data_960 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 960 _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 ; _Entry.Type macromolecule _Entry.Version_type update _Entry.Submission_date 1995-07-31 _Entry.Accession_date 1996-03-25 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination BMRB _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version 2.1 _Entry.Experimental_method NMR _Entry.Experimental_method_subtype . _Entry.Details . _Entry.BMRB_internal_directory_name . loop_ _Entry_author.Ordinal _Entry_author.Given_name _Entry_author.Family_name _Entry_author.First_initial _Entry_author.Middle_initials _Entry_author.Family_title _Entry_author.Entry_ID 1 G. Robillard . . . 960 2 R. Shulman . G. . 960 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 960 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 1 960 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 4 . . 2010-06-11 . revision BMRB 'Complete natural source information' 960 3 . . 1999-06-14 . revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 960 2 . . 1996-03-25 . reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 960 1 . . 1995-07-31 . original BMRB 'Last release in original BMRB flat-file format' 960 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 960 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; 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 _Citation.Journal_abbrev 'J. Mol. Biol.' _Citation.Journal_name_full . _Citation.Journal_volume 86 _Citation.Journal_issue . _Citation.Journal_ASTM . _Citation.Journal_ISSN . _Citation.Journal_CSD . _Citation.Book_title . _Citation.Book_chapter_title . _Citation.Book_volume . _Citation.Book_series . _Citation.Book_publisher . _Citation.Book_publisher_city . _Citation.Book_ISBN . _Citation.Conference_title . _Citation.Conference_site . _Citation.Conference_state_province . _Citation.Conference_country . _Citation.Conference_start_date . _Citation.Conference_end_date . _Citation.Conference_abstract_number . _Citation.Thesis_institution . _Citation.Thesis_institution_city . _Citation.Thesis_institution_country . _Citation.WWW_URL . _Citation.Page_first 541 _Citation.Page_last 558 _Citation.Year 1974 _Citation.Details . loop_ _Citation_author.Ordinal _Citation_author.Given_name _Citation_author.Family_name _Citation_author.First_initial _Citation_author.Middle_initials _Citation_author.Family_title _Citation_author.Entry_ID _Citation_author.Citation_ID 1 G. Robillard . . . 960 1 2 R. Shulman . G. . 960 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_chymotrypsinogen_A _Assembly.Sf_category assembly _Assembly.Sf_framecode system_chymotrypsinogen_A _Assembly.Entry_ID 960 _Assembly.ID 1 _Assembly.Name 'chymotrypsinogen A' _Assembly.BMRB_code . _Assembly.Number_of_components . _Assembly.Organic_ligands . _Assembly.Metal_ions . _Assembly.Non_standard_bonds . _Assembly.Ambiguous_conformational_states . _Assembly.Ambiguous_chem_comp_sites . _Assembly.Molecules_in_chemical_exchange . _Assembly.Paramagnetic . _Assembly.Thiol_state . _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Entity_assembly.ID _Entity_assembly.Entity_assembly_name _Entity_assembly.Entity_ID _Entity_assembly.Entity_label _Entity_assembly.Asym_ID _Entity_assembly.PDB_chain_ID _Entity_assembly.Experimental_data_reported _Entity_assembly.Physical_state _Entity_assembly.Conformational_isomer _Entity_assembly.Chemical_exchange_state _Entity_assembly.Magnetic_equivalence_group_code _Entity_assembly.Role _Entity_assembly.Details _Entity_assembly.Entry_ID _Entity_assembly.Assembly_ID 1 'chymotrypsinogen A' 1 $chymotrypsinogen_A . . . . . . . . . 960 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'chymotrypsinogen A' system 960 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_chymotrypsinogen_A _Entity.Sf_category entity _Entity.Sf_framecode chymotrypsinogen_A _Entity.Entry_ID 960 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'chymotrypsinogen A' _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can ; CGVPAIQPVLSGLSRIVNGE EAVPGSWPWQVSLQDKTGFH FCGGSLINENWVVTAAHCGV TTSDVVVAGEFDQGSSSEKI QKLKIAKVFKNSKYNSLTIN NDITLLKLSTAASFSQTVSA VCLPSASDDFAAGTTCVVTG WGLTRYTNANTPDRLQQASL PLLSNTNCKKYWGTKIKDAM ICAGASGVSSCMGDSGGPLV CKKNGAWTLVGIVSWGSSTC STSTPGVYARVTALVNWVQQ TLAAN ; _Entity.Polymer_seq_one_letter_code ; CGVPAIQPVLSGLSRIVNGE EAVPGSWPWQVSLQDKTGFH FCGGSLINENWVVTAAHCGV TTSDVVVAGEFDQGSSSEKI QKLKIAKVFKNSKYNSLTIN NDITLLKLSTAASFSQTVSA VCLPSASDDFAAGTTCVVTG WGLTRYTNANTPDRLQQASL PLLSNTNCKKYWGTKIKDAM ICAGASGVSSCMGDSGGPLV CKKNGAWTLVGIVSWGSSTC STSTPGVYARVTALVNWVQQ TLAAN ; _Entity.Target_identifier . _Entity.Polymer_author_defined_seq . _Entity.Polymer_author_seq_details . _Entity.Ambiguous_conformational_states . _Entity.Ambiguous_chem_comp_sites . _Entity.Nstd_monomer . _Entity.Nstd_chirality . _Entity.Nstd_linkage . _Entity.Nonpolymer_comp_ID . _Entity.Nonpolymer_comp_label . _Entity.Number_of_monomers 245 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state . _Entity.Src_method . _Entity.Parent_entity_ID 1 _Entity.Fragment . _Entity.Mutation . _Entity.EC_number 3.4.21.1 _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-28 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 4865 . BCAa . . . . . 100.00 241 97.96 97.96 1.18e-167 . . . . 960 1 2 no BMRB 6881 . bovine_alpha_chymotrypsin . . . . . 100.00 241 97.96 97.96 1.34e-167 . . . . 960 1 3 no BMRB 961 . chymotrypsin . . . . . 93.88 230 100.00 100.00 1.10e-163 . . . . 960 1 4 no BMRB 962 . "chymotrypsinogen A" . . . . . 100.00 245 100.00 100.00 3.51e-175 . . . . 960 1 5 no BMRB 963 . chymotrypsin . . . . . 93.88 230 100.00 100.00 1.10e-163 . . . . 960 1 6 no BMRB 964 . "chymotrypsinogen A" . . . . . 100.00 245 100.00 100.00 3.51e-175 . . . . 960 1 7 no BMRB 965 . chymotrypsin . . . . . 93.88 230 100.00 100.00 1.10e-163 . . . . 960 1 8 no BMRB 966 . "chymotrypsinogen A" . . . . . 100.00 245 100.00 100.00 3.51e-175 . . . . 960 1 9 no BMRB 967 . chymotrypsin . . . . . 93.88 230 100.00 100.00 1.10e-163 . . . . 960 1 10 no PDB 1AB9 . "Crystal Structure Of Bovine Gamma-Chymotrypsin" . . . . . 53.47 131 99.24 99.24 1.42e-86 . . . . 960 1 11 no PDB 1ACB . "Crystal And Molecular Structure Of The Bovine Alpha-Chymotrypsin-Eglin C Complex At 2.0 Angstroms Resolution" . . . . . 100.00 245 99.59 99.59 1.36e-174 . . . . 960 1 12 no PDB 1AFQ . "Crystal Structure Of Bovine Gamma-Chymotrypsin Complexed With A Synthetic Inhibitor" . . . . . 53.47 131 99.24 99.24 1.42e-86 . . . . 960 1 13 no PDB 1CA0 . "Bovine Chymotrypsin Complexed To Appi" . . . . . 53.47 131 99.24 99.24 1.42e-86 . . . . 960 1 14 no PDB 1CBW . "Bovine Chymotrypsin Complexed To Bpti" . . . . . 53.47 131 99.24 99.24 1.42e-86 . . . . 960 1 15 no PDB 1CGI . "Three-Dimensional Structure Of The Complexes Between Bovine ChymotrypsinogenA And Two Recombinant Variants Of Human Pancreatic " . . . . . 100.00 245 99.59 99.59 1.36e-174 . . . . 960 1 16 no PDB 1CGJ . "Three-Dimensional Structure Of The Complexes Between Bovine ChymotrypsinogenA And Two Recombinant Variants Of Human Pancreatic " . . . . . 100.00 245 99.59 99.59 1.36e-174 . . . . 960 1 17 no PDB 1CHG . "Chymotrypsinogen,2.5 Angstroms Crystal Structure, Comparison With Alpha-Chymotrypsin,And Implications For Zymogen Activation" . . . . . 100.00 245 99.59 99.59 1.36e-174 . . . . 960 1 18 no PDB 1CHO . "Crystal And Molecular Structures Of The Complex Of Alpha- Chymotrypsin With Its Inhibitor Turkey Ovomucoid Third Domain At 1.8 " . . . . . 53.47 131 99.24 99.24 1.42e-86 . . . . 960 1 19 no PDB 1DLK . "Crystal Structure Analysis Of Delta-Chymotrypsin Bound To A Peptidyl Chloromethyl Ketone Inhibitor" . . . . . 93.88 230 99.57 99.57 5.74e-163 . . . . 960 1 20 no PDB 1EX3 . "Crystal Structure Of Bovine Chymotrypsinogen A (Tetragonal)" . . . . . 100.00 245 99.59 99.59 1.36e-174 . . . . 960 1 21 no PDB 1GCD . 'Refined Crystal Structure Of "aged" And "non-Aged" Organophosphoryl Conjugates Of Gamma-Chymotrypsin' . . . . . 100.00 245 99.59 99.59 1.36e-174 . . . . 960 1 22 no PDB 1GCT . "Is Gamma-Chymotrypsin A Tetrapeptide Acyl-Enzyme Adduct Of Gamma- Chymotrypsin?" . . . . . 53.47 131 99.24 99.24 1.42e-86 . . . . 960 1 23 no PDB 1GG6 . "Crystal Stucture Of Gamma Chymotrypsin With N-Acetyl- Phenylalanine Trifluoromethyl Ketone Bound At The Active Site" . . . . . 53.47 131 99.24 99.24 1.42e-86 . . . . 960 1 24 no PDB 1GGD . "Crystal Stucture Of Gamma Chymotrypsin With N-Acetyl-Leucil- Phenylalanine Aldehyde Bound At The Active Site" . . . . . 53.47 131 99.24 99.24 1.42e-86 . . . . 960 1 25 no PDB 1GHA . "A Second Active Site In Chymotrypsin? The X-Ray Crystal Structure Of N-Acetyl-D-Tryptophan Bound To Gamma-Chymotrypsin" . . . . . 53.47 131 99.24 99.24 1.42e-86 . . . . 960 1 26 no PDB 1GHB . "A Second Active Site In Chymotrypsin? The X-Ray Crystal Structure Of N-Acetyl-D-Tryptophan Bound To Gamma-Chymotrypsin" . . . . . 53.47 131 99.24 99.24 1.42e-86 . . . . 960 1 27 no PDB 1GL0 . "Structure Of The Complex Between Bovine Alpha-Chymotrypsin And Pmp-D2v, An Inhibitor From The Insect Locusta Migratoria" . . . . . 100.00 245 99.59 99.59 1.36e-174 . . . . 960 1 28 no PDB 1GL1 . "Structure Of The Complex Between Bovine Alpha-Chymotrypsin And Pmp-C, An Inhibitor From The Insect Locusta Migratoria" . . . . . 100.00 245 99.59 99.59 1.36e-174 . . . . 960 1 29 no PDB 1GMC . "The X-Ray Crystal Structure Of The Tetrahedral Intermediate Of Gamma- Chymotrypsin In Hexane" . . . . . 53.47 131 99.24 99.24 1.42e-86 . . . . 960 1 30 no PDB 1GMD . "X-ray Crystal Structure Of Gamma-chymotrypsin In Hexane" . . . . . 53.47 131 99.24 99.24 1.42e-86 . . . . 960 1 31 no PDB 1GMH . 'Refined Crystal Structure Of "aged" And "non-Aged" Organophosphoryl Conjugates Of Gamma-Chymotrypsin' . . . . . 53.47 131 99.24 99.24 1.42e-86 . . . . 960 1 32 no PDB 1HJA . "Lys 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Alpha-Chymotrypsin" . . . . . 53.47 131 99.24 99.24 1.42e-86 . . . . 960 1 33 no PDB 1K2I . "Crystal Structure Of Gamma-Chymotrypsin In Complex With 7- Hydroxycoumarin" . . . . . 100.00 245 99.59 99.59 1.36e-174 . . . . 960 1 34 no PDB 1MTN . "Bovine Alpha-Chymotrypsin:bpti Crystallization" . . . . . 53.47 131 99.24 99.24 1.42e-86 . . . . 960 1 35 no PDB 1N8O . "Crystal Structure Of A Complex Between Bovine Chymotrypsin And Ecotin" . . . . . 53.47 131 99.24 99.24 1.42e-86 . . . . 960 1 36 no PDB 1OXG . "Crystal Structure Of A Complex Formed Between Organic Solvent Treated Bovine Alpha-Chymotrypsin And Its Autocatalytically Produ" . . . . . 100.00 245 99.59 99.59 1.36e-174 . . . . 960 1 37 no 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 99.59 99.59 1.36e-174 . . . . 960 1 38 no 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 99.59 99.59 1.36e-174 . . . . 960 1 39 no 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 99.59 99.59 1.36e-174 . . . . 960 1 40 no 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 99.59 99.59 1.36e-174 . . . . 960 1 41 no PDB 1T7C . "Crystal Structure Of The P1 Glu Bpti Mutant- Bovine Chymotrypsin Complex" . . . . . 100.00 245 99.59 99.59 1.36e-174 . . . . 960 1 42 no PDB 1T8L . "Crystal Structure Of The P1 Met Bpti Mutant- Bovine Chymotrypsin Complex" . . . . . 100.00 245 99.59 99.59 1.36e-174 . . . . 960 1 43 no PDB 1T8M . "Crystal Structure Of The P1 His Bpti Mutant- Bovine Chymotrypsin Complex" . . . . . 100.00 245 99.59 99.59 1.36e-174 . . . . 960 1 44 no PDB 1T8N . "Crystal Structure Of The P1 Thr Bpti Mutant- Bovine Chymotrypsin Complex" . . . . . 100.00 245 99.59 99.59 1.36e-174 . . . . 960 1 45 no PDB 1T8O . "Crystal Structure Of The P1 Trp Bpti Mutant- Bovine Chymotrypsin Complex" . . . . . 100.00 245 99.59 99.59 1.36e-174 . . . . 960 1 46 no PDB 1VGC . "Gamma-Chymotrypsin L-Para-Chloro-1-Acetamido Boronic Acid Inhibitor Complex" . . . . . 53.47 131 99.24 99.24 1.42e-86 . . . . 960 1 47 no PDB 1YPH . "High Resolution Structure Of Bovine Alpha-Chymotrypsin" . . . . . 53.47 131 99.24 99.24 1.42e-86 . . . . 960 1 48 no 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 99.59 99.59 1.36e-174 . . . . 960 1 49 no PDB 2CHA . "The Structure Of Crystalline Alpha-Chymotrypsin, v.The Atomic Structure Of Tosyl-Alpha-Chymotrypsin At 2 Angstroms Resolution" . . . . . 53.47 131 99.24 99.24 1.42e-86 . . . . 960 1 50 no PDB 2GCH . "Refined Crystal Structure Of Gamma-chymotrypsin At 1.9 Angstroms Resolution" . . . . . 53.47 131 99.24 99.24 1.42e-86 . . . . 960 1 51 no 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" . . . . . 53.47 131 99.24 99.24 1.42e-86 . . . . 960 1 52 no PDB 2GMT . "Three-Dimensional Structure Of Chymotrypsin Inactivated With (2s) N- Acetyl-L-Alanyl-L-Phenylalanyl-Chloroethyl Ketone: Implica" . . . . . 53.47 131 99.24 99.24 1.42e-86 . . . . 960 1 53 no PDB 2P8O . "Crystal Structure Of A Benzohydroxamic AcidVANADATE Complex Bound To Chymotrypsin A" . . . . . 53.47 131 99.24 99.24 1.42e-86 . . . . 960 1 54 no PDB 2VGC . "Gamma-Chymotrypsin D-Para-Chloro-1-Acetamido Boronic Acid Inhibitor Complex" . . . . . 53.47 131 99.24 99.24 1.42e-86 . . . . 960 1 55 no PDB 2Y6T . "Molecular Recognition Of Chymotrypsin By The Serine Protease Inhibitor Ecotin From Yersinia Pestis" . . . . . 100.00 245 99.59 99.59 1.36e-174 . . . . 960 1 56 no PDB 3BG4 . "The Crystal Structure Of Guamerin In Complex With Chymotrypsin And The Development Of An Elastase-Specific Inhibitor" . . . . . 53.47 131 99.24 99.24 1.42e-86 . . . . 960 1 57 no PDB 3GCH . "Chemistry Of Caged Enzymes. Binding Of Photoreversible Cinnamates To Chymotrypsin" . . . . . 53.47 131 99.24 99.24 1.42e-86 . . . . 960 1 58 no 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" . . . . . 53.47 131 99.24 99.24 1.42e-86 . . . . 960 1 59 no PDB 3RU4 . "Crystal Structure Of The Bowman-Birk Serine Protease Inhibitor Btci In Complex With Trypsin And Chymotrypsin" . . . . . 53.47 131 99.24 99.24 1.42e-86 . . . . 960 1 60 no PDB 3T62 . "Crystal Structure Of Recombinant Kunitz Type Serine Protease Inhibitor-1 From The Caribbean Sea Anemone Stichodactyla Helianthu" . . . . . 100.00 245 99.59 99.59 1.36e-174 . . . . 960 1 61 no PDB 3VGC . "Gamma-Chymotrypsin L-Naphthyl-1-Acetamido Boronic Acid Acid Inhibitor Complex" . . . . . 53.47 131 99.24 99.24 1.42e-86 . . . . 960 1 62 no PDB 4CHA . "Structure Of Alpha-Chymotrypsin Refined At 1.68 Angstroms Resolution" . . . . . 53.47 131 99.24 99.24 1.42e-86 . . . . 960 1 63 no PDB 4GCH . "Structure And Activity Of Two Photoreversible Cinnamates Bound To Chymotrypsin" . . . . . 53.47 131 99.24 99.24 1.42e-86 . . . . 960 1 64 no PDB 4Q2K . "Bovine Alpha Chymotrypsin Bound To A Cyclic Peptide Inhibitor, 5b" . . . . . 100.00 245 99.59 99.59 1.36e-174 . . . . 960 1 65 no PDB 4VGC . "Gamma-Chymotrypsin D-Naphthyl-1-Acetamido Boronic Acid Inhibitor Complex" . . . . . 53.47 131 99.24 99.24 1.42e-86 . . . . 960 1 66 no PDB 5CHA . "The Refinement And The Structure Of The Dimer Of Alpha- Chymotrypsin At 1.67-Angstroms Resolution" . . . . . 53.47 131 99.24 99.24 1.42e-86 . . . . 960 1 67 no PDB 5GCH . "Chemistry Of Caged Enzymes II. Photoactivation Of Inhibited Chymotrypsin" . . . . . 53.47 131 99.24 99.24 1.42e-86 . . . . 960 1 68 no PDB 6CHA . "Structure Of A Tetrahedral Transition State Complex Of Alpha-Chymotrypsin At 1.8-Angstroms Resolution" . . . . . 53.47 131 99.24 99.24 1.42e-86 . . . . 960 1 69 no PDB 6GCH . "Structure Of Chymotrypsin-Trifluoromethyl Ketone Inhibitor Complexes. Comparison Of Slowly And Rapidly Equilibrating Inhibitors" . . . . . 53.47 131 99.24 99.24 1.42e-86 . . . . 960 1 70 no PDB 7GCH . "Structure Of Chymotrypsin-Trifluoromethyl Ketone Inhibitor Complexes. Comparison Of Slowly And Rapidly Equilibrating Inhibitors" . . . . . 53.47 131 99.24 99.24 1.42e-86 . . . . 960 1 71 no PDB 8GCH . "Gamma-Chymotrypsin Is A Complex Of Alpha-Chymotrypsin With Its Own Autolysis Products" . . . . . 53.47 131 99.24 99.24 1.42e-86 . . . . 960 1 72 no REF XP_003583409 . "PREDICTED: chymotrypsinogen A [Bos taurus]" . . . . . 100.00 300 99.59 99.59 3.43e-174 . . . . 960 1 73 no REF XP_003587247 . "PREDICTED: chymotrypsinogen A [Bos taurus]" . . . . . 100.00 300 99.59 99.59 3.43e-174 . . . . 960 1 74 no REF XP_005894372 . "PREDICTED: chymotrypsinogen A-like [Bos mutus]" . . . . . 100.00 263 97.96 98.78 3.49e-171 . . . . 960 1 75 no SP P00766 . "RecName: Full=Chymotrypsinogen A; Contains: RecName: Full=Chymotrypsin A chain A; Contains: RecName: Full=Chymotrypsin A chain " . . . . . 100.00 245 99.59 99.59 1.36e-174 . . . . 960 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'chymotrypsinogen A' common 960 1 stop_ loop_ _Entity_comp_index.ID _Entity_comp_index.Auth_seq_ID _Entity_comp_index.Comp_ID _Entity_comp_index.Comp_label _Entity_comp_index.Entry_ID _Entity_comp_index.Entity_ID 1 . CYS . 960 1 2 . GLY . 960 1 3 . VAL . 960 1 4 . PRO . 960 1 5 . ALA . 960 1 6 . ILE . 960 1 7 . GLN . 960 1 8 . PRO . 960 1 9 . VAL . 960 1 10 . LEU . 960 1 11 . SER . 960 1 12 . GLY . 960 1 13 . LEU . 960 1 14 . SER . 960 1 15 . ARG . 960 1 16 . ILE . 960 1 17 . VAL . 960 1 18 . ASN . 960 1 19 . GLY . 960 1 20 . GLU . 960 1 21 . GLU . 960 1 22 . ALA . 960 1 23 . VAL . 960 1 24 . PRO . 960 1 25 . GLY . 960 1 26 . SER . 960 1 27 . TRP . 960 1 28 . PRO . 960 1 29 . TRP . 960 1 30 . GLN . 960 1 31 . VAL . 960 1 32 . SER . 960 1 33 . LEU . 960 1 34 . GLN . 960 1 35 . ASP . 960 1 36 . LYS . 960 1 37 . THR . 960 1 38 . GLY . 960 1 39 . PHE . 960 1 40 . HIS . 960 1 41 . PHE . 960 1 42 . CYS . 960 1 43 . GLY . 960 1 44 . GLY . 960 1 45 . SER . 960 1 46 . LEU . 960 1 47 . ILE . 960 1 48 . ASN . 960 1 49 . GLU . 960 1 50 . ASN . 960 1 51 . TRP . 960 1 52 . VAL . 960 1 53 . VAL . 960 1 54 . THR . 960 1 55 . ALA . 960 1 56 . ALA . 960 1 57 . HIS . 960 1 58 . CYS . 960 1 59 . GLY . 960 1 60 . VAL . 960 1 61 . THR . 960 1 62 . THR . 960 1 63 . SER . 960 1 64 . ASP . 960 1 65 . VAL . 960 1 66 . VAL . 960 1 67 . VAL . 960 1 68 . ALA . 960 1 69 . GLY . 960 1 70 . GLU . 960 1 71 . PHE . 960 1 72 . ASP . 960 1 73 . GLN . 960 1 74 . GLY . 960 1 75 . SER . 960 1 76 . SER . 960 1 77 . SER . 960 1 78 . GLU . 960 1 79 . LYS . 960 1 80 . ILE . 960 1 81 . GLN . 960 1 82 . LYS . 960 1 83 . LEU . 960 1 84 . LYS . 960 1 85 . ILE . 960 1 86 . ALA . 960 1 87 . LYS . 960 1 88 . VAL . 960 1 89 . PHE . 960 1 90 . LYS . 960 1 91 . ASN . 960 1 92 . SER . 960 1 93 . LYS . 960 1 94 . TYR . 960 1 95 . ASN . 960 1 96 . SER . 960 1 97 . LEU . 960 1 98 . THR . 960 1 99 . ILE . 960 1 100 . ASN . 960 1 101 . ASN . 960 1 102 . ASP . 960 1 103 . ILE . 960 1 104 . THR . 960 1 105 . LEU . 960 1 106 . LEU . 960 1 107 . LYS . 960 1 108 . LEU . 960 1 109 . SER . 960 1 110 . THR . 960 1 111 . ALA . 960 1 112 . ALA . 960 1 113 . SER . 960 1 114 . PHE . 960 1 115 . SER . 960 1 116 . GLN . 960 1 117 . THR . 960 1 118 . VAL . 960 1 119 . SER . 960 1 120 . ALA . 960 1 121 . VAL . 960 1 122 . CYS . 960 1 123 . LEU . 960 1 124 . PRO . 960 1 125 . SER . 960 1 126 . ALA . 960 1 127 . SER . 960 1 128 . ASP . 960 1 129 . ASP . 960 1 130 . PHE . 960 1 131 . ALA . 960 1 132 . ALA . 960 1 133 . GLY . 960 1 134 . THR . 960 1 135 . THR . 960 1 136 . CYS . 960 1 137 . VAL . 960 1 138 . VAL . 960 1 139 . THR . 960 1 140 . GLY . 960 1 141 . TRP . 960 1 142 . GLY . 960 1 143 . LEU . 960 1 144 . THR . 960 1 145 . ARG . 960 1 146 . TYR . 960 1 147 . THR . 960 1 148 . ASN . 960 1 149 . ALA . 960 1 150 . ASN . 960 1 151 . THR . 960 1 152 . PRO . 960 1 153 . ASP . 960 1 154 . ARG . 960 1 155 . LEU . 960 1 156 . GLN . 960 1 157 . GLN . 960 1 158 . ALA . 960 1 159 . SER . 960 1 160 . LEU . 960 1 161 . PRO . 960 1 162 . LEU . 960 1 163 . LEU . 960 1 164 . SER . 960 1 165 . ASN . 960 1 166 . THR . 960 1 167 . ASN . 960 1 168 . CYS . 960 1 169 . LYS . 960 1 170 . LYS . 960 1 171 . TYR . 960 1 172 . TRP . 960 1 173 . GLY . 960 1 174 . THR . 960 1 175 . LYS . 960 1 176 . ILE . 960 1 177 . LYS . 960 1 178 . ASP . 960 1 179 . ALA . 960 1 180 . MET . 960 1 181 . ILE . 960 1 182 . CYS . 960 1 183 . ALA . 960 1 184 . GLY . 960 1 185 . ALA . 960 1 186 . SER . 960 1 187 . GLY . 960 1 188 . VAL . 960 1 189 . SER . 960 1 190 . SER . 960 1 191 . CYS . 960 1 192 . MET . 960 1 193 . GLY . 960 1 194 . ASP . 960 1 195 . SER . 960 1 196 . GLY . 960 1 197 . GLY . 960 1 198 . PRO . 960 1 199 . LEU . 960 1 200 . VAL . 960 1 201 . CYS . 960 1 202 . LYS . 960 1 203 . LYS . 960 1 204 . ASN . 960 1 205 . GLY . 960 1 206 . ALA . 960 1 207 . TRP . 960 1 208 . THR . 960 1 209 . LEU . 960 1 210 . VAL . 960 1 211 . GLY . 960 1 212 . ILE . 960 1 213 . VAL . 960 1 214 . SER . 960 1 215 . TRP . 960 1 216 . GLY . 960 1 217 . SER . 960 1 218 . SER . 960 1 219 . THR . 960 1 220 . CYS . 960 1 221 . SER . 960 1 222 . THR . 960 1 223 . SER . 960 1 224 . THR . 960 1 225 . PRO . 960 1 226 . GLY . 960 1 227 . VAL . 960 1 228 . TYR . 960 1 229 . ALA . 960 1 230 . ARG . 960 1 231 . VAL . 960 1 232 . THR . 960 1 233 . ALA . 960 1 234 . LEU . 960 1 235 . VAL . 960 1 236 . ASN . 960 1 237 . TRP . 960 1 238 . VAL . 960 1 239 . GLN . 960 1 240 . GLN . 960 1 241 . THR . 960 1 242 . LEU . 960 1 243 . ALA . 960 1 244 . ALA . 960 1 245 . ASN . 960 1 stop_ loop_ _Entity_poly_seq.Hetero _Entity_poly_seq.Mon_ID _Entity_poly_seq.Num _Entity_poly_seq.Comp_index_ID _Entity_poly_seq.Entry_ID _Entity_poly_seq.Entity_ID . CYS 1 1 960 1 . GLY 2 2 960 1 . VAL 3 3 960 1 . PRO 4 4 960 1 . ALA 5 5 960 1 . ILE 6 6 960 1 . GLN 7 7 960 1 . PRO 8 8 960 1 . VAL 9 9 960 1 . LEU 10 10 960 1 . SER 11 11 960 1 . GLY 12 12 960 1 . LEU 13 13 960 1 . SER 14 14 960 1 . ARG 15 15 960 1 . ILE 16 16 960 1 . VAL 17 17 960 1 . ASN 18 18 960 1 . GLY 19 19 960 1 . GLU 20 20 960 1 . GLU 21 21 960 1 . ALA 22 22 960 1 . VAL 23 23 960 1 . PRO 24 24 960 1 . GLY 25 25 960 1 . SER 26 26 960 1 . TRP 27 27 960 1 . PRO 28 28 960 1 . TRP 29 29 960 1 . GLN 30 30 960 1 . VAL 31 31 960 1 . SER 32 32 960 1 . LEU 33 33 960 1 . GLN 34 34 960 1 . ASP 35 35 960 1 . LYS 36 36 960 1 . THR 37 37 960 1 . GLY 38 38 960 1 . PHE 39 39 960 1 . HIS 40 40 960 1 . PHE 41 41 960 1 . CYS 42 42 960 1 . GLY 43 43 960 1 . GLY 44 44 960 1 . SER 45 45 960 1 . LEU 46 46 960 1 . ILE 47 47 960 1 . ASN 48 48 960 1 . GLU 49 49 960 1 . ASN 50 50 960 1 . TRP 51 51 960 1 . VAL 52 52 960 1 . VAL 53 53 960 1 . THR 54 54 960 1 . ALA 55 55 960 1 . ALA 56 56 960 1 . HIS 57 57 960 1 . CYS 58 58 960 1 . GLY 59 59 960 1 . VAL 60 60 960 1 . THR 61 61 960 1 . THR 62 62 960 1 . SER 63 63 960 1 . ASP 64 64 960 1 . VAL 65 65 960 1 . VAL 66 66 960 1 . VAL 67 67 960 1 . ALA 68 68 960 1 . GLY 69 69 960 1 . GLU 70 70 960 1 . PHE 71 71 960 1 . ASP 72 72 960 1 . GLN 73 73 960 1 . GLY 74 74 960 1 . SER 75 75 960 1 . SER 76 76 960 1 . SER 77 77 960 1 . GLU 78 78 960 1 . LYS 79 79 960 1 . ILE 80 80 960 1 . GLN 81 81 960 1 . LYS 82 82 960 1 . LEU 83 83 960 1 . LYS 84 84 960 1 . ILE 85 85 960 1 . ALA 86 86 960 1 . LYS 87 87 960 1 . VAL 88 88 960 1 . PHE 89 89 960 1 . LYS 90 90 960 1 . ASN 91 91 960 1 . SER 92 92 960 1 . LYS 93 93 960 1 . TYR 94 94 960 1 . ASN 95 95 960 1 . SER 96 96 960 1 . LEU 97 97 960 1 . THR 98 98 960 1 . ILE 99 99 960 1 . ASN 100 100 960 1 . ASN 101 101 960 1 . ASP 102 102 960 1 . ILE 103 103 960 1 . THR 104 104 960 1 . LEU 105 105 960 1 . LEU 106 106 960 1 . LYS 107 107 960 1 . LEU 108 108 960 1 . SER 109 109 960 1 . THR 110 110 960 1 . ALA 111 111 960 1 . ALA 112 112 960 1 . SER 113 113 960 1 . PHE 114 114 960 1 . SER 115 115 960 1 . GLN 116 116 960 1 . THR 117 117 960 1 . VAL 118 118 960 1 . SER 119 119 960 1 . ALA 120 120 960 1 . VAL 121 121 960 1 . CYS 122 122 960 1 . LEU 123 123 960 1 . PRO 124 124 960 1 . SER 125 125 960 1 . ALA 126 126 960 1 . SER 127 127 960 1 . ASP 128 128 960 1 . ASP 129 129 960 1 . PHE 130 130 960 1 . ALA 131 131 960 1 . ALA 132 132 960 1 . GLY 133 133 960 1 . THR 134 134 960 1 . THR 135 135 960 1 . CYS 136 136 960 1 . VAL 137 137 960 1 . VAL 138 138 960 1 . THR 139 139 960 1 . GLY 140 140 960 1 . TRP 141 141 960 1 . GLY 142 142 960 1 . LEU 143 143 960 1 . THR 144 144 960 1 . ARG 145 145 960 1 . TYR 146 146 960 1 . THR 147 147 960 1 . ASN 148 148 960 1 . ALA 149 149 960 1 . ASN 150 150 960 1 . THR 151 151 960 1 . PRO 152 152 960 1 . ASP 153 153 960 1 . ARG 154 154 960 1 . LEU 155 155 960 1 . GLN 156 156 960 1 . GLN 157 157 960 1 . ALA 158 158 960 1 . SER 159 159 960 1 . LEU 160 160 960 1 . PRO 161 161 960 1 . LEU 162 162 960 1 . LEU 163 163 960 1 . SER 164 164 960 1 . ASN 165 165 960 1 . THR 166 166 960 1 . ASN 167 167 960 1 . CYS 168 168 960 1 . LYS 169 169 960 1 . LYS 170 170 960 1 . TYR 171 171 960 1 . TRP 172 172 960 1 . GLY 173 173 960 1 . THR 174 174 960 1 . LYS 175 175 960 1 . ILE 176 176 960 1 . LYS 177 177 960 1 . ASP 178 178 960 1 . ALA 179 179 960 1 . MET 180 180 960 1 . ILE 181 181 960 1 . CYS 182 182 960 1 . ALA 183 183 960 1 . GLY 184 184 960 1 . ALA 185 185 960 1 . SER 186 186 960 1 . GLY 187 187 960 1 . VAL 188 188 960 1 . SER 189 189 960 1 . SER 190 190 960 1 . CYS 191 191 960 1 . MET 192 192 960 1 . GLY 193 193 960 1 . ASP 194 194 960 1 . SER 195 195 960 1 . GLY 196 196 960 1 . GLY 197 197 960 1 . PRO 198 198 960 1 . LEU 199 199 960 1 . VAL 200 200 960 1 . CYS 201 201 960 1 . LYS 202 202 960 1 . LYS 203 203 960 1 . ASN 204 204 960 1 . GLY 205 205 960 1 . ALA 206 206 960 1 . TRP 207 207 960 1 . THR 208 208 960 1 . LEU 209 209 960 1 . VAL 210 210 960 1 . GLY 211 211 960 1 . ILE 212 212 960 1 . VAL 213 213 960 1 . SER 214 214 960 1 . TRP 215 215 960 1 . GLY 216 216 960 1 . SER 217 217 960 1 . SER 218 218 960 1 . THR 219 219 960 1 . CYS 220 220 960 1 . SER 221 221 960 1 . THR 222 222 960 1 . SER 223 223 960 1 . THR 224 224 960 1 . PRO 225 225 960 1 . GLY 226 226 960 1 . VAL 227 227 960 1 . TYR 228 228 960 1 . ALA 229 229 960 1 . ARG 230 230 960 1 . VAL 231 231 960 1 . THR 232 232 960 1 . ALA 233 233 960 1 . LEU 234 234 960 1 . VAL 235 235 960 1 . ASN 236 236 960 1 . TRP 237 237 960 1 . VAL 238 238 960 1 . GLN 239 239 960 1 . GLN 240 240 960 1 . THR 241 241 960 1 . LEU 242 242 960 1 . ALA 243 243 960 1 . ALA 244 244 960 1 . ASN 245 245 960 1 stop_ save_ #################### # Natural source # #################### save_natural_source _Entity_natural_src_list.Sf_category natural_source _Entity_natural_src_list.Sf_framecode natural_source _Entity_natural_src_list.Entry_ID 960 _Entity_natural_src_list.ID 1 loop_ _Entity_natural_src.ID _Entity_natural_src.Entity_ID _Entity_natural_src.Entity_label _Entity_natural_src.Entity_chimera_segment_ID _Entity_natural_src.NCBI_taxonomy_ID _Entity_natural_src.Type _Entity_natural_src.Common _Entity_natural_src.Organism_name_scientific _Entity_natural_src.Organism_name_common _Entity_natural_src.Organism_acronym _Entity_natural_src.ICTVdb_decimal_code _Entity_natural_src.Superkingdom _Entity_natural_src.Kingdom _Entity_natural_src.Genus _Entity_natural_src.Species _Entity_natural_src.Strain _Entity_natural_src.Variant _Entity_natural_src.Subvariant _Entity_natural_src.Organ _Entity_natural_src.Tissue _Entity_natural_src.Tissue_fraction _Entity_natural_src.Cell_line _Entity_natural_src.Cell_type _Entity_natural_src.ATCC_number _Entity_natural_src.Organelle _Entity_natural_src.Cellular_location _Entity_natural_src.Fragment _Entity_natural_src.Fraction _Entity_natural_src.Secretion _Entity_natural_src.Plasmid _Entity_natural_src.Plasmid_details _Entity_natural_src.Gene_mnemonic _Entity_natural_src.Dev_stage _Entity_natural_src.Details _Entity_natural_src.Citation_ID _Entity_natural_src.Citation_label _Entity_natural_src.Entry_ID _Entity_natural_src.Entity_natural_src_list_ID 1 1 $chymotrypsinogen_A . 9909 organism . 'Bos primigenius' cow . . Eukaryota Metazoa Bos primigenius generic . . . . . . . . . . . . . . . . . . . . 960 1 stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Entity_experimental_src_list.Sf_category experimental_source _Entity_experimental_src_list.Sf_framecode experimental_source _Entity_experimental_src_list.Entry_ID 960 _Entity_experimental_src_list.ID 1 loop_ _Entity_experimental_src.ID _Entity_experimental_src.Entity_ID _Entity_experimental_src.Entity_label _Entity_experimental_src.Entity_chimera_segment_ID _Entity_experimental_src.Production_method _Entity_experimental_src.Host_org_scientific_name _Entity_experimental_src.Host_org_name_common _Entity_experimental_src.Host_org_details _Entity_experimental_src.Host_org_NCBI_taxonomy_ID _Entity_experimental_src.Host_org_genus _Entity_experimental_src.Host_org_species _Entity_experimental_src.Host_org_strain _Entity_experimental_src.Host_org_variant _Entity_experimental_src.Host_org_subvariant _Entity_experimental_src.Host_org_organ _Entity_experimental_src.Host_org_tissue _Entity_experimental_src.Host_org_tissue_fraction _Entity_experimental_src.Host_org_cell_line _Entity_experimental_src.Host_org_cell_type _Entity_experimental_src.Host_org_cellular_location _Entity_experimental_src.Host_org_organelle _Entity_experimental_src.Host_org_gene _Entity_experimental_src.Host_org_culture_collection _Entity_experimental_src.Host_org_ATCC_number _Entity_experimental_src.Vector_type _Entity_experimental_src.PDBview_host_org_vector_name _Entity_experimental_src.PDBview_plasmid_name _Entity_experimental_src.Vector_name _Entity_experimental_src.Vector_details _Entity_experimental_src.Vendor_name _Entity_experimental_src.Host_org_dev_stage _Entity_experimental_src.Details _Entity_experimental_src.Citation_ID _Entity_experimental_src.Citation_label _Entity_experimental_src.Entry_ID _Entity_experimental_src.Entity_experimental_src_list_ID 1 1 $chymotrypsinogen_A . 'not available' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 960 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Sample.Sf_category sample _Sample.Sf_framecode sample_one _Sample.Entry_ID 960 _Sample.ID 1 _Sample.Type solution _Sample.Sub_type . _Sample.Details . _Sample.Aggregate_sample_number . _Sample.Solvent_system . _Sample.Preparation_date . _Sample.Preparation_expiration_date . _Sample.Polycrystallization_protocol . _Sample.Single_crystal_protocol . _Sample.Crystal_grow_apparatus . _Sample.Crystal_grow_atmosphere . _Sample.Crystal_grow_details . _Sample.Crystal_grow_method . _Sample.Crystal_grow_method_cit_ID . _Sample.Crystal_grow_pH . _Sample.Crystal_grow_pH_range . _Sample.Crystal_grow_pressure . _Sample.Crystal_grow_pressure_esd . _Sample.Crystal_grow_seeding . _Sample.Crystal_grow_seeding_cit_ID . _Sample.Crystal_grow_temp . _Sample.Crystal_grow_temp_details . _Sample.Crystal_grow_temp_esd . _Sample.Crystal_grow_time . _Sample.Oriented_sample_prep_protocol . _Sample.Lyophilization_cryo_protectant . _Sample.Storage_protocol . save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode sample_condition_set_one _Sample_condition_list.Entry_ID 960 _Sample_condition_list.ID 1 _Sample_condition_list.Details . loop_ _Sample_condition_variable.Type _Sample_condition_variable.Val _Sample_condition_variable.Val_err _Sample_condition_variable.Val_units _Sample_condition_variable.Entry_ID _Sample_condition_variable.Sample_condition_list_ID pH 9.5 . na 960 1 temperature 277 . K 960 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode spectrometer_list _NMR_spectrometer.Entry_ID 960 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details 'spectrometer information not available' _NMR_spectrometer.Manufacturer unknown _NMR_spectrometer.Model unknown _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 0 save_ save_NMR_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode NMR_spectrometer_list _NMR_spectrometer_list.Entry_ID 960 _NMR_spectrometer_list.ID 1 loop_ _NMR_spectrometer_view.ID _NMR_spectrometer_view.Name _NMR_spectrometer_view.Manufacturer _NMR_spectrometer_view.Model _NMR_spectrometer_view.Serial_number _NMR_spectrometer_view.Field_strength _NMR_spectrometer_view.Details _NMR_spectrometer_view.Citation_ID _NMR_spectrometer_view.Citation_label _NMR_spectrometer_view.Entry_ID _NMR_spectrometer_view.NMR_spectrometer_list_ID 1 spectrometer_1 unknown unknown . 0 'spectrometer information not available' . . 960 1 stop_ save_ ############################# # NMR applied experiments # ############################# save_experiment_list _Experiment_list.Sf_category experiment_list _Experiment_list.Sf_framecode experiment_list _Experiment_list.Entry_ID 960 _Experiment_list.ID 1 _Experiment_list.Details . loop_ _Experiment.ID _Experiment.Name _Experiment.Raw_data_flag _Experiment.NMR_spec_expt_ID _Experiment.NMR_spec_expt_label _Experiment.MS_expt_ID _Experiment.MS_expt_label _Experiment.SAXS_expt_ID _Experiment.SAXS_expt_label _Experiment.FRET_expt_ID _Experiment.FRET_expt_label _Experiment.EMR_expt_ID _Experiment.EMR_expt_label _Experiment.Sample_ID _Experiment.Sample_label _Experiment.Sample_state _Experiment.Sample_volume _Experiment.Sample_volume_units _Experiment.Sample_condition_list_ID _Experiment.Sample_condition_list_label _Experiment.Sample_spinning_rate _Experiment.Sample_angle _Experiment.NMR_tube_type _Experiment.NMR_spectrometer_ID _Experiment.NMR_spectrometer_label _Experiment.NMR_spectrometer_probe_ID _Experiment.NMR_spectrometer_probe_label _Experiment.NMR_spectral_processing_ID _Experiment.NMR_spectral_processing_label _Experiment.Mass_spectrometer_ID _Experiment.Mass_spectrometer_label _Experiment.Xray_instrument_ID _Experiment.Xray_instrument_label _Experiment.Fluorescence_instrument_ID _Experiment.Fluorescence_instrument_label _Experiment.EMR_instrument_ID _Experiment.EMR_instrument_label _Experiment.Chromatographic_system_ID _Experiment.Chromatographic_system_label _Experiment.Chromatographic_column_ID _Experiment.Chromatographic_column_label _Experiment.Entry_ID _Experiment.Experiment_list_ID 1 . . . . . . . . . . . . 1 $sample_one . . . 1 $sample_condition_set_one . . . 1 $spectrometer_list . . . . . . . . . . . . . . . . 960 1 stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chem_shift_reference_par_set_one _Chem_shift_reference.Entry_ID 960 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H . DSS . . . . . ppm 0 . . . . . . 1 $entry_citation . . 1 $entry_citation 960 1 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 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode 'chemical_shift_assignment_data_set_one' _Assigned_chem_shift_list.Entry_ID 960 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $sample_condition_set_one _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chem_shift_reference_par_set_one _Assigned_chem_shift_list.Chem_shift_1H_err . _Assigned_chem_shift_list.Chem_shift_13C_err . _Assigned_chem_shift_list.Chem_shift_15N_err . _Assigned_chem_shift_list.Chem_shift_31P_err . _Assigned_chem_shift_list.Chem_shift_2H_err . _Assigned_chem_shift_list.Chem_shift_19F_err . _Assigned_chem_shift_list.Error_derivation_method . _Assigned_chem_shift_list.Details . _Assigned_chem_shift_list.Text_data_format . _Assigned_chem_shift_list.Text_data . loop_ _Chem_shift_experiment.Experiment_ID _Chem_shift_experiment.Experiment_name _Chem_shift_experiment.Sample_ID _Chem_shift_experiment.Sample_label _Chem_shift_experiment.Sample_state _Chem_shift_experiment.Entry_ID _Chem_shift_experiment.Assigned_chem_shift_list_ID . . 1 $sample_one . 960 1 stop_ loop_ _Atom_chem_shift.ID _Atom_chem_shift.Assembly_atom_ID _Atom_chem_shift.Entity_assembly_ID _Atom_chem_shift.Entity_ID _Atom_chem_shift.Comp_index_ID _Atom_chem_shift.Seq_ID _Atom_chem_shift.Comp_ID _Atom_chem_shift.Atom_ID _Atom_chem_shift.Atom_type _Atom_chem_shift.Atom_isotope_number _Atom_chem_shift.Val _Atom_chem_shift.Val_err _Atom_chem_shift.Assign_fig_of_merit _Atom_chem_shift.Ambiguity_code _Atom_chem_shift.Occupancy _Atom_chem_shift.Resonance_ID _Atom_chem_shift.Auth_entity_assembly_ID _Atom_chem_shift.Auth_asym_ID _Atom_chem_shift.Auth_seq_ID _Atom_chem_shift.Auth_comp_ID _Atom_chem_shift.Auth_atom_ID _Atom_chem_shift.Details _Atom_chem_shift.Entry_ID _Atom_chem_shift.Assigned_chem_shift_list_ID 1 . 1 1 57 57 HIS HD1 H 1 15 . . 1 . . . . . . . . 960 1 stop_ save_