data_963 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; High Resolution Nuclear Magnetic Resonance Studies of the Active Site of Chymotrypsin II. Polarization of Histidine 57 by Substrate Analogues and Competitive Inhibitors ; _BMRB_accession_number 963 _BMRB_flat_file_name bmr963.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-03-25 _Entry_origination BMRB _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 Robillard G. . . 2 Shulman R. G. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 1 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-11 revision BMRB 'Complete natural source information' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Robillard, G., Shulman, R.G., "High Resolution Nuclear Magnetic Resonance Studies of the Active Site of Chymotrypsin II. Polarization of Histidine 57 by Substrate Analogues and Competitive Inhibitors," J. Mol. Biol. 86, 541-558 (1974). ; _Citation_title ; High Resolution Nuclear Magnetic Resonance Studies of the Active Site of Chymotrypsin II. Polarization of Histidine 57 by Substrate Analogues and Competitive Inhibitors ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Robillard G. . . 2 Shulman R. G. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 86 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 541 _Page_last 558 _Year 1974 _Details . save_ ################################## # Molecular system description # ################################## save_system_chymotrypsin _Saveframe_category molecular_system _Mol_system_name chymotrypsin _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label chymotrypsin $chymotrypsin stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_chymotrypsin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common chymotrypsin _Name_variant 'A-delta chymotrypsin(16-245)' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 230 _Mol_residue_sequence ; IVNGEEAVPGSWPWQVSLQD KTGFHFCGGSLINENWVVTA AHCGVTTSDVVVAGEFDQGS SSEKIQKLKIAKVFKNSKYN SLTINNDITLLKLSTAASFS QTVSAVCLPSASDDFAAGTT CVVTGWGLTRYTNANTPDRL QQASLPLLSNTNCKKYWGTK IKDAMICAGASGVSSCMGDS GGPLVCKKNGAWTLVGIVSW GSSTCSTSTPGVYARVTALV NWVQQTLAAN ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 ILE 2 2 VAL 3 3 ASN 4 4 GLY 5 5 GLU 6 6 GLU 7 7 ALA 8 8 VAL 9 9 PRO 10 10 GLY 11 11 SER 12 12 TRP 13 13 PRO 14 14 TRP 15 15 GLN 16 16 VAL 17 17 SER 18 18 LEU 19 19 GLN 20 20 ASP 21 21 LYS 22 22 THR 23 23 GLY 24 24 PHE 25 25 HIS 26 26 PHE 27 27 CYS 28 28 GLY 29 29 GLY 30 30 SER 31 31 LEU 32 32 ILE 33 33 ASN 34 34 GLU 35 35 ASN 36 36 TRP 37 37 VAL 38 38 VAL 39 39 THR 40 40 ALA 41 41 ALA 42 42 HIS 43 43 CYS 44 44 GLY 45 45 VAL 46 46 THR 47 47 THR 48 48 SER 49 49 ASP 50 50 VAL 51 51 VAL 52 52 VAL 53 53 ALA 54 54 GLY 55 55 GLU 56 56 PHE 57 57 ASP 58 58 GLN 59 59 GLY 60 60 SER 61 61 SER 62 62 SER 63 63 GLU 64 64 LYS 65 65 ILE 66 66 GLN 67 67 LYS 68 68 LEU 69 69 LYS 70 70 ILE 71 71 ALA 72 72 LYS 73 73 VAL 74 74 PHE 75 75 LYS 76 76 ASN 77 77 SER 78 78 LYS 79 79 TYR 80 80 ASN 81 81 SER 82 82 LEU 83 83 THR 84 84 ILE 85 85 ASN 86 86 ASN 87 87 ASP 88 88 ILE 89 89 THR 90 90 LEU 91 91 LEU 92 92 LYS 93 93 LEU 94 94 SER 95 95 THR 96 96 ALA 97 97 ALA 98 98 SER 99 99 PHE 100 100 SER 101 101 GLN 102 102 THR 103 103 VAL 104 104 SER 105 105 ALA 106 106 VAL 107 107 CYS 108 108 LEU 109 109 PRO 110 110 SER 111 111 ALA 112 112 SER 113 113 ASP 114 114 ASP 115 115 PHE 116 116 ALA 117 117 ALA 118 118 GLY 119 119 THR 120 120 THR 121 121 CYS 122 122 VAL 123 123 VAL 124 124 THR 125 125 GLY 126 126 TRP 127 127 GLY 128 128 LEU 129 129 THR 130 130 ARG 131 131 TYR 132 132 THR 133 133 ASN 134 134 ALA 135 135 ASN 136 136 THR 137 137 PRO 138 138 ASP 139 139 ARG 140 140 LEU 141 141 GLN 142 142 GLN 143 143 ALA 144 144 SER 145 145 LEU 146 146 PRO 147 147 LEU 148 148 LEU 149 149 SER 150 150 ASN 151 151 THR 152 152 ASN 153 153 CYS 154 154 LYS 155 155 LYS 156 156 TYR 157 157 TRP 158 158 GLY 159 159 THR 160 160 LYS 161 161 ILE 162 162 LYS 163 163 ASP 164 164 ALA 165 165 MET 166 166 ILE 167 167 CYS 168 168 ALA 169 169 GLY 170 170 ALA 171 171 SER 172 172 GLY 173 173 VAL 174 174 SER 175 175 SER 176 176 CYS 177 177 MET 178 178 GLY 179 179 ASP 180 180 SER 181 181 GLY 182 182 GLY 183 183 PRO 184 184 LEU 185 185 VAL 186 186 CYS 187 187 LYS 188 188 LYS 189 189 ASN 190 190 GLY 191 191 ALA 192 192 TRP 193 193 THR 194 194 LEU 195 195 VAL 196 196 GLY 197 197 ILE 198 198 VAL 199 199 SER 200 200 TRP 201 201 GLY 202 202 SER 203 203 SER 204 204 THR 205 205 CYS 206 206 SER 207 207 THR 208 208 SER 209 209 THR 210 210 PRO 211 211 GLY 212 212 VAL 213 213 TYR 214 214 ALA 215 215 ARG 216 216 VAL 217 217 THR 218 218 ALA 219 219 LEU 220 220 VAL 221 221 ASN 222 222 TRP 223 223 VAL 224 224 GLN 225 225 GLN 226 226 THR 227 227 LEU 228 228 ALA 229 229 ALA 230 230 ASN stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-20 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 BMRB 4865 BCAa 100.00 241 98.70 98.70 6.93e-160 BMRB 6881 bovine_alpha_chymotrypsin 100.00 241 98.70 98.70 8.08e-160 BMRB 960 "chymotrypsinogen A" 100.00 245 100.00 100.00 7.26e-164 BMRB 961 chymotrypsin 100.00 230 100.00 100.00 5.16e-164 BMRB 962 "chymotrypsinogen A" 100.00 245 100.00 100.00 7.26e-164 BMRB 964 "chymotrypsinogen A" 100.00 245 100.00 100.00 7.26e-164 BMRB 965 chymotrypsin 100.00 230 100.00 100.00 5.16e-164 BMRB 966 "chymotrypsinogen A" 100.00 245 100.00 100.00 7.26e-164 BMRB 967 chymotrypsin 100.00 230 100.00 100.00 5.16e-164 PDB 1AB9 "Crystal Structure Of Bovine Gamma-Chymotrypsin" 56.96 131 99.24 99.24 4.85e-87 PDB 1ACB "Crystal And Molecular Structure Of The Bovine Alpha-Chymotrypsin-Eglin C Complex At 2.0 Angstroms Resolution" 100.00 245 99.57 99.57 3.96e-163 PDB 1AFQ "Crystal Structure Of Bovine Gamma-Chymotrypsin Complexed With A Synthetic Inhibitor" 56.96 131 99.24 99.24 4.85e-87 PDB 1CA0 "Bovine Chymotrypsin Complexed To Appi" 56.96 131 99.24 99.24 4.85e-87 PDB 1CBW "Bovine Chymotrypsin Complexed To Bpti" 56.96 131 99.24 99.24 4.85e-87 PDB 1CGI "Three-Dimensional Structure Of The Complexes Between Bovine ChymotrypsinogenA And Two Recombinant Variants Of Human Pancreatic " 100.00 245 99.57 99.57 3.96e-163 PDB 1CGJ "Three-Dimensional Structure Of The Complexes Between Bovine ChymotrypsinogenA And Two Recombinant Variants Of Human Pancreatic " 100.00 245 99.57 99.57 3.96e-163 PDB 1CHG "Chymotrypsinogen,2.5 Angstroms Crystal Structure, Comparison With Alpha-Chymotrypsin,And Implications For Zymogen Activation" 100.00 245 99.57 99.57 3.96e-163 PDB 1CHO "Crystal And Molecular Structures Of The Complex Of Alpha- Chymotrypsin With Its Inhibitor Turkey Ovomucoid Third Domain At 1.8 " 56.96 131 99.24 99.24 4.85e-87 PDB 1DLK "Crystal Structure Analysis Of Delta-Chymotrypsin Bound To A Peptidyl Chloromethyl Ketone Inhibitor" 100.00 230 99.57 99.57 2.19e-163 PDB 1EX3 "Crystal Structure Of Bovine Chymotrypsinogen A (Tetragonal)" 100.00 245 99.57 99.57 3.96e-163 PDB 1GCD 'Refined Crystal Structure Of "aged" And "non-Aged" Organophosphoryl Conjugates Of Gamma-Chymotrypsin' 100.00 245 99.57 99.57 3.96e-163 PDB 1GCT "Is Gamma-Chymotrypsin A Tetrapeptide Acyl-Enzyme Adduct Of Gamma- Chymotrypsin?" 56.96 131 99.24 99.24 4.85e-87 PDB 1GG6 "Crystal Stucture Of Gamma Chymotrypsin With N-Acetyl- Phenylalanine Trifluoromethyl Ketone Bound At The Active Site" 56.96 131 99.24 99.24 4.85e-87 PDB 1GGD "Crystal Stucture Of Gamma Chymotrypsin With N-Acetyl-Leucil- Phenylalanine Aldehyde Bound At The Active Site" 56.96 131 99.24 99.24 4.85e-87 PDB 1GHA "A Second Active Site In Chymotrypsin? The X-Ray Crystal Structure Of N-Acetyl-D-Tryptophan Bound To Gamma-Chymotrypsin" 56.96 131 99.24 99.24 4.85e-87 PDB 1GHB "A Second Active Site In Chymotrypsin? The X-Ray Crystal Structure Of N-Acetyl-D-Tryptophan Bound To Gamma-Chymotrypsin" 56.96 131 99.24 99.24 4.85e-87 PDB 1GL0 "Structure Of The Complex Between Bovine Alpha-Chymotrypsin And Pmp-D2v, An Inhibitor From The Insect Locusta Migratoria" 100.00 245 99.57 99.57 3.96e-163 PDB 1GL1 "Structure Of The Complex Between Bovine Alpha-Chymotrypsin And Pmp-C, An Inhibitor From The Insect Locusta Migratoria" 100.00 245 99.57 99.57 3.96e-163 PDB 1GMC "The X-Ray Crystal Structure Of The Tetrahedral Intermediate Of Gamma- Chymotrypsin In Hexane" 56.96 131 99.24 99.24 4.85e-87 PDB 1GMD "X-ray Crystal Structure Of Gamma-chymotrypsin In Hexane" 56.96 131 99.24 99.24 4.85e-87 PDB 1GMH 'Refined Crystal Structure Of "aged" And "non-Aged" Organophosphoryl Conjugates Of Gamma-Chymotrypsin' 56.96 131 99.24 99.24 4.85e-87 PDB 1HJA "Lys 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Alpha-Chymotrypsin" 56.96 131 99.24 99.24 4.85e-87 PDB 1K2I "Crystal Structure Of Gamma-Chymotrypsin In Complex With 7- Hydroxycoumarin" 100.00 245 99.57 99.57 3.96e-163 PDB 1MTN "Bovine Alpha-Chymotrypsin:bpti Crystallization" 56.96 131 99.24 99.24 4.85e-87 PDB 1N8O "Crystal Structure Of A Complex Between Bovine Chymotrypsin And Ecotin" 56.96 131 99.24 99.24 4.85e-87 PDB 1OXG "Crystal Structure Of A Complex Formed Between Organic Solvent Treated Bovine Alpha-Chymotrypsin And Its Autocatalytically Produ" 100.00 245 99.57 99.57 3.96e-163 PDB 1P2M "Structural Consequences Of Accommodation Of Four Non- Cognate Amino-Acid Residues In The S1 Pocket Of Bovine Trypsin And Chymot" 100.00 245 99.57 99.57 3.96e-163 PDB 1P2N "Structural Consequences Of Accommodation Of Four Non- Cognate Amino-acid Residues In The S1 Pocket Of Bovine Trypsin And Chymot" 100.00 245 99.57 99.57 3.96e-163 PDB 1P2O "Structural Consequences Of Accommodation Of Four Non- Cognate Amino-Acid Residues In The S1 Pocket Of Bovine Trypsin And Chymot" 100.00 245 99.57 99.57 3.96e-163 PDB 1P2Q "Structural Consequences Of Accommodation Of Four Non- Cognate Amino-Acid Residues In The S1 Pocket Of Bovine Trypsin And Chymot" 100.00 245 99.57 99.57 3.96e-163 PDB 1T7C "Crystal Structure Of The P1 Glu Bpti Mutant- Bovine Chymotrypsin Complex" 100.00 245 99.57 99.57 3.96e-163 PDB 1T8L "Crystal Structure Of The P1 Met Bpti Mutant- Bovine Chymotrypsin Complex" 100.00 245 99.57 99.57 3.96e-163 PDB 1T8M "Crystal Structure Of The P1 His Bpti Mutant- Bovine Chymotrypsin Complex" 100.00 245 99.57 99.57 3.96e-163 PDB 1T8N "Crystal Structure Of The P1 Thr Bpti Mutant- Bovine Chymotrypsin Complex" 100.00 245 99.57 99.57 3.96e-163 PDB 1T8O "Crystal Structure Of The P1 Trp Bpti Mutant- Bovine Chymotrypsin Complex" 100.00 245 99.57 99.57 3.96e-163 PDB 1VGC "Gamma-Chymotrypsin L-Para-Chloro-1-Acetamido Boronic Acid Inhibitor Complex" 56.96 131 99.24 99.24 4.85e-87 PDB 1YPH "High Resolution Structure Of Bovine Alpha-Chymotrypsin" 56.96 131 99.24 99.24 4.85e-87 PDB 2CGA "Bovine Chymotrypsinogen A. X-Ray Crystal Structure Analysis And Refinement Of A New Crystal Form At 1.8 Angstroms Resolution" 100.00 245 99.57 99.57 3.96e-163 PDB 2CHA "The Structure Of Crystalline Alpha-Chymotrypsin, v.The Atomic Structure Of Tosyl-Alpha-Chymotrypsin At 2 Angstroms Resolution" 56.96 131 99.24 99.24 4.85e-87 PDB 2GCH "Refined Crystal Structure Of Gamma-chymotrypsin At 1.9 Angstroms Resolution" 56.96 131 99.24 99.24 4.85e-87 PDB 2GCT "Structure Of Gamma-Chymotrypsin In The Range Ph 2.0 To Ph 10.5 Suggests That Gamma-Chymotrypsin Is A Covalent Acyl-Enzyme Adduc" 56.96 131 99.24 99.24 4.85e-87 PDB 2GMT "Three-Dimensional Structure Of Chymotrypsin Inactivated With (2s) N- Acetyl-L-Alanyl-L-Phenylalanyl-Chloroethyl Ketone: Implica" 56.96 131 99.24 99.24 4.85e-87 PDB 2P8O "Crystal Structure Of A Benzohydroxamic AcidVANADATE Complex Bound To Chymotrypsin A" 56.96 131 99.24 99.24 4.85e-87 PDB 2VGC "Gamma-Chymotrypsin D-Para-Chloro-1-Acetamido Boronic Acid Inhibitor Complex" 56.96 131 99.24 99.24 4.85e-87 PDB 2Y6T "Molecular Recognition Of Chymotrypsin By The Serine Protease Inhibitor Ecotin From Yersinia Pestis" 100.00 245 99.57 99.57 3.96e-163 PDB 3BG4 "The Crystal Structure Of Guamerin In Complex With Chymotrypsin And The Development Of An Elastase-Specific Inhibitor" 56.96 131 99.24 99.24 4.85e-87 PDB 3GCH "Chemistry Of Caged Enzymes. Binding Of Photoreversible Cinnamates To Chymotrypsin" 56.96 131 99.24 99.24 4.85e-87 PDB 3GCT "Structure Of Gamma-Chymotrypsin In The Range pH 2.0 To pH 10.5 Suggests That Gamma-Chymotrypsin Is A Covalent Acyl-Enzyme Adduc" 56.96 131 99.24 99.24 4.85e-87 PDB 3RU4 "Crystal Structure Of The Bowman-Birk Serine Protease Inhibitor Btci In Complex With Trypsin And Chymotrypsin" 56.96 131 99.24 99.24 4.85e-87 PDB 3T62 "Crystal Structure Of Recombinant Kunitz Type Serine Protease Inhibitor-1 From The Caribbean Sea Anemone Stichodactyla Helianthu" 100.00 245 99.57 99.57 3.96e-163 PDB 3VGC "Gamma-Chymotrypsin L-Naphthyl-1-Acetamido Boronic Acid Acid Inhibitor Complex" 56.96 131 99.24 99.24 4.85e-87 PDB 4CHA "Structure Of Alpha-Chymotrypsin Refined At 1.68 Angstroms Resolution" 56.96 131 99.24 99.24 4.85e-87 PDB 4GCH "Structure And Activity Of Two Photoreversible Cinnamates Bound To Chymotrypsin" 56.96 131 99.24 99.24 4.85e-87 PDB 4Q2K "Bovine Alpha Chymotrypsin Bound To A Cyclic Peptide Inhibitor, 5b" 100.00 245 99.57 99.57 3.96e-163 PDB 4VGC "Gamma-Chymotrypsin D-Naphthyl-1-Acetamido Boronic Acid Inhibitor Complex" 56.96 131 99.24 99.24 4.85e-87 PDB 5CHA "The Refinement And The Structure Of The Dimer Of Alpha- Chymotrypsin At 1.67-Angstroms Resolution" 56.96 131 99.24 99.24 4.85e-87 PDB 5GCH "Chemistry Of Caged Enzymes II. Photoactivation Of Inhibited Chymotrypsin" 56.96 131 99.24 99.24 4.85e-87 PDB 6CHA "Structure Of A Tetrahedral Transition State Complex Of Alpha-Chymotrypsin At 1.8-Angstroms Resolution" 56.96 131 99.24 99.24 4.85e-87 PDB 6GCH "Structure Of Chymotrypsin-Trifluoromethyl Ketone Inhibitor Complexes. Comparison Of Slowly And Rapidly Equilibrating Inhibitors" 56.96 131 99.24 99.24 4.85e-87 PDB 7GCH "Structure Of Chymotrypsin-Trifluoromethyl Ketone Inhibitor Complexes. Comparison Of Slowly And Rapidly Equilibrating Inhibitors" 56.96 131 99.24 99.24 4.85e-87 PDB 8GCH "Gamma-Chymotrypsin Is A Complex Of Alpha-Chymotrypsin With Its Own Autolysis Products" 56.96 131 99.24 99.24 4.85e-87 REF XP_003583409 "PREDICTED: chymotrypsinogen A [Bos taurus]" 100.00 300 99.57 99.57 7.60e-163 REF XP_003587247 "PREDICTED: chymotrypsinogen A [Bos taurus]" 100.00 300 99.57 99.57 7.60e-163 REF XP_005894372 "PREDICTED: chymotrypsinogen A-like [Bos mutus]" 100.00 263 97.83 98.70 1.43e-159 SP P00766 "RecName: Full=Chymotrypsinogen A; Contains: RecName: Full=Chymotrypsin A chain A; Contains: RecName: Full=Chymotrypsin A chain " 100.00 245 99.57 99.57 3.96e-163 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $chymotrypsin 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 $chymotrypsin 'not available' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 9.5 . na temperature 277 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _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 _Indirect_shift_ratio_citation_label _Correction_value_citation_label DSS H . . ppm 0 . . . . . $entry_citation $entry_citation 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_assignment_data_set_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_condition_set_one _Chem_shift_reference_set_label $chem_shift_reference_par_set_one _Mol_system_component_name chymotrypsin _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 . 42 HIS HD1 H 15.9 . 1 stop_ save_