 1 . ILE 122 122 18387 1 . VAL 123 123 18387 1 . ALA 124 124 18387 1 . LYS 125 125 18387 1 . GLU 126 126 18387 1 . LEU 127 127 18387 1 . ARG 128 128 18387 1 . GLY 129 129 18387 1 . ASP 130 130 18387 1 . ASP 131 131 18387 1 . LEU 132 132 18387 1 . TYR 133 133 18387 1 . ASN 134 134 18387 1 . THR 135 135 18387 1 . VAL 136 136 18387 1 . GLU 137 137 18387 1 . LYS 138 138 18387 1 . PHE 139 139 18387 1 . VAL 140 140 18387 1 . ASN 141 141 18387 1 . GLY 142 142 18387 1 . ALA 143 143 18387 1 . LYS 144 144 18387 1 . GLU 145 145 18387 1 . GLY 146 146 18387 1 . HIS 147 147 18387 1 . HIS 148 148 18387 1 . HIS 149 149 18387 1 . HIS 150 150 18387 1 . HIS 151 151 18387 1 . HIS 152 152 18387 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 18387 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Subvariant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Cellular_location _Entity_natural_src.Fragment _Entity_natural_src.Fraction _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Plasmid_details _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Dev_stage _Entity_natural_src.Details _Entity_natural_src.Citation_ID _Entity_natural_src.Citation_label _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $thiol:disulfide_interchange_protein . 29523 organism . 'Bacteroides sp.' 'Bacteroides sp.' . . Bacteria . Bacteroides sp. . . . . . . . . . . . . . . . . . . . . . 18387 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 18387 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_subvariant _Entity_experimental_src.Host_org_organ _Entity_experimental_src.Host_org_tissue _Entity_experimental_src.Host_org_tissue_fraction _Entity_experimental_src.Host_org_cell_line _Entity_experimental_src.Host_org_cell_type _Entity_experimental_src.Host_org_cellular_location _Entity_experimental_src.Host_org_organelle _Entity_experimental_src.Host_org_gene _Entity_experimental_src.Host_org_culture_collection _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Host_org_dev_stage _Entity_experimental_src.Details _Entity_experimental_src.Citation_ID _Entity_experimental_src.Citation_label _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $thiol:disulfide_interchange_protein . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli BL21(DE3) . . . . . . . . . . . . pET . . 'modified pET26' . . . . . . 18387 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 18387 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details '20mM Na phosphate buffer, 50mM NaCl, pH 7.0, 1mM DTT, 1mM EDTA' _Sample.Aggregate_sample_number . _Sample.Solvent_system '90% H2O, 10% D2O' _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 'thiol:disulfide interchange protein' '[U-13C; U-15N]' . . 1 $thiol:disulfide_interchange_protein . . 1 . . mM . . . . 18387 1 2 'sodium phosphate' 'natural abundance' . . . . . . 20 . . mM . . . . 18387 1 3 'sodium chloride' 'natural abundance' . . . . . . 50 . . mM . . . . 18387 1 4 DTT 'natural abundance' . . . . . . 1 . . mM . . . . 18387 1 5 EDTA 'natural abundance' . . . . . . 1 . . mM . . . . 18387 1 stop_ save_ save_sample_2 _Sample.Sf_category sample _Sample.Sf_framecode sample_2 _Sample.Entry_ID 18387 _Sample.ID 2 _Sample.Type solution _Sample.Sub_type . _Sample.Details '20mM Na phosphate buffer, 50mM NaCl, pD6.6, 1mM DTT, 1mM EDTA' _Sample.Aggregate_sample_number . _Sample.Solvent_system '100% D2O' _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 'thiol:disulfide interchange protein' '[U-13C; U-15N]' . . 1 $thiol:disulfide_interchange_protein . . 1 . . mM . . . . 18387 2 2 'sodium phosphate' 'natural abundance' . . . . . . 20 . . mM . . . . 18387 2 3 'sodium chloride' 'natural abundance' . . . . . . 50 . . mM . . . . 18387 2 4 DTT 'natural abundance' . . . . . . 1 . . mM . . . . 18387 2 5 EDTA 'natural abundance' . . . . . . 1 . . mM . . . . 18387 2 stop_ save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_conditions_1 _Sample_condition_list.Entry_ID 18387 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID 'ionic strength' 70 . mM 18387 1 pH 7.0 . pH 18387 1 pressure 1 . atm 18387 1 temperature 303 . K 18387 1 stop_ save_ ############################ # Computer software used # ############################ save_CNS _Software.Sf_category software _Software.Sf_framecode CNS _Software.Entry_ID 18387 _Software.ID 1 _Software.Name CNS _Software.Version 1.21 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Brunger A. T. et.al.' . . 18387 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID refinement 18387 1 'structure solution' 18387 1 stop_ save_ save_CCPN _Software.Sf_category software _Software.Sf_framecode CCPN _Software.Entry_ID 18387 _Software.ID 2 _Software.Name CCPN _Software.Version 2.1.5 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID CCPN . . 18387 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 18387 2 'peak picking' 18387 2 stop_ save_ save_ARIA _Software.Sf_category software _Software.Sf_framecode ARIA _Software.Entry_ID 18387 _Software.ID 3 _Software.Name ARIA _Software.Version 2.3 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Linge, O'Donoghue and Nilges' . . 18387 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'data analysis' 18387 3 stop_ save_ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 18387 _Software.ID 4 _Software.Name NMRPipe _Software.Version 5.4 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . 18387 4 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 18387 4 stop_ save_ save_MDDNMR _Software.Sf_category software _Software.Sf_framecode MDDNMR _Software.Entry_ID 18387 _Software.ID 5 _Software.Name MDDNMR _Software.Version 2.0 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID '(MDDNMR) Orekhov, Jaravine, Kazimierczuk' . . 18387 5 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID collection 18387 5 processing 18387 5 stop_ save_ save_MDDGUI _Software.Sf_category software _Software.Sf_framecode MDDGUI _Software.Entry_ID 18387 _Software.ID 6 _Software.Name MDDGUI _Software.Version 1.0 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID '(MDDGUI) Lemak, Gutmanas, Chitayat, Karra, Fares, Sunnerhagen, Arrowsmith' . . 18387 6 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID collection 18387 6 processing 18387 6 stop_ save_ save_VNMRJ _Software.Sf_category software _Software.Sf_framecode VNMRJ _Software.Entry_ID 18387 _Software.ID 7 _Software.Name VNMRJ _Software.Version 2.2D _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Varian . . 18387 7 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID collection 18387 7 stop_ save_ save_TOPSPIN _Software.Sf_category software _Software.Sf_framecode TOPSPIN _Software.Entry_ID 18387 _Software.ID 8 _Software.Name TOPSPIN _Software.Version 2.1 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Bruker Biospin' . . 18387 8 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID collection 18387 8 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_1 _NMR_spectrometer.Entry_ID 18387 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Varian _NMR_spectrometer.Model Inova _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_2 _NMR_spectrometer.Entry_ID 18387 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 900 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 18387 _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 spectrometer_1 Varian Inova . 600 . 1 $citations 18387 1 2 spectrometer_2 Bruker Avance . 900 . . . 18387 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 18387 _Experiment_list.ID 1 _Experiment_list.Details '3D experiments acquired with NUS using the Orekhov (MDDNMR) approach and processed using either MDDNMR (Orekhov) or MDDGUI(Gutmanas)' 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 '15N HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18387 1 2 '15N NOESY-HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18387 1 3 '13C CT-HSQC' no . . . . . . . . . . 2 $sample_2 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18387 1 4 'aromatic 13C HSQC' no . . . . . . . . . . 2 $sample_2 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18387 1 5 '13C NOESY-HSQC' no . . . . . . . . . . 2 $sample_2 isotropic . . 1 $sample_conditions_1 . . . 2 $spectrometer_2 . . . . . . . . . . . . . . . . 18387 1 6 '13C aromatic NOESY-HSQC' no . . . . . . . . . . 2 $sample_2 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18387 1 7 HNCO no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18387 1 8 HNCACO no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18387 1 9 HNCA no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18387 1 10 HNCOCA no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18387 1 11 HNCACB no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18387 1 12 CBCACONH no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 18387 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference_1 _Chem_shift_reference.Entry_ID 18387 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details 'Chemical Shifts reference to internal DSS' loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID C 13 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.251449530 . . . . . . . . . 18387 1 H 1 DSS 'methyl protons' . . . . ppm 0.00 internal direct 1.000000000 . . . . . . . . . 18387 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.101329118 . . . . . . . . . 18387 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_assigned_chem_shift_list_1 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list_1 _Assigned_chem_shift_list.Entry_ID 18387 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_conditions_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference_1 _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 '15N HSQC' . . . 18387 1 3 '13C CT-HSQC' . . . 18387 1 4 'aromatic 13C HSQC' . . . 18387 1 7 HNCO . . . 18387 1 8 HNCACO . . . 18387 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 2 2 SER HA H 1 3.992 0.002 . 1 . . . A 2 SER HA . 18387 1 2 . 1 1 2 2 SER HB2 H 1 3.934 0.001 . 1 . . . A 2 SER HB2 . 18387 1 3 . 1 1 2 2 SER HB3 H 1 3.934 0.001 . 1 . . . A 2 SER HB3 . 18387 1 4 . 1 1 2 2 SER CA C 13 57.555 0.007 . 1 . . . A 2 SER CA . 18387 1 5 . 1 1 2 2 SER CB C 13 64.977 0.014 . 1 . . . A 2 SER CB . 18387 1 6 . 1 1 3 3 LEU HA H 1 4.439 0.002 . 1 . . . A 3 LEU HA . 18387 1 7 . 1 1 3 3 LEU HB2 H 1 1.456 0.002 . 2 . . . A 3 LEU HB2 . 18387 1 8 . 1 1 3 3 LEU HB3 H 1 1.587 0.002 . 2 . . . A 3 LEU HB3 . 18387 1 9 . 1 1 3 3 LEU HG H 1 1.530 0.001 . 1 . . . A 3 LEU HG . 18387 1 10 . 1 1 3 3 LEU HD11 H 1 0.812 0.004 . 2 . . . A 3 LEU HD11 . 18387 1 11 . 1 1 3 3 LEU HD12 H 1 0.812 0.004 . 2 . . . A 3 LEU HD12 . 18387 1 12 . 1 1 3 3 LEU HD13 H 1 0.812 0.004 . 2 . . . A 3 LEU HD13 . 18387 1 13 . 1 1 3 3 LEU HD21 H 1 0.868 0.002 . 2 . . . A 3 LEU HD21 . 18387 1 14 . 1 1 3 3 LEU HD22 H 1 0.868 0.002 . 2 . . . A 3 LEU HD22 . 18387 1 15 . 1 1 3 3 LEU HD23 H 1 0.868 0.002 . 2 . . . A 3 LEU HD23 . 18387 1 16 . 1 1 3 3 LEU C C 13 176.631 0.011 . 1 . . . A 3 LEU C . 18387 1 17 . 1 1 3 3 LEU CA C 13 54.564 0.018 . 1 . . . A 3 LEU CA . 18387 1 18 . 1 1 3 3 LEU CB C 13 42.724 0.009 . 1 . . . A 3 LEU CB . 18387 1 19 . 1 1 3 3 LEU CG C 13 27.260 0.015 . 1 . . . A 3 LEU CG . 18387 1 20 . 1 1 3 3 LEU CD1 C 13 25.607 0.013 . 2 . . . A 3 LEU CD1 . 18387 1 21 . 1 1 3 3 LEU CD2 C 13 23.949 0.006 . 2 . . . A 3 LEU CD2 . 18387 1 22 . 1 1 4 4 ALA H H 1 8.483 0.001 . 1 . . . A 4 ALA H . 18387 1 23 . 1 1 4 4 ALA HA H 1 4.379 0.000 . 1 . . . A 4 ALA HA . 18387 1 24 . 1 1 4 4 ALA HB1 H 1 1.415 0.001 . 1 . . . A 4 ALA HB1 . 18387 1 25 . 1 1 4 4 ALA HB2 H 1 1.415 0.001 . 1 . . . A 4 ALA HB2 . 18387 1 26 . 1 1 4 4 ALA HB3 H 1 1.415 0.001 . 1 . . . A 4 ALA HB3 . 18387 1 27 . 1 1 4 4 ALA C C 13 179.642 0.000 . 1 . . . A 4 ALA C . 18387 1 28 . 1 1 4 4 ALA CA C 13 51.735 0.012 . 1 . . . A 4 ALA CA . 18387 1 29 . 1 1 4 4 ALA CB C 13 19.752 0.015 . 1 . . . A 4 ALA CB . 18387 1 30 . 1 1 4 4 ALA N N 15 125.483 0.005 . 1 . . . A 4 ALA N . 18387 1 31 . 1 1 5 5 THR HA H 1 3.845 0.003 . 1 . . . A 5 THR HA . 18387 1 32 . 1 1 5 5 THR HB H 1 4.192 0.000 . 1 . . . A 5 THR HB . 18387 1 33 . 1 1 5 5 THR HG21 H 1 1.190 0.001 . 1 . . . A 5 THR HG21 . 18387 1 34 . 1 1 5 5 THR HG22 H 1 1.190 0.001 . 1 . . . A 5 THR HG22 . 18387 1 35 . 1 1 5 5 THR HG23 H 1 1.190 0.001 . 1 . . . A 5 THR HG23 . 18387 1 36 . 1 1 5 5 THR C C 13 175.487 0.006 . 1 . . . A 5 THR C . 18387 1 37 . 1 1 5 5 THR CA C 13 64.531 0.026 . 1 . . . A 5 THR CA . 18387 1 38 . 1 1 5 5 THR CB C 13 68.108 0.018 . 1 . . . A 5 THR CB . 18387 1 39 . 1 1 5 5 THR CG2 C 13 22.701 0.001 . 1 . . . A 5 THR CG2 . 18387 1 40 . 1 1 6 6 GLY H H 1 9.511 0.003 . 1 . . . A 6 GLY H . 18387 1 41 . 1 1 6 6 GLY HA2 H 1 4.470 0.002 . 2 . . . A 6 GLY HA2 . 18387 1 42 . 1 1 6 6 GLY HA3 H 1 3.660 0.002 . 2 . . . A 6 GLY HA3 . 18387 1 43 . 1 1 6 6 GLY C C 13 174.324 0.009 . 1 . . . A 6 GLY C . 18387 1 44 . 1 1 6 6 GLY CA C 13 44.835 0.016 . 1 . . . A 6 GLY CA . 18387 1 45 . 1 1 6 6 GLY N N 15 114.298 0.027 . 1 . . . A 6 GLY N . 18387 1 46 . 1 1 7 7 SER H H 1 7.736 0.003 . 1 . . . A 7 SER H . 18387 1 47 . 1 1 7 7 SER HA H 1 4.500 0.001 . 1 . . . A 7 SER HA . 18387 1 48 . 1 1 7 7 SER HB2 H 1 3.824 0.001 . 2 . . . A 7 SER HB2 . 18387 1 49 . 1 1 7 7 SER HB3 H 1 3.930 0.002 . 2 . . . A 7 SER HB3 . 18387 1 50 . 1 1 7 7 SER C C 13 173.315 0.011 . 1 . . . A 7 SER C . 18387 1 51 . 1 1 7 7 SER CA C 13 58.915 0.024 . 1 . . . A 7 SER CA . 18387 1 52 . 1 1 7 7 SER CB C 13 64.308 0.018 . 1 . . . A 7 SER CB . 18387 1 53 . 1 1 7 7 SER N N 15 115.270 0.012 . 1 . . . A 7 SER N . 18387 1 54 . 1 1 8 8 VAL H H 1 8.632 0.002 . 1 . . . A 8 VAL H . 18387 1 55 . 1 1 8 8 VAL HA H 1 3.832 0.001 . 1 . . . A 8 VAL HA . 18387 1 56 . 1 1 8 8 VAL HB H 1 1.908 0.000 . 1 . . . A 8 VAL HB . 18387 1 57 . 1 1 8 8 VAL HG11 H 1 0.889 0.002 . 2 . . . A 8 VAL HG11 . 18387 1 58 . 1 1 8 8 VAL HG12 H 1 0.889 0.002 . 2 . . . A 8 VAL HG12 . 18387 1 59 . 1 1 8 8 VAL HG13 H 1 0.889 0.002 . 2 . . . A 8 VAL HG13 . 18387 1 60 . 1 1 8 8 VAL HG21 H 1 1.016 0.002 . 2 . . . A 8 VAL HG21 . 18387 1 61 . 1 1 8 8 VAL HG22 H 1 1.016 0.002 . 2 . . . A 8 VAL HG22 . 18387 1 62 . 1 1 8 8 VAL HG23 H 1 1.016 0.002 . 2 . . . A 8 VAL HG23 . 18387 1 63 . 1 1 8 8 VAL C C 13 176.673 0.007 . 1 . . . A 8 VAL C . 18387 1 64 . 1 1 8 8 VAL CA C 13 63.673 0.019 . 1 . . . A 8 VAL CA . 18387 1 65 . 1 1 8 8 VAL CB C 13 32.222 0.024 . 1 . . . A 8 VAL CB . 18387 1 66 . 1 1 8 8 VAL CG1 C 13 21.451 0.004 . 2 . . . A 8 VAL CG1 . 18387 1 67 . 1 1 8 8 VAL CG2 C 13 22.205 0.001 . 2 . . . A 8 VAL CG2 . 18387 1 68 . 1 1 8 8 VAL N N 15 123.708 0.020 . 1 . . . A 8 VAL N . 18387 1 69 . 1 1 9 9 ALA H H 1 8.448 0.002 . 1 . . . A 9 ALA H . 18387 1 70 . 1 1 9 9 ALA HA H 1 4.263 0.003 . 1 . . . A 9 ALA HA . 18387 1 71 . 1 1 9 9 ALA HB1 H 1 1.577 0.002 . 1 . . . A 9 ALA HB1 . 18387 1 72 . 1 1 9 9 ALA HB2 H 1 1.577 0.002 . 1 . . . A 9 ALA HB2 . 18387 1 73 . 1 1 9 9 ALA HB3 H 1 1.577 0.002 . 1 . . . A 9 ALA HB3 . 18387 1 74 . 1 1 9 9 ALA C C 13 175.404 0.000 . 1 . . . A 9 ALA C . 18387 1 75 . 1 1 9 9 ALA CA C 13 50.955 0.010 . 1 . . . A 9 ALA CA . 18387 1 76 . 1 1 9 9 ALA CB C 13 18.030 0.014 . 1 . . . A 9 ALA CB . 18387 1 77 . 1 1 9 9 ALA N N 15 133.040 0.019 . 1 . . . A 9 ALA N . 18387 1 78 . 1 1 10 10 PRO HA H 1 4.331 0.001 . 1 . . . A 10 PRO HA . 18387 1 79 . 1 1 10 10 PRO HB2 H 1 1.926 0.002 . 2 . . . A 10 PRO HB2 . 18387 1 80 . 1 1 10 10 PRO HB3 H 1 2.350 0.001 . 2 . . . A 10 PRO HB3 . 18387 1 81 . 1 1 10 10 PRO HG2 H 1 1.336 0.002 . 2 . . . A 10 PRO HG2 . 18387 1 82 . 1 1 10 10 PRO HG3 H 1 1.661 0.001 . 2 . . . A 10 PRO HG3 . 18387 1 83 . 1 1 10 10 PRO HD2 H 1 2.567 0.001 . 2 . . . A 10 PRO HD2 . 18387 1 84 . 1 1 10 10 PRO HD3 H 1 3.961 0.002 . 2 . . . A 10 PRO HD3 . 18387 1 85 . 1 1 10 10 PRO C C 13 175.071 0.006 . 1 . . . A 10 PRO C . 18387 1 86 . 1 1 10 10 PRO CA C 13 62.641 0.049 . 1 . . . A 10 PRO CA . 18387 1 87 . 1 1 10 10 PRO CB C 13 32.324 0.008 . 1 . . . A 10 PRO CB . 18387 1 88 . 1 1 10 10 PRO CG C 13 27.299 0.008 . 1 . . . A 10 PRO CG . 18387 1 89 . 1 1 10 10 PRO CD C 13 51.316 0.006 . 1 . . . A 10 PRO CD . 18387 1 90 . 1 1 11 11 ALA H H 1 8.221 0.001 . 1 . . . A 11 ALA H . 18387 1 91 . 1 1 11 11 ALA HA H 1 4.244 0.001 . 1 . . . A 11 ALA HA . 18387 1 92 . 1 1 11 11 ALA HB1 H 1 1.428 0.000 . 1 . . . A 11 ALA HB1 . 18387 1 93 . 1 1 11 11 ALA HB2 H 1 1.428 0.000 . 1 . . . A 11 ALA HB2 . 18387 1 94 . 1 1 11 11 ALA HB3 H 1 1.428 0.000 . 1 . . . A 11 ALA HB3 . 18387 1 95 . 1 1 11 11 ALA C C 13 177.688 0.006 . 1 . . . A 11 ALA C . 18387 1 96 . 1 1 11 11 ALA CA C 13 53.621 0.024 . 1 . . . A 11 ALA CA . 18387 1 97 . 1 1 11 11 ALA CB C 13 19.327 0.029 . 1 . . . A 11 ALA CB . 18387 1 98 . 1 1 11 11 ALA N N 15 124.172 0.006 . 1 . . . A 11 ALA N . 18387 1 99 . 1 1 12 12 ILE H H 1 7.693 0.001 . 1 . . . A 12 ILE H . 18387 1 100 . 1 1 12 12 ILE HA H 1 4.328 0.001 . 1 . . . A 12 ILE HA . 18387 1 101 . 1 1 12 12 ILE HB H 1 1.866 0.003 . 1 . . . A 12 ILE HB . 18387 1 102 . 1 1 12 12 ILE HG12 H 1 1.181 0.003 . 2 . . . A 12 ILE HG12 . 18387 1 103 . 1 1 12 12 ILE HG13 H 1 2.270 0.003 . 2 . . . A 12 ILE HG13 . 18387 1 104 . 1 1 12 12 ILE HG21 H 1 1.105 0.005 . 1 . . . A 12 ILE HG21 . 18387 1 105 . 1 1 12 12 ILE HG22 H 1 1.105 0.005 . 1 . . . A 12 ILE HG22 . 18387 1 106 . 1 1 12 12 ILE HG23 H 1 1.105 0.005 . 1 . . . A 12 ILE HG23 . 18387 1 107 . 1 1 12 12 ILE HD11 H 1 0.981 0.003 . 1 . . . A 12 ILE HD11 . 18387 1 108 . 1 1 12 12 ILE HD12 H 1 0.981 0.003 . 1 . . . A 12 ILE HD12 . 18387 1 109 . 1 1 12 12 ILE HD13 H 1 0.981 0.003 . 1 . . . A 12 ILE HD13 . 18387 1 110 . 1 1 12 12 ILE C C 13 175.013 0.024 . 1 . . . A 12 ILE C . 18387 1 111 . 1 1 12 12 ILE CA C 13 62.166 0.024 . 1 . . . A 12 ILE CA . 18387 1 112 . 1 1 12 12 ILE CB C 13 44.290 0.006 . 1 . . . A 12 ILE CB . 18387 1 113 . 1 1 12 12 ILE CG1 C 13 27.353 0.018 . 1 . . . A 12 ILE CG1 . 18387 1 114 . 1 1 12 12 ILE CG2 C 13 19.157 0.002 . 1 . . . A 12 ILE CG2 . 18387 1 115 . 1 1 12 12 ILE CD1 C 13 15.999 0.001 . 1 . . . A 12 ILE CD1 . 18387 1 116 . 1 1 12 12 ILE N N 15 117.815 0.026 . 1 . . . A 12 ILE N . 18387 1 117 . 1 1 13 13 THR H H 1 8.363 0.001 . 1 . . . A 13 THR H . 18387 1 118 . 1 1 13 13 THR HA H 1 4.840 0.001 . 1 . . . A 13 THR HA . 18387 1 119 . 1 1 13 13 THR HB H 1 3.878 0.000 . 1 . . . A 13 THR HB . 18387 1 120 . 1 1 13 13 THR HG21 H 1 1.160 0.001 . 1 . . . A 13 THR HG21 . 18387 1 121 . 1 1 13 13 THR HG22 H 1 1.160 0.001 . 1 . . . A 13 THR HG22 . 18387 1 122 . 1 1 13 13 THR HG23 H 1 1.160 0.001 . 1 . . . A 13 THR HG23 . 18387 1 123 . 1 1 13 13 THR C C 13 172.625 0.011 . 1 . . . A 13 THR C . 18387 1 124 . 1 1 13 13 THR CA C 13 62.297 0.018 . 1 . . . A 13 THR CA . 18387 1 125 . 1 1 13 13 THR CB C 13 71.585 0.018 . 1 . . . A 13 THR CB . 18387 1 126 . 1 1 13 13 THR CG2 C 13 21.640 0.004 . 1 . . . A 13 THR CG2 . 18387 1 127 . 1 1 13 13 THR N N 15 121.186 0.030 . 1 . . . A 13 THR N . 18387 1 128 . 1 1 14 14 GLY H H 1 7.993 0.002 . 1 . . . A 14 GLY H . 18387 1 129 . 1 1 14 14 GLY HA2 H 1 3.404 0.002 . 2 . . . A 14 GLY HA2 . 18387 1 130 . 1 1 14 14 GLY HA3 H 1 4.522 0.002 . 2 . . . A 14 GLY HA3 . 18387 1 131 . 1 1 14 14 GLY C C 13 170.040 0.002 . 1 . . . A 14 GLY C . 18387 1 132 . 1 1 14 14 GLY CA C 13 44.390 0.012 . 1 . . . A 14 GLY CA . 18387 1 133 . 1 1 14 14 GLY N N 15 110.785 0.010 . 1 . . . A 14 GLY N . 18387 1 134 . 1 1 15 15 ILE H H 1 7.973 0.001 . 1 . . . A 15 ILE H . 18387 1 135 . 1 1 15 15 ILE HA H 1 5.125 0.003 . 1 . . . A 15 ILE HA . 18387 1 136 . 1 1 15 15 ILE HB H 1 1.868 0.002 . 1 . . . A 15 ILE HB . 18387 1 137 . 1 1 15 15 ILE HG12 H 1 1.358 0.003 . 2 . . . A 15 ILE HG12 . 18387 1 138 . 1 1 15 15 ILE HG13 H 1 1.469 0.001 . 2 . . . A 15 ILE HG13 . 18387 1 139 . 1 1 15 15 ILE HG21 H 1 1.068 0.003 . 1 . . . A 15 ILE HG21 . 18387 1 140 . 1 1 15 15 ILE HG22 H 1 1.068 0.003 . 1 . . . A 15 ILE HG22 . 18387 1 141 . 1 1 15 15 ILE HG23 H 1 1.068 0.003 . 1 . . . A 15 ILE HG23 . 18387 1 142 . 1 1 15 15 ILE HD11 H 1 0.735 0.002 . 1 . . . A 15 ILE HD11 . 18387 1 143 . 1 1 15 15 ILE HD12 H 1 0.735 0.002 . 1 . . . A 15 ILE HD12 . 18387 1 144 . 1 1 15 15 ILE HD13 H 1 0.735 0.002 . 1 . . . A 15 ILE HD13 . 18387 1 145 . 1 1 15 15 ILE C C 13 176.359 0.004 . 1 . . . A 15 ILE C . 18387 1 146 . 1 1 15 15 ILE CA C 13 58.614 0.017 . 1 . . . A 15 ILE CA . 18387 1 147 . 1 1 15 15 ILE CB C 13 38.639 0.007 . 1 . . . A 15 ILE CB . 18387 1 148 . 1 1 15 15 ILE CG1 C 13 27.263 0.017 . 1 . . . A 15 ILE CG1 . 18387 1 149 . 1 1 15 15 ILE CG2 C 13 17.731 0.001 . 1 . . . A 15 ILE CG2 . 18387 1 150 . 1 1 15 15 ILE CD1 C 13 11.007 0.014 . 1 . . . A 15 ILE CD1 . 18387 1 151 . 1 1 15 15 ILE N N 15 119.088 0.027 . 1 . . . A 15 ILE N . 18387 1 152 . 1 1 16 16 ASP H H 1 9.335 0.002 . 1 . . . A 16 ASP H . 18387 1 153 . 1 1 16 16 ASP HA H 1 5.849 0.002 . 1 . . . A 16 ASP HA . 18387 1 154 . 1 1 16 16 ASP HB2 H 1 2.824 0.003 . 2 . . . A 16 ASP HB2 . 18387 1 155 . 1 1 16 16 ASP HB3 H 1 3.771 0.001 . 2 . . . A 16 ASP HB3 . 18387 1 156 . 1 1 16 16 ASP C C 13 179.190 0.003 . 1 . . . A 16 ASP C . 18387 1 157 . 1 1 16 16 ASP CA C 13 52.880 0.014 . 1 . . . A 16 ASP CA . 18387 1 158 . 1 1 16 16 ASP CB C 13 42.275 0.011 . 1 . . . A 16 ASP CB . 18387 1 159 . 1 1 16 16 ASP N N 15 126.633 0.009 . 1 . . . A 16 ASP N . 18387 1 160 . 1 1 17 17 LEU H H 1 8.071 0.002 . 1 . . . A 17 LEU H . 18387 1 161 . 1 1 17 17 LEU HA H 1 4.174 0.003 . 1 . . . A 17 LEU HA . 18387 1 162 . 1 1 17 17 LEU HB2 H 1 1.567 0.003 . 2 . . . A 17 LEU HB2 . 18387 1 163 . 1 1 17 17 LEU HB3 H 1 1.810 0.002 . 2 . . . A 17 LEU HB3 . 18387 1 164 . 1 1 17 17 LEU HG H 1 1.624 0.001 . 1 . . . A 17 LEU HG . 18387 1 165 . 1 1 17 17 LEU HD11 H 1 0.423 0.003 . 2 . . . A 17 LEU HD11 . 18387 1 166 . 1 1 17 17 LEU HD12 H 1 0.423 0.003 . 2 . . . A 17 LEU HD12 . 18387 1 167 . 1 1 17 17 LEU HD13 H 1 0.423 0.003 . 2 . . . A 17 LEU HD13 . 18387 1 168 . 1 1 17 17 LEU HD21 H 1 0.854 0.001 . 2 . . . A 17 LEU HD21 . 18387 1 169 . 1 1 17 17 LEU HD22 H 1 0.854 0.001 . 2 . . . A 17 LEU HD22 . 18387 1 170 . 1 1 17 17 LEU HD23 H 1 0.854 0.001 . 2 . . . A 17 LEU HD23 . 18387 1 171 . 1 1 17 17 LEU C C 13 178.432 0.031 . 1 . . . A 17 LEU C . 18387 1 172 . 1 1 17 17 LEU CA C 13 57.981 0.019 . 1 . . . A 17 LEU CA . 18387 1 173 . 1 1 17 17 LEU CB C 13 42.986 0.012 . 1 . . . A 17 LEU CB . 18387 1 174 . 1 1 17 17 LEU CG C 13 27.532 0.009 . 1 . . . A 17 LEU CG . 18387 1 175 . 1 1 17 17 LEU CD1 C 13 24.280 0.005 . 2 . . . A 17 LEU CD1 . 18387 1 176 . 1 1 17 17 LEU CD2 C 13 25.554 0.004 . 2 . . . A 17 LEU CD2 . 18387 1 177 . 1 1 17 17 LEU N N 15 116.648 0.009 . 1 . . . A 17 LEU N . 18387 1 178 . 1 1 18 18 LYS H H 1 8.207 0.001 . 1 . . . A 18 LYS H . 18387 1 179 . 1 1 18 18 LYS HA H 1 4.509 0.001 . 1 . . . A 18 LYS HA . 18387 1 180 . 1 1 18 18 LYS HB2 H 1 1.946 0.001 . 2 . . . A 18 LYS HB2 . 18387 1 181 . 1 1 18 18 LYS HB3 H 1 2.101 0.001 . 2 . . . A 18 LYS HB3 . 18387 1 182 . 1 1 18 18 LYS HG2 H 1 1.420 0.001 . 2 . . . A 18 LYS HG2 . 18387 1 183 . 1 1 18 18 LYS HG3 H 1 1.500 0.002 . 2 . . . A 18 LYS HG3 . 18387 1 184 . 1 1 18 18 LYS HD2 H 1 1.718 0.001 . 1 . . . A 18 LYS HD2 . 18387 1 185 . 1 1 18 18 LYS HD3 H 1 1.718 0.001 . 1 . . . A 18 LYS HD3 . 18387 1 186 . 1 1 18 18 LYS HE2 H 1 3.017 0.000 . 1 . . . A 18 LYS HE2 . 18387 1 187 . 1 1 18 18 LYS HE3 H 1 3.017 0.000 . 1 . . . A 18 LYS HE3 . 18387 1 188 . 1 1 18 18 LYS C C 13 176.793 0.005 . 1 . . . A 18 LYS C . 18387 1 189 . 1 1 18 18 LYS CA C 13 55.435 0.019 . 1 . . . A 18 LYS CA . 18387 1 190 . 1 1 18 18 LYS CB C 13 33.063 0.008 . 1 . . . A 18 LYS CB . 18387 1 191 . 1 1 18 18 LYS CG C 13 25.370 0.010 . 1 . . . A 18 LYS CG . 18387 1 192 . 1 1 18 18 LYS CD C 13 28.884 0.004 . 1 . . . A 18 LYS CD . 18387 1 193 . 1 1 18 18 LYS CE C 13 42.071 0.000 . 1 . . . A 18 LYS CE . 18387 1 194 . 1 1 18 18 LYS N N 15 117.401 0.033 . 1 . . . A 18 LYS N . 18387 1 195 . 1 1 19 19 GLY H H 1 8.099 0.002 . 1 . . . A 19 GLY H . 18387 1 196 . 1 1 19 19 GLY HA2 H 1 4.334 0.002 . 2 . . . A 19 GLY HA2 . 18387 1 197 . 1 1 19 19 GLY HA3 H 1 3.666 0.003 . 2 . . . A 19 GLY HA3 . 18387 1 198 . 1 1 19 19 GLY C C 13 174.649 0.002 . 1 . . . A 19 GLY C . 18387 1 199 . 1 1 19 19 GLY CA C 13 45.597 0.018 . 1 . . . A 19 GLY CA . 18387 1 200 . 1 1 19 19 GLY N N 15 108.061 0.007 . 1 . . . A 19 GLY N . 18387 1 201 . 1 1 20 20 ASN H H 1 8.945 0.001 . 1 . . . A 20 ASN H . 18387 1 202 . 1 1 20 20 ASN HA H 1 4.905 0.001 . 1 . . . A 20 ASN HA . 18387 1 203 . 1 1 20 20 ASN HB2 H 1 2.702 0.001 . 2 . . . A 20 ASN HB2 . 18387 1 204 . 1 1 20 20 ASN HB3 H 1 2.894 0.002 . 2 . . . A 20 ASN HB3 . 18387 1 205 . 1 1 20 20 ASN HD21 H 1 8.320 0.001 . 1 . . . A 20 ASN HD21 . 18387 1 206 . 1 1 20 20 ASN HD22 H 1 7.043 0.001 . 1 . . . A 20 ASN HD22 . 18387 1 207 . 1 1 20 20 ASN C C 13 174.827 0.012 . 1 . . . A 20 ASN C . 18387 1 208 . 1 1 20 20 ASN CA C 13 52.467 0.023 . 1 . . . A 20 ASN CA . 18387 1 209 . 1 1 20 20 ASN CB C 13 39.676 0.018 . 1 . . . A 20 ASN CB . 18387 1 210 . 1 1 20 20 ASN N N 15 121.012 0.005 . 1 . . . A 20 ASN N . 18387 1 211 . 1 1 20 20 ASN ND2 N 15 116.476 0.012 . 1 . . . A 20 ASN ND2 . 18387 1 212 . 1 1 21 21 SER H H 1 8.740 0.001 . 1 . . . A 21 SER H . 18387 1 213 . 1 1 21 21 SER HA H 1 5.000 0.003 . 1 . . . A 21 SER HA . 18387 1 214 . 1 1 21 21 SER HB2 H 1 3.751 0.001 . 1 . . . A 21 SER HB2 . 18387 1 215 . 1 1 21 21 SER HB3 H 1 3.752 0.001 . 1 . . . A 21 SER HB3 . 18387 1 216 . 1 1 21 21 SER C C 13 174.911 0.022 . 1 . . . A 21 SER C . 18387 1 217 . 1 1 21 21 SER CA C 13 58.730 0.018 . 1 . . . A 21 SER CA . 18387 1 218 . 1 1 21 21 SER CB C 13 63.162 0.019 . 1 . . . A 21 SER CB . 18387 1 219 . 1 1 21 21 SER N N 15 117.285 0.003 . 1 . . . A 21 SER N . 18387 1 220 . 1 1 22 22 VAL H H 1 9.125 0.001 . 1 . . . A 22 VAL H . 18387 1 221 . 1 1 22 22 VAL HA H 1 4.380 0.002 . 1 . . . A 22 VAL HA . 18387 1 222 . 1 1 22 22 VAL HB H 1 2.114 0.001 . 1 . . . A 22 VAL HB . 18387 1 223 . 1 1 22 22 VAL HG11 H 1 1.097 0.004 . 2 . . . A 22 VAL HG11 . 18387 1 224 . 1 1 22 22 VAL HG12 H 1 1.097 0.004 . 2 . . . A 22 VAL HG12 . 18387 1 225 . 1 1 22 22 VAL HG13 H 1 1.097 0.004 . 2 . . . A 22 VAL HG13 . 18387 1 226 . 1 1 22 22 VAL HG21 H 1 1.332 0.003 . 2 . . . A 22 VAL HG21 . 18387 1 227 . 1 1 22 22 VAL HG22 H 1 1.332 0.003 . 2 . . . A 22 VAL HG22 . 18387 1 228 . 1 1 22 22 VAL HG23 H 1 1.332 0.003 . 2 . . . A 22 VAL HG23 . 18387 1 229 . 1 1 22 22 VAL C C 13 176.276 0.006 . 1 . . . A 22 VAL C . 18387 1 230 . 1 1 22 22 VAL CA C 13 62.953 0.010 . 1 . . . A 22 VAL CA . 18387 1 231 . 1 1 22 22 VAL CB C 13 35.582 0.007 . 1 . . . A 22 VAL CB . 18387 1 232 . 1 1 22 22 VAL CG1 C 13 21.795 0.007 . 2 . . . A 22 VAL CG1 . 18387 1 233 . 1 1 22 22 VAL CG2 C 13 22.048 0.005 . 2 . . . A 22 VAL CG2 . 18387 1 234 . 1 1 22 22 VAL N N 15 128.665 0.007 . 1 . . . A 22 VAL N . 18387 1 235 . 1 1 23 23 SER H H 1 8.971 0.001 . 1 . . . A 23 SER H . 18387 1 236 . 1 1 23 23 SER HA H 1 5.878 0.003 . 1 . . . A 23 SER HA . 18387 1 237 . 1 1 23 23 SER HB2 H 1 3.796 0.000 . 2 . . . A 23 SER HB2 . 18387 1 238 . 1 1 23 23 SER HB3 H 1 4.026 0.002 . 2 . . . A 23 SER HB3 . 18387 1 239 . 1 1 23 23 SER C C 13 174.436 0.005 . 1 . . . A 23 SER C . 18387 1 240 . 1 1 23 23 SER CA C 13 57.101 0.022 . 1 . . . A 23 SER CA . 18387 1 241 . 1 1 23 23 SER CB C 13 66.078 0.018 . 1 . . . A 23 SER CB . 18387 1 242 . 1 1 23 23 SER N N 15 127.457 0.016 . 1 . . . A 23 SER N . 18387 1 243 . 1 1 24 24 LEU H H 1 8.450 0.001 . 1 . . . A 24 LEU H . 18387 1 244 . 1 1 24 24 LEU HA H 1 3.467 0.003 . 1 . . . A 24 LEU HA . 18387 1 245 . 1 1 24 24 LEU HB2 H 1 1.328 0.001 . 2 . . . A 24 LEU HB2 . 18387 1 246 . 1 1 24 24 LEU HB3 H 1 2.039 0.002 . 2 . . . A 24 LEU HB3 . 18387 1 247 . 1 1 24 24 LEU HG H 1 1.585 0.001 . 1 . . . A 24 LEU HG . 18387 1 248 . 1 1 24 24 LEU HD11 H 1 0.992 0.003 . 2 . . . A 24 LEU HD11 . 18387 1 249 . 1 1 24 24 LEU HD12 H 1 0.992 0.003 . 2 . . . A 24 LEU HD12 . 18387 1 250 . 1 1 24 24 LEU HD13 H 1 0.992 0.003 . 2 . . . A 24 LEU HD13 . 18387 1 251 . 1 1 24 24 LEU HD21 H 1 0.710 0.003 . 2 . . . A 24 LEU HD21 . 18387 1 252 . 1 1 24 24 LEU HD22 H 1 0.710 0.003 . 2 . . . A 24 LEU HD22 . 18387 1 253 . 1 1 24 24 LEU HD23 H 1 0.710 0.003 . 2 . . . A 24 LEU HD23 . 18387 1 254 . 1 1 24 24 LEU C C 13 179.852 0.011 . 1 . . . A 24 LEU C . 18387 1 255 . 1 1 24 24 LEU CA C 13 58.203 0.014 . 1 . . . A 24 LEU CA . 18387 1 256 . 1 1 24 24 LEU CB C 13 41.978 0.020 . 1 . . . A 24 LEU CB . 18387 1 257 . 1 1 24 24 LEU CG C 13 27.020 0.000 . 1 . . . A 24 LEU CG . 18387 1 258 . 1 1 24 24 LEU CD1 C 13 26.839 0.015 . 2 . . . A 24 LEU CD1 . 18387 1 259 . 1 1 24 24 LEU CD2 C 13 23.972 0.006 . 2 . . . A 24 LEU CD2 . 18387 1 260 . 1 1 24 24 LEU N N 15 126.734 0.007 . 1 . . . A 24 LEU N . 18387 1 261 . 1 1 25 25 ASN H H 1 8.505 0.001 . 1 . . . A 25 ASN H . 18387 1 262 . 1 1 25 25 ASN HA H 1 4.242 0.002 . 1 . . . A 25 ASN HA . 18387 1 263 . 1 1 25 25 ASN HB2 H 1 2.687 0.001 . 2 . . . A 25 ASN HB2 . 18387 1 264 . 1 1 25 25 ASN HB3 H 1 2.816 0.001 . 2 . . . A 25 ASN HB3 . 18387 1 265 . 1 1 25 25 ASN HD21 H 1 6.870 0.000 . 1 . . . A 25 ASN HD21 . 18387 1 266 . 1 1 25 25 ASN HD22 H 1 7.738 0.000 . 1 . . . A 25 ASN HD22 . 18387 1 267 . 1 1 25 25 ASN C C 13 176.246 0.003 . 1 . . . A 25 ASN C . 18387 1 268 . 1 1 25 25 ASN CA C 13 55.370 0.032 . 1 . . . A 25 ASN CA . 18387 1 269 . 1 1 25 25 ASN CB C 13 38.771 0.011 . 1 . . . A 25 ASN CB . 18387 1 270 . 1 1 25 25 ASN N N 15 115.642 0.012 . 1 . . . A 25 ASN N . 18387 1 271 . 1 1 25 25 ASN ND2 N 15 113.486 0.015 . 1 . . . A 25 ASN ND2 . 18387 1 272 . 1 1 26 26 ASP H H 1 7.731 0.001 . 1 . . . A 26 ASP H . 18387 1 273 . 1 1 26 26 ASP HA H 1 4.205 0.002 . 1 . . . A 26 ASP HA . 18387 1 274 . 1 1 26 26 ASP HB2 H 1 2.108 0.002 . 2 . . . A 26 ASP HB2 . 18387 1 275 . 1 1 26 26 ASP HB3 H 1 2.326 0.003 . 2 . . . A 26 ASP HB3 . 18387 1 276 . 1 1 26 26 ASP C C 13 176.708 0.006 . 1 . . . A 26 ASP C . 18387 1 277 . 1 1 26 26 ASP CA C 13 56.525 0.013 . 1 . . . A 26 ASP CA . 18387 1 278 . 1 1 26 26 ASP CB C 13 39.280 0.012 . 1 . . . A 26 ASP CB . 18387 1 279 . 1 1 26 26 ASP N N 15 119.722 0.018 . 1 . . . A 26 ASP N . 18387 1 280 . 1 1 27 27 PHE H H 1 7.390 0.001 . 1 . . . A 27 PHE H . 18387 1 281 . 1 1 27 27 PHE HA H 1 4.480 0.002 . 1 . . . A 27 PHE HA . 18387 1 282 . 1 1 27 27 PHE HB2 H 1 2.428 0.002 . 2 . . . A 27 PHE HB2 . 18387 1 283 . 1 1 27 27 PHE HB3 H 1 3.156 0.003 . 2 . . . A 27 PHE HB3 . 18387 1 284 . 1 1 27 27 PHE HD1 H 1 6.978 0.002 . 3 . . . A 27 PHE HD1 . 18387 1 285 . 1 1 27 27 PHE HD2 H 1 6.978 0.002 . 3 . . . A 27 PHE HD2 . 18387 1 286 . 1 1 27 27 PHE HE1 H 1 7.034 0.004 . 3 . . . A 27 PHE HE1 . 18387 1 287 . 1 1 27 27 PHE HE2 H 1 7.034 0.004 . 3 . . . A 27 PHE HE2 . 18387 1 288 . 1 1 27 27 PHE HZ H 1 7.078 0.001 . 1 . . . A 27 PHE HZ . 18387 1 289 . 1 1 27 27 PHE C C 13 174.227 0.010 . 1 . . . A 27 PHE C . 18387 1 290 . 1 1 27 27 PHE CA C 13 57.071 0.028 . 1 . . . A 27 PHE CA . 18387 1 291 . 1 1 27 27 PHE CB C 13 39.719 0.012 . 1 . . . A 27 PHE CB . 18387 1 292 . 1 1 27 27 PHE CD1 C 13 131.753 0.011 . 3 . . . A 27 PHE CD1 . 18387 1 293 . 1 1 27 27 PHE CD2 C 13 131.753 0.011 . 3 . . . A 27 PHE CD2 . 18387 1 294 . 1 1 27 27 PHE CE1 C 13 131.837 0.004 . 3 . . . A 27 PHE CE1 . 18387 1 295 . 1 1 27 27 PHE CE2 C 13 131.837 0.004 . 3 . . . A 27 PHE CE2 . 18387 1 296 . 1 1 27 27 PHE CZ C 13 128.527 0.019 . 1 . . . A 27 PHE CZ . 18387 1 297 . 1 1 27 27 PHE N N 15 116.827 0.026 . 1 . . . A 27 PHE N . 18387 1 298 . 1 1 28 28 LYS H H 1 6.883 0.002 . 1 . . . A 28 LYS H . 18387 1 299 . 1 1 28 28 LYS HA H 1 4.387 0.003 . 1 . . . A 28 LYS HA . 18387 1 300 . 1 1 28 28 LYS HB2 H 1 1.722 0.002 . 2 . . . A 28 LYS HB2 . 18387 1 301 . 1 1 28 28 LYS HB3 H 1 1.826 0.001 . 2 . . . A 28 LYS HB3 . 18387 1 302 . 1 1 28 28 LYS HG2 H 1 1.459 0.002 . 2 . . . A 28 LYS HG2 . 18387 1 303 . 1 1 28 28 LYS HG3 H 1 1.581 0.002 . 2 . . . A 28 LYS HG3 . 18387 1 304 . 1 1 28 28 LYS HD2 H 1 1.679 0.002 . 1 . . . A 28 LYS HD2 . 18387 1 305 . 1 1 28 28 LYS HD3 H 1 1.679 0.002 . 1 . . . A 28 LYS HD3 . 18387 1 306 . 1 1 28 28 LYS HE2 H 1 2.966 0.002 . 1 . . . A 28 LYS HE2 . 18387 1 307 . 1 1 28 28 LYS HE3 H 1 2.966 0.002 . 1 . . . A 28 LYS HE3 . 18387 1 308 . 1 1 28 28 LYS C C 13 177.845 0.001 . 1 . . . A 28 LYS C . 18387 1 309 . 1 1 28 28 LYS CA C 13 58.002 0.024 . 1 . . . A 28 LYS CA . 18387 1 310 . 1 1 28 28 LYS CB C 13 32.544 0.017 . 1 . . . A 28 LYS CB . 18387 1 311 . 1 1 28 28 LYS CG C 13 25.408 0.004 . 1 . . . A 28 LYS CG . 18387 1 312 . 1 1 28 28 LYS CD C 13 28.903 0.000 . 1 . . . A 28 LYS CD . 18387 1 313 . 1 1 28 28 LYS CE C 13 42.155 0.000 . 1 . . . A 28 LYS CE . 18387 1 314 . 1 1 28 28 LYS N N 15 120.357 0.007 . 1 . . . A 28 LYS N . 18387 1 315 . 1 1 29 29 GLY H H 1 8.930 0.001 . 1 . . . A 29 GLY H . 18387 1 316 . 1 1 29 29 GLY HA2 H 1 4.622 0.002 . 2 . . . A 29 GLY HA2 . 18387 1 317 . 1 1 29 29 GLY HA3 H 1 3.612 0.004 . 2 . . . A 29 GLY HA3 . 18387 1 318 . 1 1 29 29 GLY C C 13 173.799 0.005 . 1 . . . A 29 GLY C . 18387 1 319 . 1 1 29 29 GLY CA C 13 44.988 0.027 . 1 . . . A 29 GLY CA . 18387 1 320 . 1 1 29 29 GLY N N 15 112.653 0.004 . 1 . . . A 29 GLY N . 18387 1 321 . 1 1 30 30 LYS H H 1 8.098 0.001 . 1 . . . A 30 LYS H . 18387 1 322 . 1 1 30 30 LYS HA H 1 4.635 0.002 . 1 . . . A 30 LYS HA . 18387 1 323 . 1 1 30 30 LYS HB2 H 1 1.713 0.003 . 1 . . . A 30 LYS HB2 . 18387 1 324 . 1 1 30 30 LYS HB3 H 1 1.713 0.003 . 1 . . . A 30 LYS HB3 . 18387 1 325 . 1 1 30 30 LYS HG2 H 1 1.230 0.001 . 2 . . . A 30 LYS HG2 . 18387 1 326 . 1 1 30 30 LYS HG3 H 1 1.464 0.002 . 2 . . . A 30 LYS HG3 . 18387 1 327 . 1 1 30 30 LYS HD2 H 1 1.473 0.003 . 2 . . . A 30 LYS HD2 . 18387 1 328 . 1 1 30 30 LYS HD3 H 1 1.574 0.004 . 2 . . . A 30 LYS HD3 . 18387 1 329 . 1 1 30 30 LYS HE2 H 1 3.085 0.001 . 1 . . . A 30 LYS HE2 . 18387 1 330 . 1 1 30 30 LYS HE3 H 1 3.084 0.001 . 1 . . . A 30 LYS HE3 . 18387 1 331 . 1 1 30 30 LYS C C 13 176.505 0.014 . 1 . . . A 30 LYS C . 18387 1 332 . 1 1 30 30 LYS CA C 13 55.180 0.014 . 1 . . . A 30 LYS CA . 18387 1 333 . 1 1 30 30 LYS CB C 13 34.857 0.016 . 1 . . . A 30 LYS CB . 18387 1 334 . 1 1 30 30 LYS CG C 13 26.033 0.009 . 1 . . . A 30 LYS CG . 18387 1 335 . 1 1 30 30 LYS CD C 13 30.130 0.012 . 1 . . . A 30 LYS CD . 18387 1 336 . 1 1 30 30 LYS CE C 13 42.277 0.000 . 1 . . . A 30 LYS CE . 18387 1 337 . 1 1 30 30 LYS N N 15 120.516 0.005 . 1 . . . A 30 LYS N . 18387 1 338 . 1 1 31 31 TYR H H 1 8.263 0.001 . 1 . . . A 31 TYR H . 18387 1 339 . 1 1 31 31 TYR HA H 1 4.654 0.005 . 1 . . . A 31 TYR HA . 18387 1 340 . 1 1 31 31 TYR HB2 H 1 2.921 0.002 . 2 . . . A 31 TYR HB2 . 18387 1 341 . 1 1 31 31 TYR HB3 H 1 3.094 0.003 . 2 . . . A 31 TYR HB3 . 18387 1 342 . 1 1 31 31 TYR HD1 H 1 7.139 0.002 . 3 . . . A 31 TYR HD1 . 18387 1 343 . 1 1 31 31 TYR HD2 H 1 7.139 0.002 . 3 . . . A 31 TYR HD2 . 18387 1 344 . 1 1 31 31 TYR HE1 H 1 6.815 0.002 . 3 . . . A 31 TYR HE1 . 18387 1 345 . 1 1 31 31 TYR HE2 H 1 6.815 0.002 . 3 . . . A 31 TYR HE2 . 18387 1 346 . 1 1 31 31 TYR C C 13 175.551 0.012 . 1 . . . A 31 TYR C . 18387 1 347 . 1 1 31 31 TYR CA C 13 60.165 0.010 . 1 . . . A 31 TYR CA . 18387 1 348 . 1 1 31 31 TYR CB C 13 41.193 0.018 . 1 . . . A 31 TYR CB . 18387 1 349 . 1 1 31 31 TYR CD1 C 13 133.648 0.005 . 3 . . . A 31 TYR CD1 . 18387 1 350 . 1 1 31 31 TYR CD2 C 13 133.648 0.005 . 3 . . . A 31 TYR CD2 . 18387 1 351 . 1 1 31 31 TYR CE1 C 13 118.806 0.037 . 3 . . . A 31 TYR CE1 . 18387 1 352 . 1 1 31 31 TYR CE2 C 13 118.806 0.037 . 3 . . . A 31 TYR CE2 . 18387 1 353 . 1 1 31 31 TYR N N 15 117.383 0.037 . 1 . . . A 31 TYR N . 18387 1 354 . 1 1 32 32 VAL H H 1 9.244 0.003 . 1 . . . A 32 VAL H . 18387 1 355 . 1 1 32 32 VAL HA H 1 4.439 0.002 . 1 . . . A 32 VAL HA . 18387 1 356 . 1 1 32 32 VAL HB H 1 1.632 0.002 . 1 . . . A 32 VAL HB . 18387 1 357 . 1 1 32 32 VAL HG11 H 1 0.474 0.004 . 2 . . . A 32 VAL HG11 . 18387 1 358 . 1 1 32 32 VAL HG12 H 1 0.474 0.004 . 2 . . . A 32 VAL HG12 . 18387 1 359 . 1 1 32 32 VAL HG13 H 1 0.474 0.004 . 2 . . . A 32 VAL HG13 . 18387 1 360 . 1 1 32 32 VAL HG21 H 1 0.519 0.004 . 2 . . . A 32 VAL HG21 . 18387 1 361 . 1 1 32 32 VAL HG22 H 1 0.519 0.004 . 2 . . . A 32 VAL HG22 . 18387 1 362 . 1 1 32 32 VAL HG23 H 1 0.519 0.004 . 2 . . . A 32 VAL HG23 . 18387 1 363 . 1 1 32 32 VAL C C 13 175.975 0.017 . 1 . . . A 32 VAL C . 18387 1 364 . 1 1 32 32 VAL CA C 13 59.706 0.009 . 1 . . . A 32 VAL CA . 18387 1 365 . 1 1 32 32 VAL CB C 13 35.507 0.010 . 1 . . . A 32 VAL CB . 18387 1 366 . 1 1 32 32 VAL CG1 C 13 22.528 0.040 . 2 . . . A 32 VAL CG1 . 18387 1 367 . 1 1 32 32 VAL CG2 C 13 22.653 0.012 . 2 . . . A 32 VAL CG2 . 18387 1 368 . 1 1 32 32 VAL N N 15 120.900 0.008 . 1 . . . A 32 VAL N . 18387 1 369 . 1 1 33 33 LEU H H 1 8.161 0.001 . 1 . . . A 33 LEU H . 18387 1 370 . 1 1 33 33 LEU HA H 1 5.173 0.003 . 1 . . . A 33 LEU HA . 18387 1 371 . 1 1 33 33 LEU HB2 H 1 1.727 0.003 . 2 . . . A 33 LEU HB2 . 18387 1 372 . 1 1 33 33 LEU HB3 H 1 1.502 0.003 . 2 . . . A 33 LEU HB3 . 18387 1 373 . 1 1 33 33 LEU HG H 1 1.495 0.002 . 1 . . . A 33 LEU HG . 18387 1 374 . 1 1 33 33 LEU HD11 H 1 0.755 0.001 . 2 . . . A 33 LEU HD11 . 18387 1 375 . 1 1 33 33 LEU HD12 H 1 0.755 0.001 . 2 . . . A 33 LEU HD12 . 18387 1 376 . 1 1 33 33 LEU HD13 H 1 0.755 0.001 . 2 . . . A 33 LEU HD13 . 18387 1 377 . 1 1 33 33 LEU HD21 H 1 0.802 0.005 . 2 . . . A 33 LEU HD21 . 18387 1 378 . 1 1 33 33 LEU HD22 H 1 0.802 0.005 . 2 . . . A 33 LEU HD22 . 18387 1 379 . 1 1 33 33 LEU HD23 H 1 0.802 0.005 . 2 . . . A 33 LEU HD23 . 18387 1 380 . 1 1 33 33 LEU C C 13 174.693 0.010 . 1 . . . A 33 LEU C . 18387 1 381 . 1 1 33 33 LEU CA C 13 53.348 0.007 . 1 . . . A 33 LEU CA . 18387 1 382 . 1 1 33 33 LEU CB C 13 44.321 0.018 . 1 . . . A 33 LEU CB . 18387 1 383 . 1 1 33 33 LEU CG C 13 26.786 0.000 . 1 . . . A 33 LEU CG . 18387 1 384 . 1 1 33 33 LEU CD1 C 13 27.443 0.012 . 2 . . . A 33 LEU CD1 . 18387 1 385 . 1 1 33 33 LEU CD2 C 13 26.842 0.013 . 2 . . . A 33 LEU CD2 . 18387 1 386 . 1 1 33 33 LEU N N 15 130.058 0.007 . 1 . . . A 33 LEU N . 18387 1 387 . 1 1 34 34 VAL H H 1 9.296 0.002 . 1 . . . A 34 VAL H . 18387 1 388 . 1 1 34 34 VAL HA H 1 4.982 0.003 . 1 . . . A 34 VAL HA . 18387 1 389 . 1 1 34 34 VAL HB H 1 2.028 0.002 . 1 . . . A 34 VAL HB . 18387 1 390 . 1 1 34 34 VAL HG11 H 1 0.465 0.004 . 2 . . . A 34 VAL HG11 . 18387 1 391 . 1 1 34 34 VAL HG12 H 1 0.465 0.004 . 2 . . . A 34 VAL HG12 . 18387 1 392 . 1 1 34 34 VAL HG13 H 1 0.465 0.004 . 2 . . . A 34 VAL HG13 . 18387 1 393 . 1 1 34 34 VAL HG21 H 1 0.966 0.005 . 2 . . . A 34 VAL HG21 . 18387 1 394 . 1 1 34 34 VAL HG22 H 1 0.966 0.005 . 2 . . . A 34 VAL HG22 . 18387 1 395 . 1 1 34 34 VAL HG23 H 1 0.966 0.005 . 2 . . . A 34 VAL HG23 . 18387 1 396 . 1 1 34 34 VAL C C 13 174.285 0.005 . 1 . . . A 34 VAL C . 18387 1 397 . 1 1 34 34 VAL CA C 13 61.506 0.009 . 1 . . . A 34 VAL CA . 18387 1 398 . 1 1 34 34 VAL CB C 13 32.378 0.015 . 1 . . . A 34 VAL CB . 18387 1 399 . 1 1 34 34 VAL CG1 C 13 22.413 0.033 . 2 . . . A 34 VAL CG1 . 18387 1 400 . 1 1 34 34 VAL CG2 C 13 22.871 0.028 . 2 . . . A 34 VAL CG2 . 18387 1 401 . 1 1 34 34 VAL N N 15 129.232 0.013 . 1 . . . A 34 VAL N . 18387 1 402 . 1 1 35 35 ASP H H 1 8.015 0.001 . 1 . . . A 35 ASP H . 18387 1 403 . 1 1 35 35 ASP HA H 1 5.349 0.003 . 1 . . . A 35 ASP HA . 18387 1 404 . 1 1 35 35 ASP HB2 H 1 2.092 0.003 . 2 . . . A 35 ASP HB2 . 18387 1 405 . 1 1 35 35 ASP HB3 H 1 2.673 0.003 . 2 . . . A 35 ASP HB3 . 18387 1 406 . 1 1 35 35 ASP C C 13 174.258 0.008 . 1 . . . A 35 ASP C . 18387 1 407 . 1 1 35 35 ASP CA C 13 51.054 0.014 . 1 . . . A 35 ASP CA . 18387 1 408 . 1 1 35 35 ASP CB C 13 40.462 0.016 . 1 . . . A 35 ASP CB . 18387 1 409 . 1 1 35 35 ASP N N 15 123.675 0.008 . 1 . . . A 35 ASP N . 18387 1 410 . 1 1 36 36 PHE H H 1 9.171 0.001 . 1 . . . A 36 PHE H . 18387 1 411 . 1 1 36 36 PHE HA H 1 5.935 0.004 . 1 . . . A 36 PHE HA . 18387 1 412 . 1 1 36 36 PHE HB2 H 1 3.000 0.003 . 2 . . . A 36 PHE HB2 . 18387 1 413 . 1 1 36 36 PHE HB3 H 1 3.626 0.004 . 2 . . . A 36 PHE HB3 . 18387 1 414 . 1 1 36 36 PHE HD1 H 1 7.322 0.002 . 3 . . . A 36 PHE HD1 . 18387 1 415 . 1 1 36 36 PHE HD2 H 1 7.322 0.002 . 3 . . . A 36 PHE HD2 . 18387 1 416 . 1 1 36 36 PHE HE1 H 1 6.681 0.004 . 3 . . . A 36 PHE HE1 . 18387 1 417 . 1 1 36 36 PHE HE2 H 1 6.681 0.004 . 3 . . . A 36 PHE HE2 . 18387 1 418 . 1 1 36 36 PHE HZ H 1 5.688 0.003 . 1 . . . A 36 PHE HZ . 18387 1 419 . 1 1 36 36 PHE C C 13 175.432 0.012 . 1 . . . A 36 PHE C . 18387 1 420 . 1 1 36 36 PHE CA C 13 58.095 0.019 . 1 . . . A 36 PHE CA . 18387 1 421 . 1 1 36 36 PHE CB C 13 40.030 0.012 . 1 . . . A 36 PHE CB . 18387 1 422 . 1 1 36 36 PHE CD1 C 13 132.435 0.040 . 3 . . . A 36 PHE CD1 . 18387 1 423 . 1 1 36 36 PHE CD2 C 13 132.435 0.040 . 3 . . . A 36 PHE CD2 . 18387 1 424 . 1 1 36 36 PHE CE1 C 13 130.492 0.038 . 3 . . . A 36 PHE CE1 . 18387 1 425 . 1 1 36 36 PHE CE2 C 13 130.492 0.038 . 3 . . . A 36 PHE CE2 . 18387 1 426 . 1 1 36 36 PHE CZ C 13 130.247 0.051 . 1 . . . A 36 PHE CZ . 18387 1 427 . 1 1 36 36 PHE N N 15 126.959 0.009 . 1 . . . A 36 PHE N . 18387 1 428 . 1 1 37 37 TRP H H 1 9.280 0.002 . 1 . . . A 37 TRP H . 18387 1 429 . 1 1 37 37 TRP HA H 1 5.757 0.003 . 1 . . . A 37 TRP HA . 18387 1 430 . 1 1 37 37 TRP HB2 H 1 3.184 0.001 . 2 . . . A 37 TRP HB2 . 18387 1 431 . 1 1 37 37 TRP HB3 H 1 3.427 0.002 . 2 . . . A 37 TRP HB3 . 18387 1 432 . 1 1 37 37 TRP HD1 H 1 7.714 0.002 . 1 . . . A 37 TRP HD1 . 18387 1 433 . 1 1 37 37 TRP HE1 H 1 10.442 0.000 . 1 . . . A 37 TRP HE1 . 18387 1 434 . 1 1 37 37 TRP HE3 H 1 7.233 0.003 . 1 . . . A 37 TRP HE3 . 18387 1 435 . 1 1 37 37 TRP HZ2 H 1 7.443 0.000 . 1 . . . A 37 TRP HZ2 . 18387 1 436 . 1 1 37 37 TRP HZ3 H 1 6.704 0.004 . 1 . . . A 37 TRP HZ3 . 18387 1 437 . 1 1 37 37 TRP HH2 H 1 7.051 0.003 . 1 . . . A 37 TRP HH2 . 18387 1 438 . 1 1 37 37 TRP C C 13 172.412 0.003 . 1 . . . A 37 TRP C . 18387 1 439 . 1 1 37 37 TRP CA C 13 55.909 0.005 . 1 . . . A 37 TRP CA . 18387 1 440 . 1 1 37 37 TRP CB C 13 32.680 0.017 . 1 . . . A 37 TRP CB . 18387 1 441 . 1 1 37 37 TRP CD1 C 13 128.589 0.008 . 1 . . . A 37 TRP CD1 . 18387 1 442 . 1 1 37 37 TRP CE3 C 13 120.303 0.026 . 1 . . . A 37 TRP CE3 . 18387 1 443 . 1 1 37 37 TRP CZ2 C 13 115.169 0.015 . 1 . . . A 37 TRP CZ2 . 18387 1 444 . 1 1 37 37 TRP CZ3 C 13 120.109 0.029 . 1 . . . A 37 TRP CZ3 . 18387 1 445 . 1 1 37 37 TRP CH2 C 13 122.803 0.044 . 1 . . . A 37 TRP CH2 . 18387 1 446 . 1 1 37 37 TRP N N 15 120.839 0.010 . 1 . . . A 37 TRP N . 18387 1 447 . 1 1 37 37 TRP NE1 N 15 130.018 0.009 . 1 . . . A 37 TRP NE1 . 18387 1 448 . 1 1 38 38 PHE H H 1 7.062 0.002 . 1 . . . A 38 PHE H . 18387 1 449 . 1 1 38 38 PHE HA H 1 3.933 0.001 . 1 . . . A 38 PHE HA . 18387 1 450 . 1 1 38 38 PHE HB2 H 1 2.553 0.003 . 2 . . . A 38 PHE HB2 . 18387 1 451 . 1 1 38 38 PHE HB3 H 1 3.137 0.003 . 2 . . . A 38 PHE HB3 . 18387 1 452 . 1 1 38 38 PHE HD1 H 1 6.709 0.001 . 3 . . . A 38 PHE HD1 . 18387 1 453 . 1 1 38 38 PHE HD2 H 1 6.709 0.001 . 3 . . . A 38 PHE HD2 . 18387 1 454 . 1 1 38 38 PHE HE1 H 1 6.937 0.000 . 3 . . . A 38 PHE HE1 . 18387 1 455 . 1 1 38 38 PHE HE2 H 1 6.937 0.000 . 3 . . . A 38 PHE HE2 . 18387 1 456 . 1 1 38 38 PHE HZ H 1 7.251 0.000 . 1 . . . A 38 PHE HZ . 18387 1 457 . 1 1 38 38 PHE C C 13 176.141 0.002 . 1 . . . A 38 PHE C . 18387 1 458 . 1 1 38 38 PHE CA C 13 57.011 0.013 . 1 . . . A 38 PHE CA . 18387 1 459 . 1 1 38 38 PHE CB C 13 39.619 0.010 . 1 . . . A 38 PHE CB . 18387 1 460 . 1 1 38 38 PHE CD1 C 13 132.770 0.006 . 3 . . . A 38 PHE CD1 . 18387 1 461 . 1 1 38 38 PHE CD2 C 13 132.770 0.006 . 3 . . . A 38 PHE CD2 . 18387 1 462 . 1 1 38 38 PHE CE1 C 13 131.316 0.010 . 3 . . . A 38 PHE CE1 . 18387 1 463 . 1 1 38 38 PHE CE2 C 13 131.316 0.010 . 3 . . . A 38 PHE CE2 . 18387 1 464 . 1 1 38 38 PHE CZ C 13 129.732 0.002 . 1 . . . A 38 PHE CZ . 18387 1 465 . 1 1 38 38 PHE N N 15 109.215 0.004 . 1 . . . A 38 PHE N . 18387 1 466 . 1 1 39 39 ALA H H 1 10.355 0.000 . 1 . . . A 39 ALA H . 18387 1 467 . 1 1 39 39 ALA HA H 1 4.065 0.003 . 1 . . . A 39 ALA HA . 18387 1 468 . 1 1 39 39 ALA HB1 H 1 1.473 0.002 . 1 . . . A 39 ALA HB1 . 18387 1 469 . 1 1 39 39 ALA HB2 H 1 1.473 0.002 . 1 . . . A 39 ALA HB2 . 18387 1 470 . 1 1 39 39 ALA HB3 H 1 1.473 0.002 . 1 . . . A 39 ALA HB3 . 18387 1 471 . 1 1 39 39 ALA C C 13 179.349 0.005 . 1 . . . A 39 ALA C . 18387 1 472 . 1 1 39 39 ALA CA C 13 56.064 0.019 . 1 . . . A 39 ALA CA . 18387 1 473 . 1 1 39 39 ALA CB C 13 19.897 0.016 . 1 . . . A 39 ALA CB . 18387 1 474 . 1 1 39 39 ALA N N 15 125.193 0.004 . 1 . . . A 39 ALA N . 18387 1 475 . 1 1 40 40 GLY H H 1 8.583 0.001 . 1 . . . A 40 GLY H . 18387 1 476 . 1 1 40 40 GLY HA2 H 1 4.073 0.002 . 2 . . . A 40 GLY HA2 . 18387 1 477 . 1 1 40 40 GLY HA3 H 1 3.730 0.003 . 2 . . . A 40 GLY HA3 . 18387 1 478 . 1 1 40 40 GLY C C 13 172.732 0.004 . 1 . . . A 40 GLY C . 18387 1 479 . 1 1 40 40 GLY CA C 13 44.936 0.017 . 1 . . . A 40 GLY CA . 18387 1 480 . 1 1 40 40 GLY N N 15 103.437 0.005 . 1 . . . A 40 GLY N . 18387 1 481 . 1 1 41 41 CYS H H 1 6.946 0.002 . 1 . . . A 41 CYS H . 18387 1 482 . 1 1 41 41 CYS HA H 1 4.404 0.001 . 1 . . . A 41 CYS HA . 18387 1 483 . 1 1 41 41 CYS HB2 H 1 1.668 0.005 . 2 . . . A 41 CYS HB2 . 18387 1 484 . 1 1 41 41 CYS HB3 H 1 2.341 0.002 . 2 . . . A 41 CYS HB3 . 18387 1 485 . 1 1 41 41 CYS C C 13 176.620 0.000 . 1 . . . A 41 CYS C . 18387 1 486 . 1 1 41 41 CYS CA C 13 58.375 0.007 . 1 . . . A 41 CYS CA . 18387 1 487 . 1 1 41 41 CYS CB C 13 28.376 0.016 . 1 . . . A 41 CYS CB . 18387 1 488 . 1 1 41 41 CYS N N 15 124.859 0.004 . 1 . . . A 41 CYS N . 18387 1 489 . 1 1 42 42 SER HA H 1 4.040 0.001 . 1 . . . A 42 SER HA . 18387 1 490 . 1 1 42 42 SER HB2 H 1 3.632 0.001 . 2 . . . A 42 SER HB2 . 18387 1 491 . 1 1 42 42 SER HB3 H 1 3.691 0.000 . 2 . . . A 42 SER HB3 . 18387 1 492 . 1 1 42 42 SER CA C 13 61.552 0.010 . 1 . . . A 42 SER CA . 18387 1 493 . 1 1 42 42 SER CB C 13 62.675 0.015 . 1 . . . A 42 SER CB . 18387 1 494 . 1 1 43 43 TRP HA H 1 4.549 0.001 . 1 . . . A 43 TRP HA . 18387 1 495 . 1 1 43 43 TRP HB2 H 1 3.389 0.002 . 2 . . . A 43 TRP HB2 . 18387 1 496 . 1 1 43 43 TRP HB3 H 1 3.589 0.003 . 2 . . . A 43 TRP HB3 . 18387 1 497 . 1 1 43 43 TRP HD1 H 1 7.546 0.001 . 1 . . . A 43 TRP HD1 . 18387 1 498 . 1 1 43 43 TRP HE1 H 1 10.337 0.000 . 1 . . . A 43 TRP HE1 . 18387 1 499 . 1 1 43 43 TRP HE3 H 1 7.814 0.002 . 1 . . . A 43 TRP HE3 . 18387 1 500 . 1 1 43 43 TRP HZ2 H 1 7.627 0.001 . 1 . . . A 43 TRP HZ2 . 18387 1 501 . 1 1 43 43 TRP HZ3 H 1 7.294 0.002 . 1 . . . A 43 TRP HZ3 . 18387 1 502 . 1 1 43 43 TRP HH2 H 1 7.351 0.000 . 1 . . . A 43 TRP HH2 . 18387 1 503 . 1 1 43 43 TRP C C 13 180.400 0.008 . 1 . . . A 43 TRP C . 18387 1 504 . 1 1 43 43 TRP CA C 13 60.249 0.017 . 1 . . . A 43 TRP CA . 18387 1 505 . 1 1 43 43 TRP CB C 13 29.592 0.015 . 1 . . . A 43 TRP CB . 18387 1 506 . 1 1 43 43 TRP CD1 C 13 128.274 0.017 . 1 . . . A 43 TRP CD1 . 18387 1 507 . 1 1 43 43 TRP CE3 C 13 120.831 0.029 . 1 . . . A 43 TRP CE3 . 18387 1 508 . 1 1 43 43 TRP CZ2 C 13 115.380 0.009 . 1 . . . A 43 TRP CZ2 . 18387 1 509 . 1 1 43 43 TRP CZ3 C 13 122.558 0.018 . 1 . . . A 43 TRP CZ3 . 18387 1 510 . 1 1 43 43 TRP CH2 C 13 125.220 0.015 . 1 . . . A 43 TRP CH2 . 18387 1 511 . 1 1 43 43 TRP N N 15 129.748 0.000 . 1 . . . A 43 TRP N . 18387 1 512 . 1 1 43 43 TRP NE1 N 15 129.693 0.007 . 1 . . . A 43 TRP NE1 . 18387 1 513 . 1 1 44 44 CYS H H 1 9.591 0.001 . 1 . . . A 44 CYS H . 18387 1 514 . 1 1 44 44 CYS HA H 1 4.251 0.004 . 1 . . . A 44 CYS HA . 18387 1 515 . 1 1 44 44 CYS HB2 H 1 3.254 0.005 . 2 . . . A 44 CYS HB2 . 18387 1 516 . 1 1 44 44 CYS HB3 H 1 3.821 0.006 . 2 . . . A 44 CYS HB3 . 18387 1 517 . 1 1 44 44 CYS C C 13 178.643 0.009 . 1 . . . A 44 CYS C . 18387 1 518 . 1 1 44 44 CYS CA C 13 64.849 0.012 . 1 . . . A 44 CYS CA . 18387 1 519 . 1 1 44 44 CYS CB C 13 29.422 0.014 . 1 . . . A 44 CYS CB . 18387 1 520 . 1 1 44 44 CYS N N 15 124.462 0.008 . 1 . . . A 44 CYS N . 18387 1 521 . 1 1 45 45 ARG H H 1 7.955 0.001 . 1 . . . A 45 ARG H . 18387 1 522 . 1 1 45 45 ARG HA H 1 4.176 0.002 . 1 . . . A 45 ARG HA . 18387 1 523 . 1 1 45 45 ARG HB2 H 1 1.900 0.002 . 2 . . . A 45 ARG HB2 . 18387 1 524 . 1 1 45 45 ARG HB3 H 1 2.267 0.001 . 2 . . . A 45 ARG HB3 . 18387 1 525 . 1 1 45 45 ARG HG2 H 1 2.015 0.003 . 1 . . . A 45 ARG HG2 . 18387 1 526 . 1 1 45 45 ARG HG3 H 1 2.015 0.003 . 1 . . . A 45 ARG HG3 . 18387 1 527 . 1 1 45 45 ARG HD2 H 1 3.626 0.003 . 2 . . . A 45 ARG HD2 . 18387 1 528 . 1 1 45 45 ARG HD3 H 1 3.149 0.002 . 2 . . . A 45 ARG HD3 . 18387 1 529 . 1 1 45 45 ARG HE H 1 9.329 0.000 . 1 . . . A 45 ARG HE . 18387 1 530 . 1 1 45 45 ARG C C 13 180.302 0.010 . 1 . . . A 45 ARG C . 18387 1 531 . 1 1 45 45 ARG CA C 13 56.943 0.012 . 1 . . . A 45 ARG CA . 18387 1 532 . 1 1 45 45 ARG CB C 13 27.631 0.029 . 1 . . . A 45 ARG CB . 18387 1 533 . 1 1 45 45 ARG CG C 13 25.769 0.005 . 1 . . . A 45 ARG CG . 18387 1 534 . 1 1 45 45 ARG CD C 13 40.015 0.008 . 1 . . . A 45 ARG CD . 18387 1 535 . 1 1 45 45 ARG N N 15 117.248 0.025 . 1 . . . A 45 ARG N . 18387 1 536 . 1 1 45 45 ARG NE N 15 81.954 0.011 . 1 . . . A 45 ARG NE . 18387 1 537 . 1 1 46 46 LYS H H 1 8.129 0.001 . 1 . . . A 46 LYS H . 18387 1 538 . 1 1 46 46 LYS HA H 1 4.272 0.002 . 1 . . . A 46 LYS HA . 18387 1 539 . 1 1 46 46 LYS HB2 H 1 2.148 0.003 . 2 . . . A 46 LYS HB2 . 18387 1 540 . 1 1 46 46 LYS HB3 H 1 2.202 0.006 . 2 . . . A 46 LYS HB3 . 18387 1 541 . 1 1 46 46 LYS HG2 H 1 1.624 0.001 . 2 . . . A 46 LYS HG2 . 18387 1 542 . 1 1 46 46 LYS HG3 H 1 1.756 0.002 . 2 . . . A 46 LYS HG3 . 18387 1 543 . 1 1 46 46 LYS HD2 H 1 1.564 0.003 . 2 . . . A 46 LYS HD2 . 18387 1 544 . 1 1 46 46 LYS HD3 H 1 1.755 0.003 . 2 . . . A 46 LYS HD3 . 18387 1 545 . 1 1 46 46 LYS HE2 H 1 2.888 0.001 . 1 . . . A 46 LYS HE2 . 18387 1 546 . 1 1 46 46 LYS HE3 H 1 2.888 0.001 . 1 . . . A 46 LYS HE3 . 18387 1 547 . 1 1 46 46 LYS C C 13 177.755 0.005 . 1 . . . A 46 LYS C . 18387 1 548 . 1 1 46 46 LYS CA C 13 58.769 0.012 . 1 . . . A 46 LYS CA . 18387 1 549 . 1 1 46 46 LYS CB C 13 33.157 0.016 . 1 . . . A 46 LYS CB . 18387 1 550 . 1 1 46 46 LYS CG C 13 26.257 0.003 . 1 . . . A 46 LYS CG . 18387 1 551 . 1 1 46 46 LYS CD C 13 29.566 0.009 . 1 . . . A 46 LYS CD . 18387 1 552 . 1 1 46 46 LYS CE C 13 42.020 0.005 . 1 . . . A 46 LYS CE . 18387 1 553 . 1 1 46 46 LYS N N 15 120.318 0.013 . 1 . . . A 46 LYS N . 18387 1 554 . 1 1 47 47 GLU H H 1 7.386 0.002 . 1 . . . A 47 GLU H . 18387 1 555 . 1 1 47 47 GLU HA H 1 4.891 0.002 . 1 . . . A 47 GLU HA . 18387 1 556 . 1 1 47 47 GLU HB2 H 1 2.071 0.003 . 2 . . . A 47 GLU HB2 . 18387 1 557 . 1 1 47 47 GLU HB3 H 1 2.498 0.003 . 2 . . . A 47 GLU HB3 . 18387 1 558 . 1 1 47 47 GLU HG2 H 1 2.403 0.001 . 2 . . . A 47 GLU HG2 . 18387 1 559 . 1 1 47 47 GLU HG3 H 1 2.615 0.002 . 2 . . . A 47 GLU HG3 . 18387 1 560 . 1 1 47 47 GLU C C 13 178.701 0.002 . 1 . . . A 47 GLU C . 18387 1 561 . 1 1 47 47 GLU CA C 13 56.554 0.014 . 1 . . . A 47 GLU CA . 18387 1 562 . 1 1 47 47 GLU CB C 13 29.766 0.014 . 1 . . . A 47 GLU CB . 18387 1 563 . 1 1 47 47 GLU CG C 13 36.128 0.008 . 1 . . . A 47 GLU CG . 18387 1 564 . 1 1 47 47 GLU N N 15 114.278 0.014 . 1 . . . A 47 GLU N . 18387 1 565 . 1 1 48 48 THR H H 1 7.810 0.001 . 1 . . . A 48 THR H . 18387 1 566 . 1 1 48 48 THR HA H 1 4.048 0.002 . 1 . . . A 48 THR HA . 18387 1 567 . 1 1 48 48 THR HB H 1 4.450 0.002 . 1 . . . A 48 THR HB . 18387 1 568 . 1 1 48 48 THR HG21 H 1 1.287 0.002 . 1 . . . A 48 THR HG21 . 18387 1 569 . 1 1 48 48 THR HG22 H 1 1.287 0.002 . 1 . . . A 48 THR HG22 . 18387 1 570 . 1 1 48 48 THR HG23 H 1 1.287 0.002 . 1 . . . A 48 THR HG23 . 18387 1 571 . 1 1 48 48 THR C C 13 172.392 0.000 . 1 . . . A 48 THR C . 18387 1 572 . 1 1 48 48 THR CA C 13 69.426 0.011 . 1 . . . A 48 THR CA . 18387 1 573 . 1 1 48 48 THR CB C 13 66.906 0.027 . 1 . . . A 48 THR CB . 18387 1 574 . 1 1 48 48 THR CG2 C 13 23.166 0.008 . 1 . . . A 48 THR CG2 . 18387 1 575 . 1 1 48 48 THR N N 15 115.665 0.011 . 1 . . . A 48 THR N . 18387 1 576 . 1 1 49 49 PRO HA H 1 4.289 0.002 . 1 . . . A 49 PRO HA . 18387 1 577 . 1 1 49 49 PRO HB2 H 1 1.331 0.001 . 2 . . . A 49 PRO HB2 . 18387 1 578 . 1 1 49 49 PRO HB3 H 1 2.190 0.001 . 2 . . . A 49 PRO HB3 . 18387 1 579 . 1 1 49 49 PRO HG2 H 1 1.862 0.001 . 2 . . . A 49 PRO HG2 . 18387 1 580 . 1 1 49 49 PRO HG3 H 1 1.949 0.001 . 2 . . . A 49 PRO HG3 . 18387 1 581 . 1 1 49 49 PRO HD2 H 1 3.649 0.001 . 2 . . . A 49 PRO HD2 . 18387 1 582 . 1 1 49 49 PRO HD3 H 1 3.828 0.004 . 2 . . . A 49 PRO HD3 . 18387 1 583 . 1 1 49 49 PRO C C 13 179.828 0.000 . 1 . . . A 49 PRO C . 18387 1 584 . 1 1 49 49 PRO CA C 13 66.599 0.014 . 1 . . . A 49 PRO CA . 18387 1 585 . 1 1 49 49 PRO CB C 13 31.034 0.012 . 1 . . . A 49 PRO CB . 18387 1 586 . 1 1 49 49 PRO CG C 13 28.535 0.008 . 1 . . . A 49 PRO CG . 18387 1 587 . 1 1 49 49 PRO CD C 13 49.995 0.005 . 1 . . . A 49 PRO CD . 18387 1 588 . 1 1 50 50 TYR H H 1 7.071 0.002 . 1 . . . A 50 TYR H . 18387 1 589 . 1 1 50 50 TYR HA H 1 4.138 0.004 . 1 . . . A 50 TYR HA . 18387 1 590 . 1 1 50 50 TYR HB2 H 1 3.233 0.004 . 1 . . . A 50 TYR HB2 . 18387 1 591 . 1 1 50 50 TYR HB3 H 1 3.233 0.004 . 1 . . . A 50 TYR HB3 . 18387 1 592 . 1 1 50 50 TYR HD1 H 1 7.198 0.004 . 3 . . . A 50 TYR HD1 . 18387 1 593 . 1 1 50 50 TYR HD2 H 1 7.198 0.004 . 3 . . . A 50 TYR HD2 . 18387 1 594 . 1 1 50 50 TYR HE1 H 1 6.995 0.002 . 3 . . . A 50 TYR HE1 . 18387 1 595 . 1 1 50 50 TYR HE2 H 1 6.995 0.002 . 3 . . . A 50 TYR HE2 . 18387 1 596 . 1 1 50 50 TYR C C 13 179.488 0.014 . 1 . . . A 50 TYR C . 18387 1 597 . 1 1 50 50 TYR CA C 13 61.135 0.015 . 1 . . . A 50 TYR CA . 18387 1 598 . 1 1 50 50 TYR CB C 13 38.301 0.022 . 1 . . . A 50 TYR CB . 18387 1 599 . 1 1 50 50 TYR CD1 C 13 133.620 0.025 . 3 . . . A 50 TYR CD1 . 18387 1 600 . 1 1 50 50 TYR CD2 C 13 133.620 0.025 . 3 . . . A 50 TYR CD2 . 18387 1 601 . 1 1 50 50 TYR CE1 C 13 119.094 0.038 . 3 . . . A 50 TYR CE1 . 18387 1 602 . 1 1 50 50 TYR CE2 C 13 119.094 0.038 . 3 . . . A 50 TYR CE2 . 18387 1 603 . 1 1 50 50 TYR N N 15 116.950 0.021 . 1 . . . A 50 TYR N . 18387 1 604 . 1 1 51 51 LEU H H 1 8.243 0.001 . 1 . . . A 51 LEU H . 18387 1 605 . 1 1 51 51 LEU HA H 1 3.670 0.002 . 1 . . . A 51 LEU HA . 18387 1 606 . 1 1 51 51 LEU HB2 H 1 0.812 0.005 . 2 . . . A 51 LEU HB2 . 18387 1 607 . 1 1 51 51 LEU HB3 H 1 2.013 0.002 . 2 . . . A 51 LEU HB3 . 18387 1 608 . 1 1 51 51 LEU HG H 1 1.602 0.002 . 1 . . . A 51 LEU HG . 18387 1 609 . 1 1 51 51 LEU HD11 H 1 0.606 0.003 . 2 . . . A 51 LEU HD11 . 18387 1 610 . 1 1 51 51 LEU HD12 H 1 0.606 0.003 . 2 . . . A 51 LEU HD12 . 18387 1 611 . 1 1 51 51 LEU HD13 H 1 0.606 0.003 . 2 . . . A 51 LEU HD13 . 18387 1 612 . 1 1 51 51 LEU HD21 H 1 0.790 0.002 . 2 . . . A 51 LEU HD21 . 18387 1 613 . 1 1 51 51 LEU HD22 H 1 0.790 0.002 . 2 . . . A 51 LEU HD22 . 18387 1 614 . 1 1 51 51 LEU HD23 H 1 0.790 0.002 . 2 . . . A 51 LEU HD23 . 18387 1 615 . 1 1 51 51 LEU C C 13 178.072 0.024 . 1 . . . A 51 LEU C . 18387 1 616 . 1 1 51 51 LEU CA C 13 58.676 0.012 . 1 . . . A 51 LEU CA . 18387 1 617 . 1 1 51 51 LEU CB C 13 42.617 0.025 . 1 . . . A 51 LEU CB . 18387 1 618 . 1 1 51 51 LEU CG C 13 27.203 0.000 . 1 . . . A 51 LEU CG . 18387 1 619 . 1 1 51 51 LEU CD1 C 13 25.684 0.005 . 2 . . . A 51 LEU CD1 . 18387 1 620 . 1 1 51 51 LEU CD2 C 13 26.746 0.014 . 2 . . . A 51 LEU CD2 . 18387 1 621 . 1 1 51 51 LEU N N 15 123.989 0.013 . 1 . . . A 51 LEU N . 18387 1 622 . 1 1 52 52 LEU H H 1 9.085 0.000 . 1 . . . A 52 LEU H . 18387 1 623 . 1 1 52 52 LEU HA H 1 4.327 0.005 . 1 . . . A 52 LEU HA . 18387 1 624 . 1 1 52 52 LEU HB2 H 1 1.783 0.002 . 2 . . . A 52 LEU HB2 . 18387 1 625 . 1 1 52 52 LEU HB3 H 1 1.834 0.005 . 2 . . . A 52 LEU HB3 . 18387 1 626 . 1 1 52 52 LEU HG H 1 1.836 0.004 . 1 . . . A 52 LEU HG . 18387 1 627 . 1 1 52 52 LEU HD11 H 1 1.127 0.003 . 2 . . . A 52 LEU HD11 . 18387 1 628 . 1 1 52 52 LEU HD12 H 1 1.127 0.003 . 2 . . . A 52 LEU HD12 . 18387 1 629 . 1 1 52 52 LEU HD13 H 1 1.127 0.003 . 2 . . . A 52 LEU HD13 . 18387 1 630 . 1 1 52 52 LEU HD21 H 1 1.089 0.003 . 2 . . . A 52 LEU HD21 . 18387 1 631 . 1 1 52 52 LEU HD22 H 1 1.089 0.003 . 2 . . . A 52 LEU HD22 . 18387 1 632 . 1 1 52 52 LEU HD23 H 1 1.089 0.003 . 2 . . . A 52 LEU HD23 . 18387 1 633 . 1 1 52 52 LEU C C 13 178.704 0.007 . 1 . . . A 52 LEU C . 18387 1 634 . 1 1 52 52 LEU CA C 13 58.575 0.014 . 1 . . . A 52 LEU CA . 18387 1 635 . 1 1 52 52 LEU CB C 13 42.738 0.006 . 1 . . . A 52 LEU CB . 18387 1 636 . 1 1 52 52 LEU CG C 13 27.580 0.004 . 1 . . . A 52 LEU CG . 18387 1 637 . 1 1 52 52 LEU CD1 C 13 24.862 0.005 . 2 . . . A 52 LEU CD1 . 18387 1 638 . 1 1 52 52 LEU CD2 C 13 24.735 0.010 . 2 . . . A 52 LEU CD2 . 18387 1 639 . 1 1 52 52 LEU N N 15 119.857 0.012 . 1 . . . A 52 LEU N . 18387 1 640 . 1 1 53 53 LYS H H 1 7.807 0.003 . 1 . . . A 53 LYS H . 18387 1 641 . 1 1 53 53 LYS HA H 1 4.109 0.003 . 1 . . . A 53 LYS HA . 18387 1 642 . 1 1 53 53 LYS HB2 H 1 1.921 0.002 . 2 . . . A 53 LYS HB2 . 18387 1 643 . 1 1 53 53 LYS HB3 H 1 2.055 0.002 . 2 . . . A 53 LYS HB3 . 18387 1 644 . 1 1 53 53 LYS HG2 H 1 1.362 0.004 . 2 . . . A 53 LYS HG2 . 18387 1 645 . 1 1 53 53 LYS HG3 H 1 1.459 0.002 . 2 . . . A 53 LYS HG3 . 18387 1 646 . 1 1 53 53 LYS HD2 H 1 1.379 0.002 . 2 . . . A 53 LYS HD2 . 18387 1 647 . 1 1 53 53 LYS HD3 H 1 1.538 0.002 . 2 . . . A 53 LYS HD3 . 18387 1 648 . 1 1 53 53 LYS HE2 H 1 2.144 0.002 . 2 . . . A 53 LYS HE2 . 18387 1 649 . 1 1 53 53 LYS HE3 H 1 2.466 0.002 . 2 . . . A 53 LYS HE3 . 18387 1 650 . 1 1 53 53 LYS C C 13 179.786 0.004 . 1 . . . A 53 LYS C . 18387 1 651 . 1 1 53 53 LYS CA C 13 59.721 0.018 . 1 . . . A 53 LYS CA . 18387 1 652 . 1 1 53 53 LYS CB C 13 33.159 0.011 . 1 . . . A 53 LYS CB . 18387 1 653 . 1 1 53 53 LYS CG C 13 24.921 0.013 . 1 . . . A 53 LYS CG . 18387 1 654 . 1 1 53 53 LYS CD C 13 29.996 0.009 . 1 . . . A 53 LYS CD . 18387 1 655 . 1 1 53 53 LYS CE C 13 41.306 0.006 . 1 . . . A 53 LYS CE . 18387 1 656 . 1 1 53 53 LYS N N 15 118.658 0.024 . 1 . . . A 53 LYS N . 18387 1 657 . 1 1 54 54 THR H H 1 7.771 0.003 . 1 . . . A 54 THR H . 18387 1 658 . 1 1 54 54 THR HA H 1 3.965 0.003 . 1 . . . A 54 THR HA . 18387 1 659 . 1 1 54 54 THR HB H 1 4.293 0.002 . 1 . . . A 54 THR HB . 18387 1 660 . 1 1 54 54 THR HG21 H 1 1.065 0.003 . 1 . . . A 54 THR HG21 . 18387 1 661 . 1 1 54 54 THR HG22 H 1 1.065 0.003 . 1 . . . A 54 THR HG22 . 18387 1 662 . 1 1 54 54 THR HG23 H 1 1.065 0.003 . 1 . . . A 54 THR HG23 . 18387 1 663 . 1 1 54 54 THR C C 13 175.328 0.004 . 1 . . . A 54 THR C . 18387 1 664 . 1 1 54 54 THR CA C 13 67.683 0.008 . 1 . . . A 54 THR CA . 18387 1 665 . 1 1 54 54 THR CB C 13 68.452 0.021 . 1 . . . A 54 THR CB . 18387 1 666 . 1 1 54 54 THR CG2 C 13 22.684 0.009 . 1 . . . A 54 THR CG2 . 18387 1 667 . 1 1 54 54 THR N N 15 116.869 0.008 . 1 . . . A 54 THR N . 18387 1 668 . 1 1 55 55 TYR H H 1 9.145 0.001 . 1 . . . A 55 TYR H . 18387 1 669 . 1 1 55 55 TYR HA H 1 4.272 0.003 . 1 . . . A 55 TYR HA . 18387 1 670 . 1 1 55 55 TYR HB2 H 1 3.165 0.002 . 2 . . . A 55 TYR HB2 . 18387 1 671 . 1 1 55 55 TYR HB3 H 1 3.259 0.005 . 2 . . . A 55 TYR HB3 . 18387 1 672 . 1 1 55 55 TYR HD1 H 1 7.149 0.002 . 3 . . . A 55 TYR HD1 . 18387 1 673 . 1 1 55 55 TYR HD2 H 1 7.149 0.002 . 3 . . . A 55 TYR HD2 . 18387 1 674 . 1 1 55 55 TYR HE1 H 1 7.146 0.003 . 3 . . . A 55 TYR HE1 . 18387 1 675 . 1 1 55 55 TYR HE2 H 1 7.146 0.003 . 3 . . . A 55 TYR HE2 . 18387 1 676 . 1 1 55 55 TYR C C 13 176.809 0.005 . 1 . . . A 55 TYR C . 18387 1 677 . 1 1 55 55 TYR CA C 13 62.737 0.032 . 1 . . . A 55 TYR CA . 18387 1 678 . 1 1 55 55 TYR CB C 13 39.280 0.018 . 1 . . . A 55 TYR CB . 18387 1 679 . 1 1 55 55 TYR CD1 C 13 132.921 0.010 . 3 . . . A 55 TYR CD1 . 18387 1 680 . 1 1 55 55 TYR CD2 C 13 132.921 0.010 . 3 . . . A 55 TYR CD2 . 18387 1 681 . 1 1 55 55 TYR CE1 C 13 119.031 0.026 . 3 . . . A 55 TYR CE1 . 18387 1 682 . 1 1 55 55 TYR CE2 C 13 119.031 0.026 . 3 . . . A 55 TYR CE2 . 18387 1 683 . 1 1 55 55 TYR N N 15 122.202 0.008 . 1 . . . A 55 TYR N . 18387 1 684 . 1 1 56 56 ASN H H 1 8.850 0.001 . 1 . . . A 56 ASN H . 18387 1 685 . 1 1 56 56 ASN HA H 1 4.263 0.002 . 1 . . . A 56 ASN HA . 18387 1 686 . 1 1 56 56 ASN HB2 H 1 2.768 0.001 . 2 . . . A 56 ASN HB2 . 18387 1 687 . 1 1 56 56 ASN HB3 H 1 2.867 0.003 . 2 . . . A 56 ASN HB3 . 18387 1 688 . 1 1 56 56 ASN HD21 H 1 7.088 0.001 . 1 . . . A 56 ASN HD21 . 18387 1 689 . 1 1 56 56 ASN HD22 H 1 7.494 0.000 . 1 . . . A 56 ASN HD22 . 18387 1 690 . 1 1 56 56 ASN C C 13 177.427 0.003 . 1 . . . A 56 ASN C . 18387 1 691 . 1 1 56 56 ASN CA C 13 55.930 0.026 . 1 . . . A 56 ASN CA . 18387 1 692 . 1 1 56 56 ASN CB C 13 37.954 0.018 . 1 . . . A 56 ASN CB . 18387 1 693 . 1 1 56 56 ASN N N 15 113.858 0.006 . 1 . . . A 56 ASN N . 18387 1 694 . 1 1 56 56 ASN ND2 N 15 111.483 0.012 . 1 . . . A 56 ASN ND2 . 18387 1 695 . 1 1 57 57 ALA H H 1 7.436 0.001 . 1 . . . A 57 ALA H . 18387 1 696 . 1 1 57 57 ALA HA H 1 4.064 0.001 . 1 . . . A 57 ALA HA . 18387 1 697 . 1 1 57 57 ALA HB1 H 1 0.822 0.002 . 1 . . . A 57 ALA HB1 . 18387 1 698 . 1 1 57 57 ALA HB2 H 1 0.822 0.002 . 1 . . . A 57 ALA HB2 . 18387 1 699 . 1 1 57 57 ALA HB3 H 1 0.822 0.002 . 1 . . . A 57 ALA HB3 . 18387 1 700 . 1 1 57 57 ALA C C 13 180.445 0.007 . 1 . . . A 57 ALA C . 18387 1 701 . 1 1 57 57 ALA CA C 13 54.351 0.017 . 1 . . . A 57 ALA CA . 18387 1 702 . 1 1 57 57 ALA CB C 13 19.194 0.021 . 1 . . . A 57 ALA CB . 18387 1 703 . 1 1 57 57 ALA N N 15 118.829 0.011 . 1 . . . A 57 ALA N . 18387 1 704 . 1 1 58 58 PHE H H 1 7.480 0.001 . 1 . . . A 58 PHE H . 18387 1 705 . 1 1 58 58 PHE HA H 1 4.921 0.003 . 1 . . . A 58 PHE HA . 18387 1 706 . 1 1 58 58 PHE HB2 H 1 2.262 0.002 . 2 . . . A 58 PHE HB2 . 18387 1 707 . 1 1 58 58 PHE HB3 H 1 3.079 0.003 . 2 . . . A 58 PHE HB3 . 18387 1 708 . 1 1 58 58 PHE HD1 H 1 6.892 0.003 . 3 . . . A 58 PHE HD1 . 18387 1 709 . 1 1 58 58 PHE HD2 H 1 6.892 0.003 . 3 . . . A 58 PHE HD2 . 18387 1 710 . 1 1 58 58 PHE HE1 H 1 6.682 0.004 . 3 . . . A 58 PHE HE1 . 18387 1 711 . 1 1 58 58 PHE HE2 H 1 6.682 0.004 . 3 . . . A 58 PHE HE2 . 18387 1 712 . 1 1 58 58 PHE C C 13 176.999 0.004 . 1 . . . A 58 PHE C . 18387 1 713 . 1 1 58 58 PHE CA C 13 58.067 0.013 . 1 . . . A 58 PHE CA . 18387 1 714 . 1 1 58 58 PHE CB C 13 40.490 0.013 . 1 . . . A 58 PHE CB . 18387 1 715 . 1 1 58 58 PHE CD1 C 13 132.311 0.040 . 3 . . . A 58 PHE CD1 . 18387 1 716 . 1 1 58 58 PHE CD2 C 13 132.311 0.040 . 3 . . . A 58 PHE CD2 . 18387 1 717 . 1 1 58 58 PHE CE1 C 13 130.321 0.047 . 3 . . . A 58 PHE CE1 . 18387 1 718 . 1 1 58 58 PHE CE2 C 13 130.321 0.047 . 3 . . . A 58 PHE CE2 . 18387 1 719 . 1 1 58 58 PHE N N 15 112.082 0.036 . 1 . . . A 58 PHE N . 18387 1 720 . 1 1 59 59 LYS H H 1 8.411 0.001 . 1 . . . A 59 LYS H . 18387 1 721 . 1 1 59 59 LYS HA H 1 4.803 0.002 . 1 . . . A 59 LYS HA . 18387 1 722 . 1 1 59 59 LYS HB2 H 1 1.430 0.002 . 2 . . . A 59 LYS HB2 . 18387 1 723 . 1 1 59 59 LYS HB3 H 1 1.697 0.001 . 2 . . . A 59 LYS HB3 . 18387 1 724 . 1 1 59 59 LYS HG2 H 1 1.183 0.003 . 2 . . . A 59 LYS HG2 . 18387 1 725 . 1 1 59 59 LYS HG3 H 1 1.325 0.002 . 2 . . . A 59 LYS HG3 . 18387 1 726 . 1 1 59 59 LYS HD2 H 1 1.129 0.001 . 2 . . . A 59 LYS HD2 . 18387 1 727 . 1 1 59 59 LYS HD3 H 1 1.304 0.003 . 2 . . . A 59 LYS HD3 . 18387 1 728 . 1 1 59 59 LYS HE2 H 1 2.989 0.002 . 1 . . . A 59 LYS HE2 . 18387 1 729 . 1 1 59 59 LYS HE3 H 1 2.989 0.002 . 1 . . . A 59 LYS HE3 . 18387 1 730 . 1 1 59 59 LYS C C 13 177.157 0.026 . 1 . . . A 59 LYS C . 18387 1 731 . 1 1 59 59 LYS CA C 13 59.081 0.016 . 1 . . . A 59 LYS CA . 18387 1 732 . 1 1 59 59 LYS CB C 13 30.568 0.009 . 1 . . . A 59 LYS CB . 18387 1 733 . 1 1 59 59 LYS CG C 13 23.082 0.004 . 1 . . . A 59 LYS CG . 18387 1 734 . 1 1 59 59 LYS CD C 13 29.423 0.006 . 1 . . . A 59 LYS CD . 18387 1 735 . 1 1 59 59 LYS CE C 13 42.225 0.000 . 1 . . . A 59 LYS CE . 18387 1 736 . 1 1 59 59 LYS N N 15 120.666 0.023 . 1 . . . A 59 LYS N . 18387 1 737 . 1 1 60 60 ASP H H 1 8.574 0.001 . 1 . . . A 60 ASP H . 18387 1 738 . 1 1 60 60 ASP HA H 1 5.125 0.002 . 1 . . . A 60 ASP HA . 18387 1 739 . 1 1 60 60 ASP HB2 H 1 2.645 0.000 . 2 . . . A 60 ASP HB2 . 18387 1 740 . 1 1 60 60 ASP HB3 H 1 2.937 0.002 . 2 . . . A 60 ASP HB3 . 18387 1 741 . 1 1 60 60 ASP C C 13 176.889 0.017 . 1 . . . A 60 ASP C . 18387 1 742 . 1 1 60 60 ASP CA C 13 54.649 0.017 . 1 . . . A 60 ASP CA . 18387 1 743 . 1 1 60 60 ASP CB C 13 40.712 0.014 . 1 . . . A 60 ASP CB . 18387 1 744 . 1 1 60 60 ASP N N 15 118.908 0.011 . 1 . . . A 60 ASP N . 18387 1 745 . 1 1 61 61 LYS H H 1 8.278 0.001 . 1 . . . A 61 LYS H . 18387 1 746 . 1 1 61 61 LYS HA H 1 4.714 0.001 . 1 . . . A 61 LYS HA . 18387 1 747 . 1 1 61 61 LYS HB2 H 1 1.836 0.002 . 2 . . . A 61 LYS HB2 . 18387 1 748 . 1 1 61 61 LYS HB3 H 1 2.331 0.001 . 2 . . . A 61 LYS HB3 . 18387 1 749 . 1 1 61 61 LYS HG2 H 1 1.478 0.002 . 2 . . . A 61 LYS HG2 . 18387 1 750 . 1 1 61 61 LYS HG3 H 1 1.601 0.001 . 2 . . . A 61 LYS HG3 . 18387 1 751 . 1 1 61 61 LYS HD2 H 1 1.787 0.002 . 2 . . . A 61 LYS HD2 . 18387 1 752 . 1 1 61 61 LYS HD3 H 1 1.839 0.002 . 2 . . . A 61 LYS HD3 . 18387 1 753 . 1 1 61 61 LYS HE2 H 1 3.119 0.002 . 1 . . . A 61 LYS HE2 . 18387 1 754 . 1 1 61 61 LYS HE3 H 1 3.119 0.002 . 1 . . . A 61 LYS HE3 . 18387 1 755 . 1 1 61 61 LYS C C 13 175.968 0.000 . 1 . . . A 61 LYS C . 18387 1 756 . 1 1 61 61 LYS CA C 13 55.137 0.008 . 1 . . . A 61 LYS CA . 18387 1 757 . 1 1 61 61 LYS CB C 13 33.078 0.010 . 1 . . . A 61 LYS CB . 18387 1 758 . 1 1 61 61 LYS CG C 13 25.385 0.006 . 1 . . . A 61 LYS CG . 18387 1 759 . 1 1 61 61 LYS CD C 13 29.540 0.015 . 1 . . . A 61 LYS CD . 18387 1 760 . 1 1 61 61 LYS CE C 13 42.295 0.007 . 1 . . . A 61 LYS CE . 18387 1 761 . 1 1 61 61 LYS N N 15 121.021 0.010 . 1 . . . A 61 LYS N . 18387 1 762 . 1 1 62 62 GLY HA2 H 1 4.360 0.001 . 2 . . . A 62 GLY HA2 . 18387 1 763 . 1 1 62 62 GLY HA3 H 1 3.908 0.001 . 2 . . . A 62 GLY HA3 . 18387 1 764 . 1 1 62 62 GLY C C 13 173.837 0.000 . 1 . . . A 62 GLY C . 18387 1 765 . 1 1 62 62 GLY CA C 13 47.050 0.014 . 1 . . . A 62 GLY CA . 18387 1 766 . 1 1 63 63 PHE H H 1 7.413 0.002 . 1 . . . A 63 PHE H . 18387 1 767 . 1 1 63 63 PHE HA H 1 6.033 0.002 . 1 . . . A 63 PHE HA . 18387 1 768 . 1 1 63 63 PHE HB2 H 1 2.896 0.004 . 1 . . . A 63 PHE HB2 . 18387 1 769 . 1 1 63 63 PHE HB3 H 1 2.896 0.004 . 1 . . . A 63 PHE HB3 . 18387 1 770 . 1 1 63 63 PHE HD1 H 1 6.817 0.004 . 3 . . . A 63 PHE HD1 . 18387 1 771 . 1 1 63 63 PHE HD2 H 1 6.817 0.004 . 3 . . . A 63 PHE HD2 . 18387 1 772 . 1 1 63 63 PHE HE1 H 1 6.934 0.004 . 3 . . . A 63 PHE HE1 . 18387 1 773 . 1 1 63 63 PHE HE2 H 1 6.934 0.004 . 3 . . . A 63 PHE HE2 . 18387 1 774 . 1 1 63 63 PHE HZ H 1 6.805 0.003 . 1 . . . A 63 PHE HZ . 18387 1 775 . 1 1 63 63 PHE C C 13 173.613 0.014 . 1 . . . A 63 PHE C . 18387 1 776 . 1 1 63 63 PHE CA C 13 55.850 0.011 . 1 . . . A 63 PHE CA . 18387 1 777 . 1 1 63 63 PHE CB C 13 42.675 0.016 . 1 . . . A 63 PHE CB . 18387 1 778 . 1 1 63 63 PHE CD1 C 13 131.641 0.000 . 3 . . . A 63 PHE CD1 . 18387 1 779 . 1 1 63 63 PHE CD2 C 13 131.641 0.000 . 3 . . . A 63 PHE CD2 . 18387 1 780 . 1 1 63 63 PHE CE1 C 13 131.384 0.015 . 3 . . . A 63 PHE CE1 . 18387 1 781 . 1 1 63 63 PHE CE2 C 13 131.384 0.015 . 3 . . . A 63 PHE CE2 . 18387 1 782 . 1 1 63 63 PHE CZ C 13 129.792 0.025 . 1 . . . A 63 PHE CZ . 18387 1 783 . 1 1 63 63 PHE N N 15 120.476 0.020 . 1 . . . A 63 PHE N . 18387 1 784 . 1 1 64 64 THR H H 1 7.665 0.003 . 1 . . . A 64 THR H . 18387 1 785 . 1 1 64 64 THR HA H 1 4.097 0.002 . 1 . . . A 64 THR HA . 18387 1 786 . 1 1 64 64 THR HB H 1 3.982 0.000 . 1 . . . A 64 THR HB . 18387 1 787 . 1 1 64 64 THR HG21 H 1 0.510 0.003 . 1 . . . A 64 THR HG21 . 18387 1 788 . 1 1 64 64 THR HG22 H 1 0.510 0.003 . 1 . . . A 64 THR HG22 . 18387 1 789 . 1 1 64 64 THR HG23 H 1 0.510 0.003 . 1 . . . A 64 THR HG23 . 18387 1 790 . 1 1 64 64 THR C C 13 170.397 0.004 . 1 . . . A 64 THR C . 18387 1 791 . 1 1 64 64 THR CA C 13 60.261 0.020 . 1 . . . A 64 THR CA . 18387 1 792 . 1 1 64 64 THR CB C 13 69.507 0.020 . 1 . . . A 64 THR CB . 18387 1 793 . 1 1 64 64 THR CG2 C 13 18.405 0.008 . 1 . . . A 64 THR CG2 . 18387 1 794 . 1 1 64 64 THR N N 15 119.903 0.022 . 1 . . . A 64 THR N . 18387 1 795 . 1 1 65 65 ILE H H 1 7.321 0.001 . 1 . . . A 65 ILE H . 18387 1 796 . 1 1 65 65 ILE HA H 1 4.476 0.003 . 1 . . . A 65 ILE HA . 18387 1 797 . 1 1 65 65 ILE HB H 1 0.432 0.005 . 1 . . . A 65 ILE HB . 18387 1 798 . 1 1 65 65 ILE HG12 H 1 0.686 0.002 . 2 . . . A 65 ILE HG12 . 18387 1 799 . 1 1 65 65 ILE HG13 H 1 1.316 0.004 . 2 . . . A 65 ILE HG13 . 18387 1 800 . 1 1 65 65 ILE HG21 H 1 -0.164 0.003 . 1 . . . A 65 ILE HG21 . 18387 1 801 . 1 1 65 65 ILE HG22 H 1 -0.164 0.003 . 1 . . . A 65 ILE HG22 . 18387 1 802 . 1 1 65 65 ILE HG23 H 1 -0.164 0.003 . 1 . . . A 65 ILE HG23 . 18387 1 803 . 1 1 65 65 ILE HD11 H 1 -0.021 0.003 . 1 . . . A 65 ILE HD11 . 18387 1 804 . 1 1 65 65 ILE HD12 H 1 -0.021 0.003 . 1 . . . A 65 ILE HD12 . 18387 1 805 . 1 1 65 65 ILE HD13 H 1 -0.021 0.003 . 1 . . . A 65 ILE HD13 . 18387 1 806 . 1 1 65 65 ILE C C 13 173.056 0.004 . 1 . . . A 65 ILE C . 18387 1 807 . 1 1 65 65 ILE CA C 13 59.708 0.012 . 1 . . . A 65 ILE CA . 18387 1 808 . 1 1 65 65 ILE CB C 13 39.845 0.011 . 1 . . . A 65 ILE CB . 18387 1 809 . 1 1 65 65 ILE CG1 C 13 28.040 0.006 . 1 . . . A 65 ILE CG1 . 18387 1 810 . 1 1 65 65 ILE CG2 C 13 14.821 0.007 . 1 . . . A 65 ILE CG2 . 18387 1 811 . 1 1 65 65 ILE CD1 C 13 14.605 0.002 . 1 . . . A 65 ILE CD1 . 18387 1 812 . 1 1 65 65 ILE N N 15 117.277 0.030 . 1 . . . A 65 ILE N . 18387 1 813 . 1 1 66 66 TYR H H 1 9.038 0.002 . 1 . . . A 66 TYR H . 18387 1 814 . 1 1 66 66 TYR HA H 1 5.247 0.003 . 1 . . . A 66 TYR HA . 18387 1 815 . 1 1 66 66 TYR HB2 H 1 2.041 0.003 . 2 . . . A 66 TYR HB2 . 18387 1 816 . 1 1 66 66 TYR HB3 H 1 2.683 0.003 . 2 . . . A 66 TYR HB3 . 18387 1 817 . 1 1 66 66 TYR HD1 H 1 6.799 0.002 . 3 . . . A 66 TYR HD1 . 18387 1 818 . 1 1 66 66 TYR HD2 H 1 6.799 0.002 . 3 . . . A 66 TYR HD2 . 18387 1 819 . 1 1 66 66 TYR HE1 H 1 6.429 0.002 . 3 . . . A 66 TYR HE1 . 18387 1 820 . 1 1 66 66 TYR HE2 H 1 6.429 0.002 . 3 . . . A 66 TYR HE2 . 18387 1 821 . 1 1 66 66 TYR C C 13 174.074 0.012 . 1 . . . A 66 TYR C . 18387 1 822 . 1 1 66 66 TYR CA C 13 54.965 0.014 . 1 . . . A 66 TYR CA . 18387 1 823 . 1 1 66 66 TYR CB C 13 41.117 0.014 . 1 . . . A 66 TYR CB . 18387 1 824 . 1 1 66 66 TYR CD1 C 13 132.881 0.020 . 3 . . . A 66 TYR CD1 . 18387 1 825 . 1 1 66 66 TYR CD2 C 13 132.881 0.020 . 3 . . . A 66 TYR CD2 . 18387 1 826 . 1 1 66 66 TYR CE1 C 13 117.973 0.025 . 3 . . . A 66 TYR CE1 . 18387 1 827 . 1 1 66 66 TYR CE2 C 13 117.973 0.025 . 3 . . . A 66 TYR CE2 . 18387 1 828 . 1 1 66 66 TYR N N 15 131.968 0.010 . 1 . . . A 66 TYR N . 18387 1 829 . 1 1 67 67 GLY H H 1 9.188 0.001 . 1 . . . A 67 GLY H . 18387 1 830 . 1 1 67 67 GLY HA2 H 1 4.732 0.003 . 2 . . . A 67 GLY HA2 . 18387 1 831 . 1 1 67 67 GLY HA3 H 1 4.260 0.003 . 2 . . . A 67 GLY HA3 . 18387 1 832 . 1 1 67 67 GLY C C 13 172.461 0.002 . 1 . . . A 67 GLY C . 18387 1 833 . 1 1 67 67 GLY CA C 13 45.000 0.018 . 1 . . . A 67 GLY CA . 18387 1 834 . 1 1 67 67 GLY N N 15 114.364 0.003 . 1 . . . A 67 GLY N . 18387 1 835 . 1 1 68 68 VAL H H 1 9.309 0.003 . 1 . . . A 68 VAL H . 18387 1 836 . 1 1 68 68 VAL HA H 1 4.136 0.002 . 1 . . . A 68 VAL HA . 18387 1 837 . 1 1 68 68 VAL HB H 1 1.521 0.001 . 1 . . . A 68 VAL HB . 18387 1 838 . 1 1 68 68 VAL HG11 H 1 0.094 0.002 . 2 . . . A 68 VAL HG11 . 18387 1 839 . 1 1 68 68 VAL HG12 H 1 0.094 0.002 . 2 . . . A 68 VAL HG12 . 18387 1 840 . 1 1 68 68 VAL HG13 H 1 0.094 0.002 . 2 . . . A 68 VAL HG13 . 18387 1 841 . 1 1 68 68 VAL HG21 H 1 0.681 0.003 . 2 . . . A 68 VAL HG21 . 18387 1 842 . 1 1 68 68 VAL HG22 H 1 0.681 0.003 . 2 . . . A 68 VAL HG22 . 18387 1 843 . 1 1 68 68 VAL HG23 H 1 0.681 0.003 . 2 . . . A 68 VAL HG23 . 18387 1 844 . 1 1 68 68 VAL C C 13 173.822 0.010 . 1 . . . A 68 VAL C . 18387 1 845 . 1 1 68 68 VAL CA C 13 61.498 0.014 . 1 . . . A 68 VAL CA . 18387 1 846 . 1 1 68 68 VAL CB C 13 33.558 0.011 . 1 . . . A 68 VAL CB . 18387 1 847 . 1 1 68 68 VAL CG1 C 13 21.401 0.004 . 2 . . . A 68 VAL CG1 . 18387 1 848 . 1 1 68 68 VAL CG2 C 13 22.448 0.005 . 2 . . . A 68 VAL CG2 . 18387 1 849 . 1 1 68 68 VAL N N 15 126.938 0.033 . 1 . . . A 68 VAL N . 18387 1 850 . 1 1 69 69 SER H H 1 8.124 0.001 . 1 . . . A 69 SER H . 18387 1 851 . 1 1 69 69 SER HA H 1 5.527 0.005 . 1 . . . A 69 SER HA . 18387 1 852 . 1 1 69 69 SER HB2 H 1 3.109 0.002 . 1 . . . A 69 SER HB2 . 18387 1 853 . 1 1 69 69 SER HB3 H 1 3.109 0.002 . 1 . . . A 69 SER HB3 . 18387 1 854 . 1 1 69 69 SER C C 13 175.753 0.020 . 1 . . . A 69 SER C . 18387 1 855 . 1 1 69 69 SER CA C 13 54.407 0.012 . 1 . . . A 69 SER CA . 18387 1 856 . 1 1 69 69 SER CB C 13 63.630 0.022 . 1 . . . A 69 SER CB . 18387 1 857 . 1 1 69 69 SER N N 15 118.813 0.025 . 1 . . . A 69 SER N . 18387 1 858 . 1 1 70 70 THR H H 1 7.656 0.001 . 1 . . . A 70 THR H . 18387 1 859 . 1 1 70 70 THR HA H 1 4.381 0.002 . 1 . . . A 70 THR HA . 18387 1 860 . 1 1 70 70 THR HB H 1 4.409 0.003 . 1 . . . A 70 THR HB . 18387 1 861 . 1 1 70 70 THR HG21 H 1 1.256 0.003 . 1 . . . A 70 THR HG21 . 18387 1 862 . 1 1 70 70 THR HG22 H 1 1.256 0.003 . 1 . . . A 70 THR HG22 . 18387 1 863 . 1 1 70 70 THR HG23 H 1 1.256 0.003 . 1 . . . A 70 THR HG23 . 18387 1 864 . 1 1 70 70 THR C C 13 175.001 0.013 . 1 . . . A 70 THR C . 18387 1 865 . 1 1 70 70 THR CA C 13 60.259 0.020 . 1 . . . A 70 THR CA . 18387 1 866 . 1 1 70 70 THR CB C 13 67.291 0.021 . 1 . . . A 70 THR CB . 18387 1 867 . 1 1 70 70 THR CG2 C 13 22.614 0.006 . 1 . . . A 70 THR CG2 . 18387 1 868 . 1 1 70 70 THR N N 15 113.861 0.008 . 1 . . . A 70 THR N . 18387 1 869 . 1 1 71 71 ASP H H 1 8.931 0.001 . 1 . . . A 71 ASP H . 18387 1 870 . 1 1 71 71 ASP HA H 1 4.070 0.002 . 1 . . . A 71 ASP HA . 18387 1 871 . 1 1 71 71 ASP HB2 H 1 2.116 0.003 . 2 . . . A 71 ASP HB2 . 18387 1 872 . 1 1 71 71 ASP HB3 H 1 2.357 0.002 . 2 . . . A 71 ASP HB3 . 18387 1 873 . 1 1 71 71 ASP C C 13 175.685 0.004 . 1 . . . A 71 ASP C . 18387 1 874 . 1 1 71 71 ASP CA C 13 57.612 0.018 . 1 . . . A 71 ASP CA . 18387 1 875 . 1 1 71 71 ASP CB C 13 42.369 0.006 . 1 . . . A 71 ASP CB . 18387 1 876 . 1 1 71 71 ASP N N 15 125.133 0.010 . 1 . . . A 71 ASP N . 18387 1 877 . 1 1 72 72 ARG H H 1 8.057 0.001 . 1 . . . A 72 ARG H . 18387 1 878 . 1 1 72 72 ARG HA H 1 4.195 0.002 . 1 . . . A 72 ARG HA . 18387 1 879 . 1 1 72 72 ARG HB2 H 1 1.822 0.001 . 2 . . . A 72 ARG HB2 . 18387 1 880 . 1 1 72 72 ARG HB3 H 1 1.897 0.001 . 2 . . . A 72 ARG HB3 . 18387 1 881 . 1 1 72 72 ARG HG2 H 1 1.730 0.001 . 1 . . . A 72 ARG HG2 . 18387 1 882 . 1 1 72 72 ARG HG3 H 1 1.730 0.000 . 1 . . . A 72 ARG HG3 . 18387 1 883 . 1 1 72 72 ARG HD2 H 1 3.226 0.001 . 1 . . . A 72 ARG HD2 . 18387 1 884 . 1 1 72 72 ARG HD3 H 1 3.226 0.001 . 1 . . . A 72 ARG HD3 . 18387 1 885 . 1 1 72 72 ARG C C 13 177.300 0.007 . 1 . . . A 72 ARG C . 18387 1 886 . 1 1 72 72 ARG CA C 13 56.809 0.022 . 1 . . . A 72 ARG CA . 18387 1 887 . 1 1 72 72 ARG CB C 13 31.111 0.010 . 1 . . . A 72 ARG CB . 18387 1 888 . 1 1 72 72 ARG CG C 13 27.641 0.004 . 1 . . . A 72 ARG CG . 18387 1 889 . 1 1 72 72 ARG CD C 13 43.189 0.006 . 1 . . . A 72 ARG CD . 18387 1 890 . 1 1 72 72 ARG N N 15 118.814 0.028 . 1 . . . A 72 ARG N . 18387 1 891 . 1 1 73 73 ARG H H 1 8.639 0.001 . 1 . . . A 73 ARG H . 18387 1 892 . 1 1 73 73 ARG HA H 1 4.754 0.001 . 1 . . . A 73 ARG HA . 18387 1 893 . 1 1 73 73 ARG HB2 H 1 1.935 0.001 . 1 . . . A 73 ARG HB2 . 18387 1 894 . 1 1 73 73 ARG HB3 H 1 1.935 0.002 . 1 . . . A 73 ARG HB3 . 18387 1 895 . 1 1 73 73 ARG HG2 H 1 1.619 0.001 . 1 . . . A 73 ARG HG2 . 18387 1 896 . 1 1 73 73 ARG HG3 H 1 1.619 0.001 . 1 . . . A 73 ARG HG3 . 18387 1 897 . 1 1 73 73 ARG HD2 H 1 3.291 0.000 . 1 . . . A 73 ARG HD2 . 18387 1 898 . 1 1 73 73 ARG HD3 H 1 3.291 0.000 . 1 . . . A 73 ARG HD3 . 18387 1 899 . 1 1 73 73 ARG C C 13 176.503 0.000 . 1 . . . A 73 ARG C . 18387 1 900 . 1 1 73 73 ARG CA C 13 54.536 0.021 . 1 . . . A 73 ARG CA . 18387 1 901 . 1 1 73 73 ARG CB C 13 31.028 0.012 . 1 . . . A 73 ARG CB . 18387 1 902 . 1 1 73 73 ARG CG C 13 27.060 0.003 . 1 . . . A 73 ARG CG . 18387 1 903 . 1 1 73 73 ARG CD C 13 43.339 0.006 . 1 . . . A 73 ARG CD . 18387 1 904 . 1 1 73 73 ARG N N 15 118.174 0.011 . 1 . . . A 73 ARG N . 18387 1 905 . 1 1 74 74 GLU H H 1 9.129 0.001 . 1 . . . A 74 GLU H . 18387 1 906 . 1 1 74 74 GLU HA H 1 4.079 0.003 . 1 . . . A 74 GLU HA . 18387 1 907 . 1 1 74 74 GLU HB2 H 1 2.098 0.001 . 2 . . . A 74 GLU HB2 . 18387 1 908 . 1 1 74 74 GLU HB3 H 1 2.236 0.002 . 2 . . . A 74 GLU HB3 . 18387 1 909 . 1 1 74 74 GLU HG2 H 1 2.399 0.003 . 2 . . . A 74 GLU HG2 . 18387 1 910 . 1 1 74 74 GLU HG3 H 1 2.457 0.001 . 2 . . . A 74 GLU HG3 . 18387 1 911 . 1 1 74 74 GLU C C 13 178.107 0.006 . 1 . . . A 74 GLU C . 18387 1 912 . 1 1 74 74 GLU CA C 13 59.785 0.008 . 1 . . . A 74 GLU CA . 18387 1 913 . 1 1 74 74 GLU CB C 13 30.098 0.011 . 1 . . . A 74 GLU CB . 18387 1 914 . 1 1 74 74 GLU CG C 13 36.559 0.008 . 1 . . . A 74 GLU CG . 18387 1 915 . 1 1 74 74 GLU N N 15 127.609 0.022 . 1 . . . A 74 GLU N . 18387 1 916 . 1 1 75 75 GLU H H 1 9.745 0.000 . 1 . . . A 75 GLU H . 18387 1 917 . 1 1 75 75 GLU HA H 1 4.100 0.001 . 1 . . . A 75 GLU HA . 18387 1 918 . 1 1 75 75 GLU HB2 H 1 2.032 0.002 . 1 . . . A 75 GLU HB2 . 18387 1 919 . 1 1 75 75 GLU HB3 H 1 2.032 0.002 . 1 . . . A 75 GLU HB3 . 18387 1 920 . 1 1 75 75 GLU HG2 H 1 2.384 0.001 . 1 . . . A 75 GLU HG2 . 18387 1 921 . 1 1 75 75 GLU HG3 H 1 2.384 0.001 . 1 . . . A 75 GLU HG3 . 18387 1 922 . 1 1 75 75 GLU C C 13 178.993 0.004 . 1 . . . A 75 GLU C . 18387 1 923 . 1 1 75 75 GLU CA C 13 60.127 0.011 . 1 . . . A 75 GLU CA . 18387 1 924 . 1 1 75 75 GLU CB C 13 29.291 0.022 . 1 . . . A 75 GLU CB . 18387 1 925 . 1 1 75 75 GLU CG C 13 36.597 0.001 . 1 . . . A 75 GLU CG . 18387 1 926 . 1 1 75 75 GLU N N 15 117.874 0.003 . 1 . . . A 75 GLU N . 18387 1 927 . 1 1 76 76 ASP H H 1 7.004 0.002 . 1 . . . A 76 ASP H . 18387 1 928 . 1 1 76 76 ASP HA H 1 4.366 0.001 . 1 . . . A 76 ASP HA . 18387 1 929 . 1 1 76 76 ASP HB2 H 1 2.596 0.001 . 2 . . . A 76 ASP HB2 . 18387 1 930 . 1 1 76 76 ASP HB3 H 1 2.932 0.002 . 2 . . . A 76 ASP HB3 . 18387 1 931 . 1 1 76 76 ASP C C 13 178.107 0.002 . 1 . . . A 76 ASP C . 18387 1 932 . 1 1 76 76 ASP CA C 13 56.973 0.017 . 1 . . . A 76 ASP CA . 18387 1 933 . 1 1 76 76 ASP CB C 13 40.520 0.012 . 1 . . . A 76 ASP CB . 18387 1 934 . 1 1 76 76 ASP N N 15 119.182 0.011 . 1 . . . A 76 ASP N . 18387 1 935 . 1 1 77 77 TRP H H 1 7.112 0.002 . 1 . . . A 77 TRP H . 18387 1 936 . 1 1 77 77 TRP HA H 1 4.149 0.003 . 1 . . . A 77 TRP HA . 18387 1 937 . 1 1 77 77 TRP HB2 H 1 3.030 0.003 . 2 . . . A 77 TRP HB2 . 18387 1 938 . 1 1 77 77 TRP HB3 H 1 3.645 0.003 . 2 . . . A 77 TRP HB3 . 18387 1 939 . 1 1 77 77 TRP HD1 H 1 6.876 0.002 . 1 . . . A 77 TRP HD1 . 18387 1 940 . 1 1 77 77 TRP HE1 H 1 11.170 0.001 . 1 . . . A 77 TRP HE1 . 18387 1 941 . 1 1 77 77 TRP HE3 H 1 7.657 0.003 . 1 . . . A 77 TRP HE3 . 18387 1 942 . 1 1 77 77 TRP HZ2 H 1 6.831 0.003 . 1 . . . A 77 TRP HZ2 . 18387 1 943 . 1 1 77 77 TRP HZ3 H 1 7.013 0.002 . 1 . . . A 77 TRP HZ3 . 18387 1 944 . 1 1 77 77 TRP HH2 H 1 6.943 0.002 . 1 . . . A 77 TRP HH2 . 18387 1 945 . 1 1 77 77 TRP C C 13 176.236 0.004 . 1 . . . A 77 TRP C . 18387 1 946 . 1 1 77 77 TRP CA C 13 60.483 0.015 . 1 . . . A 77 TRP CA . 18387 1 947 . 1 1 77 77 TRP CB C 13 28.535 0.013 . 1 . . . A 77 TRP CB . 18387 1 948 . 1 1 77 77 TRP CD1 C 13 126.552 0.029 . 1 . . . A 77 TRP CD1 . 18387 1 949 . 1 1 77 77 TRP CE3 C 13 121.124 0.025 . 1 . . . A 77 TRP CE3 . 18387 1 950 . 1 1 77 77 TRP CZ2 C 13 113.897 0.020 . 1 . . . A 77 TRP CZ2 . 18387 1 951 . 1 1 77 77 TRP CZ3 C 13 121.829 0.025 . 1 . . . A 77 TRP CZ3 . 18387 1 952 . 1 1 77 77 TRP CH2 C 13 125.313 0.022 . 1 . . . A 77 TRP CH2 . 18387 1 953 . 1 1 77 77 TRP N N 15 123.008 0.013 . 1 . . . A 77 TRP N . 18387 1 954 . 1 1 77 77 TRP NE1 N 15 133.176 0.003 . 1 . . . A 77 TRP NE1 . 18387 1 955 . 1 1 78 78 LYS H H 1 8.431 0.001 . 1 . . . A 78 LYS H . 18387 1 956 . 1 1 78 78 LYS HA H 1 3.245 0.002 . 1 . . . A 78 LYS HA . 18387 1 957 . 1 1 78 78 LYS HB2 H 1 1.721 0.002 . 1 . . . A 78 LYS HB2 . 18387 1 958 . 1 1 78 78 LYS HB3 H 1 1.721 0.003 . 1 . . . A 78 LYS HB3 . 18387 1 959 . 1 1 78 78 LYS HG2 H 1 1.045 0.002 . 1 . . . A 78 LYS HG2 . 18387 1 960 . 1 1 78 78 LYS HG3 H 1 1.045 0.002 . 1 . . . A 78 LYS HG3 . 18387 1 961 . 1 1 78 78 LYS HD2 H 1 1.704 0.002 . 1 . . . A 78 LYS HD2 . 18387 1 962 . 1 1 78 78 LYS HD3 H 1 1.705 0.003 . 1 . . . A 78 LYS HD3 . 18387 1 963 . 1 1 78 78 LYS HE2 H 1 3.001 0.004 . 2 . . . A 78 LYS HE2 . 18387 1 964 . 1 1 78 78 LYS HE3 H 1 3.040 0.003 . 2 . . . A 78 LYS HE3 . 18387 1 965 . 1 1 78 78 LYS C C 13 179.426 0.001 . 1 . . . A 78 LYS C . 18387 1 966 . 1 1 78 78 LYS CA C 13 60.432 0.014 . 1 . . . A 78 LYS CA . 18387 1 967 . 1 1 78 78 LYS CB C 13 32.745 0.013 . 1 . . . A 78 LYS CB . 18387 1 968 . 1 1 78 78 LYS CG C 13 27.318 0.003 . 1 . . . A 78 LYS CG . 18387 1 969 . 1 1 78 78 LYS CD C 13 29.762 0.006 . 1 . . . A 78 LYS CD . 18387 1 970 . 1 1 78 78 LYS CE C 13 42.394 0.013 . 1 . . . A 78 LYS CE . 18387 1 971 . 1 1 78 78 LYS N N 15 115.727 0.026 . 1 . . . A 78 LYS N . 18387 1 972 . 1 1 79 79 LYS H H 1 7.690 0.001 . 1 . . . A 79 LYS H . 18387 1 973 . 1 1 79 79 LYS HA H 1 4.020 0.001 . 1 . . . A 79 LYS HA . 18387 1 974 . 1 1 79 79 LYS HB2 H 1 1.891 0.004 . 2 . . . A 79 LYS HB2 . 18387 1 975 . 1 1 79 79 LYS HB3 H 1 1.939 0.002 . 2 . . . A 79 LYS HB3 . 18387 1 976 . 1 1 79 79 LYS HG2 H 1 1.389 0.001 . 2 . . . A 79 LYS HG2 . 18387 1 977 . 1 1 79 79 LYS HG3 H 1 1.530 0.001 . 2 . . . A 79 LYS HG3 . 18387 1 978 . 1 1 79 79 LYS HD2 H 1 1.724 0.000 . 1 . . . A 79 LYS HD2 . 18387 1 979 . 1 1 79 79 LYS HD3 H 1 1.724 0.002 . 1 . . . A 79 LYS HD3 . 18387 1 980 . 1 1 79 79 LYS HE2 H 1 2.994 0.002 . 1 . . . A 79 LYS HE2 . 18387 1 981 . 1 1 79 79 LYS HE3 H 1 2.994 0.002 . 1 . . . A 79 LYS HE3 . 18387 1 982 . 1 1 79 79 LYS C C 13 178.239 0.005 . 1 . . . A 79 LYS C . 18387 1 983 . 1 1 79 79 LYS CA C 13 59.067 0.018 . 1 . . . A 79 LYS CA . 18387 1 984 . 1 1 79 79 LYS CB C 13 32.463 0.021 . 1 . . . A 79 LYS CB . 18387 1 985 . 1 1 79 79 LYS CG C 13 24.907 0.015 . 1 . . . A 79 LYS CG . 18387 1 986 . 1 1 79 79 LYS CD C 13 29.300 0.000 . 1 . . . A 79 LYS CD . 18387 1 987 . 1 1 79 79 LYS CE C 13 41.962 0.000 . 1 . . . A 79 LYS CE . 18387 1 988 . 1 1 79 79 LYS N N 15 118.321 0.021 . 1 . . . A 79 LYS N . 18387 1 989 . 1 1 80 80 ALA H H 1 7.560 0.001 . 1 . . . A 80 ALA H . 18387 1 990 . 1 1 80 80 ALA HA H 1 4.155 0.002 . 1 . . . A 80 ALA HA . 18387 1 991 . 1 1 80 80 ALA HB1 H 1 1.704 0.003 . 1 . . . A 80 ALA HB1 . 18387 1 992 . 1 1 80 80 ALA HB2 H 1 1.704 0.003 . 1 . . . A 80 ALA HB2 . 18387 1 993 . 1 1 80 80 ALA HB3 H 1 1.704 0.003 . 1 . . . A 80 ALA HB3 . 18387 1 994 . 1 1 80 80 ALA C C 13 178.811 0.008 . 1 . . . A 80 ALA C . 18387 1 995 . 1 1 80 80 ALA CA C 13 55.087 0.017 . 1 . . . A 80 ALA CA . 18387 1 996 . 1 1 80 80 ALA CB C 13 18.758 0.015 . 1 . . . A 80 ALA CB . 18387 1 997 . 1 1 80 80 ALA N N 15 120.679 0.013 . 1 . . . A 80 ALA N . 18387 1 998 . 1 1 81 81 ILE H H 1 7.514 0.001 . 1 . . . A 81 ILE H . 18387 1 999 . 1 1 81 81 ILE HA H 1 3.402 0.002 . 1 . . . A 81 ILE HA . 18387 1 1000 . 1 1 81 81 ILE HB H 1 1.243 0.002 . 1 . . . A 81 ILE HB . 18387 1 1001 . 1 1 81 81 ILE HG12 H 1 1.567 0.004 . 2 . . . A 81 ILE HG12 . 18387 1 1002 . 1 1 81 81 ILE HG13 H 1 0.601 0.003 . 2 . . . A 81 ILE HG13 . 18387 1 1003 . 1 1 81 81 ILE HG21 H 1 0.181 0.003 . 1 . . . A 81 ILE HG21 . 18387 1 1004 . 1 1 81 81 ILE HG22 H 1 0.181 0.003 . 1 . . . A 81 ILE HG22 . 18387 1 1005 . 1 1 81 81 ILE HG23 H 1 0.181 0.003 . 1 . . . A 81 ILE HG23 . 18387 1 1006 . 1 1 81 81 ILE HD11 H 1 -0.153 0.003 . 1 . . . A 81 ILE HD11 . 18387 1 1007 . 1 1 81 81 ILE HD12 H 1 -0.153 0.003 . 1 . . . A 81 ILE HD12 . 18387 1 1008 . 1 1 81 81 ILE HD13 H 1 -0.153 0.003 . 1 . . . A 81 ILE HD13 . 18387 1 1009 . 1 1 81 81 ILE C C 13 178.113 0.004 . 1 . . . A 81 ILE C . 18387 1 1010 . 1 1 81 81 ILE CA C 13 64.520 0.010 . 1 . . . A 81 ILE CA . 18387 1 1011 . 1 1 81 81 ILE CB C 13 38.204 0.027 . 1 . . . A 81 ILE CB . 18387 1 1012 . 1 1 81 81 ILE CG1 C 13 29.237 0.006 . 1 . . . A 81 ILE CG1 . 18387 1 1013 . 1 1 81 81 ILE CG2 C 13 16.050 0.002 . 1 . . . A 81 ILE CG2 . 18387 1 1014 . 1 1 81 81 ILE CD1 C 13 13.916 0.004 . 1 . . . A 81 ILE CD1 . 18387 1 1015 . 1 1 81 81 ILE N N 15 118.019 0.011 . 1 . . . A 81 ILE N . 18387 1 1016 . 1 1 82 82 GLU H H 1 7.401 0.001 . 1 . . . A 82 GLU H . 18387 1 1017 . 1 1 82 82 GLU HA H 1 4.094 0.002 . 1 . . . A 82 GLU HA . 18387 1 1018 . 1 1 82 82 GLU HB2 H 1 2.066 0.001 . 1 . . . A 82 GLU HB2 . 18387 1 1019 . 1 1 82 82 GLU HB3 H 1 2.066 0.001 . 1 . . . A 82 GLU HB3 . 18387 1 1020 . 1 1 82 82 GLU HG2 H 1 2.287 0.002 . 2 . . . A 82 GLU HG2 . 18387 1 1021 . 1 1 82 82 GLU HG3 H 1 2.316 0.001 . 2 . . . A 82 GLU HG3 . 18387 1 1022 . 1 1 82 82 GLU C C 13 179.558 0.001 . 1 . . . A 82 GLU C . 18387 1 1023 . 1 1 82 82 GLU CA C 13 58.580 0.014 . 1 . . . A 82 GLU CA . 18387 1 1024 . 1 1 82 82 GLU CB C 13 29.383 0.023 . 1 . . . A 82 GLU CB . 18387 1 1025 . 1 1 82 82 GLU CG C 13 36.097 0.019 . 1 . . . A 82 GLU CG . 18387 1 1026 . 1 1 82 82 GLU N N 15 117.252 0.033 . 1 . . . A 82 GLU N . 18387 1 1027 . 1 1 83 83 GLU H H 1 8.191 0.001 . 1 . . . A 83 GLU H . 18387 1 1028 . 1 1 83 83 GLU HA H 1 3.898 0.001 . 1 . . . A 83 GLU HA . 18387 1 1029 . 1 1 83 83 GLU HB2 H 1 1.862 0.002 . 2 . . . A 83 GLU HB2 . 18387 1 1030 . 1 1 83 83 GLU HB3 H 1 2.075 0.002 . 2 . . . A 83 GLU HB3 . 18387 1 1031 . 1 1 83 83 GLU HG2 H 1 2.225 0.001 . 2 . . . A 83 GLU HG2 . 18387 1 1032 . 1 1 83 83 GLU HG3 H 1 2.511 0.002 . 2 . . . A 83 GLU HG3 . 18387 1 1033 . 1 1 83 83 GLU C C 13 178.740 0.002 . 1 . . . A 83 GLU C . 18387 1 1034 . 1 1 83 83 GLU CA C 13 58.999 0.016 . 1 . . . A 83 GLU CA . 18387 1 1035 . 1 1 83 83 GLU CB C 13 29.920 0.010 . 1 . . . A 83 GLU CB . 18387 1 1036 . 1 1 83 83 GLU CG C 13 36.578 0.006 . 1 . . . A 83 GLU CG . 18387 1 1037 . 1 1 83 83 GLU N N 15 119.340 0.008 . 1 . . . A 83 GLU N . 18387 1 1038 . 1 1 84 84 ASP H H 1 8.252 0.001 . 1 . . . A 84 ASP H . 18387 1 1039 . 1 1 84 84 ASP HA H 1 4.274 0.002 . 1 . . . A 84 ASP HA . 18387 1 1040 . 1 1 84 84 ASP HB2 H 1 2.411 0.002 . 2 . . . A 84 ASP HB2 . 18387 1 1041 . 1 1 84 84 ASP HB3 H 1 2.596 0.002 . 2 . . . A 84 ASP HB3 . 18387 1 1042 . 1 1 84 84 ASP C C 13 175.597 0.005 . 1 . . . A 84 ASP C . 18387 1 1043 . 1 1 84 84 ASP CA C 13 55.047 0.020 . 1 . . . A 84 ASP CA . 18387 1 1044 . 1 1 84 84 ASP CB C 13 39.896 0.007 . 1 . . . A 84 ASP CB . 18387 1 1045 . 1 1 84 84 ASP N N 15 118.449 0.022 . 1 . . . A 84 ASP N . 18387 1 1046 . 1 1 85 85 LYS H H 1 7.890 0.001 . 1 . . . A 85 LYS H . 18387 1 1047 . 1 1 85 85 LYS HA H 1 3.173 0.002 . 1 . . . A 85 LYS HA . 18387 1 1048 . 1 1 85 85 LYS HB2 H 1 2.076 0.001 . 1 . . . A 85 LYS HB2 . 18387 1 1049 . 1 1 85 85 LYS HB3 H 1 2.076 0.002 . 1 . . . A 85 LYS HB3 . 18387 1 1050 . 1 1 85 85 LYS HG2 H 1 1.345 0.001 . 1 . . . A 85 LYS HG2 . 18387 1 1051 . 1 1 85 85 LYS HG3 H 1 1.345 0.002 . 1 . . . A 85 LYS HG3 . 18387 1 1052 . 1 1 85 85 LYS HD2 H 1 1.803 0.003 . 2 . . . A 85 LYS HD2 . 18387 1 1053 . 1 1 85 85 LYS HD3 H 1 1.662 0.001 . 2 . . . A 85 LYS HD3 . 18387 1 1054 . 1 1 85 85 LYS C C 13 176.856 0.032 . 1 . . . A 85 LYS C . 18387 1 1055 . 1 1 85 85 LYS CA C 13 55.973 0.026 . 1 . . . A 85 LYS CA . 18387 1 1056 . 1 1 85 85 LYS CB C 13 28.868 0.019 . 1 . . . A 85 LYS CB . 18387 1 1057 . 1 1 85 85 LYS CG C 13 24.764 0.001 . 1 . . . A 85 LYS CG . 18387 1 1058 . 1 1 85 85 LYS CD C 13 29.128 0.004 . 1 . . . A 85 LYS CD . 18387 1 1059 . 1 1 85 85 LYS N N 15 116.410 0.025 . 1 . . . A 85 LYS N . 18387 1 1060 . 1 1 86 86 SER H H 1 7.327 0.002 . 1 . . . A 86 SER H . 18387 1 1061 . 1 1 86 86 SER HA H 1 3.139 0.003 . 1 . . . A 86 SER HA . 18387 1 1062 . 1 1 86 86 SER HB2 H 1 1.946 0.003 . 2 . . . A 86 SER HB2 . 18387 1 1063 . 1 1 86 86 SER HB3 H 1 2.407 0.002 . 2 . . . A 86 SER HB3 . 18387 1 1064 . 1 1 86 86 SER C C 13 175.805 0.008 . 1 . . . A 86 SER C . 18387 1 1065 . 1 1 86 86 SER CA C 13 53.637 0.028 . 1 . . . A 86 SER CA . 18387 1 1066 . 1 1 86 86 SER CB C 13 60.736 0.013 . 1 . . . A 86 SER CB . 18387 1 1067 . 1 1 86 86 SER N N 15 112.295 0.010 . 1 . . . A 86 SER N . 18387 1 1068 . 1 1 87 87 TYR H H 1 6.933 0.001 . 1 . . . A 87 TYR H . 18387 1 1069 . 1 1 87 87 TYR HA H 1 4.305 0.003 . 1 . . . A 87 TYR HA . 18387 1 1070 . 1 1 87 87 TYR HB2 H 1 2.538 0.001 . 2 . . . A 87 TYR HB2 . 18387 1 1071 . 1 1 87 87 TYR HB3 H 1 3.310 0.003 . 2 . . . A 87 TYR HB3 . 18387 1 1072 . 1 1 87 87 TYR HD1 H 1 6.823 0.002 . 3 . . . A 87 TYR HD1 . 18387 1 1073 . 1 1 87 87 TYR HD2 H 1 6.823 0.002 . 3 . . . A 87 TYR HD2 . 18387 1 1074 . 1 1 87 87 TYR HE1 H 1 6.629 0.002 . 3 . . . A 87 TYR HE1 . 18387 1 1075 . 1 1 87 87 TYR HE2 H 1 6.629 0.002 . 3 . . . A 87 TYR HE2 . 18387 1 1076 . 1 1 87 87 TYR C C 13 177.064 0.003 . 1 . . . A 87 TYR C . 18387 1 1077 . 1 1 87 87 TYR CA C 13 57.223 0.015 . 1 . . . A 87 TYR CA . 18387 1 1078 . 1 1 87 87 TYR CB C 13 36.353 0.018 . 1 . . . A 87 TYR CB . 18387 1 1079 . 1 1 87 87 TYR CD1 C 13 132.337 0.022 . 3 . . . A 87 TYR CD1 . 18387 1 1080 . 1 1 87 87 TYR CD2 C 13 132.337 0.022 . 3 . . . A 87 TYR CD2 . 18387 1 1081 . 1 1 87 87 TYR CE1 C 13 118.254 0.020 . 3 . . . A 87 TYR CE1 . 18387 1 1082 . 1 1 87 87 TYR CE2 C 13 118.254 0.020 . 3 . . . A 87 TYR CE2 . 18387 1 1083 . 1 1 87 87 TYR N N 15 120.962 0.004 . 1 . . . A 87 TYR N . 18387 1 1084 . 1 1 88 88 TRP H H 1 6.552 0.001 . 1 . . . A 88 TRP H . 18387 1 1085 . 1 1 88 88 TRP HA H 1 4.851 0.001 . 1 . . . A 88 TRP HA . 18387 1 1086 . 1 1 88 88 TRP HB2 H 1 1.945 0.003 . 2 . . . A 88 TRP HB2 . 18387 1 1087 . 1 1 88 88 TRP HB3 H 1 2.927 0.002 . 2 . . . A 88 TRP HB3 . 18387 1 1088 . 1 1 88 88 TRP HD1 H 1 6.703 0.002 . 1 . . . A 88 TRP HD1 . 18387 1 1089 . 1 1 88 88 TRP HE1 H 1 9.588 0.001 . 1 . . . A 88 TRP HE1 . 18387 1 1090 . 1 1 88 88 TRP HE3 H 1 6.709 0.004 . 1 . . . A 88 TRP HE3 . 18387 1 1091 . 1 1 88 88 TRP HZ2 H 1 7.103 0.002 . 1 . . . A 88 TRP HZ2 . 18387 1 1092 . 1 1 88 88 TRP HZ3 H 1 6.629 0.004 . 1 . . . A 88 TRP HZ3 . 18387 1 1093 . 1 1 88 88 TRP HH2 H 1 6.796 0.003 . 1 . . . A 88 TRP HH2 . 18387 1 1094 . 1 1 88 88 TRP C C 13 175.456 0.005 . 1 . . . A 88 TRP C . 18387 1 1095 . 1 1 88 88 TRP CA C 13 56.236 0.012 . 1 . . . A 88 TRP CA . 18387 1 1096 . 1 1 88 88 TRP CB C 13 25.727 0.013 . 1 . . . A 88 TRP CB . 18387 1 1097 . 1 1 88 88 TRP CD1 C 13 125.646 0.036 . 1 . . . A 88 TRP CD1 . 18387 1 1098 . 1 1 88 88 TRP CE3 C 13 120.113 0.024 . 1 . . . A 88 TRP CE3 . 18387 1 1099 . 1 1 88 88 TRP CZ2 C 13 114.904 0.025 . 1 . . . A 88 TRP CZ2 . 18387 1 1100 . 1 1 88 88 TRP CZ3 C 13 120.873 0.034 . 1 . . . A 88 TRP CZ3 . 18387 1 1101 . 1 1 88 88 TRP CH2 C 13 125.362 0.028 . 1 . . . A 88 TRP CH2 . 18387 1 1102 . 1 1 88 88 TRP N N 15 118.597 0.007 . 1 . . . A 88 TRP N . 18387 1 1103 . 1 1 88 88 TRP NE1 N 15 132.159 0.010 . 1 . . . A 88 TRP NE1 . 18387 1 1104 . 1 1 89 89 ASN H H 1 7.864 0.002 . 1 . . . A 89 ASN H . 18387 1 1105 . 1 1 89 89 ASN HA H 1 5.049 0.002 . 1 . . . A 89 ASN HA . 18387 1 1106 . 1 1 89 89 ASN HB2 H 1 2.719 0.003 . 2 . . . A 89 ASN HB2 . 18387 1 1107 . 1 1 89 89 ASN HB3 H 1 3.334 0.001 . 2 . . . A 89 ASN HB3 . 18387 1 1108 . 1 1 89 89 ASN C C 13 173.773 0.003 . 1 . . . A 89 ASN C . 18387 1 1109 . 1 1 89 89 ASN CA C 13 55.456 0.027 . 1 . . . A 89 ASN CA . 18387 1 1110 . 1 1 89 89 ASN CB C 13 39.197 0.016 . 1 . . . A 89 ASN CB . 18387 1 1111 . 1 1 89 89 ASN N N 15 118.067 0.029 . 1 . . . A 89 ASN N . 18387 1 1112 . 1 1 90 90 GLN H H 1 7.904 0.001 . 1 . . . A 90 GLN H . 18387 1 1113 . 1 1 90 90 GLN HA H 1 5.497 0.003 . 1 . . . A 90 GLN HA . 18387 1 1114 . 1 1 90 90 GLN HB2 H 1 2.178 0.004 . 2 . . . A 90 GLN HB2 . 18387 1 1115 . 1 1 90 90 GLN HB3 H 1 1.916 0.005 . 2 . . . A 90 GLN HB3 . 18387 1 1116 . 1 1 90 90 GLN HE21 H 1 7.251 0.001 . 1 . . . A 90 GLN HE21 . 18387 1 1117 . 1 1 90 90 GLN HE22 H 1 5.354 0.001 . 1 . . . A 90 GLN HE22 . 18387 1 1118 . 1 1 90 90 GLN C C 13 176.491 0.005 . 1 . . . A 90 GLN C . 18387 1 1119 . 1 1 90 90 GLN CA C 13 55.460 0.014 . 1 . . . A 90 GLN CA . 18387 1 1120 . 1 1 90 90 GLN CB C 13 31.227 0.013 . 1 . . . A 90 GLN CB . 18387 1 1121 . 1 1 90 90 GLN N N 15 125.392 0.007 . 1 . . . A 90 GLN N . 18387 1 1122 . 1 1 90 90 GLN NE2 N 15 112.354 0.014 . 1 . . . A 90 GLN NE2 . 18387 1 1123 . 1 1 91 91 VAL H H 1 9.585 0.001 . 1 . . . A 91 VAL H . 18387 1 1124 . 1 1 91 91 VAL HA H 1 5.480 0.003 . 1 . . . A 91 VAL HA . 18387 1 1125 . 1 1 91 91 VAL HB H 1 1.790 0.002 . 1 . . . A 91 VAL HB . 18387 1 1126 . 1 1 91 91 VAL HG11 H 1 0.662 0.003 . 2 . . . A 91 VAL HG11 . 18387 1 1127 . 1 1 91 91 VAL HG12 H 1 0.662 0.003 . 2 . . . A 91 VAL HG12 . 18387 1 1128 . 1 1 91 91 VAL HG13 H 1 0.662 0.003 . 2 . . . A 91 VAL HG13 . 18387 1 1129 . 1 1 91 91 VAL HG21 H 1 0.963 0.004 . 2 . . . A 91 VAL HG21 . 18387 1 1130 . 1 1 91 91 VAL HG22 H 1 0.963 0.004 . 2 . . . A 91 VAL HG22 . 18387 1 1131 . 1 1 91 91 VAL HG23 H 1 0.963 0.004 . 2 . . . A 91 VAL HG23 . 18387 1 1132 . 1 1 91 91 VAL C C 13 174.248 0.028 . 1 . . . A 91 VAL C . 18387 1 1133 . 1 1 91 91 VAL CA C 13 59.006 0.025 . 1 . . . A 91 VAL CA . 18387 1 1134 . 1 1 91 91 VAL CB C 13 36.638 0.009 . 1 . . . A 91 VAL CB . 18387 1 1135 . 1 1 91 91 VAL CG1 C 13 17.515 0.004 . 2 . . . A 91 VAL CG1 . 18387 1 1136 . 1 1 91 91 VAL CG2 C 13 22.164 0.005 . 2 . . . A 91 VAL CG2 . 18387 1 1137 . 1 1 91 91 VAL N N 15 114.434 0.006 . 1 . . . A 91 VAL N . 18387 1 1138 . 1 1 92 92 LEU H H 1 8.941 0.002 . 1 . . . A 92 LEU H . 18387 1 1139 . 1 1 92 92 LEU HA H 1 4.069 0.003 . 1 . . . A 92 LEU HA . 18387 1 1140 . 1 1 92 92 LEU HB2 H 1 -1.332 0.002 . 2 . . . A 92 LEU HB2 . 18387 1 1141 . 1 1 92 92 LEU HB3 H 1 0.906 0.003 . 2 . . . A 92 LEU HB3 . 18387 1 1142 . 1 1 92 92 LEU HG H 1 0.867 0.002 . 1 . . . A 92 LEU HG . 18387 1 1143 . 1 1 92 92 LEU HD11 H 1 0.125 0.003 . 2 . . . A 92 LEU HD11 . 18387 1 1144 . 1 1 92 92 LEU HD12 H 1 0.125 0.003 . 2 . . . A 92 LEU HD12 . 18387 1 1145 . 1 1 92 92 LEU HD13 H 1 0.125 0.003 . 2 . . . A 92 LEU HD13 . 18387 1 1146 . 1 1 92 92 LEU HD21 H 1 0.333 0.002 . 2 . . . A 92 LEU HD21 . 18387 1 1147 . 1 1 92 92 LEU HD22 H 1 0.333 0.002 . 2 . . . A 92 LEU HD22 . 18387 1 1148 . 1 1 92 92 LEU HD23 H 1 0.333 0.002 . 2 . . . A 92 LEU HD23 . 18387 1 1149 . 1 1 92 92 LEU C C 13 177.696 0.007 . 1 . . . A 92 LEU C . 18387 1 1150 . 1 1 92 92 LEU CA C 13 52.844 0.016 . 1 . . . A 92 LEU CA . 18387 1 1151 . 1 1 92 92 LEU CB C 13 42.947 0.025 . 1 . . . A 92 LEU CB . 18387 1 1152 . 1 1 92 92 LEU CG C 13 25.731 0.009 . 1 . . . A 92 LEU CG . 18387 1 1153 . 1 1 92 92 LEU CD1 C 13 23.296 0.013 . 2 . . . A 92 LEU CD1 . 18387 1 1154 . 1 1 92 92 LEU CD2 C 13 26.117 0.007 . 2 . . . A 92 LEU CD2 . 18387 1 1155 . 1 1 92 92 LEU N N 15 126.910 0.014 . 1 . . . A 92 LEU N . 18387 1 1156 . 1 1 93 93 LEU H H 1 8.038 0.000 . 1 . . . A 93 LEU H . 18387 1 1157 . 1 1 93 93 LEU HA H 1 4.400 0.003 . 1 . . . A 93 LEU HA . 18387 1 1158 . 1 1 93 93 LEU HB2 H 1 1.288 0.002 . 2 . . . A 93 LEU HB2 . 18387 1 1159 . 1 1 93 93 LEU HB3 H 1 1.723 0.002 . 2 . . . A 93 LEU HB3 . 18387 1 1160 . 1 1 93 93 LEU HG H 1 1.621 0.001 . 1 . . . A 93 LEU HG . 18387 1 1161 . 1 1 93 93 LEU HD11 H 1 0.918 0.003 . 2 . . . A 93 LEU HD11 . 18387 1 1162 . 1 1 93 93 LEU HD12 H 1 0.918 0.003 . 2 . . . A 93 LEU HD12 . 18387 1 1163 . 1 1 93 93 LEU HD13 H 1 0.918 0.003 . 2 . . . A 93 LEU HD13 . 18387 1 1164 . 1 1 93 93 LEU HD21 H 1 0.873 0.001 . 2 . . . A 93 LEU HD21 . 18387 1 1165 . 1 1 93 93 LEU HD22 H 1 0.873 0.001 . 2 . . . A 93 LEU HD22 . 18387 1 1166 . 1 1 93 93 LEU HD23 H 1 0.873 0.001 . 2 . . . A 93 LEU HD23 . 18387 1 1167 . 1 1 93 93 LEU C C 13 177.291 0.010 . 1 . . . A 93 LEU C . 18387 1 1168 . 1 1 93 93 LEU CA C 13 54.951 0.023 . 1 . . . A 93 LEU CA . 18387 1 1169 . 1 1 93 93 LEU CB C 13 43.179 0.007 . 1 . . . A 93 LEU CB . 18387 1 1170 . 1 1 93 93 LEU CG C 13 26.884 0.000 . 1 . . . A 93 LEU CG . 18387 1 1171 . 1 1 93 93 LEU CD1 C 13 23.773 0.011 . 2 . . . A 93 LEU CD1 . 18387 1 1172 . 1 1 93 93 LEU CD2 C 13 26.931 0.005 . 2 . . . A 93 LEU CD2 . 18387 1 1173 . 1 1 93 93 LEU N N 15 125.673 0.005 . 1 . . . A 93 LEU N . 18387 1 1174 . 1 1 94 94 GLN H H 1 9.298 0.001 . 1 . . . A 94 GLN H . 18387 1 1175 . 1 1 94 94 GLN HA H 1 4.237 0.001 . 1 . . . A 94 GLN HA . 18387 1 1176 . 1 1 94 94 GLN HB2 H 1 2.006 0.001 . 2 . . . A 94 GLN HB2 . 18387 1 1177 . 1 1 94 94 GLN HB3 H 1 2.268 0.001 . 2 . . . A 94 GLN HB3 . 18387 1 1178 . 1 1 94 94 GLN HG2 H 1 2.403 0.003 . 2 . . . A 94 GLN HG2 . 18387 1 1179 . 1 1 94 94 GLN HG3 H 1 2.548 0.001 . 2 . . . A 94 GLN HG3 . 18387 1 1180 . 1 1 94 94 GLN HE21 H 1 6.968 0.001 . 1 . . . A 94 GLN HE21 . 18387 1 1181 . 1 1 94 94 GLN HE22 H 1 7.428 0.000 . 1 . . . A 94 GLN HE22 . 18387 1 1182 . 1 1 94 94 GLN C C 13 178.246 0.004 . 1 . . . A 94 GLN C . 18387 1 1183 . 1 1 94 94 GLN CA C 13 55.775 0.019 . 1 . . . A 94 GLN CA . 18387 1 1184 . 1 1 94 94 GLN CB C 13 29.255 0.013 . 1 . . . A 94 GLN CB . 18387 1 1185 . 1 1 94 94 GLN CG C 13 34.989 0.005 . 1 . . . A 94 GLN CG . 18387 1 1186 . 1 1 94 94 GLN N N 15 122.206 0.007 . 1 . . . A 94 GLN N . 18387 1 1187 . 1 1 94 94 GLN NE2 N 15 113.011 0.013 . 1 . . . A 94 GLN NE2 . 18387 1 1188 . 1 1 95 95 LYS H H 1 8.645 0.001 . 1 . . . A 95 LYS H . 18387 1 1189 . 1 1 95 95 LYS HA H 1 3.966 0.001 . 1 . . . A 95 LYS HA . 18387 1 1190 . 1 1 95 95 LYS HB2 H 1 1.832 0.002 . 2 . . . A 95 LYS HB2 . 18387 1 1191 . 1 1 95 95 LYS HB3 H 1 1.928 0.002 . 2 . . . A 95 LYS HB3 . 18387 1 1192 . 1 1 95 95 LYS HG2 H 1 1.461 0.002 . 2 . . . A 95 LYS HG2 . 18387 1 1193 . 1 1 95 95 LYS HG3 H 1 1.500 0.000 . 2 . . . A 95 LYS HG3 . 18387 1 1194 . 1 1 95 95 LYS HD2 H 1 1.717 0.001 . 1 . . . A 95 LYS HD2 . 18387 1 1195 . 1 1 95 95 LYS HD3 H 1 1.717 0.001 . 1 . . . A 95 LYS HD3 . 18387 1 1196 . 1 1 95 95 LYS HE2 H 1 3.045 0.000 . 1 . . . A 95 LYS HE2 . 18387 1 1197 . 1 1 95 95 LYS HE3 H 1 3.045 0.000 . 1 . . . A 95 LYS HE3 . 18387 1 1198 . 1 1 95 95 LYS C C 13 178.787 0.006 . 1 . . . A 95 LYS C . 18387 1 1199 . 1 1 95 95 LYS CA C 13 60.072 0.019 . 1 . . . A 95 LYS CA . 18387 1 1200 . 1 1 95 95 LYS CB C 13 32.465 0.013 . 1 . . . A 95 LYS CB . 18387 1 1201 . 1 1 95 95 LYS CG C 13 24.238 0.007 . 1 . . . A 95 LYS CG . 18387 1 1202 . 1 1 95 95 LYS CD C 13 29.342 0.000 . 1 . . . A 95 LYS CD . 18387 1 1203 . 1 1 95 95 LYS CE C 13 41.995 0.000 . 1 . . . A 95 LYS CE . 18387 1 1204 . 1 1 95 95 LYS N N 15 122.668 0.010 . 1 . . . A 95 LYS N . 18387 1 1205 . 1 1 96 96 ASP H H 1 8.606 0.001 . 1 . . . A 96 ASP H . 18387 1 1206 . 1 1 96 96 ASP HA H 1 4.580 0.001 . 1 . . . A 96 ASP HA . 18387 1 1207 . 1 1 96 96 ASP HB2 H 1 2.560 0.001 . 2 . . . A 96 ASP HB2 . 18387 1 1208 . 1 1 96 96 ASP HB3 H 1 2.863 0.001 . 2 . . . A 96 ASP HB3 . 18387 1 1209 . 1 1 96 96 ASP C C 13 176.220 0.001 . 1 . . . A 96 ASP C . 18387 1 1210 . 1 1 96 96 ASP CA C 13 56.346 0.005 . 1 . . . A 96 ASP CA . 18387 1 1211 . 1 1 96 96 ASP CB C 13 40.557 0.006 . 1 . . . A 96 ASP CB . 18387 1 1212 . 1 1 96 96 ASP N N 15 116.775 0.024 . 1 . . . A 96 ASP N . 18387 1 1213 . 1 1 97 97 ASP H H 1 7.988 0.001 . 1 . . . A 97 ASP H . 18387 1 1214 . 1 1 97 97 ASP HA H 1 4.927 0.002 . 1 . . . A 97 ASP HA . 18387 1 1215 . 1 1 97 97 ASP HB2 H 1 2.845 0.001 . 2 . . . A 97 ASP HB2 . 18387 1 1216 . 1 1 97 97 ASP HB3 H 1 2.937 0.001 . 2 . . . A 97 ASP HB3 . 18387 1 1217 . 1 1 97 97 ASP C C 13 176.954 0.002 . 1 . . . A 97 ASP C . 18387 1 1218 . 1 1 97 97 ASP CA C 13 55.359 0.019 . 1 . . . A 97 ASP CA . 18387 1 1219 . 1 1 97 97 ASP CB C 13 42.324 0.008 . 1 . . . A 97 ASP CB . 18387 1 1220 . 1 1 97 97 ASP N N 15 118.213 0.011 . 1 . . . A 97 ASP N . 18387 1 1221 . 1 1 98 98 VAL H H 1 7.098 0.001 . 1 . . . A 98 VAL H . 18387 1 1222 . 1 1 98 98 VAL HA H 1 3.416 0.003 . 1 . . . A 98 VAL HA . 18387 1 1223 . 1 1 98 98 VAL HB H 1 2.023 0.002 . 1 . . . A 98 VAL HB . 18387 1 1224 . 1 1 98 98 VAL HG11 H 1 0.944 0.003 . 2 . . . A 98 VAL HG11 . 18387 1 1225 . 1 1 98 98 VAL HG12 H 1 0.944 0.003 . 2 . . . A 98 VAL HG12 . 18387 1 1226 . 1 1 98 98 VAL HG13 H 1 0.944 0.003 . 2 . . . A 98 VAL HG13 . 18387 1 1227 . 1 1 98 98 VAL HG21 H 1 1.005 0.001 . 2 . . . A 98 VAL HG21 . 18387 1 1228 . 1 1 98 98 VAL HG22 H 1 1.005 0.001 . 2 . . . A 98 VAL HG22 . 18387 1 1229 . 1 1 98 98 VAL HG23 H 1 1.005 0.001 . 2 . . . A 98 VAL HG23 . 18387 1 1230 . 1 1 98 98 VAL C C 13 176.470 0.010 . 1 . . . A 98 VAL C . 18387 1 1231 . 1 1 98 98 VAL CA C 13 67.778 0.016 . 1 . . . A 98 VAL CA . 18387 1 1232 . 1 1 98 98 VAL CB C 13 32.391 0.016 . 1 . . . A 98 VAL CB . 18387 1 1233 . 1 1 98 98 VAL CG1 C 13 21.402 0.003 . 2 . . . A 98 VAL CG1 . 18387 1 1234 . 1 1 98 98 VAL CG2 C 13 23.454 0.005 . 2 . . . A 98 VAL CG2 . 18387 1 1235 . 1 1 98 98 VAL N N 15 118.907 0.005 . 1 . . . A 98 VAL N . 18387 1 1236 . 1 1 99 99 LYS H H 1 8.304 0.001 . 1 . . . A 99 LYS H . 18387 1 1237 . 1 1 99 99 LYS HA H 1 3.943 0.001 . 1 . . . A 99 LYS HA . 18387 1 1238 . 1 1 99 99 LYS HB2 H 1 1.857 0.002 . 1 . . . A 99 LYS HB2 . 18387 1 1239 . 1 1 99 99 LYS HB3 H 1 1.857 0.002 . 1 . . . A 99 LYS HB3 . 18387 1 1240 . 1 1 99 99 LYS HG2 H 1 1.401 0.003 . 2 . . . A 99 LYS HG2 . 18387 1 1241 . 1 1 99 99 LYS HG3 H 1 1.505 0.002 . 2 . . . A 99 LYS HG3 . 18387 1 1242 . 1 1 99 99 LYS HD2 H 1 1.695 0.001 . 1 . . . A 99 LYS HD2 . 18387 1 1243 . 1 1 99 99 LYS HD3 H 1 1.695 0.001 . 1 . . . A 99 LYS HD3 . 18387 1 1244 . 1 1 99 99 LYS HE2 H 1 3.008 0.001 . 1 . . . A 99 LYS HE2 . 18387 1 1245 . 1 1 99 99 LYS HE3 H 1 3.008 0.001 . 1 . . . A 99 LYS HE3 . 18387 1 1246 . 1 1 99 99 LYS C C 13 178.762 0.007 . 1 . . . A 99 LYS C . 18387 1 1247 . 1 1 99 99 LYS CA C 13 60.145 0.022 . 1 . . . A 99 LYS CA . 18387 1 1248 . 1 1 99 99 LYS CB C 13 32.012 0.025 . 1 . . . A 99 LYS CB . 18387 1 1249 . 1 1 99 99 LYS CG C 13 24.629 0.001 . 1 . . . A 99 LYS CG . 18387 1 1250 . 1 1 99 99 LYS CD C 13 29.427 0.000 . 1 . . . A 99 LYS CD . 18387 1 1251 . 1 1 99 99 LYS CE C 13 42.137 0.000 . 1 . . . A 99 LYS CE . 18387 1 1252 . 1 1 99 99 LYS N N 15 117.909 0.027 . 1 . . . A 99 LYS N . 18387 1 1253 . 1 1 100 100 ASP H H 1 8.024 0.000 . 1 . . . A 100 ASP H . 18387 1 1254 . 1 1 100 100 ASP HA H 1 4.478 0.001 . 1 . . . A 100 ASP HA . 18387 1 1255 . 1 1 100 100 ASP HB2 H 1 2.812 0.001 . 1 . . . A 100 ASP HB2 . 18387 1 1256 . 1 1 100 100 ASP HB3 H 1 2.812 0.001 . 1 . . . A 100 ASP HB3 . 18387 1 1257 . 1 1 100 100 ASP C C 13 179.694 0.014 . 1 . . . A 100 ASP C . 18387 1 1258 . 1 1 100 100 ASP CA C 13 57.526 0.016 . 1 . . . A 100 ASP CA . 18387 1 1259 . 1 1 100 100 ASP CB C 13 40.828 0.010 . 1 . . . A 100 ASP CB . 18387 1 1260 . 1 1 100 100 ASP N N 15 117.843 0.019 . 1 . . . A 100 ASP N . 18387 1 1261 . 1 1 101 101 VAL H H 1 8.205 0.002 . 1 . . . A 101 VAL H . 18387 1 1262 . 1 1 101 101 VAL HA H 1 3.995 0.003 . 1 . . . A 101 VAL HA . 18387 1 1263 . 1 1 101 101 VAL HB H 1 2.201 0.002 . 1 . . . A 101 VAL HB . 18387 1 1264 . 1 1 101 101 VAL HG11 H 1 1.132 0.005 . 2 . . . A 101 VAL HG11 . 18387 1 1265 . 1 1 101 101 VAL HG12 H 1 1.132 0.005 . 2 . . . A 101 VAL HG12 . 18387 1 1266 . 1 1 101 101 VAL HG13 H 1 1.132 0.005 . 2 . . . A 101 VAL HG13 . 18387 1 1267 . 1 1 101 101 VAL HG21 H 1 1.369 0.003 . 2 . . . A 101 VAL HG21 . 18387 1 1268 . 1 1 101 101 VAL HG22 H 1 1.369 0.003 . 2 . . . A 101 VAL HG22 . 18387 1 1269 . 1 1 101 101 VAL HG23 H 1 1.369 0.003 . 2 . . . A 101 VAL HG23 . 18387 1 1270 . 1 1 101 101 VAL C C 13 178.533 0.003 . 1 . . . A 101 VAL C . 18387 1 1271 . 1 1 101 101 VAL CA C 13 67.002 0.015 . 1 . . . A 101 VAL CA . 18387 1 1272 . 1 1 101 101 VAL CB C 13 32.037 0.011 . 1 . . . A 101 VAL CB . 18387 1 1273 . 1 1 101 101 VAL CG1 C 13 22.925 0.007 . 2 . . . A 101 VAL CG1 . 18387 1 1274 . 1 1 101 101 VAL CG2 C 13 23.818 0.016 . 2 . . . A 101 VAL CG2 . 18387 1 1275 . 1 1 101 101 VAL N N 15 122.202 0.008 . 1 . . . A 101 VAL N . 18387 1 1276 . 1 1 102 102 LEU H H 1 8.422 0.001 . 1 . . . A 102 LEU H . 18387 1 1277 . 1 1 102 102 LEU HA H 1 3.780 0.003 . 1 . . . A 102 LEU HA . 18387 1 1278 . 1 1 102 102 LEU HB2 H 1 1.460 0.001 . 2 . . . A 102 LEU HB2 . 18387 1 1279 . 1 1 102 102 LEU HB3 H 1 1.953 0.002 . 2 . . . A 102 LEU HB3 . 18387 1 1280 . 1 1 102 102 LEU HG H 1 2.041 0.003 . 1 . . . A 102 LEU HG . 18387 1 1281 . 1 1 102 102 LEU HD11 H 1 0.924 0.003 . 2 . . . A 102 LEU HD11 . 18387 1 1282 . 1 1 102 102 LEU HD12 H 1 0.924 0.003 . 2 . . . A 102 LEU HD12 . 18387 1 1283 . 1 1 102 102 LEU HD13 H 1 0.924 0.003 . 2 . . . A 102 LEU HD13 . 18387 1 1284 . 1 1 102 102 LEU HD21 H 1 0.779 0.002 . 2 . . . A 102 LEU HD21 . 18387 1 1285 . 1 1 102 102 LEU HD22 H 1 0.779 0.002 . 2 . . . A 102 LEU HD22 . 18387 1 1286 . 1 1 102 102 LEU HD23 H 1 0.779 0.002 . 2 . . . A 102 LEU HD23 . 18387 1 1287 . 1 1 102 102 LEU C C 13 180.254 0.008 . 1 . . . A 102 LEU C . 18387 1 1288 . 1 1 102 102 LEU CA C 13 58.941 0.010 . 1 . . . A 102 LEU CA . 18387 1 1289 . 1 1 102 102 LEU CB C 13 40.439 0.012 . 1 . . . A 102 LEU CB . 18387 1 1290 . 1 1 102 102 LEU CG C 13 27.241 0.004 . 1 . . . A 102 LEU CG . 18387 1 1291 . 1 1 102 102 LEU CD1 C 13 25.387 0.004 . 2 . . . A 102 LEU CD1 . 18387 1 1292 . 1 1 102 102 LEU CD2 C 13 22.998 0.010 . 2 . . . A 102 LEU CD2 . 18387 1 1293 . 1 1 102 102 LEU N N 15 118.798 0.020 . 1 . . . A 102 LEU N . 18387 1 1294 . 1 1 103 103 GLU H H 1 8.262 0.001 . 1 . . . A 103 GLU H . 18387 1 1295 . 1 1 103 103 GLU HA H 1 4.135 0.002 . 1 . . . A 103 GLU HA . 18387 1 1296 . 1 1 103 103 GLU HB2 H 1 2.100 0.001 . 2 . . . A 103 GLU HB2 . 18387 1 1297 . 1 1 103 103 GLU HB3 H 1 2.203 0.002 . 2 . . . A 103 GLU HB3 . 18387 1 1298 . 1 1 103 103 GLU HG2 H 1 2.252 0.000 . 2 . . . A 103 GLU HG2 . 18387 1 1299 . 1 1 103 103 GLU HG3 H 1 2.489 0.001 . 2 . . . A 103 GLU HG3 . 18387 1 1300 . 1 1 103 103 GLU C C 13 180.910 0.007 . 1 . . . A 103 GLU C . 18387 1 1301 . 1 1 103 103 GLU CA C 13 59.403 0.019 . 1 . . . A 103 GLU CA . 18387 1 1302 . 1 1 103 103 GLU CB C 13 29.731 0.013 . 1 . . . A 103 GLU CB . 18387 1 1303 . 1 1 103 103 GLU CG C 13 36.918 0.004 . 1 . . . A 103 GLU CG . 18387 1 1304 . 1 1 103 103 GLU N N 15 116.915 0.065 . 1 . . . A 103 GLU N . 18387 1 1305 . 1 1 104 104 SER H H 1 8.544 0.001 . 1 . . . A 104 SER H . 18387 1 1306 . 1 1 104 104 SER HA H 1 4.216 0.001 . 1 . . . A 104 SER HA . 18387 1 1307 . 1 1 104 104 SER HB2 H 1 3.969 0.003 . 2 . . . A 104 SER HB2 . 18387 1 1308 . 1 1 104 104 SER HB3 H 1 4.072 0.002 . 2 . . . A 104 SER HB3 . 18387 1 1309 . 1 1 104 104 SER C C 13 175.455 0.002 . 1 . . . A 104 SER C . 18387 1 1310 . 1 1 104 104 SER CA C 13 62.019 0.023 . 1 . . . A 104 SER CA . 18387 1 1311 . 1 1 104 104 SER CB C 13 62.891 0.016 . 1 . . . A 104 SER CB . 18387 1 1312 . 1 1 104 104 SER N N 15 117.866 0.020 . 1 . . . A 104 SER N . 18387 1 1313 . 1 1 105 105 TYR H H 1 7.691 0.001 . 1 . . . A 105 TYR H . 18387 1 1314 . 1 1 105 105 TYR HA H 1 4.272 0.002 . 1 . . . A 105 TYR HA . 18387 1 1315 . 1 1 105 105 TYR HB2 H 1 2.412 0.003 . 2 . . . A 105 TYR HB2 . 18387 1 1316 . 1 1 105 105 TYR HB3 H 1 2.735 0.002 . 2 . . . A 105 TYR HB3 . 18387 1 1317 . 1 1 105 105 TYR HD1 H 1 7.447 0.002 . 3 . . . A 105 TYR HD1 . 18387 1 1318 . 1 1 105 105 TYR HD2 H 1 7.447 0.002 . 3 . . . A 105 TYR HD2 . 18387 1 1319 . 1 1 105 105 TYR HE1 H 1 6.691 0.003 . 3 . . . A 105 TYR HE1 . 18387 1 1320 . 1 1 105 105 TYR HE2 H 1 6.691 0.003 . 3 . . . A 105 TYR HE2 . 18387 1 1321 . 1 1 105 105 TYR C C 13 174.750 0.031 . 1 . . . A 105 TYR C . 18387 1 1322 . 1 1 105 105 TYR CA C 13 59.859 0.019 . 1 . . . A 105 TYR CA . 18387 1 1323 . 1 1 105 105 TYR CB C 13 39.711 0.008 . 1 . . . A 105 TYR CB . 18387 1 1324 . 1 1 105 105 TYR CD1 C 13 133.417 0.016 . 3 . . . A 105 TYR CD1 . 18387 1 1325 . 1 1 105 105 TYR CD2 C 13 133.417 0.016 . 3 . . . A 105 TYR CD2 . 18387 1 1326 . 1 1 105 105 TYR CE1 C 13 118.965 0.015 . 3 . . . A 105 TYR CE1 . 18387 1 1327 . 1 1 105 105 TYR CE2 C 13 118.965 0.015 . 3 . . . A 105 TYR CE2 . 18387 1 1328 . 1 1 105 105 TYR N N 15 117.278 0.029 . 1 . . . A 105 TYR N . 18387 1 1329 . 1 1 106 106 CYS H H 1 7.862 0.001 . 1 . . . A 106 CYS H . 18387 1 1330 . 1 1 106 106 CYS HA H 1 3.895 0.001 . 1 . . . A 106 CYS HA . 18387 1 1331 . 1 1 106 106 CYS HB2 H 1 2.956 0.000 . 2 . . . A 106 CYS HB2 . 18387 1 1332 . 1 1 106 106 CYS HB3 H 1 3.044 0.001 . 2 . . . A 106 CYS HB3 . 18387 1 1333 . 1 1 106 106 CYS C C 13 174.056 0.011 . 1 . . . A 106 CYS C . 18387 1 1334 . 1 1 106 106 CYS CA C 13 59.610 0.019 . 1 . . . A 106 CYS CA . 18387 1 1335 . 1 1 106 106 CYS CB C 13 25.032 0.024 . 1 . . . A 106 CYS CB . 18387 1 1336 . 1 1 106 106 CYS N N 15 116.897 0.014 . 1 . . . A 106 CYS N . 18387 1 1337 . 1 1 107 107 ILE H H 1 7.707 0.001 . 1 . . . A 107 ILE H . 18387 1 1338 . 1 1 107 107 ILE HA H 1 3.339 0.002 . 1 . . . A 107 ILE HA . 18387 1 1339 . 1 1 107 107 ILE HB H 1 1.227 0.003 . 1 . . . A 107 ILE HB . 18387 1 1340 . 1 1 107 107 ILE HG12 H 1 0.759 0.006 . 2 . . . A 107 ILE HG12 . 18387 1 1341 . 1 1 107 107 ILE HG13 H 1 -0.596 0.003 . 2 . . . A 107 ILE HG13 . 18387 1 1342 . 1 1 107 107 ILE HG21 H 1 0.108 0.002 . 1 . . . A 107 ILE HG21 . 18387 1 1343 . 1 1 107 107 ILE HG22 H 1 0.108 0.002 . 1 . . . A 107 ILE HG22 . 18387 1 1344 . 1 1 107 107 ILE HG23 H 1 0.108 0.002 . 1 . . . A 107 ILE HG23 . 18387 1 1345 . 1 1 107 107 ILE HD11 H 1 -0.512 0.002 . 1 . . . A 107 ILE HD11 . 18387 1 1346 . 1 1 107 107 ILE HD12 H 1 -0.512 0.002 . 1 . . . A 107 ILE HD12 . 18387 1 1347 . 1 1 107 107 ILE HD13 H 1 -0.512 0.002 . 1 . . . A 107 ILE HD13 . 18387 1 1348 . 1 1 107 107 ILE C C 13 176.793 0.000 . 1 . . . A 107 ILE C . 18387 1 1349 . 1 1 107 107 ILE CA C 13 62.745 0.017 . 1 . . . A 107 ILE CA . 18387 1 1350 . 1 1 107 107 ILE CB C 13 38.079 0.007 . 1 . . . A 107 ILE CB . 18387 1 1351 . 1 1 107 107 ILE CG1 C 13 27.437 0.007 . 1 . . . A 107 ILE CG1 . 18387 1 1352 . 1 1 107 107 ILE CG2 C 13 17.110 0.005 . 1 . . . A 107 ILE CG2 . 18387 1 1353 . 1 1 107 107 ILE CD1 C 13 12.128 0.006 . 1 . . . A 107 ILE CD1 . 18387 1 1354 . 1 1 107 107 ILE N N 15 118.885 0.020 . 1 . . . A 107 ILE N . 18387 1 1355 . 1 1 108 108 VAL H H 1 8.656 0.002 . 1 . . . A 108 VAL H . 18387 1 1356 . 1 1 108 108 VAL HA H 1 4.274 0.002 . 1 . . . A 108 VAL HA . 18387 1 1357 . 1 1 108 108 VAL HB H 1 2.220 0.001 . 1 . . . A 108 VAL HB . 18387 1 1358 . 1 1 108 108 VAL HG11 H 1 0.840 0.001 . 2 . . . A 108 VAL HG11 . 18387 1 1359 . 1 1 108 108 VAL HG12 H 1 0.840 0.001 . 2 . . . A 108 VAL HG12 . 18387 1 1360 . 1 1 108 108 VAL HG13 H 1 0.840 0.001 . 2 . . . A 108 VAL HG13 . 18387 1 1361 . 1 1 108 108 VAL HG21 H 1 0.853 0.002 . 2 . . . A 108 VAL HG21 . 18387 1 1362 . 1 1 108 108 VAL HG22 H 1 0.853 0.002 . 2 . . . A 108 VAL HG22 . 18387 1 1363 . 1 1 108 108 VAL HG23 H 1 0.853 0.002 . 2 . . . A 108 VAL HG23 . 18387 1 1364 . 1 1 108 108 VAL C C 13 175.476 0.008 . 1 . . . A 108 VAL C . 18387 1 1365 . 1 1 108 108 VAL CA C 13 61.624 0.012 . 1 . . . A 108 VAL CA . 18387 1 1366 . 1 1 108 108 VAL CB C 13 33.008 0.009 . 1 . . . A 108 VAL CB . 18387 1 1367 . 1 1 108 108 VAL CG1 C 13 19.418 0.003 . 2 . . . A 108 VAL CG1 . 18387 1 1368 . 1 1 108 108 VAL CG2 C 13 21.241 0.005 . 2 . . . A 108 VAL CG2 . 18387 1 1369 . 1 1 108 108 VAL N N 15 123.983 0.013 . 1 . . . A 108 VAL N . 18387 1 1370 . 1 1 109 109 GLY H H 1 7.500 0.001 . 1 . . . A 109 GLY H . 18387 1 1371 . 1 1 109 109 GLY HA2 H 1 4.112 0.002 . 2 . . . A 109 GLY HA2 . 18387 1 1372 . 1 1 109 109 GLY HA3 H 1 3.900 0.001 . 2 . . . A 109 GLY HA3 . 18387 1 1373 . 1 1 109 109 GLY C C 13 169.982 0.003 . 1 . . . A 109 GLY C . 18387 1 1374 . 1 1 109 109 GLY CA C 13 44.603 0.019 . 1 . . . A 109 GLY CA . 18387 1 1375 . 1 1 109 109 GLY N N 15 110.120 0.007 . 1 . . . A 109 GLY N . 18387 1 1376 . 1 1 110 110 PHE H H 1 8.203 0.002 . 1 . . . A 110 PHE H . 18387 1 1377 . 1 1 110 110 PHE HA H 1 4.774 0.001 . 1 . . . A 110 PHE HA . 18387 1 1378 . 1 1 110 110 PHE HB2 H 1 3.098 0.002 . 2 . . . A 110 PHE HB2 . 18387 1 1379 . 1 1 110 110 PHE HB3 H 1 3.124 0.002 . 2 . . . A 110 PHE HB3 . 18387 1 1380 . 1 1 110 110 PHE HD1 H 1 7.447 0.002 . 3 . . . A 110 PHE HD1 . 18387 1 1381 . 1 1 110 110 PHE HD2 H 1 7.447 0.002 . 3 . . . A 110 PHE HD2 . 18387 1 1382 . 1 1 110 110 PHE HE1 H 1 7.220 0.003 . 3 . . . A 110 PHE HE1 . 18387 1 1383 . 1 1 110 110 PHE HE2 H 1 7.220 0.003 . 3 . . . A 110 PHE HE2 . 18387 1 1384 . 1 1 110 110 PHE HZ H 1 7.130 0.002 . 1 . . . A 110 PHE HZ . 18387 1 1385 . 1 1 110 110 PHE C C 13 174.361 0.000 . 1 . . . A 110 PHE C . 18387 1 1386 . 1 1 110 110 PHE CA C 13 55.687 0.005 . 1 . . . A 110 PHE CA . 18387 1 1387 . 1 1 110 110 PHE CB C 13 41.951 0.022 . 1 . . . A 110 PHE CB . 18387 1 1388 . 1 1 110 110 PHE CD1 C 13 132.204 0.014 . 3 . . . A 110 PHE CD1 . 18387 1 1389 . 1 1 110 110 PHE CD2 C 13 132.204 0.014 . 3 . . . A 110 PHE CD2 . 18387 1 1390 . 1 1 110 110 PHE CE1 C 13 131.153 0.027 . 3 . . . A 110 PHE CE1 . 18387 1 1391 . 1 1 110 110 PHE CE2 C 13 131.153 0.027 . 3 . . . A 110 PHE CE2 . 18387 1 1392 . 1 1 110 110 PHE CZ C 13 129.735 0.014 . 1 . . . A 110 PHE CZ . 18387 1 1393 . 1 1 110 110 PHE N N 15 115.276 0.013 . 1 . . . A 110 PHE N . 18387 1 1394 . 1 1 111 111 PRO HA H 1 5.359 0.003 . 1 . . . A 111 PRO HA . 18387 1 1395 . 1 1 111 111 PRO HB2 H 1 2.320 0.003 . 2 . . . A 111 PRO HB2 . 18387 1 1396 . 1 1 111 111 PRO HB3 H 1 3.177 0.003 . 2 . . . A 111 PRO HB3 . 18387 1 1397 . 1 1 111 111 PRO HG2 H 1 1.943 0.001 . 2 . . . A 111 PRO HG2 . 18387 1 1398 . 1 1 111 111 PRO HG3 H 1 2.102 0.001 . 2 . . . A 111 PRO HG3 . 18387 1 1399 . 1 1 111 111 PRO HD2 H 1 3.569 0.001 . 2 . . . A 111 PRO HD2 . 18387 1 1400 . 1 1 111 111 PRO HD3 H 1 3.825 0.001 . 2 . . . A 111 PRO HD3 . 18387 1 1401 . 1 1 111 111 PRO C C 13 175.691 0.012 . 1 . . . A 111 PRO C . 18387 1 1402 . 1 1 111 111 PRO CA C 13 63.157 0.009 . 1 . . . A 111 PRO CA . 18387 1 1403 . 1 1 111 111 PRO CB C 13 35.304 0.011 . 1 . . . A 111 PRO CB . 18387 1 1404 . 1 1 111 111 PRO CG C 13 25.005 0.006 . 1 . . . A 111 PRO CG . 18387 1 1405 . 1 1 111 111 PRO CD C 13 50.768 0.005 . 1 . . . A 111 PRO CD . 18387 1 1406 . 1 1 112 112 HIS H H 1 8.952 0.001 . 1 . . . A 112 HIS H . 18387 1 1407 . 1 1 112 112 HIS HA H 1 4.963 0.005 . 1 . . . A 112 HIS HA . 18387 1 1408 . 1 1 112 112 HIS HB2 H 1 3.108 0.002 . 2 . . . A 112 HIS HB2 . 18387 1 1409 . 1 1 112 112 HIS HB3 H 1 3.379 0.003 . 2 . . . A 112 HIS HB3 . 18387 1 1410 . 1 1 112 112 HIS HE1 H 1 7.746 0.002 . 1 . . . A 112 HIS HE1 . 18387 1 1411 . 1 1 112 112 HIS C C 13 173.649 0.004 . 1 . . . A 112 HIS C . 18387 1 1412 . 1 1 112 112 HIS CA C 13 57.074 0.035 . 1 . . . A 112 HIS CA . 18387 1 1413 . 1 1 112 112 HIS CB C 13 32.197 0.007 . 1 . . . A 112 HIS CB . 18387 1 1414 . 1 1 112 112 HIS CE1 C 13 138.885 0.000 . 1 . . . A 112 HIS CE1 . 18387 1 1415 . 1 1 112 112 HIS N N 15 123.708 0.007 . 1 . . . A 112 HIS N . 18387 1 1416 . 1 1 113 113 ILE H H 1 8.808 0.002 . 1 . . . A 113 ILE H . 18387 1 1417 . 1 1 113 113 ILE HA H 1 5.697 0.003 . 1 . . . A 113 ILE HA . 18387 1 1418 . 1 1 113 113 ILE HB H 1 2.219 0.004 . 1 . . . A 113 ILE HB . 18387 1 1419 . 1 1 113 113 ILE HG12 H 1 1.791 0.002 . 2 . . . A 113 ILE HG12 . 18387 1 1420 . 1 1 113 113 ILE HG13 H 1 1.187 0.002 . 2 . . . A 113 ILE HG13 . 18387 1 1421 . 1 1 113 113 ILE HG21 H 1 0.800 0.004 . 1 . . . A 113 ILE HG21 . 18387 1 1422 . 1 1 113 113 ILE HG22 H 1 0.800 0.004 . 1 . . . A 113 ILE HG22 . 18387 1 1423 . 1 1 113 113 ILE HG23 H 1 0.800 0.004 . 1 . . . A 113 ILE HG23 . 18387 1 1424 . 1 1 113 113 ILE HD11 H 1 0.932 0.002 . 1 . . . A 113 ILE HD11 . 18387 1 1425 . 1 1 113 113 ILE HD12 H 1 0.932 0.002 . 1 . . . A 113 ILE HD12 . 18387 1 1426 . 1 1 113 113 ILE HD13 H 1 0.932 0.002 . 1 . . . A 113 ILE HD13 . 18387 1 1427 . 1 1 113 113 ILE C C 13 176.130 0.005 . 1 . . . A 113 ILE C . 18387 1 1428 . 1 1 113 113 ILE CA C 13 60.995 0.014 . 1 . . . A 113 ILE CA . 18387 1 1429 . 1 1 113 113 ILE CB C 13 38.055 0.019 . 1 . . . A 113 ILE CB . 18387 1 1430 . 1 1 113 113 ILE CG1 C 13 28.268 0.005 . 1 . . . A 113 ILE CG1 . 18387 1 1431 . 1 1 113 113 ILE CG2 C 13 19.171 0.009 . 1 . . . A 113 ILE CG2 . 18387 1 1432 . 1 1 113 113 ILE CD1 C 13 13.354 0.014 . 1 . . . A 113 ILE CD1 . 18387 1 1433 . 1 1 113 113 ILE N N 15 128.596 0.007 . 1 . . . A 113 ILE N . 18387 1 1434 . 1 1 114 114 ILE H H 1 8.721 0.001 . 1 . . . A 114 ILE H . 18387 1 1435 . 1 1 114 114 ILE HA H 1 4.973 0.003 . 1 . . . A 114 ILE HA . 18387 1 1436 . 1 1 114 114 ILE HB H 1 2.215 0.003 . 1 . . . A 114 ILE HB . 18387 1 1437 . 1 1 114 114 ILE HG12 H 1 1.463 0.005 . 2 . . . A 114 ILE HG12 . 18387 1 1438 . 1 1 114 114 ILE HG13 H 1 1.662 0.002 . 2 . . . A 114 ILE HG13 . 18387 1 1439 . 1 1 114 114 ILE HG21 H 1 1.140 0.002 . 1 . . . A 114 ILE HG21 . 18387 1 1440 . 1 1 114 114 ILE HG22 H 1 1.140 0.002 . 1 . . . A 114 ILE HG22 . 18387 1 1441 . 1 1 114 114 ILE HG23 H 1 1.140 0.002 . 1 . . . A 114 ILE HG23 . 18387 1 1442 . 1 1 114 114 ILE HD11 H 1 1.317 0.003 . 1 . . . A 114 ILE HD11 . 18387 1 1443 . 1 1 114 114 ILE HD12 H 1 1.317 0.003 . 1 . . . A 114 ILE HD12 . 18387 1 1444 . 1 1 114 114 ILE HD13 H 1 1.317 0.003 . 1 . . . A 114 ILE HD13 . 18387 1 1445 . 1 1 114 114 ILE C C 13 173.186 0.000 . 1 . . . A 114 ILE C . 18387 1 1446 . 1 1 114 114 ILE CA C 13 58.730 0.008 . 1 . . . A 114 ILE CA . 18387 1 1447 . 1 1 114 114 ILE CB C 13 42.540 0.011 . 1 . . . A 114 ILE CB . 18387 1 1448 . 1 1 114 114 ILE CG1 C 13 27.189 0.007 . 1 . . . A 114 ILE CG1 . 18387 1 1449 . 1 1 114 114 ILE CG2 C 13 18.795 0.009 . 1 . . . A 114 ILE CG2 . 18387 1 1450 . 1 1 114 114 ILE CD1 C 13 15.166 0.003 . 1 . . . A 114 ILE CD1 . 18387 1 1451 . 1 1 114 114 ILE N N 15 119.668 0.010 . 1 . . . A 114 ILE N . 18387 1 1452 . 1 1 115 115 LEU H H 1 8.665 0.002 . 1 . . . A 115 LEU H . 18387 1 1453 . 1 1 115 115 LEU HA H 1 5.275 0.003 . 1 . . . A 115 LEU HA . 18387 1 1454 . 1 1 115 115 LEU HB2 H 1 0.914 0.003 . 2 . . . A 115 LEU HB2 . 18387 1 1455 . 1 1 115 115 LEU HB3 H 1 1.800 0.002 . 2 . . . A 115 LEU HB3 . 18387 1 1456 . 1 1 115 115 LEU HG H 1 1.272 0.003 . 1 . . . A 115 LEU HG . 18387 1 1457 . 1 1 115 115 LEU HD11 H 1 0.415 0.001 . 2 . . . A 115 LEU HD11 . 18387 1 1458 . 1 1 115 115 LEU HD12 H 1 0.415 0.001 . 2 . . . A 115 LEU HD12 . 18387 1 1459 . 1 1 115 115 LEU HD13 H 1 0.415 0.001 . 2 . . . A 115 LEU HD13 . 18387 1 1460 . 1 1 115 115 LEU HD21 H 1 1.027 0.003 . 2 . . . A 115 LEU HD21 . 18387 1 1461 . 1 1 115 115 LEU HD22 H 1 1.027 0.003 . 2 . . . A 115 LEU HD22 . 18387 1 1462 . 1 1 115 115 LEU HD23 H 1 1.027 0.003 . 2 . . . A 115 LEU HD23 . 18387 1 1463 . 1 1 115 115 LEU C C 13 173.601 0.015 . 1 . . . A 115 LEU C . 18387 1 1464 . 1 1 115 115 LEU CA C 13 53.782 0.012 . 1 . . . A 115 LEU CA . 18387 1 1465 . 1 1 115 115 LEU CB C 13 46.134 0.006 . 1 . . . A 115 LEU CB . 18387 1 1466 . 1 1 115 115 LEU CG C 13 27.437 0.015 . 1 . . . A 115 LEU CG . 18387 1 1467 . 1 1 115 115 LEU CD1 C 13 27.533 0.008 . 2 . . . A 115 LEU CD1 . 18387 1 1468 . 1 1 115 115 LEU CD2 C 13 23.540 0.004 . 2 . . . A 115 LEU CD2 . 18387 1 1469 . 1 1 115 115 LEU N N 15 122.770 0.013 . 1 . . . A 115 LEU N . 18387 1 1470 . 1 1 116 116 VAL H H 1 9.472 0.002 . 1 . . . A 116 VAL H . 18387 1 1471 . 1 1 116 116 VAL HA H 1 4.858 0.002 . 1 . . . A 116 VAL HA . 18387 1 1472 . 1 1 116 116 VAL HB H 1 2.193 0.003 . 1 . . . A 116 VAL HB . 18387 1 1473 . 1 1 116 116 VAL HG11 H 1 0.991 0.003 . 2 . . . A 116 VAL HG11 . 18387 1 1474 . 1 1 116 116 VAL HG12 H 1 0.991 0.003 . 2 . . . A 116 VAL HG12 . 18387 1 1475 . 1 1 116 116 VAL HG13 H 1 0.991 0.003 . 2 . . . A 116 VAL HG13 . 18387 1 1476 . 1 1 116 116 VAL HG21 H 1 1.050 0.003 . 2 . . . A 116 VAL HG21 . 18387 1 1477 . 1 1 116 116 VAL HG22 H 1 1.050 0.003 . 2 . . . A 116 VAL HG22 . 18387 1 1478 . 1 1 116 116 VAL HG23 H 1 1.050 0.003 . 2 . . . A 116 VAL HG23 . 18387 1 1479 . 1 1 116 116 VAL C C 13 174.565 0.002 . 1 . . . A 116 VAL C . 18387 1 1480 . 1 1 116 116 VAL CA C 13 60.804 0.008 . 1 . . . A 116 VAL CA . 18387 1 1481 . 1 1 116 116 VAL CB C 13 33.915 0.008 . 1 . . . A 116 VAL CB . 18387 1 1482 . 1 1 116 116 VAL CG1 C 13 22.954 0.005 . 2 . . . A 116 VAL CG1 . 18387 1 1483 . 1 1 116 116 VAL CG2 C 13 21.260 0.011 . 2 . . . A 116 VAL CG2 . 18387 1 1484 . 1 1 116 116 VAL N N 15 130.411 0.006 . 1 . . . A 116 VAL N . 18387 1 1485 . 1 1 117 117 ASP H H 1 9.429 0.002 . 1 . . . A 117 ASP H . 18387 1 1486 . 1 1 117 117 ASP HA H 1 4.392 0.004 . 1 . . . A 117 ASP HA . 18387 1 1487 . 1 1 117 117 ASP HB2 H 1 2.614 0.002 . 2 . . . A 117 ASP HB2 . 18387 1 1488 . 1 1 117 117 ASP HB3 H 1 2.962 0.002 . 2 . . . A 117 ASP HB3 . 18387 1 1489 . 1 1 117 117 ASP C C 13 176.567 0.000 . 1 . . . A 117 ASP C . 18387 1 1490 . 1 1 117 117 ASP CA C 13 52.600 0.008 . 1 . . . A 117 ASP CA . 18387 1 1491 . 1 1 117 117 ASP CB C 13 40.584 0.013 . 1 . . . A 117 ASP CB . 18387 1 1492 . 1 1 117 117 ASP N N 15 127.896 0.005 . 1 . . . A 117 ASP N . 18387 1 1493 . 1 1 118 118 PRO HA H 1 4.194 0.002 . 1 . . . A 118 PRO HA . 18387 1 1494 . 1 1 118 118 PRO HB2 H 1 1.685 0.003 . 2 . . . A 118 PRO HB2 . 18387 1 1495 . 1 1 118 118 PRO HB3 H 1 1.824 0.002 . 2 . . . A 118 PRO HB3 . 18387 1 1496 . 1 1 118 118 PRO HG2 H 1 1.061 0.003 . 2 . . . A 118 PRO HG2 . 18387 1 1497 . 1 1 118 118 PRO HG3 H 1 1.800 0.001 . 2 . . . A 118 PRO HG3 . 18387 1 1498 . 1 1 118 118 PRO HD2 H 1 1.581 0.002 . 2 . . . A 118 PRO HD2 . 18387 1 1499 . 1 1 118 118 PRO HD3 H 1 3.102 0.004 . 2 . . . A 118 PRO HD3 . 18387 1 1500 . 1 1 118 118 PRO C C 13 177.534 0.007 . 1 . . . A 118 PRO C . 18387 1 1501 . 1 1 118 118 PRO CA C 13 65.165 0.015 . 1 . . . A 118 PRO CA . 18387 1 1502 . 1 1 118 118 PRO CB C 13 32.813 0.005 . 1 . . . A 118 PRO CB . 18387 1 1503 . 1 1 118 118 PRO CG C 13 28.192 0.028 . 1 . . . A 118 PRO CG . 18387 1 1504 . 1 1 118 118 PRO CD C 13 50.443 0.009 . 1 . . . A 118 PRO CD . 18387 1 1505 . 1 1 119 119 GLU H H 1 7.733 0.003 . 1 . . . A 119 GLU H . 18387 1 1506 . 1 1 119 119 GLU HA H 1 4.339 0.002 . 1 . . . A 119 GLU HA . 18387 1 1507 . 1 1 119 119 GLU HB2 H 1 2.060 0.001 . 2 . . . A 119 GLU HB2 . 18387 1 1508 . 1 1 119 119 GLU HB3 H 1 2.247 0.003 . 2 . . . A 119 GLU HB3 . 18387 1 1509 . 1 1 119 119 GLU HG2 H 1 2.202 0.000 . 1 . . . A 119 GLU HG2 . 18387 1 1510 . 1 1 119 119 GLU HG3 H 1 2.202 0.000 . 1 . . . A 119 GLU HG3 . 18387 1 1511 . 1 1 119 119 GLU C C 13 176.722 0.006 . 1 . . . A 119 GLU C . 18387 1 1512 . 1 1 119 119 GLU CA C 13 55.639 0.009 . 1 . . . A 119 GLU CA . 18387 1 1513 . 1 1 119 119 GLU CB C 13 30.577 0.013 . 1 . . . A 119 GLU CB . 18387 1 1514 . 1 1 119 119 GLU CG C 13 37.136 0.000 . 1 . . . A 119 GLU CG . 18387 1 1515 . 1 1 119 119 GLU N N 15 114.015 0.041 . 1 . . . A 119 GLU N . 18387 1 1516 . 1 1 120 120 GLY H H 1 8.588 0.002 . 1 . . . A 120 GLY H . 18387 1 1517 . 1 1 120 120 GLY HA2 H 1 4.273 0.005 . 2 . . . A 120 GLY HA2 . 18387 1 1518 . 1 1 120 120 GLY HA3 H 1 3.430 0.001 . 2 . . . A 120 GLY HA3 . 18387 1 1519 . 1 1 120 120 GLY C C 13 174.110 0.005 . 1 . . . A 120 GLY C . 18387 1 1520 . 1 1 120 120 GLY CA C 13 45.396 0.014 . 1 . . . A 120 GLY CA . 18387 1 1521 . 1 1 120 120 GLY N N 15 108.218 0.009 . 1 . . . A 120 GLY N . 18387 1 1522 . 1 1 121 121 LYS H H 1 8.600 0.002 . 1 . . . A 121 LYS H . 18387 1 1523 . 1 1 121 121 LYS HA H 1 4.859 0.002 . 1 . . . A 121 LYS HA . 18387 1 1524 . 1 1 121 121 LYS HB2 H 1 1.338 0.003 . 2 . . . A 121 LYS HB2 . 18387 1 1525 . 1 1 121 121 LYS HB3 H 1 1.863 0.003 . 2 . . . A 121 LYS HB3 . 18387 1 1526 . 1 1 121 121 LYS HG2 H 1 1.152 0.002 . 2 . . . A 121 LYS HG2 . 18387 1 1527 . 1 1 121 121 LYS HG3 H 1 1.262 0.001 . 2 . . . A 121 LYS HG3 . 18387 1 1528 . 1 1 121 121 LYS HD2 H 1 1.580 0.003 . 2 . . . A 121 LYS HD2 . 18387 1 1529 . 1 1 121 121 LYS HD3 H 1 1.611 0.003 . 2 . . . A 121 LYS HD3 . 18387 1 1530 . 1 1 121 121 LYS HE2 H 1 2.923 0.001 . 1 . . . A 121 LYS HE2 . 18387 1 1531 . 1 1 121 121 LYS HE3 H 1 2.923 0.001 . 1 . . . A 121 LYS HE3 . 18387 1 1532 . 1 1 121 121 LYS C C 13 176.458 0.002 . 1 . . . A 121 LYS C . 18387 1 1533 . 1 1 121 121 LYS CA C 13 54.962 0.012 . 1 . . . A 121 LYS CA . 18387 1 1534 . 1 1 121 121 LYS CB C 13 33.452 0.008 . 1 . . . A 121 LYS CB . 18387 1 1535 . 1 1 121 121 LYS CG C 13 25.563 0.008 . 1 . . . A 121 LYS CG . 18387 1 1536 . 1 1 121 121 LYS CD C 13 28.846 0.007 . 1 . . . A 121 LYS CD . 18387 1 1537 . 1 1 121 121 LYS CE C 13 41.982 0.009 . 1 . . . A 121 LYS CE . 18387 1 1538 . 1 1 121 121 LYS N N 15 121.778 0.007 . 1 . . . A 121 LYS N . 18387 1 1539 . 1 1 122 122 ILE H H 1 9.006 0.001 . 1 . . . A 122 ILE H . 18387 1 1540 . 1 1 122 122 ILE HA H 1 4.272 0.003 . 1 . . . A 122 ILE HA . 18387 1 1541 . 1 1 122 122 ILE HB H 1 1.925 0.003 . 1 . . . A 122 ILE HB . 18387 1 1542 . 1 1 122 122 ILE HG12 H 1 1.118 0.004 . 2 . . . A 122 ILE HG12 . 18387 1 1543 . 1 1 122 122 ILE HG13 H 1 1.871 0.007 . 2 . . . A 122 ILE HG13 . 18387 1 1544 . 1 1 122 122 ILE HG21 H 1 0.933 0.002 . 1 . . . A 122 ILE HG21 . 18387 1 1545 . 1 1 122 122 ILE HG22 H 1 0.933 0.002 . 1 . . . A 122 ILE HG22 . 18387 1 1546 . 1 1 122 122 ILE HG23 H 1 0.933 0.002 . 1 . . . A 122 ILE HG23 . 18387 1 1547 . 1 1 122 122 ILE HD11 H 1 0.988 0.002 . 1 . . . A 122 ILE HD11 . 18387 1 1548 . 1 1 122 122 ILE HD12 H 1 0.988 0.002 . 1 . . . A 122 ILE HD12 . 18387 1 1549 . 1 1 122 122 ILE HD13 H 1 0.988 0.002 . 1 . . . A 122 ILE HD13 . 18387 1 1550 . 1 1 122 122 ILE C C 13 177.084 0.007 . 1 . . . A 122 ILE C . 18387 1 1551 . 1 1 122 122 ILE CA C 13 62.819 0.038 . 1 . . . A 122 ILE CA . 18387 1 1552 . 1 1 122 122 ILE CB C 13 38.648 0.009 . 1 . . . A 122 ILE CB . 18387 1 1553 . 1 1 122 122 ILE CG1 C 13 29.154 0.005 . 1 . . . A 122 ILE CG1 . 18387 1 1554 . 1 1 122 122 ILE CG2 C 13 17.279 0.003 . 1 . . . A 122 ILE CG2 . 18387 1 1555 . 1 1 122 122 ILE CD1 C 13 14.819 0.002 . 1 . . . A 122 ILE CD1 . 18387 1 1556 . 1 1 122 122 ILE N N 15 122.058 0.008 . 1 . . . A 122 ILE N . 18387 1 1557 . 1 1 123 123 VAL H H 1 9.054 0.001 . 1 . . . A 123 VAL H . 18387 1 1558 . 1 1 123 123 VAL HA H 1 4.755 0.002 . 1 . . . A 123 VAL HA . 18387 1 1559 . 1 1 123 123 VAL HB H 1 2.243 0.002 . 1 . . . A 123 VAL HB . 18387 1 1560 . 1 1 123 123 VAL HG11 H 1 0.948 0.004 . 2 . . . A 123 VAL HG11 . 18387 1 1561 . 1 1 123 123 VAL HG12 H 1 0.948 0.004 . 2 . . . A 123 VAL HG12 . 18387 1 1562 . 1 1 123 123 VAL HG13 H 1 0.948 0.004 . 2 . . . A 123 VAL HG13 . 18387 1 1563 . 1 1 123 123 VAL HG21 H 1 0.216 0.003 . 2 . . . A 123 VAL HG21 . 18387 1 1564 . 1 1 123 123 VAL HG22 H 1 0.216 0.003 . 2 . . . A 123 VAL HG22 . 18387 1 1565 . 1 1 123 123 VAL HG23 H 1 0.216 0.003 . 2 . . . A 123 VAL HG23 . 18387 1 1566 . 1 1 123 123 VAL C C 13 175.584 0.002 . 1 . . . A 123 VAL C . 18387 1 1567 . 1 1 123 123 VAL CA C 13 61.151 0.006 . 1 . . . A 123 VAL CA . 18387 1 1568 . 1 1 123 123 VAL CB C 13 33.401 0.011 . 1 . . . A 123 VAL CB . 18387 1 1569 . 1 1 123 123 VAL CG1 C 13 22.778 0.005 . 2 . . . A 123 VAL CG1 . 18387 1 1570 . 1 1 123 123 VAL CG2 C 13 18.230 0.017 . 2 . . . A 123 VAL CG2 . 18387 1 1571 . 1 1 123 123 VAL N N 15 120.561 0.008 . 1 . . . A 123 VAL N . 18387 1 1572 . 1 1 124 124 ALA H H 1 7.793 0.001 . 1 . . . A 124 ALA H . 18387 1 1573 . 1 1 124 124 ALA HA H 1 4.657 0.001 . 1 . . . A 124 ALA HA . 18387 1 1574 . 1 1 124 124 ALA HB1 H 1 1.473 0.004 . 1 . . . A 124 ALA HB1 . 18387 1 1575 . 1 1 124 124 ALA HB2 H 1 1.473 0.004 . 1 . . . A 124 ALA HB2 . 18387 1 1576 . 1 1 124 124 ALA HB3 H 1 1.473 0.004 . 1 . . . A 124 ALA HB3 . 18387 1 1577 . 1 1 124 124 ALA C C 13 174.832 0.004 . 1 . . . A 124 ALA C . 18387 1 1578 . 1 1 124 124 ALA CA C 13 52.460 0.019 . 1 . . . A 124 ALA CA . 18387 1 1579 . 1 1 124 124 ALA CB C 13 22.830 0.010 . 1 . . . A 124 ALA CB . 18387 1 1580 . 1 1 124 124 ALA N N 15 121.102 0.010 . 1 . . . A 124 ALA N . 18387 1 1581 . 1 1 125 125 LYS H H 1 8.872 0.001 . 1 . . . A 125 LYS H . 18387 1 1582 . 1 1 125 125 LYS HA H 1 5.033 0.002 . 1 . . . A 125 LYS HA . 18387 1 1583 . 1 1 125 125 LYS HB2 H 1 1.893 0.002 . 1 . . . A 125 LYS HB2 . 18387 1 1584 . 1 1 125 125 LYS HB3 H 1 1.893 0.002 . 1 . . . A 125 LYS HB3 . 18387 1 1585 . 1 1 125 125 LYS HG2 H 1 1.332 0.003 . 2 . . . A 125 LYS HG2 . 18387 1 1586 . 1 1 125 125 LYS HG3 H 1 1.380 0.002 . 2 . . . A 125 LYS HG3 . 18387 1 1587 . 1 1 125 125 LYS HD2 H 1 1.769 0.002 . 1 . . . A 125 LYS HD2 . 18387 1 1588 . 1 1 125 125 LYS HD3 H 1 1.769 0.002 . 1 . . . A 125 LYS HD3 . 18387 1 1589 . 1 1 125 125 LYS HE2 H 1 3.074 0.001 . 1 . . . A 125 LYS HE2 . 18387 1 1590 . 1 1 125 125 LYS HE3 H 1 3.074 0.001 . 1 . . . A 125 LYS HE3 . 18387 1 1591 . 1 1 125 125 LYS C C 13 173.417 0.010 . 1 . . . A 125 LYS C . 18387 1 1592 . 1 1 125 125 LYS CA C 13 55.141 0.017 . 1 . . . A 125 LYS CA . 18387 1 1593 . 1 1 125 125 LYS CB C 13 36.651 0.007 . 1 . . . A 125 LYS CB . 18387 1 1594 . 1 1 125 125 LYS CG C 13 23.625 0.025 . 1 . . . A 125 LYS CG . 18387 1 1595 . 1 1 125 125 LYS CD C 13 29.414 0.000 . 1 . . . A 125 LYS CD . 18387 1 1596 . 1 1 125 125 LYS CE C 13 42.426 0.000 . 1 . . . A 125 LYS CE . 18387 1 1597 . 1 1 125 125 LYS N N 15 117.637 0.008 . 1 . . . A 125 LYS N . 18387 1 1598 . 1 1 126 126 GLU H H 1 7.941 0.001 . 1 . . . A 126 GLU H . 18387 1 1599 . 1 1 126 126 GLU HA H 1 3.998 0.001 . 1 . . . A 126 GLU HA . 18387 1 1600 . 1 1 126 126 GLU HB2 H 1 2.134 0.000 . 2 . . . A 126 GLU HB2 . 18387 1 1601 . 1 1 126 126 GLU HB3 H 1 2.195 0.002 . 2 . . . A 126 GLU HB3 . 18387 1 1602 . 1 1 126 126 GLU HG2 H 1 2.193 0.003 . 1 . . . A 126 GLU HG2 . 18387 1 1603 . 1 1 126 126 GLU HG3 H 1 2.192 0.002 . 1 . . . A 126 GLU HG3 . 18387 1 1604 . 1 1 126 126 GLU C C 13 175.998 0.009 . 1 . . . A 126 GLU C . 18387 1 1605 . 1 1 126 126 GLU CA C 13 56.962 0.016 . 1 . . . A 126 GLU CA . 18387 1 1606 . 1 1 126 126 GLU CB C 13 26.435 0.012 . 1 . . . A 126 GLU CB . 18387 1 1607 . 1 1 126 126 GLU CG C 13 37.143 0.011 . 1 . . . A 126 GLU CG . 18387 1 1608 . 1 1 126 126 GLU N N 15 115.236 0.010 . 1 . . . A 126 GLU N . 18387 1 1609 . 1 1 127 127 LEU H H 1 7.300 0.001 . 1 . . . A 127 LEU H . 18387 1 1610 . 1 1 127 127 LEU HA H 1 4.382 0.002 . 1 . . . A 127 LEU HA . 18387 1 1611 . 1 1 127 127 LEU HB2 H 1 0.889 0.002 . 2 . . . A 127 LEU HB2 . 18387 1 1612 . 1 1 127 127 LEU HB3 H 1 1.474 0.002 . 2 . . . A 127 LEU HB3 . 18387 1 1613 . 1 1 127 127 LEU HG H 1 1.361 0.003 . 1 . . . A 127 LEU HG . 18387 1 1614 . 1 1 127 127 LEU HD11 H 1 0.688 0.003 . 2 . . . A 127 LEU HD11 . 18387 1 1615 . 1 1 127 127 LEU HD12 H 1 0.688 0.003 . 2 . . . A 127 LEU HD12 . 18387 1 1616 . 1 1 127 127 LEU HD13 H 1 0.688 0.003 . 2 . . . A 127 LEU HD13 . 18387 1 1617 . 1 1 127 127 LEU HD21 H 1 0.787 0.002 . 2 . . . A 127 LEU HD21 . 18387 1 1618 . 1 1 127 127 LEU HD22 H 1 0.787 0.002 . 2 . . . A 127 LEU HD22 . 18387 1 1619 . 1 1 127 127 LEU HD23 H 1 0.787 0.002 . 2 . . . A 127 LEU HD23 . 18387 1 1620 . 1 1 127 127 LEU C C 13 176.766 0.004 . 1 . . . A 127 LEU C . 18387 1 1621 . 1 1 127 127 LEU CA C 13 54.609 0.024 . 1 . . . A 127 LEU CA . 18387 1 1622 . 1 1 127 127 LEU CB C 13 43.963 0.020 . 1 . . . A 127 LEU CB . 18387 1 1623 . 1 1 127 127 LEU CG C 13 27.033 0.014 . 1 . . . A 127 LEU CG . 18387 1 1624 . 1 1 127 127 LEU CD1 C 13 26.323 0.006 . 2 . . . A 127 LEU CD1 . 18387 1 1625 . 1 1 127 127 LEU CD2 C 13 23.560 0.011 . 2 . . . A 127 LEU CD2 . 18387 1 1626 . 1 1 127 127 LEU N N 15 118.584 0.009 . 1 . . . A 127 LEU N . 18387 1 1627 . 1 1 128 128 ARG H H 1 7.929 0.001 . 1 . . . A 128 ARG H . 18387 1 1628 . 1 1 128 128 ARG HA H 1 4.475 0.001 . 1 . . . A 128 ARG HA . 18387 1 1629 . 1 1 128 128 ARG HB2 H 1 1.632 0.002 . 2 . . . A 128 ARG HB2 . 18387 1 1630 . 1 1 128 128 ARG HB3 H 1 1.945 0.001 . 2 . . . A 128 ARG HB3 . 18387 1 1631 . 1 1 128 128 ARG HG2 H 1 1.351 0.001 . 2 . . . A 128 ARG HG2 . 18387 1 1632 . 1 1 128 128 ARG HG3 H 1 1.541 0.002 . 2 . . . A 128 ARG HG3 . 18387 1 1633 . 1 1 128 128 ARG HD2 H 1 3.147 0.002 . 2 . . . A 128 ARG HD2 . 18387 1 1634 . 1 1 128 128 ARG HD3 H 1 3.212 0.001 . 2 . . . A 128 ARG HD3 . 18387 1 1635 . 1 1 128 128 ARG C C 13 177.113 0.031 . 1 . . . A 128 ARG C . 18387 1 1636 . 1 1 128 128 ARG CA C 13 53.390 0.036 . 1 . . . A 128 ARG CA . 18387 1 1637 . 1 1 128 128 ARG CB C 13 34.612 0.010 . 1 . . . A 128 ARG CB . 18387 1 1638 . 1 1 128 128 ARG CG C 13 26.802 0.010 . 1 . . . A 128 ARG CG . 18387 1 1639 . 1 1 128 128 ARG CD C 13 41.953 0.009 . 1 . . . A 128 ARG CD . 18387 1 1640 . 1 1 128 128 ARG N N 15 118.625 0.014 . 1 . . . A 128 ARG N . 18387 1 1641 . 1 1 129 129 GLY H H 1 10.649 0.001 . 1 . . . A 129 GLY H . 18387 1 1642 . 1 1 129 129 GLY HA2 H 1 3.324 0.002 . 2 . . . A 129 GLY HA2 . 18387 1 1643 . 1 1 129 129 GLY HA3 H 1 1.885 0.002 . 2 . . . A 129 GLY HA3 . 18387 1 1644 . 1 1 129 129 GLY C C 13 175.931 0.003 . 1 . . . A 129 GLY C . 18387 1 1645 . 1 1 129 129 GLY CA C 13 45.461 0.021 . 1 . . . A 129 GLY CA . 18387 1 1646 . 1 1 129 129 GLY N N 15 114.010 0.005 . 1 . . . A 129 GLY N . 18387 1 1647 . 1 1 130 130 ASP H H 1 8.540 0.001 . 1 . . . A 130 ASP H . 18387 1 1648 . 1 1 130 130 ASP HA H 1 4.532 0.003 . 1 . . . A 130 ASP HA . 18387 1 1649 . 1 1 130 130 ASP HB2 H 1 2.544 0.002 . 2 . . . A 130 ASP HB2 . 18387 1 1650 . 1 1 130 130 ASP HB3 H 1 2.760 0.001 . 2 . . . A 130 ASP HB3 . 18387 1 1651 . 1 1 130 130 ASP C C 13 177.507 0.014 . 1 . . . A 130 ASP C . 18387 1 1652 . 1 1 130 130 ASP CA C 13 57.372 0.009 . 1 . . . A 130 ASP CA . 18387 1 1653 . 1 1 130 130 ASP CB C 13 40.903 0.007 . 1 . . . A 130 ASP CB . 18387 1 1654 . 1 1 130 130 ASP N N 15 123.975 0.009 . 1 . . . A 130 ASP N . 18387 1 1655 . 1 1 131 131 ASP H H 1 7.907 0.001 . 1 . . . A 131 ASP H . 18387 1 1656 . 1 1 131 131 ASP HA H 1 4.570 0.002 . 1 . . . A 131 ASP HA . 18387 1 1657 . 1 1 131 131 ASP HB2 H 1 2.738 0.001 . 2 . . . A 131 ASP HB2 . 18387 1 1658 . 1 1 131 131 ASP HB3 H 1 2.932 0.001 . 2 . . . A 131 ASP HB3 . 18387 1 1659 . 1 1 131 131 ASP C C 13 179.038 0.008 . 1 . . . A 131 ASP C . 18387 1 1660 . 1 1 131 131 ASP CA C 13 56.983 0.016 . 1 . . . A 131 ASP CA . 18387 1 1661 . 1 1 131 131 ASP CB C 13 40.934 0.013 . 1 . . . A 131 ASP CB . 18387 1 1662 . 1 1 131 131 ASP N N 15 116.806 0.013 . 1 . . . A 131 ASP N . 18387 1 1663 . 1 1 132 132 LEU H H 1 7.542 0.003 . 1 . . . A 132 LEU H . 18387 1 1664 . 1 1 132 132 LEU HA H 1 3.791 0.002 . 1 . . . A 132 LEU HA . 18387 1 1665 . 1 1 132 132 LEU HB2 H 1 1.583 0.002 . 2 . . . A 132 LEU HB2 . 18387 1 1666 . 1 1 132 132 LEU HB3 H 1 1.820 0.003 . 2 . . . A 132 LEU HB3 . 18387 1 1667 . 1 1 132 132 LEU HG H 1 1.415 0.002 . 1 . . . A 132 LEU HG . 18387 1 1668 . 1 1 132 132 LEU HD11 H 1 0.790 0.002 . 2 . . . A 132 LEU HD11 . 18387 1 1669 . 1 1 132 132 LEU HD12 H 1 0.790 0.002 . 2 . . . A 132 LEU HD12 . 18387 1 1670 . 1 1 132 132 LEU HD13 H 1 0.790 0.002 . 2 . . . A 132 LEU HD13 . 18387 1 1671 . 1 1 132 132 LEU HD21 H 1 0.925 0.003 . 2 . . . A 132 LEU HD21 . 18387 1 1672 . 1 1 132 132 LEU HD22 H 1 0.925 0.003 . 2 . . . A 132 LEU HD22 . 18387 1 1673 . 1 1 132 132 LEU HD23 H 1 0.925 0.003 . 2 . . . A 132 LEU HD23 . 18387 1 1674 . 1 1 132 132 LEU C C 13 176.343 0.008 . 1 . . . A 132 LEU C . 18387 1 1675 . 1 1 132 132 LEU CA C 13 59.784 0.016 . 1 . . . A 132 LEU CA . 18387 1 1676 . 1 1 132 132 LEU CB C 13 41.768 0.016 . 1 . . . A 132 LEU CB . 18387 1 1677 . 1 1 132 132 LEU CG C 13 27.588 0.015 . 1 . . . A 132 LEU CG . 18387 1 1678 . 1 1 132 132 LEU CD1 C 13 26.238 0.019 . 2 . . . A 132 LEU CD1 . 18387 1 1679 . 1 1 132 132 LEU CD2 C 13 27.822 0.019 . 2 . . . A 132 LEU CD2 . 18387 1 1680 . 1 1 132 132 LEU N N 15 123.869 0.010 . 1 . . . A 132 LEU N . 18387 1 1681 . 1 1 133 133 TYR H H 1 7.384 0.001 . 1 . . . A 133 TYR H . 18387 1 1682 . 1 1 133 133 TYR HA H 1 3.996 0.003 . 1 . . . A 133 TYR HA . 18387 1 1683 . 1 1 133 133 TYR HB2 H 1 3.006 0.003 . 2 . . . A 133 TYR HB2 . 18387 1 1684 . 1 1 133 133 TYR HB3 H 1 3.246 0.002 . 2 . . . A 133 TYR HB3 . 18387 1 1685 . 1 1 133 133 TYR HD1 H 1 7.210 0.005 . 3 . . . A 133 TYR HD1 . 18387 1 1686 . 1 1 133 133 TYR HD2 H 1 7.210 0.005 . 3 . . . A 133 TYR HD2 . 18387 1 1687 . 1 1 133 133 TYR HE1 H 1 6.663 0.003 . 3 . . . A 133 TYR HE1 . 18387 1 1688 . 1 1 133 133 TYR HE2 H 1 6.663 0.003 . 3 . . . A 133 TYR HE2 . 18387 1 1689 . 1 1 133 133 TYR C C 13 177.426 0.006 . 1 . . . A 133 TYR C . 18387 1 1690 . 1 1 133 133 TYR CA C 13 62.133 0.011 . 1 . . . A 133 TYR CA . 18387 1 1691 . 1 1 133 133 TYR CB C 13 38.576 0.017 . 1 . . . A 133 TYR CB . 18387 1 1692 . 1 1 133 133 TYR CD1 C 13 133.885 0.027 . 3 . . . A 133 TYR CD1 . 18387 1 1693 . 1 1 133 133 TYR CD2 C 13 133.885 0.027 . 3 . . . A 133 TYR CD2 . 18387 1 1694 . 1 1 133 133 TYR CE1 C 13 118.516 0.019 . 3 . . . A 133 TYR CE1 . 18387 1 1695 . 1 1 133 133 TYR CE2 C 13 118.516 0.019 . 3 . . . A 133 TYR CE2 . 18387 1 1696 . 1 1 133 133 TYR N N 15 120.042 0.009 . 1 . . . A 133 TYR N . 18387 1 1697 . 1 1 134 134 ASN H H 1 8.399 0.001 . 1 . . . A 134 ASN H . 18387 1 1698 . 1 1 134 134 ASN HA H 1 4.403 0.002 . 1 . . . A 134 ASN HA . 18387 1 1699 . 1 1 134 134 ASN HB2 H 1 2.921 0.001 . 1 . . . A 134 ASN HB2 . 18387 1 1700 . 1 1 134 134 ASN HB3 H 1 2.921 0.001 . 1 . . . A 134 ASN HB3 . 18387 1 1701 . 1 1 134 134 ASN HD21 H 1 7.018 0.001 . 1 . . . A 134 ASN HD21 . 18387 1 1702 . 1 1 134 134 ASN HD22 H 1 7.841 0.000 . 1 . . . A 134 ASN HD22 . 18387 1 1703 . 1 1 134 134 ASN C C 13 178.703 0.005 . 1 . . . A 134 ASN C . 18387 1 1704 . 1 1 134 134 ASN CA C 13 55.809 0.016 . 1 . . . A 134 ASN CA . 18387 1 1705 . 1 1 134 134 ASN CB C 13 38.208 0.029 . 1 . . . A 134 ASN CB . 18387 1 1706 . 1 1 134 134 ASN N N 15 114.936 0.016 . 1 . . . A 134 ASN N . 18387 1 1707 . 1 1 134 134 ASN ND2 N 15 112.061 0.024 . 1 . . . A 134 ASN ND2 . 18387 1 1708 . 1 1 135 135 THR H H 1 8.265 0.002 . 1 . . . A 135 THR H . 18387 1 1709 . 1 1 135 135 THR HA H 1 3.920 0.002 . 1 . . . A 135 THR HA . 18387 1 1710 . 1 1 135 135 THR HB H 1 4.190 0.001 . 1 . . . A 135 THR HB . 18387 1 1711 . 1 1 135 135 THR HG21 H 1 1.249 0.002 . 1 . . . A 135 THR HG21 . 18387 1 1712 . 1 1 135 135 THR HG22 H 1 1.249 0.002 . 1 . . . A 135 THR HG22 . 18387 1 1713 . 1 1 135 135 THR HG23 H 1 1.249 0.002 . 1 . . . A 135 THR HG23 . 18387 1 1714 . 1 1 135 135 THR C C 13 175.323 0.015 . 1 . . . A 135 THR C . 18387 1 1715 . 1 1 135 135 THR CA C 13 67.402 0.024 . 1 . . . A 135 THR CA . 18387 1 1716 . 1 1 135 135 THR CB C 13 68.111 0.023 . 1 . . . A 135 THR CB . 18387 1 1717 . 1 1 135 135 THR CG2 C 13 21.453 0.005 . 1 . . . A 135 THR CG2 . 18387 1 1718 . 1 1 135 135 THR N N 15 117.387 0.036 . 1 . . . A 135 THR N . 18387 1 1719 . 1 1 136 136 VAL H H 1 7.595 0.001 . 1 . . . A 136 VAL H . 18387 1 1720 . 1 1 136 136 VAL HA H 1 3.015 0.001 . 1 . . . A 136 VAL HA . 18387 1 1721 . 1 1 136 136 VAL HB H 1 1.530 0.002 . 1 . . . A 136 VAL HB . 18387 1 1722 . 1 1 136 136 VAL HG11 H 1 -0.569 0.002 . 2 . . . A 136 VAL HG11 . 18387 1 1723 . 1 1 136 136 VAL HG12 H 1 -0.569 0.002 . 2 . . . A 136 VAL HG12 . 18387 1 1724 . 1 1 136 136 VAL HG13 H 1 -0.569 0.002 . 2 . . . A 136 VAL HG13 . 18387 1 1725 . 1 1 136 136 VAL HG21 H 1 0.819 0.003 . 2 . . . A 136 VAL HG21 . 18387 1 1726 . 1 1 136 136 VAL HG22 H 1 0.819 0.003 . 2 . . . A 136 VAL HG22 . 18387 1 1727 . 1 1 136 136 VAL HG23 H 1 0.819 0.003 . 2 . . . A 136 VAL HG23 . 18387 1 1728 . 1 1 136 136 VAL C C 13 176.457 0.006 . 1 . . . A 136 VAL C . 18387 1 1729 . 1 1 136 136 VAL CA C 13 68.272 0.016 . 1 . . . A 136 VAL CA . 18387 1 1730 . 1 1 136 136 VAL CB C 13 30.941 0.003 . 1 . . . A 136 VAL CB . 18387 1 1731 . 1 1 136 136 VAL CG1 C 13 21.999 0.003 . 2 . . . A 136 VAL CG1 . 18387 1 1732 . 1 1 136 136 VAL CG2 C 13 24.568 0.014 . 2 . . . A 136 VAL CG2 . 18387 1 1733 . 1 1 136 136 VAL N N 15 121.207 0.015 . 1 . . . A 136 VAL N . 18387 1 1734 . 1 1 137 137 GLU H H 1 8.114 0.001 . 1 . . . A 137 GLU H . 18387 1 1735 . 1 1 137 137 GLU HA H 1 2.682 0.001 . 1 . . . A 137 GLU HA . 18387 1 1736 . 1 1 137 137 GLU HB2 H 1 1.661 0.002 . 2 . . . A 137 GLU HB2 . 18387 1 1737 . 1 1 137 137 GLU HB3 H 1 1.998 0.001 . 2 . . . A 137 GLU HB3 . 18387 1 1738 . 1 1 137 137 GLU HG2 H 1 2.077 0.005 . 2 . . . A 137 GLU HG2 . 18387 1 1739 . 1 1 137 137 GLU HG3 H 1 2.134 0.002 . 2 . . . A 137 GLU HG3 . 18387 1 1740 . 1 1 137 137 GLU C C 13 177.482 0.005 . 1 . . . A 137 GLU C . 18387 1 1741 . 1 1 137 137 GLU CA C 13 59.930 0.014 . 1 . . . A 137 GLU CA . 18387 1 1742 . 1 1 137 137 GLU CB C 13 29.782 0.011 . 1 . . . A 137 GLU CB . 18387 1 1743 . 1 1 137 137 GLU CG C 13 36.647 0.011 . 1 . . . A 137 GLU CG . 18387 1 1744 . 1 1 137 137 GLU N N 15 118.266 0.039 . 1 . . . A 137 GLU N . 18387 1 1745 . 1 1 138 138 LYS H H 1 7.133 0.001 . 1 . . . A 138 LYS H . 18387 1 1746 . 1 1 138 138 LYS HA H 1 3.768 0.002 . 1 . . . A 138 LYS HA . 18387 1 1747 . 1 1 138 138 LYS HB2 H 1 1.687 0.001 . 2 . . . A 138 LYS HB2 . 18387 1 1748 . 1 1 138 138 LYS HB3 H 1 1.762 0.002 . 2 . . . A 138 LYS HB3 . 18387 1 1749 . 1 1 138 138 LYS HG2 H 1 1.043 0.002 . 2 . . . A 138 LYS HG2 . 18387 1 1750 . 1 1 138 138 LYS HG3 H 1 1.300 0.001 . 2 . . . A 138 LYS HG3 . 18387 1 1751 . 1 1 138 138 LYS HD2 H 1 1.459 0.001 . 1 . . . A 138 LYS HD2 . 18387 1 1752 . 1 1 138 138 LYS HD3 H 1 1.459 0.001 . 1 . . . A 138 LYS HD3 . 18387 1 1753 . 1 1 138 138 LYS HE2 H 1 2.679 0.000 . 2 . . . A 138 LYS HE2 . 18387 1 1754 . 1 1 138 138 LYS HE3 H 1 2.743 0.003 . 2 . . . A 138 LYS HE3 . 18387 1 1755 . 1 1 138 138 LYS C C 13 179.193 0.010 . 1 . . . A 138 LYS C . 18387 1 1756 . 1 1 138 138 LYS CA C 13 59.040 0.027 . 1 . . . A 138 LYS CA . 18387 1 1757 . 1 1 138 138 LYS CB C 13 32.158 0.010 . 1 . . . A 138 LYS CB . 18387 1 1758 . 1 1 138 138 LYS CG C 13 24.617 0.012 . 1 . . . A 138 LYS CG . 18387 1 1759 . 1 1 138 138 LYS CD C 13 29.299 0.009 . 1 . . . A 138 LYS CD . 18387 1 1760 . 1 1 138 138 LYS CE C 13 41.890 0.009 . 1 . . . A 138 LYS CE . 18387 1 1761 . 1 1 138 138 LYS N N 15 116.431 0.014 . 1 . . . A 138 LYS N . 18387 1 1762 . 1 1 139 139 PHE H H 1 7.338 0.002 . 1 . . . A 139 PHE H . 18387 1 1763 . 1 1 139 139 PHE HA H 1 4.010 0.002 . 1 . . . A 139 PHE HA . 18387 1 1764 . 1 1 139 139 PHE HB2 H 1 2.223 0.003 . 2 . . . A 139 PHE HB2 . 18387 1 1765 . 1 1 139 139 PHE HB3 H 1 2.308 0.002 . 2 . . . A 139 PHE HB3 . 18387 1 1766 . 1 1 139 139 PHE HD1 H 1 7.456 0.003 . 3 . . . A 139 PHE HD1 . 18387 1 1767 . 1 1 139 139 PHE HD2 H 1 7.456 0.003 . 3 . . . A 139 PHE HD2 . 18387 1 1768 . 1 1 139 139 PHE HE1 H 1 7.322 0.002 . 3 . . . A 139 PHE HE1 . 18387 1 1769 . 1 1 139 139 PHE HE2 H 1 7.322 0.002 . 3 . . . A 139 PHE HE2 . 18387 1 1770 . 1 1 139 139 PHE C C 13 177.855 0.001 . 1 . . . A 139 PHE C . 18387 1 1771 . 1 1 139 139 PHE CA C 13 62.384 0.016 . 1 . . . A 139 PHE CA . 18387 1 1772 . 1 1 139 139 PHE CB C 13 39.352 0.008 . 1 . . . A 139 PHE CB . 18387 1 1773 . 1 1 139 139 PHE CD1 C 13 132.604 0.026 . 3 . . . A 139 PHE CD1 . 18387 1 1774 . 1 1 139 139 PHE CD2 C 13 132.604 0.026 . 3 . . . A 139 PHE CD2 . 18387 1 1775 . 1 1 139 139 PHE CE1 C 13 131.287 0.024 . 3 . . . A 139 PHE CE1 . 18387 1 1776 . 1 1 139 139 PHE CE2 C 13 131.287 0.024 . 3 . . . A 139 PHE CE2 . 18387 1 1777 . 1 1 139 139 PHE N N 15 116.336 0.042 . 1 . . . A 139 PHE N . 18387 1 1778 . 1 1 140 140 VAL H H 1 8.332 0.001 . 1 . . . A 140 VAL H . 18387 1 1779 . 1 1 140 140 VAL HA H 1 3.524 0.001 . 1 . . . A 140 VAL HA . 18387 1 1780 . 1 1 140 140 VAL HB H 1 1.464 0.002 . 1 . . . A 140 VAL HB . 18387 1 1781 . 1 1 140 140 VAL HG11 H 1 0.770 0.003 . 2 . . . A 140 VAL HG11 . 18387 1 1782 . 1 1 140 140 VAL HG12 H 1 0.770 0.003 . 2 . . . A 140 VAL HG12 . 18387 1 1783 . 1 1 140 140 VAL HG13 H 1 0.770 0.003 . 2 . . . A 140 VAL HG13 . 18387 1 1784 . 1 1 140 140 VAL HG21 H 1 0.336 0.002 . 2 . . . A 140 VAL HG21 . 18387 1 1785 . 1 1 140 140 VAL HG22 H 1 0.336 0.002 . 2 . . . A 140 VAL HG22 . 18387 1 1786 . 1 1 140 140 VAL HG23 H 1 0.336 0.002 . 2 . . . A 140 VAL HG23 . 18387 1 1787 . 1 1 140 140 VAL C C 13 177.747 0.017 . 1 . . . A 140 VAL C . 18387 1 1788 . 1 1 140 140 VAL CA C 13 65.242 0.015 . 1 . . . A 140 VAL CA . 18387 1 1789 . 1 1 140 140 VAL CB C 13 31.390 0.015 . 1 . . . A 140 VAL CB . 18387 1 1790 . 1 1 140 140 VAL CG1 C 13 21.906 0.005 . 2 . . . A 140 VAL CG1 . 18387 1 1791 . 1 1 140 140 VAL CG2 C 13 22.576 0.009 . 2 . . . A 140 VAL CG2 . 18387 1 1792 . 1 1 140 140 VAL N N 15 116.491 0.008 . 1 . . . A 140 VAL N . 18387 1 1793 . 1 1 141 141 ASN H H 1 7.862 0.001 . 1 . . . A 141 ASN H . 18387 1 1794 . 1 1 141 141 ASN HA H 1 4.826 0.001 . 1 . . . A 141 ASN HA . 18387 1 1795 . 1 1 141 141 ASN HB2 H 1 2.788 0.004 . 2 . . . A 141 ASN HB2 . 18387 1 1796 . 1 1 141 141 ASN HB3 H 1 2.842 0.003 . 2 . . . A 141 ASN HB3 . 18387 1 1797 . 1 1 141 141 ASN HD21 H 1 6.914 0.000 . 1 . . . A 141 ASN HD21 . 18387 1 1798 . 1 1 141 141 ASN HD22 H 1 7.804 0.000 . 1 . . . A 141 ASN HD22 . 18387 1 1799 . 1 1 141 141 ASN C C 13 176.997 0.008 . 1 . . . A 141 ASN C . 18387 1 1800 . 1 1 141 141 ASN CA C 13 53.677 0.023 . 1 . . . A 141 ASN CA . 18387 1 1801 . 1 1 141 141 ASN CB C 13 38.448 0.020 . 1 . . . A 141 ASN CB . 18387 1 1802 . 1 1 141 141 ASN N N 15 116.956 0.011 . 1 . . . A 141 ASN N . 18387 1 1803 . 1 1 141 141 ASN ND2 N 15 111.238 0.007 . 1 . . . A 141 ASN ND2 . 18387 1 1804 . 1 1 142 142 GLY H H 1 7.466 0.002 . 1 . . . A 142 GLY H . 18387 1 1805 . 1 1 142 142 GLY HA2 H 1 3.976 0.002 . 2 . . . A 142 GLY HA2 . 18387 1 1806 . 1 1 142 142 GLY HA3 H 1 3.902 0.001 . 2 . . . A 142 GLY HA3 . 18387 1 1807 . 1 1 142 142 GLY C C 13 174.336 0.002 . 1 . . . A 142 GLY C . 18387 1 1808 . 1 1 142 142 GLY CA C 13 45.985 0.017 . 1 . . . A 142 GLY CA . 18387 1 1809 . 1 1 142 142 GLY N N 15 107.938 0.005 . 1 . . . A 142 GLY N . 18387 1 1810 . 1 1 143 143 ALA H H 1 7.950 0.001 . 1 . . . A 143 ALA H . 18387 1 1811 . 1 1 143 143 ALA HA H 1 4.341 0.001 . 1 . . . A 143 ALA HA . 18387 1 1812 . 1 1 143 143 ALA HB1 H 1 1.473 0.004 . 1 . . . A 143 ALA HB1 . 18387 1 1813 . 1 1 143 143 ALA HB2 H 1 1.473 0.004 . 1 . . . A 143 ALA HB2 . 18387 1 1814 . 1 1 143 143 ALA HB3 H 1 1.473 0.004 . 1 . . . A 143 ALA HB3 . 18387 1 1815 . 1 1 143 143 ALA C C 13 178.212 0.003 . 1 . . . A 143 ALA C . 18387 1 1816 . 1 1 143 143 ALA CA C 13 52.826 0.023 . 1 . . . A 143 ALA CA . 18387 1 1817 . 1 1 143 143 ALA CB C 13 19.244 0.025 . 1 . . . A 143 ALA CB . 18387 1 1818 . 1 1 143 143 ALA N N 15 123.441 0.007 . 1 . . . A 143 ALA N . 18387 1 1819 . 1 1 144 144 LYS H H 1 8.187 0.001 . 1 . . . A 144 LYS H . 18387 1 1820 . 1 1 144 144 LYS HA H 1 4.295 0.003 . 1 . . . A 144 LYS HA . 18387 1 1821 . 1 1 144 144 LYS HB2 H 1 1.793 0.001 . 2 . . . A 144 LYS HB2 . 18387 1 1822 . 1 1 144 144 LYS HB3 H 1 1.858 0.001 . 2 . . . A 144 LYS HB3 . 18387 1 1823 . 1 1 144 144 LYS HG2 H 1 1.456 0.002 . 1 . . . A 144 LYS HG2 . 18387 1 1824 . 1 1 144 144 LYS HG3 H 1 1.456 0.002 . 1 . . . A 144 LYS HG3 . 18387 1 1825 . 1 1 144 144 LYS HD2 H 1 1.690 0.000 . 1 . . . A 144 LYS HD2 . 18387 1 1826 . 1 1 144 144 LYS HD3 H 1 1.690 0.000 . 1 . . . A 144 LYS HD3 . 18387 1 1827 . 1 1 144 144 LYS HE2 H 1 3.024 0.001 . 1 . . . A 144 LYS HE2 . 18387 1 1828 . 1 1 144 144 LYS HE3 H 1 3.024 0.001 . 1 . . . A 144 LYS HE3 . 18387 1 1829 . 1 1 144 144 LYS C C 13 176.945 0.004 . 1 . . . A 144 LYS C . 18387 1 1830 . 1 1 144 144 LYS CA C 13 56.519 0.021 . 1 . . . A 144 LYS CA . 18387 1 1831 . 1 1 144 144 LYS CB C 13 33.030 0.011 . 1 . . . A 144 LYS CB . 18387 1 1832 . 1 1 144 144 LYS CG C 13 24.763 0.000 . 1 . . . A 144 LYS CG . 18387 1 1833 . 1 1 144 144 LYS CD C 13 29.002 0.000 . 1 . . . A 144 LYS CD . 18387 1 1834 . 1 1 144 144 LYS CE C 13 42.078 0.000 . 1 . . . A 144 LYS CE . 18387 1 1835 . 1 1 144 144 LYS N N 15 120.149 0.009 . 1 . . . A 144 LYS N . 18387 1 1836 . 1 1 145 145 GLU H H 1 8.363 0.001 . 1 . . . A 145 GLU H . 18387 1 1837 . 1 1 145 145 GLU HA H 1 4.295 0.001 . 1 . . . A 145 GLU HA . 18387 1 1838 . 1 1 145 145 GLU HB2 H 1 1.970 0.001 . 2 . . . A 145 GLU HB2 . 18387 1 1839 . 1 1 145 145 GLU HB3 H 1 2.077 0.001 . 2 . . . A 145 GLU HB3 . 18387 1 1840 . 1 1 145 145 GLU HG2 H 1 2.293 0.001 . 1 . . . A 145 GLU HG2 . 18387 1 1841 . 1 1 145 145 GLU HG3 H 1 2.293 0.001 . 1 . . . A 145 GLU HG3 . 18387 1 1842 . 1 1 145 145 GLU C C 13 177.116 0.024 . 1 . . . A 145 GLU C . 18387 1 1843 . 1 1 145 145 GLU CA C 13 56.903 0.014 . 1 . . . A 145 GLU CA . 18387 1 1844 . 1 1 145 145 GLU CB C 13 30.242 0.017 . 1 . . . A 145 GLU CB . 18387 1 1845 . 1 1 145 145 GLU CG C 13 36.408 0.000 . 1 . . . A 145 GLU CG . 18387 1 1846 . 1 1 145 145 GLU N N 15 120.992 0.061 . 1 . . . A 145 GLU N . 18387 1 1847 . 1 1 146 146 GLY H H 1 8.371 0.001 . 1 . . . A 146 GLY H . 18387 1 1848 . 1 1 146 146 GLY HA2 H 1 3.910 0.000 . 2 . . . A 146 GLY HA2 . 18387 1 1849 . 1 1 146 146 GLY HA3 H 1 3.961 0.000 . 2 . . . A 146 GLY HA3 . 18387 1 1850 . 1 1 146 146 GLY C C 13 174.108 0.000 . 1 . . . A 146 GLY C . 18387 1 1851 . 1 1 146 146 GLY CA C 13 45.401 0.009 . 1 . . . A 146 GLY CA . 18387 1 1852 . 1 1 146 146 GLY N N 15 109.467 0.007 . 1 . . . A 146 GLY N . 18387 1 1853 . 1 1 151 151 HIS HA H 1 4.609 0.001 . 1 . . . A 151 HIS HA . 18387 1 1854 . 1 1 151 151 HIS C C 13 174.258 0.000 . 1 . . . A 151 HIS C . 18387 1 1855 . 1 1 151 151 HIS CA C 13 56.165 0.020 . 1 . . . A 151 HIS CA . 18387 1 1856 . 1 1 151 151 HIS CB C 13 30.833 0.000 . 1 . . . A 151 HIS CB . 18387 1 1857 . 1 1 152 152 HIS H H 1 7.964 0.000 . 1 . . . A 152 HIS H . 18387 1 1858 . 1 1 152 152 HIS C C 13 179.586 0.000 . 1 . . . A 152 HIS C . 18387 1 1859 . 1 1 152 152 HIS CA C 13 57.656 0.000 . 1 . . . A 152 HIS CA . 18387 1 1860 . 1 1 152 152 HIS CB C 13 31.022 0.000 . 1 . . . A 152 HIS CB . 18387 1 1861 . 1 1 152 152 HIS N N 15 125.705 0.009 . 1 . . . A 152 HIS N . 18387 1 stop_ save_