data_4865 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, 15N Chemical shift Assignment for OMTKY3 bound to bovine Chymotrypsin Aa ; _BMRB_accession_number 4865 _BMRB_flat_file_name bmr4865.str _Entry_type original _Submission_date 2000-10-17 _Accession_date 2000-10-18 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Song Jikui . . 2 Markley John L . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 45 "13C chemical shifts" 85 "15N chemical shifts" 46 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2001-06-01 update author 'update of publication' 2000-12-01 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 4864 'free form' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; NMR Chemical shift mapping of the binding site of a protein proteinase inhibitor: changes in the 1H, 13C and 15N NMR chemical shifts of turkey ovomucoid third domain upon binding to bovine chymotrypsin Aa ; _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 Song Jikui . . 2 Markley John L . stop_ _Journal_abbreviation 'J. Mol. Recognit.' _Journal_volume 14 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 166 _Page_last 171 _Year 2001 _Details . loop_ _Keyword 'OMTKY3:CTR complex' stop_ save_ ################################## # Molecular system description # ################################## save_system_OMTKY3_CTR _Saveframe_category molecular_system _Mol_system_name 'Turkey Ovomucoid Third Domain bound to bovine chymotrypsin Aa' _Abbreviation_common OMTKY3_CTR _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label OMTKY3 $OMTKY3_CTR 'bovine chymotrypsin Aa' $BCAa stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state monomer _System_paramagnetic no _System_thiol_state 'all disulfide bound' _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_OMTKY3_CTR _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'Ovomucoid Third Domain from Turkey' _Abbreviation_common OMTKY3 _Molecular_mass . _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 56 _Mol_residue_sequence ; LAAVSVDCSEYPKPACTLEY RPLCGSDNKTYGNKCNFCNA VVESNGTLTLSHFGKC ; loop_ _Residue_seq_code _Residue_label 1 LEU 2 ALA 3 ALA 4 VAL 5 SER 6 VAL 7 ASP 8 CYS 9 SER 10 GLU 11 TYR 12 PRO 13 LYS 14 PRO 15 ALA 16 CYS 17 THR 18 LEU 19 GLU 20 TYR 21 ARG 22 PRO 23 LEU 24 CYS 25 GLY 26 SER 27 ASP 28 ASN 29 LYS 30 THR 31 TYR 32 GLY 33 ASN 34 LYS 35 CYS 36 ASN 37 PHE 38 CYS 39 ASN 40 ALA 41 VAL 42 VAL 43 GLU 44 SER 45 ASN 46 GLY 47 THR 48 LEU 49 THR 50 LEU 51 SER 52 HIS 53 PHE 54 GLY 55 LYS 56 CYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-01-21 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 6881 bovine_alpha_chymotrypsin 100.00 241 99.59 99.59 1.07e-171 BMRB 960 "chymotrypsinogen A" 101.66 245 97.96 97.96 8.14e-168 BMRB 961 chymotrypsin 95.44 230 98.70 98.70 7.27e-160 BMRB 962 "chymotrypsinogen A" 101.66 245 97.96 97.96 8.14e-168 BMRB 963 chymotrypsin 95.44 230 98.70 98.70 7.27e-160 BMRB 964 "chymotrypsinogen A" 101.66 245 97.96 97.96 8.14e-168 BMRB 965 chymotrypsin 95.44 230 98.70 98.70 7.27e-160 BMRB 966 "chymotrypsinogen A" 101.66 245 97.96 97.96 8.14e-168 BMRB 967 chymotrypsin 95.44 230 98.70 98.70 7.27e-160 PDB 1AB9 "Crystal Structure Of Bovine Gamma-Chymotrypsin" 54.36 131 100.00 100.00 1.69e-87 PDB 1ACB "Crystal And Molecular Structure Of The Bovine Alpha-Chymotrypsin-Eglin C Complex At 2.0 Angstroms Resolution" 101.66 245 98.37 98.37 1.84e-168 PDB 1AFQ "Crystal Structure Of Bovine Gamma-Chymotrypsin Complexed With A Synthetic Inhibitor" 54.36 131 100.00 100.00 1.69e-87 PDB 1CA0 "Bovine Chymotrypsin Complexed To Appi" 54.36 131 100.00 100.00 1.69e-87 PDB 1CBW "Bovine Chymotrypsin Complexed To Bpti" 54.36 131 100.00 100.00 1.69e-87 PDB 1CGI "Three-Dimensional Structure Of The Complexes Between Bovine ChymotrypsinogenA And Two Recombinant Variants Of Human Pancreatic " 101.66 245 98.37 98.37 1.84e-168 PDB 1CGJ "Three-Dimensional Structure Of The Complexes Between Bovine ChymotrypsinogenA And Two Recombinant Variants Of Human Pancreatic " 101.66 245 98.37 98.37 1.84e-168 PDB 1CHG "Chymotrypsinogen,2.5 Angstroms Crystal Structure, Comparison With Alpha-Chymotrypsin,And Implications For Zymogen Activation" 101.66 245 98.37 98.37 1.84e-168 PDB 1CHO "Crystal And Molecular Structures Of The Complex Of Alpha- Chymotrypsin With Its Inhibitor Turkey Ovomucoid Third Domain At 1.8 " 54.36 131 100.00 100.00 1.69e-87 PDB 1DLK "Crystal Structure Analysis Of Delta-Chymotrypsin Bound To A Peptidyl Chloromethyl Ketone Inhibitor" 95.44 230 99.13 99.13 1.38e-160 PDB 1EX3 "Crystal Structure Of Bovine Chymotrypsinogen A (Tetragonal)" 101.66 245 98.37 98.37 1.84e-168 PDB 1GCD 'Refined Crystal Structure Of "aged" And "non-Aged" Organophosphoryl Conjugates Of Gamma-Chymotrypsin' 101.66 245 98.37 98.37 1.84e-168 PDB 1GCT "Is Gamma-Chymotrypsin A Tetrapeptide Acyl-Enzyme Adduct Of Gamma- Chymotrypsin?" 54.36 131 100.00 100.00 1.69e-87 PDB 1GG6 "Crystal Stucture Of Gamma Chymotrypsin With N-Acetyl- Phenylalanine Trifluoromethyl Ketone Bound At The Active Site" 54.36 131 100.00 100.00 1.69e-87 PDB 1GGD "Crystal Stucture Of Gamma Chymotrypsin With N-Acetyl-Leucil- Phenylalanine Aldehyde Bound At The Active Site" 54.36 131 100.00 100.00 1.69e-87 PDB 1GHA "A Second Active Site In Chymotrypsin? The X-Ray Crystal Structure Of N-Acetyl-D-Tryptophan Bound To Gamma-Chymotrypsin" 54.36 131 100.00 100.00 1.69e-87 PDB 1GHB "A Second Active Site In Chymotrypsin? The X-Ray Crystal Structure Of N-Acetyl-D-Tryptophan Bound To Gamma-Chymotrypsin" 54.36 131 100.00 100.00 1.69e-87 PDB 1GL0 "Structure Of The Complex Between Bovine Alpha-Chymotrypsin And Pmp-D2v, An Inhibitor From The Insect Locusta Migratoria" 101.66 245 98.37 98.37 1.84e-168 PDB 1GL1 "Structure Of The Complex Between Bovine Alpha-Chymotrypsin And Pmp-C, An Inhibitor From The Insect Locusta Migratoria" 101.66 245 98.37 98.37 1.84e-168 PDB 1GMC "The X-Ray Crystal Structure Of The Tetrahedral Intermediate Of Gamma- Chymotrypsin In Hexane" 54.36 131 100.00 100.00 1.69e-87 PDB 1GMD "X-ray Crystal Structure Of Gamma-chymotrypsin In Hexane" 54.36 131 100.00 100.00 1.69e-87 PDB 1GMH 'Refined Crystal Structure Of "aged" And "non-Aged" Organophosphoryl Conjugates Of Gamma-Chymotrypsin' 54.36 131 100.00 100.00 1.69e-87 PDB 1HJA "Lys 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Alpha-Chymotrypsin" 54.36 131 100.00 100.00 1.69e-87 PDB 1K2I "Crystal Structure Of Gamma-Chymotrypsin In Complex With 7- Hydroxycoumarin" 101.66 245 98.37 98.37 1.84e-168 PDB 1MTN "Bovine Alpha-Chymotrypsin:bpti Crystallization" 54.36 131 100.00 100.00 1.69e-87 PDB 1N8O "Crystal Structure Of A Complex Between Bovine Chymotrypsin And Ecotin" 54.36 131 100.00 100.00 1.69e-87 PDB 1OXG "Crystal Structure Of A Complex Formed Between Organic Solvent Treated Bovine Alpha-Chymotrypsin And Its Autocatalytically Produ" 101.66 245 98.37 98.37 1.84e-168 PDB 1P2M "Structural Consequences Of Accommodation Of Four Non- Cognate Amino-Acid Residues In The S1 Pocket Of Bovine Trypsin And Chymot" 101.66 245 98.37 98.37 1.84e-168 PDB 1P2N "Structural Consequences Of Accommodation Of Four Non- Cognate Amino-acid Residues In The S1 Pocket Of Bovine Trypsin And Chymot" 101.66 245 98.37 98.37 1.84e-168 PDB 1P2O "Structural Consequences Of Accommodation Of Four Non- Cognate Amino-Acid Residues In The S1 Pocket Of Bovine Trypsin And Chymot" 101.66 245 98.37 98.37 1.84e-168 PDB 1P2Q "Structural Consequences Of Accommodation Of Four Non- Cognate Amino-Acid Residues In The S1 Pocket Of Bovine Trypsin And Chymot" 101.66 245 98.37 98.37 1.84e-168 PDB 1T7C "Crystal Structure Of The P1 Glu Bpti Mutant- Bovine Chymotrypsin Complex" 101.66 245 98.37 98.37 1.84e-168 PDB 1T8L "Crystal Structure Of The P1 Met Bpti Mutant- Bovine Chymotrypsin Complex" 101.66 245 98.37 98.37 1.84e-168 PDB 1T8M "Crystal Structure Of The P1 His Bpti Mutant- Bovine Chymotrypsin Complex" 101.66 245 98.37 98.37 1.84e-168 PDB 1T8N "Crystal Structure Of The P1 Thr Bpti Mutant- Bovine Chymotrypsin Complex" 101.66 245 98.37 98.37 1.84e-168 PDB 1T8O "Crystal Structure Of The P1 Trp Bpti Mutant- Bovine Chymotrypsin Complex" 101.66 245 98.37 98.37 1.84e-168 PDB 1VGC "Gamma-Chymotrypsin L-Para-Chloro-1-Acetamido Boronic Acid Inhibitor Complex" 54.36 131 100.00 100.00 1.69e-87 PDB 1YPH "High Resolution Structure Of Bovine Alpha-Chymotrypsin" 54.36 131 100.00 100.00 1.69e-87 PDB 2CGA "Bovine Chymotrypsinogen A. X-Ray Crystal Structure Analysis And Refinement Of A New Crystal Form At 1.8 Angstroms Resolution" 101.66 245 98.37 98.37 1.84e-168 PDB 2CHA "The Structure Of Crystalline Alpha-Chymotrypsin, v.The Atomic Structure Of Tosyl-Alpha-Chymotrypsin At 2 Angstroms Resolution" 54.36 131 100.00 100.00 1.69e-87 PDB 2GCH "Refined Crystal Structure Of Gamma-chymotrypsin At 1.9 Angstroms Resolution" 54.36 131 100.00 100.00 1.69e-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" 54.36 131 100.00 100.00 1.69e-87 PDB 2GMT "Three-Dimensional Structure Of Chymotrypsin Inactivated With (2s) N- Acetyl-L-Alanyl-L-Phenylalanyl-Chloroethyl Ketone: Implica" 54.36 131 100.00 100.00 1.69e-87 PDB 2P8O "Crystal Structure Of A Benzohydroxamic AcidVANADATE Complex Bound To Chymotrypsin A" 54.36 131 100.00 100.00 1.69e-87 PDB 2VGC "Gamma-Chymotrypsin D-Para-Chloro-1-Acetamido Boronic Acid Inhibitor Complex" 54.36 131 100.00 100.00 1.69e-87 PDB 2Y6T "Molecular Recognition Of Chymotrypsin By The Serine Protease Inhibitor Ecotin From Yersinia Pestis" 101.66 245 98.37 98.37 1.84e-168 PDB 3BG4 "The Crystal Structure Of Guamerin In Complex With Chymotrypsin And The Development Of An Elastase-Specific Inhibitor" 54.36 131 100.00 100.00 1.69e-87 PDB 3GCH "Chemistry Of Caged Enzymes. Binding Of Photoreversible Cinnamates To Chymotrypsin" 54.36 131 100.00 100.00 1.69e-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" 54.36 131 100.00 100.00 1.69e-87 PDB 3RU4 "Crystal Structure Of The Bowman-Birk Serine Protease Inhibitor Btci In Complex With Trypsin And Chymotrypsin" 54.36 131 100.00 100.00 1.69e-87 PDB 3T62 "Crystal Structure Of Recombinant Kunitz Type Serine Protease Inhibitor-1 From The Caribbean Sea Anemone Stichodactyla Helianthu" 101.66 245 98.37 98.37 1.84e-168 PDB 3VGC "Gamma-Chymotrypsin L-Naphthyl-1-Acetamido Boronic Acid Acid Inhibitor Complex" 54.36 131 100.00 100.00 1.69e-87 PDB 4CHA "Structure Of Alpha-Chymotrypsin Refined At 1.68 Angstroms Resolution" 54.36 131 100.00 100.00 1.69e-87 PDB 4GCH "Structure And Activity Of Two Photoreversible Cinnamates Bound To Chymotrypsin" 54.36 131 100.00 100.00 1.69e-87 PDB 4Q2K "Bovine Alpha Chymotrypsin Bound To A Cyclic Peptide Inhibitor, 5b" 101.66 245 98.37 98.37 1.84e-168 PDB 4VGC "Gamma-Chymotrypsin D-Naphthyl-1-Acetamido Boronic Acid Inhibitor Complex" 54.36 131 100.00 100.00 1.69e-87 PDB 5CHA "The Refinement And The Structure Of The Dimer Of Alpha- Chymotrypsin At 1.67-Angstroms Resolution" 54.36 131 100.00 100.00 1.69e-87 PDB 5GCH "Chemistry Of Caged Enzymes II. Photoactivation Of Inhibited Chymotrypsin" 54.36 131 100.00 100.00 1.69e-87 PDB 6CHA "Structure Of A Tetrahedral Transition State Complex Of Alpha-Chymotrypsin At 1.8-Angstroms Resolution" 54.36 131 100.00 100.00 1.69e-87 PDB 6GCH "Structure Of Chymotrypsin-Trifluoromethyl Ketone Inhibitor Complexes. Comparison Of Slowly And Rapidly Equilibrating Inhibitors" 54.36 131 100.00 100.00 1.69e-87 PDB 7GCH "Structure Of Chymotrypsin-Trifluoromethyl Ketone Inhibitor Complexes. Comparison Of Slowly And Rapidly Equilibrating Inhibitors" 54.36 131 100.00 100.00 1.69e-87 PDB 8GCH "Gamma-Chymotrypsin Is A Complex Of Alpha-Chymotrypsin With Its Own Autolysis Products" 54.36 131 100.00 100.00 1.69e-87 REF XP_003583409 "PREDICTED: chymotrypsinogen A [Bos taurus]" 101.66 300 98.37 98.37 5.58e-168 REF XP_003587247 "PREDICTED: chymotrypsinogen A [Bos taurus]" 101.66 300 98.37 98.37 5.58e-168 SP P00766 "RecName: Full=Chymotrypsinogen A; Contains: RecName: Full=Chymotrypsin A chain A; Contains: RecName: Full=Chymotrypsin A chain " 101.66 245 98.37 98.37 1.84e-168 stop_ save_ save_BCAa _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'bovine chymotrypsin Aa' _Abbreviation_common BCAa _Molecular_mass . _Mol_thiol_state 'not reported' _Details . _Residue_count 241 _Mol_residue_sequence ; CGVPAIQPVLSGLIVNGEEA VPGSWPWQVSLQDKTGFHFC GGSLINENWVVTAAHCGVTT SDVVVAGEFDQGSSSEKIQK LKIAKVFKNSKYNSLTINND ITLLKLSTAASFSQTVSAVC LPSASDDFAAGTTCVTTGWG LTRYANTPDRLQQASLPLLS NTNCKKYWGTKIKDAMICAG ASGVSSCMGDSGGPLVCKKN GAWTLVGIVSWGSSTCSTST PGVYARVTALVNWVQQTLAA N ; loop_ _Residue_seq_code _Residue_label 1 CYS 2 GLY 3 VAL 4 PRO 5 ALA 6 ILE 7 GLN 8 PRO 9 VAL 10 LEU 11 SER 12 GLY 13 LEU 14 ILE 15 VAL 16 ASN 17 GLY 18 GLU 19 GLU 20 ALA 21 VAL 22 PRO 23 GLY 24 SER 25 TRP 26 PRO 27 TRP 28 GLN 29 VAL 30 SER 31 LEU 32 GLN 33 ASP 34 LYS 35 THR 36 GLY 37 PHE 38 HIS 39 PHE 40 CYS 41 GLY 42 GLY 43 SER 44 LEU 45 ILE 46 ASN 47 GLU 48 ASN 49 TRP 50 VAL 51 VAL 52 THR 53 ALA 54 ALA 55 HIS 56 CYS 57 GLY 58 VAL 59 THR 60 THR 61 SER 62 ASP 63 VAL 64 VAL 65 VAL 66 ALA 67 GLY 68 GLU 69 PHE 70 ASP 71 GLN 72 GLY 73 SER 74 SER 75 SER 76 GLU 77 LYS 78 ILE 79 GLN 80 LYS 81 LEU 82 LYS 83 ILE 84 ALA 85 LYS 86 VAL 87 PHE 88 LYS 89 ASN 90 SER 91 LYS 92 TYR 93 ASN 94 SER 95 LEU 96 THR 97 ILE 98 ASN 99 ASN 100 ASP 101 ILE 102 THR 103 LEU 104 LEU 105 LYS 106 LEU 107 SER 108 THR 109 ALA 110 ALA 111 SER 112 PHE 113 SER 114 GLN 115 THR 116 VAL 117 SER 118 ALA 119 VAL 120 CYS 121 LEU 122 PRO 123 SER 124 ALA 125 SER 126 ASP 127 ASP 128 PHE 129 ALA 130 ALA 131 GLY 132 THR 133 THR 134 CYS 135 VAL 136 THR 137 THR 138 GLY 139 TRP 140 GLY 141 LEU 142 THR 143 ARG 144 TYR 145 ALA 146 ASN 147 THR 148 PRO 149 ASP 150 ARG 151 LEU 152 GLN 153 GLN 154 ALA 155 SER 156 LEU 157 PRO 158 LEU 159 LEU 160 SER 161 ASN 162 THR 163 ASN 164 CYS 165 LYS 166 LYS 167 TYR 168 TRP 169 GLY 170 THR 171 LYS 172 ILE 173 LYS 174 ASP 175 ALA 176 MET 177 ILE 178 CYS 179 ALA 180 GLY 181 ALA 182 SER 183 GLY 184 VAL 185 SER 186 SER 187 CYS 188 MET 189 GLY 190 ASP 191 SER 192 GLY 193 GLY 194 PRO 195 LEU 196 VAL 197 CYS 198 LYS 199 LYS 200 ASN 201 GLY 202 ALA 203 TRP 204 THR 205 LEU 206 VAL 207 GLY 208 ILE 209 VAL 210 SER 211 TRP 212 GLY 213 SER 214 SER 215 THR 216 CYS 217 SER 218 THR 219 SER 220 THR 221 PRO 222 GLY 223 VAL 224 TYR 225 ALA 226 ARG 227 VAL 228 THR 229 ALA 230 LEU 231 VAL 232 ASN 233 TRP 234 VAL 235 GLN 236 GLN 237 THR 238 LEU 239 ALA 240 ALA 241 ASN stop_ _Sequence_homology_query_date 2008-08-19 _Sequence_homology_query_revised_last_date 2008-08-19 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value SWISS-PROT P00766 'Chymotrypsinogen A [Contains: Chymotrypsin A chain A; Chymotrypsin A chain B; Chymotrypsin A chain C]' 101.66 245 98.37 98.37 4.53e-133 REF XP_608091 'PREDICTED: chymotrypsinogen B1 [Bos taurus]' 101.66 300 98.37 98.37 2.34e-133 PDB 8GCH 'Gamma-Chymotrypsin Is A Complex Of Alpha-Chymotrypsin With Its Own Autolysis Products' 54.36 131 100.00 100.00 6.71e-70 PDB 7GCH 'Structure Of Chymotrypsin-Trifluoromethyl Ketone Inhibitor Complexes. Comparison Of Slowly And Rapidly Equilibrating Inhibitors' 54.36 131 100.00 100.00 6.71e-70 PDB 6GCH 'Structure Of Chymotrypsin-Trifluoromethyl Ketone Inhibitor Complexes. Comparison Of Slowly And Rapidly Equilibrating Inhibitors' 54.36 131 100.00 100.00 6.71e-70 PDB 6CHA 'Structure Of A Tetrahedral Transition State Complex Of Alpha-Chymotrypsin At 1.8-Angstroms Resolution' 54.36 131 100.00 100.00 6.71e-70 PDB 5GCH 'Chemistry Of Caged Enzymes II. Photoactivation Of Inhibited Chymotrypsin' 54.36 131 100.00 100.00 6.71e-70 PDB 5CHA 'The Refinement And The Structure Of The Dimer Of Alpha- Chymotrypsin At 1.67-Angstroms Resolution' 54.36 131 100.00 100.00 6.71e-70 PDB 4VGC 'Gamma-Chymotrypsin D-Naphthyl-1-Acetamido Boronic Acid Inhibitor Complex' 54.36 131 100.00 100.00 6.71e-70 PDB 4GCH 'Structure And Activity Of Two Photoreversible Cinnamates Bound To Chymotrypsin' 54.36 131 100.00 100.00 6.71e-70 PDB 4CHA 'Structure Of Alpha-Chymotrypsin Refined At 1.68 Angstroms Resolution' 54.36 131 100.00 100.00 6.71e-70 PDB 3VGC 'Gamma-Chymotrypsin L-Naphthyl-1-Acetamido Boronic Acid Acid Inhibitor Complex' 54.36 131 100.00 100.00 6.71e-70 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 Adduct At Low pH' 54.36 131 100.00 100.00 6.71e-70 PDB 3GCH 'Chemistry Of Caged Enzymes. Binding Of Photoreversible Cinnamates To Chymotrypsin' 101.66 245 98.37 98.37 6.76e-133 PDB 3BG4 'The Crystal Structure Of Guamerin In Complex With Chymotrypsin And The Development Of An Elastase-Specific Inhibitor' 54.36 131 100.00 100.00 6.71e-70 PDB 2VGC 'Gamma-Chymotrypsin D-Para-Chloro-1-Acetamido Boronic Acid Inhibitor Complex' 54.36 131 100.00 100.00 6.71e-70 PDB 2P8O 'Crystal Structure Of A Benzohydroxamic AcidVANADATE Complex Bound To Chymotrypsin A' 54.36 131 100.00 100.00 6.71e-70 PDB 2GMT 'Three-Dimensional Structure Of Chymotrypsin Inactivated With (2s) N-Acetyl-L-Alanyl-L-Phenylalanyl-Chloroethyl Ketone: Implications For The Mechanism Of Inactivation Of Serine Proteases By Chloroketones' 101.66 245 98.37 98.37 6.76e-133 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 Adduct At Low Ph' 101.66 245 98.37 98.37 6.76e-133 PDB 2GCH 'Refined Crystal Structure Of Gamma-Chymotrypsin At 1.9 Angstroms Resolution' 54.36 131 100.00 100.00 6.71e-70 PDB 2CHA 'The Structure Of Crystalline Alpha-Chymotrypsin, v.The Atomic Structure Of Tosyl-Alpha-Chymotrypsin At 2 Angstroms Resolution' 54.36 131 100.00 100.00 6.71e-70 PDB 2CGA 'Bovine Chymotrypsinogen A. X-Ray Crystal Structure Analysis And Refinement Of A New Crystal Form At 1.8 Angstroms Resolution' 101.66 245 98.37 98.37 4.53e-133 PDB 1YPH 'High Resolution Structure Of Bovine Alpha-Chymotrypsin' 54.36 131 100.00 100.00 6.71e-70 PDB 1VGC 'Gamma-Chymotrypsin L-Para-Chloro-1-Acetamido Boronic Acid Inhibitor Complex' 54.36 131 100.00 100.00 6.71e-70 PDB 1T8O 'Crystal Structure Of The P1 Trp Bpti Mutant- Bovine Chymotrypsin Complex' 101.66 245 98.37 98.37 4.53e-133 PDB 1T8N 'Crystal Structure Of The P1 Thr Bpti Mutant- Bovine Chymotrypsin Complex' 101.66 245 98.37 98.37 4.53e-133 PDB 1T8M 'Crystal Structure Of The P1 His Bpti Mutant- Bovine Chymotrypsin Complex' 101.66 245 98.37 98.37 4.53e-133 PDB 1T8L 'Crystal Structure Of The P1 Met Bpti Mutant- Bovine Chymotrypsin Complex' 101.66 245 98.37 98.37 4.53e-133 PDB 1T7C 'Crystal Structure Of The P1 Glu Bpti Mutant- Bovine Chymotrypsin Complex' 101.66 245 98.37 98.37 4.53e-133 PDB 1P2Q 'Structural Consequences Of Accommodation Of Four Non- Cognate Amino-Acid Residues In The S1 Pocket Of Bovine Trypsin And Chymotrypsin' 101.66 245 98.37 98.37 4.53e-133 PDB 1P2O 'Structural Consequences Of Accommodation Of Four Non- Cognate Amino-Acid Residues In The S1 Pocket Of Bovine Trypsin And Chymotrypsin' 101.66 245 98.37 98.37 4.53e-133 PDB 1P2N 'Structural Consequences Of Accommodation Of Four Non- Cognate Amino-Acid Residues In The S1 Pocket Of Bovine Trypsin And Chymotrypsin' 101.66 245 98.37 98.37 4.53e-133 PDB 1P2M 'Structural Consequences Of Accommodation Of Four Non- Cognate Amino-Acid Residues In The S1 Pocket Of Bovine Trypsin And Chymotrypsin' 101.66 245 98.37 98.37 4.53e-133 PDB 1OXG 'Crystal Structure Of A Complex Formed Between Organic Solvent Treated Bovine Alpha-Chymotrypsin And Its Autocatalytically Produced Highly Potent 14-Residue Peptide At 2.2 Resolution' 101.66 245 98.37 98.37 4.53e-133 PDB 1N8O 'Crystal Structure Of A Complex Between Bovine Chymotrypsin And Ecotin' 54.36 131 100.00 100.00 6.71e-70 PDB 1MTN 'Bovine Alpha-Chymotrypsin:bpti Crystallization' 54.36 131 100.00 100.00 6.71e-70 PDB 1K2I 'Crystal Structure Of Gamma-Chymotrypsin In Complex With 7- Hydroxycoumarin' 101.66 245 98.37 98.37 4.53e-133 PDB 1HJA 'Lys 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Alpha-Chymotrypsin' 54.36 131 100.00 100.00 6.71e-70 PDB 1GMH 'Refined Crystal Structure Of "aged" And "non-Aged" Organophosphoryl Conjugates Of Gamma-Chymotrypsin' 54.36 131 100.00 100.00 6.71e-70 PDB 1GMD 'X-Ray Crystal Structure Of Gamma-Chymotrypsin In Hexane' 54.36 131 100.00 100.00 6.71e-70 PDB 1GMC 'The X-Ray Crystal Structure Of The Tetrahedral Intermediate Of Gamma-Chymotrypsin In Hexane' 54.36 131 100.00 100.00 6.71e-70 PDB 1GL1 'Structure Of The Complex Between Bovine Alpha-Chymotrypsin And Pmp-C, An Inhibitor From The Insect Locusta Migratoria' 101.66 245 98.37 98.37 4.53e-133 PDB 1GL0 'Structure Of The Complex Between Bovine Alpha-Chymotrypsin And Pmp-D2v, An Inhibitor From The Insect Locusta Migratoria' 101.66 245 98.37 98.37 4.53e-133 PDB 1GHB 'A Second Active Site In Chymotrypsin? The X-Ray Crystal Structure Of N-Acetyl-D-Tryptophan Bound To Gamma- Chymotrypsin' 101.66 245 98.37 98.37 6.76e-133 PDB 1GHA 'A Second Active Site In Chymotrypsin? The X-Ray Crystal Structure Of N-Acetyl-D-Tryptophan Bound To Gamma- Chymotrypsin' 54.36 131 100.00 100.00 6.71e-70 PDB 1GGD 'Crystal Stucture Of Gamma Chymotrypsin With N-Acetyl-Leucil- Phenylalanine Aldehyde Bound At The Active Site' 54.36 131 100.00 100.00 6.71e-70 PDB 1GG6 'Crystal Stucture Of Gamma Chymotrypsin With N-Acetyl- Phenylalanine Trifluoromethyl Ketone Bound At The Active Site' 54.36 131 100.00 100.00 6.71e-70 PDB 1GCT 'Is Gamma-Chymotrypsin A Tetrapeptide Acyl-Enzyme Adduct Of Gamma-Chymotrypsin?' 101.66 245 98.37 98.37 6.76e-133 PDB 1GCD 'Refined Crystal Structure Of "aged" And "non-Aged" Organophosphoryl Conjugates Of Gamma-Chymotrypsin' 101.66 245 98.37 98.37 4.53e-133 PDB 1EX3 'Crystal Structure Of Bovine Chymotrypsinogen A (Tetragonal)' 101.66 245 98.37 98.37 4.53e-133 PDB 1DLK 'Crystal Structure Analysis Of Delta-Chymotrypsin Bound To A Peptidyl Chloromethyl Ketone Inhibitor' 95.44 230 99.13 99.13 6.94e-127 PDB 1CHO 'Crystal And Molecular Structures Of The Complex Of Alpha- Chymotrypsin With Its Inhibitor Turkey Ovomucoid Third Domain At 1.8 Angstroms Resolution' 54.36 131 100.00 100.00 6.71e-70 PDB 1CHG 'Chymotrypsinogen,2.5 Angstroms Crystal Structure, Comparison With Alpha-Chymotrypsin,And Implications For Zymogen Activation' 101.66 245 98.37 98.37 4.53e-133 PDB 1CGJ 'Three-Dimensional Structure Of The Complexes Between Bovine ChymotrypsinogenA And Two Recombinant Variants Of Human Pancreatic Secretory Trypsin Inhibitor (Kazal-Type)' 101.66 245 98.37 98.37 4.53e-133 PDB 1CGI 'Three-Dimensional Structure Of The Complexes Between Bovine ChymotrypsinogenA And Two Recombinant Variants Of Human Pancreatic Secretory Trypsin Inhibitor (Kazal-Type)' 101.66 245 98.37 98.37 4.53e-133 PDB 1CBW 'Bovine Chymotrypsin Complexed To Bpti' 54.36 131 100.00 100.00 6.71e-70 PDB 1CA0 'Bovine Chymotrypsin Complexed To Appi' 54.36 131 100.00 100.00 6.71e-70 PDB 1AFQ 'Crystal Structure Of Bovine Gamma-Chymotrypsin Complexed With A Synthetic Inhibitor' 54.36 131 100.00 100.00 6.71e-70 PDB 1ACB 'Crystal And Molecular Structure Of The Bovine Alpha- Chymotrypsin-Eglin C Complex At 2.0 Angstroms Resolution' 101.66 245 98.37 98.37 4.53e-133 PDB 1AB9 'Crystal Structure Of Bovine Gamma-Chymotrypsin' 54.36 131 100.00 100.00 6.71e-70 BMRB 967 chymotrypsin 95.44 230 98.70 98.70 2.47e-126 BMRB 965 chymotrypsin 95.44 230 98.70 98.70 2.47e-126 BMRB 963 chymotrypsin 95.44 230 98.70 98.70 2.47e-126 BMRB 961 chymotrypsin 95.44 230 98.70 98.70 2.47e-126 BMRB 6881 'bovine alpha-chymotrypsin' 100.00 241 99.59 99.59 1.72e-135 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $OMTKY3_CTR Turkey 9103 Eukaryota Metazoa Meleagris Gallopavo $BCAa 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 $OMTKY3_CTR 'recombinant technology' . . . . . $BCAa 'purified from the natural source' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_Sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $OMTKY3_CTR 2 mM '[U-13C; U-15N]' $BCAa 2 mM . stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DMX _Field_strength 600 _Details . save_ ############################# # NMR applied experiments # ############################# save_HNCA_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _Sample_label . save_ save_HN(CO)CA_2 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _Sample_label . save_ save_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _Sample_label . save_ save_NMR_spec_expt__0_1 _Saveframe_category NMR_applied_experiment _Experiment_name HNCA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_2 _Saveframe_category NMR_applied_experiment _Experiment_name HN(CO)CA _BMRB_pulse_sequence_accession_number . _Details . save_ save_NMR_spec_expt__0_3 _Saveframe_category NMR_applied_experiment _Experiment_name HNCO _BMRB_pulse_sequence_accession_number . _Details . save_ ####################### # Sample conditions # ####################### save_condition_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 7.3 0.2 n/a temperature 298 1 K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS H 1 'methyl protons' ppm 0.0 internal direct . . . 1.0 DSS N 15 'methyl protons' ppm 0.0 . indirect . . . 0.101329118 DSS C 13 'methyl protons' ppm 0.0 . indirect . . . 0.251449530 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_shifts_OMTKY3_pH7.3 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label HNCA HN(CO)CA HNCO stop_ loop_ _Sample_label $Sample_1 stop_ _Sample_conditions_label $condition_1 _Chem_shift_reference_set_label $chemical_shift_reference _Mol_system_component_name OMTKY3 _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 . 8 CYS C C 176.88 0.1 1 2 . 8 CYS H H 8.88 0.05 1 3 . 8 CYS N N 126.88 0.1 1 4 . 9 SER C C 175.63 0.1 1 5 . 9 SER CA C 62.30 0.1 1 6 . 9 SER H H 8.72 0.05 1 7 . 9 SER N N 120.51 0.1 1 8 . 10 GLU C C 174.32 0.1 1 9 . 10 GLU CA C 56.82 0.1 1 10 . 10 GLU H H 8.87 0.05 1 11 . 10 GLU N N 119.92 0.1 1 12 . 11 TYR CA C 58.19 0.1 1 13 . 11 TYR H H 7.50 0.05 1 14 . 11 TYR N N 119.83 0.1 1 15 . 12 PRO C C 175.51 0.1 1 16 . 12 PRO CA C 62.23 0.1 1 17 . 13 LYS CA C 53.88 0.1 1 18 . 13 LYS H H 9.52 0.05 1 19 . 13 LYS N N 120.66 0.1 1 20 . 14 PRO C C 175.06 0.1 1 21 . 14 PRO CA C 63.24 0.1 1 22 . 15 ALA C C 176.08 0.1 1 23 . 15 ALA CA C 50.02 0.1 1 24 . 15 ALA H H 7.29 0.05 1 25 . 15 ALA N N 123.93 0.1 1 26 . 16 CYS C C 175.52 0.1 1 27 . 16 CYS CA C 51.30 0.1 1 28 . 16 CYS H H 8.87 0.05 1 29 . 16 CYS N N 116.23 0.1 1 30 . 17 THR C C 176.41 0.1 1 31 . 17 THR CA C 62.62 0.1 1 32 . 17 THR H H 7.77 0.05 1 33 . 17 THR N N 111.47 0.1 1 34 . 18 LEU CA C 55.20 0.1 1 35 . 18 LEU H H 8.21 0.05 1 36 . 18 LEU N N 120.10 0.1 1 37 . 19 GLU C C 175.10 0.1 1 38 . 19 GLU H H 7.95 0.05 1 39 . 19 GLU N N 131.45 0.1 1 40 . 20 TYR CA C 57.02 0.1 1 41 . 20 TYR H H 9.11 0.05 1 42 . 20 TYR N N 123.99 0.1 1 43 . 21 ARG HE H 6.98 0.05 1 44 . 21 ARG NE N 116.38 0.1 1 45 . 23 LEU C C 173.68 0.1 1 46 . 24 CYS C C 175.63 0.1 1 47 . 24 CYS CA C 54.48 0.1 1 48 . 24 CYS H H 8.22 0.05 1 49 . 24 CYS N N 121.90 0.1 1 50 . 25 GLY C C 174.86 0.1 1 51 . 25 GLY CA C 45.38 0.1 1 52 . 25 GLY H H 9.39 0.05 1 53 . 25 GLY N N 116.69 0.1 1 54 . 26 SER C C 173.80 0.1 1 55 . 26 SER CA C 60.87 0.1 1 56 . 26 SER H H 9.36 0.05 1 57 . 26 SER N N 119.15 0.1 1 58 . 27 ASP C C 176.27 0.1 1 59 . 27 ASP CA C 53.11 0.1 1 60 . 27 ASP H H 8.44 0.05 1 61 . 27 ASP N N 122.47 0.1 1 62 . 28 ASN C C 173.74 0.1 1 63 . 28 ASN CA C 55.00 0.1 1 64 . 28 ASN H H 8.66 0.05 1 65 . 28 ASN N N 117.01 0.1 1 66 . 29 LYS C C 174.43 0.1 1 67 . 29 LYS CA C 55.00 0.1 1 68 . 29 LYS H H 7.89 0.05 1 69 . 29 LYS N N 120.80 0.1 1 70 . 30 THR C C 174.57 0.1 1 71 . 30 THR CA C 62.58 0.1 1 72 . 30 THR H H 8.19 0.05 1 73 . 30 THR N N 122.19 0.1 1 74 . 31 TYR C C 176.93 0.1 1 75 . 31 TYR CA C 58.14 0.1 1 76 . 31 TYR H H 9.75 0.05 1 77 . 31 TYR N N 131.16 0.1 1 78 . 32 GLY C C 171.36 0.1 1 79 . 32 GLY CA C 47.91 0.1 1 80 . 32 GLY H H 9.09 0.05 1 81 . 32 GLY N N 110.28 0.1 1 82 . 33 ASN C C 175.93 0.1 1 83 . 33 ASN CA C 51.83 0.1 1 84 . 33 ASN H H 7.77 0.05 1 85 . 33 ASN N N 109.99 0.1 1 86 . 33 ASN ND2 N 118.60 0.1 1 87 . 34 LYS C C 175.81 0.1 1 88 . 34 LYS CA C 60.22 0.1 1 89 . 34 LYS H H 9.01 0.05 1 90 . 34 LYS N N 119.93 0.1 1 91 . 35 CYS C C 175.84 0.1 1 92 . 35 CYS CA C 58.24 0.1 1 93 . 35 CYS H H 8.14 0.05 1 94 . 35 CYS N N 122.46 0.1 1 95 . 36 ASN C C 178.32 0.1 1 96 . 36 ASN CA C 56.41 0.1 1 97 . 36 ASN H H 8.40 0.05 1 98 . 36 ASN N N 118.95 0.1 1 99 . 37 PHE C C 175.94 0.1 1 100 . 37 PHE CA C 61.23 0.1 1 101 . 37 PHE H H 8.53 0.05 1 102 . 37 PHE N N 119.85 0.1 1 103 . 38 CYS C C 177.64 0.1 1 104 . 38 CYS CA C 55.34 0.1 1 105 . 38 CYS H H 9.13 0.05 1 106 . 38 CYS N N 117.91 0.1 1 107 . 39 ASN C C 177.48 0.1 1 108 . 39 ASN CA C 56.33 0.1 1 109 . 39 ASN H H 8.02 0.05 1 110 . 39 ASN N N 120.38 0.1 1 111 . 40 ALA C C 181.16 0.1 1 112 . 40 ALA CA C 54.82 0.1 1 113 . 40 ALA H H 7.44 0.05 1 114 . 40 ALA N N 125.30 0.1 1 115 . 41 VAL C C 181.44 0.1 1 116 . 41 VAL CA C 66.82 0.1 1 117 . 41 VAL H H 8.57 0.05 1 118 . 41 VAL N N 124.35 0.1 1 119 . 42 VAL C C 179.28 0.1 1 120 . 42 VAL CA C 66.00 0.1 1 121 . 42 VAL H H 7.94 0.05 1 122 . 42 VAL N N 120.29 0.1 1 123 . 43 GLU C C 177.04 0.1 1 124 . 43 GLU CA C 58.34 0.1 1 125 . 43 GLU H H 7.76 0.05 1 126 . 43 GLU N N 122.39 0.1 1 127 . 44 SER C C 175.55 0.1 1 128 . 44 SER CA C 59.13 0.1 1 129 . 44 SER H H 7.83 0.05 1 130 . 44 SER N N 114.43 0.1 1 131 . 45 ASN C C 175.51 0.1 1 132 . 45 ASN CA C 54.27 0.1 1 133 . 45 ASN H H 8.49 0.05 1 134 . 45 ASN N N 121.77 0.1 1 135 . 46 GLY C C 174.97 0.1 1 136 . 46 GLY CA C 45.71 0.1 1 137 . 46 GLY H H 8.01 0.05 1 138 . 46 GLY N N 104.48 0.1 1 139 . 47 THR CA C 63.19 0.1 1 140 . 47 THR H H 7.61 0.05 1 141 . 47 THR N N 111.88 0.1 1 142 . 48 LEU C C 174.58 0.1 1 143 . 48 LEU CA C 55.45 0.1 1 144 . 48 LEU H H 7.75 0.05 1 145 . 48 LEU N N 126.01 0.1 1 146 . 49 THR C C 173.22 0.1 1 147 . 49 THR CA C 59.31 0.1 1 148 . 49 THR H H 8.56 0.05 1 149 . 49 THR N N 117.18 0.1 1 150 . 50 LEU C C 176.59 0.1 1 151 . 50 LEU CA C 54.74 0.1 1 152 . 50 LEU H H 8.73 0.05 1 153 . 50 LEU N N 123.16 0.1 1 154 . 51 SER C C 174.98 0.1 1 155 . 51 SER CA C 60.35 0.1 1 156 . 51 SER H H 8.91 0.05 1 157 . 51 SER N N 124.02 0.1 1 158 . 52 HIS C C 173.06 0.1 1 159 . 52 HIS CA C 55.03 0.1 1 160 . 52 HIS H H 7.24 0.05 1 161 . 52 HIS N N 109.96 0.1 1 162 . 53 PHE C C 177.04 0.1 1 163 . 53 PHE CA C 60.18 0.1 1 164 . 53 PHE H H 8.94 0.05 1 165 . 53 PHE N N 120.69 0.1 1 166 . 54 GLY C C 170.64 0.1 1 167 . 54 GLY CA C 44.05 0.1 1 168 . 54 GLY H H 8.26 0.05 1 169 . 54 GLY N N 114.86 0.1 1 170 . 55 LYS C C 178.21 0.1 1 171 . 55 LYS CA C 56.19 0.1 1 172 . 55 LYS H H 7.81 0.05 1 173 . 55 LYS N N 114.02 0.1 1 174 . 56 CYS CA C 55.75 0.1 1 175 . 56 CYS H H 8.19 0.05 1 176 . 56 CYS N N 125.54 0.1 1 stop_ save_