data_4868 #Corrected using PDB structure: 9PTI_ # #N.B. (Observed* = Observed shift + Offset correction) # #After reference correction, the following residues still #have a HN chemical shift difference (obs*-pred) greater than 2.0ppm: #NUM AA CS Observed* Predicted # 37 G H 4.16 6.71 # #The average CS difference between predicted and observed: #HA CA CB CO N HN #-0.01 N/A N/A N/A N/A -0.16 # #bmr4868.str.corr chemical shifts have been re-referenced with the following #offsets (these values have been added to the original bmr4868.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 +/-0.08 # #The Correlation Coefficients between predicted and observed #chemical shifts are: #HA CA CB CO N HN #0.935 N/A N/A N/A N/A 0.844 # #The RMSD between predicted and observed* (reference #corrected) chemical shifts are: #HA CA CB CO N HN #0.142 N/A N/A N/A N/A 0.287 # ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequential 1H assignments for BPTI-R52 (= BPTI with Met to Arg mutation at position 52) ; 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 Neuhaus David . . 4 Creighton Thomas E. . stop_ _BMRB_accession_number 4868 _BMRB_flat_file_name bmr4868.str _Entry_type new _Submission_date 2000-10-19 _Accession_date 2000-10-19 _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' 347 stop_ loop_ _Related_BMRB_accession_number 2169 4855 stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_title ; Two-dimensional 1H nuclear magnetic resonance study of the (5-55) single-disulphide folding intermediate of bovine pancreatic trypsin inhibitor ; _Citation_status published _Citation_type journal _MEDLINE_UI_code 92071964 _PubMed_ID ? 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 Neuhaus David . . 4 Creighton Thomas E. . stop_ _Journal_abbreviation "J. Mol. Biol." _Journal_volume 222 _Page_first 373 _Page_last 390 _Year 1991 loop_ _Keyword "NMR" "disulphide bonds" "bovine pancreatic trypsin inhibitor (BPTI)" "protein folding" "folding intermediate" stop_ save_ ################################## # Molecular system description # ################################## save_system_BPTI-R52 _Saveframe_category molecular_system _Mol_system_name BPTI-R52 _Abbreviation_common BPTI-R52 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label BPTI-R52 $BPTI-R52 stop_ _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Database_entry_details PDB 1B0C "C Chain C, Evidence Of A Common Decamer In Three Crystal Structures Of Bpti, Crystallized From Thiocyanate, Chloride Or Sulfate" . PDB 3BTK "I Chain I, The Crystal Structures Of The Complexes Between Bovine Beta- Trypsin And Ten P1 Variants Of Bpti" . PDB 1BZ5 "A Chain A, Evidence Of A Common Decamer In Three Crystal Structures Of Bpti, Crystallize From Thiocyanate, Chloride Or Sulfate" . PDB 1BHC "A Chain A, Bovine Pancreatic Trypsin Inhibitor Crystallized From Thiocyanate" . PDB 2KAI "I Chain I, Kallikrein A (E.C.3.4.21.8) Complex With Bovine Pancreatic Trypsin Inhibitor" . PDB 6PTI "Bovine Pancreatic Trypsin Inhibitor (BPTI,Crystal Form III)" . PDB 2HEX "C Chain C, Decamers Observed In The Crystals Of Bovine Pancreatic Trypsin Inhibitor" . PDB 1MTN "D Chain D, Bovine Alpha-Chymotrypsin:bpti Crystallization" . PDB 1CBW "D Chain D, Bovine Chymotrypsin Complexed To Bpti" . PDB 1BTH "P Chain P, Structure Of Thrombin Complexed With Bovine Pancreatic Trypsin Inhibitor" . PDB 1BZX "I Chain I, The Crystal Structure Of Anionic Salmon Trypsin In Complex With Bovine Pancreatic Trypsin Inhibitor" . PDB 2PTC "I Chain I, Beta-Trypsin (E.C.3.4.21.4) Complex With Pancreatic Trypsin Inhibitor" . PDB 1TPA "I Chain I, Anhydro-Trypsin (E.C.3.4.21.4) Complex With Pancreatic Trypsin Inhibitor" . PDB 2TGP "I Chain I, Trypsinogen Complex With Pancreatic Trypsin Inhibitor" . PDB 3TPI "I Chain I, Trypsinogen Complex With Pancreatic Trypsin Inhibitor And Ile-Val" . PDB 4PTI "Trypsin Inhibitor" . PDB 9PTI "Basic Pancreatic Trypsin Inhibitor (Met 52 Oxidized)" . PDB 1BPI "Bovine Pancreatic Trypsin Inhibitor (Bpti) (Crystal Form Ii)" . PDB 5PTI "Trypsin Inhibitor (Crystal Form II)" . PDB 1FY8 "I Chain I, Crystal Structure Of The Deltaile16val17 Rat Anionic Trypsinogen-Bpti Complex" . PDB 1D0D "B Chain B, Crystal Structure Of Tick Anticoagulant Protein Complexed With Bovine Pancreatic Trypsin Inhibitor" . PDB 2TPI "I Chain I, Trypsinogen - Pancreatic Trypsin Inhibitor - Ile-Val Complex (2.4 M Magnesium Sulfate)" . PDB 3TGJ "I Chain I, S195a Trypsinogen Complexed With Bovine Pancreatic Trypsin Inhibitor (Bpti)" . PDB 3TGI "I Chain I, Wild-Type Rat Anionic Trypsin Complexed With Bovine Pancreatic Trypsin Inhibitor (Bpti)" . stop_ save_ ######################## # Monomeric polymers # ######################## save_BPTI-R52 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common BPTI-R52 _Name_variant . _Abbreviation_common BPTI-R52 _Mol_thiol_state 'all disulfide bound' ############################## # Polymer residue sequence # ############################## _Residue_count 58 _Mol_residue_sequence ; RPDFCLEPPYTGPCKARIIR YFYNAKAGLCQTFVYGGCRA KRNNFKSAEDCRRTCGGA ; 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 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 CYS 56 GLY 57 GLY 58 ALA stop_ _Sequence_homology_query_date 2004-07-29 _Sequence_homology_query_revised_last_date 2004-06-24 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 1UUA "A Chain A, Solution Structure Of A TruncatedBovine Pancreatic Trypsin Inhibitor, 3-58 Bpti" 103.57 56 98 98 8e-28 PDB 1B0C "A Chain A, Evidence Of A Common Decamer InThree Crystal Structures Of Bpti, Crystallized FromThiocyanate, Chloride Or Sulfate" 100.00 58 98 98 7e-30 PDB 1BHC "A Chain A, Bovine Pancreatic TrypsinInhibitor Crystallized From Thiocyanate" 100.00 58 98 98 7e-30 PDB 1BPI "Bovine Pancreatic Trypsin Inhibitor (Bpti)(Crystal Form Ii)" 100.00 58 98 98 7e-30 PDB 1BTH "P Chain P, Structure Of Thrombin ComplexedWith Bovine Pancreatic Trypsin Inhibitor" 100.00 58 98 98 7e-30 PDB 1BZ5 "A Chain A, Evidence Of A Common Decamer InThree Crystal Structures Of Bpti, Crystallize FromThiocyanate, Chloride Or Sulfate" 100.00 58 98 98 7e-30 PDB 1BZX "I Chain I, The Crystal Structure Of AnionicSalmon Trypsin In Complex With Bovine PancreaticTrypsin Inhibitor" 100.00 58 98 98 7e-30 PDB 1CBW "D Chain D, Bovine Chymotrypsin Complexed ToBpti" 100.00 58 98 98 7e-30 PDB 1D0D "B Chain B, Crystal Structure Of TickAnticoagulant Protein Complexed With Bovine PancreaticTrypsin Inhibitor" 100.00 58 98 98 7e-30 PDB 1EAW "B Chain B, Crystal Structure Of The Mtsp1(Matriptase)-Bpti (Aprotinin) Complex" 100.00 58 98 98 7e-30 PDB 1FY8 "I Chain I, Crystal Structure Of TheDeltaile16val17 Rat Anionic Trypsinogen-Bpti Complex" 100.00 58 98 98 7e-30 PDB 1MTN "D Chain D, Bovine Alpha-Chymotrypsin:bptiCrystallization" 100.00 58 98 98 7e-30 PDB 1OA5 "5 Chain 5, The Solution Structure Of BovinePancreatic Trypsin Inhibitor At High Pressure" 100.00 58 98 98 3e-29 PDB 1OA6 "5 Chain 5, The Solution Structure Of BovinePancreatic Trypsin Inhibitor At High Pressure" 100.00 58 98 98 3e-29 PDB 1PIT "Trypsin Inhibitor (Nmr, 20 Structures)" 100.00 58 98 98 3e-29 PDB 1TPA "I Chain I, Anhydro-Trypsin (E.C.3.4.21.4)Complex With Pancreatic Trypsin Inhibitor" 100.00 58 98 98 7e-30 PDB 2HEX "A Chain A, Decamers Observed In The CrystalsOf Bovine Pancreatic Trypsin Inhibitor" 100.00 58 98 98 7e-30 PDB 2KAI "I Chain I, Kallikrein A (E.C.3.4.21.8) ComplexWith Bovine Pancreatic Trypsin Inhibitor" 100.00 58 98 98 7e-30 PDB 2PTC "I Chain I, Beta-Trypsin (E.C.3.4.21.4) ComplexWith Pancreatic Trypsin Inhibitor" 100.00 58 98 98 7e-30 PDB 2TGP "I Chain I, Trypsinogen Complex With PancreaticTrypsin Inhibitor" 100.00 58 98 98 7e-30 PDB 3BTK "I Chain I, The Crystal Structures Of TheComplexes Between Bovine Beta- Trypsin And Ten P1Variants Of Bpti" 100.00 58 98 98 7e-30 PDB 3TPI "I Chain I, Trypsinogen Complex With PancreaticTrypsin Inhibitor And Ile-Val" 100.00 58 98 98 7e-30 PDB 4PTI "Trypsin Inhibitor" 100.00 58 98 98 7e-30 PDB 5PTI "Structure Of Bovine Pancreatic TrypsinInhibitor. Results Of Joint Neutron And X-RayRefinement Of Crystal Form II" 100.00 58 98 98 7e-30 PDB 6PTI "Bovine Pancreatic Trypsin Inhibitor(BPTI,Crystal Form III)" 100.00 58 98 98 7e-30 PDB 9PTI "Basic Pancreatic Trypsin Inhibitor (Met 52Oxidized)" 100.00 58 98 98 7e-30 PDB 2TPI "I Chain I, Trypsinogen - Pancreatic TrypsinInhibitor - Ile-Val Complex (2.4 M Magnesium Sulfate)" 98.31 59 98 98 7e-30 PDB 1F5R "I Chain I, Rat Trypsinogen Mutant ComplexedWith Bovine Pancreatic Trypsin Inhibitor" 89.23 65 98 98 7e-30 PDB 1F7Z "I Chain I, Rat Trypsinogen K15a ComplexedWith Bovine Pancreatic Trypsin Inhibitor" 89.23 65 98 98 7e-30 PDB 3TGI "I Chain I, Wild-Type Rat Anionic TrypsinComplexed With Bovine Pancreatic Trypsin Inhibitor(Bpti)" 89.23 65 98 98 7e-30 PDB 3TGJ "I Chain I, S195a Trypsinogen Complexed WithBovine Pancreatic Trypsin Inhibitor (Bpti)" 89.23 65 98 98 7e-30 PDB 3TGK "I Chain I, Trypsinogen Mutant D194n AndDeletion Of Ile 16-Val 17 Complexed With BovinePancreatic Trypsin Inhibitor (Bpti)" 89.23 65 98 98 7e-30 PDB 1CO7 "I Chain I, R117h Mutant Rat Anionic TrypsinComplexed With Bovine Pancreatic Trypsin Inhibitor(Bpti)" 58.59 99 98 98 7e-30 EMBL CAA27063.1 "unnamed protein product [Bos taurus]" 100.00 58 98 98 7e-30 EMBL CAA28371.1 "unnamed protein product [syntheticconstruct]" 98.31 59 98 98 7e-30 EMBL CAA37967.1 "aprotinin [synthetic construct]" 98.31 59 98 98 7e-30 EMBL CAA27062.1 "unnamed protein product [Bos taurus]" 65.17 89 98 98 7e-30 EMBL CAA28886.1 "trypsin ihibitor precursor [Bos taurus]" 63.04 92 98 98 7e-30 GenBank AAB25189.1 "major cationic kallikrein inhibitor[cattle, posterior pituitary gland, Peptide, 58 aa]" 100.00 58 98 98 7e-30 GenBank AAD13685.1 "trypsin inhibitor [Bos taurus]" 58.00 100 98 98 7e-30 PIR TIBO "basic proteinase inhibitor precursor - bovine" 58.00 100 98 98 7e-30 PRF 1405218A "aprotinin analog" 101.75 57 98 98 2e-29 PRF 681071A "inhibitor,basic pancreatic trypsin" 100.00 58 98 98 7e-30 PRF 1405218D "aprotinin analog" 98.31 59 98 98 7e-30 REF NP_001001554.1 "trypsin inhibitor precursor [Bostaurus]" 58.00 100 98 98 7e-30 SWISS-PROT P00974 "BPT1_BOVIN Pancreatic trypsin inhibitorprecursor (Basic protease inhibitor) (BPI) (BPTI)(Aprotinin)" 58.00 100 98 98 7e-30 stop_ 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 BPTI-R52 5 CYS SG BPTI-R52 55 CYS SG single disulfide BPTI-R52 14 CYS SG BPTI-R52 38 CYS SG single disulfide BPTI-R52 30 CYS SG BPTI-R52 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 $BPTI-R52 "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 $BPTI-R52 'recombinant technology' "E. coli" Escherichia coli . plasmid pLcIICLM ; See Nagai et al., (1988) Nature, 332, 284-286 ; 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 $BPTI-R52 . mM 2 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 $BPTI-R52 . mM 2 3 . D2O 100 % . . . stop_ save_ ############################ # Computer software used # ############################ save_UXNMR _Saveframe_category software _Name UXNMR loop_ _Task "data acquisition" "data processing" stop_ _Details "Versions of UXNMR as available in the period 1990 - 1991" save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model AM _Field_strength 500 save_ save_NMR_spectrometer_2 _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 NOESY TOCSY DQ ; _Details ; DQ = Double Quantum Coherence experiment Mareci and Freeman (1983) J. Magn. Reson. 51, 531-535 ; 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 283 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 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 BPTI-R52 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 4.38 0.01 1 2 1 ARG HB2 H 1.78 0.01 2 3 1 ARG HB3 H 1.89 0.01 2 4 1 ARG HG2 H 1.29 0.01 2 5 1 ARG HG3 H 1.44 0.01 2 6 1 ARG HD2 H 2.75 0.01 2 7 1 ARG HD3 H 3.07 0.01 2 8 1 ARG HE H 7.06 0.01 1 9 2 PRO HA H 4.33 0.01 1 10 2 PRO HB2 H 0.90 0.01 2 11 2 PRO HB3 H 2.05 0.01 2 12 2 PRO HG2 H 1.59 0.01 2 13 2 PRO HG3 H 1.89 0.01 2 14 2 PRO HD2 H 3.60 0.01 2 15 2 PRO HD3 H 3.73 0.01 2 16 3 ASP H H 8.85 0.01 1 17 3 ASP HA H 4.32 0.01 1 18 3 ASP HB2 H 2.77 0.01 1 19 3 ASP HB3 H 2.77 0.01 1 20 4 PHE H H 8.09 0.01 1 21 4 PHE HA H 4.61 0.01 1 22 4 PHE HB2 H 2.99 0.01 2 23 4 PHE HB3 H 3.36 0.01 2 24 4 PHE HD1 H 7.02 0.01 1 25 4 PHE HD2 H 7.02 0.01 1 26 4 PHE HE1 H 7.38 0.01 1 27 4 PHE HE2 H 7.38 0.01 1 28 4 PHE HZ H 7.32 0.01 1 29 5 CYS H H 7.50 0.01 1 30 5 CYS HA H 4.36 0.01 1 31 5 CYS HB2 H 2.76 0.01 2 32 5 CYS HB3 H 2.86 0.01 2 33 6 LEU H H 7.66 0.01 1 34 6 LEU HA H 4.48 0.01 1 35 6 LEU HB2 H 1.84 0.01 1 36 6 LEU HB3 H 1.84 0.01 1 37 6 LEU HG H 1.71 0.01 1 38 6 LEU HD1 H 0.86 0.01 2 39 6 LEU HD2 H 0.96 0.01 2 40 7 GLU H H 7.50 0.01 1 41 7 GLU HA H 4.60 0.01 1 42 7 GLU HB2 H 2.19 0.01 2 43 7 GLU HB3 H 2.23 0.01 2 44 7 GLU HG2 H 2.55 0.01 2 45 7 GLU HG3 H 2.66 0.01 2 46 8 PRO HA H 4.66 0.01 1 47 8 PRO HB2 H 1.86 0.01 2 48 8 PRO HB3 H 2.47 0.01 2 49 8 PRO HG2 H 2.14 0.01 1 50 8 PRO HG3 H 2.14 0.01 1 51 8 PRO HD2 H 3.74 0.01 2 52 8 PRO HD3 H 3.98 0.01 2 53 9 PRO HA H 3.72 0.01 1 54 9 PRO HB2 H 0.03 0.01 2 55 9 PRO HB3 H 0.18 0.01 2 56 9 PRO HG2 H 0.22 0.01 2 57 9 PRO HG3 H 1.29 0.01 2 58 9 PRO HD2 H 3.06 0.01 2 59 9 PRO HD3 H 3.40 0.01 2 60 10 TYR H H 7.95 0.01 1 61 10 TYR HA H 4.95 0.01 1 62 10 TYR HB2 H 2.98 0.01 1 63 10 TYR HB3 H 2.98 0.01 1 64 10 TYR HD1 H 7.33 0.01 1 65 10 TYR HD2 H 7.33 0.01 1 66 10 TYR HE1 H 7.10 0.01 1 67 10 TYR HE2 H 7.10 0.01 1 68 11 THR H H 9.15 0.01 1 69 11 THR HA H 4.52 0.01 1 70 11 THR HB H 4.07 0.01 1 71 11 THR HG2 H 1.39 0.01 1 72 12 GLY H H 7.31 0.01 1 73 12 GLY HA2 H 3.26 0.01 2 74 12 GLY HA3 H 3.88 0.01 2 75 13 PRO HA H 4.56 0.01 1 76 13 PRO HB2 H 2.10 0.01 4 77 13 PRO HB3 H 2.15 0.01 2 78 13 PRO HG2 H 2.00 0.01 2 79 13 PRO HD2 H 3.58 0.01 2 80 13 PRO HD3 H 3.66 0.01 2 81 14 CYS H H 8.80 0.01 1 82 14 CYS HA H 4.60 0.01 1 83 14 CYS HB2 H 2.80 0.01 2 84 14 CYS HB3 H 3.48 0.01 2 85 15 LYS H H 8.09 0.01 1 86 15 LYS HA H 4.42 0.01 1 87 15 LYS HB2 H 1.60 0.01 2 88 15 LYS HB3 H 2.09 0.01 4 89 15 LYS HG2 H 1.31 0.01 2 90 15 LYS HG3 H 1.43 0.01 2 91 15 LYS HD2 H 1.55 0.01 2 92 15 LYS HE2 H 2.96 0.01 4 93 15 LYS HZ H 7.50 0.01 1 94 16 ALA H H 8.26 0.01 1 95 16 ALA HA H 4.29 0.01 1 96 16 ALA HB H 1.18 0.01 1 97 17 ARG H H 8.38 0.01 1 98 17 ARG HA H 4.31 0.01 1 99 17 ARG HB2 H 1.48 0.01 4 100 17 ARG HB3 H 1.60 0.01 2 101 17 ARG HG2 H 1.31 0.01 2 102 17 ARG HD2 H 3.11 0.01 2 103 17 ARG HD3 H 3.16 0.01 2 104 17 ARG HE H 7.27 0.01 1 105 18 ILE H H 8.24 0.01 1 106 18 ILE HA H 4.20 0.01 1 107 18 ILE HB H 1.85 0.01 1 108 18 ILE HG12 H 1.01 0.01 2 109 18 ILE HG13 H 1.39 0.01 2 110 18 ILE HG2 H 0.98 0.01 1 111 18 ILE HD1 H 0.70 0.01 1 112 19 ILE H H 8.88 0.01 1 113 19 ILE HA H 4.29 0.01 1 114 19 ILE HB H 1.95 0.01 1 115 19 ILE HG12 H 1.39 0.01 2 116 19 ILE HG13 H 1.49 0.01 2 117 19 ILE HG2 H 0.72 0.01 1 118 19 ILE HD1 H 0.68 0.01 1 119 20 ARG H H 8.48 0.01 1 120 20 ARG HA H 4.73 0.01 1 121 20 ARG HB2 H 0.80 0.01 2 122 20 ARG HB3 H 1.80 0.01 4 123 20 ARG HG2 H 1.30 0.01 2 124 20 ARG HD2 H 2.99 0.01 2 125 20 ARG HD3 H 3.51 0.01 2 126 20 ARG HE H 7.52 0.01 1 127 20 ARG HH11 H 6.87 0.01 9 128 20 ARG HH12 H 7.21 0.01 9 129 21 TYR H H 9.27 0.01 1 130 21 TYR HA H 5.73 0.01 1 131 21 TYR HB2 H 2.71 0.01 1 132 21 TYR HB3 H 2.71 0.01 1 133 21 TYR HD1 H 6.74 0.01 1 134 21 TYR HD2 H 6.74 0.01 1 135 21 TYR HE1 H 6.79 0.01 1 136 21 TYR HE2 H 6.79 0.01 1 137 22 PHE H H 9.97 0.01 1 138 22 PHE HA H 5.24 0.01 1 139 22 PHE HB2 H 2.79 0.01 2 140 22 PHE HB3 H 2.95 0.01 2 141 22 PHE HD1 H 7.13 0.01 1 142 22 PHE HD2 H 7.13 0.01 1 143 22 PHE HE1 H 7.29 0.01 1 144 22 PHE HE2 H 7.29 0.01 1 145 22 PHE HZ H 7.38 0.01 1 146 23 TYR H H 10.71 0.01 1 147 23 TYR HA H 4.19 0.01 1 148 23 TYR HB2 H 2.69 0.01 2 149 23 TYR HB3 H 3.53 0.01 2 150 23 TYR HD1 H 7.01 0.01 1 151 23 TYR HD2 H 7.27 0.01 1 152 23 TYR HE1 H 6.36 0.01 1 153 23 TYR HE2 H 6.38 0.01 1 154 24 ASN H H 7.75 0.01 1 155 24 ASN HA H 4.55 0.01 1 156 24 ASN HB2 H 2.20 0.01 2 157 24 ASN HB3 H 2.88 0.01 2 158 24 ASN HD21 H 7.26 0.01 9 159 24 ASN HD22 H 8.12 0.01 9 160 25 ALA H H 8.75 0.01 1 161 25 ALA HA H 3.78 0.01 1 162 25 ALA HB H 1.58 0.01 1 163 26 LYS H H 8.07 0.01 1 164 26 LYS HA H 4.06 0.01 1 165 26 LYS HB2 H 1.91 0.01 1 166 26 LYS HB3 H 1.91 0.01 1 167 26 LYS HG2 H 1.45 0.01 2 168 26 LYS HG3 H 1.52 0.01 2 169 26 LYS HD2 H 1.74 0.01 2 170 26 LYS HE2 H 3.04 0.01 2 171 26 LYS HZ H 7.61 0.01 1 172 27 ALA H H 6.85 0.01 1 173 27 ALA HA H 4.27 0.01 1 174 27 ALA HB H 1.19 0.01 1 175 28 GLY H H 8.22 0.01 1 176 28 GLY HA2 H 3.64 0.01 2 177 28 GLY HA3 H 3.91 0.01 2 178 29 LEU H H 6.78 0.01 1 179 29 LEU HA H 4.78 0.01 1 180 29 LEU HB2 H 1.39 0.01 2 181 29 LEU HB3 H 1.61 0.01 2 182 29 LEU HG H 1.43 0.01 1 183 29 LEU HD1 H 0.80 0.01 2 184 29 LEU HD2 H 0.87 0.01 2 185 30 CYS H H 9.06 0.01 1 186 30 CYS HA H 5.46 0.01 1 187 30 CYS HB2 H 2.62 0.01 2 188 30 CYS HB3 H 3.66 0.01 2 189 31 GLN H H 9.10 0.01 1 190 31 GLN HA H 4.87 0.01 1 191 31 GLN HB2 H 1.75 0.01 2 192 31 GLN HB3 H 2.20 0.01 2 193 31 GLN HG2 H 1.94 0.01 2 194 31 GLN HG3 H 2.26 0.01 2 195 31 GLN HE21 H 7.16 0.01 9 196 31 GLN HE22 H 7.51 0.01 9 197 32 THR H H 8.15 0.01 1 198 32 THR HA H 5.34 0.01 1 199 32 THR HB H 4.06 0.01 1 200 32 THR HG2 H 0.60 0.01 1 201 33 PHE H H 9.45 0.01 1 202 33 PHE HA H 4.86 0.01 1 203 33 PHE HB2 H 2.93 0.01 2 204 33 PHE HB3 H 3.07 0.01 2 205 33 PHE HD1 H 7.06 0.01 1 206 33 PHE HD2 H 7.06 0.01 1 207 33 PHE HE1 H 7.10 0.01 1 208 33 PHE HE2 H 7.10 0.01 1 209 33 PHE HZ H 6.99 0.01 1 210 34 VAL H H 8.50 0.01 1 211 34 VAL HA H 3.90 0.01 1 212 34 VAL HB H 1.95 0.01 1 213 34 VAL HG1 H 0.69 0.01 2 214 34 VAL HG2 H 0.81 0.01 2 215 35 TYR H H 9.50 0.01 1 216 35 TYR HA H 4.88 0.01 1 217 35 TYR HB2 H 2.48 0.01 2 218 35 TYR HB3 H 2.66 0.01 2 219 35 TYR HD1 H 6.69 0.01 3 220 35 TYR HD2 H 7.79 0.01 3 221 35 TYR HE1 H 6.78 0.01 3 222 35 TYR HE2 H 6.89 0.01 3 223 35 TYR HH H 9.97 0.01 1 224 36 GLY H H 8.70 0.01 1 225 36 GLY HA2 H 3.23 0.01 2 226 36 GLY HA3 H 4.34 0.01 2 227 37 GLY H H 4.32 0.01 1 228 37 GLY HA2 H 2.94 0.01 2 229 37 GLY HA3 H 4.22 0.01 2 230 38 CYS H H 7.77 0.01 1 231 38 CYS HA H 4.98 0.01 1 232 38 CYS HB2 H 3.04 0.01 2 233 38 CYS HB3 H 4.00 0.01 2 234 39 ARG H H 9.19 0.01 1 235 39 ARG HA H 3.97 0.01 1 236 39 ARG HB2 H 2.25 0.01 2 237 39 ARG HB3 H 2.34 0.01 2 238 39 ARG HG2 H 1.58 0.01 2 239 39 ARG HD2 H 3.19 0.01 2 240 39 ARG HD3 H 3.30 0.01 2 241 39 ARG HE H 7.37 0.01 1 242 40 ALA H H 7.49 0.01 1 243 40 ALA HA H 4.10 0.01 1 244 40 ALA HB H 1.20 0.01 1 245 41 LYS H H 8.41 0.01 1 246 41 LYS HA H 4.46 0.01 1 247 41 LYS HB2 H 1.67 0.01 2 248 41 LYS HB3 H 2.26 0.01 2 249 41 LYS HG2 H 1.34 0.01 4 250 41 LYS HG3 H 1.51 0.01 4 251 41 LYS HE2 H 2.06 0.01 9 252 41 LYS HZ H 7.24 0.01 9 253 42 ARG H H 8.41 0.01 1 254 42 ARG HA H 3.64 0.01 1 255 42 ARG HB2 H 0.27 0.01 2 256 42 ARG HB3 H 1.00 0.01 2 257 42 ARG HG2 H 1.22 0.01 2 258 42 ARG HG3 H 1.52 0.01 2 259 42 ARG HD2 H 2.66 0.01 2 260 42 ARG HD3 H 2.85 0.01 2 261 42 ARG HE H 7.18 0.01 1 262 43 ASN H H 7.24 0.01 1 263 43 ASN HA H 5.07 0.01 1 264 43 ASN HB2 H 3.23 0.01 2 265 43 ASN HB3 H 3.34 0.01 2 266 43 ASN HD21 H 7.89 0.01 9 267 43 ASN HD22 H 7.92 0.01 9 268 44 ASN H H 6.82 0.01 1 269 44 ASN HA H 4.90 0.01 1 270 44 ASN HB2 H 2.52 0.01 2 271 44 ASN HB3 H 2.81 0.01 2 272 44 ASN HD21 H 3.34 0.01 9 273 44 ASN HD22 H 7.92 0.01 9 274 45 PHE H H 10.07 0.01 1 275 45 PHE HA H 5.14 0.01 1 276 45 PHE HB2 H 2.80 0.01 2 277 45 PHE HB3 H 3.42 0.01 2 278 45 PHE HD1 H 7.26 0.01 4 279 45 PHE HD2 H 7.60 0.01 4 280 45 PHE HE1 H 7.51 0.01 4 281 45 PHE HE2 H 8.19 0.01 3 282 45 PHE HZ H 7.68 0.01 1 283 46 LYS H H 10.11 0.01 1 284 46 LYS HA H 4.36 0.01 1 285 46 LYS HB2 H 1.97 0.01 2 286 46 LYS HB3 H 2.13 0.01 2 287 46 LYS HG2 H 1.44 0.01 4 288 46 LYS HG3 H 1.65 0.01 4 289 46 LYS HD2 H 1.80 0.01 4 290 46 LYS HE2 H 3.05 0.01 4 291 46 LYS HZ H 7.65 0.01 1 292 47 SER H H 7.53 0.01 1 293 47 SER HA H 4.58 0.01 1 294 47 SER HB2 H 3.87 0.01 2 295 47 SER HB3 H 4.13 0.01 2 296 48 ALA H H 8.29 0.01 1 297 48 ALA HA H 3.11 0.01 1 298 48 ALA HB H 1.01 0.01 1 299 49 GLU H H 8.63 0.01 1 300 49 GLU HA H 3.86 0.01 1 301 49 GLU HB2 H 1.83 0.01 2 302 49 GLU HB3 H 2.03 0.01 2 303 49 GLU HG2 H 2.23 0.01 2 304 49 GLU HG3 H 2.35 0.01 2 305 50 ASP H H 7.90 0.01 1 306 50 ASP HA H 4.31 0.01 1 307 50 ASP HB2 H 2.77 0.01 2 308 50 ASP HB3 H 2.95 0.01 2 309 51 CYS H H 7.03 0.01 1 310 51 CYS HA H 1.79 0.01 1 311 51 CYS HB2 H 2.84 0.01 2 312 51 CYS HB3 H 3.18 0.01 2 313 52 ARG H H 8.69 0.01 1 314 52 ARG HA H 3.64 0.01 1 315 52 ARG HB2 H 1.75 0.01 2 316 52 ARG HB3 H 1.81 0.01 2 317 52 ARG HG2 H 1.52 0.01 2 318 52 ARG HD2 H 3.11 0.01 2 319 52 ARG HD3 H 3.23 0.01 2 320 52 ARG HE H 7.44 0.01 1 321 52 ARG HH11 H 6.73 0.01 9 322 52 ARG HH12 H 6.94 0.01 9 323 53 ARG H H 8.32 0.01 1 324 53 ARG HA H 3.94 0.01 1 325 53 ARG HB2 H 1.85 0.01 2 326 53 ARG HB3 H 1.93 0.01 2 327 53 ARG HG2 H 1.60 0.01 2 328 53 ARG HG3 H 1.74 0.01 2 329 53 ARG HD2 H 3.24 0.01 2 330 53 ARG HE H 7.37 0.01 1 331 54 THR H H 7.49 0.01 1 332 54 THR HA H 4.09 0.01 1 333 54 THR HB H 3.98 0.01 1 334 54 THR HG2 H 1.64 0.01 1 335 55 CYS H H 8.41 0.01 1 336 55 CYS HA H 4.64 0.01 1 337 55 CYS HB2 H 2.17 0.01 2 338 55 CYS HB3 H 2.31 0.01 2 339 56 GLY H H 7.87 0.01 1 340 56 GLY HA2 H 3.84 0.01 1 341 56 GLY HA3 H 3.84 0.01 1 342 57 GLY H H 8.33 0.01 1 343 57 GLY HA2 H 3.88 0.01 2 344 57 GLY HA3 H 3.98 0.01 2 345 58 ALA H H 8.10 0.01 1 346 58 ALA HA H 4.02 0.01 1 347 58 ALA HB H 1.33 0.01 1 stop_ save_ ####################################### # Cited references within the entry # ####################################### save_ref_1 _Saveframe_category citation _MEDLINE_UI_code 92071964 _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 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_3 _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_4 _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_5 _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_6 _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_7 _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_