data_4877 #Corrected using PDB structure: 2FI4I # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a HA chemical shift difference (obs*-pred) greater than 0.7ppm: #NUM AA CS Observed* Predicted # 9 P HA 4.39 3.62 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.02 N/A N/A N/A N/A -0.24 # #bmr4877.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr4877.str file): #HA CA CB CO N HN #N/A N/A N/A N/A N/A N/A # #The 95% confidence intervals for the above recommended offsets are: # HA CA CB CO N HN #+/-0.04 N/A N/A N/A N/A +/-0.12 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.896 N/A N/A N/A N/A 0.723 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.157 N/A N/A N/A N/A 0.422 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 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 ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 "van Mierlo" Carlo P.M. . 2 Kemmink Johan . . 3 Neuhaus David . . 4 Darby Nigel J. . 5 Creighton Thomas E. . stop_ _BMRB_accession_number 4877 _BMRB_flat_file_name bmr4877.str _Entry_type new _Submission_date 2000-10-24 _Accession_date 2000-10-24 _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' 337 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2002-08-12 update BMRB "Modify the saveframe name." 2000-11-29 original author "Original release." 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" 4873 "(30-51)Ser BPTI folding intermediate" 4875 "(30-51, 5-14)Ser BPTI folding intermediate" stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; 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 ; _Citation_status published _Citation_type journal _MEDLINE_UI_code 1960732 _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 "van Mierlo" Carlo P.M. . 2 Kemmink Johan . . 3 Neuhaus David . . 4 Darby Nigel J. . 5 Creighton Thomas E. . stop_ _Journal_abbreviation "J. Mol. Biol." _Journal_volume 235 _Page_first 1044 _Page_last 1061 _Year 1994 loop_ _Keyword "NMR" "disulphide bonds" "bovine pancreatic trypsin inhibitor (BPTI)" "protein folding" "folding intermediate" stop_ save_ ################################## # Molecular system description # ################################## save_(30-51_5-38)Ser_BPTI_folding_intermediate _Saveframe_category molecular_system _Mol_system_name "(30-51, 5-38)Ser BPTI folding intermediate" _Abbreviation_common "(30-51, 5-38)Ser BPTI folding intermediate" _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label "(30-51, 5-38)Ser BPTI" $(30-51_5-38)_BPTI stop_ _System_physical_state native _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, 5-38) folding intermediate in BPTI folding ; stop_ save_ ######################## # Monomeric polymers # ######################## save_(30-51_5-38)_BPTI _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common "(30-51, 5-38)Ser BPTI folding intermediate" _Name_variant . _Abbreviation_common "(30-51, 5-38) BPTI" _Mol_thiol_state 'all disulfide bound' ############################## # Polymer residue sequence # ############################## _Residue_count 58 _Mol_residue_sequence ; RPDFCLEPPYTGPSKARIIR YFYNAKAGLCQTFVYGGCRA KRNNFKSAEDCRRTSGGA ; 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 SER 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 GLY 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 ARG 53 ARG 54 THR 55 SER 56 GLY 57 GLY 58 ALA stop_ _Sequence_homology_query_date 2004-07-29 _Sequence_homology_query_revised_last_date 2002-08-18 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, 5-38)Ser BPTI" 5 CYS SG "(30-51, 5-38)Ser BPTI" 38 CYS SG single disulfide "(30-51, 5-38)Ser BPTI" 30 CYS SG "(30-51, 5-38)Ser 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_5-38)_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_name _Details $(30-51_5-38)_BPTI 'recombinant technology' "E. coli" Escherichia coli . . ; See: Darby et al.(1991) FEBS Letters 279, 61 - 64; van Mierlo et al. (1993) J. Mol. Biol. 229, 1125 - 1146; Darby and Creighton (1993) J. Mol. Biol. 232, 873 - 896 ; stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details ; 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_5-38)_BPTI . mM 1.5 3 . H2O 90 % . . . D2O 10 % . . . stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details ; 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_5-38)_BPTI . mM 1.5 3 . D2O 100 % . . . stop_ save_ ############################ # Computer software used # ############################ save_UXNMR _Saveframe_category software _Name UXNMR loop_ _Task "data acquisition" "data processing" stop_ _Details "Software versions available in 1991 - 1992." 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 ; _Details ; DQ = double quantum coherence experiment (see: Mareci and Freeman, (1983) J. Magn. Reson. 51, 531 - 535; Wagner and Zuiderweg (1983) Biochem. Biophys. Res. Commun. 113, 854 - 860. ; 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 n/a temperature 271 0.5 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference 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 . internal . . stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # Index Value Definition # # # # 1 Unique # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups # # 3 Aromatic atoms on opposite sides of the ring # # (e.g. Tyr HE1 and HE2 protons) # # 4 Intraresidue ambiguities (e.g. Lys HG and # # HD protons) # # 5 Interresidue ambiguities (Lys 12 vs. Lys 27) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_CSR_1 _Saveframe_category assigned_chemical_shifts _Details ; The N-terminal 15 residues of the molecule are flexible, all peptide bonds were predominantly trans, but a second population of the N-terminal part of the protein, comprising approximately 12 % of the molecules was also present, presumably due to the presence of a cis peptide bond. These signals were so weak, however, that it was not possible to assign this species. The HE1, HE2 and HZ protons of Phe4 resonate between 7.20 -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 $sample_2 stop_ _Sample_conditions_label $Ex-cond_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name "(30-51, 5-38)Ser 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 ARG HA H 4.41 0.01 1 2 1 ARG HB2 H 1.97 0.01 2 3 1 ARG HG2 H 1.73 0.01 1 4 1 ARG HG3 H 1.73 0.01 1 5 1 ARG HD2 H 3.24 0.01 1 6 1 ARG HD3 H 3.24 0.01 1 7 1 ARG HE H 7.37 0.01 1 8 2 PRO HA H 4.46 0.01 1 9 2 PRO HB2 H 1.72 0.01 2 10 2 PRO HB3 H 2.23 0.01 2 11 2 PRO HG2 H 1.97 0.01 1 12 2 PRO HG3 H 1.97 0.01 9 13 2 PRO HD2 H 3.57 0.01 2 14 2 PRO HD3 H 3.74 0.01 2 15 3 ASP H H 8.62 0.01 1 16 3 ASP HA H 4.53 0.01 1 17 3 ASP HB2 H 2.58 0.01 2 18 3 ASP HB3 H 2.67 0.01 2 19 4 PHE H H 8.28 0.01 1 20 4 PHE HA H 4.60 0.01 1 21 4 PHE HB2 H 3.03 0.01 2 22 4 PHE HB3 H 3.08 0.01 2 23 4 PHE HD1 H 7.23 0.01 1 24 4 PHE HD2 H 7.23 0.01 1 25 4 PHE HE1 H 7.20 0.01 3 26 4 PHE HE2 H 7.40 0.01 3 27 4 PHE HZ H 7.20 0.01 1 28 5 CYS H H 8.45 0.01 1 29 5 CYS HA H 4.60 0.01 1 30 5 CYS HB2 H 2.97 0.01 2 31 5 CYS HB3 H 3.06 0.01 2 32 6 LEU H H 8.54 0.01 1 33 6 LEU HA H 4.40 0.01 1 34 6 LEU HB2 H 1.61 0.01 1 35 6 LEU HB3 H 1.61 0.01 1 36 6 LEU HG H 1.61 0.01 1 37 6 LEU HD1 H 0.90 0.01 2 38 6 LEU HD2 H 0.97 0.01 2 39 7 GLU H H 8.48 0.01 1 40 7 GLU HA H 4.61 0.01 1 41 7 GLU HB2 H 1.87 0.01 2 42 7 GLU HB3 H 2.04 0.01 2 43 7 GLU HG2 H 2.31 0.01 1 44 7 GLU HG3 H 2.31 0.01 1 45 8 PRO HA H 4.71 0.01 1 46 8 PRO HB2 H 1.90 0.01 2 47 8 PRO HB3 H 2.35 0.01 2 48 8 PRO HG2 H 2.02 0.01 1 49 8 PRO HG3 H 2.02 0.01 1 50 8 PRO HD2 H 3.71 0.01 2 51 8 PRO HD3 H 3.84 0.01 2 52 9 PRO HA H 4.41 0.01 1 53 9 PRO HB2 H 1.85 0.01 2 54 9 PRO HB3 H 2.27 0.01 2 55 9 PRO HG2 H 2.02 0.01 1 56 9 PRO HG3 H 2.02 0.01 1 57 9 PRO HD2 H 3.63 0.01 2 58 9 PRO HD3 H 3.82 0.01 2 59 10 TYR H H 8.58 0.01 1 60 10 TYR HA H 4.67 0.01 1 61 10 TYR HB2 H 2.92 0.01 2 62 10 TYR HB3 H 3.09 0.01 2 63 10 TYR HD1 H 7.13 0.01 1 64 10 TYR HD2 H 7.13 0.01 1 65 10 TYR HE1 H 6.78 0.01 1 66 10 TYR HE2 H 6.78 0.01 1 67 11 THR H H 8.32 0.01 1 68 11 THR HA H 4.39 0.01 1 69 11 THR HB H 4.27 0.01 1 70 11 THR HG2 H 1.11 0.01 1 71 12 GLY H H 6.90 0.01 1 72 12 GLY HA2 H 3.98 0.01 2 73 12 GLY HA3 H 4.08 0.01 2 74 13 PRO HA H 4.51 0.01 1 75 13 PRO HB2 H 2.00 0.01 2 76 13 PRO HB3 H 2.34 0.01 2 77 13 PRO HG2 H 2.08 0.01 2 78 13 PRO HD2 H 3.66 0.01 1 79 13 PRO HD3 H 3.66 0.01 1 80 14 SER H H 8.70 0.01 1 81 14 SER HA H 4.38 0.01 1 82 14 SER HB2 H 3.87 0.01 2 83 14 SER HB3 H 3.93 0.01 2 84 15 LYS H H 8.51 0.01 1 85 15 LYS HA H 4.29 0.01 1 86 15 LYS HB2 H 1.73 0.01 9 87 15 LYS HB3 H 1.85 0.01 4 88 15 LYS HG2 H 1.40 0.01 4 89 15 LYS HG3 H 1.40 0.01 4 90 15 LYS HD2 H 1.64 0.01 1 91 15 LYS HD3 H 1.64 0.01 1 92 15 LYS HE2 H 2.91 0.01 1 93 15 LYS HE3 H 2.91 0.01 1 94 15 LYS HZ H 7.60 0.01 1 95 16 ALA H H 8.16 0.01 1 96 16 ALA HA H 4.31 0.01 1 97 16 ALA HB H 1.38 0.01 1 98 17 ARG H H 8.27 0.01 1 99 17 ARG HA H 4.26 0.01 1 100 17 ARG HB2 H 1.69 0.01 1 101 17 ARG HB3 H 1.69 0.01 9 102 17 ARG HG2 H 1.50 0.01 2 103 17 ARG HG3 H 1.60 0.01 2 104 17 ARG HD2 H 3.10 0.01 1 105 17 ARG HD3 H 3.10 0.01 1 106 17 ARG HE H 7.27 0.01 1 107 18 ILE H H 8.67 0.01 1 108 18 ILE HA H 4.18 0.01 1 109 18 ILE HB H 1.95 0.01 1 110 18 ILE HG12 H 1.20 0.01 2 111 18 ILE HG13 H 1.55 0.01 2 112 18 ILE HG2 H 0.86 0.01 1 113 18 ILE HD1 H 0.87 0.01 1 114 19 ILE H H 8.57 0.01 1 115 19 ILE HA H 4.47 0.01 1 116 19 ILE HB H 1.86 0.01 1 117 19 ILE HG12 H 1.29 0.01 2 118 19 ILE HG13 H 1.44 0.01 2 119 19 ILE HG2 H 0.71 0.01 1 120 19 ILE HD1 H 0.71 0.01 1 121 20 ARG H H 8.32 0.01 1 122 20 ARG HA H 4.70 0.01 1 123 20 ARG HB2 H 0.95 0.01 2 124 20 ARG HB3 H 1.97 0.01 9 125 20 ARG HG2 H 1.31 0.01 4 126 20 ARG HD2 H 2.87 0.01 9 127 20 ARG HD3 H 3.03 0.01 9 128 21 TYR H H 8.98 0.01 1 129 21 TYR HA H 5.74 0.01 1 130 21 TYR HB2 H 2.72 0.01 1 131 21 TYR HB3 H 2.72 0.01 1 132 21 TYR HD1 H 6.71 0.01 1 133 21 TYR HD2 H 6.71 0.01 1 134 21 TYR HE1 H 6.78 0.01 1 135 21 TYR HE2 H 6.78 0.01 1 136 22 PHE H H 9.88 0.01 1 137 22 PHE HA H 5.40 0.01 1 138 22 PHE HB2 H 3.02 0.01 2 139 22 PHE HB3 H 3.18 0.01 2 140 22 PHE HD1 H 7.16 0.01 1 141 22 PHE HD2 H 7.16 0.01 1 142 22 PHE HE1 H 7.27 0.01 1 143 22 PHE HE2 H 7.27 0.01 1 144 22 PHE HZ H 7.34 0.01 1 145 23 TYR H H 9.80 0.01 1 146 23 TYR HA H 4.47 0.01 1 147 23 TYR HB2 H 3.00 0.01 2 148 23 TYR HB3 H 3.09 0.01 2 149 23 TYR HD1 H 7.01 0.01 1 150 23 TYR HD2 H 7.01 0.01 1 151 23 TYR HE1 H 6.55 0.01 1 152 23 TYR HE2 H 6.55 0.01 1 153 24 ASN H H 8.00 0.01 1 154 24 ASN HA H 4.55 0.01 1 155 24 ASN HB2 H 2.26 0.01 2 156 24 ASN HB3 H 2.91 0.01 2 157 24 ASN HD21 H 8.14 0.01 9 158 24 ASN HD22 H 7.30 0.01 9 159 25 ALA H H 8.51 0.01 1 160 25 ALA HA H 3.63 0.01 1 161 25 ALA HB H 1.53 0.01 1 162 26 LYS H H 8.01 0.01 1 163 26 LYS HA H 4.09 0.01 1 164 26 LYS HB2 H 1.92 0.01 1 165 26 LYS HB3 H 1.92 0.01 1 166 26 LYS HG2 H 1.45 0.01 2 167 26 LYS HG3 H 1.52 0.01 2 168 26 LYS HD2 H 1.73 0.01 1 169 26 LYS HD3 H 1.73 0.01 1 170 26 LYS HE2 H 3.01 0.01 1 171 26 LYS HE3 H 3.01 0.01 1 172 26 LYS HZ H 7.65 0.01 1 173 27 ALA H H 6.92 0.01 1 174 27 ALA HA H 4.29 0.01 1 175 27 ALA HB H 1.22 0.01 1 176 28 GLY H H 8.18 0.01 1 177 28 GLY HA2 H 3.76 0.01 2 178 28 GLY HA3 H 3.96 0.01 2 179 29 LEU H H 6.94 0.01 1 180 29 LEU HA H 4.91 0.01 1 181 29 LEU HB2 H 1.38 0.01 2 182 29 LEU HB3 H 1.58 0.01 2 183 29 LEU HG H 1.47 0.01 1 184 29 LEU HD1 H 0.84 0.01 2 185 29 LEU HD2 H 0.89 0.01 2 186 30 CYS H H 9.27 0.01 1 187 30 CYS HA H 5.42 0.01 1 188 30 CYS HB2 H 2.60 0.01 2 189 30 CYS HB3 H 3.58 0.01 2 190 31 GLN H H 9.21 0.01 1 191 31 GLN HA H 4.89 0.01 1 192 31 GLN HB2 H 1.74 0.01 2 193 31 GLN HB3 H 2.10 0.01 2 194 31 GLN HG2 H 2.05 0.01 2 195 31 GLN HG3 H 2.27 0.01 2 196 31 GLN HE21 H 7.62 0.01 9 197 31 GLN HE22 H 7.24 0.01 9 198 32 THR H H 8.30 0.01 1 199 32 THR HA H 4.86 0.01 1 200 32 THR HB H 4.03 0.01 1 201 32 THR HG2 H 0.78 0.01 1 202 33 PHE H H 8.87 0.01 1 203 33 PHE HA H 4.85 0.01 1 204 33 PHE HB2 H 2.96 0.01 2 205 33 PHE HB3 H 3.15 0.01 2 206 33 PHE HD1 H 7.12 0.01 1 207 33 PHE HD2 H 7.12 0.01 1 208 33 PHE HE1 H 7.29 0.01 9 209 33 PHE HE2 H 7.29 0.01 9 210 33 PHE HZ H 7.19 0.01 9 211 34 VAL H H 8.52 0.01 1 212 34 VAL HA H 4.07 0.01 1 213 34 VAL HB H 1.91 0.01 1 214 34 VAL HG1 H 0.81 0.01 2 215 34 VAL HG2 H 0.85 0.01 2 216 35 TYR H H 8.74 0.01 1 217 35 TYR HA H 4.36 0.01 1 218 35 TYR HB2 H 2.47 0.01 2 219 35 TYR HB3 H 2.79 0.01 2 220 35 TYR HD1 H 7.05 0.01 1 221 35 TYR HD2 H 7.05 0.01 1 222 35 TYR HE1 H 6.87 0.01 1 223 35 TYR HE2 H 6.87 0.01 1 224 36 GLY H H 8.23 0.01 1 225 36 GLY HA2 H 3.74 0.01 2 226 36 GLY HA3 H 3.88 0.01 2 227 37 GLY H H 7.52 0.01 9 228 37 GLY HA2 H 3.81 0.01 9 229 37 GLY HA3 H 3.97 0.01 9 230 38 CYS H H 8.77 0.01 9 231 38 CYS HA H 4.58 0.01 9 232 38 CYS HB2 H 3.09 0.01 9 233 38 CYS HB3 H 3.18 0.01 9 234 40 ALA H H 8.24 0.01 1 235 40 ALA HA H 4.24 0.01 1 236 40 ALA HB H 1.34 0.01 1 237 41 LYS H H 8.24 0.01 9 238 41 LYS HA H 4.22 0.01 1 239 41 LYS HB2 H 1.68 0.01 9 240 41 LYS HB3 H 1.81 0.01 9 241 42 ARG H H 8.11 0.01 1 242 42 ARG HA H 4.30 0.01 1 243 42 ARG HB2 H 1.80 0.01 9 244 42 ARG HG2 H 1.56 0.01 9 245 42 ARG HD2 H 2.81 0.01 9 246 42 ARG HD3 H 2.93 0.01 9 247 42 ARG HE H 7.17 0.01 9 248 43 ASN H H 8.65 0.01 1 249 43 ASN HA H 4.66 0.01 1 250 43 ASN HB2 H 2.75 0.01 2 251 43 ASN HB3 H 2.87 0.01 2 252 43 ASN HD21 H 7.94 0.01 9 253 43 ASN HD22 H 7.46 0.01 9 254 44 ASN H H 7.88 0.01 1 255 44 ASN HA H 5.36 0.01 1 256 44 ASN HB2 H 2.76 0.01 1 257 44 ASN HB3 H 2.76 0.01 1 258 44 ASN HD21 H 7.72 0.01 9 259 44 ASN HD22 H 6.79 0.01 9 260 45 PHE H H 9.49 0.01 1 261 45 PHE HA H 5.07 0.01 1 262 45 PHE HB2 H 2.72 0.01 2 263 45 PHE HB3 H 3.41 0.01 2 264 45 PHE HD1 H 7.23 0.01 1 265 45 PHE HD2 H 7.23 0.01 1 266 45 PHE HE1 H 7.49 0.01 1 267 45 PHE HE2 H 7.49 0.01 1 268 45 PHE HZ H 7.36 0.01 1 269 46 LYS H H 9.94 0.01 1 270 46 LYS HA H 4.40 0.01 1 271 46 LYS HB2 H 2.04 0.01 1 272 46 LYS HB3 H 2.04 0.01 1 273 46 LYS HG2 H 1.56 0.01 1 274 46 LYS HG3 H 1.56 0.01 9 275 46 LYS HD2 H 1.77 0.01 9 276 46 LYS HD3 H 1.77 0.01 9 277 46 LYS HE2 H 3.04 0.01 9 278 46 LYS HE3 H 3.04 0.01 9 279 46 LYS HZ H 7.72 0.01 9 280 47 SER H H 7.49 0.01 1 281 47 SER HA H 4.59 0.01 1 282 47 SER HB2 H 3.84 0.01 2 283 47 SER HB3 H 4.11 0.01 2 284 48 ALA H H 8.35 0.01 1 285 48 ALA HA H 3.00 0.01 1 286 48 ALA HB H 1.02 0.01 1 287 49 GLU H H 8.76 0.01 1 288 49 GLU HA H 3.84 0.01 1 289 49 GLU HB2 H 1.80 0.01 2 290 49 GLU HB3 H 1.99 0.01 2 291 49 GLU HG2 H 2.20 0.01 2 292 49 GLU HG3 H 2.35 0.01 2 293 50 ASP H H 7.89 0.01 1 294 50 ASP HA H 4.28 0.01 1 295 50 ASP HB2 H 2.72 0.01 2 296 50 ASP HB3 H 2.86 0.01 2 297 51 CYS H H 7.11 0.01 1 298 51 CYS HA H 1.85 0.01 1 299 51 CYS HB2 H 2.71 0.01 2 300 51 CYS HB3 H 3.09 0.01 2 301 52 ARG H H 8.69 0.01 1 302 52 ARG HA H 3.76 0.01 1 303 52 ARG HB2 H 1.74 0.01 1 304 52 ARG HB3 H 1.74 0.01 1 305 52 ARG HG2 H 1.49 0.01 2 306 52 ARG HG3 H 1.66 0.01 2 307 52 ARG HD2 H 3.10 0.01 1 308 52 ARG HD3 H 3.10 0.01 1 309 52 ARG HE H 7.44 0.01 1 310 52 ARG HH11 H 6.71 0.01 9 311 52 ARG HH12 H 6.94 0.01 9 312 53 ARG H H 8.05 0.01 1 313 53 ARG HA H 3.96 0.01 1 314 53 ARG HB2 H 1.81 0.01 2 315 53 ARG HB3 H 1.89 0.01 2 316 53 ARG HG2 H 1.58 0.01 2 317 53 ARG HG3 H 1.71 0.01 2 318 53 ARG HD2 H 3.20 0.01 1 319 53 ARG HD3 H 3.20 0.01 1 320 53 ARG HE H 7.38 0.01 1 321 54 THR H H 7.47 0.01 1 322 54 THR HA H 4.14 0.01 1 323 54 THR HB H 3.98 0.01 1 324 54 THR HG2 H 1.38 0.01 1 325 55 SER H H 7.90 0.01 1 326 55 SER HA H 4.09 0.01 1 327 55 SER HB2 H 3.11 0.01 1 328 55 SER HB3 H 3.11 0.01 1 329 56 GLY H H 7.93 0.01 1 330 56 GLY HA2 H 3.80 0.01 2 331 56 GLY HA3 H 3.97 0.01 2 332 57 GLY H H 8.12 0.01 1 333 57 GLY HA2 H 3.83 0.01 2 334 57 GLY HA3 H 3.98 0.01 2 335 58 ALA H H 7.95 0.01 1 336 58 ALA HA H 4.19 0.01 1 337 58 ALA HB H 1.39 0.01 1 stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _MEDLINE_UI_code 91138763 _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_2 _Saveframe_category citation _MEDLINE_UI_code 92071963 _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_3 _Saveframe_category citation _MEDLINE_UI_code 92235860 _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_4 _Saveframe_category citation _MEDLINE_UI_code 92357714 _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_5 _Saveframe_category citation _MEDLINE_UI_code 93188004 _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_6 _Saveframe_category citation _MEDLINE_UI_code 94118338 _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_