data_5375 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structure of BPTI_8A mutant ; _BMRB_accession_number 5375 _BMRB_flat_file_name bmr5375.str _Entry_type original _Submission_date 2002-05-13 _Accession_date 2002-05-13 _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 Cierpicki T. . . 2 Otlewski J. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 coupling_constants 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 322 "coupling constants" 39 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2003-01-06 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 5381 'BPTI A16V mutant.' stop_ _Original_release_date 2002-05-13 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR Structures of Two Variants of Bovine Pancreatic Trypsin Inhibitor (BPTI) reveal Unexpected Influence of Mutations on Protein Structure and Stability ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code 22195730 _PubMed_ID 12206780 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Cierpicki T. . . 2 Otlewski J. . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 321 _Journal_issue 4 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 647 _Page_last 658 _Year 2002 _Details . loop_ _Keyword BPTI 'Kunitz fold' stop_ save_ ################################## # Molecular system description # ################################## save_system_anneal10_2 _Saveframe_category molecular_system _Mol_system_name anneal10_2 _Abbreviation_common BPTI_8A _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'pancreatic trypsin inhibitor' $BPTI_8A 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_8A _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'pancreatic trypsin inhibitor' _Abbreviation_common BPTI_8A _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 58 _Mol_residue_sequence ; RPDFCLEPPYAGACRAAAAR YFYNAKAGLCQTFAYGACAA KRNNFKSAEDCLRTCGGA ; 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 ALA 12 GLY 13 ALA 14 CYS 15 ARG 16 ALA 17 ALA 18 ALA 19 ALA 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 ALA 35 TYR 36 GLY 37 ALA 38 CYS 39 ALA 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 LEU 53 ARG 54 THR 55 CYS 56 GLY 57 GLY 58 ALA stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value PDB 1LD6 'Structure Of Bpti_8a Mutant' 100.00 58 100.00 100.00 2.11e-24 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $BPTI_8A Cow 9913 Eukaryota Metazoa Bos taurus 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_8A 'recombinant technology' 'E. coli' Escherichia coli . . 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_8A 3 mM . H2O 90 % . D2O 10 % . stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version 1.8 loop_ _Task processing stop_ _Details 'Delaglio, F.; Grzesiek, S.; Vuister, G.; Zhu, G.; Pfeifer, J.; Bax, A.' save_ save_Sparky _Saveframe_category software _Name SPARKY _Version 3.95 loop_ _Task 'data analysis' stop_ _Details 'Goddard, T.D.; Kneller, D.G.' save_ save_DYANA _Saveframe_category software _Name DYANA _Version 1.5 loop_ _Task 'structure solution' stop_ _Details 'Guntert, P.; Mumenthaler, C.; Herrmann, T.' save_ save_CNS _Saveframe_category software _Name CNS _Version 1.0 loop_ _Task refinement stop_ _Details ; Brunger, A.T.; Adams, P.D.; Clore, G.M.; DeLano, W.L., Gros,P.; Grosse-Kunstleve, R.W.; Jiang, J.S.; Kuszewski, J.; Nilges, M.; Pannu, N.S.; Read, R.J.; Rice, L.M.; Simonson, T.; Warren, G.L. ; save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _Field_strength 500 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D TOCSY' _Sample_label . save_ save_2D_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D NOESY' _Sample_label . save_ save_DQF-COSY_3 _Saveframe_category NMR_applied_experiment _Experiment_name DQF-COSY _Sample_label . save_ ####################### # Sample conditions # ####################### save_sample_cond_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0 . M pH 2.9 . n/a pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _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 . ppm . . . . . . 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 TOCSY' '2D NOESY' DQF-COSY stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name 'pancreatic trypsin inhibitor' _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 . 1 ARG HA H 4.38 . 1 2 . 1 ARG HB2 H 1.83 . 2 3 . 1 ARG HB3 H 1.90 . 2 4 . 1 ARG HG2 H 1.38 . 2 5 . 1 ARG HG3 H 1.51 . 2 6 . 1 ARG HD2 H 2.85 . 2 7 . 1 ARG HD3 H 3.07 . 2 8 . 1 ARG HE H 7.11 . 1 9 . 2 PRO HA H 4.32 . 1 10 . 2 PRO HB2 H 0.91 . 1 11 . 2 PRO HB3 H 2.02 . 1 12 . 2 PRO HG2 H 1.62 . 1 13 . 2 PRO HG3 H 1.89 . 1 14 . 2 PRO HD2 H 3.61 . 1 15 . 2 PRO HD3 H 3.73 . 1 16 . 3 ASP H H 8.95 . 1 17 . 3 ASP HA H 4.31 . 1 18 . 3 ASP HB2 H 2.96 . 1 19 . 3 ASP HB3 H 2.96 . 1 20 . 4 PHE H H 7.70 . 1 21 . 4 PHE HA H 4.60 . 1 22 . 4 PHE HB2 H 3.42 . 1 23 . 4 PHE HB3 H 3.06 . 1 24 . 4 PHE HD1 H 7.08 . 1 25 . 4 PHE HD2 H 7.08 . 1 26 . 4 PHE HE1 H 7.40 . 1 27 . 4 PHE HE2 H 7.40 . 1 28 . 4 PHE HZ H 7.36 . 1 29 . 5 CYS H H 7.37 . 1 30 . 5 CYS HA H 4.38 . 1 31 . 5 CYS HB2 H 2.78 . 2 32 . 5 CYS HB3 H 2.84 . 2 33 . 6 LEU H H 7.57 . 1 34 . 6 LEU HA H 4.32 . 1 35 . 6 LEU HB2 H 1.88 . 1 36 . 6 LEU HB3 H 1.88 . 1 37 . 6 LEU HG H 1.69 . 1 38 . 6 LEU HD1 H 0.97 . 1 39 . 6 LEU HD2 H 0.86 . 1 40 . 7 GLU H H 7.46 . 1 41 . 7 GLU HA H 4.84 . 1 42 . 7 GLU HB2 H 2.23 . 2 43 . 7 GLU HB3 H 2.38 . 2 44 . 7 GLU HG2 H 2.67 . 1 45 . 7 GLU HG3 H 2.67 . 1 46 . 8 PRO HA H 4.88 . 1 47 . 8 PRO HB2 H 2.37 . 1 48 . 8 PRO HB3 H 2.37 . 1 49 . 8 PRO HG2 H 2.09 . 2 50 . 8 PRO HG3 H 2.14 . 2 51 . 8 PRO HD2 H 3.88 . 2 52 . 8 PRO HD3 H 4.25 . 2 53 . 9 PRO HA H 4.72 . 1 54 . 9 PRO HB2 H 1.48 . 2 55 . 9 PRO HB3 H 1.84 . 2 56 . 9 PRO HG2 H 0.95 . 2 57 . 9 PRO HG3 H 1.08 . 2 58 . 9 PRO HD2 H 3.23 . 1 59 . 9 PRO HD3 H 3.23 . 1 60 . 10 TYR H H 8.25 . 1 61 . 10 TYR HA H 4.90 . 1 62 . 10 TYR HB2 H 2.90 . 2 63 . 10 TYR HB3 H 3.00 . 2 64 . 10 TYR HD1 H 6.95 . 1 65 . 10 TYR HD2 H 6.95 . 1 66 . 10 TYR HE1 H 6.67 . 1 67 . 10 TYR HE2 H 6.67 . 1 68 . 11 ALA H H 8.47 . 1 69 . 11 ALA HA H 4.47 . 1 70 . 11 ALA HB H 1.36 . 1 71 . 12 GLY H H 7.71 . 1 72 . 12 GLY HA2 H 3.83 . 2 73 . 12 GLY HA3 H 4.17 . 2 74 . 13 ALA H H 8.51 . 1 75 . 13 ALA HA H 4.41 . 1 76 . 13 ALA HB H 1.31 . 1 77 . 14 CYS H H 7.79 . 1 78 . 14 CYS HA H 4.44 . 1 79 . 14 CYS HB2 H 2.61 . 2 80 . 14 CYS HB3 H 3.30 . 2 81 . 15 ARG H H 8.40 . 1 82 . 15 ARG HA H 4.23 . 1 83 . 15 ARG HB2 H 1.69 . 2 84 . 15 ARG HB3 H 1.80 . 2 85 . 15 ARG HG2 H 1.56 . 2 86 . 15 ARG HG3 H 1.60 . 2 87 . 15 ARG HD2 H 3.17 . 1 88 . 15 ARG HD3 H 3.17 . 1 89 . 15 ARG HE H 7.17 . 1 90 . 16 ALA H H 8.27 . 1 91 . 16 ALA HA H 4.21 . 1 92 . 16 ALA HB H 1.32 . 1 93 . 17 ALA H H 8.30 . 1 94 . 17 ALA HA H 4.36 . 1 95 . 17 ALA HB H 1.30 . 1 96 . 18 ALA H H 7.86 . 1 97 . 18 ALA HA H 4.31 . 1 98 . 18 ALA HB H 1.38 . 1 99 . 19 ALA H H 8.35 . 1 100 . 19 ALA HA H 4.35 . 1 101 . 19 ALA HB H 1.40 . 1 102 . 20 ARG H H 7.83 . 1 103 . 20 ARG HA H 4.88 . 1 104 . 20 ARG HB2 H 1.80 . 2 105 . 20 ARG HB3 H 2.29 . 2 106 . 20 ARG HG2 H 1.64 . 2 107 . 20 ARG HG3 H 1.68 . 2 108 . 20 ARG HD2 H 3.19 . 2 109 . 20 ARG HD3 H 3.30 . 2 110 . 20 ARG HE H 7.63 . 1 111 . 21 TYR H H 9.03 . 1 112 . 21 TYR HA H 5.29 . 1 113 . 21 TYR HB2 H 2.60 . 1 114 . 21 TYR HB3 H 2.60 . 1 115 . 21 TYR HD1 H 6.61 . 1 116 . 21 TYR HD2 H 6.61 . 1 117 . 21 TYR HE1 H 6.76 . 1 118 . 21 TYR HE2 H 6.76 . 1 119 . 22 PHE H H 9.21 . 1 120 . 22 PHE HA H 5.16 . 1 121 . 22 PHE HB2 H 2.84 . 1 122 . 22 PHE HB3 H 3.00 . 1 123 . 22 PHE HD1 H 6.45 . 1 124 . 22 PHE HD2 H 6.45 . 1 125 . 22 PHE HE1 H 6.96 . 1 126 . 22 PHE HE2 H 6.96 . 1 127 . 22 PHE HZ H 7.16 . 1 128 . 23 TYR H H 10.45 . 1 129 . 23 TYR HA H 4.36 . 1 130 . 23 TYR HB2 H 2.80 . 1 131 . 23 TYR HB3 H 3.49 . 1 132 . 23 TYR HD1 H 7.20 . 1 133 . 23 TYR HD2 H 7.20 . 1 134 . 23 TYR HE1 H 6.36 . 1 135 . 23 TYR HE2 H 6.36 . 1 136 . 24 ASN H H 8.22 . 1 137 . 24 ASN HA H 4.62 . 1 138 . 24 ASN HB2 H 2.24 . 1 139 . 24 ASN HB3 H 2.91 . 1 140 . 24 ASN HD21 H 7.16 . 1 141 . 24 ASN HD22 H 7.92 . 1 142 . 25 ALA H H 8.60 . 1 143 . 25 ALA HA H 3.81 . 1 144 . 25 ALA HB H 1.62 . 1 145 . 26 LYS H H 7.97 . 1 146 . 26 LYS HA H 4.09 . 1 147 . 26 LYS HB2 H 1.92 . 1 148 . 26 LYS HB3 H 1.92 . 1 149 . 26 LYS HG2 H 1.46 . 2 150 . 26 LYS HG3 H 1.54 . 2 151 . 26 LYS HD2 H 1.74 . 1 152 . 26 LYS HD3 H 1.74 . 1 153 . 26 LYS HE2 H 3.05 . 1 154 . 26 LYS HE3 H 3.05 . 1 155 . 27 ALA H H 6.84 . 1 156 . 27 ALA HA H 4.29 . 1 157 . 27 ALA HB H 1.17 . 1 158 . 28 GLY H H 8.12 . 1 159 . 28 GLY HA2 H 3.63 . 1 160 . 28 GLY HA3 H 3.90 . 1 161 . 29 LEU H H 6.77 . 1 162 . 29 LEU HA H 4.65 . 1 163 . 29 LEU HB2 H 1.36 . 2 164 . 29 LEU HB3 H 1.61 . 2 165 . 29 LEU HG H 1.61 . 1 166 . 29 LEU HD1 H 0.74 . 2 167 . 29 LEU HD2 H 0.84 . 2 168 . 30 CYS H H 8.79 . 1 169 . 30 CYS HA H 5.42 . 1 170 . 30 CYS HB2 H 2.53 . 1 171 . 30 CYS HB3 H 3.45 . 1 172 . 31 GLN H H 8.80 . 1 173 . 31 GLN HA H 4.75 . 1 174 . 31 GLN HB2 H 1.51 . 2 175 . 31 GLN HG2 H 1.80 . 2 176 . 31 GLN HG3 H 1.91 . 2 177 . 31 GLN HE21 H 6.95 . 2 178 . 31 GLN HE22 H 7.43 . 2 179 . 32 THR H H 7.99 . 1 180 . 32 THR HA H 4.85 . 1 181 . 32 THR HB H 4.18 . 1 182 . 32 THR HG2 H 0.66 . 1 183 . 33 PHE H H 7.66 . 1 184 . 33 PHE HA H 4.47 . 1 185 . 33 PHE HB2 H 2.87 . 2 186 . 33 PHE HB3 H 3.09 . 2 187 . 33 PHE HD1 H 7.04 . 1 188 . 33 PHE HD2 H 7.04 . 1 189 . 33 PHE HE1 H 7.14 . 1 190 . 33 PHE HE2 H 7.14 . 1 191 . 33 PHE HZ H 7.54 . 1 192 . 34 ALA H H 8.75 . 1 193 . 34 ALA HA H 4.40 . 1 194 . 34 ALA HB H 1.41 . 1 195 . 35 TYR HA H 4.29 . 1 196 . 35 TYR HB2 H 2.96 . 2 197 . 35 TYR HB3 H 3.06 . 2 198 . 35 TYR HD1 H 7.13 . 1 199 . 35 TYR HD2 H 7.13 . 1 200 . 35 TYR HE1 H 6.83 . 1 201 . 35 TYR HE2 H 6.83 . 1 202 . 36 GLY H H 8.28 . 1 203 . 36 GLY HA2 H 3.65 . 2 204 . 36 GLY HA3 H 3.94 . 2 205 . 37 ALA H H 7.75 . 1 206 . 37 ALA HA H 4.40 . 1 207 . 37 ALA HB H 1.26 . 1 208 . 38 CYS H H 8.62 . 1 209 . 38 CYS HA H 4.33 . 1 210 . 38 CYS HB2 H 1.69 . 2 211 . 38 CYS HB3 H 2.63 . 2 212 . 39 ALA H H 7.83 . 1 213 . 39 ALA HA H 4.12 . 1 214 . 39 ALA HB H 1.10 . 1 215 . 40 ALA H H 8.50 . 1 216 . 40 ALA HA H 4.46 . 1 217 . 40 ALA HB H 1.50 . 1 218 . 41 LYS H H 8.32 . 1 219 . 41 LYS HA H 3.90 . 1 220 . 41 LYS HB2 H 1.78 . 2 221 . 41 LYS HB3 H 1.82 . 2 222 . 41 LYS HG2 H 1.40 . 2 223 . 41 LYS HG3 H 1.46 . 2 224 . 41 LYS HD2 H 1.68 . 1 225 . 41 LYS HD3 H 1.68 . 1 226 . 41 LYS HE2 H 2.99 . 1 227 . 41 LYS HE3 H 2.99 . 1 228 . 42 ARG H H 8.01 . 1 229 . 42 ARG HA H 3.81 . 1 230 . 42 ARG HB2 H 0.78 . 2 231 . 42 ARG HB3 H 1.21 . 2 232 . 42 ARG HG2 H 1.38 . 1 233 . 42 ARG HG3 H 1.38 . 1 234 . 42 ARG HD2 H 2.83 . 2 235 . 42 ARG HD3 H 2.89 . 2 236 . 42 ARG HE H 6.97 . 1 237 . 43 ASN H H 7.68 . 1 238 . 43 ASN HA H 5.02 . 1 239 . 43 ASN HB2 H 3.29 . 1 240 . 43 ASN HB3 H 3.36 . 1 241 . 43 ASN HD21 H 7.92 . 2 242 . 43 ASN HD22 H 8.24 . 2 243 . 44 ASN H H 6.24 . 1 244 . 44 ASN HA H 5.16 . 1 245 . 44 ASN HB2 H 2.53 . 2 246 . 44 ASN HB3 H 2.72 . 2 247 . 44 ASN HD21 H 6.61 . 2 248 . 44 ASN HD22 H 7.23 . 2 249 . 45 PHE H H 10.17 . 1 250 . 45 PHE HA H 5.13 . 1 251 . 45 PHE HB2 H 2.77 . 1 252 . 45 PHE HB3 H 3.37 . 1 253 . 45 PHE HD1 H 7.35 . 1 254 . 45 PHE HD2 H 7.35 . 1 255 . 45 PHE HE1 H 7.89 . 1 256 . 45 PHE HE2 H 7.89 . 1 257 . 45 PHE HZ H 7.67 . 1 258 . 46 LYS H H 9.66 . 1 259 . 46 LYS HA H 4.44 . 1 260 . 46 LYS HB2 H 2.05 . 1 261 . 46 LYS HB3 H 2.05 . 1 262 . 46 LYS HG2 H 1.60 . 2 263 . 46 LYS HG3 H 1.63 . 2 264 . 46 LYS HD2 H 1.80 . 1 265 . 46 LYS HD3 H 1.80 . 1 266 . 46 LYS HE2 H 3.08 . 1 267 . 46 LYS HE3 H 3.08 . 1 268 . 46 LYS HZ H 7.62 . 3 269 . 47 SER H H 7.44 . 1 270 . 47 SER HA H 4.68 . 1 271 . 47 SER HB2 H 4.12 . 1 272 . 47 SER HB3 H 3.87 . 1 273 . 48 ALA H H 8.26 . 1 274 . 48 ALA HA H 3.03 . 1 275 . 48 ALA HB H 0.94 . 1 276 . 49 GLU H H 8.33 . 1 277 . 49 GLU HA H 3.91 . 1 278 . 49 GLU HB2 H 1.86 . 2 279 . 49 GLU HB3 H 2.05 . 2 280 . 49 GLU HG2 H 2.40 . 2 281 . 49 GLU HG3 H 2.47 . 2 282 . 50 ASP H H 7.89 . 1 283 . 50 ASP HA H 4.30 . 1 284 . 50 ASP HB2 H 2.84 . 2 285 . 50 ASP HB3 H 3.04 . 2 286 . 51 CYS H H 7.04 . 1 287 . 51 CYS HA H 1.80 . 1 288 . 51 CYS HB2 H 2.78 . 1 289 . 51 CYS HB3 H 3.16 . 1 290 . 52 LEU H H 8.56 . 1 291 . 52 LEU HA H 3.68 . 1 292 . 52 LEU HB2 H 1.48 . 2 293 . 52 LEU HB3 H 1.66 . 2 294 . 52 LEU HG H 1.66 . 1 295 . 52 LEU HD1 H 0.83 . 2 296 . 52 LEU HD2 H 0.87 . 2 297 . 53 ARG H H 8.33 . 1 298 . 53 ARG HA H 3.95 . 1 299 . 53 ARG HB2 H 1.84 . 2 300 . 53 ARG HB3 H 1.89 . 2 301 . 53 ARG HG2 H 1.63 . 2 302 . 53 ARG HG3 H 1.74 . 2 303 . 53 ARG HD2 H 3.19 . 1 304 . 53 ARG HD3 H 3.19 . 1 305 . 53 ARG HE H 7.17 . 1 306 . 54 THR H H 7.40 . 1 307 . 54 THR HA H 4.09 . 1 308 . 54 THR HB H 3.98 . 1 309 . 54 THR HG2 H 1.62 . 1 310 . 55 CYS H H 8.26 . 1 311 . 55 CYS HA H 4.67 . 1 312 . 55 CYS HB2 H 2.04 . 2 313 . 55 CYS HB3 H 2.21 . 2 314 . 56 GLY H H 7.93 . 1 315 . 56 GLY HA2 H 3.79 . 2 316 . 56 GLY HA3 H 3.88 . 2 317 . 57 GLY H H 8.22 . 1 318 . 57 GLY HA2 H 3.92 . 1 319 . 57 GLY HA3 H 3.92 . 1 320 . 58 ALA H H 8.14 . 1 321 . 58 ALA HA H 4.20 . 1 322 . 58 ALA HB H 1.36 . 1 stop_ save_ ######################## # Coupling constants # ######################## save_coupling_constant_set_1 _Saveframe_category coupling_constants _Details . loop_ _Experiment_label '2D TOCSY' '2D NOESY' DQF-COSY stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_cond_1 _Spectrometer_frequency_1H 500 _Mol_system_component_name 'pancreatic trypsin inhibitor' _Text_data_format . _Text_data . loop_ _Coupling_constant_ID _Coupling_constant_code _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_name _Coupling_constant_value _Coupling_constant_min_value _Coupling_constant_max_value _Coupling_constant_value_error 1 3JHNHA 3 ASP H 3 ASP HA 2.8 . . 1.0 2 3JHNHA 5 CYS H 5 CYS HA 4.0 . . 1.0 3 3JHNHA 6 LEU H 6 LEU HA 7.8 . . 1.0 4 3JHNHA 7 GLU H 7 GLU HA 5.7 . . 1.0 5 3JHNHA 10 TYR H 10 TYR HA 7.5 . . 1.0 6 3JHNHA 13 ALA H 13 ALA HA 7.2 . . 1.0 7 3JHNHA 14 CYS H 14 CYS HA 6.2 . . 1.0 8 3JHNHA 15 ARG H 15 ARG HA 7.3 . . 1.0 9 3JHNHA 16 ALA H 16 ALA HA 6.1 . . 1.0 10 3JHNHA 17 ALA H 17 ALA HA 7.0 . . 1.0 11 3JHNHA 18 ALA H 18 ALA HA 5.5 . . 1.0 12 3JHNHA 19 ALA H 19 ALA HA 6.3 . . 1.0 13 3JHNHA 20 ARG H 20 ARG HA 9.0 . . 1.0 14 3JHNHA 21 TYR H 21 TYR HA 10.2 . . 1.0 15 3JHNHA 22 PHE H 22 PHE HA 8.7 . . 1.0 16 3JHNHA 23 TYR H 23 TYR HA 6.9 . . 1.0 17 3JHNHA 25 ALA H 25 ALA HA 3.8 . . 1.0 18 3JHNHA 27 ALA H 27 ALA HA 8.2 . . 1.0 19 3JHNHA 30 CYS H 30 CYS HA 9.0 . . 1.0 20 3JHNHA 31 GLN H 31 GLN HA 9.7 . . 1.0 21 3JHNHA 32 THR H 32 THR HA 5.8 . . 1.0 22 3JHNHA 34 ALA H 34 ALA HA 6.0 . . 1.0 23 3JHNHA 37 ALA H 37 ALA HA 4.7 . . 1.0 24 3JHNHA 38 CYS H 38 CYS HA 7.3 . . 1.0 25 3JHNHA 39 ALA H 39 ALA HA 5.4 . . 1.0 26 3JHNHA 41 LYS H 41 LYS HA 4.3 . . 1.0 27 3JHNHA 42 ARG H 42 ARG HA 7.6 . . 1.0 28 3JHNHA 43 ASN H 43 ASN HA 7.6 . . 1.0 29 3JHNHA 44 ASN H 44 ASN HA 7.7 . . 1.0 30 3JHNHA 45 PHE H 45 PHE HA 10.1 . . 1.0 31 3JHNHA 46 LYS H 46 LYS HA 4.4 . . 1.0 32 3JHNHA 48 ALA H 48 ALA HA 3.8 . . 1.0 33 3JHNHA 49 GLU H 49 GLU HA 4.3 . . 1.0 34 3JHNHA 50 ASP H 50 ASP HA 4.6 . . 1.0 35 3JHNHA 51 CYS H 51 CYS HA 4.8 . . 1.0 36 3JHNHA 52 LEU H 52 LEU HA 3.7 . . 1.0 37 3JHNHA 53 ARG H 53 ARG HA 4.5 . . 1.0 38 3JHNHA 54 THR H 54 THR HA 6.6 . . 1.0 39 3JHNHA 58 ALA H 58 ALA HA 6.3 . . 1.0 stop_ save_