data_4873 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Partially folded conformation of the (30-51) intermediate in the disulphide folding pathway of bovine pancreatic trypsin inhibitor. 1H and 15N resonance assignments and determination of backbone dynamics from 15N relaxation measurements ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 "van Mierlo" Carlo P.M. . 2 Darby Nigel J. . 3 Keeler James . . 4 Neuhaus David . . 5 Creighton Thomas E. . stop_ _BMRB_accession_number 4873 _BMRB_flat_file_name bmr4873.str _Entry_type new _Submission_date 2000-10-23 _Accession_date 2000-10-23 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count '1H chemical shifts' 343 '15N chemical shifts' 54 stop_ loop_ _Related_BMRB_accession_number _Relationship 2169 "(5-55)Ser BPTI folding intermediate" 4855 "(14-38, 30-51)Ser BPTI folding intermediate" 4868 "BPTI-R52" 4875 "(30-51, 5-14)Ser BPTI folding intermediate" 4877 "(30-51, 5-38)Ser BPTI folding intermediate" stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Partially folded conformation of the (30-51) intermediate in the disulphide folding pathway of bovine pancreatic trypsin inhibitor. 1H and 15N resonance assignments and determination of backbone dynamics from 15N relaxation measurements. ; _Citation_status published _Citation_type journal _MEDLINE_UI_code 93188004 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 "van Mierlo" Carlo P.M. . 2 Darby Nigel J. . 3 Keeler James . . 4 Neuhaus David . . 5 Creighton Thomas E. . stop_ _Journal_abbreviation "J. Mol. Biol." _Journal_volume 229 _Page_first 1125 _Page_last 1146 _Year 1993 loop_ _Keyword NMR "disulfide bonds" "bovine pancreatic trypsin inhibitor (BPTI)" "protein folding" "folding intermediate" stop_ save_ ################################## # Molecular system description # ################################## save_system_(30-51)Ser_BPTI_folding_intermediate _Saveframe_category molecular_system _Mol_system_name "(30-51)Ser BPTI folding intermediate" _Abbreviation_common "(30-51)Ser BPTI folding intermediate" loop_ _Mol_system_component_name _Mol_label "(30-51) BPTI" $(30-51)_BPTI stop_ _System_physical_state denatured _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Biological_function ; The species discussed is a stable mimick of the (30-51) folding intermediate in BPTI folding ; stop_ save_ ######################## # Monomeric polymers # ######################## save_(30-51)_BPTI _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "(30-51)Ser BPTI folding intermediate" _Name_variant . _Abbreviation_common "(30-51) BPTI" _Mol_thiol_state 'all disulfide bound' ############################## # Polymer residue sequence # ############################## _Residue_count 59 _Mol_residue_sequence ; MRPDFSLEPPYTGPSKARII RYFYNAKAGLCQTFVYGGSR AKRNNFKSAEDCRRTSGGA ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ARG 3 PRO 4 ASP 5 PHE 6 SER 7 LEU 8 GLU 9 PRO 10 PRO 11 TYR 12 THR 13 GLY 14 PRO 15 SER 16 LYS 17 ALA 18 ARG 19 ILE 20 ILE 21 ARG 22 TYR 23 PHE 24 TYR 25 ASN 26 ALA 27 LYS 28 ALA 29 GLY 30 LEU 31 CYS 32 GLN 33 THR 34 PHE 35 VAL 36 TYR 37 GLY 38 GLY 39 SER 40 ARG 41 ALA 42 LYS 43 ARG 44 ASN 45 ASN 46 PHE 47 LYS 48 SER 49 ALA 50 GLU 51 ASP 52 CYS 53 ARG 54 ARG 55 THR 56 SER 57 GLY 58 GLY 59 ALA stop_ _Sequence_homology_query_date 2009-06-13 _Sequence_homology_query_revised_last_date 2007-03-08 save_ ######################################## # Molecular bond linkage definitions # ######################################## save_crosslink_bonds _Saveframe_category crosslink_bonds loop_ _Bond_order _Bond_type _Atom_one_mol_system_component_name _Atom_one_residue_seq_code _Atom_one_residue_label _Atom_one_atom_name _Atom_two_mol_system_component_name _Atom_two_residue_seq_code _Atom_two_residue_label _Atom_two_atom_name single disulfide "(30-51) BPTI" 30 CYS SG "(30-51) BPTI" 51 CYS SG stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $(30-51)_BPTI 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_type _Vector_name _Details $(30-51)_BPTI 'recombinant technology' "E. coli" Escherichia coli . plasmid pET-3a ; See van mierlo et al., J. Mol. Biol. (1993) 229, 1125-1146. ; stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details ; 15N-enriched (30-51), Met residue at position -1. no salt was added to the sample, pH 4.6, the pH was adjusted by adding small amounts of NaOH ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $(30-51)_BPTI . mM 2 3 "[U-15N]" H2O 90 % . . . D2O 10 % . . . stop_ save_ ############################ # Computer software used # ############################ save_UXNMR _Saveframe_category software _Name UXNMR loop_ _Task "data acquisition" "data processing" stop_ _Details "UXNMR versions as available in 1990 - 1992 were used." save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AMX _Field_strength 500 save_ ############################# # NMR applied experiments # ############################# save_NMR_applied_experiment _Saveframe_category NMR_applied_experiment _Experiment_name ; DQF-COSY DQ NOESY ROESY TOCSY HMQC HSQC 2D HMQC-NOESY 2D HSQC-NOESY 2D HSQC-TOCSY {1H-15N} NOE 15N T1 15N T2 ; save_ ####################### # Sample conditions # ####################### save_Ex-cond_1 _Saveframe_category sample_conditions loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 4.6 0.1 pH temperature 271 0.5 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details ; 15N Chemical shifts are referenced to external 15NH4Cl (2.9 M in 1 M HCl) at 20 C, 24.93 ppm relative to NH3 (Levy and Lichter (1979) Nitrogen-15 nuclear magnetic resonance spectroscopy. John Wiley & Sons, New York). ; 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 TSP H 1 'methyl protons' ppm 0.00 internal direct . . . 1.0 NH4Cl N 15 'ammonia nitrogen' ppm ? external ? . . . . stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique (geminal atoms and geminal methyl # # groups with identical chemical shifts # # are assumed to be assigned to # # stereospecific atoms) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 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) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_CSR_1 _Saveframe_category assigned_chemical_shifts _Details ; Several exchange phenomena were observed by NMR (see J. Mol. Biol. (1993) 229, 1125 - 1146). The HE1, HE2 and HZ protons of Phe5 resonate between 7.24 - 7.40 ppm, it was not possible to determine their exact resonance position due to near coincidence of these resonances. ; loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $CSR_1 _Mol_system_component_name "(30-51) BPTI" loop_ _Atom_shift_assign_ID _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 1 MET HA H 4.15 0.01 1 2 1 MET HB2 H 2.15 0.01 1 3 1 MET HB3 H 2.15 0.01 1 4 1 MET HG2 H 2.60 0.01 1 5 1 MET HG3 H 2.60 0.01 1 6 1 MET HE H 2.08 0.01 1 7 2 ARG H H 8.94 0.01 1 8 2 ARG HA H 4.68 0.01 1 9 2 ARG HB2 H 1.80 0.01 2 10 2 ARG HB3 H 1.89 0.01 2 11 2 ARG HG2 H 1.72 0.01 1 12 2 ARG HG3 H 1.72 0.01 1 13 2 ARG HD2 H 3.22 0.01 1 14 2 ARG HD3 H 3.22 0.01 1 15 2 ARG HE H 7.37 0.01 1 16 2 ARG N N 126.8 0.2 1 17 3 PRO HA H 4.37 0.01 1 18 3 PRO HB2 H 1.73 0.01 2 19 3 PRO HB3 H 2.20 0.01 2 20 3 PRO HG2 H 2.00 0.01 1 21 3 PRO HG3 H 2.00 0.01 1 22 3 PRO HD2 H 3.66 0.01 2 23 3 PRO HD3 H 3.87 0.01 2 24 4 ASP H H 8.50 0.01 1 25 4 ASP HA H 4.53 0.01 1 26 4 ASP HB2 H 2.65 0.01 1 27 4 ASP HB3 H 2.65 0.01 1 28 4 ASP N N 121.3 0.2 1 29 5 PHE H H 8.32 0.01 1 30 5 PHE HA H 4.62 0.01 1 31 5 PHE HB2 H 3.04 0.01 2 32 5 PHE HB3 H 3.20 0.01 2 33 5 PHE HD1 H 7.26 0.01 1 34 5 PHE HD2 H 7.26 0.01 1 35 5 PHE HE1 H 7.24 0.01 3 36 5 PHE HE2 H 7.40 0.01 3 37 5 PHE HZ H 7.24 0.01 3 38 5 PHE N N 122.6 0.2 1 39 6 SER H H 8.34 0.01 1 40 6 SER HA H 4.35 0.01 1 41 6 SER HB2 H 3.81 0.01 2 42 6 SER HB3 H 3.84 0.01 2 43 6 SER N N 118.8 0.2 1 44 7 LEU H H 8.31 0.01 1 45 7 LEU HA H 4.37 0.01 1 46 7 LEU HB2 H 1.64 0.01 1 47 7 LEU HB3 H 1.64 0.01 1 48 7 LEU HG H 1.64 0.01 1 49 7 LEU HD1 H 0.90 0.01 2 50 7 LEU HD2 H 0.96 0.01 2 51 7 LEU N N 125.2 0.2 1 52 8 GLU H H 8.37 0.01 1 53 8 GLU HA H 4.59 0.01 1 54 8 GLU HB2 H 1.90 0.01 2 55 8 GLU HB3 H 2.06 0.01 2 56 8 GLU HG2 H 2.38 0.01 1 57 8 GLU HG3 H 2.38 0.01 1 58 8 GLU N N 124.4 0.2 1 59 9 PRO HA H 4.71 0.01 1 60 9 PRO HB2 H 1.89 0.01 2 61 9 PRO HB3 H 2.36 0.01 2 62 9 PRO HG2 H 2.05 0.01 1 63 9 PRO HG3 H 2.05 0.01 1 64 9 PRO HD2 H 3.69 0.01 2 65 9 PRO HD3 H 3.84 0.01 2 66 10 PRO HA H 4.42 0.01 1 67 10 PRO HB2 H 1.83 0.01 4 68 10 PRO HB3 H 2.26 0.01 2 69 10 PRO HG2 H 1.98 0.01 4 70 10 PRO HG3 H 1.98 0.01 4 71 10 PRO HD2 H 3.64 0.01 2 72 10 PRO HD3 H 3.84 0.01 2 73 11 TYR H H 8.63 0.01 1 74 11 TYR HA H 4.63 0.01 1 75 11 TYR HB2 H 2.90 0.01 2 76 11 TYR HB3 H 3.15 0.01 2 77 11 TYR HD1 H 7.15 0.01 1 78 11 TYR HD2 H 7.15 0.01 1 79 11 TYR HE1 H 6.79 0.01 1 80 11 TYR HE2 H 6.79 0.01 1 81 11 TYR N N 123.5 0.2 1 82 12 THR H H 8.33 0.01 1 83 12 THR HA H 4.34 0.01 1 84 12 THR HB H 4.25 0.01 1 85 12 THR HG2 H 1.11 0.01 1 86 12 THR N N 119.9 0.2 1 87 13 GLY H H 6.78 0.01 1 88 13 GLY HA2 H 3.98 0.01 1 89 13 GLY HA3 H 3.98 0.01 1 90 13 GLY N N 111.0 0.2 1 91 14 PRO HA H 4.50 0.01 1 92 14 PRO HB2 H 1.96 0.01 4 93 14 PRO HB3 H 2.33 0.01 2 94 14 PRO HG2 H 2.05 0.01 2 95 14 PRO HD2 H 3.64 0.01 1 96 14 PRO HD3 H 3.64 0.01 1 97 15 SER H H 8.71 0.01 1 98 15 SER HA H 4.41 0.01 1 99 15 SER HB2 H 3.87 0.01 2 100 15 SER HB3 H 3.93 0.01 2 101 15 SER N N 118.4 0.2 1 102 16 LYS H H 8.62 0.01 1 103 16 LYS HA H 4.31 0.01 1 104 16 LYS HB2 H 1.87 0.01 4 105 16 LYS HG2 H 1.40 0.01 4 106 16 LYS HG3 H 1.46 0.01 4 107 16 LYS HD2 H 1.64 0.01 2 108 16 LYS HE2 H 2.91 0.01 2 109 16 LYS HZ H 7.59 0.01 1 110 16 LYS N N 125.4 0.2 1 111 17 ALA H H 8.29 0.01 1 112 17 ALA HA H 4.26 0.01 1 113 17 ALA HB H 1.36 0.01 1 114 17 ALA N N 125.9 0.2 1 115 18 ARG H H 8.42 0.01 1 116 18 ARG HA H 4.32 0.01 1 117 18 ARG HB2 H 1.73 0.01 9 118 18 ARG HB3 H 1.73 0.01 1 119 18 ARG HG2 H 1.52 0.01 2 120 18 ARG HG3 H 1.64 0.01 2 121 18 ARG HD2 H 3.14 0.01 1 122 18 ARG HD3 H 3.14 0.01 1 123 18 ARG HE H 7.28 0.01 1 124 18 ARG N N 122.7 0.2 1 125 19 ILE H H 8.66 0.01 1 126 19 ILE HA H 4.20 0.01 1 127 19 ILE HB H 1.94 0.01 1 128 19 ILE HG12 H 1.18 0.01 2 129 19 ILE HG13 H 1.51 0.01 2 130 19 ILE HG2 H 0.87 0.01 1 131 19 ILE HD1 H 0.87 0.01 1 132 19 ILE N N 126.6 0.2 1 133 20 ILE H H 8.58 0.01 1 134 20 ILE HA H 4.47 0.01 1 135 20 ILE HB H 1.85 0.01 1 136 20 ILE HG12 H 1.28 0.01 2 137 20 ILE HG13 H 1.44 0.01 2 138 20 ILE HG2 H 0.70 0.01 1 139 20 ILE HD1 H 0.72 0.01 1 140 20 ILE N N 128.9 0.2 1 141 21 ARG H H 8.36 0.01 1 142 21 ARG HA H 4.71 0.01 1 143 21 ARG HB2 H 1.01 0.01 2 144 21 ARG HB3 H 1.94 0.01 9 145 21 ARG HG2 H 1.33 0.01 4 146 21 ARG HD2 H 2.90 0.01 9 147 21 ARG HD3 H 3.05 0.01 9 148 21 ARG N N 128.6 0.2 1 149 22 TYR H H 8.99 0.01 1 150 22 TYR HA H 5.71 0.01 1 151 22 TYR HB2 H 2.71 0.01 1 152 22 TYR HB3 H 2.71 0.01 1 153 22 TYR HD1 H 6.70 0.01 1 154 22 TYR HD2 H 6.70 0.01 1 155 22 TYR HE1 H 6.76 0.01 1 156 22 TYR HE2 H 6.76 0.01 1 157 22 TYR N N 116.9 0.2 1 158 23 PHE H H 9.89 0.01 1 159 23 PHE HA H 5.38 0.01 1 160 23 PHE HB2 H 3.02 0.01 2 161 23 PHE HB3 H 3.14 0.01 2 162 23 PHE HD1 H 7.14 0.01 1 163 23 PHE HD2 H 7.14 0.01 1 164 23 PHE HE1 H 7.27 0.01 1 165 23 PHE HE2 H 7.27 0.01 1 166 23 PHE HZ H 7.34 0.01 1 167 23 PHE N N 121.5 0.2 1 168 24 TYR H H 9.80 0.01 1 169 24 TYR HA H 4.45 0.01 1 170 24 TYR HB2 H 2.96 0.01 2 171 24 TYR HB3 H 3.02 0.01 2 172 24 TYR HD1 H 7.00 0.01 1 173 24 TYR HD2 H 7.00 0.01 1 174 24 TYR HE1 H 6.54 0.01 1 175 24 TYR HE2 H 6.54 0.01 1 176 24 TYR N N 124.5 0.2 1 177 25 ASN H H 8.01 0.01 1 178 25 ASN HA H 4.52 0.01 1 179 25 ASN HB2 H 2.24 0.01 2 180 25 ASN HB3 H 2.90 0.01 2 181 25 ASN HD21 H 7.30 0.01 9 182 25 ASN HD22 H 8.13 0.01 9 183 25 ASN N N 129.3 0.2 1 184 26 ALA H H 8.50 0.01 1 185 26 ALA HA H 3.63 0.01 1 186 26 ALA HB H 1.52 0.01 1 187 26 ALA N N 128.8 0.2 1 188 27 LYS H H 8.02 0.01 1 189 27 LYS HA H 4.08 0.01 1 190 27 LYS HB2 H 1.90 0.01 1 191 27 LYS HB3 H 1.90 0.01 1 192 27 LYS HG2 H 1.43 0.01 2 193 27 LYS HG3 H 1.51 0.01 2 194 27 LYS HD2 H 1.72 0.01 2 195 27 LYS HE2 H 3.00 0.01 2 196 27 LYS HZ H 7.64 0.01 1 197 27 LYS N N 119.3 0.2 1 198 28 ALA H H 6.93 0.01 1 199 28 ALA HA H 4.28 0.01 1 200 28 ALA HB H 1.21 0.01 1 201 28 ALA N N 119.9 0.2 1 202 29 GLY H H 8.19 0.01 1 203 29 GLY HA2 H 3.77 0.01 2 204 29 GLY HA3 H 3.96 0.01 2 205 29 GLY N N 109.4 0.01 1 206 30 LEU H H 6.94 0.01 1 207 30 LEU HA H 4.91 0.01 1 208 30 LEU HB2 H 1.38 0.01 2 209 30 LEU HB3 H 1.58 0.01 2 210 30 LEU HG H 1.46 0.01 1 211 30 LEU HD1 H 0.84 0.01 2 212 30 LEU HD2 H 0.89 0.01 2 213 30 LEU N N 117.4 0.2 1 214 31 CYS H H 9.25 0.01 1 215 31 CYS HA H 5.40 0.01 1 216 31 CYS HB2 H 2.60 0.01 2 217 31 CYS HB3 H 3.57 0.01 2 218 31 CYS N N 122.0 0.2 1 219 32 GLN H H 9.23 0.01 1 220 32 GLN HA H 4.89 0.01 1 221 32 GLN HB2 H 1.74 0.01 2 222 32 GLN HB3 H 2.10 0.01 2 223 32 GLN HG2 H 2.06 0.01 2 224 32 GLN HG3 H 2.26 0.01 2 225 32 GLN HE21 H 7.25 0.01 9 226 32 GLN HE22 H 7.63 0.01 9 227 32 GLN N N 125.7 0.2 1 228 33 THR H H 8.33 0.01 1 229 33 THR HA H 4.85 0.01 1 230 33 THR HB H 4.03 0.01 1 231 33 THR HG2 H 0.78 0.01 1 232 33 THR N N 112.2 0.2 1 233 34 PHE H H 8.91 0.01 1 234 34 PHE HA H 4.83 0.01 1 235 34 PHE HB2 H 2.94 0.01 2 236 34 PHE HB3 H 3.14 0.01 2 237 34 PHE HD1 H 7.11 0.01 1 238 34 PHE HD2 H 7.11 0.01 1 239 34 PHE HE1 H 7.28 0.01 9 240 34 PHE HE2 H 7.28 0.01 9 241 34 PHE HZ H 7.17 0.01 9 242 34 PHE N N 119.8 0.2 1 243 35 VAL H H 8.49 0.01 1 244 35 VAL HA H 4.04 0.01 1 245 35 VAL HB H 1.90 0.01 1 246 35 VAL HG1 H 0.81 0.01 2 247 35 VAL HG2 H 0.85 0.01 2 248 35 VAL N N 122.3 0.01 1 249 36 TYR H H 8.78 0.01 1 250 36 TYR HA H 4.39 0.01 1 251 36 TYR HB2 H 2.48 0.01 2 252 36 TYR HB3 H 2.76 0.01 2 253 36 TYR HD1 H 7.09 0.01 1 254 36 TYR HD2 H 7.09 0.01 1 255 36 TYR HE1 H 6.88 0.01 1 256 36 TYR HE2 H 6.88 0.01 1 257 36 TYR N N 130.6 0.2 1 258 37 GLY H H 8.38 0.01 1 259 37 GLY HA2 H 3.84 0.01 2 260 37 GLY N N 116.3 0.2 1 261 38 GLY H H 7.21 0.01 1 262 38 GLY HA2 H 3.75 0.01 2 263 38 GLY HA3 H 3.94 0.01 2 264 38 GLY N N 108.7 0.2 1 265 39 SER H H 8.29 0.01 1 266 39 SER HA H 4.40 0.01 1 267 39 SER HB2 H 3.85 0.01 2 268 39 SER HB3 H 3.92 0.01 2 269 39 SER N N 116.8 0.2 1 270 40 ARG H H 8.52 0.01 1 271 40 ARG HA H 4.28 0.01 1 272 40 ARG HB2 H 1.75 0.01 9 273 40 ARG HB3 H 1.83 0.01 9 274 40 ARG HG2 H 1.62 0.01 4 275 40 ARG HD2 H 3.07 0.01 9 276 40 ARG HD3 H 3.07 0.01 9 277 40 ARG HE H 7.17 0.01 9 278 40 ARG N N 124.2 0.2 1 279 41 ALA H H 8.28 0.01 1 280 41 ALA HA H 4.24 0.01 1 281 41 ALA HB H 1.34 0.01 1 282 41 ALA N N 125.9 0.2 1 283 42 LYS H H 8.32 0.01 1 284 42 LYS HA H 4.27 0.01 1 285 42 LYS HB2 H 1.70 0.01 9 286 42 LYS HB3 H 1.84 0.01 9 287 42 LYS N N 121.9 0.2 1 288 43 ARG H H 8.13 0.01 1 289 43 ARG HA H 4.27 0.01 1 290 43 ARG HB2 H 1.82 0.01 9 291 43 ARG HG2 H 1.57 0.01 9 292 43 ARG HD2 H 2.84 0.01 9 293 43 ARG HD3 H 2.94 0.01 9 294 43 ARG HE H 7.20 0.01 9 295 43 ARG N N 121.5 0.2 1 296 44 ASN H H 8.65 0.01 1 297 44 ASN HA H 4.63 0.01 1 298 44 ASN HB2 H 2.73 0.01 2 299 44 ASN HB3 H 2.89 0.01 2 300 44 ASN HD21 H 7.46 0.01 9 301 44 ASN HD22 H 7.94 0.01 9 302 44 ASN N N 121.4 0.2 1 303 45 ASN H H 7.82 0.01 1 304 45 ASN HA H 5.31 0.01 1 305 45 ASN HB2 H 2.72 0.01 1 306 45 ASN HB3 H 2.72 0.01 1 307 45 ASN HD21 H 6.53 0.01 9 308 45 ASN HD22 H 7.70 0.01 9 309 45 ASN N N 119.2 0.2 1 310 46 PHE H H 9.48 0.01 1 311 46 PHE HA H 5.05 0.01 1 312 46 PHE HB2 H 2.72 0.01 2 313 46 PHE HB3 H 3.40 0.01 2 314 46 PHE HD1 H 7.23 0.01 1 315 46 PHE HD2 H 7.23 0.01 1 316 46 PHE HE1 H 7.49 0.01 1 317 46 PHE HE2 H 7.49 0.01 1 318 46 PHE HZ H 7.36 0.01 1 319 46 PHE N N 119.5 0.2 1 320 47 LYS H H 9.94 0.01 1 321 47 LYS HA H 4.39 0.01 1 322 47 LYS HB2 H 2.03 0.01 1 323 47 LYS HB3 H 2.03 0.01 1 324 47 LYS HG2 H 1.55 0.01 9 325 47 LYS HG3 H 1.55 0.01 1 326 47 LYS HD2 H 1.78 0.01 9 327 47 LYS HE2 H 3.03 0.01 9 328 47 LYS HZ H 7.71 0.01 9 329 47 LYS N N 121.8 0.2 1 330 48 SER H H 7.50 0.01 1 331 48 SER HA H 4.59 0.01 1 332 48 SER HB2 H 3.83 0.01 2 333 48 SER HB3 H 4.11 0.01 2 334 48 SER N N 110.9 0.2 1 335 49 ALA H H 8.36 0.01 1 336 49 ALA HA H 3.00 0.01 1 337 49 ALA HB H 1.01 0.01 1 338 49 ALA N N 127.1 0.2 1 339 50 GLU H H 8.74 0.01 1 340 50 GLU HA H 3.84 0.01 1 341 50 GLU HB2 H 1.82 0.01 2 342 50 GLU HB3 H 2.00 0.01 2 343 50 GLU HG2 H 2.21 0.01 2 344 50 GLU HG3 H 2.35 0.01 2 345 50 GLU N N 119.4 0.2 1 346 51 ASP H H 7.90 0.01 1 347 51 ASP HA H 4.28 0.01 1 348 51 ASP HB2 H 2.72 0.01 2 349 51 ASP HB3 H 2.85 0.01 2 350 51 ASP N N 121.3 0.2 1 351 52 CYS H H 7.12 0.01 1 352 52 CYS HA H 1.85 0.01 1 353 52 CYS HB2 H 2.69 0.01 2 354 52 CYS HB3 H 3.09 0.01 2 355 52 CYS N N 120.1 0.2 1 356 53 ARG H H 8.69 0.01 1 357 53 ARG HA H 3.75 0.01 1 358 53 ARG HB2 H 1.65 0.01 2 359 53 ARG HB3 H 1.74 0.01 2 360 53 ARG HG2 H 1.50 0.01 2 361 53 ARG HD2 H 3.06 0.01 2 362 53 ARG HD3 H 3.11 0.01 2 363 53 ARG HE H 7.44 0.01 1 364 53 ARG HH11 H 6.72 0.01 9 365 53 ARG HH12 H 6.95 0.01 9 366 53 ARG N N 125.6 0.2 1 367 54 ARG H H 8.08 0.01 1 368 54 ARG HA H 3.95 0.01 1 369 54 ARG HB2 H 1.82 0.01 2 370 54 ARG HB3 H 1.87 0.01 2 371 54 ARG HG2 H 1.58 0.01 2 372 54 ARG HG3 H 1.70 0.01 2 373 54 ARG HD2 H 3.20 0.01 2 374 54 ARG HE H 7.37 0.01 1 375 54 ARG N N 120.3 0.2 1 376 55 THR H H 7.49 0.01 1 377 55 THR HA H 4.13 0.01 1 378 55 THR HB H 3.97 0.01 1 379 55 THR HG2 H 1.37 0.01 1 380 55 THR N N 113.8 0.2 1 381 56 SER H H 7.89 0.01 1 382 56 SER HA H 4.08 0.01 1 383 56 SER HB2 H 3.12 0.01 1 384 56 SER HB3 H 3.12 0.01 1 385 56 SER N N 116.7 0.2 1 386 57 GLY H H 7.90 0.01 1 387 57 GLY HA2 H 3.80 0.01 2 388 57 GLY HA3 H 3.97 0.01 2 389 57 GLY N N 111.0 0.2 1 390 58 GLY H H 8.13 0.01 1 391 58 GLY HA2 H 3.83 0.01 2 392 58 GLY HA3 H 3.97 0.01 2 393 58 GLY N N 109.5 0.2 1 394 59 ALA H H 7.96 0.01 1 395 59 ALA HA H 4.18 0.01 1 396 59 ALA HB H 1.38 0.01 1 397 59 ALA N N 129.6 0.2 1 stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _MEDLINE_UI_code 1960732 _Citation_full ; van Mierlo CP, Darby NJ, Neuhaus D, Creighton TE. Two-dimensional 1H nuclear magnetic resonance study of the (5-55) single-disulphide folding intermediate of bovine pancreatic trypsin inhibitor. J Mol Biol. 1991 Nov 20;222(2):373-90 ; save_ save_ref_2 _Saveframe_category citation _MEDLINE_UI_code 1704858 _Citation_full ; Darby NJ, van Mierlo CP, Creighton TE. The 5-55 single-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor. FEBS Lett. 1991 Feb 11;279(1):61-4. ; save_ save_ref_3 _Saveframe_category citation _MEDLINE_UI_code 1960731 _Citation_full ; van Mierlo CP, Darby NJ, Neuhaus D, Creighton TE. (14-38, 30-51) double-disulphide intermediate in folding of bovine pancreatic trypsin inhibitor: a two-dimensional 1H nuclear magnetic resonance study. J Mol Biol. 1991 Nov 20;222(2):353-71. ; save_ save_ref_4 _Saveframe_category citation _MEDLINE_UI_code 1373775 _Citation_full ; Darby NJ, van Mierlo CP, Scott GH, Neuhaus D, Creighton TE. Kinetic roles and conformational properties of the non-native two-disulphide intermediates in the refolding of bovine pancreatic trypsin inhibitor. J Mol Biol. 1992 Apr 20;224(4):905-11. ; save_ save_ref_5 _Saveframe_category citation _MEDLINE_UI_code 1379719 _Citation_full ; van Mierlo CP, Darby NJ, Creighton TE. The partially folded conformation of the Cys-30 Cys-51 intermediate in the disulfide folding pathway of bovine pancreatic trypsin inhibitor. Proc Natl Acad Sci U S A. 1992 Aug 1;89(15):6775-9. ; save_ save_ref_6 _Saveframe_category citation _MEDLINE_UI_code 7680380 _Citation_full ; van Mierlo CP, Darby NJ, Keeler J, Neuhaus D, Creighton TE. Partially folded conformation of the (30-51) intermediate in the disulphide folding pathway of bovine pancreatic trypsin inhibitor. 1H and 15N resonance assignments and determination of backbone dynamics from 15N relaxation measurements. J Mol Biol. 1993 Feb 20;229(4):1125-46. ; save_ save_ref_7 _Saveframe_category citation _MEDLINE_UI_code 7507172 _Citation_full ; van Mierlo CP, Kemmink J, Neuhaus D, Darby NJ, Creighton TE. 1H NMR analysis of the partly-folded non-native two-disulphide intermediates (30-51,5-14) and (30-51,5-38) in the folding pathway of bovine pancreatic trypsin inhibitor. J Mol Biol. 1994 Jan 21;235(3):1044-61. ; save_