data_18234 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 18234 _Entry.Title ; Solution structure of P1-CheY/P2 complex in bacterial chemotaxis ; _Entry.Type macromolecule _Entry.Version_type original _Entry.Submission_date 2012-02-01 _Entry.Accession_date 2012-02-01 _Entry.Last_release_date 2012-10-22 _Entry.Original_release_date 2012-10-22 _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 Frederick dahlquist . . . 18234 2 Guoya Mo . . . 18234 3 Hongjun Zhou . . . 18234 4 Tetsuya Kamamura . . . 18234 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' . 18234 stop_ loop_ _Struct_keywords.Keywords _Struct_keywords.Text _Struct_keywords.Entry_ID Chemotaxis . 18234 'Histidine phosphotransfer domain' . 18234 'Response Regulator' . 18234 'Two Component Signaling system' . 18234 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 18234 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '15N chemical shifts' 108 18234 '1H chemical shifts' 108 18234 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 1 . . 2012-10-22 2012-02-01 original author . 18234 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID PDB 1EAY 'Entry was use for calculation in this molecular system.' 18234 PDB 1I5N 'Entry was use for calculation in this molecular system.' 18234 PDB 2LP4 'BMRB Entry Tracking System' 18234 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 18234 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _Citation.Title 'Solution structure of P1-CheY/P2 complex in bacterial chemotaxis' _Citation.Status 'in preparation' _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full . _Citation.Journal_volume . _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first . _Citation.Page_last . _Citation.Year . _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 Guoya Mo . . . 18234 1 2 Hongjun Zhou . . . 18234 1 3 Tetsuya Kamamura . . . 18234 1 4 Frederick dahlquist . . . 18234 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_assembly _Assembly.Sf_category assembly _Assembly.Sf_framecode assembly _Assembly.Entry_ID 18234 _Assembly.ID 1 _Assembly.Name 'P1-CheY/P2 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 CheA_P1P2 1 $CheA_P1P2 A . no native no no . . . 18234 1 2 CheY 2 $CheY B . yes native no no . . . 18234 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_CheA_P1P2 _Entity.Sf_category entity _Entity.Sf_framecode CheA_P1P2 _Entity.Entry_ID 18234 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name CheA_P1P2 _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 ; MSMDISDFYQTFFDEADELL ADMEQHLLDLVPESPDAEQL NAIFRAAHSIKGGAGTFGFT ILQETTHLMENLLDEARRGE MQLNTDIINLFLETKDIMQE QLDAYKNSEEPDAASFEYIC NALRQLALEAKGETPSAVTR LSVVAKSEPQDEQSRSQSPR RIILSRLKAGEVDLLEEELG HLTTLTDVVKGADSLSAILP GDIAEDDITAVLCFVIEADQ ITFET ; _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 225 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not reported' _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 24991.010 _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 2LP4 . "Solution Structure Of P1-CheyP2 COMPLEX IN BACTERIAL CHEMOTAXIS" . . . . . 100.00 225 100.00 100.00 4.13e-160 . . . . 18234 1 2 no EMBL CQF39165 . "chemotaxis protein CheA [Salmonella enterica subsp. enterica serovar Typhimurium str. DT104]" . . . . . 58.67 147 100.00 100.00 7.49e-89 . . . . 18234 1 3 no GB EIQ53621 . "fused chemotactic sensory histidine kinase in two-component regulatory system with CheB and CheY [Shigella sonnei 4822-66]" . . . . . 69.78 586 97.45 98.73 3.84e-98 . . . . 18234 1 4 no REF WP_042351715 . "chemotaxis protein CheA, partial [Escherichia coli]" . . . . . 60.89 566 97.08 98.54 6.85e-83 . . . . 18234 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 . 18234 1 2 . SER . 18234 1 3 . MET . 18234 1 4 . ASP . 18234 1 5 . ILE . 18234 1 6 . SER . 18234 1 7 . ASP . 18234 1 8 . PHE . 18234 1 9 . TYR . 18234 1 10 . GLN . 18234 1 11 . THR . 18234 1 12 . PHE . 18234 1 13 . PHE . 18234 1 14 . ASP . 18234 1 15 . GLU . 18234 1 16 . ALA . 18234 1 17 . ASP . 18234 1 18 . GLU . 18234 1 19 . LEU . 18234 1 20 . LEU . 18234 1 21 . ALA . 18234 1 22 . ASP . 18234 1 23 . MET . 18234 1 24 . GLU . 18234 1 25 . GLN . 18234 1 26 . HIS . 18234 1 27 . LEU . 18234 1 28 . LEU . 18234 1 29 . ASP . 18234 1 30 . LEU . 18234 1 31 . VAL . 18234 1 32 . PRO . 18234 1 33 . GLU . 18234 1 34 . SER . 18234 1 35 . PRO . 18234 1 36 . ASP . 18234 1 37 . ALA . 18234 1 38 . GLU . 18234 1 39 . GLN . 18234 1 40 . LEU . 18234 1 41 . ASN . 18234 1 42 . ALA . 18234 1 43 . ILE . 18234 1 44 . PHE . 18234 1 45 . ARG . 18234 1 46 . ALA . 18234 1 47 . ALA . 18234 1 48 . HIS . 18234 1 49 . SER . 18234 1 50 . ILE . 18234 1 51 . LYS . 18234 1 52 . GLY . 18234 1 53 . GLY . 18234 1 54 . ALA . 18234 1 55 . GLY . 18234 1 56 . THR . 18234 1 57 . PHE . 18234 1 58 . GLY . 18234 1 59 . PHE . 18234 1 60 . THR . 18234 1 61 . ILE . 18234 1 62 . LEU . 18234 1 63 . GLN . 18234 1 64 . GLU . 18234 1 65 . THR . 18234 1 66 . THR . 18234 1 67 . HIS . 18234 1 68 . LEU . 18234 1 69 . MET . 18234 1 70 . GLU . 18234 1 71 . ASN . 18234 1 72 . LEU . 18234 1 73 . LEU . 18234 1 74 . ASP . 18234 1 75 . GLU . 18234 1 76 . ALA . 18234 1 77 . ARG . 18234 1 78 . ARG . 18234 1 79 . GLY . 18234 1 80 . GLU . 18234 1 81 . MET . 18234 1 82 . GLN . 18234 1 83 . LEU . 18234 1 84 . ASN . 18234 1 85 . THR . 18234 1 86 . ASP . 18234 1 87 . ILE . 18234 1 88 . ILE . 18234 1 89 . ASN . 18234 1 90 . LEU . 18234 1 91 . PHE . 18234 1 92 . LEU . 18234 1 93 . GLU . 18234 1 94 . THR . 18234 1 95 . LYS . 18234 1 96 . ASP . 18234 1 97 . ILE . 18234 1 98 . MET . 18234 1 99 . GLN . 18234 1 100 . GLU . 18234 1 101 . GLN . 18234 1 102 . LEU . 18234 1 103 . ASP . 18234 1 104 . ALA . 18234 1 105 . TYR . 18234 1 106 . LYS . 18234 1 107 . ASN . 18234 1 108 . SER . 18234 1 109 . GLU . 18234 1 110 . GLU . 18234 1 111 . PRO . 18234 1 112 . ASP . 18234 1 113 . ALA . 18234 1 114 . ALA . 18234 1 115 . SER . 18234 1 116 . PHE . 18234 1 117 . GLU . 18234 1 118 . TYR . 18234 1 119 . ILE . 18234 1 120 . CYS . 18234 1 121 . ASN . 18234 1 122 . ALA . 18234 1 123 . LEU . 18234 1 124 . ARG . 18234 1 125 . GLN . 18234 1 126 . LEU . 18234 1 127 . ALA . 18234 1 128 . LEU . 18234 1 129 . GLU . 18234 1 130 . ALA . 18234 1 131 . LYS . 18234 1 132 . GLY . 18234 1 133 . GLU . 18234 1 134 . THR . 18234 1 135 . PRO . 18234 1 136 . SER . 18234 1 137 . ALA . 18234 1 138 . VAL . 18234 1 139 . THR . 18234 1 140 . ARG . 18234 1 141 . LEU . 18234 1 142 . SER . 18234 1 143 . VAL . 18234 1 144 . VAL . 18234 1 145 . ALA . 18234 1 146 . LYS . 18234 1 147 . SER . 18234 1 148 . GLU . 18234 1 149 . PRO . 18234 1 150 . GLN . 18234 1 151 . ASP . 18234 1 152 . GLU . 18234 1 153 . GLN . 18234 1 154 . SER . 18234 1 155 . ARG . 18234 1 156 . SER . 18234 1 157 . GLN . 18234 1 158 . SER . 18234 1 159 . PRO . 18234 1 160 . ARG . 18234 1 161 . ARG . 18234 1 162 . ILE . 18234 1 163 . ILE . 18234 1 164 . LEU . 18234 1 165 . SER . 18234 1 166 . ARG . 18234 1 167 . LEU . 18234 1 168 . LYS . 18234 1 169 . ALA . 18234 1 170 . GLY . 18234 1 171 . GLU . 18234 1 172 . VAL . 18234 1 173 . ASP . 18234 1 174 . LEU . 18234 1 175 . LEU . 18234 1 176 . GLU . 18234 1 177 . GLU . 18234 1 178 . GLU . 18234 1 179 . LEU . 18234 1 180 . GLY . 18234 1 181 . HIS . 18234 1 182 . LEU . 18234 1 183 . THR . 18234 1 184 . THR . 18234 1 185 . LEU . 18234 1 186 . THR . 18234 1 187 . ASP . 18234 1 188 . VAL . 18234 1 189 . VAL . 18234 1 190 . LYS . 18234 1 191 . GLY . 18234 1 192 . ALA . 18234 1 193 . ASP . 18234 1 194 . SER . 18234 1 195 . LEU . 18234 1 196 . SER . 18234 1 197 . ALA . 18234 1 198 . ILE . 18234 1 199 . LEU . 18234 1 200 . PRO . 18234 1 201 . GLY . 18234 1 202 . ASP . 18234 1 203 . ILE . 18234 1 204 . ALA . 18234 1 205 . GLU . 18234 1 206 . ASP . 18234 1 207 . ASP . 18234 1 208 . ILE . 18234 1 209 . THR . 18234 1 210 . ALA . 18234 1 211 . VAL . 18234 1 212 . LEU . 18234 1 213 . CYS . 18234 1 214 . PHE . 18234 1 215 . VAL . 18234 1 216 . ILE . 18234 1 217 . GLU . 18234 1 218 . ALA . 18234 1 219 . ASP . 18234 1 220 . GLN . 18234 1 221 . ILE . 18234 1 222 . THR . 18234 1 223 . PHE . 18234 1 224 . GLU . 18234 1 225 . THR . 18234 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 18234 1 . SER 2 2 18234 1 . MET 3 3 18234 1 . ASP 4 4 18234 1 . ILE 5 5 18234 1 . SER 6 6 18234 1 . ASP 7 7 18234 1 . PHE 8 8 18234 1 . TYR 9 9 18234 1 . GLN 10 10 18234 1 . THR 11 11 18234 1 . PHE 12 12 18234 1 . PHE 13 13 18234 1 . ASP 14 14 18234 1 . GLU 15 15 18234 1 . ALA 16 16 18234 1 . ASP 17 17 18234 1 . GLU 18 18 18234 1 . LEU 19 19 18234 1 . LEU 20 20 18234 1 . ALA 21 21 18234 1 . ASP 22 22 18234 1 . MET 23 23 18234 1 . GLU 24 24 18234 1 . GLN 25 25 18234 1 . HIS 26 26 18234 1 . LEU 27 27 18234 1 . LEU 28 28 18234 1 . ASP 29 29 18234 1 . LEU 30 30 18234 1 . VAL 31 31 18234 1 . PRO 32 32 18234 1 . GLU 33 33 18234 1 . SER 34 34 18234 1 . PRO 35 35 18234 1 . ASP 36 36 18234 1 . ALA 37 37 18234 1 . GLU 38 38 18234 1 . GLN 39 39 18234 1 . LEU 40 40 18234 1 . ASN 41 41 18234 1 . ALA 42 42 18234 1 . ILE 43 43 18234 1 . PHE 44 44 18234 1 . ARG 45 45 18234 1 . ALA 46 46 18234 1 . ALA 47 47 18234 1 . HIS 48 48 18234 1 . SER 49 49 18234 1 . ILE 50 50 18234 1 . LYS 51 51 18234 1 . GLY 52 52 18234 1 . GLY 53 53 18234 1 . ALA 54 54 18234 1 . GLY 55 55 18234 1 . THR 56 56 18234 1 . PHE 57 57 18234 1 . GLY 58 58 18234 1 . PHE 59 59 18234 1 . THR 60 60 18234 1 . ILE 61 61 18234 1 . LEU 62 62 18234 1 . GLN 63 63 18234 1 . GLU 64 64 18234 1 . THR 65 65 18234 1 . THR 66 66 18234 1 . HIS 67 67 18234 1 . LEU 68 68 18234 1 . MET 69 69 18234 1 . GLU 70 70 18234 1 . ASN 71 71 18234 1 . LEU 72 72 18234 1 . LEU 73 73 18234 1 . ASP 74 74 18234 1 . GLU 75 75 18234 1 . ALA 76 76 18234 1 . ARG 77 77 18234 1 . ARG 78 78 18234 1 . GLY 79 79 18234 1 . GLU 80 80 18234 1 . MET 81 81 18234 1 . GLN 82 82 18234 1 . LEU 83 83 18234 1 . ASN 84 84 18234 1 . THR 85 85 18234 1 . ASP 86 86 18234 1 . ILE 87 87 18234 1 . ILE 88 88 18234 1 . ASN 89 89 18234 1 . LEU 90 90 18234 1 . PHE 91 91 18234 1 . LEU 92 92 18234 1 . GLU 93 93 18234 1 . THR 94 94 18234 1 . LYS 95 95 18234 1 . ASP 96 96 18234 1 . ILE 97 97 18234 1 . MET 98 98 18234 1 . GLN 99 99 18234 1 . GLU 100 100 18234 1 . GLN 101 101 18234 1 . LEU 102 102 18234 1 . ASP 103 103 18234 1 . ALA 104 104 18234 1 . TYR 105 105 18234 1 . LYS 106 106 18234 1 . ASN 107 107 18234 1 . SER 108 108 18234 1 . GLU 109 109 18234 1 . GLU 110 110 18234 1 . PRO 111 111 18234 1 . ASP 112 112 18234 1 . ALA 113 113 18234 1 . ALA 114 114 18234 1 . SER 115 115 18234 1 . PHE 116 116 18234 1 . GLU 117 117 18234 1 . TYR 118 118 18234 1 . ILE 119 119 18234 1 . CYS 120 120 18234 1 . ASN 121 121 18234 1 . ALA 122 122 18234 1 . LEU 123 123 18234 1 . ARG 124 124 18234 1 . GLN 125 125 18234 1 . LEU 126 126 18234 1 . ALA 127 127 18234 1 . LEU 128 128 18234 1 . GLU 129 129 18234 1 . ALA 130 130 18234 1 . LYS 131 131 18234 1 . GLY 132 132 18234 1 . GLU 133 133 18234 1 . THR 134 134 18234 1 . PRO 135 135 18234 1 . SER 136 136 18234 1 . ALA 137 137 18234 1 . VAL 138 138 18234 1 . THR 139 139 18234 1 . ARG 140 140 18234 1 . LEU 141 141 18234 1 . SER 142 142 18234 1 . VAL 143 143 18234 1 . VAL 144 144 18234 1 . ALA 145 145 18234 1 . LYS 146 146 18234 1 . SER 147 147 18234 1 . GLU 148 148 18234 1 . PRO 149 149 18234 1 . GLN 150 150 18234 1 . ASP 151 151 18234 1 . GLU 152 152 18234 1 . GLN 153 153 18234 1 . SER 154 154 18234 1 . ARG 155 155 18234 1 . SER 156 156 18234 1 . GLN 157 157 18234 1 . SER 158 158 18234 1 . PRO 159 159 18234 1 . ARG 160 160 18234 1 . ARG 161 161 18234 1 . ILE 162 162 18234 1 . ILE 163 163 18234 1 . LEU 164 164 18234 1 . SER 165 165 18234 1 . ARG 166 166 18234 1 . LEU 167 167 18234 1 . LYS 168 168 18234 1 . ALA 169 169 18234 1 . GLY 170 170 18234 1 . GLU 171 171 18234 1 . VAL 172 172 18234 1 . ASP 173 173 18234 1 . LEU 174 174 18234 1 . LEU 175 175 18234 1 . GLU 176 176 18234 1 . GLU 177 177 18234 1 . GLU 178 178 18234 1 . LEU 179 179 18234 1 . GLY 180 180 18234 1 . HIS 181 181 18234 1 . LEU 182 182 18234 1 . THR 183 183 18234 1 . THR 184 184 18234 1 . LEU 185 185 18234 1 . THR 186 186 18234 1 . ASP 187 187 18234 1 . VAL 188 188 18234 1 . VAL 189 189 18234 1 . LYS 190 190 18234 1 . GLY 191 191 18234 1 . ALA 192 192 18234 1 . ASP 193 193 18234 1 . SER 194 194 18234 1 . LEU 195 195 18234 1 . SER 196 196 18234 1 . ALA 197 197 18234 1 . ILE 198 198 18234 1 . LEU 199 199 18234 1 . PRO 200 200 18234 1 . GLY 201 201 18234 1 . ASP 202 202 18234 1 . ILE 203 203 18234 1 . ALA 204 204 18234 1 . GLU 205 205 18234 1 . ASP 206 206 18234 1 . ASP 207 207 18234 1 . ILE 208 208 18234 1 . THR 209 209 18234 1 . ALA 210 210 18234 1 . VAL 211 211 18234 1 . LEU 212 212 18234 1 . CYS 213 213 18234 1 . PHE 214 214 18234 1 . VAL 215 215 18234 1 . ILE 216 216 18234 1 . GLU 217 217 18234 1 . ALA 218 218 18234 1 . ASP 219 219 18234 1 . GLN 220 220 18234 1 . ILE 221 221 18234 1 . THR 222 222 18234 1 . PHE 223 223 18234 1 . GLU 224 224 18234 1 . THR 225 225 18234 1 stop_ save_ save_CheY _Entity.Sf_category entity _Entity.Sf_framecode CheY _Entity.Entry_ID 18234 _Entity.ID 2 _Entity.BMRB_code . _Entity.Name CheY _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID Y _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; ADKELKFLVVDDFSTMRRIV RNLLKELGFNNVEEAEDGVD ALNKLQAGGYGFVISDWNMP NMDGLELLKTIRADGAMSAL PVLMVTAEAKKENIIAAAQA GASGYVVKPFTAATLEEKLN KIFEKLGM ; _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 128 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic no _Entity.Thiol_state 'not reported' _Entity.Src_method man _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight 13981.248 _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-30 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 BMRB 2950 . "che Y protein" . . . . . 100.00 129 100.00 100.00 5.18e-85 . . . . 18234 2 2 no BMRB 2951 . "che Y protein" . . . . . 100.00 129 100.00 100.00 5.18e-85 . . . . 18234 2 3 no BMRB 3440 . "che Y protein" . . . . . 100.00 129 99.22 100.00 1.38e-84 . . . . 18234 2 4 no BMRB 4083 . CheY . . . . . 100.00 128 100.00 100.00 8.66e-85 . . . . 18234 2 5 no BMRB 4472 . CheY . . . . . 100.00 129 100.00 100.00 5.18e-85 . . . . 18234 2 6 no PDB 1A0O . "Chey-Binding Domain Of Chea In Complex With Chey" . . . . . 100.00 128 100.00 100.00 8.66e-85 . . . . 18234 2 7 no PDB 1AB5 . "Structure Of Chey Mutant F14n, V21t" . . . . . 97.66 125 98.40 98.40 9.29e-81 . . . . 18234 2 8 no PDB 1AB6 . "Structure Of Chey Mutant F14n, V86t" . . . . . 97.66 125 98.40 98.40 9.29e-81 . . . . 18234 2 9 no PDB 1BDJ . "Complex Structure Of Hpt Domain And Chey" . . . . . 100.00 128 100.00 100.00 8.66e-85 . . . . 18234 2 10 no PDB 1C4W . "1.9 A Structure Of A-Thiophosphonate Modified Chey D57c" . . . . . 100.00 128 99.22 99.22 7.20e-84 . . . . 18234 2 11 no PDB 1CEY . "Assignments, Secondary Structure, Global Fold, And Dynamics Of Chemotaxis Y Protein Using Three-And Four-Dimensional Heteronucl" . . . . . 99.22 128 100.00 100.00 2.67e-84 . . . . 18234 2 12 no PDB 1CHN . "Magnesium Binding To The Bacterial Chemotaxis Protein Chey Results In Large Conformational Changes Involving Its Functional Sur" . . . . . 100.00 128 100.00 100.00 8.66e-85 . . . . 18234 2 13 no PDB 1CYE . "Three Dimensional Structure Of Chemotactic Che Y Protein In Aqueous Solution By Nuclear Magnetic Resonance Methods" . . . . . 100.00 129 99.22 100.00 1.38e-84 . . . . 18234 2 14 no PDB 1D4Z . "Crystal Structure Of Chey-95iv, A Hyperactive Chey Mutant" . . . . . 100.00 128 99.22 100.00 1.37e-84 . . . . 18234 2 15 no PDB 1DJM . "Solution Structure Of Bef3-Activated Chey From Escherichia Coli" . . . . . 100.00 129 100.00 100.00 5.18e-85 . . . . 18234 2 16 no PDB 1E6K . "Two-Component Signal Transduction System D12a Mutant Of Chey" . . . . . 100.00 130 98.44 99.22 1.82e-83 . . . . 18234 2 17 no PDB 1E6L . "Two-Component Signal Transduction System D13a Mutant Of Chey" . . . . . 99.22 127 99.21 99.21 3.36e-83 . . . . 18234 2 18 no PDB 1E6M . "Two-Component Signal Transduction System D57a Mutant Of Chey" . . . . . 100.00 128 98.44 99.22 2.15e-83 . . . . 18234 2 19 no PDB 1EAY . "Chey-Binding (P2) Domain Of Chea In Complex With Chey From Escherichia Coli" . . . . . 100.00 128 100.00 100.00 8.66e-85 . . . . 18234 2 20 no PDB 1EHC . "Structure Of Signal Transduction Protein Chey" . . . . . 100.00 128 99.22 99.22 6.82e-84 . . . . 18234 2 21 no PDB 1F4V . "Crystal Structure Of Activated Chey Bound To The N-Terminus Of Flim" . . . . . 100.00 128 100.00 100.00 8.66e-85 . . . . 18234 2 22 no PDB 1FFG . "Chey-Binding Domain Of Chea In Complex With Chey At 2.1 A Resolution" . . . . . 100.00 128 100.00 100.00 8.66e-85 . . . . 18234 2 23 no PDB 1FFS . "Chey-Binding Domain Of Chea In Complex With Chey From Crystals Soaked In Acetyl Phosphate" . . . . . 100.00 128 100.00 100.00 8.66e-85 . . . . 18234 2 24 no PDB 1FFW . "Chey-Binding Domain Of Chea In Complex With Chey With A Bound Imido Diphosphate" . . . . . 100.00 128 100.00 100.00 8.66e-85 . . . . 18234 2 25 no PDB 1FQW . "Crystal Structure Of Activated Chey" . . . . . 100.00 128 100.00 100.00 8.66e-85 . . . . 18234 2 26 no PDB 1JBE . "1.08 A Structure Of Apo-Chey Reveals Meta-Active Conformation" . . . . . 100.00 128 98.44 98.44 8.13e-83 . . . . 18234 2 27 no PDB 1KMI . "Crystal Structure Of An E.Coli Chemotaxis Protein, Chez" . . . . . 100.00 129 100.00 100.00 5.18e-85 . . . . 18234 2 28 no PDB 1MIH . "A Role For Chey Glu 89 In Chez-Mediated Dephosphorylation Of The E. Coli Chemotaxis Response Regulator Chey" . . . . . 100.00 129 99.22 99.22 4.08e-84 . . . . 18234 2 29 no PDB 1VLZ . "Uncoupled Phosphorylation And Activation In Bacterial Chemotaxis: The 2.1 Angstrom Structure Of A Threonine To Isoleucine Mutan" . . . . . 100.00 128 99.22 99.22 6.82e-84 . . . . 18234 2 30 no PDB 1YMU . "Signal Transduction Protein Chey Mutant With Met 17 Replaced By Gly (M17g)" . . . . . 100.00 130 98.44 99.22 4.04e-83 . . . . 18234 2 31 no PDB 1ZDM . "Crystal Structure Of Activated Chey Bound To Xe" . . . . . 100.00 129 99.22 99.22 7.44e-84 . . . . 18234 2 32 no PDB 2B1J . "Crystal Structure Of Unphosphorylated Chey Bound To The N- Terminus Of Flim" . . . . . 100.00 128 100.00 100.00 8.66e-85 . . . . 18234 2 33 no PDB 2CHE . "Structure Of The Mg2+-Bound Form Of Chey And Mechanism Of Phosphoryl Transfer In Bacterial Chemotaxis" . . . . . 100.00 128 97.66 99.22 3.62e-83 . . . . 18234 2 34 no PDB 2CHF . "Structure Of The Mg2+-Bound Form Of Chey And The Mechanism Of Phosphoryl Transfer In Bacterial Chemotaxis" . . . . . 100.00 128 97.66 99.22 3.62e-83 . . . . 18234 2 35 no PDB 2FKA . "Crystal Structure Of Mg(2+) And Bef(3)(-)-Bound Chey In Complex With Chez(200-214) Solved From A F432 Crystal Grown In Caps (Ph" . . . . . 100.00 129 97.66 99.22 2.24e-83 . . . . 18234 2 36 no PDB 2FLK . "Crystal Structure Of Chey In Complex With Chez(200-214) Solved From A F432 Crystal Grown In Caps (Ph 10.5)" . . . . . 100.00 129 97.66 99.22 2.24e-83 . . . . 18234 2 37 no PDB 2FLW . "Crystal Structure Of Mg2+ And Bef3- Ound Chey In Complex With Chez 200-214 Solved From A F432 Crystal Grown In Hepes (ph 7.5)" . . . . . 100.00 129 97.66 99.22 2.24e-83 . . . . 18234 2 38 no PDB 2FMF . "Crystal Structure Of Chey In Complex With Chez 200-214 Solved From A F432 Crystal Grown In Hepes (ph 7.5)" . . . . . 100.00 129 97.66 99.22 2.24e-83 . . . . 18234 2 39 no PDB 2FMH . "Crystal Structure Of Mg2+ And Bef3- Bound Chey In Complex With Chez 200-214 Solved From A F432 Crystal Grown In Tris (Ph 8.4)" . . . . . 100.00 129 97.66 99.22 2.24e-83 . . . . 18234 2 40 no PDB 2FMI . "Crystal Structure Of Chey In Complex With Chez 200-214 Solved From A F432 Crystal Grown In Tris (Ph 8.4)" . . . . . 100.00 129 97.66 99.22 2.24e-83 . . . . 18234 2 41 no PDB 2FMK . "Crystal Structure Of Mg2+ And Bef3- Bound Chey In Complex With Chez 200-214 Solved From A P2(1)2(1)2 Crystal Grown In Mes (Ph 6" . . . . . 100.00 129 97.66 99.22 2.24e-83 . . . . 18234 2 42 no PDB 2ID7 . "1.75 A Structure Of T87i Phosphono-Chey" . . . . . 100.00 128 98.44 98.44 6.05e-83 . . . . 18234 2 43 no PDB 2ID9 . "1.85 A Structure Of T87i/y106w Phosphono-chey" . . . . . 100.00 128 97.66 98.44 4.76e-82 . . . . 18234 2 44 no PDB 2IDM . "2.00 A Structure Of T87iY106W PHOSPHONO-Chey" . . . . . 100.00 128 97.66 98.44 4.76e-82 . . . . 18234 2 45 no PDB 2LP4 . "Solution Structure Of P1-CheyP2 COMPLEX IN BACTERIAL CHEMOTAXIS" . . . . . 100.00 128 100.00 100.00 8.66e-85 . . . . 18234 2 46 no PDB 2PL9 . "Crystal Structure Of Chey-mg(2+)-bef(3)(-) In Complex With Chez(c19) Peptide Solved From A P2(1)2(1)2 Crystal" . . . . . 100.00 128 97.66 99.22 3.62e-83 . . . . 18234 2 47 no PDB 2PMC . "Crystal Structure Of Chey-mg(2+) In Complex With Chez(c15) Peptide Solved From A P1 Crystal" . . . . . 100.00 128 97.66 99.22 3.62e-83 . . . . 18234 2 48 no PDB 3CHY . "Crystal Structure Of Escherichia Coli Chey Refined At 1.7- Angstrom Resolution" . . . . . 100.00 128 100.00 100.00 8.66e-85 . . . . 18234 2 49 no PDB 3F7N . "Crystal Structure Of Chey Triple Mutant F14e, N59m, E89l Complexed With Bef3- And Mn2+" . . . . . 100.00 128 97.66 97.66 5.37e-81 . . . . 18234 2 50 no PDB 3FFT . "Crystal Structure Of Chey Double Mutant F14e, E89r Complexed With Bef3- And Mn2+" . . . . . 100.00 128 98.44 98.44 1.24e-82 . . . . 18234 2 51 no PDB 3FFW . "Crystal Structure Of Chey Triple Mutant F14q, N59k, E89y Complexed With Bef3- And Mn2+" . . . . . 100.00 128 97.66 97.66 1.29e-81 . . . . 18234 2 52 no PDB 3FFX . "Crystal Structure Of Chey Triple Mutant F14e, N59r, E89h Complexed With Bef3- And Mn2+" . . . . . 100.00 128 97.66 97.66 4.66e-82 . . . . 18234 2 53 no PDB 3FGZ . "Crystal Structure Of Chey Triple Mutant F14e, N59m, E89r Complexed With Bef3- And Mn2+" . . . . . 100.00 128 97.66 97.66 1.88e-81 . . . . 18234 2 54 no PDB 3MYY . "Structure Of E. Coli Chey Mutant A113p Bound To Beryllium Fluoride" . . . . . 100.00 128 99.22 99.22 4.36e-84 . . . . 18234 2 55 no PDB 3OLV . "Structural And Functional Effects Of Substitution At Position T+1 In Chey: Cheya88v-Bef3-Mg Complex" . . . . . 100.00 129 99.22 99.22 2.39e-84 . . . . 18234 2 56 no PDB 3OLW . "Structural And Functional Effects Of Substitution At Position T+1 In Chey: Cheya88t-Bef3-Mn Complex" . . . . . 100.00 129 99.22 99.22 2.07e-84 . . . . 18234 2 57 no PDB 3OLX . "Structural And Functional Effects Of Substitution At Position T+1 In Chey: Cheya88s-Bef3-Mn Complex" . . . . . 100.00 129 99.22 100.00 1.45e-84 . . . . 18234 2 58 no PDB 3OLY . "Structural And Functional Effects Of Substitution At Position T+1 In Chey: Cheya88m-Bef3-Mn Complex" . . . . . 100.00 129 99.22 99.22 3.18e-84 . . . . 18234 2 59 no PDB 3OO0 . "Structure Of Apo Chey A113p" . . . . . 100.00 129 99.22 99.22 3.86e-84 . . . . 18234 2 60 no PDB 3OO1 . "Structure Of E. Coli Chey Mutant A113p In The Absence Of Sulfate" . . . . . 100.00 129 99.22 99.22 3.86e-84 . . . . 18234 2 61 no PDB 3RVJ . "Structure Of The Chey-Bef3 Complex With Substitutions At 59 And 89: N59d And E89q" . . . . . 100.00 132 98.44 100.00 5.72e-84 . . . . 18234 2 62 no PDB 3RVK . "Structure Of The Chey-Mn2+ Complex With Substitutions At 59 And 89: N59d E89q" . . . . . 100.00 132 98.44 100.00 5.72e-84 . . . . 18234 2 63 no PDB 3RVL . "Structure Of The Chey-Bef3 Complex With Substitutions At 59 And 89: N59d And E89r" . . . . . 100.00 132 98.44 99.22 1.30e-83 . . . . 18234 2 64 no PDB 3RVM . "Structure Of The Chey-Mn2+ Complex With Substitutions At 59 And 89: N59d And E89r" . . . . . 100.00 132 98.44 99.22 1.30e-83 . . . . 18234 2 65 no PDB 3RVN . "Structure Of The Chey-Bef3 Complex With Substitutions At 59 And 89: N59d And E89y" . . . . . 100.00 132 98.44 99.22 2.22e-83 . . . . 18234 2 66 no PDB 3RVO . "Structure Of Chey-Mn2+ Complex With Substitutions At 59 And 89: N59d E89y" . . . . . 100.00 132 98.44 99.22 2.22e-83 . . . . 18234 2 67 no PDB 3RVP . "Structure Of The Chey-Bef3 Complex With Substitutions At 59 And 89: N59d And E89k" . . . . . 100.00 132 98.44 100.00 1.04e-83 . . . . 18234 2 68 no PDB 3RVQ . "Structure Of The Chey-Mn2+ Complex With Substitutions At 59 And 89: N59d E89k" . . . . . 100.00 132 98.44 100.00 1.04e-83 . . . . 18234 2 69 no PDB 3RVR . "Structure Of The Cheyn59dE89R MOLYBDATE COMPLEX" . . . . . 100.00 132 98.44 99.22 1.30e-83 . . . . 18234 2 70 no PDB 3RVS . "Structure Of The Cheyn59dE89R TUNGSTATE COMPLEX" . . . . . 100.00 132 98.44 99.22 1.30e-83 . . . . 18234 2 71 no PDB 5CHY . "Structure Of Chemotaxis Protein Chey" . . . . . 100.00 128 99.22 100.00 4.55e-84 . . . . 18234 2 72 no PDB 6CHY . "Structure Of Chemotaxis Protein Chey" . . . . . 100.00 128 98.44 99.22 3.87e-83 . . . . 18234 2 73 no DBJ BAA15698 . "chemotaxis regulator transmitting signal to flagellar motor component [Escherichia coli str. K-12 substr. W3110]" . . . . . 100.00 129 100.00 100.00 5.18e-85 . . . . 18234 2 74 no DBJ BAB36015 . "chemotaxis protein CheY [Escherichia coli O157:H7 str. Sakai]" . . . . . 100.00 129 100.00 100.00 5.18e-85 . . . . 18234 2 75 no DBJ BAG77641 . "chemotactic response regulator CheY [Escherichia coli SE11]" . . . . . 100.00 129 100.00 100.00 5.18e-85 . . . . 18234 2 76 no DBJ BAI25973 . "chemotaxis regulator CheY, transmitting signal to flagellar motor component [Escherichia coli O26:H11 str. 11368]" . . . . . 100.00 129 100.00 100.00 5.18e-85 . . . . 18234 2 77 no DBJ BAI30936 . "chemotaxis regulator CheY, transmitting signal to flagellar motor component [Escherichia coli O103:H2 str. 12009]" . . . . . 100.00 129 100.00 100.00 5.18e-85 . . . . 18234 2 78 no EMBL CAD05667 . "chemotaxis protein CheY [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" . . . . . 100.00 129 97.66 99.22 2.24e-83 . . . . 18234 2 79 no EMBL CAP76371 . "chemotaxis protein cheY [Escherichia coli LF82]" . . . . . 100.00 129 100.00 100.00 5.18e-85 . . . . 18234 2 80 no EMBL CAQ32359 . "chemotaxis regulator transmitting signal to flagellar motor component [Escherichia coli BL21(DE3)]" . . . . . 100.00 129 100.00 100.00 5.18e-85 . . . . 18234 2 81 no EMBL CAQ98822 . "chemotaxis regulator transmitting signal to flagellar motor component [Escherichia coli IAI1]" . . . . . 100.00 129 100.00 100.00 5.18e-85 . . . . 18234 2 82 no EMBL CAR03242 . "chemotaxis regulator transmitting signal to flagellar motor component [Escherichia coli S88]" . . . . . 100.00 129 99.22 100.00 1.63e-84 . . . . 18234 2 83 no GB AAA23570 . "cheY protein [Escherichia coli]" . . . . . 100.00 129 99.22 99.22 3.86e-84 . . . . 18234 2 84 no GB AAA23577 . "CheY [Escherichia coli]" . . . . . 100.00 129 100.00 100.00 5.18e-85 . . . . 18234 2 85 no GB AAA27037 . "CheY [Salmonella enterica subsp. enterica serovar Typhimurium]" . . . . . 100.00 129 97.66 99.22 2.24e-83 . . . . 18234 2 86 no GB AAC74952 . "chemotaxis regulator transmitting signal to flagellar motor component [Escherichia coli str. K-12 substr. MG1655]" . . . . . 100.00 129 100.00 100.00 5.18e-85 . . . . 18234 2 87 no GB AAG56872 . "chemotaxis regulator transmits chemoreceptor signals to flagelllar motor components [Escherichia coli O157:H7 str. EDL933]" . . . . . 100.00 129 100.00 100.00 5.18e-85 . . . . 18234 2 88 no PIR AH0745 . "chemotaxis protein CheY [imported] - Salmonella enterica subsp. enterica serovar Typhi (strain CT18)" . . . . . 100.00 129 97.66 99.22 2.24e-83 . . . . 18234 2 89 no REF NP_288319 . "chemotaxis regulatory protein CheY [Escherichia coli O157:H7 str. EDL933]" . . . . . 100.00 129 100.00 100.00 5.18e-85 . . . . 18234 2 90 no REF NP_310619 . "chemotaxis regulatory protein CheY [Escherichia coli O157:H7 str. Sakai]" . . . . . 100.00 129 100.00 100.00 5.18e-85 . . . . 18234 2 91 no REF NP_416396 . "chemotaxis regulator transmitting signal to flagellar motor component [Escherichia coli str. K-12 substr. MG1655]" . . . . . 100.00 129 100.00 100.00 5.18e-85 . . . . 18234 2 92 no REF NP_456482 . "chemotaxis protein CheY [Salmonella enterica subsp. enterica serovar Typhi str. CT18]" . . . . . 100.00 129 97.66 99.22 2.24e-83 . . . . 18234 2 93 no REF NP_460873 . "chemotaxis regulatory protein CheY [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" . . . . . 100.00 129 97.66 99.22 2.24e-83 . . . . 18234 2 94 no SP P0A2D5 . "RecName: Full=Chemotaxis protein CheY [Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]" . . . . . 100.00 129 97.66 99.22 2.24e-83 . . . . 18234 2 95 no SP P0A2D6 . "RecName: Full=Chemotaxis protein CheY [Salmonella enterica subsp. enterica serovar Typhi]" . . . . . 100.00 129 97.66 99.22 2.24e-83 . . . . 18234 2 96 no SP P0AE67 . "RecName: Full=Chemotaxis protein CheY [Escherichia coli K-12]" . . . . . 100.00 129 100.00 100.00 5.18e-85 . . . . 18234 2 97 no SP P0AE68 . "RecName: Full=Chemotaxis protein CheY [Escherichia coli O157:H7]" . . . . . 100.00 129 100.00 100.00 5.18e-85 . . . . 18234 2 98 no SP P0AE69 . "RecName: Full=Chemotaxis protein CheY [Shigella flexneri]" . . . . . 100.00 129 100.00 100.00 5.18e-85 . . . . 18234 2 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 2 ALA . 18234 2 2 3 ASP . 18234 2 3 4 LYS . 18234 2 4 5 GLU . 18234 2 5 6 LEU . 18234 2 6 7 LYS . 18234 2 7 8 PHE . 18234 2 8 9 LEU . 18234 2 9 10 VAL . 18234 2 10 11 VAL . 18234 2 11 12 ASP . 18234 2 12 13 ASP . 18234 2 13 14 PHE . 18234 2 14 15 SER . 18234 2 15 16 THR . 18234 2 16 17 MET . 18234 2 17 18 ARG . 18234 2 18 19 ARG . 18234 2 19 20 ILE . 18234 2 20 21 VAL . 18234 2 21 22 ARG . 18234 2 22 23 ASN . 18234 2 23 24 LEU . 18234 2 24 25 LEU . 18234 2 25 26 LYS . 18234 2 26 27 GLU . 18234 2 27 28 LEU . 18234 2 28 29 GLY . 18234 2 29 30 PHE . 18234 2 30 31 ASN . 18234 2 31 32 ASN . 18234 2 32 33 VAL . 18234 2 33 34 GLU . 18234 2 34 35 GLU . 18234 2 35 36 ALA . 18234 2 36 37 GLU . 18234 2 37 38 ASP . 18234 2 38 39 GLY . 18234 2 39 40 VAL . 18234 2 40 41 ASP . 18234 2 41 42 ALA . 18234 2 42 43 LEU . 18234 2 43 44 ASN . 18234 2 44 45 LYS . 18234 2 45 46 LEU . 18234 2 46 47 GLN . 18234 2 47 48 ALA . 18234 2 48 49 GLY . 18234 2 49 50 GLY . 18234 2 50 51 TYR . 18234 2 51 52 GLY . 18234 2 52 53 PHE . 18234 2 53 54 VAL . 18234 2 54 55 ILE . 18234 2 55 56 SER . 18234 2 56 57 ASP . 18234 2 57 58 TRP . 18234 2 58 59 ASN . 18234 2 59 60 MET . 18234 2 60 61 PRO . 18234 2 61 62 ASN . 18234 2 62 63 MET . 18234 2 63 64 ASP . 18234 2 64 65 GLY . 18234 2 65 66 LEU . 18234 2 66 67 GLU . 18234 2 67 68 LEU . 18234 2 68 69 LEU . 18234 2 69 70 LYS . 18234 2 70 71 THR . 18234 2 71 72 ILE . 18234 2 72 73 ARG . 18234 2 73 74 ALA . 18234 2 74 75 ASP . 18234 2 75 76 GLY . 18234 2 76 77 ALA . 18234 2 77 78 MET . 18234 2 78 79 SER . 18234 2 79 80 ALA . 18234 2 80 81 LEU . 18234 2 81 82 PRO . 18234 2 82 83 VAL . 18234 2 83 84 LEU . 18234 2 84 85 MET . 18234 2 85 86 VAL . 18234 2 86 87 THR . 18234 2 87 88 ALA . 18234 2 88 89 GLU . 18234 2 89 90 ALA . 18234 2 90 91 LYS . 18234 2 91 92 LYS . 18234 2 92 93 GLU . 18234 2 93 94 ASN . 18234 2 94 95 ILE . 18234 2 95 96 ILE . 18234 2 96 97 ALA . 18234 2 97 98 ALA . 18234 2 98 99 ALA . 18234 2 99 100 GLN . 18234 2 100 101 ALA . 18234 2 101 102 GLY . 18234 2 102 103 ALA . 18234 2 103 104 SER . 18234 2 104 105 GLY . 18234 2 105 106 TYR . 18234 2 106 107 VAL . 18234 2 107 108 VAL . 18234 2 108 109 LYS . 18234 2 109 110 PRO . 18234 2 110 111 PHE . 18234 2 111 112 THR . 18234 2 112 113 ALA . 18234 2 113 114 ALA . 18234 2 114 115 THR . 18234 2 115 116 LEU . 18234 2 116 117 GLU . 18234 2 117 118 GLU . 18234 2 118 119 LYS . 18234 2 119 120 LEU . 18234 2 120 121 ASN . 18234 2 121 122 LYS . 18234 2 122 123 ILE . 18234 2 123 124 PHE . 18234 2 124 125 GLU . 18234 2 125 126 LYS . 18234 2 126 127 LEU . 18234 2 127 128 GLY . 18234 2 128 129 MET . 18234 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 . ALA 1 1 18234 2 . ASP 2 2 18234 2 . LYS 3 3 18234 2 . GLU 4 4 18234 2 . LEU 5 5 18234 2 . LYS 6 6 18234 2 . PHE 7 7 18234 2 . LEU 8 8 18234 2 . VAL 9 9 18234 2 . VAL 10 10 18234 2 . ASP 11 11 18234 2 . ASP 12 12 18234 2 . PHE 13 13 18234 2 . SER 14 14 18234 2 . THR 15 15 18234 2 . MET 16 16 18234 2 . ARG 17 17 18234 2 . ARG 18 18 18234 2 . ILE 19 19 18234 2 . VAL 20 20 18234 2 . ARG 21 21 18234 2 . ASN 22 22 18234 2 . LEU 23 23 18234 2 . LEU 24 24 18234 2 . LYS 25 25 18234 2 . GLU 26 26 18234 2 . LEU 27 27 18234 2 . GLY 28 28 18234 2 . PHE 29 29 18234 2 . ASN 30 30 18234 2 . ASN 31 31 18234 2 . VAL 32 32 18234 2 . GLU 33 33 18234 2 . GLU 34 34 18234 2 . ALA 35 35 18234 2 . GLU 36 36 18234 2 . ASP 37 37 18234 2 . GLY 38 38 18234 2 . VAL 39 39 18234 2 . ASP 40 40 18234 2 . ALA 41 41 18234 2 . LEU 42 42 18234 2 . ASN 43 43 18234 2 . LYS 44 44 18234 2 . LEU 45 45 18234 2 . GLN 46 46 18234 2 . ALA 47 47 18234 2 . GLY 48 48 18234 2 . GLY 49 49 18234 2 . TYR 50 50 18234 2 . GLY 51 51 18234 2 . PHE 52 52 18234 2 . VAL 53 53 18234 2 . ILE 54 54 18234 2 . SER 55 55 18234 2 . ASP 56 56 18234 2 . TRP 57 57 18234 2 . ASN 58 58 18234 2 . MET 59 59 18234 2 . PRO 60 60 18234 2 . ASN 61 61 18234 2 . MET 62 62 18234 2 . ASP 63 63 18234 2 . GLY 64 64 18234 2 . LEU 65 65 18234 2 . GLU 66 66 18234 2 . LEU 67 67 18234 2 . LEU 68 68 18234 2 . LYS 69 69 18234 2 . THR 70 70 18234 2 . ILE 71 71 18234 2 . ARG 72 72 18234 2 . ALA 73 73 18234 2 . ASP 74 74 18234 2 . GLY 75 75 18234 2 . ALA 76 76 18234 2 . MET 77 77 18234 2 . SER 78 78 18234 2 . ALA 79 79 18234 2 . LEU 80 80 18234 2 . PRO 81 81 18234 2 . VAL 82 82 18234 2 . LEU 83 83 18234 2 . MET 84 84 18234 2 . VAL 85 85 18234 2 . THR 86 86 18234 2 . ALA 87 87 18234 2 . GLU 88 88 18234 2 . ALA 89 89 18234 2 . LYS 90 90 18234 2 . LYS 91 91 18234 2 . GLU 92 92 18234 2 . ASN 93 93 18234 2 . ILE 94 94 18234 2 . ILE 95 95 18234 2 . ALA 96 96 18234 2 . ALA 97 97 18234 2 . ALA 98 98 18234 2 . GLN 99 99 18234 2 . ALA 100 100 18234 2 . GLY 101 101 18234 2 . ALA 102 102 18234 2 . SER 103 103 18234 2 . GLY 104 104 18234 2 . TYR 105 105 18234 2 . VAL 106 106 18234 2 . VAL 107 107 18234 2 . LYS 108 108 18234 2 . PRO 109 109 18234 2 . PHE 110 110 18234 2 . THR 111 111 18234 2 . ALA 112 112 18234 2 . ALA 113 113 18234 2 . THR 114 114 18234 2 . LEU 115 115 18234 2 . GLU 116 116 18234 2 . GLU 117 117 18234 2 . LYS 118 118 18234 2 . LEU 119 119 18234 2 . ASN 120 120 18234 2 . LYS 121 121 18234 2 . ILE 122 122 18234 2 . PHE 123 123 18234 2 . GLU 124 124 18234 2 . LYS 125 125 18234 2 . LEU 126 126 18234 2 . GLY 127 127 18234 2 . MET 128 128 18234 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 18234 _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 $CheA_P1P2 . 562 organism . 'Escherichia coli' 'Escherichia coli' . . Bacteria . Escherichia coli . . . . . . . . . . . . . . . . . . . . . 18234 1 2 2 $CheY . 562 organism . 'Escherichia coli' 'Escherichia coli' . . Bacteria . Escherichia coli . . . . . . . . . . . . . . . . . . . . . 18234 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 18234 _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 $CheA_P1P2 . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . pQE12 . . . . . . 18234 1 2 2 $CheY . 'recombinant technology' 'Escherichia coli' . . . Escherichia coli . . . . . . . . . . . . . . . . pCW . . . . . . 18234 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Sample.Sf_category sample _Sample.Sf_framecode sample_1 _Sample.Entry_ID 18234 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details '50 mM sodium phosphate, pH 6.5. 5 mM DTT, 0.2% sodium azide' _Sample.Aggregate_sample_number . _Sample.Solvent_system '92% H2O/8% 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 CheY '[U-15N; U-2H]' . . 2 $CheY . . 200 . . mM . . . . 18234 1 2 'CheA P1' [U-2H] . . 1 $CheA_P1P2 . . 3000 . . mM . . . . 18234 1 3 'CheA P2' [U-2H] . . 1 $CheA_P1P2 . . 250 . . mM . . . . 18234 1 4 'sodium phosphate' 'natural abundance' . . . . . . 50 . . mM . . . . 18234 1 5 DTT 'natural abundance' . . . . . . 5 . . mM . . . . 18234 1 6 'sodium azide' 'natural abundance' . . . . . . 0.2 . . % . . . . 18234 1 7 H2O 'natural abundance' . . . . . . 92 . . % . . . . 18234 1 8 D2O 'natural abundance' . . . . . . 8 . . % . . . . 18234 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 18234 _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' 0.05 . M 18234 1 pH 6.5 . pH 18234 1 pressure 1 . atm 18234 1 temperature 273 . K 18234 1 stop_ save_ ############################ # Computer software used # ############################ save_ANSIG3.3 _Software.Sf_category software _Software.Sf_framecode ANSIG3.3 _Software.Entry_ID 18234 _Software.ID 1 _Software.Name ANSIG3.3 _Software.Version . _Software.Details . loop_ _Vendor.Name _Vendor.Address _Vendor.Electronic_address _Vendor.Entry_ID _Vendor.Software_ID Kraulis . . 18234 1 stop_ loop_ _Task.Task _Task.Entry_ID _Task.Software_ID 'chemical shift assignment' 18234 1 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 18234 _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 18234 _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 . . . 18234 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 18234 _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 . . . . . . . . . . . . . . . . 18234 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 18234 _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 H 1 DSS 'methyl protons' . . . . ppm 0.00 internal direct 1.000000000 . . . . . . . . . 18234 1 N 15 DSS 'methyl protons' . . . . ppm 0.00 na indirect 0.101329118 . . . . . . . . . 18234 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 18234 _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 '2D 1H-15N HSQC' . . . 18234 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 . 2 2 2 2 ASP H H 1 8.589 0.02 . 1 . . . Y 3 ASP H . 18234 1 2 . 2 2 2 2 ASP N N 15 121.39 0.2 . 1 . . . Y 3 ASP N . 18234 1 3 . 2 2 3 3 LYS H H 1 8.529 0.02 . 1 . . . Y 4 LYS H . 18234 1 4 . 2 2 3 3 LYS N N 15 122.47 0.2 . 1 . . . Y 4 LYS N . 18234 1 5 . 2 2 4 4 GLU H H 1 8.702 0.02 . 1 . . . Y 5 GLU H . 18234 1 6 . 2 2 4 4 GLU N N 15 119.02 0.2 . 1 . . . Y 5 GLU N . 18234 1 7 . 2 2 5 5 LEU H H 1 7.530 0.02 . 1 . . . Y 6 LEU H . 18234 1 8 . 2 2 5 5 LEU N N 15 124.23 0.2 . 1 . . . Y 6 LEU N . 18234 1 9 . 2 2 6 6 LYS H H 1 8.486 0.02 . 1 . . . Y 7 LYS H . 18234 1 10 . 2 2 6 6 LYS N N 15 126.09 0.2 . 1 . . . Y 7 LYS N . 18234 1 11 . 2 2 7 7 PHE H H 1 9.206 0.02 . 1 . . . Y 8 PHE H . 18234 1 12 . 2 2 7 7 PHE N N 15 128.54 0.2 . 1 . . . Y 8 PHE N . 18234 1 13 . 2 2 8 8 LEU H H 1 8.827 0.02 . 1 . . . Y 9 LEU H . 18234 1 14 . 2 2 8 8 LEU N N 15 121.92 0.2 . 1 . . . Y 9 LEU N . 18234 1 15 . 2 2 9 9 VAL H H 1 8.983 0.02 . 1 . . . Y 10 VAL H . 18234 1 16 . 2 2 9 9 VAL N N 15 127.28 0.2 . 1 . . . Y 10 VAL N . 18234 1 17 . 2 2 10 10 VAL H H 1 9.251 0.02 . 1 . . . Y 11 VAL H . 18234 1 18 . 2 2 10 10 VAL N N 15 127.25 0.2 . 1 . . . Y 11 VAL N . 18234 1 19 . 2 2 11 11 ASP H H 1 8.144 0.02 . 1 . . . Y 12 ASP H . 18234 1 20 . 2 2 11 11 ASP N N 15 123.77 0.2 . 1 . . . Y 12 ASP N . 18234 1 21 . 2 2 12 12 ASP H H 1 9.709 0.02 . 1 . . . Y 13 ASP H . 18234 1 22 . 2 2 12 12 ASP N N 15 124.94 0.2 . 1 . . . Y 13 ASP N . 18234 1 23 . 2 2 14 14 SER H H 1 9.493 0.02 . 1 . . . Y 15 SER H . 18234 1 24 . 2 2 14 14 SER N N 15 126.80 0.2 . 1 . . . Y 15 SER N . 18234 1 25 . 2 2 15 15 THR H H 1 7.372 0.02 . 1 . . . Y 16 THR H . 18234 1 26 . 2 2 15 15 THR N N 15 116.70 0.2 . 1 . . . Y 16 THR N . 18234 1 27 . 2 2 16 16 MET H H 1 6.326 0.02 . 1 . . . Y 17 MET H . 18234 1 28 . 2 2 16 16 MET N N 15 119.00 0.2 . 1 . . . Y 17 MET N . 18234 1 29 . 2 2 17 17 ARG H H 1 7.515 0.02 . 1 . . . Y 18 ARG H . 18234 1 30 . 2 2 17 17 ARG N N 15 116.67 0.2 . 1 . . . Y 18 ARG N . 18234 1 31 . 2 2 18 18 ARG H H 1 7.638 0.02 . 1 . . . Y 19 ARG H . 18234 1 32 . 2 2 18 18 ARG N N 15 116.98 0.2 . 1 . . . Y 19 ARG N . 18234 1 33 . 2 2 19 19 ILE H H 1 7.789 0.02 . 1 . . . Y 20 ILE H . 18234 1 34 . 2 2 19 19 ILE N N 15 120.79 0.2 . 1 . . . Y 20 ILE N . 18234 1 35 . 2 2 20 20 VAL H H 1 8.389 0.02 . 1 . . . Y 21 VAL H . 18234 1 36 . 2 2 20 20 VAL N N 15 119.34 0.2 . 1 . . . Y 21 VAL N . 18234 1 37 . 2 2 21 21 ARG H H 1 8.622 0.02 . 1 . . . Y 22 ARG H . 18234 1 38 . 2 2 21 21 ARG N N 15 119.43 0.2 . 1 . . . Y 22 ARG N . 18234 1 39 . 2 2 23 23 LEU H H 1 8.490 0.02 . 1 . . . Y 24 LEU H . 18234 1 40 . 2 2 23 23 LEU N N 15 123.39 0.2 . 1 . . . Y 24 LEU N . 18234 1 41 . 2 2 25 25 LYS H H 1 7.932 0.02 . 1 . . . Y 26 LYS H . 18234 1 42 . 2 2 25 25 LYS N N 15 120.62 0.2 . 1 . . . Y 26 LYS N . 18234 1 43 . 2 2 26 26 GLU H H 1 7.985 0.02 . 1 . . . Y 27 GLU H . 18234 1 44 . 2 2 26 26 GLU N N 15 122.29 0.2 . 1 . . . Y 27 GLU N . 18234 1 45 . 2 2 27 27 LEU H H 1 7.431 0.02 . 1 . . . Y 28 LEU H . 18234 1 46 . 2 2 27 27 LEU N N 15 117.21 0.2 . 1 . . . Y 28 LEU N . 18234 1 47 . 2 2 28 28 GLY H H 1 7.735 0.02 . 1 . . . Y 29 GLY H . 18234 1 48 . 2 2 28 28 GLY N N 15 106.17 0.2 . 1 . . . Y 29 GLY N . 18234 1 49 . 2 2 29 29 PHE H H 1 8.188 0.02 . 1 . . . Y 30 PHE H . 18234 1 50 . 2 2 29 29 PHE N N 15 121.14 0.2 . 1 . . . Y 30 PHE N . 18234 1 51 . 2 2 30 30 ASN H H 1 8.305 0.02 . 1 . . . Y 31 ASN H . 18234 1 52 . 2 2 30 30 ASN N N 15 118.22 0.2 . 1 . . . Y 31 ASN N . 18234 1 53 . 2 2 31 31 ASN H H 1 9.874 0.02 . 1 . . . Y 32 ASN H . 18234 1 54 . 2 2 31 31 ASN N N 15 124.51 0.2 . 1 . . . Y 32 ASN N . 18234 1 55 . 2 2 32 32 VAL H H 1 7.522 0.02 . 1 . . . Y 33 VAL H . 18234 1 56 . 2 2 32 32 VAL N N 15 122.03 0.2 . 1 . . . Y 33 VAL N . 18234 1 57 . 2 2 33 33 GLU H H 1 9.124 0.02 . 1 . . . Y 34 GLU H . 18234 1 58 . 2 2 33 33 GLU N N 15 126.88 0.2 . 1 . . . Y 34 GLU N . 18234 1 59 . 2 2 34 34 GLU H H 1 8.933 0.02 . 1 . . . Y 35 GLU H . 18234 1 60 . 2 2 34 34 GLU N N 15 120.80 0.2 . 1 . . . Y 35 GLU N . 18234 1 61 . 2 2 35 35 ALA H H 1 8.878 0.02 . 1 . . . Y 36 ALA H . 18234 1 62 . 2 2 35 35 ALA N N 15 120.50 0.2 . 1 . . . Y 36 ALA N . 18234 1 63 . 2 2 36 36 GLU H H 1 9.476 0.02 . 1 . . . Y 37 GLU H . 18234 1 64 . 2 2 36 36 GLU N N 15 117.42 0.2 . 1 . . . Y 37 GLU N . 18234 1 65 . 2 2 37 37 ASP H H 1 7.450 0.02 . 1 . . . Y 38 ASP H . 18234 1 66 . 2 2 37 37 ASP N N 15 131.50 0.2 . 1 . . . Y 38 ASP N . 18234 1 67 . 2 2 38 38 GLY H H 1 8.148 0.02 . 1 . . . Y 39 GLY H . 18234 1 68 . 2 2 38 38 GLY N N 15 102.39 0.2 . 1 . . . Y 39 GLY N . 18234 1 69 . 2 2 39 39 VAL H H 1 7.962 0.02 . 1 . . . Y 40 VAL H . 18234 1 70 . 2 2 39 39 VAL N N 15 122.62 0.2 . 1 . . . Y 40 VAL N . 18234 1 71 . 2 2 40 40 ASP H H 1 8.518 0.02 . 1 . . . Y 41 ASP H . 18234 1 72 . 2 2 40 40 ASP N N 15 121.11 0.2 . 1 . . . Y 41 ASP N . 18234 1 73 . 2 2 41 41 ALA H H 1 8.337 0.02 . 1 . . . Y 42 ALA H . 18234 1 74 . 2 2 41 41 ALA N N 15 116.97 0.2 . 1 . . . Y 42 ALA N . 18234 1 75 . 2 2 42 42 LEU H H 1 8.121 0.02 . 1 . . . Y 43 LEU H . 18234 1 76 . 2 2 42 42 LEU N N 15 118.28 0.2 . 1 . . . Y 43 LEU N . 18234 1 77 . 2 2 45 45 LEU H H 1 8.748 0.02 . 1 . . . Y 46 LEU H . 18234 1 78 . 2 2 45 45 LEU N N 15 118.53 0.2 . 1 . . . Y 46 LEU N . 18234 1 79 . 2 2 46 46 GLN H H 1 7.865 0.02 . 1 . . . Y 47 GLN H . 18234 1 80 . 2 2 46 46 GLN N N 15 116.82 0.2 . 1 . . . Y 47 GLN N . 18234 1 81 . 2 2 47 47 ALA H H 1 7.611 0.02 . 1 . . . Y 48 ALA H . 18234 1 82 . 2 2 47 47 ALA N N 15 120.46 0.2 . 1 . . . Y 48 ALA N . 18234 1 83 . 2 2 48 48 GLY H H 1 7.574 0.02 . 1 . . . Y 49 GLY H . 18234 1 84 . 2 2 48 48 GLY N N 15 104.28 0.2 . 1 . . . Y 49 GLY N . 18234 1 85 . 2 2 49 49 GLY H H 1 8.367 0.02 . 1 . . . Y 50 GLY H . 18234 1 86 . 2 2 49 49 GLY N N 15 103.81 0.2 . 1 . . . Y 50 GLY N . 18234 1 87 . 2 2 50 50 TYR H H 1 8.126 0.02 . 1 . . . Y 51 TYR H . 18234 1 88 . 2 2 50 50 TYR N N 15 118.74 0.2 . 1 . . . Y 51 TYR N . 18234 1 89 . 2 2 51 51 GLY H H 1 9.556 0.02 . 1 . . . Y 52 GLY H . 18234 1 90 . 2 2 51 51 GLY N N 15 106.90 0.2 . 1 . . . Y 52 GLY N . 18234 1 91 . 2 2 52 52 PHE H H 1 7.527 0.02 . 1 . . . Y 53 PHE H . 18234 1 92 . 2 2 52 52 PHE N N 15 121.38 0.2 . 1 . . . Y 53 PHE N . 18234 1 93 . 2 2 53 53 VAL H H 1 8.246 0.02 . 1 . . . Y 54 VAL H . 18234 1 94 . 2 2 53 53 VAL N N 15 127.15 0.2 . 1 . . . Y 54 VAL N . 18234 1 95 . 2 2 54 54 ILE H H 1 9.235 0.02 . 1 . . . Y 55 ILE H . 18234 1 96 . 2 2 54 54 ILE N N 15 128.13 0.2 . 1 . . . Y 55 ILE N . 18234 1 97 . 2 2 55 55 SER H H 1 8.678 0.02 . 1 . . . Y 56 SER H . 18234 1 98 . 2 2 55 55 SER N N 15 118.20 0.2 . 1 . . . Y 56 SER N . 18234 1 99 . 2 2 56 56 ASP H H 1 8.412 0.02 . 1 . . . Y 57 ASP H . 18234 1 100 . 2 2 56 56 ASP N N 15 127.29 0.2 . 1 . . . Y 57 ASP N . 18234 1 101 . 2 2 58 58 ASN H H 1 8.716 0.02 . 1 . . . Y 59 ASN H . 18234 1 102 . 2 2 58 58 ASN N N 15 116.98 0.2 . 1 . . . Y 59 ASN N . 18234 1 103 . 2 2 61 61 ASN H H 1 8.598 0.02 . 1 . . . Y 62 ASN H . 18234 1 104 . 2 2 61 61 ASN N N 15 112.14 0.2 . 1 . . . Y 62 ASN N . 18234 1 105 . 2 2 62 62 MET H H 1 9.192 0.02 . 1 . . . Y 63 MET H . 18234 1 106 . 2 2 62 62 MET N N 15 122.95 0.2 . 1 . . . Y 63 MET N . 18234 1 107 . 2 2 63 63 ASP H H 1 8.518 0.02 . 1 . . . Y 64 ASP H . 18234 1 108 . 2 2 63 63 ASP N N 15 126.54 0.2 . 1 . . . Y 64 ASP N . 18234 1 109 . 2 2 65 65 LEU H H 1 7.733 0.02 . 1 . . . Y 66 LEU H . 18234 1 110 . 2 2 65 65 LEU N N 15 121.87 0.2 . 1 . . . Y 66 LEU N . 18234 1 111 . 2 2 66 66 GLU H H 1 8.085 0.02 . 1 . . . Y 67 GLU H . 18234 1 112 . 2 2 66 66 GLU N N 15 119.47 0.2 . 1 . . . Y 67 GLU N . 18234 1 113 . 2 2 67 67 LEU H H 1 8.299 0.02 . 1 . . . Y 68 LEU H . 18234 1 114 . 2 2 67 67 LEU N N 15 123.91 0.2 . 1 . . . Y 68 LEU N . 18234 1 115 . 2 2 68 68 LEU H H 1 8.249 0.02 . 1 . . . Y 69 LEU H . 18234 1 116 . 2 2 68 68 LEU N N 15 120.64 0.2 . 1 . . . Y 69 LEU N . 18234 1 117 . 2 2 69 69 LYS H H 1 8.400 0.02 . 1 . . . Y 70 LYS H . 18234 1 118 . 2 2 69 69 LYS N N 15 116.08 0.2 . 1 . . . Y 70 LYS N . 18234 1 119 . 2 2 70 70 THR H H 1 8.028 0.02 . 1 . . . Y 71 THR H . 18234 1 120 . 2 2 70 70 THR N N 15 117.49 0.2 . 1 . . . Y 71 THR N . 18234 1 121 . 2 2 71 71 ILE H H 1 8.459 0.02 . 1 . . . Y 72 ILE H . 18234 1 122 . 2 2 71 71 ILE N N 15 123.64 0.2 . 1 . . . Y 72 ILE N . 18234 1 123 . 2 2 72 72 ARG H H 1 8.112 0.02 . 1 . . . Y 73 ARG H . 18234 1 124 . 2 2 72 72 ARG N N 15 113.35 0.2 . 1 . . . Y 73 ARG N . 18234 1 125 . 2 2 73 73 ALA H H 1 7.286 0.02 . 1 . . . Y 74 ALA H . 18234 1 126 . 2 2 73 73 ALA N N 15 118.90 0.2 . 1 . . . Y 74 ALA N . 18234 1 127 . 2 2 74 74 ASP H H 1 7.399 0.02 . 1 . . . Y 75 ASP H . 18234 1 128 . 2 2 74 74 ASP N N 15 121.87 0.2 . 1 . . . Y 75 ASP N . 18234 1 129 . 2 2 75 75 GLY H H 1 8.728 0.02 . 1 . . . Y 76 GLY H . 18234 1 130 . 2 2 75 75 GLY N N 15 112.23 0.2 . 1 . . . Y 76 GLY N . 18234 1 131 . 2 2 76 76 ALA H H 1 8.558 0.02 . 1 . . . Y 77 ALA H . 18234 1 132 . 2 2 76 76 ALA N N 15 121.97 0.2 . 1 . . . Y 77 ALA N . 18234 1 133 . 2 2 77 77 MET H H 1 8.477 0.02 . 1 . . . Y 78 MET H . 18234 1 134 . 2 2 77 77 MET N N 15 116.18 0.2 . 1 . . . Y 78 MET N . 18234 1 135 . 2 2 78 78 SER H H 1 7.436 0.02 . 1 . . . Y 79 SER H . 18234 1 136 . 2 2 78 78 SER N N 15 112.91 0.2 . 1 . . . Y 79 SER N . 18234 1 137 . 2 2 79 79 ALA H H 1 8.246 0.02 . 1 . . . Y 80 ALA H . 18234 1 138 . 2 2 79 79 ALA N N 15 123.08 0.2 . 1 . . . Y 80 ALA N . 18234 1 139 . 2 2 80 80 LEU H H 1 7.816 0.02 . 1 . . . Y 81 LEU H . 18234 1 140 . 2 2 80 80 LEU N N 15 124.13 0.2 . 1 . . . Y 81 LEU N . 18234 1 141 . 2 2 82 82 VAL H H 1 7.731 0.02 . 1 . . . Y 83 VAL H . 18234 1 142 . 2 2 82 82 VAL N N 15 118.86 0.2 . 1 . . . Y 83 VAL N . 18234 1 143 . 2 2 83 83 LEU H H 1 9.135 0.02 . 1 . . . Y 84 LEU H . 18234 1 144 . 2 2 83 83 LEU N N 15 130.45 0.2 . 1 . . . Y 84 LEU N . 18234 1 145 . 2 2 84 84 MET H H 1 7.855 0.02 . 1 . . . Y 85 MET H . 18234 1 146 . 2 2 84 84 MET N N 15 124.08 0.2 . 1 . . . Y 85 MET N . 18234 1 147 . 2 2 85 85 VAL H H 1 9.198 0.02 . 1 . . . Y 86 VAL H . 18234 1 148 . 2 2 85 85 VAL N N 15 124.81 0.2 . 1 . . . Y 86 VAL N . 18234 1 149 . 2 2 86 86 THR H H 1 8.715 0.02 . 1 . . . Y 87 THR H . 18234 1 150 . 2 2 86 86 THR N N 15 116.56 0.2 . 1 . . . Y 87 THR N . 18234 1 151 . 2 2 87 87 ALA H H 1 8.807 0.02 . 1 . . . Y 88 ALA H . 18234 1 152 . 2 2 87 87 ALA N N 15 125.46 0.2 . 1 . . . Y 88 ALA N . 18234 1 153 . 2 2 89 89 ALA H H 1 9.090 0.02 . 1 . . . Y 90 ALA H . 18234 1 154 . 2 2 89 89 ALA N N 15 129.99 0.2 . 1 . . . Y 90 ALA N . 18234 1 155 . 2 2 90 90 LYS H H 1 7.197 0.02 . 1 . . . Y 91 LYS H . 18234 1 156 . 2 2 90 90 LYS N N 15 121.03 0.2 . 1 . . . Y 91 LYS N . 18234 1 157 . 2 2 92 92 GLU H H 1 9.648 0.02 . 1 . . . Y 93 GLU H . 18234 1 158 . 2 2 92 92 GLU N N 15 116.28 0.2 . 1 . . . Y 93 GLU N . 18234 1 159 . 2 2 93 93 ASN H H 1 7.116 0.02 . 1 . . . Y 94 ASN H . 18234 1 160 . 2 2 93 93 ASN N N 15 117.03 0.2 . 1 . . . Y 94 ASN N . 18234 1 161 . 2 2 94 94 ILE H H 1 7.546 0.02 . 1 . . . Y 95 ILE H . 18234 1 162 . 2 2 94 94 ILE N N 15 121.11 0.2 . 1 . . . Y 95 ILE N . 18234 1 163 . 2 2 95 95 ILE H H 1 8.172 0.02 . 1 . . . Y 96 ILE H . 18234 1 164 . 2 2 95 95 ILE N N 15 117.16 0.2 . 1 . . . Y 96 ILE N . 18234 1 165 . 2 2 96 96 ALA H H 1 7.541 0.02 . 1 . . . Y 97 ALA H . 18234 1 166 . 2 2 96 96 ALA N N 15 120.06 0.2 . 1 . . . Y 97 ALA N . 18234 1 167 . 2 2 97 97 ALA H H 1 8.524 0.02 . 1 . . . Y 98 ALA H . 18234 1 168 . 2 2 97 97 ALA N N 15 119.15 0.2 . 1 . . . Y 98 ALA N . 18234 1 169 . 2 2 99 99 GLN H H 1 8.974 0.02 . 1 . . . Y 100 GLN H . 18234 1 170 . 2 2 99 99 GLN N N 15 118.21 0.2 . 1 . . . Y 100 GLN N . 18234 1 171 . 2 2 100 100 ALA H H 1 7.624 0.02 . 1 . . . Y 101 ALA H . 18234 1 172 . 2 2 100 100 ALA N N 15 117.99 0.2 . 1 . . . Y 101 ALA N . 18234 1 173 . 2 2 102 102 ALA H H 1 8.726 0.02 . 1 . . . Y 103 ALA H . 18234 1 174 . 2 2 102 102 ALA N N 15 123.64 0.2 . 1 . . . Y 103 ALA N . 18234 1 175 . 2 2 103 103 SER H H 1 9.114 0.02 . 1 . . . Y 104 SER H . 18234 1 176 . 2 2 103 103 SER N N 15 115.00 0.2 . 1 . . . Y 104 SER N . 18234 1 177 . 2 2 104 104 GLY H H 1 7.442 0.02 . 1 . . . Y 105 GLY H . 18234 1 178 . 2 2 104 104 GLY N N 15 103.25 0.2 . 1 . . . Y 105 GLY N . 18234 1 179 . 2 2 105 105 TYR H H 1 8.524 0.02 . 1 . . . Y 106 TYR H . 18234 1 180 . 2 2 105 105 TYR N N 15 118.86 0.2 . 1 . . . Y 106 TYR N . 18234 1 181 . 2 2 107 107 VAL H H 1 8.089 0.02 . 1 . . . Y 108 VAL H . 18234 1 182 . 2 2 107 107 VAL N N 15 127.36 0.2 . 1 . . . Y 108 VAL N . 18234 1 183 . 2 2 108 108 LYS H H 1 8.376 0.02 . 1 . . . Y 109 LYS H . 18234 1 184 . 2 2 108 108 LYS N N 15 123.48 0.2 . 1 . . . Y 109 LYS N . 18234 1 185 . 2 2 110 110 PHE H H 1 7.583 0.02 . 1 . . . Y 111 PHE H . 18234 1 186 . 2 2 110 110 PHE N N 15 115.95 0.2 . 1 . . . Y 111 PHE N . 18234 1 187 . 2 2 111 111 THR H H 1 7.916 0.02 . 1 . . . Y 112 THR H . 18234 1 188 . 2 2 111 111 THR N N 15 130.47 0.2 . 1 . . . Y 112 THR N . 18234 1 189 . 2 2 112 112 ALA H H 1 9.188 0.02 . 1 . . . Y 113 ALA H . 18234 1 190 . 2 2 112 112 ALA N N 15 122.65 0.2 . 1 . . . Y 113 ALA N . 18234 1 191 . 2 2 113 113 ALA H H 1 8.212 0.02 . 1 . . . Y 114 ALA H . 18234 1 192 . 2 2 113 113 ALA N N 15 118.69 0.2 . 1 . . . Y 114 ALA N . 18234 1 193 . 2 2 115 115 LEU H H 1 8.235 0.02 . 1 . . . Y 116 LEU H . 18234 1 194 . 2 2 115 115 LEU N N 15 121.77 0.2 . 1 . . . Y 116 LEU N . 18234 1 195 . 2 2 116 116 GLU H H 1 8.857 0.02 . 1 . . . Y 117 GLU H . 18234 1 196 . 2 2 116 116 GLU N N 15 119.06 0.2 . 1 . . . Y 117 GLU N . 18234 1 197 . 2 2 117 117 GLU H H 1 7.670 0.02 . 1 . . . Y 118 GLU H . 18234 1 198 . 2 2 117 117 GLU N N 15 117.75 0.2 . 1 . . . Y 118 GLU N . 18234 1 199 . 2 2 119 119 LEU H H 1 8.543 0.02 . 1 . . . Y 120 LEU H . 18234 1 200 . 2 2 119 119 LEU N N 15 118.40 0.2 . 1 . . . Y 120 LEU N . 18234 1 201 . 2 2 120 120 ASN H H 1 8.605 0.02 . 1 . . . Y 121 ASN H . 18234 1 202 . 2 2 120 120 ASN N N 15 115.13 0.2 . 1 . . . Y 121 ASN N . 18234 1 203 . 2 2 121 121 LYS H H 1 7.585 0.02 . 1 . . . Y 122 LYS H . 18234 1 204 . 2 2 121 121 LYS N N 15 119.73 0.2 . 1 . . . Y 122 LYS N . 18234 1 205 . 2 2 122 122 ILE H H 1 7.385 0.02 . 1 . . . Y 123 ILE H . 18234 1 206 . 2 2 122 122 ILE N N 15 120.98 0.2 . 1 . . . Y 123 ILE N . 18234 1 207 . 2 2 123 123 PHE H H 1 9.111 0.02 . 1 . . . Y 124 PHE H . 18234 1 208 . 2 2 123 123 PHE N N 15 117.66 0.2 . 1 . . . Y 124 PHE N . 18234 1 209 . 2 2 124 124 GLU H H 1 8.330 0.02 . 1 . . . Y 125 GLU H . 18234 1 210 . 2 2 124 124 GLU N N 15 119.19 0.2 . 1 . . . Y 125 GLU N . 18234 1 211 . 2 2 125 125 LYS H H 1 8.317 0.02 . 1 . . . Y 126 LYS H . 18234 1 212 . 2 2 125 125 LYS N N 15 121.31 0.2 . 1 . . . Y 126 LYS N . 18234 1 213 . 2 2 127 127 GLY H H 1 7.966 0.02 . 1 . . . Y 128 GLY H . 18234 1 214 . 2 2 127 127 GLY N N 15 110.53 0.2 . 1 . . . Y 128 GLY N . 18234 1 215 . 2 2 128 128 MET H H 1 8.432 0.02 . 1 . . . Y 129 MET H . 18234 1 216 . 2 2 128 128 MET N N 15 124.43 0.2 . 1 . . . Y 129 MET N . 18234 1 stop_ save_