data_16449 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 16449 _Entry.Title ; Structure of the XPF-single strand DNA complex ; _Entry.Type macromolecule _Entry.Version_type new _Entry.Submission_date 2009-08-16 _Entry.Accession_date 2009-08-16 _Entry.Last_release_date . _Entry.Original_release_date . _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 _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 Devashish Das . . . 16449 2 Gert Folkers . E. . 16449 3 Marc Dijk . V. . 16449 4 Nicolaas Jaspers . G.J. . 16449 5 Jan Hoeijmakers . H.J. . 16449 6 Robert Kaptein . . . 16449 7 Rolf Boelens . . . 16449 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 'not applicable' 'not applicable' . 16449 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID HhH . 16449 NER . 16449 'Protein-ssDNA complex' . 16449 XPF/ERCC1 . 16449 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 16449 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '13C chemical shifts' 199 16449 '15N chemical shifts' 73 16449 '1H chemical shifts' 435 16449 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 2 . . 2014-05-16 2009-08-16 update BMRB 'update entry citation' 16449 1 . . 2012-08-03 2009-08-16 original author 'original release' 16449 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 18343 'free 10nts ssDNA' 16449 PDB 1z00 . 16449 PDB 2aq0 . 16449 PDB 2KN7 'BMRB Entry Tracking System' 16449 stop_ save_ ############### # Citations # ############### save_citations _Citation.Sf_category citations _Citation.Sf_framecode citations _Citation.Entry_ID 16449 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID 22483113 _Citation.Full_citation . _Citation.Title 'The structure of the XPF-ssDNA complex underscores the distinct roles of the XPF and ERCC1 helix- hairpin-helix domains in ss/ds DNA recognition.' _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Structure _Citation.Journal_name_full 'Structure (London, England : 1993)' _Citation.Journal_volume 20 _Citation.Journal_issue 4 _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 667 _Citation.Page_last 675 _Citation.Year 2012 _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 Devashish Das . . . 16449 1 2 Gert Folkers . E. . 16449 1 3 Marc 'van Dijk' . . . 16449 1 4 Nicolaas Jaspers . G.J. . 16449 1 5 Jan Hoeijmakers . H.J. . 16449 1 6 Robert Kaptein . . . 16449 1 7 Rolf Boelens . . . 16449 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 16449 _Assembly.ID 1 _Assembly.Name 'XPF DNA complex' _Assembly.BMRB_code . _Assembly.Number_of_components 2 _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 XPF 1 $entity_1 A . yes native no no . . . 16449 1 2 'DNA chain' 2 $DNA B . no native no no . . . 16449 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_entity_1 _Entity.Sf_category entity _Entity.Sf_framecode entity_1 _Entity.Entry_ID 16449 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name entity_1 _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 ; EKYNPGPQDFLLKMPGVNAK NCRSLMHHVKNIAELAALSQ DELTSILGNAANAKQLYDFI HTSFAEVEKYNPGPKDFLLK MPGVNAKNCRSLMHHVKNIA ELAALSQDELTSILGNAANA KQLYDFIHTSFAEV ; _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 134 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'all free' _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 14828.994 _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 2KN7 . "Structure Of The Xpf-Single Strand Dna Complex" . . . . . 50.00 67 98.51 100.00 2.17e-39 . . . . 16449 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 10 GLU . 16449 1 2 11 LYS . 16449 1 3 12 TYR . 16449 1 4 13 ASN . 16449 1 5 14 PRO . 16449 1 6 15 GLY . 16449 1 7 16 PRO . 16449 1 8 17 GLN . 16449 1 9 18 ASP . 16449 1 10 19 PHE . 16449 1 11 20 LEU . 16449 1 12 21 LEU . 16449 1 13 22 LYS . 16449 1 14 23 MET . 16449 1 15 24 PRO . 16449 1 16 25 GLY . 16449 1 17 26 VAL . 16449 1 18 27 ASN . 16449 1 19 28 ALA . 16449 1 20 29 LYS . 16449 1 21 30 ASN . 16449 1 22 31 CYS . 16449 1 23 32 ARG . 16449 1 24 33 SER . 16449 1 25 34 LEU . 16449 1 26 35 MET . 16449 1 27 36 HIS . 16449 1 28 37 HIS . 16449 1 29 38 VAL . 16449 1 30 39 LYS . 16449 1 31 40 ASN . 16449 1 32 41 ILE . 16449 1 33 42 ALA . 16449 1 34 43 GLU . 16449 1 35 44 LEU . 16449 1 36 45 ALA . 16449 1 37 46 ALA . 16449 1 38 47 LEU . 16449 1 39 48 SER . 16449 1 40 49 GLN . 16449 1 41 50 ASP . 16449 1 42 51 GLU . 16449 1 43 52 LEU . 16449 1 44 53 THR . 16449 1 45 54 SER . 16449 1 46 55 ILE . 16449 1 47 56 LEU . 16449 1 48 57 GLY . 16449 1 49 58 ASN . 16449 1 50 59 ALA . 16449 1 51 60 ALA . 16449 1 52 61 ASN . 16449 1 53 62 ALA . 16449 1 54 63 LYS . 16449 1 55 64 GLN . 16449 1 56 65 LEU . 16449 1 57 66 TYR . 16449 1 58 67 ASP . 16449 1 59 68 PHE . 16449 1 60 69 ILE . 16449 1 61 70 HIS . 16449 1 62 71 THR . 16449 1 63 72 SER . 16449 1 64 73 PHE . 16449 1 65 74 ALA . 16449 1 66 75 GLU . 16449 1 67 76 VAL . 16449 1 68 77 GLU . 16449 1 69 78 LYS . 16449 1 70 79 TYR . 16449 1 71 80 ASN . 16449 1 72 81 PRO . 16449 1 73 82 GLY . 16449 1 74 83 PRO . 16449 1 75 84 LYS . 16449 1 76 85 ASP . 16449 1 77 86 PHE . 16449 1 78 87 LEU . 16449 1 79 88 LEU . 16449 1 80 89 LYS . 16449 1 81 90 MET . 16449 1 82 91 PRO . 16449 1 83 92 GLY . 16449 1 84 93 VAL . 16449 1 85 94 ASN . 16449 1 86 95 ALA . 16449 1 87 96 LYS . 16449 1 88 97 ASN . 16449 1 89 98 CYS . 16449 1 90 99 ARG . 16449 1 91 100 SER . 16449 1 92 101 LEU . 16449 1 93 102 MET . 16449 1 94 103 HIS . 16449 1 95 104 HIS . 16449 1 96 105 VAL . 16449 1 97 106 LYS . 16449 1 98 107 ASN . 16449 1 99 108 ILE . 16449 1 100 109 ALA . 16449 1 101 110 GLU . 16449 1 102 111 LEU . 16449 1 103 112 ALA . 16449 1 104 113 ALA . 16449 1 105 114 LEU . 16449 1 106 115 SER . 16449 1 107 116 GLN . 16449 1 108 117 ASP . 16449 1 109 118 GLU . 16449 1 110 119 LEU . 16449 1 111 120 THR . 16449 1 112 121 SER . 16449 1 113 122 ILE . 16449 1 114 123 LEU . 16449 1 115 124 GLY . 16449 1 116 125 ASN . 16449 1 117 126 ALA . 16449 1 118 127 ALA . 16449 1 119 128 ASN . 16449 1 120 129 ALA . 16449 1 121 130 LYS . 16449 1 122 131 GLN . 16449 1 123 132 LEU . 16449 1 124 133 TYR . 16449 1 125 134 ASP . 16449 1 126 135 PHE . 16449 1 127 136 ILE . 16449 1 128 137 HIS . 16449 1 129 138 THR . 16449 1 130 139 SER . 16449 1 131 140 PHE . 16449 1 132 141 ALA . 16449 1 133 142 GLU . 16449 1 134 143 VAL . 16449 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 . GLU 1 1 16449 1 . LYS 2 2 16449 1 . TYR 3 3 16449 1 . ASN 4 4 16449 1 . PRO 5 5 16449 1 . GLY 6 6 16449 1 . PRO 7 7 16449 1 . GLN 8 8 16449 1 . ASP 9 9 16449 1 . PHE 10 10 16449 1 . LEU 11 11 16449 1 . LEU 12 12 16449 1 . LYS 13 13 16449 1 . MET 14 14 16449 1 . PRO 15 15 16449 1 . GLY 16 16 16449 1 . VAL 17 17 16449 1 . ASN 18 18 16449 1 . ALA 19 19 16449 1 . LYS 20 20 16449 1 . ASN 21 21 16449 1 . CYS 22 22 16449 1 . ARG 23 23 16449 1 . SER 24 24 16449 1 . LEU 25 25 16449 1 . MET 26 26 16449 1 . HIS 27 27 16449 1 . HIS 28 28 16449 1 . VAL 29 29 16449 1 . LYS 30 30 16449 1 . ASN 31 31 16449 1 . ILE 32 32 16449 1 . ALA 33 33 16449 1 . GLU 34 34 16449 1 . LEU 35 35 16449 1 . ALA 36 36 16449 1 . ALA 37 37 16449 1 . LEU 38 38 16449 1 . SER 39 39 16449 1 . GLN 40 40 16449 1 . ASP 41 41 16449 1 . GLU 42 42 16449 1 . LEU 43 43 16449 1 . THR 44 44 16449 1 . SER 45 45 16449 1 . ILE 46 46 16449 1 . LEU 47 47 16449 1 . GLY 48 48 16449 1 . ASN 49 49 16449 1 . ALA 50 50 16449 1 . ALA 51 51 16449 1 . ASN 52 52 16449 1 . ALA 53 53 16449 1 . LYS 54 54 16449 1 . GLN 55 55 16449 1 . LEU 56 56 16449 1 . TYR 57 57 16449 1 . ASP 58 58 16449 1 . PHE 59 59 16449 1 . ILE 60 60 16449 1 . HIS 61 61 16449 1 . THR 62 62 16449 1 . SER 63 63 16449 1 . PHE 64 64 16449 1 . ALA 65 65 16449 1 . GLU 66 66 16449 1 . VAL 67 67 16449 1 . GLU 68 68 16449 1 . LYS 69 69 16449 1 . TYR 70 70 16449 1 . ASN 71 71 16449 1 . PRO 72 72 16449 1 . GLY 73 73 16449 1 . PRO 74 74 16449 1 . LYS 75 75 16449 1 . ASP 76 76 16449 1 . PHE 77 77 16449 1 . LEU 78 78 16449 1 . LEU 79 79 16449 1 . LYS 80 80 16449 1 . MET 81 81 16449 1 . PRO 82 82 16449 1 . GLY 83 83 16449 1 . VAL 84 84 16449 1 . ASN 85 85 16449 1 . ALA 86 86 16449 1 . LYS 87 87 16449 1 . ASN 88 88 16449 1 . CYS 89 89 16449 1 . ARG 90 90 16449 1 . SER 91 91 16449 1 . LEU 92 92 16449 1 . MET 93 93 16449 1 . HIS 94 94 16449 1 . HIS 95 95 16449 1 . VAL 96 96 16449 1 . LYS 97 97 16449 1 . ASN 98 98 16449 1 . ILE 99 99 16449 1 . ALA 100 100 16449 1 . GLU 101 101 16449 1 . LEU 102 102 16449 1 . ALA 103 103 16449 1 . ALA 104 104 16449 1 . LEU 105 105 16449 1 . SER 106 106 16449 1 . GLN 107 107 16449 1 . ASP 108 108 16449 1 . GLU 109 109 16449 1 . LEU 110 110 16449 1 . THR 111 111 16449 1 . SER 112 112 16449 1 . ILE 113 113 16449 1 . LEU 114 114 16449 1 . GLY 115 115 16449 1 . ASN 116 116 16449 1 . ALA 117 117 16449 1 . ALA 118 118 16449 1 . ASN 119 119 16449 1 . ALA 120 120 16449 1 . LYS 121 121 16449 1 . GLN 122 122 16449 1 . LEU 123 123 16449 1 . TYR 124 124 16449 1 . ASP 125 125 16449 1 . PHE 126 126 16449 1 . ILE 127 127 16449 1 . HIS 128 128 16449 1 . THR 129 129 16449 1 . SER 130 130 16449 1 . PHE 131 131 16449 1 . ALA 132 132 16449 1 . GLU 133 133 16449 1 . VAL 134 134 16449 1 stop_ save_ save_DNA _Entity.Sf_category entity _Entity.Sf_framecode DNA _Entity.Entry_ID 16449 _Entity.ID 2 _Entity.BMRB_code . _Entity.Name DNA _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polydeoxyribonucleotide _Entity.Polymer_type_details . _Entity.Polymer_strand_ID B _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code CAGTGGCTGA _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 10 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not present' _Entity.Src_method man _Entity.Parent_entity_ID 2 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date . loop_ _Entity_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 . DC . 16449 2 2 . DA . 16449 2 3 . DG . 16449 2 4 . DT . 16449 2 5 . DG . 16449 2 6 . DG . 16449 2 7 . DC . 16449 2 8 . DT . 16449 2 9 . DG . 16449 2 10 . DA . 16449 2 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 . DC 1 1 16449 2 . DA 2 2 16449 2 . DG 3 3 16449 2 . DT 4 4 16449 2 . DG 5 5 16449 2 . DG 6 6 16449 2 . DC 7 7 16449 2 . DT 8 8 16449 2 . DG 9 9 16449 2 . DA 10 10 16449 2 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 16449 _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 $entity_1 . 9606 organism . 'Homo sapiens' Human . . Eukaryota Metazoa Homo sapiens . wild . . . . . . . . . . . . . . XPF . . . . 16449 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 16449 _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 $entity_1 . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . pet28B . . . . . . 16449 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_XPF-ssDNAcomplex _Sample.Sf_category sample _Sample.Sf_framecode XPF-ssDNAcomplex _Sample.Entry_ID 16449 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system '95% H2O/5% 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 'sodium phosphate' 'natural abundance' . . . . . . 80 . . mM . . . . 16449 1 2 'sodium chloride' 'natural abundance' . . . . . . 2 . . mM . . . . 16449 1 3 'AEBSF protease inhibitor' 'natural abundance' . . . . . . . 5 10 uM . . . . 16449 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 16449 _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' 100 . mM 16449 1 pH 5.2 0.2 pH 16449 1 pressure 1 . atm 16449 1 temperature 293.6 . K 16449 1 stop_ save_ ############################ # Computer software used # ############################ save_xwinnmr _Software.Sf_category software _Software.Sf_framecode xwinnmr _Software.Entry_ID 16449 _Software.ID 1 _Software.Name xwinnmr _Software.Version 3.5 _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Bruker Biospin' . . 16449 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID processing 16449 1 stop_ save_ save_CYANA _Software.Sf_category software _Software.Sf_framecode CYANA _Software.Entry_ID 16449 _Software.ID 2 _Software.Name CYANA _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Herrmann, Guntert and Wuthrich' . . 16449 2 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'structure solution' 16449 2 stop_ save_ save_CNS _Software.Sf_category software _Software.Sf_framecode CNS _Software.Entry_ID 16449 _Software.ID 3 _Software.Name CNS _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID 'Brunger, Adams, Clore, Gros, Nilges and Read' . . 16449 3 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID refinement 16449 3 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 16449 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model Avance _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 900 save_ save_spectrometer_2 _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_2 _NMR_spectrometer.Entry_ID 16449 _NMR_spectrometer.ID 2 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DRX _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 16449 _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 Bruker Avance . 900 . . . 16449 1 2 spectrometer_2 Bruker DRX . 600 . . . 16449 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 16449 _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 '3D 1H-13C NOESY' no . . . . . . . . . . 1 $XPF-ssDNAcomplex isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 16449 1 2 '3D 1H-15N NOESY' no . . . . . . . . . . 1 $XPF-ssDNAcomplex isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 16449 1 3 '3D CBCA(CO)NH' no . . . . . . . . . . 1 $XPF-ssDNAcomplex isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 16449 1 4 '2D 1H-15N HSQC' no . . . . . . . . . . 1 $XPF-ssDNAcomplex isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 16449 1 5 '2D 1H-13C HSQC' no . . . . . . . . . . 1 $XPF-ssDNAcomplex isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 16449 1 6 '3D HCCH-TOCSY' no . . . . . . . . . . 1 $XPF-ssDNAcomplex isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 16449 1 7 '3D C(CO)NH' no . . . . . . . . . . 1 $XPF-ssDNAcomplex isotropic . . 1 $sample_conditions_1 . . . . . . . . . . . . . . . . . . . . . 16449 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 16449 _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 water protons . . . . ppm 0 na direct . . . . . . . . . . 16449 1 H 1 water protons . . . . ppm 0 external direct 1 . . . . . . . . . 16449 1 N 15 water protons . . . . ppm 0 na direct . . . . . . . . . . 16449 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 16449 _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 '3D 1H-13C NOESY' . . . 16449 1 2 '3D 1H-15N NOESY' . . . 16449 1 5 '2D 1H-13C HSQC' . . . 16449 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 LYS HA H 1 4.332 0.000 . . . . . . 11 LYS HA . 16449 1 2 . 1 1 2 2 LYS HB3 H 1 1.771 0.000 . . . . . . 11 LYS HB3 . 16449 1 3 . 1 1 2 2 LYS CB C 13 34.399 0.000 . . . . . . 11 LYS CB . 16449 1 4 . 1 1 3 3 TYR HA H 1 4.646 0.000 . . . . . . 12 TYR HA . 16449 1 5 . 1 1 3 3 TYR HB2 H 1 3.021 0.007 . . . . . . 12 TYR HB2 . 16449 1 6 . 1 1 3 3 TYR HB3 H 1 3.021 0.007 . . . . . . 12 TYR HB3 . 16449 1 7 . 1 1 3 3 TYR HD1 H 1 7.128 0.027 . . . . . . 12 TYR QD . 16449 1 8 . 1 1 3 3 TYR HD2 H 1 7.128 0.027 . . . . . . 12 TYR QD . 16449 1 9 . 1 1 3 3 TYR HE1 H 1 6.840 0.010 . . . . . . 12 TYR QE . 16449 1 10 . 1 1 3 3 TYR HE2 H 1 6.840 0.010 . . . . . . 12 TYR QE . 16449 1 11 . 1 1 3 3 TYR CA C 13 58.990 0.022 . . . . . . 12 TYR CA . 16449 1 12 . 1 1 3 3 TYR CB C 13 40.218 0.012 . . . . . . 12 TYR CB . 16449 1 13 . 1 1 3 3 TYR CD1 C 13 134.283 0.152 . . . . . . 12 TYR CD . 16449 1 14 . 1 1 3 3 TYR CD2 C 13 134.283 0.152 . . . . . . 12 TYR CD . 16449 1 15 . 1 1 3 3 TYR CE1 C 13 134.400 0.000 . . . . . . 12 TYR CE . 16449 1 16 . 1 1 3 3 TYR CE2 C 13 134.400 0.000 . . . . . . 12 TYR CE . 16449 1 17 . 1 1 4 4 ASN H H 1 8.499 0.003 . . . . . . 13 ASN H . 16449 1 18 . 1 1 4 4 ASN HA H 1 5.044 0.000 . . . . . . 13 ASN HA . 16449 1 19 . 1 1 4 4 ASN HB2 H 1 2.819 0.007 . . . . . . 13 ASN HB2 . 16449 1 20 . 1 1 4 4 ASN HB3 H 1 2.658 0.005 . . . . . . 13 ASN HB3 . 16449 1 21 . 1 1 4 4 ASN HD21 H 1 7.022 0.008 . . . . . . 13 ASN HD21 . 16449 1 22 . 1 1 4 4 ASN HD22 H 1 7.745 0.004 . . . . . . 13 ASN HD22 . 16449 1 23 . 1 1 4 4 ASN CA C 13 52.014 0.173 . . . . . . 13 ASN CA . 16449 1 24 . 1 1 4 4 ASN CB C 13 40.547 0.070 . . . . . . 13 ASN CB . 16449 1 25 . 1 1 4 4 ASN N N 15 123.868 0.146 . . . . . . 13 ASN N . 16449 1 26 . 1 1 4 4 ASN ND2 N 15 113.139 0.091 . . . . . . 13 ASN ND2 . 16449 1 27 . 1 1 5 5 PRO HA H 1 4.538 0.000 . . . . . . 14 PRO HA . 16449 1 28 . 1 1 5 5 PRO HB2 H 1 2.364 0.000 . . . . . . 14 PRO HB2 . 16449 1 29 . 1 1 5 5 PRO HB3 H 1 2.117 0.000 . . . . . . 14 PRO HB3 . 16449 1 30 . 1 1 5 5 PRO HG2 H 1 2.058 0.023 . . . . . . 14 PRO HG2 . 16449 1 31 . 1 1 5 5 PRO HG3 H 1 2.058 0.023 . . . . . . 14 PRO HG3 . 16449 1 32 . 1 1 5 5 PRO HD2 H 1 3.731 0.025 . . . . . . 14 PRO HD2 . 16449 1 33 . 1 1 5 5 PRO HD3 H 1 3.446 0.014 . . . . . . 14 PRO HD3 . 16449 1 34 . 1 1 5 5 PRO CA C 13 64.395 0.090 . . . . . . 14 PRO CA . 16449 1 35 . 1 1 5 5 PRO CB C 13 33.610 0.235 . . . . . . 14 PRO CB . 16449 1 36 . 1 1 5 5 PRO CG C 13 28.519 0.250 . . . . . . 14 PRO CG . 16449 1 37 . 1 1 5 5 PRO CD C 13 51.776 0.097 . . . . . . 14 PRO CD . 16449 1 38 . 1 1 6 6 GLY H H 1 8.992 0.012 . . . . . . 15 GLY H . 16449 1 39 . 1 1 6 6 GLY HA2 H 1 4.721 0.000 . . . . . . 15 GLY HA2 . 16449 1 40 . 1 1 6 6 GLY HA3 H 1 4.232 0.003 . . . . . . 15 GLY HA3 . 16449 1 41 . 1 1 6 6 GLY CA C 13 46.033 0.088 . . . . . . 15 GLY CA . 16449 1 42 . 1 1 6 6 GLY N N 15 108.966 0.106 . . . . . . 15 GLY N . 16449 1 43 . 1 1 7 7 PRO HA H 1 4.212 0.000 . . . . . . 16 PRO HA . 16449 1 44 . 1 1 7 7 PRO HB2 H 1 1.950 0.000 . . . . . . 16 PRO HB2 . 16449 1 45 . 1 1 7 7 PRO HB3 H 1 1.950 0.000 . . . . . . 16 PRO HB3 . 16449 1 46 . 1 1 7 7 PRO HG2 H 1 1.905 0.028 . . . . . . 16 PRO HG2 . 16449 1 47 . 1 1 7 7 PRO HG3 H 1 1.630 0.007 . . . . . . 16 PRO HG3 . 16449 1 48 . 1 1 7 7 PRO HD2 H 1 3.976 0.007 . . . . . . 16 PRO HD2 . 16449 1 49 . 1 1 7 7 PRO HD3 H 1 3.647 0.020 . . . . . . 16 PRO HD3 . 16449 1 50 . 1 1 7 7 PRO CA C 13 66.936 0.199 . . . . . . 16 PRO CA . 16449 1 51 . 1 1 7 7 PRO CB C 13 33.463 0.130 . . . . . . 16 PRO CB . 16449 1 52 . 1 1 7 7 PRO CG C 13 28.953 0.067 . . . . . . 16 PRO CG . 16449 1 53 . 1 1 7 7 PRO CD C 13 50.935 0.080 . . . . . . 16 PRO CD . 16449 1 54 . 1 1 8 8 GLN H H 1 9.325 0.020 . . . . . . 17 GLN H . 16449 1 55 . 1 1 8 8 GLN HA H 1 4.005 0.008 . . . . . . 17 GLN HA . 16449 1 56 . 1 1 8 8 GLN HB2 H 1 2.314 0.001 . . . . . . 17 GLN HB2 . 16449 1 57 . 1 1 8 8 GLN HB3 H 1 2.314 0.001 . . . . . . 17 GLN HB3 . 16449 1 58 . 1 1 8 8 GLN HG2 H 1 2.450 0.012 . . . . . . 17 GLN HG2 . 16449 1 59 . 1 1 8 8 GLN HG3 H 1 2.450 0.012 . . . . . . 17 GLN HG3 . 16449 1 60 . 1 1 8 8 GLN HE21 H 1 7.110 0.000 . . . . . . 17 GLN HE21 . 16449 1 61 . 1 1 8 8 GLN HE22 H 1 7.316 0.000 . . . . . . 17 GLN HE22 . 16449 1 62 . 1 1 8 8 GLN CA C 13 60.893 0.241 . . . . . . 17 GLN CA . 16449 1 63 . 1 1 8 8 GLN CB C 13 29.196 0.055 . . . . . . 17 GLN CB . 16449 1 64 . 1 1 8 8 GLN CG C 13 35.497 0.202 . . . . . . 17 GLN CG . 16449 1 65 . 1 1 8 8 GLN N N 15 118.101 0.115 . . . . . . 17 GLN N . 16449 1 66 . 1 1 8 8 GLN NE2 N 15 110.658 0.272 . . . . . . 17 GLN NE2 . 16449 1 67 . 1 1 9 9 ASP H H 1 7.916 0.008 . . . . . . 18 ASP H . 16449 1 68 . 1 1 9 9 ASP HA H 1 4.469 0.000 . . . . . . 18 ASP HA . 16449 1 69 . 1 1 9 9 ASP HB2 H 1 3.034 0.000 . . . . . . 18 ASP HB2 . 16449 1 70 . 1 1 9 9 ASP HB3 H 1 2.809 0.000 . . . . . . 18 ASP HB3 . 16449 1 71 . 1 1 9 9 ASP CA C 13 58.500 0.118 . . . . . . 18 ASP CA . 16449 1 72 . 1 1 9 9 ASP CB C 13 42.556 0.116 . . . . . . 18 ASP CB . 16449 1 73 . 1 1 9 9 ASP N N 15 118.243 0.134 . . . . . . 18 ASP N . 16449 1 74 . 1 1 10 10 PHE H H 1 7.745 0.008 . . . . . . 19 PHE H . 16449 1 75 . 1 1 10 10 PHE HA H 1 4.272 0.000 . . . . . . 19 PHE HA . 16449 1 76 . 1 1 10 10 PHE HB2 H 1 3.559 0.004 . . . . . . 19 PHE HB2 . 16449 1 77 . 1 1 10 10 PHE HB3 H 1 3.356 0.000 . . . . . . 19 PHE HB3 . 16449 1 78 . 1 1 10 10 PHE HD1 H 1 7.321 0.003 . . . . . . 19 PHE QD . 16449 1 79 . 1 1 10 10 PHE HD2 H 1 7.321 0.003 . . . . . . 19 PHE QD . 16449 1 80 . 1 1 10 10 PHE HE1 H 1 6.737 0.010 . . . . . . 19 PHE QE . 16449 1 81 . 1 1 10 10 PHE HE2 H 1 6.737 0.010 . . . . . . 19 PHE QE . 16449 1 82 . 1 1 10 10 PHE HZ H 1 6.369 0.008 . . . . . . 19 PHE HZ . 16449 1 83 . 1 1 10 10 PHE CA C 13 62.154 0.067 . . . . . . 19 PHE CA . 16449 1 84 . 1 1 10 10 PHE CB C 13 40.638 0.074 . . . . . . 19 PHE CB . 16449 1 85 . 1 1 10 10 PHE N N 15 118.248 0.111 . . . . . . 19 PHE N . 16449 1 86 . 1 1 11 11 LEU H H 1 8.252 0.014 . . . . . . 20 LEU H . 16449 1 87 . 1 1 11 11 LEU HA H 1 4.037 0.015 . . . . . . 20 LEU HA . 16449 1 88 . 1 1 11 11 LEU HB2 H 1 1.482 0.000 . . . . . . 20 LEU HB2 . 16449 1 89 . 1 1 11 11 LEU HB3 H 1 1.482 0.000 . . . . . . 20 LEU HB3 . 16449 1 90 . 1 1 11 11 LEU HG H 1 1.480 0.000 . . . . . . 20 LEU HG . 16449 1 91 . 1 1 11 11 LEU HD11 H 1 0.217 0.000 . . . . . . 20 LEU QD1 . 16449 1 92 . 1 1 11 11 LEU HD12 H 1 0.217 0.000 . . . . . . 20 LEU QD1 . 16449 1 93 . 1 1 11 11 LEU HD13 H 1 0.217 0.000 . . . . . . 20 LEU QD1 . 16449 1 94 . 1 1 11 11 LEU HD21 H 1 0.672 0.000 . . . . . . 20 LEU QD2 . 16449 1 95 . 1 1 11 11 LEU HD22 H 1 0.672 0.000 . . . . . . 20 LEU QD2 . 16449 1 96 . 1 1 11 11 LEU HD23 H 1 0.672 0.000 . . . . . . 20 LEU QD2 . 16449 1 97 . 1 1 11 11 LEU CA C 13 59.541 0.250 . . . . . . 20 LEU CA . 16449 1 98 . 1 1 11 11 LEU CB C 13 43.561 0.166 . . . . . . 20 LEU CB . 16449 1 99 . 1 1 11 11 LEU CD1 C 13 25.616 0.058 . . . . . . 20 LEU CD1 . 16449 1 100 . 1 1 11 11 LEU CD2 C 13 25.694 0.000 . . . . . . 20 LEU CD2 . 16449 1 101 . 1 1 11 11 LEU N N 15 120.011 0.091 . . . . . . 20 LEU N . 16449 1 102 . 1 1 12 12 LEU H H 1 7.498 0.008 . . . . . . 21 LEU H . 16449 1 103 . 1 1 12 12 LEU HA H 1 3.898 0.006 . . . . . . 21 LEU HA . 16449 1 104 . 1 1 12 12 LEU HB2 H 1 1.834 0.000 . . . . . . 21 LEU HB2 . 16449 1 105 . 1 1 12 12 LEU HB3 H 1 1.637 0.000 . . . . . . 21 LEU HB3 . 16449 1 106 . 1 1 12 12 LEU HG H 1 1.855 0.007 . . . . . . 21 LEU HG . 16449 1 107 . 1 1 12 12 LEU HD11 H 1 0.831 0.000 . . . . . . 21 LEU QD1 . 16449 1 108 . 1 1 12 12 LEU HD12 H 1 0.831 0.000 . . . . . . 21 LEU QD1 . 16449 1 109 . 1 1 12 12 LEU HD13 H 1 0.831 0.000 . . . . . . 21 LEU QD1 . 16449 1 110 . 1 1 12 12 LEU HD21 H 1 0.942 0.000 . . . . . . 21 LEU QD2 . 16449 1 111 . 1 1 12 12 LEU HD22 H 1 0.942 0.000 . . . . . . 21 LEU QD2 . 16449 1 112 . 1 1 12 12 LEU HD23 H 1 0.942 0.000 . . . . . . 21 LEU QD2 . 16449 1 113 . 1 1 12 12 LEU CA C 13 57.409 0.112 . . . . . . 21 LEU CA . 16449 1 114 . 1 1 12 12 LEU CB C 13 43.198 0.007 . . . . . . 21 LEU CB . 16449 1 115 . 1 1 12 12 LEU CG C 13 28.947 0.074 . . . . . . 21 LEU CG . 16449 1 116 . 1 1 12 12 LEU CD1 C 13 24.157 0.292 . . . . . . 21 LEU CD1 . 16449 1 117 . 1 1 12 12 LEU CD2 C 13 26.255 0.134 . . . . . . 21 LEU CD2 . 16449 1 118 . 1 1 12 12 LEU N N 15 112.710 0.113 . . . . . . 21 LEU N . 16449 1 119 . 1 1 13 13 LYS H H 1 7.351 0.004 . . . . . . 22 LYS H . 16449 1 120 . 1 1 13 13 LYS HA H 1 4.404 0.003 . . . . . . 22 LYS HA . 16449 1 121 . 1 1 13 13 LYS HB2 H 1 2.100 0.000 . . . . . . 22 LYS HB2 . 16449 1 122 . 1 1 13 13 LYS HB3 H 1 1.889 0.005 . . . . . . 22 LYS HB3 . 16449 1 123 . 1 1 13 13 LYS HG2 H 1 1.598 0.000 . . . . . . 22 LYS HG2 . 16449 1 124 . 1 1 13 13 LYS HG3 H 1 1.444 0.000 . . . . . . 22 LYS HG3 . 16449 1 125 . 1 1 13 13 LYS HD2 H 1 1.617 0.018 . . . . . . 22 LYS HD2 . 16449 1 126 . 1 1 13 13 LYS HD3 H 1 1.515 0.010 . . . . . . 22 LYS HD3 . 16449 1 127 . 1 1 13 13 LYS HE3 H 1 2.899 0.013 . . . . . . 22 LYS HE3 . 16449 1 128 . 1 1 13 13 LYS CA C 13 56.713 0.120 . . . . . . 22 LYS CA . 16449 1 129 . 1 1 13 13 LYS CB C 13 34.464 0.157 . . . . . . 22 LYS CB . 16449 1 130 . 1 1 13 13 LYS CG C 13 26.298 0.078 . . . . . . 22 LYS CG . 16449 1 131 . 1 1 13 13 LYS CD C 13 29.960 0.180 . . . . . . 22 LYS CD . 16449 1 132 . 1 1 13 13 LYS CE C 13 43.415 0.023 . . . . . . 22 LYS CE . 16449 1 133 . 1 1 13 13 LYS N N 15 115.745 0.071 . . . . . . 22 LYS N . 16449 1 134 . 1 1 14 14 MET H H 1 7.738 0.005 . . . . . . 23 MET H . 16449 1 135 . 1 1 14 14 MET HA H 1 3.687 0.000 . . . . . . 23 MET HA . 16449 1 136 . 1 1 14 14 MET HB2 H 1 2.021 0.000 . . . . . . 23 MET HB2 . 16449 1 137 . 1 1 14 14 MET HB3 H 1 1.388 0.000 . . . . . . 23 MET HB3 . 16449 1 138 . 1 1 14 14 MET HG2 H 1 1.793 0.008 . . . . . . 23 MET HG2 . 16449 1 139 . 1 1 14 14 MET HG3 H 1 3.177 0.000 . . . . . . 23 MET HG3 . 16449 1 140 . 1 1 14 14 MET CA C 13 56.452 0.090 . . . . . . 23 MET CA . 16449 1 141 . 1 1 14 14 MET CB C 13 32.882 0.134 . . . . . . 23 MET CB . 16449 1 142 . 1 1 14 14 MET CG C 13 35.219 0.211 . . . . . . 23 MET CG . 16449 1 143 . 1 1 14 14 MET N N 15 121.105 0.041 . . . . . . 23 MET N . 16449 1 144 . 1 1 15 15 PRO HA H 1 4.117 0.005 . . . . . . 24 PRO HA . 16449 1 145 . 1 1 15 15 PRO HB2 H 1 2.201 0.000 . . . . . . 24 PRO HB2 . 16449 1 146 . 1 1 15 15 PRO HB3 H 1 1.639 0.006 . . . . . . 24 PRO HB3 . 16449 1 147 . 1 1 15 15 PRO HG2 H 1 1.842 0.000 . . . . . . 24 PRO HG2 . 16449 1 148 . 1 1 15 15 PRO HG3 H 1 1.756 0.005 . . . . . . 24 PRO HG3 . 16449 1 149 . 1 1 15 15 PRO HD2 H 1 2.748 0.014 . . . . . . 24 PRO HD2 . 16449 1 150 . 1 1 15 15 PRO HD3 H 1 1.942 0.004 . . . . . . 24 PRO HD3 . 16449 1 151 . 1 1 15 15 PRO CA C 13 64.908 0.089 . . . . . . 24 PRO CA . 16449 1 152 . 1 1 15 15 PRO CB C 13 33.358 0.086 . . . . . . 24 PRO CB . 16449 1 153 . 1 1 15 15 PRO CG C 13 29.533 0.309 . . . . . . 24 PRO CG . 16449 1 154 . 1 1 15 15 PRO CD C 13 50.466 0.009 . . . . . . 24 PRO CD . 16449 1 155 . 1 1 16 16 GLY H H 1 8.047 0.001 . . . . . . 25 GLY H . 16449 1 156 . 1 1 16 16 GLY HA2 H 1 4.534 0.004 . . . . . . 25 GLY HA2 . 16449 1 157 . 1 1 16 16 GLY HA3 H 1 3.426 0.000 . . . . . . 25 GLY HA3 . 16449 1 158 . 1 1 16 16 GLY CA C 13 46.145 0.135 . . . . . . 25 GLY CA . 16449 1 159 . 1 1 16 16 GLY N N 15 106.890 0.027 . . . . . . 25 GLY N . 16449 1 160 . 1 1 17 17 VAL H H 1 7.511 0.002 . . . . . . 26 VAL H . 16449 1 161 . 1 1 17 17 VAL HA H 1 4.351 0.004 . . . . . . 26 VAL HA . 16449 1 162 . 1 1 17 17 VAL HB H 1 2.223 0.004 . . . . . . 26 VAL HB . 16449 1 163 . 1 1 17 17 VAL HG11 H 1 0.724 0.006 . . . . . . 26 VAL QG1 . 16449 1 164 . 1 1 17 17 VAL HG12 H 1 0.724 0.006 . . . . . . 26 VAL QG1 . 16449 1 165 . 1 1 17 17 VAL HG13 H 1 0.724 0.006 . . . . . . 26 VAL QG1 . 16449 1 166 . 1 1 17 17 VAL HG21 H 1 0.841 0.009 . . . . . . 26 VAL QG2 . 16449 1 167 . 1 1 17 17 VAL HG22 H 1 0.841 0.009 . . . . . . 26 VAL QG2 . 16449 1 168 . 1 1 17 17 VAL HG23 H 1 0.841 0.009 . . . . . . 26 VAL QG2 . 16449 1 169 . 1 1 17 17 VAL CA C 13 63.178 0.038 . . . . . . 26 VAL CA . 16449 1 170 . 1 1 17 17 VAL CB C 13 32.850 0.106 . . . . . . 26 VAL CB . 16449 1 171 . 1 1 17 17 VAL CG1 C 13 24.485 0.080 . . . . . . 26 VAL CG1 . 16449 1 172 . 1 1 17 17 VAL CG2 C 13 23.806 0.008 . . . . . . 26 VAL CG2 . 16449 1 173 . 1 1 17 17 VAL N N 15 119.810 0.076 . . . . . . 26 VAL N . 16449 1 174 . 1 1 18 18 ASN H H 1 9.254 0.007 . . . . . . 27 ASN H . 16449 1 175 . 1 1 18 18 ASN HA H 1 4.915 0.019 . . . . . . 27 ASN HA . 16449 1 176 . 1 1 18 18 ASN HB2 H 1 3.161 0.019 . . . . . . 27 ASN HB2 . 16449 1 177 . 1 1 18 18 ASN HB3 H 1 2.879 0.023 . . . . . . 27 ASN HB3 . 16449 1 178 . 1 1 18 18 ASN HD21 H 1 6.627 0.004 . . . . . . 27 ASN HD21 . 16449 1 179 . 1 1 18 18 ASN HD22 H 1 7.807 0.000 . . . . . . 27 ASN HD22 . 16449 1 180 . 1 1 18 18 ASN CA C 13 52.870 0.000 . . . . . . 27 ASN CA . 16449 1 181 . 1 1 18 18 ASN CB C 13 41.875 0.143 . . . . . . 27 ASN CB . 16449 1 182 . 1 1 18 18 ASN N N 15 123.452 0.200 . . . . . . 27 ASN N . 16449 1 183 . 1 1 18 18 ASN ND2 N 15 115.270 0.009 . . . . . . 27 ASN ND2 . 16449 1 184 . 1 1 19 19 ALA H H 1 8.646 0.009 . . . . . . 28 ALA H . 16449 1 185 . 1 1 19 19 ALA HA H 1 4.148 0.000 . . . . . . 28 ALA HA . 16449 1 186 . 1 1 19 19 ALA HB1 H 1 1.526 0.005 . . . . . . 28 ALA QB . 16449 1 187 . 1 1 19 19 ALA HB2 H 1 1.526 0.005 . . . . . . 28 ALA QB . 16449 1 188 . 1 1 19 19 ALA HB3 H 1 1.526 0.005 . . . . . . 28 ALA QB . 16449 1 189 . 1 1 19 19 ALA CA C 13 56.360 0.091 . . . . . . 28 ALA CA . 16449 1 190 . 1 1 19 19 ALA CB C 13 19.797 0.040 . . . . . . 28 ALA CB . 16449 1 191 . 1 1 19 19 ALA N N 15 118.938 0.251 . . . . . . 28 ALA N . 16449 1 192 . 1 1 20 20 LYS H H 1 8.290 0.005 . . . . . . 29 LYS H . 16449 1 193 . 1 1 20 20 LYS HA H 1 4.348 0.001 . . . . . . 29 LYS HA . 16449 1 194 . 1 1 20 20 LYS HB2 H 1 1.942 0.003 . . . . . . 29 LYS HB2 . 16449 1 195 . 1 1 20 20 LYS HB3 H 1 1.942 0.003 . . . . . . 29 LYS HB3 . 16449 1 196 . 1 1 20 20 LYS HG2 H 1 1.569 0.001 . . . . . . 29 LYS HG2 . 16449 1 197 . 1 1 20 20 LYS HG3 H 1 1.475 0.002 . . . . . . 29 LYS HG3 . 16449 1 198 . 1 1 20 20 LYS HD2 H 1 1.756 0.006 . . . . . . 29 LYS HD2 . 16449 1 199 . 1 1 20 20 LYS HE3 H 1 3.059 0.011 . . . . . . 29 LYS HE3 . 16449 1 200 . 1 1 20 20 LYS CA C 13 59.342 0.118 . . . . . . 29 LYS CA . 16449 1 201 . 1 1 20 20 LYS CB C 13 33.906 0.177 . . . . . . 29 LYS CB . 16449 1 202 . 1 1 20 20 LYS CG C 13 26.422 0.210 . . . . . . 29 LYS CG . 16449 1 203 . 1 1 20 20 LYS CD C 13 30.520 0.126 . . . . . . 29 LYS CD . 16449 1 204 . 1 1 20 20 LYS CE C 13 43.180 0.000 . . . . . . 29 LYS CE . 16449 1 205 . 1 1 20 20 LYS N N 15 116.306 0.117 . . . . . . 29 LYS N . 16449 1 206 . 1 1 21 21 ASN H H 1 8.491 0.005 . . . . . . 30 ASN H . 16449 1 207 . 1 1 21 21 ASN HA H 1 4.820 0.005 . . . . . . 30 ASN HA . 16449 1 208 . 1 1 21 21 ASN HB2 H 1 3.210 0.007 . . . . . . 30 ASN HB2 . 16449 1 209 . 1 1 21 21 ASN HB3 H 1 2.933 0.011 . . . . . . 30 ASN HB3 . 16449 1 210 . 1 1 21 21 ASN HD21 H 1 7.629 0.005 . . . . . . 30 ASN HD21 . 16449 1 211 . 1 1 21 21 ASN HD22 H 1 7.873 0.004 . . . . . . 30 ASN HD22 . 16449 1 212 . 1 1 21 21 ASN CA C 13 54.843 0.029 . . . . . . 30 ASN CA . 16449 1 213 . 1 1 21 21 ASN CB C 13 40.223 0.099 . . . . . . 30 ASN CB . 16449 1 214 . 1 1 21 21 ASN N N 15 117.751 0.076 . . . . . . 30 ASN N . 16449 1 215 . 1 1 21 21 ASN ND2 N 15 108.930 0.189 . . . . . . 30 ASN ND2 . 16449 1 216 . 1 1 22 22 CYS H H 1 8.398 0.019 . . . . . . 31 CYS H . 16449 1 217 . 1 1 22 22 CYS HA H 1 4.019 0.009 . . . . . . 31 CYS HA . 16449 1 218 . 1 1 22 22 CYS HB2 H 1 3.050 0.003 . . . . . . 31 CYS HB2 . 16449 1 219 . 1 1 22 22 CYS HB3 H 1 2.788 0.000 . . . . . . 31 CYS HB3 . 16449 1 220 . 1 1 22 22 CYS CA C 13 63.140 0.129 . . . . . . 31 CYS CA . 16449 1 221 . 1 1 22 22 CYS CB C 13 27.619 0.140 . . . . . . 31 CYS CB . 16449 1 222 . 1 1 22 22 CYS N N 15 119.964 0.040 . . . . . . 31 CYS N . 16449 1 223 . 1 1 23 23 ARG H H 1 7.935 0.007 . . . . . . 32 ARG H . 16449 1 224 . 1 1 23 23 ARG HA H 1 4.030 0.006 . . . . . . 32 ARG HA . 16449 1 225 . 1 1 23 23 ARG HB2 H 1 1.977 0.009 . . . . . . 32 ARG HB2 . 16449 1 226 . 1 1 23 23 ARG HB3 H 1 1.910 0.000 . . . . . . 32 ARG HB3 . 16449 1 227 . 1 1 23 23 ARG HG2 H 1 1.887 0.010 . . . . . . 32 ARG HG2 . 16449 1 228 . 1 1 23 23 ARG HG3 H 1 1.659 0.000 . . . . . . 32 ARG HG3 . 16449 1 229 . 1 1 23 23 ARG HD2 H 1 3.282 0.000 . . . . . . 32 ARG HD2 . 16449 1 230 . 1 1 23 23 ARG CA C 13 60.569 0.000 . . . . . . 32 ARG CA . 16449 1 231 . 1 1 23 23 ARG CB C 13 30.293 0.112 . . . . . . 32 ARG CB . 16449 1 232 . 1 1 23 23 ARG CG C 13 28.892 0.084 . . . . . . 32 ARG CG . 16449 1 233 . 1 1 23 23 ARG CD C 13 44.388 0.083 . . . . . . 32 ARG CD . 16449 1 234 . 1 1 23 23 ARG N N 15 120.387 0.210 . . . . . . 32 ARG N . 16449 1 235 . 1 1 24 24 SER H H 1 7.832 0.007 . . . . . . 33 SER H . 16449 1 236 . 1 1 24 24 SER HA H 1 4.435 0.001 . . . . . . 33 SER HA . 16449 1 237 . 1 1 24 24 SER HB2 H 1 4.125 0.002 . . . . . . 33 SER HB2 . 16449 1 238 . 1 1 24 24 SER HB3 H 1 4.125 0.002 . . . . . . 33 SER HB3 . 16449 1 239 . 1 1 24 24 SER CA C 13 62.559 0.008 . . . . . . 33 SER CA . 16449 1 240 . 1 1 24 24 SER CB C 13 64.003 0.162 . . . . . . 33 SER CB . 16449 1 241 . 1 1 24 24 SER N N 15 115.189 0.228 . . . . . . 33 SER N . 16449 1 242 . 1 1 25 25 LEU H H 1 7.815 0.001 . . . . . . 34 LEU H . 16449 1 243 . 1 1 25 25 LEU HA H 1 4.025 0.000 . . . . . . 34 LEU HA . 16449 1 244 . 1 1 25 25 LEU HB2 H 1 1.692 0.011 . . . . . . 34 LEU HB2 . 16449 1 245 . 1 1 25 25 LEU HB3 H 1 1.692 0.011 . . . . . . 34 LEU HB3 . 16449 1 246 . 1 1 25 25 LEU HG H 1 1.535 0.000 . . . . . . 34 LEU HG . 16449 1 247 . 1 1 25 25 LEU HD11 H 1 0.797 0.000 . . . . . . 34 LEU QD1 . 16449 1 248 . 1 1 25 25 LEU HD12 H 1 0.797 0.000 . . . . . . 34 LEU QD1 . 16449 1 249 . 1 1 25 25 LEU HD13 H 1 0.797 0.000 . . . . . . 34 LEU QD1 . 16449 1 250 . 1 1 25 25 LEU CA C 13 60.261 0.069 . . . . . . 34 LEU CA . 16449 1 251 . 1 1 25 25 LEU CB C 13 43.367 0.044 . . . . . . 34 LEU CB . 16449 1 252 . 1 1 25 25 LEU CG C 13 28.241 0.159 . . . . . . 34 LEU CG . 16449 1 253 . 1 1 25 25 LEU CD1 C 13 26.640 0.068 . . . . . . 34 LEU CD1 . 16449 1 254 . 1 1 25 25 LEU N N 15 121.166 0.060 . . . . . . 34 LEU N . 16449 1 255 . 1 1 26 26 MET H H 1 8.192 0.001 . . . . . . 35 MET H . 16449 1 256 . 1 1 26 26 MET HA H 1 4.433 0.004 . . . . . . 35 MET HA . 16449 1 257 . 1 1 26 26 MET HB2 H 1 2.155 0.031 . . . . . . 35 MET HB2 . 16449 1 258 . 1 1 26 26 MET HB3 H 1 2.155 0.031 . . . . . . 35 MET HB3 . 16449 1 259 . 1 1 26 26 MET HG2 H 1 2.616 0.007 . . . . . . 35 MET HG2 . 16449 1 260 . 1 1 26 26 MET HE1 H 1 1.968 0.004 . . . . . . 35 MET QE . 16449 1 261 . 1 1 26 26 MET HE2 H 1 1.968 0.004 . . . . . . 35 MET QE . 16449 1 262 . 1 1 26 26 MET HE3 H 1 1.968 0.004 . . . . . . 35 MET QE . 16449 1 263 . 1 1 26 26 MET CA C 13 59.679 0.123 . . . . . . 35 MET CA . 16449 1 264 . 1 1 26 26 MET CB C 13 34.445 0.025 . . . . . . 35 MET CB . 16449 1 265 . 1 1 26 26 MET CG C 13 33.597 0.182 . . . . . . 35 MET CG . 16449 1 266 . 1 1 26 26 MET CE C 13 17.601 0.000 . . . . . . 35 MET CE . 16449 1 267 . 1 1 26 26 MET N N 15 114.439 0.025 . . . . . . 35 MET N . 16449 1 268 . 1 1 27 27 HIS H H 1 7.824 0.002 . . . . . . 36 HIS H . 16449 1 269 . 1 1 27 27 HIS HA H 1 4.555 0.000 . . . . . . 36 HIS HA . 16449 1 270 . 1 1 27 27 HIS HB2 H 1 3.249 0.015 . . . . . . 36 HIS HB2 . 16449 1 271 . 1 1 27 27 HIS HB3 H 1 3.249 0.015 . . . . . . 36 HIS HB3 . 16449 1 272 . 1 1 27 27 HIS HD2 H 1 7.598 0.004 . . . . . . 36 HIS HD2 . 16449 1 273 . 1 1 27 27 HIS HE1 H 1 8.088 0.000 . . . . . . 36 HIS HE1 . 16449 1 274 . 1 1 27 27 HIS CA C 13 58.839 0.193 . . . . . . 36 HIS CA . 16449 1 275 . 1 1 27 27 HIS CB C 13 31.029 0.198 . . . . . . 36 HIS CB . 16449 1 276 . 1 1 27 27 HIS N N 15 115.880 0.161 . . . . . . 36 HIS N . 16449 1 277 . 1 1 27 27 HIS ND1 N 15 218.585 0.000 . . . . . . 36 HIS ND1 . 16449 1 278 . 1 1 27 27 HIS NE2 N 15 184.603 0.000 . . . . . . 36 HIS NE2 . 16449 1 279 . 1 1 28 28 HIS H H 1 7.830 0.000 . . . . . . 37 HIS H . 16449 1 280 . 1 1 28 28 HIS HA H 1 4.551 0.000 . . . . . . 37 HIS HA . 16449 1 281 . 1 1 28 28 HIS HB2 H 1 3.368 0.000 . . . . . . 37 HIS HB2 . 16449 1 282 . 1 1 28 28 HIS HB3 H 1 3.045 0.000 . . . . . . 37 HIS HB3 . 16449 1 283 . 1 1 28 28 HIS HD2 H 1 8.025 0.000 . . . . . . 37 HIS HD2 . 16449 1 284 . 1 1 28 28 HIS HE1 H 1 8.349 0.001 . . . . . . 37 HIS HE1 . 16449 1 285 . 1 1 28 28 HIS CB C 13 34.126 0.067 . . . . . . 37 HIS CB . 16449 1 286 . 1 1 28 28 HIS N N 15 115.130 0.000 . . . . . . 37 HIS N . 16449 1 287 . 1 1 28 28 HIS NE2 N 15 229.420 0.000 . . . . . . 37 HIS NE2 . 16449 1 288 . 1 1 29 29 VAL H H 1 8.377 0.005 . . . . . . 38 VAL H . 16449 1 289 . 1 1 29 29 VAL HA H 1 4.691 0.004 . . . . . . 38 VAL HA . 16449 1 290 . 1 1 29 29 VAL HB H 1 2.386 0.000 . . . . . . 38 VAL HB . 16449 1 291 . 1 1 29 29 VAL HG11 H 1 1.095 0.007 . . . . . . 38 VAL QG1 . 16449 1 292 . 1 1 29 29 VAL HG12 H 1 1.095 0.007 . . . . . . 38 VAL QG1 . 16449 1 293 . 1 1 29 29 VAL HG13 H 1 1.095 0.007 . . . . . . 38 VAL QG1 . 16449 1 294 . 1 1 29 29 VAL HG21 H 1 1.118 0.000 . . . . . . 38 VAL QG2 . 16449 1 295 . 1 1 29 29 VAL HG22 H 1 1.118 0.000 . . . . . . 38 VAL QG2 . 16449 1 296 . 1 1 29 29 VAL HG23 H 1 1.118 0.000 . . . . . . 38 VAL QG2 . 16449 1 297 . 1 1 29 29 VAL CA C 13 61.618 0.114 . . . . . . 38 VAL CA . 16449 1 298 . 1 1 29 29 VAL CB C 13 35.847 0.248 . . . . . . 38 VAL CB . 16449 1 299 . 1 1 29 29 VAL CG1 C 13 22.060 0.083 . . . . . . 38 VAL CG1 . 16449 1 300 . 1 1 29 29 VAL CG2 C 13 25.063 0.040 . . . . . . 38 VAL CG2 . 16449 1 301 . 1 1 29 29 VAL N N 15 116.430 0.265 . . . . . . 38 VAL N . 16449 1 302 . 1 1 30 30 LYS H H 1 8.714 0.007 . . . . . . 39 LYS H . 16449 1 303 . 1 1 30 30 LYS HA H 1 4.344 0.000 . . . . . . 39 LYS HA . 16449 1 304 . 1 1 30 30 LYS HB2 H 1 1.743 0.012 . . . . . . 39 LYS HB2 . 16449 1 305 . 1 1 30 30 LYS HB3 H 1 1.691 0.005 . . . . . . 39 LYS HB3 . 16449 1 306 . 1 1 30 30 LYS HG2 H 1 1.445 0.000 . . . . . . 39 LYS HG2 . 16449 1 307 . 1 1 30 30 LYS HG3 H 1 1.556 0.000 . . . . . . 39 LYS HG3 . 16449 1 308 . 1 1 30 30 LYS HD2 H 1 1.732 0.000 . . . . . . 39 LYS HD2 . 16449 1 309 . 1 1 30 30 LYS HD3 H 1 1.732 0.000 . . . . . . 39 LYS HD3 . 16449 1 310 . 1 1 30 30 LYS HE2 H 1 3.057 0.006 . . . . . . 39 LYS HE2 . 16449 1 311 . 1 1 30 30 LYS HE3 H 1 3.057 0.006 . . . . . . 39 LYS HE3 . 16449 1 312 . 1 1 30 30 LYS CA C 13 59.309 0.088 . . . . . . 39 LYS CA . 16449 1 313 . 1 1 30 30 LYS CB C 13 35.791 0.131 . . . . . . 39 LYS CB . 16449 1 314 . 1 1 30 30 LYS CG C 13 26.309 0.199 . . . . . . 39 LYS CG . 16449 1 315 . 1 1 30 30 LYS CD C 13 30.211 0.000 . . . . . . 39 LYS CD . 16449 1 316 . 1 1 30 30 LYS CE C 13 43.333 0.031 . . . . . . 39 LYS CE . 16449 1 317 . 1 1 30 30 LYS N N 15 119.605 0.073 . . . . . . 39 LYS N . 16449 1 318 . 1 1 31 31 ASN H H 1 7.038 0.009 . . . . . . 40 ASN H . 16449 1 319 . 1 1 31 31 ASN HA H 1 3.034 0.001 . . . . . . 40 ASN HA . 16449 1 320 . 1 1 31 31 ASN HB2 H 1 2.640 0.013 . . . . . . 40 ASN HB2 . 16449 1 321 . 1 1 31 31 ASN HB3 H 1 2.349 0.013 . . . . . . 40 ASN HB3 . 16449 1 322 . 1 1 31 31 ASN HD21 H 1 7.180 0.000 . . . . . . 40 ASN HD21 . 16449 1 323 . 1 1 31 31 ASN HD22 H 1 7.297 0.014 . . . . . . 40 ASN HD22 . 16449 1 324 . 1 1 31 31 ASN CA C 13 52.261 0.156 . . . . . . 40 ASN CA . 16449 1 325 . 1 1 31 31 ASN CB C 13 41.237 0.105 . . . . . . 40 ASN CB . 16449 1 326 . 1 1 31 31 ASN N N 15 110.201 0.076 . . . . . . 40 ASN N . 16449 1 327 . 1 1 31 31 ASN ND2 N 15 111.888 0.032 . . . . . . 40 ASN ND2 . 16449 1 328 . 1 1 32 32 ILE H H 1 8.902 0.011 . . . . . . 41 ILE H . 16449 1 329 . 1 1 32 32 ILE HA H 1 3.638 0.022 . . . . . . 41 ILE HA . 16449 1 330 . 1 1 32 32 ILE HB H 1 1.868 0.009 . . . . . . 41 ILE HB . 16449 1 331 . 1 1 32 32 ILE HG12 H 1 2.107 0.006 . . . . . . 41 ILE HG12 . 16449 1 332 . 1 1 32 32 ILE HG13 H 1 1.027 0.008 . . . . . . 41 ILE HG13 . 16449 1 333 . 1 1 32 32 ILE HG21 H 1 0.822 0.017 . . . . . . 41 ILE QG2 . 16449 1 334 . 1 1 32 32 ILE HG22 H 1 0.822 0.017 . . . . . . 41 ILE QG2 . 16449 1 335 . 1 1 32 32 ILE HG23 H 1 0.822 0.017 . . . . . . 41 ILE QG2 . 16449 1 336 . 1 1 32 32 ILE HD11 H 1 0.735 0.013 . . . . . . 41 ILE QD1 . 16449 1 337 . 1 1 32 32 ILE HD12 H 1 0.735 0.013 . . . . . . 41 ILE QD1 . 16449 1 338 . 1 1 32 32 ILE HD13 H 1 0.735 0.013 . . . . . . 41 ILE QD1 . 16449 1 339 . 1 1 32 32 ILE CA C 13 66.809 0.199 . . . . . . 41 ILE CA . 16449 1 340 . 1 1 32 32 ILE CB C 13 38.116 0.273 . . . . . . 41 ILE CB . 16449 1 341 . 1 1 32 32 ILE CG1 C 13 31.935 0.137 . . . . . . 41 ILE CG1 . 16449 1 342 . 1 1 32 32 ILE CG2 C 13 17.419 0.211 . . . . . . 41 ILE CG2 . 16449 1 343 . 1 1 32 32 ILE CD1 C 13 14.860 0.140 . . . . . . 41 ILE CD1 . 16449 1 344 . 1 1 32 32 ILE N N 15 119.961 0.094 . . . . . . 41 ILE N . 16449 1 345 . 1 1 33 33 ALA H H 1 7.513 0.006 . . . . . . 42 ALA H . 16449 1 346 . 1 1 33 33 ALA HA H 1 3.786 0.000 . . . . . . 42 ALA HA . 16449 1 347 . 1 1 33 33 ALA HB1 H 1 0.917 0.000 . . . . . . 42 ALA QB . 16449 1 348 . 1 1 33 33 ALA HB2 H 1 0.917 0.000 . . . . . . 42 ALA QB . 16449 1 349 . 1 1 33 33 ALA HB3 H 1 0.917 0.000 . . . . . . 42 ALA QB . 16449 1 350 . 1 1 33 33 ALA CA C 13 56.858 0.000 . . . . . . 42 ALA CA . 16449 1 351 . 1 1 33 33 ALA CB C 13 18.415 0.000 . . . . . . 42 ALA CB . 16449 1 352 . 1 1 33 33 ALA N N 15 122.343 0.020 . . . . . . 42 ALA N . 16449 1 353 . 1 1 34 34 GLU H H 1 8.567 0.003 . . . . . . 43 GLU H . 16449 1 354 . 1 1 34 34 GLU HA H 1 4.066 0.007 . . . . . . 43 GLU HA . 16449 1 355 . 1 1 34 34 GLU HB2 H 1 2.231 0.000 . . . . . . 43 GLU HB2 . 16449 1 356 . 1 1 34 34 GLU HB3 H 1 1.980 0.000 . . . . . . 43 GLU HB3 . 16449 1 357 . 1 1 34 34 GLU HG2 H 1 2.768 0.006 . . . . . . 43 GLU HG2 . 16449 1 358 . 1 1 34 34 GLU HG3 H 1 2.330 0.009 . . . . . . 43 GLU HG3 . 16449 1 359 . 1 1 34 34 GLU CA C 13 60.516 0.000 . . . . . . 43 GLU CA . 16449 1 360 . 1 1 34 34 GLU CB C 13 31.732 0.074 . . . . . . 43 GLU CB . 16449 1 361 . 1 1 34 34 GLU CG C 13 38.214 0.094 . . . . . . 43 GLU CG . 16449 1 362 . 1 1 34 34 GLU N N 15 117.127 0.046 . . . . . . 43 GLU N . 16449 1 363 . 1 1 35 35 LEU H H 1 7.947 0.014 . . . . . . 44 LEU H . 16449 1 364 . 1 1 35 35 LEU HA H 1 4.054 0.000 . . . . . . 44 LEU HA . 16449 1 365 . 1 1 35 35 LEU HB2 H 1 2.394 0.000 . . . . . . 44 LEU HB2 . 16449 1 366 . 1 1 35 35 LEU HB3 H 1 1.658 0.014 . . . . . . 44 LEU HB3 . 16449 1 367 . 1 1 35 35 LEU HG H 1 1.016 0.005 . . . . . . 44 LEU HG . 16449 1 368 . 1 1 35 35 LEU HD11 H 1 1.071 0.003 . . . . . . 44 LEU QD1 . 16449 1 369 . 1 1 35 35 LEU HD12 H 1 1.071 0.003 . . . . . . 44 LEU QD1 . 16449 1 370 . 1 1 35 35 LEU HD13 H 1 1.071 0.003 . . . . . . 44 LEU QD1 . 16449 1 371 . 1 1 35 35 LEU HD21 H 1 1.071 0.003 . . . . . . 44 LEU QD2 . 16449 1 372 . 1 1 35 35 LEU HD22 H 1 1.071 0.003 . . . . . . 44 LEU QD2 . 16449 1 373 . 1 1 35 35 LEU HD23 H 1 1.071 0.003 . . . . . . 44 LEU QD2 . 16449 1 374 . 1 1 35 35 LEU CA C 13 59.401 0.000 . . . . . . 44 LEU CA . 16449 1 375 . 1 1 35 35 LEU CB C 13 43.859 0.128 . . . . . . 44 LEU CB . 16449 1 376 . 1 1 35 35 LEU CG C 13 28.044 0.076 . . . . . . 44 LEU CG . 16449 1 377 . 1 1 35 35 LEU CD1 C 13 26.019 0.023 . . . . . . 44 LEU CD1 . 16449 1 378 . 1 1 35 35 LEU CD2 C 13 26.019 0.023 . . . . . . 44 LEU CD2 . 16449 1 379 . 1 1 35 35 LEU N N 15 120.781 0.155 . . . . . . 44 LEU N . 16449 1 380 . 1 1 36 36 ALA H H 1 8.383 0.004 . . . . . . 45 ALA H . 16449 1 381 . 1 1 36 36 ALA HA H 1 4.018 0.000 . . . . . . 45 ALA HA . 16449 1 382 . 1 1 36 36 ALA HB1 H 1 1.327 0.000 . . . . . . 45 ALA QB . 16449 1 383 . 1 1 36 36 ALA HB2 H 1 1.327 0.000 . . . . . . 45 ALA QB . 16449 1 384 . 1 1 36 36 ALA HB3 H 1 1.327 0.000 . . . . . . 45 ALA QB . 16449 1 385 . 1 1 36 36 ALA CA C 13 54.855 0.103 . . . . . . 45 ALA CA . 16449 1 386 . 1 1 36 36 ALA CB C 13 20.209 0.022 . . . . . . 45 ALA CB . 16449 1 387 . 1 1 36 36 ALA N N 15 115.895 0.048 . . . . . . 45 ALA N . 16449 1 388 . 1 1 37 37 ALA H H 1 7.216 0.004 . . . . . . 46 ALA H . 16449 1 389 . 1 1 37 37 ALA HA H 1 4.524 0.000 . . . . . . 46 ALA HA . 16449 1 390 . 1 1 37 37 ALA HB1 H 1 1.597 0.006 . . . . . . 46 ALA QB . 16449 1 391 . 1 1 37 37 ALA HB2 H 1 1.597 0.006 . . . . . . 46 ALA QB . 16449 1 392 . 1 1 37 37 ALA HB3 H 1 1.597 0.006 . . . . . . 46 ALA QB . 16449 1 393 . 1 1 37 37 ALA CA C 13 53.042 0.108 . . . . . . 46 ALA CA . 16449 1 394 . 1 1 37 37 ALA CB C 13 20.874 0.006 . . . . . . 46 ALA CB . 16449 1 395 . 1 1 37 37 ALA N N 15 117.692 0.090 . . . . . . 46 ALA N . 16449 1 396 . 1 1 38 38 LEU H H 1 7.352 0.005 . . . . . . 47 LEU H . 16449 1 397 . 1 1 38 38 LEU HA H 1 4.553 0.000 . . . . . . 47 LEU HA . 16449 1 398 . 1 1 38 38 LEU HB2 H 1 2.087 0.011 . . . . . . 47 LEU HB2 . 16449 1 399 . 1 1 38 38 LEU HB3 H 1 1.560 0.013 . . . . . . 47 LEU HB3 . 16449 1 400 . 1 1 38 38 LEU HG H 1 2.288 0.009 . . . . . . 47 LEU HG . 16449 1 401 . 1 1 38 38 LEU HD11 H 1 0.900 0.005 . . . . . . 47 LEU QD1 . 16449 1 402 . 1 1 38 38 LEU HD12 H 1 0.900 0.005 . . . . . . 47 LEU QD1 . 16449 1 403 . 1 1 38 38 LEU HD13 H 1 0.900 0.005 . . . . . . 47 LEU QD1 . 16449 1 404 . 1 1 38 38 LEU HD21 H 1 0.979 0.000 . . . . . . 47 LEU QD2 . 16449 1 405 . 1 1 38 38 LEU HD22 H 1 0.979 0.000 . . . . . . 47 LEU QD2 . 16449 1 406 . 1 1 38 38 LEU HD23 H 1 0.979 0.000 . . . . . . 47 LEU QD2 . 16449 1 407 . 1 1 38 38 LEU CA C 13 56.632 0.220 . . . . . . 47 LEU CA . 16449 1 408 . 1 1 38 38 LEU CB C 13 44.684 0.104 . . . . . . 47 LEU CB . 16449 1 409 . 1 1 38 38 LEU CG C 13 27.423 0.346 . . . . . . 47 LEU CG . 16449 1 410 . 1 1 38 38 LEU CD1 C 13 24.054 0.096 . . . . . . 47 LEU CD1 . 16449 1 411 . 1 1 38 38 LEU CD2 C 13 29.060 0.057 . . . . . . 47 LEU CD2 . 16449 1 412 . 1 1 38 38 LEU N N 15 119.218 0.000 . . . . . . 47 LEU N . 16449 1 413 . 1 1 39 39 SER H H 1 9.445 0.008 . . . . . . 48 SER H . 16449 1 414 . 1 1 39 39 SER HA H 1 4.726 0.000 . . . . . . 48 SER HA . 16449 1 415 . 1 1 39 39 SER HB2 H 1 4.402 0.005 . . . . . . 48 SER HB2 . 16449 1 416 . 1 1 39 39 SER HB3 H 1 4.171 0.004 . . . . . . 48 SER HB3 . 16449 1 417 . 1 1 39 39 SER CA C 13 58.307 0.058 . . . . . . 48 SER CA . 16449 1 418 . 1 1 39 39 SER CB C 13 66.776 0.068 . . . . . . 48 SER CB . 16449 1 419 . 1 1 39 39 SER N N 15 118.104 0.101 . . . . . . 48 SER N . 16449 1 420 . 1 1 40 40 GLN H H 1 8.670 0.006 . . . . . . 49 GLN H . 16449 1 421 . 1 1 40 40 GLN HA H 1 3.585 0.007 . . . . . . 49 GLN HA . 16449 1 422 . 1 1 40 40 GLN HB2 H 1 1.512 0.011 . . . . . . 49 GLN HB2 . 16449 1 423 . 1 1 40 40 GLN HB3 H 1 0.914 0.021 . . . . . . 49 GLN HB3 . 16449 1 424 . 1 1 40 40 GLN HG2 H 1 2.132 0.008 . . . . . . 49 GLN HG2 . 16449 1 425 . 1 1 40 40 GLN HG3 H 1 1.721 0.003 . . . . . . 49 GLN HG3 . 16449 1 426 . 1 1 40 40 GLN HE21 H 1 6.663 0.005 . . . . . . 49 GLN HE21 . 16449 1 427 . 1 1 40 40 GLN HE22 H 1 7.461 0.002 . . . . . . 49 GLN HE22 . 16449 1 428 . 1 1 40 40 GLN CA C 13 61.509 0.014 . . . . . . 49 GLN CA . 16449 1 429 . 1 1 40 40 GLN CB C 13 28.960 0.121 . . . . . . 49 GLN CB . 16449 1 430 . 1 1 40 40 GLN CG C 13 35.028 0.236 . . . . . . 49 GLN CG . 16449 1 431 . 1 1 40 40 GLN N N 15 122.245 0.098 . . . . . . 49 GLN N . 16449 1 432 . 1 1 40 40 GLN NE2 N 15 109.743 0.053 . . . . . . 49 GLN NE2 . 16449 1 433 . 1 1 41 41 ASP H H 1 8.632 0.005 . . . . . . 50 ASP H . 16449 1 434 . 1 1 41 41 ASP HA H 1 4.351 0.003 . . . . . . 50 ASP HA . 16449 1 435 . 1 1 41 41 ASP HB2 H 1 2.599 0.000 . . . . . . 50 ASP HB2 . 16449 1 436 . 1 1 41 41 ASP HB3 H 1 2.599 0.000 . . . . . . 50 ASP HB3 . 16449 1 437 . 1 1 41 41 ASP CA C 13 58.872 0.229 . . . . . . 50 ASP CA . 16449 1 438 . 1 1 41 41 ASP CB C 13 41.472 0.082 . . . . . . 50 ASP CB . 16449 1 439 . 1 1 41 41 ASP N N 15 120.017 0.115 . . . . . . 50 ASP N . 16449 1 440 . 1 1 42 42 GLU H H 1 8.076 0.002 . . . . . . 51 GLU H . 16449 1 441 . 1 1 42 42 GLU HA H 1 4.087 0.000 . . . . . . 51 GLU HA . 16449 1 442 . 1 1 42 42 GLU HB2 H 1 2.406 0.008 . . . . . . 51 GLU HB2 . 16449 1 443 . 1 1 42 42 GLU HB3 H 1 2.004 0.013 . . . . . . 51 GLU HB3 . 16449 1 444 . 1 1 42 42 GLU HG3 H 1 2.337 0.000 . . . . . . 51 GLU HG3 . 16449 1 445 . 1 1 42 42 GLU CA C 13 60.754 0.154 . . . . . . 51 GLU CA . 16449 1 446 . 1 1 42 42 GLU CB C 13 31.386 0.164 . . . . . . 51 GLU CB . 16449 1 447 . 1 1 42 42 GLU CG C 13 38.903 0.118 . . . . . . 51 GLU CG . 16449 1 448 . 1 1 42 42 GLU N N 15 122.061 0.070 . . . . . . 51 GLU N . 16449 1 449 . 1 1 43 43 LEU H H 1 8.422 0.008 . . . . . . 52 LEU H . 16449 1 450 . 1 1 43 43 LEU HA H 1 4.021 0.011 . . . . . . 52 LEU HA . 16449 1 451 . 1 1 43 43 LEU HB2 H 1 2.161 0.000 . . . . . . 52 LEU HB2 . 16449 1 452 . 1 1 43 43 LEU HB3 H 1 1.392 0.000 . . . . . . 52 LEU HB3 . 16449 1 453 . 1 1 43 43 LEU HG H 1 1.128 0.005 . . . . . . 52 LEU HG . 16449 1 454 . 1 1 43 43 LEU HD11 H 1 0.779 0.000 . . . . . . 52 LEU QD1 . 16449 1 455 . 1 1 43 43 LEU HD12 H 1 0.779 0.000 . . . . . . 52 LEU QD1 . 16449 1 456 . 1 1 43 43 LEU HD13 H 1 0.779 0.000 . . . . . . 52 LEU QD1 . 16449 1 457 . 1 1 43 43 LEU HD21 H 1 0.964 0.003 . . . . . . 52 LEU QD2 . 16449 1 458 . 1 1 43 43 LEU HD22 H 1 0.964 0.003 . . . . . . 52 LEU QD2 . 16449 1 459 . 1 1 43 43 LEU HD23 H 1 0.964 0.003 . . . . . . 52 LEU QD2 . 16449 1 460 . 1 1 43 43 LEU CA C 13 59.530 0.000 . . . . . . 52 LEU CA . 16449 1 461 . 1 1 43 43 LEU CB C 13 44.165 0.163 . . . . . . 52 LEU CB . 16449 1 462 . 1 1 43 43 LEU CG C 13 26.788 0.230 . . . . . . 52 LEU CG . 16449 1 463 . 1 1 43 43 LEU CD1 C 13 27.951 0.000 . . . . . . 52 LEU CD1 . 16449 1 464 . 1 1 43 43 LEU CD2 C 13 25.782 0.003 . . . . . . 52 LEU CD2 . 16449 1 465 . 1 1 43 43 LEU N N 15 118.734 0.166 . . . . . . 52 LEU N . 16449 1 466 . 1 1 44 44 THR H H 1 8.471 0.009 . . . . . . 53 THR H . 16449 1 467 . 1 1 44 44 THR HA H 1 4.463 0.001 . . . . . . 53 THR HA . 16449 1 468 . 1 1 44 44 THR HB H 1 3.569 0.000 . . . . . . 53 THR HB . 16449 1 469 . 1 1 44 44 THR HG21 H 1 1.079 0.008 . . . . . . 53 THR QG2 . 16449 1 470 . 1 1 44 44 THR HG22 H 1 1.079 0.008 . . . . . . 53 THR QG2 . 16449 1 471 . 1 1 44 44 THR HG23 H 1 1.079 0.008 . . . . . . 53 THR QG2 . 16449 1 472 . 1 1 44 44 THR CA C 13 69.034 0.001 . . . . . . 53 THR CA . 16449 1 473 . 1 1 44 44 THR CB C 13 69.165 0.180 . . . . . . 53 THR CB . 16449 1 474 . 1 1 44 44 THR CG2 C 13 22.561 0.170 . . . . . . 53 THR CG2 . 16449 1 475 . 1 1 44 44 THR N N 15 119.373 0.032 . . . . . . 53 THR N . 16449 1 476 . 1 1 45 45 SER H H 1 7.626 0.003 . . . . . . 54 SER H . 16449 1 477 . 1 1 45 45 SER HA H 1 4.188 0.000 . . . . . . 54 SER HA . 16449 1 478 . 1 1 45 45 SER HB2 H 1 3.991 0.000 . . . . . . 54 SER HB2 . 16449 1 479 . 1 1 45 45 SER HB3 H 1 3.991 0.000 . . . . . . 54 SER HB3 . 16449 1 480 . 1 1 45 45 SER CA C 13 62.629 0.155 . . . . . . 54 SER CA . 16449 1 481 . 1 1 45 45 SER CB C 13 63.891 0.208 . . . . . . 54 SER CB . 16449 1 482 . 1 1 45 45 SER N N 15 116.803 0.030 . . . . . . 54 SER N . 16449 1 483 . 1 1 46 46 ILE H H 1 7.919 0.009 . . . . . . 55 ILE H . 16449 1 484 . 1 1 46 46 ILE HA H 1 3.495 0.000 . . . . . . 55 ILE HA . 16449 1 485 . 1 1 46 46 ILE HB H 1 1.578 0.000 . . . . . . 55 ILE HB . 16449 1 486 . 1 1 46 46 ILE HG12 H 1 0.220 0.011 . . . . . . 55 ILE HG12 . 16449 1 487 . 1 1 46 46 ILE HG13 H 1 1.668 0.007 . . . . . . 55 ILE HG13 . 16449 1 488 . 1 1 46 46 ILE HG21 H 1 0.777 0.001 . . . . . . 55 ILE QG2 . 16449 1 489 . 1 1 46 46 ILE HG22 H 1 0.777 0.001 . . . . . . 55 ILE QG2 . 16449 1 490 . 1 1 46 46 ILE HG23 H 1 0.777 0.001 . . . . . . 55 ILE QG2 . 16449 1 491 . 1 1 46 46 ILE HD11 H 1 0.728 0.011 . . . . . . 55 ILE QD1 . 16449 1 492 . 1 1 46 46 ILE HD12 H 1 0.728 0.011 . . . . . . 55 ILE QD1 . 16449 1 493 . 1 1 46 46 ILE HD13 H 1 0.728 0.011 . . . . . . 55 ILE QD1 . 16449 1 494 . 1 1 46 46 ILE CA C 13 65.923 0.116 . . . . . . 55 ILE CA . 16449 1 495 . 1 1 46 46 ILE CB C 13 40.764 0.106 . . . . . . 55 ILE CB . 16449 1 496 . 1 1 46 46 ILE CG1 C 13 29.889 0.199 . . . . . . 55 ILE CG1 . 16449 1 497 . 1 1 46 46 ILE CG2 C 13 18.706 0.056 . . . . . . 55 ILE CG2 . 16449 1 498 . 1 1 46 46 ILE CD1 C 13 16.226 0.202 . . . . . . 55 ILE CD1 . 16449 1 499 . 1 1 46 46 ILE N N 15 120.008 0.106 . . . . . . 55 ILE N . 16449 1 500 . 1 1 47 47 LEU H H 1 8.772 0.007 . . . . . . 56 LEU H . 16449 1 501 . 1 1 47 47 LEU HA H 1 4.273 0.000 . . . . . . 56 LEU HA . 16449 1 502 . 1 1 47 47 LEU HB2 H 1 1.900 0.000 . . . . . . 56 LEU HB2 . 16449 1 503 . 1 1 47 47 LEU HB3 H 1 1.625 0.008 . . . . . . 56 LEU HB3 . 16449 1 504 . 1 1 47 47 LEU HG H 1 1.897 0.003 . . . . . . 56 LEU HG . 16449 1 505 . 1 1 47 47 LEU HD11 H 1 0.825 0.003 . . . . . . 56 LEU QD1 . 16449 1 506 . 1 1 47 47 LEU HD12 H 1 0.825 0.003 . . . . . . 56 LEU QD1 . 16449 1 507 . 1 1 47 47 LEU HD13 H 1 0.825 0.003 . . . . . . 56 LEU QD1 . 16449 1 508 . 1 1 47 47 LEU HD21 H 1 0.769 0.004 . . . . . . 56 LEU QD2 . 16449 1 509 . 1 1 47 47 LEU HD22 H 1 0.769 0.004 . . . . . . 56 LEU QD2 . 16449 1 510 . 1 1 47 47 LEU HD23 H 1 0.769 0.004 . . . . . . 56 LEU QD2 . 16449 1 511 . 1 1 47 47 LEU CA C 13 57.374 0.102 . . . . . . 56 LEU CA . 16449 1 512 . 1 1 47 47 LEU CB C 13 43.231 0.110 . . . . . . 56 LEU CB . 16449 1 513 . 1 1 47 47 LEU CG C 13 28.250 0.022 . . . . . . 56 LEU CG . 16449 1 514 . 1 1 47 47 LEU CD1 C 13 23.600 0.062 . . . . . . 56 LEU CD1 . 16449 1 515 . 1 1 47 47 LEU CD2 C 13 26.319 0.036 . . . . . . 56 LEU CD2 . 16449 1 516 . 1 1 47 47 LEU N N 15 114.832 0.056 . . . . . . 56 LEU N . 16449 1 517 . 1 1 48 48 GLY H H 1 8.079 0.001 . . . . . . 57 GLY H . 16449 1 518 . 1 1 48 48 GLY HA2 H 1 4.185 0.000 . . . . . . 57 GLY HA2 . 16449 1 519 . 1 1 48 48 GLY HA3 H 1 3.942 0.004 . . . . . . 57 GLY HA3 . 16449 1 520 . 1 1 48 48 GLY CA C 13 47.245 0.105 . . . . . . 57 GLY CA . 16449 1 521 . 1 1 48 48 GLY N N 15 107.639 0.027 . . . . . . 57 GLY N . 16449 1 522 . 1 1 49 49 ASN H H 1 6.710 0.007 . . . . . . 58 ASN H . 16449 1 523 . 1 1 49 49 ASN HA H 1 4.853 0.005 . . . . . . 58 ASN HA . 16449 1 524 . 1 1 49 49 ASN HB2 H 1 2.871 0.001 . . . . . . 58 ASN HB2 . 16449 1 525 . 1 1 49 49 ASN HB3 H 1 2.766 0.001 . . . . . . 58 ASN HB3 . 16449 1 526 . 1 1 49 49 ASN HD21 H 1 7.105 0.007 . . . . . . 58 ASN HD21 . 16449 1 527 . 1 1 49 49 ASN HD22 H 1 7.908 0.003 . . . . . . 58 ASN HD22 . 16449 1 528 . 1 1 49 49 ASN CA C 13 55.081 0.106 . . . . . . 58 ASN CA . 16449 1 529 . 1 1 49 49 ASN CB C 13 42.985 0.277 . . . . . . 58 ASN CB . 16449 1 530 . 1 1 49 49 ASN N N 15 114.368 0.105 . . . . . . 58 ASN N . 16449 1 531 . 1 1 49 49 ASN ND2 N 15 113.828 0.066 . . . . . . 58 ASN ND2 . 16449 1 532 . 1 1 50 50 ALA H H 1 9.276 0.009 . . . . . . 59 ALA H . 16449 1 533 . 1 1 50 50 ALA HA H 1 4.320 0.000 . . . . . . 59 ALA HA . 16449 1 534 . 1 1 50 50 ALA HB1 H 1 1.501 0.000 . . . . . . 59 ALA QB . 16449 1 535 . 1 1 50 50 ALA HB2 H 1 1.501 0.000 . . . . . . 59 ALA QB . 16449 1 536 . 1 1 50 50 ALA HB3 H 1 1.501 0.000 . . . . . . 59 ALA QB . 16449 1 537 . 1 1 50 50 ALA CA C 13 56.041 0.084 . . . . . . 59 ALA CA . 16449 1 538 . 1 1 50 50 ALA CB C 13 19.795 0.060 . . . . . . 59 ALA CB . 16449 1 539 . 1 1 50 50 ALA N N 15 129.813 0.013 . . . . . . 59 ALA N . 16449 1 540 . 1 1 51 51 ALA H H 1 8.529 0.006 . . . . . . 60 ALA H . 16449 1 541 . 1 1 51 51 ALA HA H 1 4.280 0.003 . . . . . . 60 ALA HA . 16449 1 542 . 1 1 51 51 ALA HB1 H 1 1.557 0.007 . . . . . . 60 ALA QB . 16449 1 543 . 1 1 51 51 ALA HB2 H 1 1.557 0.007 . . . . . . 60 ALA QB . 16449 1 544 . 1 1 51 51 ALA HB3 H 1 1.557 0.007 . . . . . . 60 ALA QB . 16449 1 545 . 1 1 51 51 ALA C C 13 56.633 0.000 . . . . . . 60 ALA C . 16449 1 546 . 1 1 51 51 ALA CA C 13 56.488 0.072 . . . . . . 60 ALA CA . 16449 1 547 . 1 1 51 51 ALA CB C 13 18.661 0.291 . . . . . . 60 ALA CB . 16449 1 548 . 1 1 51 51 ALA N N 15 123.460 0.061 . . . . . . 60 ALA N . 16449 1 549 . 1 1 52 52 ASN H H 1 8.604 0.005 . . . . . . 61 ASN H . 16449 1 550 . 1 1 52 52 ASN HA H 1 4.559 0.005 . . . . . . 61 ASN HA . 16449 1 551 . 1 1 52 52 ASN HB2 H 1 3.417 0.007 . . . . . . 61 ASN HB2 . 16449 1 552 . 1 1 52 52 ASN HB3 H 1 2.466 0.006 . . . . . . 61 ASN HB3 . 16449 1 553 . 1 1 52 52 ASN HD21 H 1 7.092 0.003 . . . . . . 61 ASN HD21 . 16449 1 554 . 1 1 52 52 ASN HD22 H 1 7.596 0.001 . . . . . . 61 ASN HD22 . 16449 1 555 . 1 1 52 52 ASN CA C 13 57.244 0.188 . . . . . . 61 ASN CA . 16449 1 556 . 1 1 52 52 ASN CB C 13 39.152 0.101 . . . . . . 61 ASN CB . 16449 1 557 . 1 1 52 52 ASN N N 15 118.330 0.079 . . . . . . 61 ASN N . 16449 1 558 . 1 1 52 52 ASN ND2 N 15 109.858 0.073 . . . . . . 61 ASN ND2 . 16449 1 559 . 1 1 53 53 ALA H H 1 7.688 0.002 . . . . . . 62 ALA H . 16449 1 560 . 1 1 53 53 ALA HA H 1 3.898 0.010 . . . . . . 62 ALA HA . 16449 1 561 . 1 1 53 53 ALA HB1 H 1 1.490 0.000 . . . . . . 62 ALA QB . 16449 1 562 . 1 1 53 53 ALA HB2 H 1 1.490 0.000 . . . . . . 62 ALA QB . 16449 1 563 . 1 1 53 53 ALA HB3 H 1 1.490 0.000 . . . . . . 62 ALA QB . 16449 1 564 . 1 1 53 53 ALA CB C 13 21.428 0.070 . . . . . . 62 ALA CB . 16449 1 565 . 1 1 53 53 ALA N N 15 119.315 0.089 . . . . . . 62 ALA N . 16449 1 566 . 1 1 54 54 LYS H H 1 8.129 0.004 . . . . . . 63 LYS H . 16449 1 567 . 1 1 54 54 LYS HA H 1 3.982 0.005 . . . . . . 63 LYS HA . 16449 1 568 . 1 1 54 54 LYS HB2 H 1 2.019 0.014 . . . . . . 63 LYS HB2 . 16449 1 569 . 1 1 54 54 LYS HB3 H 1 1.860 0.014 . . . . . . 63 LYS HB3 . 16449 1 570 . 1 1 54 54 LYS CA C 13 61.014 0.020 . . . . . . 63 LYS CA . 16449 1 571 . 1 1 54 54 LYS CB C 13 33.666 0.141 . . . . . . 63 LYS CB . 16449 1 572 . 1 1 54 54 LYS N N 15 118.393 0.043 . . . . . . 63 LYS N . 16449 1 573 . 1 1 55 55 GLN H H 1 7.813 0.013 . . . . . . 64 GLN H . 16449 1 574 . 1 1 55 55 GLN HA H 1 4.127 0.001 . . . . . . 64 GLN HA . 16449 1 575 . 1 1 55 55 GLN HB2 H 1 2.214 0.002 . . . . . . 64 GLN HB2 . 16449 1 576 . 1 1 55 55 GLN HB3 H 1 1.883 0.007 . . . . . . 64 GLN HB3 . 16449 1 577 . 1 1 55 55 GLN HG2 H 1 2.628 0.003 . . . . . . 64 GLN HG2 . 16449 1 578 . 1 1 55 55 GLN HG3 H 1 2.401 0.003 . . . . . . 64 GLN HG3 . 16449 1 579 . 1 1 55 55 GLN HE21 H 1 6.841 0.004 . . . . . . 64 GLN HE21 . 16449 1 580 . 1 1 55 55 GLN HE22 H 1 7.372 0.009 . . . . . . 64 GLN HE22 . 16449 1 581 . 1 1 55 55 GLN CA C 13 60.557 0.215 . . . . . . 64 GLN CA . 16449 1 582 . 1 1 55 55 GLN CB C 13 30.405 0.000 . . . . . . 64 GLN CB . 16449 1 583 . 1 1 55 55 GLN CG C 13 36.020 0.112 . . . . . . 64 GLN CG . 16449 1 584 . 1 1 55 55 GLN N N 15 116.122 0.234 . . . . . . 64 GLN N . 16449 1 585 . 1 1 55 55 GLN NE2 N 15 110.110 0.223 . . . . . . 64 GLN NE2 . 16449 1 586 . 1 1 56 56 LEU H H 1 7.964 0.006 . . . . . . 65 LEU H . 16449 1 587 . 1 1 56 56 LEU HA H 1 4.400 0.000 . . . . . . 65 LEU HA . 16449 1 588 . 1 1 56 56 LEU HB2 H 1 1.971 0.000 . . . . . . 65 LEU HB2 . 16449 1 589 . 1 1 56 56 LEU HB3 H 1 1.864 0.000 . . . . . . 65 LEU HB3 . 16449 1 590 . 1 1 56 56 LEU HG H 1 0.931 0.002 . . . . . . 65 LEU HG . 16449 1 591 . 1 1 56 56 LEU HD11 H 1 1.115 0.007 . . . . . . 65 LEU QD1 . 16449 1 592 . 1 1 56 56 LEU HD12 H 1 1.115 0.007 . . . . . . 65 LEU QD1 . 16449 1 593 . 1 1 56 56 LEU HD13 H 1 1.115 0.007 . . . . . . 65 LEU QD1 . 16449 1 594 . 1 1 56 56 LEU CA C 13 59.520 0.037 . . . . . . 65 LEU CA . 16449 1 595 . 1 1 56 56 LEU CB C 13 43.067 0.086 . . . . . . 65 LEU CB . 16449 1 596 . 1 1 56 56 LEU CG C 13 28.583 0.130 . . . . . . 65 LEU CG . 16449 1 597 . 1 1 56 56 LEU CD1 C 13 24.855 0.044 . . . . . . 65 LEU CD1 . 16449 1 598 . 1 1 56 56 LEU N N 15 122.243 0.179 . . . . . . 65 LEU N . 16449 1 599 . 1 1 57 57 TYR H H 1 9.050 0.006 . . . . . . 66 TYR H . 16449 1 600 . 1 1 57 57 TYR HA H 1 3.876 0.010 . . . . . . 66 TYR HA . 16449 1 601 . 1 1 57 57 TYR HB2 H 1 3.107 0.002 . . . . . . 66 TYR HB2 . 16449 1 602 . 1 1 57 57 TYR HB3 H 1 3.107 0.002 . . . . . . 66 TYR HB3 . 16449 1 603 . 1 1 57 57 TYR HD1 H 1 7.105 0.004 . . . . . . 66 TYR QD . 16449 1 604 . 1 1 57 57 TYR HD2 H 1 7.105 0.004 . . . . . . 66 TYR QD . 16449 1 605 . 1 1 57 57 TYR CA C 13 64.496 0.139 . . . . . . 66 TYR CA . 16449 1 606 . 1 1 57 57 TYR CB C 13 40.608 0.101 . . . . . . 66 TYR CB . 16449 1 607 . 1 1 57 57 TYR N N 15 119.993 0.051 . . . . . . 66 TYR N . 16449 1 608 . 1 1 58 58 ASP H H 1 9.534 0.004 . . . . . . 67 ASP H . 16449 1 609 . 1 1 58 58 ASP HA H 1 4.511 0.014 . . . . . . 67 ASP HA . 16449 1 610 . 1 1 58 58 ASP HB2 H 1 3.013 0.007 . . . . . . 67 ASP HB2 . 16449 1 611 . 1 1 58 58 ASP HB3 H 1 2.599 0.011 . . . . . . 67 ASP HB3 . 16449 1 612 . 1 1 58 58 ASP CA C 13 58.704 0.062 . . . . . . 67 ASP CA . 16449 1 613 . 1 1 58 58 ASP CB C 13 40.193 0.207 . . . . . . 67 ASP CB . 16449 1 614 . 1 1 58 58 ASP N N 15 119.553 0.061 . . . . . . 67 ASP N . 16449 1 615 . 1 1 59 59 PHE H H 1 8.130 0.004 . . . . . . 68 PHE H . 16449 1 616 . 1 1 59 59 PHE HA H 1 4.311 0.007 . . . . . . 68 PHE HA . 16449 1 617 . 1 1 59 59 PHE HB2 H 1 3.362 0.000 . . . . . . 68 PHE HB2 . 16449 1 618 . 1 1 59 59 PHE HB3 H 1 3.362 0.000 . . . . . . 68 PHE HB3 . 16449 1 619 . 1 1 59 59 PHE HD1 H 1 7.205 0.000 . . . . . . 68 PHE QD . 16449 1 620 . 1 1 59 59 PHE HD2 H 1 7.205 0.000 . . . . . . 68 PHE QD . 16449 1 621 . 1 1 59 59 PHE HE1 H 1 6.747 0.000 . . . . . . 68 PHE QE . 16449 1 622 . 1 1 59 59 PHE HE2 H 1 6.747 0.000 . . . . . . 68 PHE QE . 16449 1 623 . 1 1 59 59 PHE HZ H 1 6.407 0.000 . . . . . . 68 PHE HZ . 16449 1 624 . 1 1 59 59 PHE CA C 13 63.535 0.096 . . . . . . 68 PHE CA . 16449 1 625 . 1 1 59 59 PHE CB C 13 40.513 0.069 . . . . . . 68 PHE CB . 16449 1 626 . 1 1 59 59 PHE CD1 C 13 132.415 0.126 . . . . . . 68 PHE CD1 . 16449 1 627 . 1 1 59 59 PHE CD2 C 13 132.415 0.126 . . . . . . 68 PHE CD2 . 16449 1 628 . 1 1 59 59 PHE N N 15 124.215 0.124 . . . . . . 68 PHE N . 16449 1 629 . 1 1 60 60 ILE H H 1 7.975 0.003 . . . . . . 69 ILE H . 16449 1 630 . 1 1 60 60 ILE HA H 1 3.430 0.000 . . . . . . 69 ILE HA . 16449 1 631 . 1 1 60 60 ILE HB H 1 1.910 0.000 . . . . . . 69 ILE HB . 16449 1 632 . 1 1 60 60 ILE HG12 H 1 1.113 0.007 . . . . . . 69 ILE HG12 . 16449 1 633 . 1 1 60 60 ILE HG13 H 1 1.948 0.023 . . . . . . 69 ILE HG13 . 16449 1 634 . 1 1 60 60 ILE HG21 H 1 0.532 0.013 . . . . . . 69 ILE QG2 . 16449 1 635 . 1 1 60 60 ILE HG22 H 1 0.532 0.013 . . . . . . 69 ILE QG2 . 16449 1 636 . 1 1 60 60 ILE HG23 H 1 0.532 0.013 . . . . . . 69 ILE QG2 . 16449 1 637 . 1 1 60 60 ILE HD11 H 1 0.841 0.005 . . . . . . 69 ILE QD1 . 16449 1 638 . 1 1 60 60 ILE HD12 H 1 0.841 0.005 . . . . . . 69 ILE QD1 . 16449 1 639 . 1 1 60 60 ILE HD13 H 1 0.841 0.005 . . . . . . 69 ILE QD1 . 16449 1 640 . 1 1 60 60 ILE CA C 13 64.568 0.061 . . . . . . 69 ILE CA . 16449 1 641 . 1 1 60 60 ILE CB C 13 39.189 0.083 . . . . . . 69 ILE CB . 16449 1 642 . 1 1 60 60 ILE CG1 C 13 31.212 0.109 . . . . . . 69 ILE CG1 . 16449 1 643 . 1 1 60 60 ILE CG2 C 13 19.215 0.064 . . . . . . 69 ILE CG2 . 16449 1 644 . 1 1 60 60 ILE CD1 C 13 14.046 0.137 . . . . . . 69 ILE CD1 . 16449 1 645 . 1 1 60 60 ILE N N 15 116.957 0.108 . . . . . . 69 ILE N . 16449 1 646 . 1 1 61 61 HIS H H 1 7.442 0.003 . . . . . . 70 HIS H . 16449 1 647 . 1 1 61 61 HIS HA H 1 4.352 0.000 . . . . . . 70 HIS HA . 16449 1 648 . 1 1 61 61 HIS HB2 H 1 3.466 0.000 . . . . . . 70 HIS HB2 . 16449 1 649 . 1 1 61 61 HIS HB3 H 1 2.671 0.000 . . . . . . 70 HIS HB3 . 16449 1 650 . 1 1 61 61 HIS CA C 13 57.494 0.195 . . . . . . 70 HIS CA . 16449 1 651 . 1 1 61 61 HIS CB C 13 29.839 0.185 . . . . . . 70 HIS CB . 16449 1 652 . 1 1 61 61 HIS N N 15 112.046 0.121 . . . . . . 70 HIS N . 16449 1 653 . 1 1 62 62 THR H H 1 7.559 0.001 . . . . . . 71 THR H . 16449 1 654 . 1 1 62 62 THR HA H 1 4.261 0.003 . . . . . . 71 THR HA . 16449 1 655 . 1 1 62 62 THR HB H 1 4.073 0.000 . . . . . . 71 THR HB . 16449 1 656 . 1 1 62 62 THR HG21 H 1 1.358 0.008 . . . . . . 71 THR QG2 . 16449 1 657 . 1 1 62 62 THR HG22 H 1 1.358 0.008 . . . . . . 71 THR QG2 . 16449 1 658 . 1 1 62 62 THR HG23 H 1 1.358 0.008 . . . . . . 71 THR QG2 . 16449 1 659 . 1 1 62 62 THR CA C 13 65.560 0.115 . . . . . . 71 THR CA . 16449 1 660 . 1 1 62 62 THR CB C 13 70.770 0.068 . . . . . . 71 THR CB . 16449 1 661 . 1 1 62 62 THR CG2 C 13 21.853 0.201 . . . . . . 71 THR CG2 . 16449 1 662 . 1 1 62 62 THR N N 15 121.200 0.024 . . . . . . 71 THR N . 16449 1 663 . 1 1 63 63 SER H H 1 8.895 0.004 . . . . . . 72 SER H . 16449 1 664 . 1 1 63 63 SER HA H 1 4.750 0.002 . . . . . . 72 SER HA . 16449 1 665 . 1 1 63 63 SER HB2 H 1 4.020 0.000 . . . . . . 72 SER HB2 . 16449 1 666 . 1 1 63 63 SER HB3 H 1 3.955 0.000 . . . . . . 72 SER HB3 . 16449 1 667 . 1 1 63 63 SER CA C 13 59.271 0.103 . . . . . . 72 SER CA . 16449 1 668 . 1 1 63 63 SER CB C 13 64.765 0.095 . . . . . . 72 SER CB . 16449 1 669 . 1 1 63 63 SER N N 15 122.398 0.062 . . . . . . 72 SER N . 16449 1 670 . 1 1 64 64 PHE H H 1 8.286 0.003 . . . . . . 73 PHE H . 16449 1 671 . 1 1 64 64 PHE HA H 1 4.473 0.010 . . . . . . 73 PHE HA . 16449 1 672 . 1 1 64 64 PHE HB2 H 1 3.322 0.017 . . . . . . 73 PHE HB2 . 16449 1 673 . 1 1 64 64 PHE HB3 H 1 3.165 0.004 . . . . . . 73 PHE HB3 . 16449 1 674 . 1 1 64 64 PHE HD1 H 1 7.204 0.000 . . . . . . 73 PHE QD . 16449 1 675 . 1 1 64 64 PHE HD2 H 1 7.204 0.000 . . . . . . 73 PHE QD . 16449 1 676 . 1 1 64 64 PHE HE1 H 1 7.016 0.005 . . . . . . 73 PHE QE . 16449 1 677 . 1 1 64 64 PHE HE2 H 1 7.016 0.005 . . . . . . 73 PHE QE . 16449 1 678 . 1 1 64 64 PHE HZ H 1 6.746 0.005 . . . . . . 73 PHE HZ . 16449 1 679 . 1 1 64 64 PHE CA C 13 60.445 0.188 . . . . . . 73 PHE CA . 16449 1 680 . 1 1 64 64 PHE CB C 13 40.521 0.057 . . . . . . 73 PHE CB . 16449 1 681 . 1 1 64 64 PHE CD1 C 13 132.210 0.023 . . . . . . 73 PHE CD1 . 16449 1 682 . 1 1 64 64 PHE CD2 C 13 132.210 0.023 . . . . . . 73 PHE CD2 . 16449 1 683 . 1 1 64 64 PHE CE1 C 13 132.428 0.013 . . . . . . 73 PHE CE1 . 16449 1 684 . 1 1 64 64 PHE CE2 C 13 132.428 0.013 . . . . . . 73 PHE CE2 . 16449 1 685 . 1 1 64 64 PHE CZ C 13 129.958 0.000 . . . . . . 73 PHE CZ . 16449 1 686 . 1 1 64 64 PHE N N 15 122.118 0.086 . . . . . . 73 PHE N . 16449 1 687 . 1 1 65 65 ALA H H 1 8.272 0.001 . . . . . . 74 ALA H . 16449 1 688 . 1 1 65 65 ALA HA H 1 4.486 0.000 . . . . . . 74 ALA HA . 16449 1 689 . 1 1 65 65 ALA HB1 H 1 1.456 0.000 . . . . . . 74 ALA QB . 16449 1 690 . 1 1 65 65 ALA HB2 H 1 1.456 0.000 . . . . . . 74 ALA QB . 16449 1 691 . 1 1 65 65 ALA HB3 H 1 1.456 0.000 . . . . . . 74 ALA QB . 16449 1 692 . 1 1 65 65 ALA CA C 13 53.223 0.085 . . . . . . 74 ALA CA . 16449 1 693 . 1 1 65 65 ALA CB C 13 21.238 0.158 . . . . . . 74 ALA CB . 16449 1 694 . 1 1 65 65 ALA N N 15 120.073 0.041 . . . . . . 74 ALA N . 16449 1 695 . 1 1 66 66 GLU H H 1 8.266 0.006 . . . . . . 75 GLU H . 16449 1 696 . 1 1 66 66 GLU HA H 1 4.323 0.000 . . . . . . 75 GLU HA . 16449 1 697 . 1 1 66 66 GLU HB2 H 1 2.095 0.010 . . . . . . 75 GLU HB2 . 16449 1 698 . 1 1 66 66 GLU HB3 H 1 1.984 0.000 . . . . . . 75 GLU HB3 . 16449 1 699 . 1 1 66 66 GLU HG2 H 1 2.322 0.000 . . . . . . 75 GLU HG2 . 16449 1 700 . 1 1 66 66 GLU HG3 H 1 2.322 0.000 . . . . . . 75 GLU HG3 . 16449 1 701 . 1 1 66 66 GLU CA C 13 57.918 0.000 . . . . . . 75 GLU CA . 16449 1 702 . 1 1 66 66 GLU CB C 13 31.561 0.095 . . . . . . 75 GLU CB . 16449 1 703 . 1 1 66 66 GLU CG C 13 37.626 0.000 . . . . . . 75 GLU CG . 16449 1 704 . 1 1 66 66 GLU N N 15 120.130 0.162 . . . . . . 75 GLU N . 16449 1 705 . 1 1 75 75 LYS H H 1 8.143 0.000 . . . . . . 84 LYS H . 16449 1 706 . 1 1 75 75 LYS CB C 13 35.026 0.000 . . . . . . 84 LYS CB . 16449 1 707 . 1 1 75 75 LYS N N 15 128.740 0.000 . . . . . . 84 LYS N . 16449 1 stop_ save_