data_11013 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 11013 _Entry.Title ; The dynein stalk head, the microtubule binding domain of dynein, derived from mouse ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2007-11-03 _Entry.Accession_date 2007-11-05 _Entry.Last_release_date 2008-06-18 _Entry.Original_release_date 2008-06-18 _Entry.Origination author _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 3.0.8.100 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype solution _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 Youske Shimizu . . . 11013 2 Yusuke Kato . . . 11013 3 Hisayuki Morii . . . 11013 4 Masaki Edamatsu . . . 11013 5 Yoko Toyoshima . Yano . 11013 6 Masaru Tanokura . . . 11013 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 2 11013 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 405 11013 '15N chemical shifts' 131 11013 '1H chemical shifts' 177 11013 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 . . 2008-06-18 2007-11-03 original author . 11013 stop_ save_ ############### # Citations # ############### save_cite1 _Citation.Sf_category citations _Citation.Sf_framecode cite1 _Citation.Entry_ID 11013 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 18491033 _Citation.Full_citation . _Citation.Title 'The dynein stalk head, the microtubule binding-domain of dynein: NMR assignment and ligand binding' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev 'J. Biomol. NMR' _Citation.Journal_name_full . _Citation.Journal_volume 41 _Citation.Journal_issue 2 _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 89 _Citation.Page_last 96 _Citation.Year 2008 _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 Youske Shimizu . . . 11013 1 2 Yusuke Kato . . . 11013 1 3 Hisayuki Morii . . . 11013 1 4 Masaki Edamatsu . . . 11013 1 5 Yoko Toyoshima . Yano . 11013 1 6 Masaru Tanokura . . . 11013 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'backbone assignment' 11013 1 'dynein stalk head' 11013 1 microtubule-binding 11013 1 'NMR analysis' 11013 1 'secondary structure' 11013 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 11013 _Assembly.ID 1 _Assembly.Name 'dynein heavy chain' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic no _Assembly.Thiol_state . _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 'subunit 1' 1 $DS(8:5) A . yes native no no . . . 11013 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_DS(8:5) _Entity.Sf_category entity _Entity.Sf_framecode DS(8:5) _Entity.Entry_ID 11013 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name DS(8:5) _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; MEDLDKVEPAVIEAQNAVKS IKKQHLVEVRSMANPPAAVK LALESICLLLGESTTDWKQI RSIIMRENFIPTIVNFSAEE ISDAIREKMKKNYMSNPSYN YEIVNRASLACGPMVKWAIA QLNYADMLKRVEPLRNEHHH HHH ; _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 143 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not available' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-11-26 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 3ERR . "Microtubule Binding Domain From Mouse Cytoplasmic Dynein As A Fusion With Seryl-Trna Synthetase" . . . . . 95.10 536 98.53 98.53 2.30e-85 . . . . 11013 1 2 no PDB 3J1T . "High Affinity Dynein Microtubule Binding Domain - Tubulin Complex" . . . . . 95.10 164 100.00 100.00 8.92e-94 . . . . 11013 1 3 no PDB 3J1U . "Low Affinity Dynein Microtubule Binding Domain - Tubulin Complex" . . . . . 95.10 164 100.00 100.00 8.92e-94 . . . . 11013 1 4 no PDB 3WUQ . "Structure Of The Entire Stalk Region Of The Dynein Motor Domain" . . . . . 95.10 283 100.00 100.00 9.16e-94 . . . . 11013 1 5 no DBJ BAA02996 . "cytoplasmic dynein heavy chain [Rattus norvegicus]" . . . . . 95.10 4644 100.00 100.00 2.48e-83 . . . . 11013 1 6 no DBJ BAA20783 . "KIAA0325 protein [Homo sapiens]" . . . . . 95.10 4646 100.00 100.00 2.58e-83 . . . . 11013 1 7 no DBJ BAC65531 . "mKIAA0325 protein [Mus musculus]" . . . . . 95.10 1999 100.00 100.00 1.68e-83 . . . . 11013 1 8 no DBJ BAE90822 . "unnamed protein product [Macaca fascicularis]" . . . . . 95.10 670 100.00 100.00 1.64e-87 . . . . 11013 1 9 no DBJ BAG06711 . "DYNC1H1 variant protein [Homo sapiens]" . . . . . 95.10 4646 100.00 100.00 2.58e-83 . . . . 11013 1 10 no GB AAA41103 . "dynein heavy chain [Rattus norvegicus]" . . . . . 95.10 4644 100.00 100.00 2.58e-83 . . . . 11013 1 11 no GB AAF91078 . "cytoplasmic dynein heavy chain [Mus musculus]" . . . . . 95.10 4644 100.00 100.00 2.53e-83 . . . . 11013 1 12 no GB AAT74625 . "dynein, cytoplasmic, heavy polypeptide 1 [Homo sapiens]" . . . . . 95.10 4646 100.00 100.00 2.58e-83 . . . . 11013 1 13 no GB ACI03592 . "dynein microtubule-binding domain (103:96) fused with seryl-tRNA synthetase-monomer [synthetic construct]" . . . . . 95.10 707 100.00 100.00 2.98e-87 . . . . 11013 1 14 no GB ACI03593 . "dynein microtubule-binding domain (100:96) fused to seryl-tRNA synthase-monomer [synthetic construct]" . . . . . 95.10 704 100.00 100.00 2.45e-87 . . . . 11013 1 15 no REF NP_001193067 . "cytoplasmic dynein 1 heavy chain 1 [Bos taurus]" . . . . . 95.10 4645 100.00 100.00 2.81e-83 . . . . 11013 1 16 no REF NP_001367 . "cytoplasmic dynein 1 heavy chain 1 [Homo sapiens]" . . . . . 95.10 4646 100.00 100.00 2.58e-83 . . . . 11013 1 17 no REF NP_062099 . "cytoplasmic dynein 1 heavy chain 1 [Rattus norvegicus]" . . . . . 95.10 4644 100.00 100.00 2.58e-83 . . . . 11013 1 18 no REF NP_084514 . "cytoplasmic dynein 1 heavy chain 1 [Mus musculus]" . . . . . 95.10 4644 100.00 100.00 2.53e-83 . . . . 11013 1 19 no REF XP_001112455 . "PREDICTED: cytoplasmic dynein 1 heavy chain 1-like [Macaca mulatta]" . . . . . 95.10 4524 100.00 100.00 2.81e-83 . . . . 11013 1 20 no SP P38650 . "RecName: Full=Cytoplasmic dynein 1 heavy chain 1; AltName: Full=Cytoplasmic dynein heavy chain 1; AltName: Full=Dynein heavy ch" . . . . . 95.10 4644 100.00 100.00 2.48e-83 . . . . 11013 1 21 no SP Q14204 . "RecName: Full=Cytoplasmic dynein 1 heavy chain 1; AltName: Full=Cytoplasmic dynein heavy chain 1; AltName: Full=Dynein heavy ch" . . . . . 95.10 4646 100.00 100.00 2.58e-83 . . . . 11013 1 22 no SP Q9JHU4 . "RecName: Full=Cytoplasmic dynein 1 heavy chain 1; AltName: Full=Cytoplasmic dynein heavy chain 1; AltName: Full=Dynein heavy ch" . . . . . 95.10 4644 100.00 100.00 2.53e-83 . . . . 11013 1 23 no TPG DAA17428 . "TPA: cytoplasmic dynein 1 heavy chain 1-like [Bos taurus]" . . . . . 95.10 4645 100.00 100.00 2.81e-83 . . . . 11013 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 . 11013 1 2 . GLU . 11013 1 3 . ASP . 11013 1 4 . LEU . 11013 1 5 . ASP . 11013 1 6 . LYS . 11013 1 7 . VAL . 11013 1 8 . GLU . 11013 1 9 . PRO . 11013 1 10 . ALA . 11013 1 11 . VAL . 11013 1 12 . ILE . 11013 1 13 . GLU . 11013 1 14 . ALA . 11013 1 15 . GLN . 11013 1 16 . ASN . 11013 1 17 . ALA . 11013 1 18 . VAL . 11013 1 19 . LYS . 11013 1 20 . SER . 11013 1 21 . ILE . 11013 1 22 . LYS . 11013 1 23 . LYS . 11013 1 24 . GLN . 11013 1 25 . HIS . 11013 1 26 . LEU . 11013 1 27 . VAL . 11013 1 28 . GLU . 11013 1 29 . VAL . 11013 1 30 . ARG . 11013 1 31 . SER . 11013 1 32 . MET . 11013 1 33 . ALA . 11013 1 34 . ASN . 11013 1 35 . PRO . 11013 1 36 . PRO . 11013 1 37 . ALA . 11013 1 38 . ALA . 11013 1 39 . VAL . 11013 1 40 . LYS . 11013 1 41 . LEU . 11013 1 42 . ALA . 11013 1 43 . LEU . 11013 1 44 . GLU . 11013 1 45 . SER . 11013 1 46 . ILE . 11013 1 47 . CYS . 11013 1 48 . LEU . 11013 1 49 . LEU . 11013 1 50 . LEU . 11013 1 51 . GLY . 11013 1 52 . GLU . 11013 1 53 . SER . 11013 1 54 . THR . 11013 1 55 . THR . 11013 1 56 . ASP . 11013 1 57 . TRP . 11013 1 58 . LYS . 11013 1 59 . GLN . 11013 1 60 . ILE . 11013 1 61 . ARG . 11013 1 62 . SER . 11013 1 63 . ILE . 11013 1 64 . ILE . 11013 1 65 . MET . 11013 1 66 . ARG . 11013 1 67 . GLU . 11013 1 68 . ASN . 11013 1 69 . PHE . 11013 1 70 . ILE . 11013 1 71 . PRO . 11013 1 72 . THR . 11013 1 73 . ILE . 11013 1 74 . VAL . 11013 1 75 . ASN . 11013 1 76 . PHE . 11013 1 77 . SER . 11013 1 78 . ALA . 11013 1 79 . GLU . 11013 1 80 . GLU . 11013 1 81 . ILE . 11013 1 82 . SER . 11013 1 83 . ASP . 11013 1 84 . ALA . 11013 1 85 . ILE . 11013 1 86 . ARG . 11013 1 87 . GLU . 11013 1 88 . LYS . 11013 1 89 . MET . 11013 1 90 . LYS . 11013 1 91 . LYS . 11013 1 92 . ASN . 11013 1 93 . TYR . 11013 1 94 . MET . 11013 1 95 . SER . 11013 1 96 . ASN . 11013 1 97 . PRO . 11013 1 98 . SER . 11013 1 99 . TYR . 11013 1 100 . ASN . 11013 1 101 . TYR . 11013 1 102 . GLU . 11013 1 103 . ILE . 11013 1 104 . VAL . 11013 1 105 . ASN . 11013 1 106 . ARG . 11013 1 107 . ALA . 11013 1 108 . SER . 11013 1 109 . LEU . 11013 1 110 . ALA . 11013 1 111 . CYS . 11013 1 112 . GLY . 11013 1 113 . PRO . 11013 1 114 . MET . 11013 1 115 . VAL . 11013 1 116 . LYS . 11013 1 117 . TRP . 11013 1 118 . ALA . 11013 1 119 . ILE . 11013 1 120 . ALA . 11013 1 121 . GLN . 11013 1 122 . LEU . 11013 1 123 . ASN . 11013 1 124 . TYR . 11013 1 125 . ALA . 11013 1 126 . ASP . 11013 1 127 . MET . 11013 1 128 . LEU . 11013 1 129 . LYS . 11013 1 130 . ARG . 11013 1 131 . VAL . 11013 1 132 . GLU . 11013 1 133 . PRO . 11013 1 134 . LEU . 11013 1 135 . ARG . 11013 1 136 . ASN . 11013 1 137 . GLU . 11013 1 138 . HIS . 11013 1 139 . HIS . 11013 1 140 . HIS . 11013 1 141 . HIS . 11013 1 142 . HIS . 11013 1 143 . HIS . 11013 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 11013 1 . GLU 2 2 11013 1 . ASP 3 3 11013 1 . LEU 4 4 11013 1 . ASP 5 5 11013 1 . LYS 6 6 11013 1 . VAL 7 7 11013 1 . GLU 8 8 11013 1 . PRO 9 9 11013 1 . ALA 10 10 11013 1 . VAL 11 11 11013 1 . ILE 12 12 11013 1 . GLU 13 13 11013 1 . ALA 14 14 11013 1 . GLN 15 15 11013 1 . ASN 16 16 11013 1 . ALA 17 17 11013 1 . VAL 18 18 11013 1 . LYS 19 19 11013 1 . SER 20 20 11013 1 . ILE 21 21 11013 1 . LYS 22 22 11013 1 . LYS 23 23 11013 1 . GLN 24 24 11013 1 . HIS 25 25 11013 1 . LEU 26 26 11013 1 . VAL 27 27 11013 1 . GLU 28 28 11013 1 . VAL 29 29 11013 1 . ARG 30 30 11013 1 . SER 31 31 11013 1 . MET 32 32 11013 1 . ALA 33 33 11013 1 . ASN 34 34 11013 1 . PRO 35 35 11013 1 . PRO 36 36 11013 1 . ALA 37 37 11013 1 . ALA 38 38 11013 1 . VAL 39 39 11013 1 . LYS 40 40 11013 1 . LEU 41 41 11013 1 . ALA 42 42 11013 1 . LEU 43 43 11013 1 . GLU 44 44 11013 1 . SER 45 45 11013 1 . ILE 46 46 11013 1 . CYS 47 47 11013 1 . LEU 48 48 11013 1 . LEU 49 49 11013 1 . LEU 50 50 11013 1 . GLY 51 51 11013 1 . GLU 52 52 11013 1 . SER 53 53 11013 1 . THR 54 54 11013 1 . THR 55 55 11013 1 . ASP 56 56 11013 1 . TRP 57 57 11013 1 . LYS 58 58 11013 1 . GLN 59 59 11013 1 . ILE 60 60 11013 1 . ARG 61 61 11013 1 . SER 62 62 11013 1 . ILE 63 63 11013 1 . ILE 64 64 11013 1 . MET 65 65 11013 1 . ARG 66 66 11013 1 . GLU 67 67 11013 1 . ASN 68 68 11013 1 . PHE 69 69 11013 1 . ILE 70 70 11013 1 . PRO 71 71 11013 1 . THR 72 72 11013 1 . ILE 73 73 11013 1 . VAL 74 74 11013 1 . ASN 75 75 11013 1 . PHE 76 76 11013 1 . SER 77 77 11013 1 . ALA 78 78 11013 1 . GLU 79 79 11013 1 . GLU 80 80 11013 1 . ILE 81 81 11013 1 . SER 82 82 11013 1 . ASP 83 83 11013 1 . ALA 84 84 11013 1 . ILE 85 85 11013 1 . ARG 86 86 11013 1 . GLU 87 87 11013 1 . LYS 88 88 11013 1 . MET 89 89 11013 1 . LYS 90 90 11013 1 . LYS 91 91 11013 1 . ASN 92 92 11013 1 . TYR 93 93 11013 1 . MET 94 94 11013 1 . SER 95 95 11013 1 . ASN 96 96 11013 1 . PRO 97 97 11013 1 . SER 98 98 11013 1 . TYR 99 99 11013 1 . ASN 100 100 11013 1 . TYR 101 101 11013 1 . GLU 102 102 11013 1 . ILE 103 103 11013 1 . VAL 104 104 11013 1 . ASN 105 105 11013 1 . ARG 106 106 11013 1 . ALA 107 107 11013 1 . SER 108 108 11013 1 . LEU 109 109 11013 1 . ALA 110 110 11013 1 . CYS 111 111 11013 1 . GLY 112 112 11013 1 . PRO 113 113 11013 1 . MET 114 114 11013 1 . VAL 115 115 11013 1 . LYS 116 116 11013 1 . TRP 117 117 11013 1 . ALA 118 118 11013 1 . ILE 119 119 11013 1 . ALA 120 120 11013 1 . GLN 121 121 11013 1 . LEU 122 122 11013 1 . ASN 123 123 11013 1 . TYR 124 124 11013 1 . ALA 125 125 11013 1 . ASP 126 126 11013 1 . MET 127 127 11013 1 . LEU 128 128 11013 1 . LYS 129 129 11013 1 . ARG 130 130 11013 1 . VAL 131 131 11013 1 . GLU 132 132 11013 1 . PRO 133 133 11013 1 . LEU 134 134 11013 1 . ARG 135 135 11013 1 . ASN 136 136 11013 1 . GLU 137 137 11013 1 . HIS 138 138 11013 1 . HIS 139 139 11013 1 . HIS 140 140 11013 1 . HIS 141 141 11013 1 . HIS 142 142 11013 1 . HIS 143 143 11013 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 11013 _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 $DS(8:5) . 10090 organism . 'Mus musculus' Mouse . . Eukaryota Metazoa Mus musculus . . . . . . . . . . . . . . . . . . . . . 11013 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 11013 _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 $DS(8:5) . 'recombinant technology' 'Escherichia coli' . . 469008 Escherichia coli 'BL21-CodonPlus (DE3)' . . . . . . . . . . . . . . . pET17b . . . . . . 11013 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 11013 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _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 DS(8:5) '[U-100% 13C; U-100% 15N]' . . 1 $DS(8:5) . . 0.13 . . mM . . . . 11013 1 2 'potassium phosphate' 'natural abundance' . . . . . . 10 . . mM . . . . 11013 1 3 'potassium chloride' 'natural abundance' . . . . . . 75 . . mM . . . . 11013 1 4 D2O 'natural abundance' . . . . . . 10 . . % . . . . 11013 1 5 H2O 'natural abundance' . . . . . . 90 . . % . . . . 11013 1 6 'sodium azide' 'natural abundance' . . . . . . 0.02 . . % . . . . 11013 1 7 DTT 'natural abundance' . . . . . . 1 . . mM . . . . 11013 1 8 p-ABSF 'natural abundance' . . . . . . 0.1 . . mM . . . . 11013 1 9 sucrose 'natural abundance' . . . . . . 5 . . % . . . . 11013 1 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 11013 _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' 85 . mM 11013 1 pH 6.7 . pH 11013 1 pressure 1 . atm 11013 1 temperature 293 . K 11013 1 stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Software.Sf_category software _Software.Sf_framecode NMRPipe _Software.Entry_ID 11013 _Software.ID 1 _Software.Name NMRPipe _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . 11013 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 11013 1 stop_ save_ save_SPARKY _Software.Sf_category software _Software.Sf_framecode SPARKY _Software.Entry_ID 11013 _Software.ID 2 _Software.Name SPARKY _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Goddard . . 11013 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 11013 2 'chemical shift calculation' 11013 2 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 11013 _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_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 11013 _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 'equipped with a Cold Probe (Varian)' . . 11013 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 11013 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 '2D 1H-15N HSQC' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 11013 1 2 '3D CBCA(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 11013 1 3 '3D C(CO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 11013 1 4 '3D HNCO' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 11013 1 5 '3D HNCA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 11013 1 6 '3D HNCACB' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 11013 1 7 '3D HN(CO)CA' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 11013 1 8 '3D H(CCO)NH' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 11013 1 9 '3D 1H-15N TOCSY' no . . . . . . . . . . 1 $sample_1 isotropic . . 1 $sample_conditions_1 . . . 1 $spectrometer_1 . . . . . . . . . . . . . . . . 11013 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 11013 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.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 . indirect 0.251449530 . . . . . . . . . 11013 1 H 1 DSS 'methyl protons' . . . . ppm 0.00 internal direct 1.000000000 . . . . . . . . . 11013 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 . indirect 0.101329118 . . . . . . . . . 11013 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 11013 _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 'The list provides data from natural conformation protein' _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 '2D 1H-15N HSQC' 1 $sample_1 isotropic 11013 1 2 '3D CBCA(CO)NH' 1 $sample_1 isotropic 11013 1 3 '3D C(CO)NH' 1 $sample_1 isotropic 11013 1 4 '3D HNCO' 1 $sample_1 isotropic 11013 1 5 '3D HNCA' 1 $sample_1 isotropic 11013 1 6 '3D HNCACB' 1 $sample_1 isotropic 11013 1 7 '3D HN(CO)CA' 1 $sample_1 isotropic 11013 1 8 '3D H(CCO)NH' 1 $sample_1 isotropic 11013 1 9 '3D 1H-15N TOCSY' 1 $sample_1 isotropic 11013 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 GLU HA H 1 4.547 . . 1 . . . . 2 Glu HA . 11013 1 2 . 1 1 2 2 GLU C C 13 175.8 . . 1 . . . . 2 Glu C . 11013 1 3 . 1 1 2 2 GLU CA C 13 57.18 0.05 . 1 . . . . 2 Glu CA . 11013 1 4 . 1 1 2 2 GLU CB C 13 31.22 0.09 . 1 . . . . 2 Glu CB . 11013 1 5 . 1 1 3 3 ASP H H 1 8.711 0.003 . 1 . . . . 3 Asp H . 11013 1 6 . 1 1 3 3 ASP HA H 1 4.848 . . 1 . . . . 3 Asp HA . 11013 1 7 . 1 1 3 3 ASP C C 13 177.2 . . 1 . . . . 3 Asp C . 11013 1 8 . 1 1 3 3 ASP CA C 13 55.59 0.15 . 1 . . . . 3 Asp CA . 11013 1 9 . 1 1 3 3 ASP CB C 13 41.74 0.09 . 1 . . . . 3 Asp CB . 11013 1 10 . 1 1 3 3 ASP N N 15 121.00 0.05 . 1 . . . . 3 Asp N . 11013 1 11 . 1 1 4 4 LEU H H 1 8.551 0.003 . 1 . . . . 4 Leu H . 11013 1 12 . 1 1 4 4 LEU HA H 1 4.375 . . 1 . . . . 4 Leu HA . 11013 1 13 . 1 1 4 4 LEU C C 13 178.1 . . 1 . . . . 4 Leu C . 11013 1 14 . 1 1 4 4 LEU CA C 13 57.23 0.05 . 1 . . . . 4 Leu CA . 11013 1 15 . 1 1 4 4 LEU CB C 13 42.37 0.25 . 1 . . . . 4 Leu CB . 11013 1 16 . 1 1 4 4 LEU N N 15 122.24 0.02 . 1 . . . . 4 Leu N . 11013 1 17 . 1 1 5 5 ASP H H 1 8.507 0.004 . 1 . . . . 5 Asp H . 11013 1 18 . 1 1 5 5 ASP HA H 1 4.713 . . 1 . . . . 5 Asp HA . 11013 1 19 . 1 1 5 5 ASP C C 13 176.8 . . 1 . . . . 5 Asp C . 11013 1 20 . 1 1 5 5 ASP CA C 13 56.30 0.21 . 1 . . . . 5 Asp CA . 11013 1 21 . 1 1 5 5 ASP CB C 13 41.30 0.09 . 1 . . . . 5 Asp CB . 11013 1 22 . 1 1 5 5 ASP N N 15 118.43 0.04 . 1 . . . . 5 Asp N . 11013 1 23 . 1 1 6 6 LYS H H 1 8.056 0.004 . 1 . . . . 6 Lys H . 11013 1 24 . 1 1 6 6 LYS HA H 1 4.537 . . 1 . . . . 6 Lys HA . 11013 1 25 . 1 1 6 6 LYS CA C 13 57.37 . . 1 . . . . 6 Lys CA . 11013 1 26 . 1 1 6 6 LYS N N 15 117.99 0.03 . 1 . . . . 6 Lys N . 11013 1 27 . 1 1 11 11 VAL C C 13 177.1 . . 1 . . . . 11 Val C . 11013 1 28 . 1 1 11 11 VAL CA C 13 67.49 0.10 . 1 . . . . 11 Val CA . 11013 1 29 . 1 1 11 11 VAL CB C 13 32.98 0.18 . 1 . . . . 11 Val CB . 11013 1 30 . 1 1 12 12 ILE H H 1 7.637 0.011 . 1 . . . . 12 Ile H . 11013 1 31 . 1 1 12 12 ILE C C 13 178.9 . . 1 . . . . 12 Ile C . 11013 1 32 . 1 1 12 12 ILE CA C 13 64.70 0.25 . 1 . . . . 12 Ile CA . 11013 1 33 . 1 1 12 12 ILE CB C 13 38.55 0.07 . 1 . . . . 12 Ile CB . 11013 1 34 . 1 1 12 12 ILE N N 15 121.05 0.07 . 1 . . . . 12 Ile N . 11013 1 35 . 1 1 13 13 GLU H H 1 8.436 0.007 . 1 . . . . 13 Glu H . 11013 1 36 . 1 1 13 13 GLU HA H 1 4.280 . . 1 . . . . 13 Glu HA . 11013 1 37 . 1 1 13 13 GLU C C 13 179.8 . . 1 . . . . 13 Glu C . 11013 1 38 . 1 1 13 13 GLU CA C 13 60.10 0.19 . 1 . . . . 13 Glu CA . 11013 1 39 . 1 1 13 13 GLU CB C 13 30.45 0.01 . 1 . . . . 13 Glu CB . 11013 1 40 . 1 1 13 13 GLU N N 15 119.10 0.07 . 1 . . . . 13 Glu N . 11013 1 41 . 1 1 14 14 ALA H H 1 8.136 0.001 . 1 . . . . 14 Ala H . 11013 1 42 . 1 1 14 14 ALA C C 13 180.0 . . 1 . . . . 14 Ala C . 11013 1 43 . 1 1 14 14 ALA CA C 13 55.85 0.14 . 1 . . . . 14 Ala CA . 11013 1 44 . 1 1 14 14 ALA CB C 13 19.22 0.37 . 1 . . . . 14 Ala CB . 11013 1 45 . 1 1 14 14 ALA N N 15 121.73 0.02 . 1 . . . . 14 Ala N . 11013 1 46 . 1 1 15 15 GLN H H 1 9.200 0.004 . 1 . . . . 15 Gln H . 11013 1 47 . 1 1 15 15 GLN C C 13 178.4 . . 1 . . . . 15 Gln C . 11013 1 48 . 1 1 15 15 GLN CA C 13 60.72 0.08 . 1 . . . . 15 Gln CA . 11013 1 49 . 1 1 15 15 GLN CB C 13 29.71 0.04 . 1 . . . . 15 Gln CB . 11013 1 50 . 1 1 15 15 GLN N N 15 118.96 0.04 . 1 . . . . 15 Gln N . 11013 1 51 . 1 1 16 16 ASN H H 1 8.468 0.007 . 1 . . . . 16 Asn H . 11013 1 52 . 1 1 16 16 ASN C C 13 178.0 . . 1 . . . . 16 Asn C . 11013 1 53 . 1 1 16 16 ASN CA C 13 56.71 0.15 . 1 . . . . 16 Asn CA . 11013 1 54 . 1 1 16 16 ASN CB C 13 38.37 0.13 . 1 . . . . 16 Asn CB . 11013 1 55 . 1 1 16 16 ASN N N 15 117.28 0.09 . 1 . . . . 16 Asn N . 11013 1 56 . 1 1 17 17 ALA H H 1 8.252 0.002 . 1 . . . . 17 Ala H . 11013 1 57 . 1 1 17 17 ALA C C 13 180.7 . . 1 . . . . 17 Ala C . 11013 1 58 . 1 1 17 17 ALA CA C 13 55.70 0.06 . 1 . . . . 17 Ala CA . 11013 1 59 . 1 1 17 17 ALA CB C 13 18.41 0.17 . 1 . . . . 17 Ala CB . 11013 1 60 . 1 1 17 17 ALA N N 15 124.05 0.08 . 1 . . . . 17 Ala N . 11013 1 61 . 1 1 18 18 VAL H H 1 8.378 0.005 . 1 . . . . 18 Val H . 11013 1 62 . 1 1 18 18 VAL HA H 1 5.002 . . 1 . . . . 18 Val HA . 11013 1 63 . 1 1 18 18 VAL C C 13 177.8 . . 1 . . . . 18 Val C . 11013 1 64 . 1 1 18 18 VAL CA C 13 66.37 0.13 . 1 . . . . 18 Val CA . 11013 1 65 . 1 1 18 18 VAL CB C 13 32.35 . . 1 . . . . 18 Val CB . 11013 1 66 . 1 1 18 18 VAL N N 15 119.77 0.04 . 1 . . . . 18 Val N . 11013 1 67 . 1 1 19 19 LYS H H 1 8.288 0.006 . 1 . . . . 19 Lys H . 11013 1 68 . 1 1 19 19 LYS C C 13 177.5 . . 1 . . . . 19 Lys C . 11013 1 69 . 1 1 19 19 LYS CA C 13 59.89 0.10 . 1 . . . . 19 Lys CA . 11013 1 70 . 1 1 19 19 LYS CB C 13 33.49 0.18 . 1 . . . . 19 Lys CB . 11013 1 71 . 1 1 19 19 LYS N N 15 118.10 0.04 . 1 . . . . 19 Lys N . 11013 1 72 . 1 1 20 20 SER H H 1 7.504 0.003 . 1 . . . . 20 Ser H . 11013 1 73 . 1 1 20 20 SER HA H 1 4.568 . . 1 . . . . 20 Ser HA . 11013 1 74 . 1 1 20 20 SER C C 13 174.2 . . 1 . . . . 20 Ser C . 11013 1 75 . 1 1 20 20 SER CA C 13 59.38 0.07 . 1 . . . . 20 Ser CA . 11013 1 76 . 1 1 20 20 SER CB C 13 64.89 0.16 . 1 . . . . 20 Ser CB . 11013 1 77 . 1 1 20 20 SER N N 15 111.17 0.02 . 1 . . . . 20 Ser N . 11013 1 78 . 1 1 21 21 ILE H H 1 7.628 0.005 . 1 . . . . 21 Ile H . 11013 1 79 . 1 1 21 21 ILE C C 13 177.0 . . 1 . . . . 21 Ile C . 11013 1 80 . 1 1 21 21 ILE CA C 13 64.05 0.04 . 1 . . . . 21 Ile CA . 11013 1 81 . 1 1 21 21 ILE CB C 13 39.70 0.18 . 1 . . . . 21 Ile CB . 11013 1 82 . 1 1 21 21 ILE N N 15 124.04 0.05 . 1 . . . . 21 Ile N . 11013 1 83 . 1 1 22 22 LYS H H 1 9.136 0.007 . 1 . . . . 22 Lys H . 11013 1 84 . 1 1 22 22 LYS C C 13 178.3 . . 1 . . . . 22 Lys C . 11013 1 85 . 1 1 22 22 LYS CA C 13 56.53 0.07 . 1 . . . . 22 Lys CA . 11013 1 86 . 1 1 22 22 LYS CB C 13 33.42 0.16 . 1 . . . . 22 Lys CB . 11013 1 87 . 1 1 22 22 LYS N N 15 129.36 0.02 . 1 . . . . 22 Lys N . 11013 1 88 . 1 1 23 23 LYS H H 1 9.076 0.007 . 1 . . . . 23 Lys H . 11013 1 89 . 1 1 23 23 LYS HA H 1 5.046 . . 1 . . . . 23 Lys HA . 11013 1 90 . 1 1 23 23 LYS C C 13 179.1 . . 1 . . . . 23 Lys C . 11013 1 91 . 1 1 23 23 LYS CA C 13 60.85 0.19 . 1 . . . . 23 Lys CA . 11013 1 92 . 1 1 23 23 LYS CB C 13 32.63 0.09 . 1 . . . . 23 Lys CB . 11013 1 93 . 1 1 23 23 LYS N N 15 125.20 0.05 . 1 . . . . 23 Lys N . 11013 1 94 . 1 1 24 24 GLN H H 1 9.157 0.005 . 1 . . . . 24 Gln H . 11013 1 95 . 1 1 24 24 GLN HA H 1 5.035 . . 1 . . . . 24 Gln HA . 11013 1 96 . 1 1 24 24 GLN C C 13 178.1 . . 1 . . . . 24 Gln C . 11013 1 97 . 1 1 24 24 GLN CA C 13 59.28 0.17 . 1 . . . . 24 Gln CA . 11013 1 98 . 1 1 24 24 GLN CB C 13 28.59 0.08 . 1 . . . . 24 Gln CB . 11013 1 99 . 1 1 24 24 GLN N N 15 115.66 0.02 . 1 . . . . 24 Gln N . 11013 1 100 . 1 1 25 25 HIS H H 1 7.457 0.006 . 1 . . . . 25 His H . 11013 1 101 . 1 1 25 25 HIS C C 13 179.3 . . 1 . . . . 25 His C . 11013 1 102 . 1 1 25 25 HIS CA C 13 58.73 0.11 . 1 . . . . 25 His CA . 11013 1 103 . 1 1 25 25 HIS CB C 13 31.87 0.15 . 1 . . . . 25 His CB . 11013 1 104 . 1 1 25 25 HIS N N 15 118.29 0.07 . 1 . . . . 25 His N . 11013 1 105 . 1 1 26 26 LEU H H 1 7.809 0.004 . 1 . . . . 26 Leu H . 11013 1 106 . 1 1 26 26 LEU C C 13 178.5 . . 1 . . . . 26 Leu C . 11013 1 107 . 1 1 26 26 LEU CA C 13 58.38 0.09 . 1 . . . . 26 Leu CA . 11013 1 108 . 1 1 26 26 LEU CB C 13 42.26 0.15 . 1 . . . . 26 Leu CB . 11013 1 109 . 1 1 26 26 LEU N N 15 122.95 0.04 . 1 . . . . 26 Leu N . 11013 1 110 . 1 1 27 27 VAL H H 1 8.638 0.003 . 1 . . . . 27 Val H . 11013 1 111 . 1 1 27 27 VAL C C 13 179.0 . . 1 . . . . 27 Val C . 11013 1 112 . 1 1 27 27 VAL CA C 13 67.32 0.17 . 1 . . . . 27 Val CA . 11013 1 113 . 1 1 27 27 VAL CB C 13 32.31 0.16 . 1 . . . . 27 Val CB . 11013 1 114 . 1 1 27 27 VAL N N 15 120.66 0.03 . 1 . . . . 27 Val N . 11013 1 115 . 1 1 28 28 GLU H H 1 7.962 0.003 . 1 . . . . 28 Glu H . 11013 1 116 . 1 1 28 28 GLU HA H 1 4.283 . . 1 . . . . 28 Glu HA . 11013 1 117 . 1 1 28 28 GLU C C 13 179.2 . . 1 . . . . 28 Glu C . 11013 1 118 . 1 1 28 28 GLU CA C 13 60.40 0.07 . 1 . . . . 28 Glu CA . 11013 1 119 . 1 1 28 28 GLU CB C 13 30.77 0.08 . 1 . . . . 28 Glu CB . 11013 1 120 . 1 1 28 28 GLU N N 15 119.16 0.02 . 1 . . . . 28 Glu N . 11013 1 121 . 1 1 29 29 VAL H H 1 7.367 0.003 . 1 . . . . 29 Val H . 11013 1 122 . 1 1 29 29 VAL HA H 1 4.574 . . 1 . . . . 29 Val HA . 11013 1 123 . 1 1 29 29 VAL C C 13 177.4 . . 1 . . . . 29 Val C . 11013 1 124 . 1 1 29 29 VAL CA C 13 65.60 0.17 . 1 . . . . 29 Val CA . 11013 1 125 . 1 1 29 29 VAL CB C 13 32.45 0.09 . 1 . . . . 29 Val CB . 11013 1 126 . 1 1 29 29 VAL N N 15 116.66 0.04 . 1 . . . . 29 Val N . 11013 1 127 . 1 1 30 30 ARG H H 1 8.270 0.002 . 1 . . . . 30 Arg H . 11013 1 128 . 1 1 30 30 ARG HA H 1 3.996 . . 1 . . . . 30 Arg HA . 11013 1 129 . 1 1 30 30 ARG C C 13 177.0 . . 1 . . . . 30 Arg C . 11013 1 130 . 1 1 30 30 ARG CA C 13 59.80 0.09 . 1 . . . . 30 Arg CA . 11013 1 131 . 1 1 30 30 ARG CB C 13 30.90 0.07 . 1 . . . . 30 Arg CB . 11013 1 132 . 1 1 30 30 ARG N N 15 119.13 0.04 . 1 . . . . 30 Arg N . 11013 1 133 . 1 1 31 31 SER H H 1 7.887 0.004 . 1 . . . . 31 Ser H . 11013 1 134 . 1 1 31 31 SER HA H 1 4.582 . . 1 . . . . 31 Ser HA . 11013 1 135 . 1 1 31 31 SER C C 13 174.0 . . 1 . . . . 31 Ser C . 11013 1 136 . 1 1 31 31 SER CA C 13 59.68 0.10 . 1 . . . . 31 Ser CA . 11013 1 137 . 1 1 31 31 SER CB C 13 64.73 0.16 . 1 . . . . 31 Ser CB . 11013 1 138 . 1 1 31 31 SER N N 15 111.31 0.01 . 1 . . . . 31 Ser N . 11013 1 139 . 1 1 32 32 MET H H 1 7.771 0.005 . 1 . . . . 32 Met H . 11013 1 140 . 1 1 32 32 MET C C 13 175.4 . . 1 . . . . 32 Met C . 11013 1 141 . 1 1 32 32 MET CA C 13 57.71 0.11 . 1 . . . . 32 Met CA . 11013 1 142 . 1 1 32 32 MET CB C 13 33.69 0.23 . 1 . . . . 32 Met CB . 11013 1 143 . 1 1 32 32 MET N N 15 121.82 0.03 . 1 . . . . 32 Met N . 11013 1 144 . 1 1 33 33 ALA H H 1 8.774 0.006 . 1 . . . . 33 Ala H . 11013 1 145 . 1 1 33 33 ALA HA H 1 4.976 . . 1 . . . . 33 Ala HA . 11013 1 146 . 1 1 33 33 ALA C C 13 177.9 . . 1 . . . . 33 Ala C . 11013 1 147 . 1 1 33 33 ALA CA C 13 54.60 0.15 . 1 . . . . 33 Ala CA . 11013 1 148 . 1 1 33 33 ALA CB C 13 20.05 0.23 . 1 . . . . 33 Ala CB . 11013 1 149 . 1 1 33 33 ALA N N 15 128.15 0.01 . 1 . . . . 33 Ala N . 11013 1 150 . 1 1 34 34 ASN H H 1 8.354 0.003 . 1 . . . . 34 Asn H . 11013 1 151 . 1 1 34 34 ASN HA H 1 5.024 . . 1 . . . . 34 Asn HA . 11013 1 152 . 1 1 34 34 ASN CA C 13 51.33 . . 1 . . . . 34 Asn CA . 11013 1 153 . 1 1 34 34 ASN N N 15 114.36 0.03 . 1 . . . . 34 Asn N . 11013 1 154 . 1 1 36 36 PRO HA H 1 4.767 . . 1 . . . . 36 Pro HA . 11013 1 155 . 1 1 36 36 PRO C C 13 177.4 . . 1 . . . . 36 Pro C . 11013 1 156 . 1 1 36 36 PRO CA C 13 62.81 0.04 . 1 . . . . 36 Pro CA . 11013 1 157 . 1 1 36 36 PRO CB C 13 33.08 0.13 . 1 . . . . 36 Pro CB . 11013 1 158 . 1 1 37 37 ALA H H 1 9.069 0.004 . 1 . . . . 37 Ala H . 11013 1 159 . 1 1 37 37 ALA HA H 1 5.013 . . 1 . . . . 37 Ala HA . 11013 1 160 . 1 1 37 37 ALA C C 13 180.2 . . 1 . . . . 37 Ala C . 11013 1 161 . 1 1 37 37 ALA CA C 13 56.55 0.10 . 1 . . . . 37 Ala CA . 11013 1 162 . 1 1 37 37 ALA CB C 13 18.47 0.21 . 1 . . . . 37 Ala CB . 11013 1 163 . 1 1 37 37 ALA N N 15 127.32 0.02 . 1 . . . . 37 Ala N . 11013 1 164 . 1 1 38 38 ALA H H 1 9.202 0.004 . 1 . . . . 38 Ala H . 11013 1 165 . 1 1 38 38 ALA HA H 1 5.039 . . 1 . . . . 38 Ala HA . 11013 1 166 . 1 1 38 38 ALA C C 13 179.6 . . 1 . . . . 38 Ala C . 11013 1 167 . 1 1 38 38 ALA CA C 13 56.09 0.16 . 1 . . . . 38 Ala CA . 11013 1 168 . 1 1 38 38 ALA CB C 13 19.53 0.30 . 1 . . . . 38 Ala CB . 11013 1 169 . 1 1 38 38 ALA N N 15 117.13 0.02 . 1 . . . . 38 Ala N . 11013 1 170 . 1 1 39 39 VAL H H 1 7.025 0.002 . 1 . . . . 39 Val H . 11013 1 171 . 1 1 39 39 VAL C C 13 176.8 . . 1 . . . . 39 Val C . 11013 1 172 . 1 1 39 39 VAL CA C 13 66.10 0.19 . 1 . . . . 39 Val CA . 11013 1 173 . 1 1 39 39 VAL CB C 13 33.06 0.15 . 1 . . . . 39 Val CB . 11013 1 174 . 1 1 39 39 VAL N N 15 114.92 0.02 . 1 . . . . 39 Val N . 11013 1 175 . 1 1 40 40 LYS H H 1 7.691 0.002 . 1 . . . . 40 Lys H . 11013 1 176 . 1 1 40 40 LYS C C 13 177.8 . . 1 . . . . 40 Lys C . 11013 1 177 . 1 1 40 40 LYS CA C 13 61.56 0.11 . 1 . . . . 40 Lys CA . 11013 1 178 . 1 1 40 40 LYS CB C 13 33.21 0.22 . 1 . . . . 40 Lys CB . 11013 1 179 . 1 1 40 40 LYS N N 15 119.68 0.02 . 1 . . . . 40 Lys N . 11013 1 180 . 1 1 41 41 LEU H H 1 8.592 0.004 . 1 . . . . 41 Leu H . 11013 1 181 . 1 1 41 41 LEU C C 13 179.1 . . 1 . . . . 41 Leu C . 11013 1 182 . 1 1 41 41 LEU CA C 13 58.84 0.07 . 1 . . . . 41 Leu CA . 11013 1 183 . 1 1 41 41 LEU CB C 13 43.96 0.14 . 1 . . . . 41 Leu CB . 11013 1 184 . 1 1 41 41 LEU N N 15 117.61 0.09 . 1 . . . . 41 Leu N . 11013 1 185 . 1 1 42 42 ALA H H 1 7.897 0.002 . 1 . . . . 42 Ala H . 11013 1 186 . 1 1 42 42 ALA C C 13 181.5 . . 1 . . . . 42 Ala C . 11013 1 187 . 1 1 42 42 ALA CA C 13 56.35 0.10 . 1 . . . . 42 Ala CA . 11013 1 188 . 1 1 42 42 ALA CB C 13 19.80 0.28 . 1 . . . . 42 Ala CB . 11013 1 189 . 1 1 42 42 ALA N N 15 117.82 0.04 . 1 . . . . 42 Ala N . 11013 1 190 . 1 1 43 43 LEU H H 1 8.754 0.002 . 1 . . . . 43 Leu H . 11013 1 191 . 1 1 43 43 LEU C C 13 179.6 . . 1 . . . . 43 Leu C . 11013 1 192 . 1 1 43 43 LEU CA C 13 58.78 0.11 . 1 . . . . 43 Leu CA . 11013 1 193 . 1 1 43 43 LEU CB C 13 42.58 0.19 . 1 . . . . 43 Leu CB . 11013 1 194 . 1 1 43 43 LEU N N 15 118.39 0.01 . 1 . . . . 43 Leu N . 11013 1 195 . 1 1 44 44 GLU H H 1 9.576 0.002 . 1 . . . . 44 Glu H . 11013 1 196 . 1 1 44 44 GLU HA H 1 4.063 . . 1 . . . . 44 Glu HA . 11013 1 197 . 1 1 44 44 GLU C C 13 180.7 . . 1 . . . . 44 Glu C . 11013 1 198 . 1 1 44 44 GLU CA C 13 61.23 0.06 . 1 . . . . 44 Glu CA . 11013 1 199 . 1 1 44 44 GLU CB C 13 30.90 . . 1 . . . . 44 Glu CB . 11013 1 200 . 1 1 44 44 GLU N N 15 121.72 0.03 . 1 . . . . 44 Glu N . 11013 1 201 . 1 1 45 45 SER H H 1 7.878 0.001 . 1 . . . . 45 Ser H . 11013 1 202 . 1 1 45 45 SER C C 13 173.8 . . 1 . . . . 45 Ser C . 11013 1 203 . 1 1 45 45 SER CA C 13 62.42 0.21 . 1 . . . . 45 Ser CA . 11013 1 204 . 1 1 45 45 SER N N 15 115.84 0.03 . 1 . . . . 45 Ser N . 11013 1 205 . 1 1 46 46 ILE H H 1 7.370 0.004 . 1 . . . . 46 Ile H . 11013 1 206 . 1 1 46 46 ILE C C 13 177.6 . . 1 . . . . 46 Ile C . 11013 1 207 . 1 1 46 46 ILE CA C 13 62.78 0.08 . 1 . . . . 46 Ile CA . 11013 1 208 . 1 1 46 46 ILE CB C 13 36.52 0.16 . 1 . . . . 46 Ile CB . 11013 1 209 . 1 1 46 46 ILE N N 15 123.11 0.02 . 1 . . . . 46 Ile N . 11013 1 210 . 1 1 47 47 CYS H H 1 8.128 0.003 . 1 . . . . 47 Cys H . 11013 1 211 . 1 1 47 47 CYS C C 13 176.0 . . 1 . . . . 47 Cys C . 11013 1 212 . 1 1 47 47 CYS CA C 13 66.01 0.21 . 1 . . . . 47 Cys CA . 11013 1 213 . 1 1 47 47 CYS CB C 13 26.45 0.20 . 1 . . . . 47 Cys CB . 11013 1 214 . 1 1 47 47 CYS N N 15 117.47 0.06 . 1 . . . . 47 Cys N . 11013 1 215 . 1 1 48 48 LEU H H 1 7.929 0.001 . 1 . . . . 48 Leu H . 11013 1 216 . 1 1 48 48 LEU C C 13 179.8 . . 1 . . . . 48 Leu C . 11013 1 217 . 1 1 48 48 LEU CA C 13 58.87 0.04 . 1 . . . . 48 Leu CA . 11013 1 218 . 1 1 48 48 LEU CB C 13 41.83 0.14 . 1 . . . . 48 Leu CB . 11013 1 219 . 1 1 48 48 LEU N N 15 118.97 0.06 . 1 . . . . 48 Leu N . 11013 1 220 . 1 1 49 49 LEU H H 1 7.968 0.002 . 1 . . . . 49 Leu H . 11013 1 221 . 1 1 49 49 LEU C C 13 177.1 . . 1 . . . . 49 Leu C . 11013 1 222 . 1 1 49 49 LEU CA C 13 59.37 0.05 . 1 . . . . 49 Leu CA . 11013 1 223 . 1 1 49 49 LEU CB C 13 42.41 0.22 . 1 . . . . 49 Leu CB . 11013 1 224 . 1 1 49 49 LEU N N 15 120.76 0.02 . 1 . . . . 49 Leu N . 11013 1 225 . 1 1 50 50 LEU H H 1 7.933 0.003 . 1 . . . . 50 Leu H . 11013 1 226 . 1 1 50 50 LEU HA H 1 4.232 . . 1 . . . . 50 Leu HA . 11013 1 227 . 1 1 50 50 LEU C C 13 177.9 . . 1 . . . . 50 Leu C . 11013 1 228 . 1 1 50 50 LEU CA C 13 55.86 0.13 . 1 . . . . 50 Leu CA . 11013 1 229 . 1 1 50 50 LEU CB C 13 42.66 0.14 . 1 . . . . 50 Leu CB . 11013 1 230 . 1 1 50 50 LEU N N 15 112.81 0.03 . 1 . . . . 50 Leu N . 11013 1 231 . 1 1 51 51 GLY H H 1 8.060 0.002 . 1 . . . . 51 Gly H . 11013 1 232 . 1 1 51 51 GLY HA2 H 1 4.433 . . 2 . . . . 51 Gly HA . 11013 1 233 . 1 1 51 51 GLY C C 13 175.1 . . 1 . . . . 51 Gly C . 11013 1 234 . 1 1 51 51 GLY CA C 13 46.45 0.62 . 1 . . . . 51 Gly CA . 11013 1 235 . 1 1 51 51 GLY N N 15 107.02 0.02 . 1 . . . . 51 Gly N . 11013 1 236 . 1 1 52 52 GLU H H 1 8.496 0.005 . 1 . . . . 52 Glu H . 11013 1 237 . 1 1 52 52 GLU HA H 1 4.722 . . 1 . . . . 52 Glu HA . 11013 1 238 . 1 1 52 52 GLU C C 13 175.2 . . 1 . . . . 52 Glu C . 11013 1 239 . 1 1 52 52 GLU CA C 13 55.08 0.13 . 1 . . . . 52 Glu CA . 11013 1 240 . 1 1 52 52 GLU CB C 13 31.23 0.11 . 1 . . . . 52 Glu CB . 11013 1 241 . 1 1 52 52 GLU N N 15 122.03 0.10 . 1 . . . . 52 Glu N . 11013 1 242 . 1 1 53 53 SER H H 1 8.231 0.003 . 1 . . . . 53 Ser H . 11013 1 243 . 1 1 53 53 SER HA H 1 5.042 . . 1 . . . . 53 Ser HA . 11013 1 244 . 1 1 53 53 SER C C 13 174.4 . . 1 . . . . 53 Ser C . 11013 1 245 . 1 1 53 53 SER CA C 13 59.86 0.07 . 1 . . . . 53 Ser CA . 11013 1 246 . 1 1 53 53 SER CB C 13 64.14 0.17 . 1 . . . . 53 Ser CB . 11013 1 247 . 1 1 53 53 SER N N 15 114.43 0.02 . 1 . . . . 53 Ser N . 11013 1 248 . 1 1 54 54 THR H H 1 8.069 0.003 . 1 . . . . 54 Thr H . 11013 1 249 . 1 1 54 54 THR C C 13 172.9 . . 1 . . . . 54 Thr C . 11013 1 250 . 1 1 54 54 THR CA C 13 61.38 0.03 . 1 . . . . 54 Thr CA . 11013 1 251 . 1 1 54 54 THR CB C 13 69.21 0.15 . 1 . . . . 54 Thr CB . 11013 1 252 . 1 1 54 54 THR N N 15 118.30 0.02 . 1 . . . . 54 Thr N . 11013 1 253 . 1 1 55 55 THR H H 1 8.660 0.003 . 1 . . . . 55 Thr H . 11013 1 254 . 1 1 55 55 THR HA H 1 4.754 . . 1 . . . . 55 Thr HA . 11013 1 255 . 1 1 55 55 THR C C 13 174.0 . . 1 . . . . 55 Thr C . 11013 1 256 . 1 1 55 55 THR CA C 13 61.63 0.08 . 1 . . . . 55 Thr CA . 11013 1 257 . 1 1 55 55 THR CB C 13 69.86 0.36 . 1 . . . . 55 Thr CB . 11013 1 258 . 1 1 55 55 THR N N 15 115.19 0.07 . 1 . . . . 55 Thr N . 11013 1 259 . 1 1 56 56 ASP H H 1 8.641 0.007 . 1 . . . . 56 Asp H . 11013 1 260 . 1 1 56 56 ASP C C 13 176.9 . . 1 . . . . 56 Asp C . 11013 1 261 . 1 1 56 56 ASP CA C 13 53.91 0.17 . 1 . . . . 56 Asp CA . 11013 1 262 . 1 1 56 56 ASP CB C 13 43.23 0.06 . 1 . . . . 56 Asp CB . 11013 1 263 . 1 1 56 56 ASP N N 15 124.64 0.05 . 1 . . . . 56 Asp N . 11013 1 264 . 1 1 57 57 TRP H H 1 9.795 0.010 . 1 . . . . 57 Trp H . 11013 1 265 . 1 1 57 57 TRP HA H 1 5.058 . . 1 . . . . 57 Trp HA . 11013 1 266 . 1 1 57 57 TRP C C 13 176.1 . . 1 . . . . 57 Trp C . 11013 1 267 . 1 1 57 57 TRP CA C 13 60.24 0.09 . 1 . . . . 57 Trp CA . 11013 1 268 . 1 1 57 57 TRP CB C 13 31.00 0.10 . 1 . . . . 57 Trp CB . 11013 1 269 . 1 1 57 57 TRP N N 15 128.33 0.05 . 1 . . . . 57 Trp N . 11013 1 270 . 1 1 58 58 LYS H H 1 8.448 0.002 . 1 . . . . 58 Lys H . 11013 1 271 . 1 1 58 58 LYS C C 13 179.6 . . 1 . . . . 58 Lys C . 11013 1 272 . 1 1 58 58 LYS CA C 13 60.88 0.09 . 1 . . . . 58 Lys CA . 11013 1 273 . 1 1 58 58 LYS CB C 13 32.34 0.05 . 1 . . . . 58 Lys CB . 11013 1 274 . 1 1 58 58 LYS N N 15 116.58 0.02 . 1 . . . . 58 Lys N . 11013 1 275 . 1 1 59 59 GLN H H 1 7.601 0.003 . 1 . . . . 59 Gln H . 11013 1 276 . 1 1 59 59 GLN HA H 1 4.363 . . 1 . . . . 59 Gln HA . 11013 1 277 . 1 1 59 59 GLN C C 13 178.9 . . 1 . . . . 59 Gln C . 11013 1 278 . 1 1 59 59 GLN CA C 13 58.62 0.06 . 1 . . . . 59 Gln CA . 11013 1 279 . 1 1 59 59 GLN CB C 13 29.01 0.55 . 1 . . . . 59 Gln CB . 11013 1 280 . 1 1 59 59 GLN N N 15 118.58 0.01 . 1 . . . . 59 Gln N . 11013 1 281 . 1 1 60 60 ILE H H 1 8.412 0.005 . 1 . . . . 60 Ile H . 11013 1 282 . 1 1 60 60 ILE C C 13 177.2 . . 1 . . . . 60 Ile C . 11013 1 283 . 1 1 60 60 ILE CA C 13 66.29 0.09 . 1 . . . . 60 Ile CA . 11013 1 284 . 1 1 60 60 ILE CB C 13 38.36 0.00 . 1 . . . . 60 Ile CB . 11013 1 285 . 1 1 60 60 ILE N N 15 122.24 0.07 . 1 . . . . 60 Ile N . 11013 1 286 . 1 1 61 61 ARG H H 1 8.222 0.005 . 1 . . . . 61 Arg H . 11013 1 287 . 1 1 61 61 ARG C C 13 176.9 . . 1 . . . . 61 Arg C . 11013 1 288 . 1 1 61 61 ARG CA C 13 60.01 0.06 . 1 . . . . 61 Arg CA . 11013 1 289 . 1 1 61 61 ARG CB C 13 30.46 0.14 . 1 . . . . 61 Arg CB . 11013 1 290 . 1 1 61 61 ARG N N 15 117.10 0.04 . 1 . . . . 61 Arg N . 11013 1 291 . 1 1 62 62 SER H H 1 7.098 0.002 . 1 . . . . 62 Ser H . 11013 1 292 . 1 1 62 62 SER C C 13 176.4 . . 1 . . . . 62 Ser C . 11013 1 293 . 1 1 62 62 SER CA C 13 61.84 0.08 . 1 . . . . 62 Ser CA . 11013 1 294 . 1 1 62 62 SER CB C 13 63.78 0.08 . 1 . . . . 62 Ser CB . 11013 1 295 . 1 1 62 62 SER N N 15 111.80 0.02 . 1 . . . . 62 Ser N . 11013 1 296 . 1 1 63 63 ILE H H 1 7.718 0.004 . 1 . . . . 63 Ile H . 11013 1 297 . 1 1 63 63 ILE C C 13 177.9 . . 1 . . . . 63 Ile C . 11013 1 298 . 1 1 63 63 ILE CA C 13 66.43 0.13 . 1 . . . . 63 Ile CA . 11013 1 299 . 1 1 63 63 ILE CB C 13 38.48 0.07 . 1 . . . . 63 Ile CB . 11013 1 300 . 1 1 63 63 ILE N N 15 124.14 0.05 . 1 . . . . 63 Ile N . 11013 1 301 . 1 1 64 64 ILE H H 1 7.531 0.002 . 1 . . . . 64 Ile H . 11013 1 302 . 1 1 64 64 ILE C C 13 176.5 . . 1 . . . . 64 Ile C . 11013 1 303 . 1 1 64 64 ILE CA C 13 62.97 0.07 . 1 . . . . 64 Ile CA . 11013 1 304 . 1 1 64 64 ILE CB C 13 37.72 0.18 . 1 . . . . 64 Ile CB . 11013 1 305 . 1 1 64 64 ILE N N 15 110.00 0.01 . 1 . . . . 64 Ile N . 11013 1 306 . 1 1 65 65 MET H H 1 7.219 0.001 . 1 . . . . 65 Met H . 11013 1 307 . 1 1 65 65 MET HA H 1 4.467 . . 1 . . . . 65 Met HA . 11013 1 308 . 1 1 65 65 MET C C 13 177.1 . . 1 . . . . 65 Met C . 11013 1 309 . 1 1 65 65 MET CA C 13 55.32 0.09 . 1 . . . . 65 Met CA . 11013 1 310 . 1 1 65 65 MET CB C 13 33.23 0.13 . 1 . . . . 65 Met CB . 11013 1 311 . 1 1 65 65 MET N N 15 116.60 0.02 . 1 . . . . 65 Met N . 11013 1 312 . 1 1 66 66 ARG H H 1 7.656 0.003 . 1 . . . . 66 Arg H . 11013 1 313 . 1 1 66 66 ARG C C 13 178.9 . . 1 . . . . 66 Arg C . 11013 1 314 . 1 1 66 66 ARG CA C 13 58.23 0.09 . 1 . . . . 66 Arg CA . 11013 1 315 . 1 1 66 66 ARG CB C 13 32.06 0.03 . 1 . . . . 66 Arg CB . 11013 1 316 . 1 1 66 66 ARG N N 15 121.14 0.02 . 1 . . . . 66 Arg N . 11013 1 317 . 1 1 67 67 GLU H H 1 9.232 0.004 . 1 . . . . 67 Glu H . 11013 1 318 . 1 1 67 67 GLU HA H 1 5.002 . . 1 . . . . 67 Glu HA . 11013 1 319 . 1 1 67 67 GLU CA C 13 59.86 0.10 . 1 . . . . 67 Glu CA . 11013 1 320 . 1 1 67 67 GLU CB C 13 29.87 . . 1 . . . . 67 Glu CB . 11013 1 321 . 1 1 67 67 GLU N N 15 124.81 0.02 . 1 . . . . 67 Glu N . 11013 1 322 . 1 1 71 71 PRO C C 13 178.1 . . 1 . . . . 71 Pro C . 11013 1 323 . 1 1 71 71 PRO CA C 13 66.85 0.03 . 1 . . . . 71 Pro CA . 11013 1 324 . 1 1 71 71 PRO CB C 13 31.59 0.15 . 1 . . . . 71 Pro CB . 11013 1 325 . 1 1 72 72 THR H H 1 7.931 0.001 . 1 . . . . 72 Thr H . 11013 1 326 . 1 1 72 72 THR C C 13 176.4 . . 1 . . . . 72 Thr C . 11013 1 327 . 1 1 72 72 THR CA C 13 67.58 0.32 . 1 . . . . 72 Thr CA . 11013 1 328 . 1 1 72 72 THR CB C 13 69.28 . . 1 . . . . 72 Thr CB . 11013 1 329 . 1 1 72 72 THR N N 15 113.35 0.02 . 1 . . . . 72 Thr N . 11013 1 330 . 1 1 73 73 ILE H H 1 7.444 0.003 . 1 . . . . 73 Ile H . 11013 1 331 . 1 1 73 73 ILE C C 13 178.0 . . 1 . . . . 73 Ile C . 11013 1 332 . 1 1 73 73 ILE CA C 13 65.31 0.20 . 1 . . . . 73 Ile CA . 11013 1 333 . 1 1 73 73 ILE CB C 13 37.83 0.07 . 1 . . . . 73 Ile CB . 11013 1 334 . 1 1 73 73 ILE N N 15 121.57 0.08 . 1 . . . . 73 Ile N . 11013 1 335 . 1 1 74 74 VAL H H 1 8.371 0.001 . 1 . . . . 74 Val H . 11013 1 336 . 1 1 74 74 VAL C C 13 177.1 . . 1 . . . . 74 Val C . 11013 1 337 . 1 1 74 74 VAL CA C 13 67.73 0.21 . 1 . . . . 74 Val CA . 11013 1 338 . 1 1 74 74 VAL CB C 13 32.47 0.11 . 1 . . . . 74 Val CB . 11013 1 339 . 1 1 74 74 VAL N N 15 117.36 0.02 . 1 . . . . 74 Val N . 11013 1 340 . 1 1 75 75 ASN H H 1 8.010 0.002 . 1 . . . . 75 Asn H . 11013 1 341 . 1 1 75 75 ASN HA H 1 4.851 . . 1 . . . . 75 Asn HA . 11013 1 342 . 1 1 75 75 ASN C C 13 174.5 . . 1 . . . . 75 Asn C . 11013 1 343 . 1 1 75 75 ASN CA C 13 54.38 0.17 . 1 . . . . 75 Asn CA . 11013 1 344 . 1 1 75 75 ASN CB C 13 40.09 0.12 . 1 . . . . 75 Asn CB . 11013 1 345 . 1 1 75 75 ASN N N 15 114.48 0.02 . 1 . . . . 75 Asn N . 11013 1 346 . 1 1 76 76 PHE H H 1 7.600 0.003 . 1 . . . . 76 Phe H . 11013 1 347 . 1 1 76 76 PHE C C 13 175.2 . . 1 . . . . 76 Phe C . 11013 1 348 . 1 1 76 76 PHE CA C 13 60.32 0.05 . 1 . . . . 76 Phe CA . 11013 1 349 . 1 1 76 76 PHE CB C 13 41.61 0.16 . 1 . . . . 76 Phe CB . 11013 1 350 . 1 1 76 76 PHE N N 15 123.58 0.02 . 1 . . . . 76 Phe N . 11013 1 351 . 1 1 77 77 SER H H 1 8.208 0.004 . 1 . . . . 77 Ser H . 11013 1 352 . 1 1 77 77 SER HA H 1 5.030 . . 1 . . . . 77 Ser HA . 11013 1 353 . 1 1 77 77 SER C C 13 174.4 . . 1 . . . . 77 Ser C . 11013 1 354 . 1 1 77 77 SER CA C 13 56.70 0.09 . 1 . . . . 77 Ser CA . 11013 1 355 . 1 1 77 77 SER CB C 13 65.13 0.16 . 1 . . . . 77 Ser CB . 11013 1 356 . 1 1 77 77 SER N N 15 123.12 0.02 . 1 . . . . 77 Ser N . 11013 1 357 . 1 1 78 78 ALA H H 1 9.083 0.004 . 1 . . . . 78 Ala H . 11013 1 358 . 1 1 78 78 ALA C C 13 179.0 . . 1 . . . . 78 Ala C . 11013 1 359 . 1 1 78 78 ALA CA C 13 55.22 0.22 . 1 . . . . 78 Ala CA . 11013 1 360 . 1 1 78 78 ALA CB C 13 19.82 0.25 . 1 . . . . 78 Ala CB . 11013 1 361 . 1 1 78 78 ALA N N 15 128.78 0.03 . 1 . . . . 78 Ala N . 11013 1 362 . 1 1 79 79 GLU H H 1 8.633 0.003 . 1 . . . . 79 Glu H . 11013 1 363 . 1 1 79 79 GLU C C 13 177.0 . . 1 . . . . 79 Glu C . 11013 1 364 . 1 1 79 79 GLU CA C 13 59.39 0.09 . 1 . . . . 79 Glu CA . 11013 1 365 . 1 1 79 79 GLU CB C 13 30.19 0.08 . 1 . . . . 79 Glu CB . 11013 1 366 . 1 1 79 79 GLU N N 15 116.93 0.02 . 1 . . . . 79 Glu N . 11013 1 367 . 1 1 80 80 GLU H H 1 7.884 0.002 . 1 . . . . 80 Glu H . 11013 1 368 . 1 1 80 80 GLU HA H 1 4.424 . . 1 . . . . 80 Glu HA . 11013 1 369 . 1 1 80 80 GLU C C 13 177.1 . . 1 . . . . 80 Glu C . 11013 1 370 . 1 1 80 80 GLU CA C 13 57.04 0.08 . 1 . . . . 80 Glu CA . 11013 1 371 . 1 1 80 80 GLU CB C 13 30.58 0.08 . 1 . . . . 80 Glu CB . 11013 1 372 . 1 1 80 80 GLU N N 15 115.80 0.05 . 1 . . . . 80 Glu N . 11013 1 373 . 1 1 81 81 ILE H H 1 7.594 0.002 . 1 . . . . 81 Ile H . 11013 1 374 . 1 1 81 81 ILE C C 13 175.6 . . 1 . . . . 81 Ile C . 11013 1 375 . 1 1 81 81 ILE CA C 13 63.54 0.09 . 1 . . . . 81 Ile CA . 11013 1 376 . 1 1 81 81 ILE CB C 13 38.17 . . 1 . . . . 81 Ile CB . 11013 1 377 . 1 1 81 81 ILE N N 15 120.15 0.06 . 1 . . . . 81 Ile N . 11013 1 378 . 1 1 82 82 SER H H 1 8.013 0.003 . 1 . . . . 82 Ser H . 11013 1 379 . 1 1 82 82 SER HA H 1 4.521 . . 1 . . . . 82 Ser HA . 11013 1 380 . 1 1 82 82 SER C C 13 174.7 . . 1 . . . . 82 Ser C . 11013 1 381 . 1 1 82 82 SER CA C 13 57.87 0.09 . 1 . . . . 82 Ser CA . 11013 1 382 . 1 1 82 82 SER CB C 13 66.17 0.12 . 1 . . . . 82 Ser CB . 11013 1 383 . 1 1 82 82 SER N N 15 125.77 0.03 . 1 . . . . 82 Ser N . 11013 1 384 . 1 1 83 83 ASP H H 1 9.273 0.004 . 1 . . . . 83 Asp H . 11013 1 385 . 1 1 83 83 ASP C C 13 178.6 . . 1 . . . . 83 Asp C . 11013 1 386 . 1 1 83 83 ASP CA C 13 58.66 0.11 . 1 . . . . 83 Asp CA . 11013 1 387 . 1 1 83 83 ASP CB C 13 40.55 0.17 . 1 . . . . 83 Asp CB . 11013 1 388 . 1 1 83 83 ASP N N 15 121.97 0.02 . 1 . . . . 83 Asp N . 11013 1 389 . 1 1 84 84 ALA H H 1 8.665 0.002 . 1 . . . . 84 Ala H . 11013 1 390 . 1 1 84 84 ALA HA H 1 4.972 . . 1 . . . . 84 Ala HA . 11013 1 391 . 1 1 84 84 ALA C C 13 181.2 . . 1 . . . . 84 Ala C . 11013 1 392 . 1 1 84 84 ALA CA C 13 55.77 0.13 . 1 . . . . 84 Ala CA . 11013 1 393 . 1 1 84 84 ALA CB C 13 18.99 0.24 . 1 . . . . 84 Ala CB . 11013 1 394 . 1 1 84 84 ALA N N 15 121.40 0.03 . 1 . . . . 84 Ala N . 11013 1 395 . 1 1 85 85 ILE H H 1 7.838 0.007 . 1 . . . . 85 Ile H . 11013 1 396 . 1 1 85 85 ILE C C 13 177.7 . . 1 . . . . 85 Ile C . 11013 1 397 . 1 1 85 85 ILE CA C 13 65.40 0.13 . 1 . . . . 85 Ile CA . 11013 1 398 . 1 1 85 85 ILE CB C 13 37.75 0.09 . 1 . . . . 85 Ile CB . 11013 1 399 . 1 1 85 85 ILE N N 15 120.16 0.04 . 1 . . . . 85 Ile N . 11013 1 400 . 1 1 86 86 ARG H H 1 8.674 0.006 . 1 . . . . 86 Arg H . 11013 1 401 . 1 1 86 86 ARG C C 13 178.2 . . 1 . . . . 86 Arg C . 11013 1 402 . 1 1 86 86 ARG CA C 13 61.42 0.15 . 1 . . . . 86 Arg CA . 11013 1 403 . 1 1 86 86 ARG CB C 13 31.31 0.16 . 1 . . . . 86 Arg CB . 11013 1 404 . 1 1 86 86 ARG N N 15 120.93 0.02 . 1 . . . . 86 Arg N . 11013 1 405 . 1 1 87 87 GLU H H 1 8.290 0.002 . 1 . . . . 87 Glu H . 11013 1 406 . 1 1 87 87 GLU C C 13 178.8 . . 1 . . . . 87 Glu C . 11013 1 407 . 1 1 87 87 GLU CA C 13 59.96 0.19 . 1 . . . . 87 Glu CA . 11013 1 408 . 1 1 87 87 GLU CB C 13 30.41 0.12 . 1 . . . . 87 Glu CB . 11013 1 409 . 1 1 87 87 GLU N N 15 116.85 0.03 . 1 . . . . 87 Glu N . 11013 1 410 . 1 1 88 88 LYS H H 1 8.039 0.006 . 1 . . . . 88 Lys H . 11013 1 411 . 1 1 88 88 LYS C C 13 179.5 . . 1 . . . . 88 Lys C . 11013 1 412 . 1 1 88 88 LYS CA C 13 60.53 0.12 . 1 . . . . 88 Lys CA . 11013 1 413 . 1 1 88 88 LYS CB C 13 33.76 0.13 . 1 . . . . 88 Lys CB . 11013 1 414 . 1 1 88 88 LYS N N 15 120.31 0.07 . 1 . . . . 88 Lys N . 11013 1 415 . 1 1 89 89 MET H H 1 9.086 0.002 . 1 . . . . 89 Met H . 11013 1 416 . 1 1 89 89 MET C C 13 179.7 . . 1 . . . . 89 Met C . 11013 1 417 . 1 1 89 89 MET CA C 13 58.13 0.04 . 1 . . . . 89 Met CA . 11013 1 418 . 1 1 89 89 MET CB C 13 32.18 0.14 . 1 . . . . 89 Met CB . 11013 1 419 . 1 1 89 89 MET N N 15 118.61 0.01 . 1 . . . . 89 Met N . 11013 1 420 . 1 1 90 90 LYS H H 1 8.208 0.004 . 1 . . . . 90 Lys H . 11013 1 421 . 1 1 90 90 LYS C C 13 178.3 . . 1 . . . . 90 Lys C . 11013 1 422 . 1 1 90 90 LYS CA C 13 61.00 0.13 . 1 . . . . 90 Lys CA . 11013 1 423 . 1 1 90 90 LYS CB C 13 33.27 0.19 . 1 . . . . 90 Lys CB . 11013 1 424 . 1 1 90 90 LYS N N 15 120.21 0.01 . 1 . . . . 90 Lys N . 11013 1 425 . 1 1 91 91 LYS H H 1 8.495 0.005 . 1 . . . . 91 Lys H . 11013 1 426 . 1 1 91 91 LYS C C 13 179.0 . . 1 . . . . 91 Lys C . 11013 1 427 . 1 1 91 91 LYS CA C 13 59.47 0.13 . 1 . . . . 91 Lys CA . 11013 1 428 . 1 1 91 91 LYS CB C 13 33.81 0.26 . 1 . . . . 91 Lys CB . 11013 1 429 . 1 1 91 91 LYS N N 15 116.94 0.05 . 1 . . . . 91 Lys N . 11013 1 430 . 1 1 92 92 ASN H H 1 8.616 0.002 . 1 . . . . 92 Asn H . 11013 1 431 . 1 1 92 92 ASN HA H 1 4.821 . . 1 . . . . 92 Asn HA . 11013 1 432 . 1 1 92 92 ASN C C 13 174.8 . . 1 . . . . 92 Asn C . 11013 1 433 . 1 1 92 92 ASN CA C 13 55.01 0.12 . 1 . . . . 92 Asn CA . 11013 1 434 . 1 1 92 92 ASN CB C 13 39.88 0.11 . 1 . . . . 92 Asn CB . 11013 1 435 . 1 1 92 92 ASN N N 15 114.86 0.02 . 1 . . . . 92 Asn N . 11013 1 436 . 1 1 93 93 TYR H H 1 7.257 0.001 . 1 . . . . 93 Tyr H . 11013 1 437 . 1 1 93 93 TYR HA H 1 4.485 . . 1 . . . . 93 Tyr HA . 11013 1 438 . 1 1 93 93 TYR C C 13 175.9 . . 1 . . . . 93 Tyr C . 11013 1 439 . 1 1 93 93 TYR CA C 13 61.68 0.11 . 1 . . . . 93 Tyr CA . 11013 1 440 . 1 1 93 93 TYR CB C 13 39.08 0.05 . 1 . . . . 93 Tyr CB . 11013 1 441 . 1 1 93 93 TYR N N 15 115.24 0.03 . 1 . . . . 93 Tyr N . 11013 1 442 . 1 1 94 94 MET H H 1 8.448 0.002 . 1 . . . . 94 Met H . 11013 1 443 . 1 1 94 94 MET C C 13 177.0 . . 1 . . . . 94 Met C . 11013 1 444 . 1 1 94 94 MET CA C 13 58.55 0.10 . 1 . . . . 94 Met CA . 11013 1 445 . 1 1 94 94 MET CB C 13 33.02 0.35 . 1 . . . . 94 Met CB . 11013 1 446 . 1 1 94 94 MET N N 15 114.23 0.04 . 1 . . . . 94 Met N . 11013 1 447 . 1 1 95 95 SER H H 1 7.380 0.003 . 1 . . . . 95 Ser H . 11013 1 448 . 1 1 95 95 SER HA H 1 4.578 . . 1 . . . . 95 Ser HA . 11013 1 449 . 1 1 95 95 SER C C 13 173.8 . . 1 . . . . 95 Ser C . 11013 1 450 . 1 1 95 95 SER CA C 13 58.49 0.12 . 1 . . . . 95 Ser CA . 11013 1 451 . 1 1 95 95 SER CB C 13 64.46 0.17 . 1 . . . . 95 Ser CB . 11013 1 452 . 1 1 95 95 SER N N 15 109.02 0.02 . 1 . . . . 95 Ser N . 11013 1 453 . 1 1 96 96 ASN H H 1 7.923 0.004 . 1 . . . . 96 Asn H . 11013 1 454 . 1 1 96 96 ASN HA H 1 5.127 . . 1 . . . . 96 Asn HA . 11013 1 455 . 1 1 96 96 ASN CA C 13 51.97 0.05 . 1 . . . . 96 Asn CA . 11013 1 456 . 1 1 96 96 ASN CB C 13 40.89 . . 1 . . . . 96 Asn CB . 11013 1 457 . 1 1 96 96 ASN N N 15 125.42 0.02 . 1 . . . . 96 Asn N . 11013 1 458 . 1 1 97 97 PRO HA H 1 4.588 . . 1 . . . . 97 Pro HA . 11013 1 459 . 1 1 97 97 PRO C C 13 177.8 . . 1 . . . . 97 Pro C . 11013 1 460 . 1 1 97 97 PRO CA C 13 65.38 0.04 . 1 . . . . 97 Pro CA . 11013 1 461 . 1 1 97 97 PRO CB C 13 33.00 0.17 . 1 . . . . 97 Pro CB . 11013 1 462 . 1 1 98 98 SER H H 1 8.809 0.003 . 1 . . . . 98 Ser H . 11013 1 463 . 1 1 98 98 SER HA H 1 4.008 . . 1 . . . . 98 Ser HA . 11013 1 464 . 1 1 98 98 SER C C 13 172.7 . . 1 . . . . 98 Ser C . 11013 1 465 . 1 1 98 98 SER CA C 13 60.03 0.10 . 1 . . . . 98 Ser CA . 11013 1 466 . 1 1 98 98 SER CB C 13 63.98 0.20 . 1 . . . . 98 Ser CB . 11013 1 467 . 1 1 98 98 SER N N 15 111.84 0.02 . 1 . . . . 98 Ser N . 11013 1 468 . 1 1 99 99 TYR H H 1 8.401 0.002 . 1 . . . . 99 Tyr H . 11013 1 469 . 1 1 99 99 TYR C C 13 173.0 . . 1 . . . . 99 Tyr C . 11013 1 470 . 1 1 99 99 TYR CA C 13 58.78 0.23 . 1 . . . . 99 Tyr CA . 11013 1 471 . 1 1 99 99 TYR CB C 13 38.97 0.14 . 1 . . . . 99 Tyr CB . 11013 1 472 . 1 1 99 99 TYR N N 15 123.52 0.04 . 1 . . . . 99 Tyr N . 11013 1 473 . 1 1 100 100 ASN H H 1 7.517 0.003 . 1 . . . . 100 Asn H . 11013 1 474 . 1 1 100 100 ASN HA H 1 4.735 . . 1 . . . . 100 Asn HA . 11013 1 475 . 1 1 100 100 ASN C C 13 173.8 . . 1 . . . . 100 Asn C . 11013 1 476 . 1 1 100 100 ASN CA C 13 53.38 0.13 . 1 . . . . 100 Asn CA . 11013 1 477 . 1 1 100 100 ASN CB C 13 42.49 0.10 . 1 . . . . 100 Asn CB . 11013 1 478 . 1 1 100 100 ASN N N 15 120.27 0.02 . 1 . . . . 100 Asn N . 11013 1 479 . 1 1 101 101 TYR H H 1 9.522 0.005 . 1 . . . . 101 Tyr H . 11013 1 480 . 1 1 101 101 TYR HA H 1 5.031 . . 1 . . . . 101 Tyr HA . 11013 1 481 . 1 1 101 101 TYR C C 13 174.9 . . 1 . . . . 101 Tyr C . 11013 1 482 . 1 1 101 101 TYR CA C 13 62.97 0.12 . 1 . . . . 101 Tyr CA . 11013 1 483 . 1 1 101 101 TYR CB C 13 39.38 0.14 . 1 . . . . 101 Tyr CB . 11013 1 484 . 1 1 101 101 TYR N N 15 124.40 0.03 . 1 . . . . 101 Tyr N . 11013 1 485 . 1 1 102 102 GLU H H 1 8.533 0.002 . 1 . . . . 102 Glu H . 11013 1 486 . 1 1 102 102 GLU C C 13 179.5 . . 1 . . . . 102 Glu C . 11013 1 487 . 1 1 102 102 GLU CA C 13 61.04 0.16 . 1 . . . . 102 Glu CA . 11013 1 488 . 1 1 102 102 GLU CB C 13 29.60 0.06 . 1 . . . . 102 Glu CB . 11013 1 489 . 1 1 102 102 GLU N N 15 118.13 0.03 . 1 . . . . 102 Glu N . 11013 1 490 . 1 1 103 103 ILE H H 1 8.098 0.002 . 1 . . . . 103 Ile H . 11013 1 491 . 1 1 103 103 ILE C C 13 179.1 . . 1 . . . . 103 Ile C . 11013 1 492 . 1 1 103 103 ILE CA C 13 65.06 0.31 . 1 . . . . 103 Ile CA . 11013 1 493 . 1 1 103 103 ILE CB C 13 38.79 0.13 . 1 . . . . 103 Ile CB . 11013 1 494 . 1 1 103 103 ILE N N 15 118.26 0.01 . 1 . . . . 103 Ile N . 11013 1 495 . 1 1 104 104 VAL H H 1 8.207 0.002 . 1 . . . . 104 Val H . 11013 1 496 . 1 1 104 104 VAL C C 13 177.2 . . 1 . . . . 104 Val C . 11013 1 497 . 1 1 104 104 VAL CA C 13 67.45 0.17 . 1 . . . . 104 Val CA . 11013 1 498 . 1 1 104 104 VAL CB C 13 32.71 . . 1 . . . . 104 Val CB . 11013 1 499 . 1 1 104 104 VAL N N 15 119.81 0.02 . 1 . . . . 104 Val N . 11013 1 500 . 1 1 105 105 ASN H H 1 9.057 0.002 . 1 . . . . 105 Asn H . 11013 1 501 . 1 1 105 105 ASN C C 13 176.7 . . 1 . . . . 105 Asn C . 11013 1 502 . 1 1 105 105 ASN CA C 13 56.19 0.07 . 1 . . . . 105 Asn CA . 11013 1 503 . 1 1 105 105 ASN CB C 13 39.71 0.24 . 1 . . . . 105 Asn CB . 11013 1 504 . 1 1 105 105 ASN N N 15 117.98 0.02 . 1 . . . . 105 Asn N . 11013 1 505 . 1 1 106 106 ARG H H 1 7.138 0.004 . 1 . . . . 106 Arg H . 11013 1 506 . 1 1 106 106 ARG C C 13 177.6 . . 1 . . . . 106 Arg C . 11013 1 507 . 1 1 106 106 ARG CA C 13 58.74 0.11 . 1 . . . . 106 Arg CA . 11013 1 508 . 1 1 106 106 ARG CB C 13 30.99 0.19 . 1 . . . . 106 Arg CB . 11013 1 509 . 1 1 106 106 ARG N N 15 113.25 0.01 . 1 . . . . 106 Arg N . 11013 1 510 . 1 1 107 107 ALA H H 1 7.339 0.003 . 1 . . . . 107 Ala H . 11013 1 511 . 1 1 107 107 ALA C C 13 178.6 . . 1 . . . . 107 Ala C . 11013 1 512 . 1 1 107 107 ALA CA C 13 53.96 0.17 . 1 . . . . 107 Ala CA . 11013 1 513 . 1 1 107 107 ALA CB C 13 20.34 0.27 . 1 . . . . 107 Ala CB . 11013 1 514 . 1 1 107 107 ALA N N 15 120.62 0.03 . 1 . . . . 107 Ala N . 11013 1 515 . 1 1 108 108 SER H H 1 8.472 0.004 . 1 . . . . 108 Ser H . 11013 1 516 . 1 1 108 108 SER C C 13 174.1 . . 1 . . . . 108 Ser C . 11013 1 517 . 1 1 108 108 SER CA C 13 57.96 0.03 . 1 . . . . 108 Ser CA . 11013 1 518 . 1 1 108 108 SER CB C 13 65.47 0.15 . 1 . . . . 108 Ser CB . 11013 1 519 . 1 1 108 108 SER N N 15 112.26 0.02 . 1 . . . . 108 Ser N . 11013 1 520 . 1 1 109 109 LEU H H 1 9.129 0.005 . 1 . . . . 109 Leu H . 11013 1 521 . 1 1 109 109 LEU C C 13 179.4 . . 1 . . . . 109 Leu C . 11013 1 522 . 1 1 109 109 LEU CA C 13 57.33 0.17 . 1 . . . . 109 Leu CA . 11013 1 523 . 1 1 109 109 LEU CB C 13 42.30 0.22 . 1 . . . . 109 Leu CB . 11013 1 524 . 1 1 109 109 LEU N N 15 130.91 0.05 . 1 . . . . 109 Leu N . 11013 1 525 . 1 1 110 110 ALA H H 1 7.986 0.004 . 1 . . . . 110 Ala H . 11013 1 526 . 1 1 110 110 ALA C C 13 177.5 . . 1 . . . . 110 Ala C . 11013 1 527 . 1 1 110 110 ALA CA C 13 54.30 0.07 . 1 . . . . 110 Ala CA . 11013 1 528 . 1 1 110 110 ALA CB C 13 19.73 0.19 . 1 . . . . 110 Ala CB . 11013 1 529 . 1 1 110 110 ALA N N 15 116.62 0.04 . 1 . . . . 110 Ala N . 11013 1 530 . 1 1 111 111 CYS H H 1 7.557 0.004 . 1 . . . . 111 Cys H . 11013 1 531 . 1 1 111 111 CYS C C 13 177.4 . . 1 . . . . 111 Cys C . 11013 1 532 . 1 1 111 111 CYS CA C 13 62.42 0.11 . 1 . . . . 111 Cys CA . 11013 1 533 . 1 1 111 111 CYS CB C 13 29.35 0.29 . 1 . . . . 111 Cys CB . 11013 1 534 . 1 1 111 111 CYS N N 15 110.92 0.01 . 1 . . . . 111 Cys N . 11013 1 535 . 1 1 112 112 GLY H H 1 8.194 0.002 . 1 . . . . 112 Gly H . 11013 1 536 . 1 1 112 112 GLY CA C 13 50.06 0.22 . 1 . . . . 112 Gly CA . 11013 1 537 . 1 1 112 112 GLY N N 15 108.08 0.02 . 1 . . . . 112 Gly N . 11013 1 538 . 1 1 113 113 PRO C C 13 177.8 . . 1 . . . . 113 Pro C . 11013 1 539 . 1 1 113 113 PRO CA C 13 65.96 0.08 . 1 . . . . 113 Pro CA . 11013 1 540 . 1 1 113 113 PRO CB C 13 33.66 0.26 . 1 . . . . 113 Pro CB . 11013 1 541 . 1 1 114 114 MET H H 1 6.888 0.003 . 1 . . . . 114 Met H . 11013 1 542 . 1 1 114 114 MET C C 13 177.3 . . 1 . . . . 114 Met C . 11013 1 543 . 1 1 114 114 MET CA C 13 60.44 0.10 . 1 . . . . 114 Met CA . 11013 1 544 . 1 1 114 114 MET CB C 13 32.55 0.20 . 1 . . . . 114 Met CB . 11013 1 545 . 1 1 114 114 MET N N 15 111.95 0.03 . 1 . . . . 114 Met N . 11013 1 546 . 1 1 115 115 VAL H H 1 7.957 0.002 . 1 . . . . 115 Val H . 11013 1 547 . 1 1 115 115 VAL C C 13 177.0 . . 1 . . . . 115 Val C . 11013 1 548 . 1 1 115 115 VAL CA C 13 66.91 0.06 . 1 . . . . 115 Val CA . 11013 1 549 . 1 1 115 115 VAL CB C 13 32.62 0.12 . 1 . . . . 115 Val CB . 11013 1 550 . 1 1 115 115 VAL N N 15 119.28 0.15 . 1 . . . . 115 Val N . 11013 1 551 . 1 1 116 116 LYS H H 1 7.874 0.002 . 1 . . . . 116 Lys H . 11013 1 552 . 1 1 116 116 LYS C C 13 179.3 . . 1 . . . . 116 Lys C . 11013 1 553 . 1 1 116 116 LYS CA C 13 60.68 0.03 . 1 . . . . 116 Lys CA . 11013 1 554 . 1 1 116 116 LYS CB C 13 33.49 0.19 . 1 . . . . 116 Lys CB . 11013 1 555 . 1 1 116 116 LYS N N 15 118.78 0.02 . 1 . . . . 116 Lys N . 11013 1 556 . 1 1 117 117 TRP H H 1 8.507 0.003 . 1 . . . . 117 Trp H . 11013 1 557 . 1 1 117 117 TRP C C 13 175.6 . . 1 . . . . 117 Trp C . 11013 1 558 . 1 1 117 117 TRP CA C 13 62.95 0.15 . 1 . . . . 117 Trp CA . 11013 1 559 . 1 1 117 117 TRP CB C 13 29.11 0.26 . 1 . . . . 117 Trp CB . 11013 1 560 . 1 1 117 117 TRP N N 15 119.41 0.03 . 1 . . . . 117 Trp N . 11013 1 561 . 1 1 118 118 ALA H H 1 8.953 0.001 . 1 . . . . 118 Ala H . 11013 1 562 . 1 1 118 118 ALA C C 13 179.4 . . 1 . . . . 118 Ala C . 11013 1 563 . 1 1 118 118 ALA CA C 13 56.64 0.09 . 1 . . . . 118 Ala CA . 11013 1 564 . 1 1 118 118 ALA CB C 13 19.25 0.35 . 1 . . . . 118 Ala CB . 11013 1 565 . 1 1 118 118 ALA N N 15 123.98 0.02 . 1 . . . . 118 Ala N . 11013 1 566 . 1 1 119 119 ILE H H 1 8.381 0.003 . 1 . . . . 119 Ile H . 11013 1 567 . 1 1 119 119 ILE C C 13 177.9 . . 1 . . . . 119 Ile C . 11013 1 568 . 1 1 119 119 ILE CA C 13 66.36 0.12 . 1 . . . . 119 Ile CA . 11013 1 569 . 1 1 119 119 ILE CB C 13 39.71 0.12 . 1 . . . . 119 Ile CB . 11013 1 570 . 1 1 119 119 ILE N N 15 115.99 0.03 . 1 . . . . 119 Ile N . 11013 1 571 . 1 1 120 120 ALA H H 1 7.979 0.002 . 1 . . . . 120 Ala H . 11013 1 572 . 1 1 120 120 ALA C C 13 181.6 . . 1 . . . . 120 Ala C . 11013 1 573 . 1 1 120 120 ALA CA C 13 55.67 0.05 . 1 . . . . 120 Ala CA . 11013 1 574 . 1 1 120 120 ALA CB C 13 18.31 0.30 . 1 . . . . 120 Ala CB . 11013 1 575 . 1 1 120 120 ALA N N 15 120.50 0.02 . 1 . . . . 120 Ala N . 11013 1 576 . 1 1 121 121 GLN H H 1 8.695 0.003 . 1 . . . . 121 Gln H . 11013 1 577 . 1 1 121 121 GLN C C 13 178.3 . . 1 . . . . 121 Gln C . 11013 1 578 . 1 1 121 121 GLN CA C 13 58.54 0.04 . 1 . . . . 121 Gln CA . 11013 1 579 . 1 1 121 121 GLN CB C 13 28.61 . . 1 . . . . 121 Gln CB . 11013 1 580 . 1 1 121 121 GLN N N 15 117.72 0.02 . 1 . . . . 121 Gln N . 11013 1 581 . 1 1 122 122 LEU H H 1 8.366 0.002 . 1 . . . . 122 Leu H . 11013 1 582 . 1 1 122 122 LEU C C 13 179.0 . . 1 . . . . 122 Leu C . 11013 1 583 . 1 1 122 122 LEU CA C 13 57.95 0.03 . 1 . . . . 122 Leu CA . 11013 1 584 . 1 1 122 122 LEU CB C 13 41.44 0.10 . 1 . . . . 122 Leu CB . 11013 1 585 . 1 1 122 122 LEU N N 15 121.68 0.03 . 1 . . . . 122 Leu N . 11013 1 586 . 1 1 123 123 ASN H H 1 8.647 0.003 . 1 . . . . 123 Asn H . 11013 1 587 . 1 1 123 123 ASN C C 13 178.6 . . 1 . . . . 123 Asn C . 11013 1 588 . 1 1 123 123 ASN CA C 13 56.48 0.11 . 1 . . . . 123 Asn CA . 11013 1 589 . 1 1 123 123 ASN CB C 13 38.16 0.12 . 1 . . . . 123 Asn CB . 11013 1 590 . 1 1 123 123 ASN N N 15 117.12 0.02 . 1 . . . . 123 Asn N . 11013 1 591 . 1 1 124 124 TYR H H 1 8.338 0.003 . 1 . . . . 124 Tyr H . 11013 1 592 . 1 1 124 124 TYR C C 13 176.9 . . 1 . . . . 124 Tyr C . 11013 1 593 . 1 1 124 124 TYR CA C 13 60.83 0.22 . 1 . . . . 124 Tyr CA . 11013 1 594 . 1 1 124 124 TYR CB C 13 39.05 0.05 . 1 . . . . 124 Tyr CB . 11013 1 595 . 1 1 124 124 TYR N N 15 123.11 0.08 . 1 . . . . 124 Tyr N . 11013 1 596 . 1 1 125 125 ALA H H 1 9.066 0.002 . 1 . . . . 125 Ala H . 11013 1 597 . 1 1 125 125 ALA C C 13 180.2 . . 1 . . . . 125 Ala C . 11013 1 598 . 1 1 125 125 ALA CA C 13 56.00 0.13 . 1 . . . . 125 Ala CA . 11013 1 599 . 1 1 125 125 ALA CB C 13 18.84 0.19 . 1 . . . . 125 Ala CB . 11013 1 600 . 1 1 125 125 ALA N N 15 121.95 0.05 . 1 . . . . 125 Ala N . 11013 1 601 . 1 1 126 126 ASP H H 1 8.558 0.005 . 1 . . . . 126 Asp H . 11013 1 602 . 1 1 126 126 ASP C C 13 178.9 . . 1 . . . . 126 Asp C . 11013 1 603 . 1 1 126 126 ASP CA C 13 57.75 0.24 . 1 . . . . 126 Asp CA . 11013 1 604 . 1 1 126 126 ASP CB C 13 41.26 0.07 . 1 . . . . 126 Asp CB . 11013 1 605 . 1 1 126 126 ASP N N 15 117.46 0.05 . 1 . . . . 126 Asp N . 11013 1 606 . 1 1 127 127 MET H H 1 7.827 0.003 . 1 . . . . 127 Met H . 11013 1 607 . 1 1 127 127 MET C C 13 178.6 . . 1 . . . . 127 Met C . 11013 1 608 . 1 1 127 127 MET CA C 13 58.98 0.07 . 1 . . . . 127 Met CA . 11013 1 609 . 1 1 127 127 MET CB C 13 32.57 0.45 . 1 . . . . 127 Met CB . 11013 1 610 . 1 1 127 127 MET N N 15 120.63 0.08 . 1 . . . . 127 Met N . 11013 1 611 . 1 1 128 128 LEU H H 1 8.372 0.005 . 1 . . . . 128 Leu H . 11013 1 612 . 1 1 128 128 LEU C C 13 179.2 . . 1 . . . . 128 Leu C . 11013 1 613 . 1 1 128 128 LEU CA C 13 57.95 0.07 . 1 . . . . 128 Leu CA . 11013 1 614 . 1 1 128 128 LEU CB C 13 42.74 0.06 . 1 . . . . 128 Leu CB . 11013 1 615 . 1 1 128 128 LEU N N 15 119.89 0.05 . 1 . . . . 128 Leu N . 11013 1 616 . 1 1 129 129 LYS H H 1 7.687 0.001 . 1 . . . . 129 Lys H . 11013 1 617 . 1 1 129 129 LYS C C 13 177.4 . . 1 . . . . 129 Lys C . 11013 1 618 . 1 1 129 129 LYS CA C 13 56.90 0.11 . 1 . . . . 129 Lys CA . 11013 1 619 . 1 1 129 129 LYS CB C 13 32.71 0.08 . 1 . . . . 129 Lys CB . 11013 1 620 . 1 1 129 129 LYS N N 15 116.63 0.04 . 1 . . . . 129 Lys N . 11013 1 621 . 1 1 130 130 ARG H H 1 7.820 0.004 . 1 . . . . 130 Arg H . 11013 1 622 . 1 1 130 130 ARG C C 13 176.9 . . 1 . . . . 130 Arg C . 11013 1 623 . 1 1 130 130 ARG CA C 13 57.98 0.12 . 1 . . . . 130 Arg CA . 11013 1 624 . 1 1 130 130 ARG CB C 13 31.55 0.20 . 1 . . . . 130 Arg CB . 11013 1 625 . 1 1 130 130 ARG N N 15 119.56 0.04 . 1 . . . . 130 Arg N . 11013 1 626 . 1 1 131 131 VAL H H 1 8.094 0.004 . 1 . . . . 131 Val H . 11013 1 627 . 1 1 131 131 VAL HA H 1 4.374 . . 1 . . . . 131 Val HA . 11013 1 628 . 1 1 131 131 VAL C C 13 175.0 . . 1 . . . . 131 Val C . 11013 1 629 . 1 1 131 131 VAL CA C 13 62.73 0.18 . 1 . . . . 131 Val CA . 11013 1 630 . 1 1 131 131 VAL CB C 13 33.61 0.05 . 1 . . . . 131 Val CB . 11013 1 631 . 1 1 131 131 VAL N N 15 117.93 0.06 . 1 . . . . 131 Val N . 11013 1 632 . 1 1 132 132 GLU H H 1 8.121 0.009 . 1 . . . . 132 Glu H . 11013 1 633 . 1 1 132 132 GLU HA H 1 4.721 . . 1 . . . . 132 Glu HA . 11013 1 634 . 1 1 132 132 GLU CA C 13 55.01 0.09 . 1 . . . . 132 Glu CA . 11013 1 635 . 1 1 132 132 GLU CB C 13 31.13 . . 1 . . . . 132 Glu CB . 11013 1 636 . 1 1 132 132 GLU N N 15 122.99 0.05 . 1 . . . . 132 Glu N . 11013 1 637 . 1 1 133 133 PRO C C 13 177.2 . . 1 . . . . 133 Pro C . 11013 1 638 . 1 1 133 133 PRO CA C 13 64.27 0.13 . 1 . . . . 133 Pro CA . 11013 1 639 . 1 1 133 133 PRO CB C 13 32.78 0.18 . 1 . . . . 133 Pro CB . 11013 1 640 . 1 1 134 134 LEU H H 1 8.421 0.005 . 1 . . . . 134 Leu H . 11013 1 641 . 1 1 134 134 LEU HA H 1 4.464 . . 1 . . . . 134 Leu HA . 11013 1 642 . 1 1 134 134 LEU C C 13 177.8 . . 1 . . . . 134 Leu C . 11013 1 643 . 1 1 134 134 LEU CA C 13 56.08 0.06 . 1 . . . . 134 Leu CA . 11013 1 644 . 1 1 134 134 LEU CB C 13 42.64 0.11 . 1 . . . . 134 Leu CB . 11013 1 645 . 1 1 134 134 LEU N N 15 120.64 0.04 . 1 . . . . 134 Leu N . 11013 1 646 . 1 1 135 135 ARG H H 1 8.398 0.007 . 1 . . . . 135 Arg H . 11013 1 647 . 1 1 135 135 ARG HA H 1 4.501 . . 1 . . . . 135 Arg HA . 11013 1 648 . 1 1 135 135 ARG C C 13 176.2 . . 1 . . . . 135 Arg C . 11013 1 649 . 1 1 135 135 ARG CA C 13 57.01 0.12 . 1 . . . . 135 Arg CA . 11013 1 650 . 1 1 135 135 ARG CB C 13 31.46 0.19 . 1 . . . . 135 Arg CB . 11013 1 651 . 1 1 135 135 ARG N N 15 121.34 0.06 . 1 . . . . 135 Arg N . 11013 1 652 . 1 1 136 136 ASN H H 1 8.609 0.005 . 1 . . . . 136 Asn H . 11013 1 653 . 1 1 136 136 ASN C C 13 175.4 . . 1 . . . . 136 Asn C . 11013 1 654 . 1 1 136 136 ASN CA C 13 54.06 0.13 . 1 . . . . 136 Asn CA . 11013 1 655 . 1 1 136 136 ASN CB C 13 39.63 0.14 . 1 . . . . 136 Asn CB . 11013 1 656 . 1 1 136 136 ASN N N 15 119.50 0.03 . 1 . . . . 136 Asn N . 11013 1 657 . 1 1 137 137 GLU H H 1 8.574 0.007 . 1 . . . . 137 Glu H . 11013 1 658 . 1 1 137 137 GLU C C 13 176.3 . . 1 . . . . 137 Glu C . 11013 1 659 . 1 1 137 137 GLU CA C 13 57.54 0.09 . 1 . . . . 137 Glu CA . 11013 1 660 . 1 1 137 137 GLU CB C 13 30.82 0.18 . 1 . . . . 137 Glu CB . 11013 1 661 . 1 1 137 137 GLU N N 15 120.99 0.02 . 1 . . . . 137 Glu N . 11013 1 662 . 1 1 138 138 HIS H H 1 8.482 0.002 . 1 . . . . 138 His H . 11013 1 663 . 1 1 138 138 HIS CA C 13 55.51 . . 1 . . . . 138 His CA . 11013 1 664 . 1 1 138 138 HIS N N 15 119.41 0.06 . 1 . . . . 138 His N . 11013 1 stop_ save_ save_assigned_chem_shift_list2 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode assigned_chem_shift_list2 _Assigned_chem_shift_list.Entry_ID 11013 _Assigned_chem_shift_list.ID 2 _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 'The list provides data from deteriorated protein' _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 '2D 1H-15N HSQC' 1 $sample_1 isotropic 11013 2 2 '3D CBCA(CO)NH' 1 $sample_1 isotropic 11013 2 3 '3D C(CO)NH' 1 $sample_1 isotropic 11013 2 4 '3D HNCO' 1 $sample_1 isotropic 11013 2 5 '3D HNCA' 1 $sample_1 isotropic 11013 2 6 '3D HNCACB' 1 $sample_1 isotropic 11013 2 7 '3D HN(CO)CA' 1 $sample_1 isotropic 11013 2 8 '3D H(CCO)NH' 1 $sample_1 isotropic 11013 2 9 '3D 1H-15N TOCSY' 1 $sample_1 isotropic 11013 2 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.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 GLU C C 13 175.7 . . 1 . . . . 2 Glu C . 11013 2 2 . 1 1 2 2 GLU CA C 13 57.04 0.11 . 1 . . . . 2 Glu CA . 11013 2 3 . 1 1 2 2 GLU CB C 13 31.28 0.01 . 1 . . . . 2 Glu CB . 11013 2 4 . 1 1 3 3 ASP H H 1 8.733 0.004 . 1 . . . . 3 Asp H . 11013 2 5 . 1 1 3 3 ASP C C 13 176.6 . . 1 . . . . 3 Asp C . 11013 2 6 . 1 1 3 3 ASP CA C 13 55.23 0.30 . 1 . . . . 3 Asp CA . 11013 2 7 . 1 1 3 3 ASP CB C 13 41.79 0.09 . 1 . . . . 3 Asp CB . 11013 2 8 . 1 1 3 3 ASP N N 15 121.82 0.07 . 1 . . . . 3 Asp N . 11013 2 9 . 1 1 4 4 LEU H H 1 8.501 0.003 . 1 . . . . 4 Leu H . 11013 2 10 . 1 1 4 4 LEU C C 13 177.5 . . 1 . . . . 4 Leu C . 11013 2 11 . 1 1 4 4 LEU CA C 13 56.22 0.08 . 1 . . . . 4 Leu CA . 11013 2 12 . 1 1 4 4 LEU CB C 13 42.95 0.10 . 1 . . . . 4 Leu CB . 11013 2 13 . 1 1 4 4 LEU N N 15 122.73 0.05 . 1 . . . . 4 Leu N . 11013 2 14 . 1 1 5 5 ASP H H 1 8.500 0.001 . 1 . . . . 5 Asp H . 11013 2 15 . 1 1 5 5 ASP C C 13 176.1 . . 1 . . . . 5 Asp C . 11013 2 16 . 1 1 5 5 ASP CA C 13 55.42 0.18 . 1 . . . . 5 Asp CA . 11013 2 17 . 1 1 5 5 ASP CB C 13 41.80 0.18 . 1 . . . . 5 Asp CB . 11013 2 18 . 1 1 5 5 ASP N N 15 119.90 0.13 . 1 . . . . 5 Asp N . 11013 2 19 . 1 1 6 6 LYS H H 1 8.136 0.002 . 1 . . . . 6 Lys H . 11013 2 20 . 1 1 6 6 LYS C C 13 176.3 . . 1 . . . . 6 Lys C . 11013 2 21 . 1 1 6 6 LYS CA C 13 56.76 0.12 . 1 . . . . 6 Lys CA . 11013 2 22 . 1 1 6 6 LYS CB C 13 33.78 0.23 . 1 . . . . 6 Lys CB . 11013 2 23 . 1 1 6 6 LYS N N 15 120.83 0.02 . 1 . . . . 6 Lys N . 11013 2 24 . 1 1 7 7 VAL H H 1 8.257 0.010 . 1 . . . . 7 Val H . 11013 2 25 . 1 1 7 7 VAL C C 13 176.0 . . 1 . . . . 7 Val C . 11013 2 26 . 1 1 7 7 VAL CA C 13 62.63 0.19 . 1 . . . . 7 Val CA . 11013 2 27 . 1 1 7 7 VAL CB C 13 33.72 0.24 . 1 . . . . 7 Val CB . 11013 2 28 . 1 1 7 7 VAL N N 15 121.92 0.07 . 1 . . . . 7 Val N . 11013 2 29 . 1 1 8 8 GLU H H 1 8.708 0.007 . 1 . . . . 8 Glu H . 11013 2 30 . 1 1 8 8 GLU CA C 13 55.00 0.04 . 1 . . . . 8 Glu CA . 11013 2 31 . 1 1 8 8 GLU CB C 13 30.58 . . 1 . . . . 8 Glu CB . 11013 2 32 . 1 1 8 8 GLU N N 15 126.81 0.03 . 1 . . . . 8 Glu N . 11013 2 33 . 1 1 9 9 PRO C C 13 177.0 . . 1 . . . . 9 Pro C . 11013 2 34 . 1 1 9 9 PRO CA C 13 64.11 0.05 . 1 . . . . 9 Pro CA . 11013 2 35 . 1 1 9 9 PRO CB C 13 32.61 0.19 . 1 . . . . 9 Pro CB . 11013 2 36 . 1 1 10 10 ALA H H 1 8.603 0.003 . 1 . . . . 10 Ala H . 11013 2 37 . 1 1 10 10 ALA C C 13 178.1 . . 1 . . . . 10 Ala C . 11013 2 38 . 1 1 10 10 ALA CA C 13 53.72 0.08 . 1 . . . . 10 Ala CA . 11013 2 39 . 1 1 10 10 ALA CB C 13 19.71 0.31 . 1 . . . . 10 Ala CB . 11013 2 40 . 1 1 10 10 ALA N N 15 123.36 0.07 . 1 . . . . 10 Ala N . 11013 2 41 . 1 1 11 11 VAL H H 1 8.163 0.007 . 1 . . . . 11 Val H . 11013 2 42 . 1 1 11 11 VAL C C 13 176.6 . . 1 . . . . 11 Val C . 11013 2 43 . 1 1 11 11 VAL CA C 13 63.44 0.22 . 1 . . . . 11 Val CA . 11013 2 44 . 1 1 11 11 VAL CB C 13 33.17 . . 1 . . . . 11 Val CB . 11013 2 45 . 1 1 11 11 VAL N N 15 118.93 0.03 . 1 . . . . 11 Val N . 11013 2 46 . 1 1 12 12 ILE H H 1 8.271 0.008 . 1 . . . . 12 Ile H . 11013 2 47 . 1 1 12 12 ILE CA C 13 62.14 0.14 . 1 . . . . 12 Ile CA . 11013 2 48 . 1 1 12 12 ILE CB C 13 39.31 . . 1 . . . . 12 Ile CB . 11013 2 49 . 1 1 12 12 ILE N N 15 124.68 0.14 . 1 . . . . 12 Ile N . 11013 2 stop_ save_