data_5171 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR Structure of BPTI Mutant G37A ; _BMRB_accession_number 5171 _BMRB_flat_file_name bmr5171.str _Entry_type original _Submission_date 2001-10-03 _Accession_date 2001-10-03 _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 Battiste J. L. . 2 Li R. . . 3 Woodward C. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 283 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-05-06 original BMRB . stop_ _Original_release_date 2001-10-03 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; A Highly Destabilizing Mutation, G37A, of the Bovine Pancreatic Trypsin Inhibitor Retains the Average Native Conformation but Greatly Increases Local Flexibility ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 21830327 _PubMed_ID 11841215 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Battiste J. L. . 2 Li R. . . 3 Woodward C. . . stop_ _Journal_abbreviation Biochemistry _Journal_volume 41 _Journal_issue 7 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2237 _Page_last 2245 _Year 2002 _Details . loop_ _Keyword BPTI 'Conformational Strain' 'G37A Mutant' 'Minimized Average Structure' stop_ save_ ################################## # Molecular system description # ################################## save_system_BPTI_G37A _Saveframe_category molecular_system _Mol_system_name 'BPTI G37A, TRYPSIN INHIBITOR' _Abbreviation_common 'BPTI G37A' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'BPTI G37A' $BPTI_G37A stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_BPTI_G37A _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common BPTI _Name_variant G37A _Abbreviation_common 'BPTI G37A' _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 58 _Mol_residue_sequence ; RPDFCLEPPYTGPCKARIIR YFYNAKAGLCQTFVYGACRA KRNNFKSAEDCMRTCGGA ; loop_ _Residue_seq_code _Residue_label 1 ARG 2 PRO 3 ASP 4 PHE 5 CYS 6 LEU 7 GLU 8 PRO 9 PRO 10 TYR 11 THR 12 GLY 13 PRO 14 CYS 15 LYS 16 ALA 17 ARG 18 ILE 19 ILE 20 ARG 21 TYR 22 PHE 23 TYR 24 ASN 25 ALA 26 LYS 27 ALA 28 GLY 29 LEU 30 CYS 31 GLN 32 THR 33 PHE 34 VAL 35 TYR 36 GLY 37 ALA 38 CYS 39 ARG 40 ALA 41 LYS 42 ARG 43 ASN 44 ASN 45 PHE 46 LYS 47 SER 48 ALA 49 GLU 50 ASP 51 CYS 52 MET 53 ARG 54 THR 55 CYS 56 GLY 57 GLY 58 ALA 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 $BPTI_G37A . . . . . . 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 $BPTI_G37A . . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $BPTI_G37A 5 mM . H2O 90 % . D2O 10 % . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $BPTI_G37A 5 mM . D2O 99.9 % . stop_ save_ ############################ # Computer software used # ############################ save_VNMR _Saveframe_category software _Name VNMR _Version 6.1B loop_ _Task 'data collection' stop_ _Details . save_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 1.7 loop_ _Task 'data processing' stop_ _Details . save_ save_XEASY _Saveframe_category software _Name XEASY _Version 1.2 loop_ _Task 'data analysis' stop_ _Details . save_ save_X-PLOR _Saveframe_category software _Name X-PLOR _Version 3.851 loop_ _Task 'structure solution, refinement' stop_ _Details 'Brunger, A. T.' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Varian _Model INOVA _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_DQF-COSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details 'ionic strength is estimated from protein alone' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 30 . mM pH 4.6 . n/a pressure 1 . atm temperature 298 . K stop_ save_ save_sample_cond_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 30 . mM pH 4.6 . n/a pressure 1 . atm temperature 283 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_ref_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 . H 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_chemical_shift_set_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D NOESY' DQF-COSY stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_ref_1 _Mol_system_component_name 'BPTI G37A' _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 . 2 PRO HA H 4.28 . . 2 . 2 PRO HB3 H 0.87 . . 3 . 2 PRO HB2 H 1.99 . . 4 . 2 PRO HG3 H 1.57 . . 5 . 2 PRO HG2 H 1.84 . . 6 . 2 PRO HD3 H 3.58 . . 7 . 2 PRO HD2 H 3.68 . . 8 . 3 ASP H H 8.68 . . 9 . 3 ASP HA H 4.21 . . 10 . 3 ASP HB2 H 2.73 . . 11 . 3 ASP HB3 H 2.73 . . 12 . 4 PHE H H 7.83 . . 13 . 4 PHE HA H 4.55 . . 14 . 4 PHE HB3 H 3.31 . . 15 . 4 PHE HB2 H 2.90 . . 16 . 5 CYS H H 7.43 . . 17 . 5 CYS HA H 4.32 . . 18 . 5 CYS HB2 H 2.77 . . 19 . 5 CYS HB3 H 2.77 . . 20 . 6 LEU H H 7.55 . . 21 . 6 LEU HA H 4.48 . . 22 . 6 LEU HB2 H 1.81 . . 23 . 6 LEU HB3 H 1.81 . . 24 . 6 LEU HG H 1.66 . . 25 . 6 LEU HD1 H 0.92 . . 26 . 6 LEU HD2 H 0.82 . . 27 . 7 GLU H H 7.51 . . 28 . 7 GLU HA H 4.55 . . 29 . 7 GLU HB2 H 2.17 . . 30 . 7 GLU HB3 H 2.17 . . 31 . 7 GLU HG2 H 2.54 . . 32 . 7 GLU HG3 H 2.54 . . 33 . 8 PRO HA H 4.59 . . 34 . 8 PRO HB3 H 1.82 . . 35 . 8 PRO HB2 H 2.41 . . 36 . 8 PRO HG2 H 2.09 . . 37 . 8 PRO HG3 H 2.09 . . 38 . 8 PRO HD2 H 3.77 . . 39 . 8 PRO HD3 H 3.77 . . 40 . 9 PRO HA H 3.66 . . 41 . 9 PRO HB3 H 0.25 . . 42 . 9 PRO HB2 H 0.08 . . 43 . 9 PRO HG3 H 1.24 . . 44 . 9 PRO HG2 H 0.17 . . 45 . 9 PRO HD3 H 3.31 . . 46 . 9 PRO HD2 H 2.87 . . 47 . 10 TYR H H 7.76 . . 48 . 10 TYR HA H 4.88 . . 49 . 10 TYR HB2 H 2.95 . . 50 . 10 TYR HB3 H 2.95 . . 51 . 11 THR H H 8.93 . . 52 . 11 THR HA H 4.53 . . 53 . 11 THR HB H 4.00 . . 54 . 11 THR HG2 H 1.33 . . 55 . 12 GLY H H 7.12 . . 56 . 12 GLY HA3 H 3.21 . . 57 . 12 GLY HA2 H 3.90 . . 58 . 13 PRO HA H 4.52 . . 59 . 13 PRO HB2 H 2.10 . . 60 . 13 PRO HB3 H 2.10 . . 61 . 13 PRO HG2 H 1.94 . . 62 . 13 PRO HG3 H 1.94 . . 63 . 13 PRO HD2 H 3.58 . . 64 . 13 PRO HD3 H 3.58 . . 65 . 14 CYS H H 8.68 . . 66 . 14 CYS HA H 4.52 . . 67 . 14 CYS HB3 H 2.92 . . 68 . 14 CYS HB2 H 3.48 . . 69 . 15 LYS H H 7.98 . . 70 . 15 LYS HA H 4.31 . . 71 . 15 LYS HB3 H 1.54 . . 72 . 15 LYS HB2 H 2.02 . . 73 . 15 LYS HG2 H 1.37 . . 74 . 15 LYS HG3 H 1.37 . . 75 . 15 LYS HD2 H 1.24 . . 76 . 15 LYS HD3 H 1.24 . . 77 . 15 LYS HE2 H 2.92 . . 78 . 15 LYS HE3 H 2.92 . . 79 . 16 ALA H H 7.88 . . 80 . 16 ALA HA H 4.25 . . 81 . 16 ALA HB H 1.20 . . 82 . 17 ARG H H 8.21 . . 83 . 17 ARG HA H 4.34 . . 84 . 17 ARG HB3 H 1.56 . . 85 . 17 ARG HB2 H 1.44 . . 86 . 17 ARG HG2 H 1.27 . . 87 . 17 ARG HG3 H 1.27 . . 88 . 17 ARG HE H 7.17 . . 89 . 18 ILE H H 8.19 . . 90 . 18 ILE HA H 4.25 . . 91 . 18 ILE HB H 1.95 . . 92 . 18 ILE HG2 H 0.93 . . 93 . 18 ILE HG12 H 1.23 . . 94 . 18 ILE HG13 H 1.23 . . 95 . 18 ILE HD1 H 0.75 . . 96 . 19 ILE H H 8.64 . . 97 . 19 ILE HA H 4.30 . . 98 . 19 ILE HB H 1.91 . . 99 . 19 ILE HG2 H 0.69 . . 100 . 19 ILE HG12 H 1.38 . . 101 . 19 ILE HG13 H 1.38 . . 102 . 19 ILE HD1 H 0.65 . . 103 . 20 ARG H H 8.39 . . 104 . 20 ARG HA H 4.66 . . 105 . 20 ARG HB3 H 0.75 . . 106 . 20 ARG HB2 H 1.77 . . 107 . 20 ARG HD2 H 3.22 . . 108 . 20 ARG HD3 H 3.22 . . 109 . 20 ARG HE H 7.45 . . 110 . 21 TYR H H 9.15 . . 111 . 21 TYR HA H 5.66 . . 112 . 21 TYR HB2 H 2.66 . . 113 . 21 TYR HB3 H 2.66 . . 114 . 22 PHE H H 9.75 . . 115 . 22 PHE HA H 5.23 . . 116 . 22 PHE HB3 H 2.78 . . 117 . 22 PHE HB2 H 2.87 . . 118 . 23 TYR H H 10.52 . . 119 . 23 TYR HA H 4.26 . . 120 . 23 TYR HB3 H 2.69 . . 121 . 23 TYR HB2 H 3.42 . . 122 . 24 ASN H H 7.74 . . 123 . 24 ASN HA H 4.56 . . 124 . 24 ASN HB3 H 2.15 . . 125 . 24 ASN HB2 H 2.82 . . 126 . 24 ASN HD22 H 7.08 . . 127 . 24 ASN HD21 H 7.89 . . 128 . 25 ALA H H 8.80 . . 129 . 25 ALA HA H 3.73 . . 130 . 25 ALA HB H 1.52 . . 131 . 26 LYS H H 7.90 . . 132 . 26 LYS HA H 4.03 . . 133 . 26 LYS HB2 H 1.84 . . 134 . 26 LYS HB3 H 1.84 . . 135 . 26 LYS HG2 H 1.59 . . 136 . 26 LYS HG3 H 1.59 . . 137 . 26 LYS HD2 H 1.42 . . 138 . 26 LYS HD3 H 1.42 . . 139 . 26 LYS HE2 H 3.00 . . 140 . 26 LYS HE3 H 3.00 . . 141 . 27 ALA H H 6.79 . . 142 . 27 ALA HA H 4.25 . . 143 . 27 ALA HB H 1.15 . . 144 . 28 GLY H H 8.12 . . 145 . 28 GLY HA3 H 3.58 . . 146 . 28 GLY HA2 H 3.88 . . 147 . 29 LEU H H 6.80 . . 148 . 29 LEU HA H 4.72 . . 149 . 29 LEU HB2 H 1.55 . . 150 . 29 LEU HB3 H 1.55 . . 151 . 29 LEU HG H 1.39 . . 152 . 29 LEU HD1 H 0.82 . . 153 . 29 LEU HD2 H 0.72 . . 154 . 30 CYS H H 8.41 . . 155 . 30 CYS HA H 5.58 . . 156 . 30 CYS HB3 H 3.65 . . 157 . 30 CYS HB2 H 2.63 . . 158 . 31 GLN H H 8.74 . . 159 . 31 GLN HA H 4.79 . . 160 . 31 GLN HB3 H 1.70 . . 161 . 31 GLN HB2 H 2.16 . . 162 . 31 GLN HG2 H 2.02 . . 163 . 31 GLN HG3 H 2.02 . . 164 . 31 GLN HE22 H 6.94 . . 165 . 31 GLN HE21 H 7.42 . . 166 . 32 THR H H 8.02 . . 167 . 32 THR HA H 5.25 . . 168 . 32 THR HB H 4.01 . . 169 . 32 THR HG2 H 0.57 . . 170 . 33 PHE H H 9.32 . . 171 . 33 PHE HA H 4.82 . . 172 . 33 PHE HB3 H 2.91 . . 173 . 33 PHE HB2 H 3.05 . . 174 . 34 VAL H H 8.36 . . 175 . 34 VAL HA H 3.94 . . 176 . 34 VAL HB H 1.89 . . 177 . 34 VAL HG1 H 0.75 . . 178 . 34 VAL HG2 H 0.71 . . 179 . 35 TYR H H 9.42 . . 180 . 35 TYR HA H 4.92 . . 181 . 35 TYR HB3 H 2.48 . . 182 . 35 TYR HB2 H 2.60 . . 183 . 36 GLY H H 8.38 . . 184 . 36 GLY HA2 H 3.63 . . 185 . 36 GLY HA3 H 3.63 . . 186 . 37 ALA H H 4.36 . . 187 . 37 ALA HA H 3.28 . . 188 . 37 ALA HB H 1.44 . . 189 . 38 CYS H H 7.68 . . 190 . 38 CYS HA H 4.82 . . 191 . 38 CYS HB2 H 3.46 . . 192 . 38 CYS HB3 H 3.46 . . 193 . 39 ARG H H 9.03 . . 194 . 39 ARG HA H 3.90 . . 195 . 39 ARG HB2 H 2.22 . . 196 . 39 ARG HB3 H 2.22 . . 197 . 39 ARG HG2 H 1.56 . . 198 . 39 ARG HG3 H 1.56 . . 199 . 39 ARG HD2 H 3.20 . . 200 . 39 ARG HD3 H 3.20 . . 201 . 39 ARG HE H 7.27 . . 202 . 40 ALA H H 7.38 . . 203 . 40 ALA HA H 4.05 . . 204 . 40 ALA HB H 1.17 . . 205 . 41 LYS H H 8.34 . . 206 . 41 LYS HA H 4.40 . . 207 . 41 LYS HB3 H 1.61 . . 208 . 41 LYS HB2 H 2.20 . . 209 . 41 LYS HD2 H 1.29 . . 210 . 41 LYS HD3 H 1.29 . . 211 . 42 ARG H H 8.37 . . 212 . 42 ARG HA H 3.62 . . 213 . 42 ARG HB3 H 1.00 . . 214 . 42 ARG HB2 H 0.33 . . 215 . 42 ARG HG2 H 1.31 . . 216 . 42 ARG HG3 H 1.31 . . 217 . 42 ARG HD2 H 2.72 . . 218 . 42 ARG HD3 H 2.72 . . 219 . 42 ARG HE H 7.12 . . 220 . 43 ASN H H 7.19 . . 221 . 43 ASN HA H 5.02 . . 222 . 43 ASN HB3 H 3.23 . . 223 . 43 ASN HB2 H 3.32 . . 224 . 43 ASN HD22 H 7.76 . . 225 . 43 ASN HD21 H 7.95 . . 226 . 44 ASN H H 6.73 . . 227 . 44 ASN HA H 4.86 . . 228 . 44 ASN HB2 H 2.73 . . 229 . 44 ASN HB3 H 2.46 . . 230 . 44 ASN HD22 H 3.34 . . 231 . 44 ASN HD21 H 7.78 . . 232 . 45 PHE H H 9.92 . . 233 . 45 PHE HA H 5.09 . . 234 . 45 PHE HB3 H 2.76 . . 235 . 45 PHE HB2 H 3.37 . . 236 . 46 LYS H H 9.92 . . 237 . 46 LYS HA H 4.34 . . 238 . 46 LYS HB2 H 1.88 . . 239 . 46 LYS HB3 H 1.88 . . 240 . 47 SER H H 7.43 . . 241 . 47 SER HA H 4.49 . . 242 . 47 SER HB3 H 4.09 . . 243 . 47 SER HB2 H 3.82 . . 244 . 48 ALA H H 8.13 . . 245 . 48 ALA HA H 3.13 . . 246 . 48 ALA HB H 1.01 . . 247 . 49 GLU H H 8.56 . . 248 . 49 GLU HA H 3.83 . . 249 . 49 GLU HB2 H 1.89 . . 250 . 49 GLU HB3 H 1.89 . . 251 . 49 GLU HG2 H 2.25 . . 252 . 49 GLU HG3 H 2.25 . . 253 . 50 ASP H H 7.85 . . 254 . 50 ASP HA H 4.24 . . 255 . 50 ASP HB2 H 2.77 . . 256 . 50 ASP HB3 H 2.77 . . 257 . 51 CYS H H 6.98 . . 258 . 51 CYS HA H 1.64 . . 259 . 51 CYS HB3 H 2.85 . . 260 . 51 CYS HB2 H 3.14 . . 261 . 52 MET H H 8.58 . . 262 . 52 MET HA H 4.14 . . 263 . 52 MET HB3 H 2.02 . . 264 . 52 MET HB2 H 1.92 . . 265 . 52 MET HG2 H 2.65 . . 266 . 52 MET HG3 H 2.65 . . 267 . 53 ARG H H 8.26 . . 268 . 53 ARG HA H 3.95 . . 269 . 53 ARG HB2 H 1.86 . . 270 . 53 ARG HB3 H 1.86 . . 271 . 53 ARG HG2 H 1.64 . . 272 . 53 ARG HG3 H 1.64 . . 273 . 53 ARG HD2 H 3.18 . . 274 . 53 ARG HD3 H 3.18 . . 275 . 53 ARG HE H 7.24 . . 276 . 54 THR H H 7.36 . . 277 . 54 THR HA H 4.04 . . 278 . 54 THR HB H 3.96 . . 279 . 54 THR HG2 H 1.58 . . 280 . 55 CYS H H 8.24 . . 281 . 55 CYS HA H 4.57 . . 282 . 55 CYS HB2 H 2.12 . . 283 . 55 CYS HB3 H 2.12 . . stop_ save_