data_27037 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Alanine chemical shifts of the N-terminal domain (residues 1-215) of HtpG, the Hsp90 from Escherichia coli. Northeast Structural Genomics Consortium Target ER697A. ; _BMRB_accession_number 27037 _BMRB_flat_file_name bmr27037.str _Entry_type original _Submission_date 2017-02-24 _Accession_date 2017-02-24 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Ramelot Theresa A. . 2 Pederson Kari . . 3 Wang Huang . . 4 Maglaqui Melissa . . 5 Mao Lei . . 6 Xiao Rong A. . 7 Acton Thomas B. . 8 Everett John K. . 9 Prestegard James H. . 10 Montelione Gaetano T. . 11 Kennedy Michael A. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 39 "13C chemical shifts" 39 "15N chemical shifts" 13 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2017-06-30 update BMRB 'update entry citation' 2017-06-30 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 27038 'C-terminal dimerization domain (residues 511-624) of HtpG' stop_ _Original_release_date 2017-02-27 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR characterization of HtpG, the E. coli Hsp90, using sparse labeling with (13)C-methyl alanine ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 28653216 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Pederson Kari . . 2 Chalmers Gordon R. . 3 Gao Qi . . 4 Elnatan Daniel . . 5 Ramelot Theresa A. . 6 Ma Li-Chung C. . 7 Montelione Gaetano T. . 8 Kennedy Michael A. . 9 Agard David A. . 10 Prestegard James H. . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_name_full 'Journal of biomolecular NMR' _Journal_volume 68 _Journal_issue 3 _Journal_ISSN 1573-5001 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 225 _Page_last 236 _Year 2017 _Details . loop_ _Keyword Hsp90 stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name NTD _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label NTD $NTD stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_NTD _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common NTD _Molecular_mass . _Mol_thiol_state 'all free' loop_ _Biological_function Hsp90 chaperone stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 214 _Mol_residue_sequence ; KGQETRGFQSEVKQLLHLMI HSLYSNKEIFLRELISNASD AADKLRFRALSNPDLYEGDG ELRVRVSFDKDKRTLTISDN GVGMTRDEVIDHLGTIAKSG TKSFLESLGSDQAKDSQLIG QFGVGFYSAFIVADKVTVRT RAAGEKPENGVFWESAGEGE YTVADITKEDRGTEITLHLR EGEDEFLDDWRVRSIISKYS DHIALPVEIEKREE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 2 LYS 2 3 GLY 3 4 GLN 4 5 GLU 5 6 THR 6 7 ARG 7 8 GLY 8 9 PHE 9 10 GLN 10 11 SER 11 12 GLU 12 13 VAL 13 14 LYS 14 15 GLN 15 16 LEU 16 17 LEU 17 18 HIS 18 19 LEU 19 20 MET 20 21 ILE 21 22 HIS 22 23 SER 23 24 LEU 24 25 TYR 25 26 SER 26 27 ASN 27 28 LYS 28 29 GLU 29 30 ILE 30 31 PHE 31 32 LEU 32 33 ARG 33 34 GLU 34 35 LEU 35 36 ILE 36 37 SER 37 38 ASN 38 39 ALA 39 40 SER 40 41 ASP 41 42 ALA 42 43 ALA 43 44 ASP 44 45 LYS 45 46 LEU 46 47 ARG 47 48 PHE 48 49 ARG 49 50 ALA 50 51 LEU 51 52 SER 52 53 ASN 53 54 PRO 54 55 ASP 55 56 LEU 56 57 TYR 57 58 GLU 58 59 GLY 59 60 ASP 60 61 GLY 61 62 GLU 62 63 LEU 63 64 ARG 64 65 VAL 65 66 ARG 66 67 VAL 67 68 SER 68 69 PHE 69 70 ASP 70 71 LYS 71 72 ASP 72 73 LYS 73 74 ARG 74 75 THR 75 76 LEU 76 77 THR 77 78 ILE 78 79 SER 79 80 ASP 80 81 ASN 81 82 GLY 82 83 VAL 83 84 GLY 84 85 MET 85 86 THR 86 87 ARG 87 88 ASP 88 89 GLU 89 90 VAL 90 91 ILE 91 92 ASP 92 93 HIS 93 94 LEU 94 95 GLY 95 96 THR 96 97 ILE 97 98 ALA 98 99 LYS 99 100 SER 100 101 GLY 101 102 THR 102 103 LYS 103 104 SER 104 105 PHE 105 106 LEU 106 107 GLU 107 108 SER 108 109 LEU 109 110 GLY 110 111 SER 111 112 ASP 112 113 GLN 113 114 ALA 114 115 LYS 115 116 ASP 116 117 SER 117 118 GLN 118 119 LEU 119 120 ILE 120 121 GLY 121 122 GLN 122 123 PHE 123 124 GLY 124 125 VAL 125 126 GLY 126 127 PHE 127 128 TYR 128 129 SER 129 130 ALA 130 131 PHE 131 132 ILE 132 133 VAL 133 134 ALA 134 135 ASP 135 136 LYS 136 137 VAL 137 138 THR 138 139 VAL 139 140 ARG 140 141 THR 141 142 ARG 142 143 ALA 143 144 ALA 144 145 GLY 145 146 GLU 146 147 LYS 147 148 PRO 148 149 GLU 149 150 ASN 150 151 GLY 151 152 VAL 152 153 PHE 153 154 TRP 154 155 GLU 155 156 SER 156 157 ALA 157 158 GLY 158 159 GLU 159 160 GLY 160 161 GLU 161 162 TYR 162 163 THR 163 164 VAL 164 165 ALA 165 166 ASP 166 167 ILE 167 168 THR 168 169 LYS 169 170 GLU 170 171 ASP 171 172 ARG 172 173 GLY 173 174 THR 174 175 GLU 175 176 ILE 176 177 THR 177 178 LEU 178 179 HIS 179 180 LEU 180 181 ARG 181 182 GLU 182 183 GLY 183 184 GLU 184 185 ASP 185 186 GLU 186 187 PHE 187 188 LEU 188 189 ASP 189 190 ASP 190 191 TRP 191 192 ARG 192 193 VAL 193 194 ARG 194 195 SER 195 196 ILE 196 197 ILE 197 198 SER 198 199 LYS 199 200 TYR 200 201 SER 201 202 ASP 202 203 HIS 203 204 ILE 204 205 ALA 205 206 LEU 206 207 PRO 207 208 VAL 208 209 GLU 209 210 ILE 210 211 GLU 211 212 LYS 212 213 ARG 213 214 GLU 214 215 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic $NTD 'E. coli' 562 Bacteria . Escherichia coli HtpG stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $NTD 'recombinant technology' . Escherichia coli 'BL21(DE3) + Magic' pET15_NESG stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details 'NC sample' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $NTD 0.49 mM '[U-100% 13C; U-100% 15N]' TRIS 10 mM 'natural abundance' 'sodium chloride' 100 mM 'natural abundance' 'sodium azide' 0.02 % 'natural abundance' DTT 10 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_PINE _Saveframe_category software _Name PINE _Version . loop_ _Vendor _Address _Electronic_address 'Bahrami, Markley, Assadi, and Eghbalnia' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'peak picking' stop_ _Details . save_ save_VNMR _Saveframe_category software _Name VNMR _Version . loop_ _Vendor _Address _Electronic_address Varian . . stop_ loop_ _Task collection stop_ _Details . save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_600v _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 600 _Details . save_ save_spectrometer_850 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 850 _Details . save_ save_spectrometer_600b _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_NH2_only_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC NH2 only' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_CT_aliphatic_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC CT aliphatic' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCACB_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HBHA(CO)NH_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_11 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_12 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_13 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _BMRB_pulse_sequence_accession_number . _Details 600v save_ save_2D_1H-13C_HSQC_CT_aliphatic _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC CT aliphatic' _BMRB_pulse_sequence_accession_number . _Details 600v save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details 'sample conditions 1' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.1 0.01 M pH 7.5 .1 pH pressure 1 . atm temperature 308 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 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 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Software_label $SPARKY stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '2D 1H-13C HSQC CT aliphatic' '3D HN(CA)CO' '3D 1H-15N NOESY' '3D CBCA(CO)NH' '3D HNCACB' '3D HBHA(CO)NH' '3D HNCO' '3D HNCA' '3D HN(CO)CA' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name NTD _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 39 38 ALA H H 7.50 0.02 1 2 39 38 ALA HA H 4.26 0.02 1 3 39 38 ALA HB H 1.45 0.02 1 4 39 38 ALA C C 178.8 0.2 1 5 39 38 ALA CA C 55.0 0.2 1 6 39 38 ALA CB C 18.7 0.2 1 7 39 38 ALA N N 123.9 0.2 1 8 42 41 ALA H H 8.18 0.02 1 9 42 41 ALA HA H 4.20 0.02 1 10 42 41 ALA HB H 1.74 0.02 1 11 42 41 ALA C C 181.5 0.2 1 12 42 41 ALA CA C 54.9 0.2 1 13 42 41 ALA CB C 18.9 0.2 1 14 42 41 ALA N N 122.7 0.2 1 15 43 42 ALA H H 8.47 0.02 1 16 43 42 ALA HA H 4.16 0.02 1 17 43 42 ALA HB H 1.63 0.02 1 18 43 42 ALA C C 178.8 0.2 1 19 43 42 ALA CA C 55.3 0.2 1 20 43 42 ALA CB C 19.1 0.2 1 21 43 42 ALA N N 124.3 0.2 1 22 50 49 ALA H H 8.75 0.02 1 23 50 49 ALA HA H 4.06 0.02 1 24 50 49 ALA HB H 0.86 0.02 1 25 50 49 ALA C C 178.8 0.2 1 26 50 49 ALA CA C 52.5 0.2 1 27 50 49 ALA CB C 18.4 0.2 1 28 50 49 ALA N N 120.1 0.2 1 29 98 97 ALA H H 8.07 0.02 1 30 98 97 ALA HA H 4.26 0.02 1 31 98 97 ALA HB H 1.36 0.02 1 32 98 97 ALA C C 177.8 0.2 1 33 98 97 ALA CA C 52.9 0.2 1 34 98 97 ALA CB C 19.2 0.2 1 35 98 97 ALA N N 125.2 0.2 1 36 114 113 ALA H H 8.16 0.02 1 37 114 113 ALA HA H 4.26 0.02 1 38 114 113 ALA HB H 1.43 0.02 1 39 114 113 ALA C C 178.5 0.2 1 40 114 113 ALA CA C 53.3 0.2 1 41 114 113 ALA CB C 18.9 0.2 1 42 114 113 ALA N N 123.5 0.2 1 43 130 129 ALA H H 7.81 0.02 1 44 130 129 ALA HA H 3.57 0.02 1 45 130 129 ALA HB H 0.93 0.02 1 46 130 129 ALA C C 178.3 0.2 1 47 130 129 ALA CA C 54.8 0.2 1 48 130 129 ALA CB C 18.9 0.2 1 49 130 129 ALA N N 123.9 0.2 1 50 134 133 ALA H H 7.68 0.02 1 51 134 133 ALA HA H 5.11 0.02 1 52 134 133 ALA HB H 0.95 0.02 1 53 134 133 ALA C C 175.1 0.2 1 54 134 133 ALA CA C 51.1 0.2 1 55 134 133 ALA CB C 23.0 0.2 1 56 134 133 ALA N N 124.9 0.2 1 57 143 142 ALA H H 8.69 0.02 1 58 143 142 ALA HA H 5.01 0.02 1 59 143 142 ALA HB H 1.21 0.02 1 60 143 142 ALA C C 178.5 0.2 1 61 143 142 ALA CA C 51.0 0.2 1 62 143 142 ALA CB C 20.3 0.2 1 63 143 142 ALA N N 129.9 0.2 1 64 144 143 ALA H H 8.71 0.02 1 65 144 143 ALA HA H 4.09 0.02 1 66 144 143 ALA HB H 1.37 0.02 1 67 144 143 ALA C C 177.9 0.2 1 68 144 143 ALA CA C 52.5 0.2 1 69 144 143 ALA CB C 19.9 0.2 1 70 144 143 ALA N N 123.9 0.2 1 71 157 156 ALA H H 8.59 0.02 1 72 157 156 ALA HA H 5.24 0.02 1 73 157 156 ALA HB H 1.60 0.02 1 74 157 156 ALA C C 177.1 0.2 1 75 157 156 ALA CA C 51.8 0.2 1 76 157 156 ALA CB C 19.5 0.2 1 77 157 156 ALA N N 129.0 0.2 1 78 165 164 ALA H H 9.40 0.02 1 79 165 164 ALA HA H 4.79 0.02 1 80 165 164 ALA HB H 1.38 0.02 1 81 165 164 ALA C C 174.6 0.2 1 82 165 164 ALA CA C 51.4 0.2 1 83 165 164 ALA CB C 23.8 0.2 1 84 165 164 ALA N N 126.3 0.2 1 85 205 204 ALA H H 8.49 0.02 1 86 205 204 ALA HA H 4.46 0.02 1 87 205 204 ALA HB H 1.40 0.02 1 88 205 204 ALA C C 176.3 0.2 1 89 205 204 ALA CA C 52.2 0.2 1 90 205 204 ALA CB C 19.2 0.2 1 91 205 204 ALA N N 127.8 0.2 1 stop_ save_