data_961 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 961 _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 . . . 961 2 R. Shulman . G. . 961 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 961 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 1 961 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' 961 3 . . 1999-06-14 . revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 961 2 . . 1996-03-25 . reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 961 1 . . 1995-07-31 . original BMRB 'Last release in original BMRB flat-file format' 961 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 961 _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 . . . 961 1 2 R. Shulman . G. . 961 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_chymotrypsin _Assembly.Sf_category assembly _Assembly.Sf_framecode system_chymotrypsin _Assembly.Entry_ID 961 _Assembly.ID 1 _Assembly.Name chymotrypsin _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 chymotrypsin 1 $chymotrypsin . . . . . . . . . 961 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID chymotrypsin system 961 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_chymotrypsin _Entity.Sf_category entity _Entity.Sf_framecode chymotrypsin _Entity.Entry_ID 961 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name chymotrypsin _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 ; IVNGEEAVPGSWPWQVSLQD KTGFHFCGGSLINENWVVTA AHCGVTTSDVVVAGEFDQGS SSEKIQKLKIAKVFKNSKYN SLTINNDITLLKLSTAASFS QTVSAVCLPSASDDFAAGTT CVVTGWGLTRYTNANTPDRL QQASLPLLSNTNCKKYWGTK IKDAMICAGASGVSSCMGDS GGPLVCKKNGAWTLVGIVSW GSSTCSTSTPGVYARVTALV NWVQQTLAAN ; _Entity.Polymer_seq_one_letter_code ; IVNGEEAVPGSWPWQVSLQD KTGFHFCGGSLINENWVVTA AHCGVTTSDVVVAGEFDQGS SSEKIQKLKIAKVFKNSKYN SLTINNDITLLKLSTAASFS QTVSAVCLPSASDDFAAGTT CVVTGWGLTRYTNANTPDRL QQASLPLLSNTNCKKYWGTK IKDAMICAGASGVSSCMGDS GGPLVCKKNGAWTLVGIVSW GSSTCSTSTPGVYARVTALV NWVQQTLAAN ; _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 230 _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 98.70 98.70 9.87e-160 . . . . 961 1 2 no BMRB 6881 . bovine_alpha_chymotrypsin . . . . . 100.00 241 98.70 98.70 1.15e-159 . . . . 961 1 3 no BMRB 960 . "chymotrypsinogen A" . . . . . 100.00 245 100.00 100.00 1.03e-163 . . . . 961 1 4 no BMRB 962 . "chymotrypsinogen A" . . . . . 100.00 245 100.00 100.00 1.03e-163 . . . . 961 1 5 no BMRB 963 . chymotrypsin . . . . . 100.00 230 100.00 100.00 7.34e-164 . . . . 961 1 6 no BMRB 964 . "chymotrypsinogen A" . . . . . 100.00 245 100.00 100.00 1.03e-163 . . . . 961 1 7 no BMRB 965 . chymotrypsin . . . . . 100.00 230 100.00 100.00 7.34e-164 . . . . 961 1 8 no BMRB 966 . "chymotrypsinogen A" . . . . . 100.00 245 100.00 100.00 1.03e-163 . . . . 961 1 9 no BMRB 967 . chymotrypsin . . . . . 100.00 230 100.00 100.00 7.34e-164 . . . . 961 1 10 no PDB 1AB9 . "Crystal Structure Of Bovine Gamma-Chymotrypsin" . . . . . 56.96 131 99.24 99.24 6.90e-87 . . . . 961 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 99.57 99.57 5.63e-163 . . . . 961 1 12 no PDB 1AFQ . "Crystal Structure Of Bovine Gamma-Chymotrypsin Complexed With A Synthetic Inhibitor" . . . . . 56.96 131 99.24 99.24 6.90e-87 . . . . 961 1 13 no PDB 1CA0 . "Bovine Chymotrypsin Complexed To Appi" . . . . . 56.96 131 99.24 99.24 6.90e-87 . . . . 961 1 14 no PDB 1CBW . "Bovine Chymotrypsin Complexed To Bpti" . . . . . 56.96 131 99.24 99.24 6.90e-87 . . . . 961 1 15 no PDB 1CGI . "Three-Dimensional Structure Of The Complexes Between Bovine ChymotrypsinogenA And Two Recombinant Variants Of Human Pancreatic " . . . . . 100.00 245 99.57 99.57 5.63e-163 . . . . 961 1 16 no PDB 1CGJ . "Three-Dimensional Structure Of The Complexes Between Bovine ChymotrypsinogenA And Two Recombinant Variants Of Human Pancreatic " . . . . . 100.00 245 99.57 99.57 5.63e-163 . . . . 961 1 17 no PDB 1CHG . "Chymotrypsinogen,2.5 Angstroms Crystal Structure, Comparison With Alpha-Chymotrypsin,And Implications For Zymogen Activation" . . . . . 100.00 245 99.57 99.57 5.63e-163 . . . . 961 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 " . . . . . 56.96 131 99.24 99.24 6.90e-87 . . . . 961 1 19 no PDB 1DLK . "Crystal Structure Analysis Of Delta-Chymotrypsin Bound To A Peptidyl Chloromethyl Ketone Inhibitor" . . . . . 100.00 230 99.57 99.57 3.11e-163 . . . . 961 1 20 no PDB 1EX3 . "Crystal Structure Of Bovine Chymotrypsinogen A (Tetragonal)" . . . . . 100.00 245 99.57 99.57 5.63e-163 . . . . 961 1 21 no PDB 1GCD . 'Refined Crystal Structure Of "aged" And "non-Aged" Organophosphoryl Conjugates Of Gamma-Chymotrypsin' . . . . . 100.00 245 99.57 99.57 5.63e-163 . . . . 961 1 22 no PDB 1GCT . "Is Gamma-Chymotrypsin A Tetrapeptide Acyl-Enzyme Adduct Of Gamma- Chymotrypsin?" . . . . . 56.96 131 99.24 99.24 6.90e-87 . . . . 961 1 23 no 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 6.90e-87 . . . . 961 1 24 no 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 6.90e-87 . . . . 961 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" . . . . . 56.96 131 99.24 99.24 6.90e-87 . . . . 961 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" . . . . . 56.96 131 99.24 99.24 6.90e-87 . . . . 961 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 99.57 99.57 5.63e-163 . . . . 961 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 99.57 99.57 5.63e-163 . . . . 961 1 29 no PDB 1GMC . "The X-Ray Crystal Structure Of The Tetrahedral Intermediate Of Gamma- Chymotrypsin In Hexane" . . . . . 56.96 131 99.24 99.24 6.90e-87 . . . . 961 1 30 no PDB 1GMD . "X-ray Crystal Structure Of Gamma-chymotrypsin In Hexane" . . . . . 56.96 131 99.24 99.24 6.90e-87 . . . . 961 1 31 no PDB 1GMH . 'Refined Crystal Structure Of "aged" And "non-Aged" Organophosphoryl Conjugates Of Gamma-Chymotrypsin' . . . . . 56.96 131 99.24 99.24 6.90e-87 . . . . 961 1 32 no PDB 1HJA . "Lys 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Alpha-Chymotrypsin" . . . . . 56.96 131 99.24 99.24 6.90e-87 . . . . 961 1 33 no PDB 1K2I . "Crystal Structure Of Gamma-Chymotrypsin In Complex With 7- Hydroxycoumarin" . . . . . 100.00 245 99.57 99.57 5.63e-163 . . . . 961 1 34 no PDB 1MTN . "Bovine Alpha-Chymotrypsin:bpti Crystallization" . . . . . 56.96 131 99.24 99.24 6.90e-87 . . . . 961 1 35 no PDB 1N8O . "Crystal Structure Of A Complex Between Bovine Chymotrypsin And Ecotin" . . . . . 56.96 131 99.24 99.24 6.90e-87 . . . . 961 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 99.57 99.57 5.63e-163 . . . . 961 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 99.57 99.57 5.63e-163 . . . . 961 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 99.57 99.57 5.63e-163 . . . . 961 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 99.57 99.57 5.63e-163 . . . . 961 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 99.57 99.57 5.63e-163 . . . . 961 1 41 no PDB 1T7C . "Crystal Structure Of The P1 Glu Bpti Mutant- Bovine Chymotrypsin Complex" . . . . . 100.00 245 99.57 99.57 5.63e-163 . . . . 961 1 42 no PDB 1T8L . "Crystal Structure Of The P1 Met Bpti Mutant- Bovine Chymotrypsin Complex" . . . . . 100.00 245 99.57 99.57 5.63e-163 . . . . 961 1 43 no PDB 1T8M . "Crystal Structure Of The P1 His Bpti Mutant- Bovine Chymotrypsin Complex" . . . . . 100.00 245 99.57 99.57 5.63e-163 . . . . 961 1 44 no PDB 1T8N . "Crystal Structure Of The P1 Thr Bpti Mutant- Bovine Chymotrypsin Complex" . . . . . 100.00 245 99.57 99.57 5.63e-163 . . . . 961 1 45 no PDB 1T8O . "Crystal Structure Of The P1 Trp Bpti Mutant- Bovine Chymotrypsin Complex" . . . . . 100.00 245 99.57 99.57 5.63e-163 . . . . 961 1 46 no PDB 1VGC . "Gamma-Chymotrypsin L-Para-Chloro-1-Acetamido Boronic Acid Inhibitor Complex" . . . . . 56.96 131 99.24 99.24 6.90e-87 . . . . 961 1 47 no PDB 1YPH . "High Resolution Structure Of Bovine Alpha-Chymotrypsin" . . . . . 56.96 131 99.24 99.24 6.90e-87 . . . . 961 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 99.57 99.57 5.63e-163 . . . . 961 1 49 no 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 6.90e-87 . . . . 961 1 50 no PDB 2GCH . "Refined Crystal Structure Of Gamma-chymotrypsin At 1.9 Angstroms Resolution" . . . . . 56.96 131 99.24 99.24 6.90e-87 . . . . 961 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" . . . . . 56.96 131 99.24 99.24 6.90e-87 . . . . 961 1 52 no 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 6.90e-87 . . . . 961 1 53 no PDB 2P8O . "Crystal Structure Of A Benzohydroxamic AcidVANADATE Complex Bound To Chymotrypsin A" . . . . . 56.96 131 99.24 99.24 6.90e-87 . . . . 961 1 54 no PDB 2VGC . "Gamma-Chymotrypsin D-Para-Chloro-1-Acetamido Boronic Acid Inhibitor Complex" . . . . . 56.96 131 99.24 99.24 6.90e-87 . . . . 961 1 55 no PDB 2Y6T . "Molecular Recognition Of Chymotrypsin By The Serine Protease Inhibitor Ecotin From Yersinia Pestis" . . . . . 100.00 245 99.57 99.57 5.63e-163 . . . . 961 1 56 no 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 6.90e-87 . . . . 961 1 57 no PDB 3GCH . "Chemistry Of Caged Enzymes. Binding Of Photoreversible Cinnamates To Chymotrypsin" . . . . . 56.96 131 99.24 99.24 6.90e-87 . . . . 961 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" . . . . . 56.96 131 99.24 99.24 6.90e-87 . . . . 961 1 59 no 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 6.90e-87 . . . . 961 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 99.57 99.57 5.63e-163 . . . . 961 1 61 no PDB 3VGC . "Gamma-Chymotrypsin L-Naphthyl-1-Acetamido Boronic Acid Acid Inhibitor Complex" . . . . . 56.96 131 99.24 99.24 6.90e-87 . . . . 961 1 62 no PDB 4CHA . "Structure Of Alpha-Chymotrypsin Refined At 1.68 Angstroms Resolution" . . . . . 56.96 131 99.24 99.24 6.90e-87 . . . . 961 1 63 no PDB 4GCH . "Structure And Activity Of Two Photoreversible Cinnamates Bound To Chymotrypsin" . . . . . 56.96 131 99.24 99.24 6.90e-87 . . . . 961 1 64 no PDB 4Q2K . "Bovine Alpha Chymotrypsin Bound To A Cyclic Peptide Inhibitor, 5b" . . . . . 100.00 245 99.57 99.57 5.63e-163 . . . . 961 1 65 no PDB 4VGC . "Gamma-Chymotrypsin D-Naphthyl-1-Acetamido Boronic Acid Inhibitor Complex" . . . . . 56.96 131 99.24 99.24 6.90e-87 . . . . 961 1 66 no 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 6.90e-87 . . . . 961 1 67 no PDB 5GCH . "Chemistry Of Caged Enzymes II. Photoactivation Of Inhibited Chymotrypsin" . . . . . 56.96 131 99.24 99.24 6.90e-87 . . . . 961 1 68 no PDB 6CHA . "Structure Of A Tetrahedral Transition State Complex Of Alpha-Chymotrypsin At 1.8-Angstroms Resolution" . . . . . 56.96 131 99.24 99.24 6.90e-87 . . . . 961 1 69 no PDB 6GCH . "Structure Of Chymotrypsin-Trifluoromethyl Ketone Inhibitor Complexes. Comparison Of Slowly And Rapidly Equilibrating Inhibitors" . . . . . 56.96 131 99.24 99.24 6.90e-87 . . . . 961 1 70 no PDB 7GCH . "Structure Of Chymotrypsin-Trifluoromethyl Ketone Inhibitor Complexes. Comparison Of Slowly And Rapidly Equilibrating Inhibitors" . . . . . 56.96 131 99.24 99.24 6.90e-87 . . . . 961 1 71 no PDB 8GCH . "Gamma-Chymotrypsin Is A Complex Of Alpha-Chymotrypsin With Its Own Autolysis Products" . . . . . 56.96 131 99.24 99.24 6.90e-87 . . . . 961 1 72 no REF XP_003583409 . "PREDICTED: chymotrypsinogen A [Bos taurus]" . . . . . 100.00 300 99.57 99.57 1.08e-162 . . . . 961 1 73 no REF XP_003587247 . "PREDICTED: chymotrypsinogen A [Bos taurus]" . . . . . 100.00 300 99.57 99.57 1.08e-162 . . . . 961 1 74 no REF XP_005894372 . "PREDICTED: chymotrypsinogen A-like [Bos mutus]" . . . . . 100.00 263 97.83 98.70 2.03e-159 . . . . 961 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 99.57 99.57 5.63e-163 . . . . 961 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'A-delta chymotrypsin(16-245)' variant 961 1 chymotrypsin common 961 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 1 ILE . 961 1 2 2 VAL . 961 1 3 3 ASN . 961 1 4 4 GLY . 961 1 5 5 GLU . 961 1 6 6 GLU . 961 1 7 7 ALA . 961 1 8 8 VAL . 961 1 9 9 PRO . 961 1 10 10 GLY . 961 1 11 11 SER . 961 1 12 12 TRP . 961 1 13 13 PRO . 961 1 14 14 TRP . 961 1 15 15 GLN . 961 1 16 16 VAL . 961 1 17 17 SER . 961 1 18 18 LEU . 961 1 19 19 GLN . 961 1 20 20 ASP . 961 1 21 21 LYS . 961 1 22 22 THR . 961 1 23 23 GLY . 961 1 24 24 PHE . 961 1 25 25 HIS . 961 1 26 26 PHE . 961 1 27 27 CYS . 961 1 28 28 GLY . 961 1 29 29 GLY . 961 1 30 30 SER . 961 1 31 31 LEU . 961 1 32 32 ILE . 961 1 33 33 ASN . 961 1 34 34 GLU . 961 1 35 35 ASN . 961 1 36 36 TRP . 961 1 37 37 VAL . 961 1 38 38 VAL . 961 1 39 39 THR . 961 1 40 40 ALA . 961 1 41 41 ALA . 961 1 42 42 HIS . 961 1 43 43 CYS . 961 1 44 44 GLY . 961 1 45 45 VAL . 961 1 46 46 THR . 961 1 47 47 THR . 961 1 48 48 SER . 961 1 49 49 ASP . 961 1 50 50 VAL . 961 1 51 51 VAL . 961 1 52 52 VAL . 961 1 53 53 ALA . 961 1 54 54 GLY . 961 1 55 55 GLU . 961 1 56 56 PHE . 961 1 57 57 ASP . 961 1 58 58 GLN . 961 1 59 59 GLY . 961 1 60 60 SER . 961 1 61 61 SER . 961 1 62 62 SER . 961 1 63 63 GLU . 961 1 64 64 LYS . 961 1 65 65 ILE . 961 1 66 66 GLN . 961 1 67 67 LYS . 961 1 68 68 LEU . 961 1 69 69 LYS . 961 1 70 70 ILE . 961 1 71 71 ALA . 961 1 72 72 LYS . 961 1 73 73 VAL . 961 1 74 74 PHE . 961 1 75 75 LYS . 961 1 76 76 ASN . 961 1 77 77 SER . 961 1 78 78 LYS . 961 1 79 79 TYR . 961 1 80 80 ASN . 961 1 81 81 SER . 961 1 82 82 LEU . 961 1 83 83 THR . 961 1 84 84 ILE . 961 1 85 85 ASN . 961 1 86 86 ASN . 961 1 87 87 ASP . 961 1 88 88 ILE . 961 1 89 89 THR . 961 1 90 90 LEU . 961 1 91 91 LEU . 961 1 92 92 LYS . 961 1 93 93 LEU . 961 1 94 94 SER . 961 1 95 95 THR . 961 1 96 96 ALA . 961 1 97 97 ALA . 961 1 98 98 SER . 961 1 99 99 PHE . 961 1 100 100 SER . 961 1 101 101 GLN . 961 1 102 102 THR . 961 1 103 103 VAL . 961 1 104 104 SER . 961 1 105 105 ALA . 961 1 106 106 VAL . 961 1 107 107 CYS . 961 1 108 108 LEU . 961 1 109 109 PRO . 961 1 110 110 SER . 961 1 111 111 ALA . 961 1 112 112 SER . 961 1 113 113 ASP . 961 1 114 114 ASP . 961 1 115 115 PHE . 961 1 116 116 ALA . 961 1 117 117 ALA . 961 1 118 118 GLY . 961 1 119 119 THR . 961 1 120 120 THR . 961 1 121 121 CYS . 961 1 122 122 VAL . 961 1 123 123 VAL . 961 1 124 124 THR . 961 1 125 125 GLY . 961 1 126 126 TRP . 961 1 127 127 GLY . 961 1 128 128 LEU . 961 1 129 129 THR . 961 1 130 130 ARG . 961 1 131 131 TYR . 961 1 132 132 THR . 961 1 133 133 ASN . 961 1 134 134 ALA . 961 1 135 135 ASN . 961 1 136 136 THR . 961 1 137 137 PRO . 961 1 138 138 ASP . 961 1 139 139 ARG . 961 1 140 140 LEU . 961 1 141 141 GLN . 961 1 142 142 GLN . 961 1 143 143 ALA . 961 1 144 144 SER . 961 1 145 145 LEU . 961 1 146 146 PRO . 961 1 147 147 LEU . 961 1 148 148 LEU . 961 1 149 149 SER . 961 1 150 150 ASN . 961 1 151 151 THR . 961 1 152 152 ASN . 961 1 153 153 CYS . 961 1 154 154 LYS . 961 1 155 155 LYS . 961 1 156 156 TYR . 961 1 157 157 TRP . 961 1 158 158 GLY . 961 1 159 159 THR . 961 1 160 160 LYS . 961 1 161 161 ILE . 961 1 162 162 LYS . 961 1 163 163 ASP . 961 1 164 164 ALA . 961 1 165 165 MET . 961 1 166 166 ILE . 961 1 167 167 CYS . 961 1 168 168 ALA . 961 1 169 169 GLY . 961 1 170 170 ALA . 961 1 171 171 SER . 961 1 172 172 GLY . 961 1 173 173 VAL . 961 1 174 174 SER . 961 1 175 175 SER . 961 1 176 176 CYS . 961 1 177 177 MET . 961 1 178 178 GLY . 961 1 179 179 ASP . 961 1 180 180 SER . 961 1 181 181 GLY . 961 1 182 182 GLY . 961 1 183 183 PRO . 961 1 184 184 LEU . 961 1 185 185 VAL . 961 1 186 186 CYS . 961 1 187 187 LYS . 961 1 188 188 LYS . 961 1 189 189 ASN . 961 1 190 190 GLY . 961 1 191 191 ALA . 961 1 192 192 TRP . 961 1 193 193 THR . 961 1 194 194 LEU . 961 1 195 195 VAL . 961 1 196 196 GLY . 961 1 197 197 ILE . 961 1 198 198 VAL . 961 1 199 199 SER . 961 1 200 200 TRP . 961 1 201 201 GLY . 961 1 202 202 SER . 961 1 203 203 SER . 961 1 204 204 THR . 961 1 205 205 CYS . 961 1 206 206 SER . 961 1 207 207 THR . 961 1 208 208 SER . 961 1 209 209 THR . 961 1 210 210 PRO . 961 1 211 211 GLY . 961 1 212 212 VAL . 961 1 213 213 TYR . 961 1 214 214 ALA . 961 1 215 215 ARG . 961 1 216 216 VAL . 961 1 217 217 THR . 961 1 218 218 ALA . 961 1 219 219 LEU . 961 1 220 220 VAL . 961 1 221 221 ASN . 961 1 222 222 TRP . 961 1 223 223 VAL . 961 1 224 224 GLN . 961 1 225 225 GLN . 961 1 226 226 THR . 961 1 227 227 LEU . 961 1 228 228 ALA . 961 1 229 229 ALA . 961 1 230 230 ASN . 961 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 . ILE 1 1 961 1 . VAL 2 2 961 1 . ASN 3 3 961 1 . GLY 4 4 961 1 . GLU 5 5 961 1 . GLU 6 6 961 1 . ALA 7 7 961 1 . VAL 8 8 961 1 . PRO 9 9 961 1 . GLY 10 10 961 1 . SER 11 11 961 1 . TRP 12 12 961 1 . PRO 13 13 961 1 . TRP 14 14 961 1 . GLN 15 15 961 1 . VAL 16 16 961 1 . SER 17 17 961 1 . LEU 18 18 961 1 . GLN 19 19 961 1 . ASP 20 20 961 1 . LYS 21 21 961 1 . THR 22 22 961 1 . GLY 23 23 961 1 . PHE 24 24 961 1 . HIS 25 25 961 1 . PHE 26 26 961 1 . CYS 27 27 961 1 . GLY 28 28 961 1 . GLY 29 29 961 1 . SER 30 30 961 1 . LEU 31 31 961 1 . ILE 32 32 961 1 . ASN 33 33 961 1 . GLU 34 34 961 1 . ASN 35 35 961 1 . TRP 36 36 961 1 . VAL 37 37 961 1 . VAL 38 38 961 1 . THR 39 39 961 1 . ALA 40 40 961 1 . ALA 41 41 961 1 . HIS 42 42 961 1 . CYS 43 43 961 1 . GLY 44 44 961 1 . VAL 45 45 961 1 . THR 46 46 961 1 . THR 47 47 961 1 . SER 48 48 961 1 . ASP 49 49 961 1 . VAL 50 50 961 1 . VAL 51 51 961 1 . VAL 52 52 961 1 . ALA 53 53 961 1 . GLY 54 54 961 1 . GLU 55 55 961 1 . PHE 56 56 961 1 . ASP 57 57 961 1 . GLN 58 58 961 1 . GLY 59 59 961 1 . SER 60 60 961 1 . SER 61 61 961 1 . SER 62 62 961 1 . GLU 63 63 961 1 . LYS 64 64 961 1 . ILE 65 65 961 1 . GLN 66 66 961 1 . LYS 67 67 961 1 . LEU 68 68 961 1 . LYS 69 69 961 1 . ILE 70 70 961 1 . ALA 71 71 961 1 . LYS 72 72 961 1 . VAL 73 73 961 1 . PHE 74 74 961 1 . LYS 75 75 961 1 . ASN 76 76 961 1 . SER 77 77 961 1 . LYS 78 78 961 1 . TYR 79 79 961 1 . ASN 80 80 961 1 . SER 81 81 961 1 . LEU 82 82 961 1 . THR 83 83 961 1 . ILE 84 84 961 1 . ASN 85 85 961 1 . ASN 86 86 961 1 . ASP 87 87 961 1 . ILE 88 88 961 1 . THR 89 89 961 1 . LEU 90 90 961 1 . LEU 91 91 961 1 . LYS 92 92 961 1 . LEU 93 93 961 1 . SER 94 94 961 1 . THR 95 95 961 1 . ALA 96 96 961 1 . ALA 97 97 961 1 . SER 98 98 961 1 . PHE 99 99 961 1 . SER 100 100 961 1 . GLN 101 101 961 1 . THR 102 102 961 1 . VAL 103 103 961 1 . SER 104 104 961 1 . ALA 105 105 961 1 . VAL 106 106 961 1 . CYS 107 107 961 1 . LEU 108 108 961 1 . PRO 109 109 961 1 . SER 110 110 961 1 . ALA 111 111 961 1 . SER 112 112 961 1 . ASP 113 113 961 1 . ASP 114 114 961 1 . PHE 115 115 961 1 . ALA 116 116 961 1 . ALA 117 117 961 1 . GLY 118 118 961 1 . THR 119 119 961 1 . THR 120 120 961 1 . CYS 121 121 961 1 . VAL 122 122 961 1 . VAL 123 123 961 1 . THR 124 124 961 1 . GLY 125 125 961 1 . TRP 126 126 961 1 . GLY 127 127 961 1 . LEU 128 128 961 1 . THR 129 129 961 1 . ARG 130 130 961 1 . TYR 131 131 961 1 . THR 132 132 961 1 . ASN 133 133 961 1 . ALA 134 134 961 1 . ASN 135 135 961 1 . THR 136 136 961 1 . PRO 137 137 961 1 . ASP 138 138 961 1 . ARG 139 139 961 1 . LEU 140 140 961 1 . GLN 141 141 961 1 . GLN 142 142 961 1 . ALA 143 143 961 1 . SER 144 144 961 1 . LEU 145 145 961 1 . PRO 146 146 961 1 . LEU 147 147 961 1 . LEU 148 148 961 1 . SER 149 149 961 1 . ASN 150 150 961 1 . THR 151 151 961 1 . ASN 152 152 961 1 . CYS 153 153 961 1 . LYS 154 154 961 1 . LYS 155 155 961 1 . TYR 156 156 961 1 . TRP 157 157 961 1 . GLY 158 158 961 1 . THR 159 159 961 1 . LYS 160 160 961 1 . ILE 161 161 961 1 . LYS 162 162 961 1 . ASP 163 163 961 1 . ALA 164 164 961 1 . MET 165 165 961 1 . ILE 166 166 961 1 . CYS 167 167 961 1 . ALA 168 168 961 1 . GLY 169 169 961 1 . ALA 170 170 961 1 . SER 171 171 961 1 . GLY 172 172 961 1 . VAL 173 173 961 1 . SER 174 174 961 1 . SER 175 175 961 1 . CYS 176 176 961 1 . MET 177 177 961 1 . GLY 178 178 961 1 . ASP 179 179 961 1 . SER 180 180 961 1 . GLY 181 181 961 1 . GLY 182 182 961 1 . PRO 183 183 961 1 . LEU 184 184 961 1 . VAL 185 185 961 1 . CYS 186 186 961 1 . LYS 187 187 961 1 . LYS 188 188 961 1 . ASN 189 189 961 1 . GLY 190 190 961 1 . ALA 191 191 961 1 . TRP 192 192 961 1 . THR 193 193 961 1 . LEU 194 194 961 1 . VAL 195 195 961 1 . GLY 196 196 961 1 . ILE 197 197 961 1 . VAL 198 198 961 1 . SER 199 199 961 1 . TRP 200 200 961 1 . GLY 201 201 961 1 . SER 202 202 961 1 . SER 203 203 961 1 . THR 204 204 961 1 . CYS 205 205 961 1 . SER 206 206 961 1 . THR 207 207 961 1 . SER 208 208 961 1 . THR 209 209 961 1 . PRO 210 210 961 1 . GLY 211 211 961 1 . VAL 212 212 961 1 . TYR 213 213 961 1 . ALA 214 214 961 1 . ARG 215 215 961 1 . VAL 216 216 961 1 . THR 217 217 961 1 . ALA 218 218 961 1 . LEU 219 219 961 1 . VAL 220 220 961 1 . ASN 221 221 961 1 . TRP 222 222 961 1 . VAL 223 223 961 1 . GLN 224 224 961 1 . GLN 225 225 961 1 . THR 226 226 961 1 . LEU 227 227 961 1 . ALA 228 228 961 1 . ALA 229 229 961 1 . ASN 230 230 961 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 961 _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 $chymotrypsin . 9913 organism . 'Bos taurus' cow . . Eukaryota Metazoa Bos taurus . . . . . . . . . . . . . . . . . . . . . 961 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 961 _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 $chymotrypsin . 'not available' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 961 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Sample.Sf_category sample _Sample.Sf_framecode sample_one _Sample.Entry_ID 961 _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 961 _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 961 1 temperature 277 . K 961 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 961 _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 961 _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' . . 961 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 961 _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 . . . . . . . . . . . . . . . . 961 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 961 _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 961 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 961 _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 . 961 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 42 42 HIS HD1 H 1 14.9 . . 1 . . . . . . . . 961 1 stop_ save_