data_4865 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 4865 _Entry.Title ; Backbone 1H, 13C, 15N Chemical shift Assignment for OMTKY3 bound to bovine Chymotrypsin Aa ; _Entry.Type . _Entry.Version_type original _Entry.Submission_date 2000-10-17 _Entry.Accession_date 2000-10-18 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination author _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 Jikui Song . . . 4865 2 John Markley . L . 4865 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 4865 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 45 4865 '13C chemical shifts' 85 4865 '15N chemical shifts' 46 4865 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 1 . . 2001-06-01 . update author 'update of publication' 4865 2 . . 2000-12-01 . original author 'original release' 4865 stop_ loop_ _Related_entries.Database_name _Related_entries.Database_accession_code _Related_entries.Relationship _Related_entries.Entry_ID BMRB 4864 'free form' 4865 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 4865 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation . _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 _Citation.Journal_abbrev 'J. Mol. Recognit.' _Citation.Journal_name_full . _Citation.Journal_volume 14 _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 166 _Citation.Page_last 171 _Citation.Year 2001 _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 Jikui Song . . . 4865 1 2 John Markley . L . 4865 1 stop_ loop_ _Citation_keyword.Keyword _Citation_keyword.Entry_ID _Citation_keyword.Citation_ID 'OMTKY3:CTR complex' 4865 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_OMTKY3_CTR _Assembly.Sf_category assembly _Assembly.Sf_framecode system_OMTKY3_CTR _Assembly.Entry_ID 4865 _Assembly.ID 1 _Assembly.Name 'Turkey Ovomucoid Third Domain bound to bovine chymotrypsin Aa' _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 no _Assembly.Thiol_state 'all disulfide bound' _Assembly.Molecular_mass . _Assembly.Enzyme_commission_number . _Assembly.Details . _Assembly.DB_query_date . _Assembly.DB_query_revised_last_date . loop_ _Assembly_type.Type _Assembly_type.Entry_ID _Assembly_type.Assembly_ID monomer 4865 1 stop_ 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 OMTKY3 1 $OMTKY3_CTR . . . native . . . . . 4865 1 2 'bovine chymotrypsin Aa' 2 $BCAa . . . native . . . . . 4865 1 stop_ loop_ _Bond.ID _Bond.Type _Bond.Value_order _Bond.Assembly_atom_ID_1 _Bond.Entity_assembly_ID_1 _Bond.Entity_assembly_name_1 _Bond.Entity_ID_1 _Bond.Comp_ID_1 _Bond.Comp_index_ID_1 _Bond.Seq_ID_1 _Bond.Atom_ID_1 _Bond.Assembly_atom_ID_2 _Bond.Entity_assembly_ID_2 _Bond.Entity_assembly_name_2 _Bond.Entity_ID_2 _Bond.Comp_ID_2 _Bond.Comp_index_ID_2 _Bond.Seq_ID_2 _Bond.Atom_ID_2 _Bond.Auth_entity_assembly_ID_1 _Bond.Auth_entity_assembly_name_1 _Bond.Auth_seq_ID_1 _Bond.Auth_comp_ID_1 _Bond.Auth_atom_ID_1 _Bond.Auth_entity_assembly_ID_2 _Bond.Auth_entity_assembly_name_2 _Bond.Auth_seq_ID_2 _Bond.Auth_comp_ID_2 _Bond.Auth_atom_ID_2 _Bond.Entry_ID _Bond.Assembly_ID 1 disulfide single . 1 . . CYS 8 8 SG . 1 . 1 CYS 38 38 SG . . . . . . . . . . 4865 1 2 disulfide single . 1 . . CYS 16 16 SG . 1 . 1 CYS 35 35 SG . . . . . . . . . . 4865 1 3 disulfide single . 1 . . CYS 24 24 SG . 1 . 1 CYS 56 56 SG . . . . . . . . . . 4865 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'Turkey Ovomucoid Third Domain bound to bovine chymotrypsin Aa' system 4865 1 OMTKY3_CTR abbreviation 4865 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_OMTKY3_CTR _Entity.Sf_category entity _Entity.Sf_framecode OMTKY3_CTR _Entity.Entry_ID 4865 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'Ovomucoid Third Domain from Turkey' _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 . _Entity.Polymer_seq_one_letter_code ; LAAVSVDCSEYPKPACTLEY RPLCGSDNKTYGNKCNFCNA VVESNGTLTLSHFGKC ; _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 56 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'all disulfide bound' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _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 2015-01-29 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 6881 . bovine_alpha_chymotrypsin . . . . . 100.00 241 99.59 99.59 1.52e-171 . . . . 4865 1 2 no BMRB 960 . "chymotrypsinogen A" . . . . . 101.66 245 97.96 97.96 1.16e-167 . . . . 4865 1 3 no BMRB 961 . chymotrypsin . . . . . 95.44 230 98.70 98.70 1.03e-159 . . . . 4865 1 4 no BMRB 962 . "chymotrypsinogen A" . . . . . 101.66 245 97.96 97.96 1.16e-167 . . . . 4865 1 5 no BMRB 963 . chymotrypsin . . . . . 95.44 230 98.70 98.70 1.03e-159 . . . . 4865 1 6 no BMRB 964 . "chymotrypsinogen A" . . . . . 101.66 245 97.96 97.96 1.16e-167 . . . . 4865 1 7 no BMRB 965 . chymotrypsin . . . . . 95.44 230 98.70 98.70 1.03e-159 . . . . 4865 1 8 no BMRB 966 . "chymotrypsinogen A" . . . . . 101.66 245 97.96 97.96 1.16e-167 . . . . 4865 1 9 no BMRB 967 . chymotrypsin . . . . . 95.44 230 98.70 98.70 1.03e-159 . . . . 4865 1 10 no PDB 1AB9 . "Crystal Structure Of Bovine Gamma-Chymotrypsin" . . . . . 54.36 131 100.00 100.00 2.40e-87 . . . . 4865 1 11 no 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 2.62e-168 . . . . 4865 1 12 no PDB 1AFQ . "Crystal Structure Of Bovine Gamma-Chymotrypsin Complexed With A Synthetic Inhibitor" . . . . . 54.36 131 100.00 100.00 2.40e-87 . . . . 4865 1 13 no PDB 1CA0 . "Bovine Chymotrypsin Complexed To Appi" . . . . . 54.36 131 100.00 100.00 2.40e-87 . . . . 4865 1 14 no PDB 1CBW . "Bovine Chymotrypsin Complexed To Bpti" . . . . . 54.36 131 100.00 100.00 2.40e-87 . . . . 4865 1 15 no 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 2.62e-168 . . . . 4865 1 16 no 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 2.62e-168 . . . . 4865 1 17 no PDB 1CHG . "Chymotrypsinogen,2.5 Angstroms Crystal Structure, Comparison With Alpha-Chymotrypsin,And Implications For Zymogen Activation" . . . . . 101.66 245 98.37 98.37 2.62e-168 . . . . 4865 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 " . . . . . 54.36 131 100.00 100.00 2.40e-87 . . . . 4865 1 19 no PDB 1DLK . "Crystal Structure Analysis Of Delta-Chymotrypsin Bound To A Peptidyl Chloromethyl Ketone Inhibitor" . . . . . 95.44 230 99.13 99.13 1.96e-160 . . . . 4865 1 20 no PDB 1EX3 . "Crystal Structure Of Bovine Chymotrypsinogen A (Tetragonal)" . . . . . 101.66 245 98.37 98.37 2.62e-168 . . . . 4865 1 21 no PDB 1GCD . 'Refined Crystal Structure Of "aged" And "non-Aged" Organophosphoryl Conjugates Of Gamma-Chymotrypsin' . . . . . 101.66 245 98.37 98.37 2.62e-168 . . . . 4865 1 22 no PDB 1GCT . "Is Gamma-Chymotrypsin A Tetrapeptide Acyl-Enzyme Adduct Of Gamma- Chymotrypsin?" . . . . . 54.36 131 100.00 100.00 2.40e-87 . . . . 4865 1 23 no 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 2.40e-87 . . . . 4865 1 24 no 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 2.40e-87 . . . . 4865 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" . . . . . 54.36 131 100.00 100.00 2.40e-87 . . . . 4865 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" . . . . . 54.36 131 100.00 100.00 2.40e-87 . . . . 4865 1 27 no 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 2.62e-168 . . . . 4865 1 28 no 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 2.62e-168 . . . . 4865 1 29 no PDB 1GMC . "The X-Ray Crystal Structure Of The Tetrahedral Intermediate Of Gamma- Chymotrypsin In Hexane" . . . . . 54.36 131 100.00 100.00 2.40e-87 . . . . 4865 1 30 no PDB 1GMD . "X-ray Crystal Structure Of Gamma-chymotrypsin In Hexane" . . . . . 54.36 131 100.00 100.00 2.40e-87 . . . . 4865 1 31 no PDB 1GMH . 'Refined Crystal Structure Of "aged" And "non-Aged" Organophosphoryl Conjugates Of Gamma-Chymotrypsin' . . . . . 54.36 131 100.00 100.00 2.40e-87 . . . . 4865 1 32 no PDB 1HJA . "Lys 18 Variant Of Turkey Ovomucoid Inhibitor Third Domain Complexed With Alpha-Chymotrypsin" . . . . . 54.36 131 100.00 100.00 2.40e-87 . . . . 4865 1 33 no PDB 1K2I . "Crystal Structure Of Gamma-Chymotrypsin In Complex With 7- Hydroxycoumarin" . . . . . 101.66 245 98.37 98.37 2.62e-168 . . . . 4865 1 34 no PDB 1MTN . "Bovine Alpha-Chymotrypsin:bpti Crystallization" . . . . . 54.36 131 100.00 100.00 2.40e-87 . . . . 4865 1 35 no PDB 1N8O . "Crystal Structure Of A Complex Between Bovine Chymotrypsin And Ecotin" . . . . . 54.36 131 100.00 100.00 2.40e-87 . . . . 4865 1 36 no 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 2.62e-168 . . . . 4865 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" . . . . . 101.66 245 98.37 98.37 2.62e-168 . . . . 4865 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" . . . . . 101.66 245 98.37 98.37 2.62e-168 . . . . 4865 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" . . . . . 101.66 245 98.37 98.37 2.62e-168 . . . . 4865 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" . . . . . 101.66 245 98.37 98.37 2.62e-168 . . . . 4865 1 41 no PDB 1T7C . "Crystal Structure Of The P1 Glu Bpti Mutant- Bovine Chymotrypsin Complex" . . . . . 101.66 245 98.37 98.37 2.62e-168 . . . . 4865 1 42 no PDB 1T8L . "Crystal Structure Of The P1 Met Bpti Mutant- Bovine Chymotrypsin Complex" . . . . . 101.66 245 98.37 98.37 2.62e-168 . . . . 4865 1 43 no PDB 1T8M . "Crystal Structure Of The P1 His Bpti Mutant- Bovine Chymotrypsin Complex" . . . . . 101.66 245 98.37 98.37 2.62e-168 . . . . 4865 1 44 no PDB 1T8N . "Crystal Structure Of The P1 Thr Bpti Mutant- Bovine Chymotrypsin Complex" . . . . . 101.66 245 98.37 98.37 2.62e-168 . . . . 4865 1 45 no PDB 1T8O . "Crystal Structure Of The P1 Trp Bpti Mutant- Bovine Chymotrypsin Complex" . . . . . 101.66 245 98.37 98.37 2.62e-168 . . . . 4865 1 46 no PDB 1VGC . "Gamma-Chymotrypsin L-Para-Chloro-1-Acetamido Boronic Acid Inhibitor Complex" . . . . . 54.36 131 100.00 100.00 2.40e-87 . . . . 4865 1 47 no PDB 1YPH . "High Resolution Structure Of Bovine Alpha-Chymotrypsin" . . . . . 54.36 131 100.00 100.00 2.40e-87 . . . . 4865 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" . . . . . 101.66 245 98.37 98.37 2.62e-168 . . . . 4865 1 49 no 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 2.40e-87 . . . . 4865 1 50 no PDB 2GCH . "Refined Crystal Structure Of Gamma-chymotrypsin At 1.9 Angstroms Resolution" . . . . . 54.36 131 100.00 100.00 2.40e-87 . . . . 4865 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" . . . . . 54.36 131 100.00 100.00 2.40e-87 . . . . 4865 1 52 no 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 2.40e-87 . . . . 4865 1 53 no PDB 2P8O . "Crystal Structure Of A Benzohydroxamic AcidVANADATE Complex Bound To Chymotrypsin A" . . . . . 54.36 131 100.00 100.00 2.40e-87 . . . . 4865 1 54 no PDB 2VGC . "Gamma-Chymotrypsin D-Para-Chloro-1-Acetamido Boronic Acid Inhibitor Complex" . . . . . 54.36 131 100.00 100.00 2.40e-87 . . . . 4865 1 55 no PDB 2Y6T . "Molecular Recognition Of Chymotrypsin By The Serine Protease Inhibitor Ecotin From Yersinia Pestis" . . . . . 101.66 245 98.37 98.37 2.62e-168 . . . . 4865 1 56 no 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 2.40e-87 . . . . 4865 1 57 no PDB 3GCH . "Chemistry Of Caged Enzymes. Binding Of Photoreversible Cinnamates To Chymotrypsin" . . . . . 54.36 131 100.00 100.00 2.40e-87 . . . . 4865 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" . . . . . 54.36 131 100.00 100.00 2.40e-87 . . . . 4865 1 59 no 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 2.40e-87 . . . . 4865 1 60 no 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 2.62e-168 . . . . 4865 1 61 no PDB 3VGC . "Gamma-Chymotrypsin L-Naphthyl-1-Acetamido Boronic Acid Acid Inhibitor Complex" . . . . . 54.36 131 100.00 100.00 2.40e-87 . . . . 4865 1 62 no PDB 4CHA . "Structure Of Alpha-Chymotrypsin Refined At 1.68 Angstroms Resolution" . . . . . 54.36 131 100.00 100.00 2.40e-87 . . . . 4865 1 63 no PDB 4GCH . "Structure And Activity Of Two Photoreversible Cinnamates Bound To Chymotrypsin" . . . . . 54.36 131 100.00 100.00 2.40e-87 . . . . 4865 1 64 no PDB 4Q2K . "Bovine Alpha Chymotrypsin Bound To A Cyclic Peptide Inhibitor, 5b" . . . . . 101.66 245 98.37 98.37 2.62e-168 . . . . 4865 1 65 no PDB 4VGC . "Gamma-Chymotrypsin D-Naphthyl-1-Acetamido Boronic Acid Inhibitor Complex" . . . . . 54.36 131 100.00 100.00 2.40e-87 . . . . 4865 1 66 no 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 2.40e-87 . . . . 4865 1 67 no PDB 5GCH . "Chemistry Of Caged Enzymes II. Photoactivation Of Inhibited Chymotrypsin" . . . . . 54.36 131 100.00 100.00 2.40e-87 . . . . 4865 1 68 no PDB 6CHA . "Structure Of A Tetrahedral Transition State Complex Of Alpha-Chymotrypsin At 1.8-Angstroms Resolution" . . . . . 54.36 131 100.00 100.00 2.40e-87 . . . . 4865 1 69 no PDB 6GCH . "Structure Of Chymotrypsin-Trifluoromethyl Ketone Inhibitor Complexes. Comparison Of Slowly And Rapidly Equilibrating Inhibitors" . . . . . 54.36 131 100.00 100.00 2.40e-87 . . . . 4865 1 70 no PDB 7GCH . "Structure Of Chymotrypsin-Trifluoromethyl Ketone Inhibitor Complexes. Comparison Of Slowly And Rapidly Equilibrating Inhibitors" . . . . . 54.36 131 100.00 100.00 2.40e-87 . . . . 4865 1 71 no PDB 8GCH . "Gamma-Chymotrypsin Is A Complex Of Alpha-Chymotrypsin With Its Own Autolysis Products" . . . . . 54.36 131 100.00 100.00 2.40e-87 . . . . 4865 1 72 no REF XP_003583409 . "PREDICTED: chymotrypsinogen A [Bos taurus]" . . . . . 101.66 300 98.37 98.37 7.93e-168 . . . . 4865 1 73 no REF XP_003587247 . "PREDICTED: chymotrypsinogen A [Bos taurus]" . . . . . 101.66 300 98.37 98.37 7.93e-168 . . . . 4865 1 74 no 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 2.62e-168 . . . . 4865 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'Ovomucoid Third Domain from Turkey' common 4865 1 OMTKY3 abbreviation 4865 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 . LEU . 4865 1 2 . ALA . 4865 1 3 . ALA . 4865 1 4 . VAL . 4865 1 5 . SER . 4865 1 6 . VAL . 4865 1 7 . ASP . 4865 1 8 . CYS . 4865 1 9 . SER . 4865 1 10 . GLU . 4865 1 11 . TYR . 4865 1 12 . PRO . 4865 1 13 . LYS . 4865 1 14 . PRO . 4865 1 15 . ALA . 4865 1 16 . CYS . 4865 1 17 . THR . 4865 1 18 . LEU . 4865 1 19 . GLU . 4865 1 20 . TYR . 4865 1 21 . ARG . 4865 1 22 . PRO . 4865 1 23 . LEU . 4865 1 24 . CYS . 4865 1 25 . GLY . 4865 1 26 . SER . 4865 1 27 . ASP . 4865 1 28 . ASN . 4865 1 29 . LYS . 4865 1 30 . THR . 4865 1 31 . TYR . 4865 1 32 . GLY . 4865 1 33 . ASN . 4865 1 34 . LYS . 4865 1 35 . CYS . 4865 1 36 . ASN . 4865 1 37 . PHE . 4865 1 38 . CYS . 4865 1 39 . ASN . 4865 1 40 . ALA . 4865 1 41 . VAL . 4865 1 42 . VAL . 4865 1 43 . GLU . 4865 1 44 . SER . 4865 1 45 . ASN . 4865 1 46 . GLY . 4865 1 47 . THR . 4865 1 48 . LEU . 4865 1 49 . THR . 4865 1 50 . LEU . 4865 1 51 . SER . 4865 1 52 . HIS . 4865 1 53 . PHE . 4865 1 54 . GLY . 4865 1 55 . LYS . 4865 1 56 . CYS . 4865 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 . LEU 1 1 4865 1 . ALA 2 2 4865 1 . ALA 3 3 4865 1 . VAL 4 4 4865 1 . SER 5 5 4865 1 . VAL 6 6 4865 1 . ASP 7 7 4865 1 . CYS 8 8 4865 1 . SER 9 9 4865 1 . GLU 10 10 4865 1 . TYR 11 11 4865 1 . PRO 12 12 4865 1 . LYS 13 13 4865 1 . PRO 14 14 4865 1 . ALA 15 15 4865 1 . CYS 16 16 4865 1 . THR 17 17 4865 1 . LEU 18 18 4865 1 . GLU 19 19 4865 1 . TYR 20 20 4865 1 . ARG 21 21 4865 1 . PRO 22 22 4865 1 . LEU 23 23 4865 1 . CYS 24 24 4865 1 . GLY 25 25 4865 1 . SER 26 26 4865 1 . ASP 27 27 4865 1 . ASN 28 28 4865 1 . LYS 29 29 4865 1 . THR 30 30 4865 1 . TYR 31 31 4865 1 . GLY 32 32 4865 1 . ASN 33 33 4865 1 . LYS 34 34 4865 1 . CYS 35 35 4865 1 . ASN 36 36 4865 1 . PHE 37 37 4865 1 . CYS 38 38 4865 1 . ASN 39 39 4865 1 . ALA 40 40 4865 1 . VAL 41 41 4865 1 . VAL 42 42 4865 1 . GLU 43 43 4865 1 . SER 44 44 4865 1 . ASN 45 45 4865 1 . GLY 46 46 4865 1 . THR 47 47 4865 1 . LEU 48 48 4865 1 . THR 49 49 4865 1 . LEU 50 50 4865 1 . SER 51 51 4865 1 . HIS 52 52 4865 1 . PHE 53 53 4865 1 . GLY 54 54 4865 1 . LYS 55 55 4865 1 . CYS 56 56 4865 1 stop_ save_ save_BCAa _Entity.Sf_category entity _Entity.Sf_framecode BCAa _Entity.Entry_ID 4865 _Entity.ID 2 _Entity.BMRB_code . _Entity.Name 'bovine chymotrypsin Aa' _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 . _Entity.Polymer_seq_one_letter_code ; CGVPAIQPVLSGLIVNGEEA VPGSWPWQVSLQDKTGFHFC GGSLINENWVVTAAHCGVTT SDVVVAGEFDQGSSSEKIQK LKIAKVFKNSKYNSLTINND ITLLKLSTAASFSQTVSAVC LPSASDDFAAGTTCVTTGWG LTRYANTPDRLQQASLPLLS NTNCKKYWGTKIKDAMICAG ASGVSSCMGDSGGPLVCKKN GAWTLVGIVSWGSSTCSTST PGVYARVTALVNWVQQTLAA N ; _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 241 _Entity.Number_of_nonpolymer_components . _Entity.Paramagnetic . _Entity.Thiol_state 'not reported' _Entity.Src_method . _Entity.Parent_entity_ID . _Entity.Fragment . _Entity.Mutation . _Entity.EC_number . _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date 2008-08-19 _Entity.DB_query_revised_last_date 2008-08-19 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 . . 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 . . . . 4865 2 . . REF XP_608091 . 'PREDICTED: chymotrypsinogen B1 [Bos taurus]' . . . . . 101.66 300 98.37 98.37 2.34e-133 . . . . 4865 2 . . 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 . . . . 4865 2 . . 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 . . . . 4865 2 . . 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 . . . . 4865 2 . . 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 . . . . 4865 2 . . PDB 5GCH . 'Chemistry Of Caged Enzymes II. Photoactivation Of Inhibited Chymotrypsin' . . . . . 54.36 131 100.00 100.00 6.71e-70 . . . . 4865 2 . . 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 . . . . 4865 2 . . PDB 4VGC . 'Gamma-Chymotrypsin D-Naphthyl-1-Acetamido Boronic Acid Inhibitor Complex' . . . . . 54.36 131 100.00 100.00 6.71e-70 . . . . 4865 2 . . PDB 4GCH . 'Structure And Activity Of Two Photoreversible Cinnamates Bound To Chymotrypsin' . . . . . 54.36 131 100.00 100.00 6.71e-70 . . . . 4865 2 . . PDB 4CHA . 'Structure Of Alpha-Chymotrypsin Refined At 1.68 Angstroms Resolution' . . . . . 54.36 131 100.00 100.00 6.71e-70 . . . . 4865 2 . . PDB 3VGC . 'Gamma-Chymotrypsin L-Naphthyl-1-Acetamido Boronic Acid Acid Inhibitor Complex' . . . . . 54.36 131 100.00 100.00 6.71e-70 . . . . 4865 2 . . 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 . . . . 4865 2 . . PDB 3GCH . 'Chemistry Of Caged Enzymes. Binding Of Photoreversible Cinnamates To Chymotrypsin' . . . . . 101.66 245 98.37 98.37 6.76e-133 . . . . 4865 2 . . 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 . . . . 4865 2 . . PDB 2VGC . 'Gamma-Chymotrypsin D-Para-Chloro-1-Acetamido Boronic Acid Inhibitor Complex' . . . . . 54.36 131 100.00 100.00 6.71e-70 . . . . 4865 2 . . PDB 2P8O . 'Crystal Structure Of A Benzohydroxamic AcidVANADATE Complex Bound To Chymotrypsin A' . . . . . 54.36 131 100.00 100.00 6.71e-70 . . . . 4865 2 . . 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 . . . . 4865 2 . . 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 . . . . 4865 2 . . PDB 2GCH . 'Refined Crystal Structure Of Gamma-Chymotrypsin At 1.9 Angstroms Resolution' . . . . . 54.36 131 100.00 100.00 6.71e-70 . . . . 4865 2 . . 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 . . . . 4865 2 . . 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 . . . . 4865 2 . . PDB 1YPH . 'High Resolution Structure Of Bovine Alpha-Chymotrypsin' . . . . . 54.36 131 100.00 100.00 6.71e-70 . . . . 4865 2 . . PDB 1VGC . 'Gamma-Chymotrypsin L-Para-Chloro-1-Acetamido Boronic Acid Inhibitor Complex' . . . . . 54.36 131 100.00 100.00 6.71e-70 . . . . 4865 2 . . PDB 1T8O . 'Crystal Structure Of The P1 Trp Bpti Mutant- Bovine Chymotrypsin Complex' . . . . . 101.66 245 98.37 98.37 4.53e-133 . . . . 4865 2 . . PDB 1T8N . 'Crystal Structure Of The P1 Thr Bpti Mutant- Bovine Chymotrypsin Complex' . . . . . 101.66 245 98.37 98.37 4.53e-133 . . . . 4865 2 . . PDB 1T8M . 'Crystal Structure Of The P1 His Bpti Mutant- Bovine Chymotrypsin Complex' . . . . . 101.66 245 98.37 98.37 4.53e-133 . . . . 4865 2 . . PDB 1T8L . 'Crystal Structure Of The P1 Met Bpti Mutant- Bovine Chymotrypsin Complex' . . . . . 101.66 245 98.37 98.37 4.53e-133 . . . . 4865 2 . . PDB 1T7C . 'Crystal Structure Of The P1 Glu Bpti Mutant- Bovine Chymotrypsin Complex' . . . . . 101.66 245 98.37 98.37 4.53e-133 . . . . 4865 2 . . 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 . . . . 4865 2 . . 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 . . . . 4865 2 . . 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 . . . . 4865 2 . . 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 . . . . 4865 2 . . 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 . . . . 4865 2 . . PDB 1N8O . 'Crystal Structure Of A Complex Between Bovine Chymotrypsin And Ecotin' . . . . . 54.36 131 100.00 100.00 6.71e-70 . . . . 4865 2 . . PDB 1MTN . 'Bovine Alpha-Chymotrypsin:bpti Crystallization' . . . . . 54.36 131 100.00 100.00 6.71e-70 . . . . 4865 2 . . PDB 1K2I . 'Crystal Structure Of Gamma-Chymotrypsin In Complex With 7- Hydroxycoumarin' . . . . . 101.66 245 98.37 98.37 4.53e-133 . . . . 4865 2 . . 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 . . . . 4865 2 . . 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 . . . . 4865 2 . . PDB 1GMD . 'X-Ray Crystal Structure Of Gamma-Chymotrypsin In Hexane' . . . . . 54.36 131 100.00 100.00 6.71e-70 . . . . 4865 2 . . 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 . . . . 4865 2 . . 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 . . . . 4865 2 . . 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 . . . . 4865 2 . . 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 . . . . 4865 2 . . 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 . . . . 4865 2 . . 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 . . . . 4865 2 . . 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 . . . . 4865 2 . . PDB 1GCT . 'Is Gamma-Chymotrypsin A Tetrapeptide Acyl-Enzyme Adduct Of Gamma-Chymotrypsin?' . . . . . 101.66 245 98.37 98.37 6.76e-133 . . . . 4865 2 . . 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 . . . . 4865 2 . . PDB 1EX3 . 'Crystal Structure Of Bovine Chymotrypsinogen A (Tetragonal)' . . . . . 101.66 245 98.37 98.37 4.53e-133 . . . . 4865 2 . . 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 . . . . 4865 2 . . 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 . . . . 4865 2 . . 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 . . . . 4865 2 . . 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 . . . . 4865 2 . . 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 . . . . 4865 2 . . PDB 1CBW . 'Bovine Chymotrypsin Complexed To Bpti' . . . . . 54.36 131 100.00 100.00 6.71e-70 . . . . 4865 2 . . PDB 1CA0 . 'Bovine Chymotrypsin Complexed To Appi' . . . . . 54.36 131 100.00 100.00 6.71e-70 . . . . 4865 2 . . PDB 1AFQ . 'Crystal Structure Of Bovine Gamma-Chymotrypsin Complexed With A Synthetic Inhibitor' . . . . . 54.36 131 100.00 100.00 6.71e-70 . . . . 4865 2 . . 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 . . . . 4865 2 . . PDB 1AB9 . 'Crystal Structure Of Bovine Gamma-Chymotrypsin' . . . . . 54.36 131 100.00 100.00 6.71e-70 . . . . 4865 2 . . BMRB 967 . chymotrypsin . . . . . 95.44 230 98.70 98.70 2.47e-126 . . . . 4865 2 . . BMRB 965 . chymotrypsin . . . . . 95.44 230 98.70 98.70 2.47e-126 . . . . 4865 2 . . BMRB 963 . chymotrypsin . . . . . 95.44 230 98.70 98.70 2.47e-126 . . . . 4865 2 . . BMRB 961 . chymotrypsin . . . . . 95.44 230 98.70 98.70 2.47e-126 . . . . 4865 2 . . BMRB 6881 . 'bovine alpha-chymotrypsin' . . . . . 100.00 241 99.59 99.59 1.72e-135 . . . . 4865 2 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'bovine chymotrypsin Aa' common 4865 2 BCAa abbreviation 4865 2 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 . 4865 2 2 . GLY . 4865 2 3 . VAL . 4865 2 4 . PRO . 4865 2 5 . ALA . 4865 2 6 . ILE . 4865 2 7 . GLN . 4865 2 8 . PRO . 4865 2 9 . VAL . 4865 2 10 . LEU . 4865 2 11 . SER . 4865 2 12 . GLY . 4865 2 13 . LEU . 4865 2 14 . ILE . 4865 2 15 . VAL . 4865 2 16 . ASN . 4865 2 17 . GLY . 4865 2 18 . GLU . 4865 2 19 . GLU . 4865 2 20 . ALA . 4865 2 21 . VAL . 4865 2 22 . PRO . 4865 2 23 . GLY . 4865 2 24 . SER . 4865 2 25 . TRP . 4865 2 26 . PRO . 4865 2 27 . TRP . 4865 2 28 . GLN . 4865 2 29 . VAL . 4865 2 30 . SER . 4865 2 31 . LEU . 4865 2 32 . GLN . 4865 2 33 . ASP . 4865 2 34 . LYS . 4865 2 35 . THR . 4865 2 36 . GLY . 4865 2 37 . PHE . 4865 2 38 . HIS . 4865 2 39 . PHE . 4865 2 40 . CYS . 4865 2 41 . GLY . 4865 2 42 . GLY . 4865 2 43 . SER . 4865 2 44 . LEU . 4865 2 45 . ILE . 4865 2 46 . ASN . 4865 2 47 . GLU . 4865 2 48 . ASN . 4865 2 49 . TRP . 4865 2 50 . VAL . 4865 2 51 . VAL . 4865 2 52 . THR . 4865 2 53 . ALA . 4865 2 54 . ALA . 4865 2 55 . HIS . 4865 2 56 . CYS . 4865 2 57 . GLY . 4865 2 58 . VAL . 4865 2 59 . THR . 4865 2 60 . THR . 4865 2 61 . SER . 4865 2 62 . ASP . 4865 2 63 . VAL . 4865 2 64 . VAL . 4865 2 65 . VAL . 4865 2 66 . ALA . 4865 2 67 . GLY . 4865 2 68 . GLU . 4865 2 69 . PHE . 4865 2 70 . ASP . 4865 2 71 . GLN . 4865 2 72 . GLY . 4865 2 73 . SER . 4865 2 74 . SER . 4865 2 75 . SER . 4865 2 76 . GLU . 4865 2 77 . LYS . 4865 2 78 . ILE . 4865 2 79 . GLN . 4865 2 80 . LYS . 4865 2 81 . LEU . 4865 2 82 . LYS . 4865 2 83 . ILE . 4865 2 84 . ALA . 4865 2 85 . LYS . 4865 2 86 . VAL . 4865 2 87 . PHE . 4865 2 88 . LYS . 4865 2 89 . ASN . 4865 2 90 . SER . 4865 2 91 . LYS . 4865 2 92 . TYR . 4865 2 93 . ASN . 4865 2 94 . SER . 4865 2 95 . LEU . 4865 2 96 . THR . 4865 2 97 . ILE . 4865 2 98 . ASN . 4865 2 99 . ASN . 4865 2 100 . ASP . 4865 2 101 . ILE . 4865 2 102 . THR . 4865 2 103 . LEU . 4865 2 104 . LEU . 4865 2 105 . LYS . 4865 2 106 . LEU . 4865 2 107 . SER . 4865 2 108 . THR . 4865 2 109 . ALA . 4865 2 110 . ALA . 4865 2 111 . SER . 4865 2 112 . PHE . 4865 2 113 . SER . 4865 2 114 . GLN . 4865 2 115 . THR . 4865 2 116 . VAL . 4865 2 117 . SER . 4865 2 118 . ALA . 4865 2 119 . VAL . 4865 2 120 . CYS . 4865 2 121 . LEU . 4865 2 122 . PRO . 4865 2 123 . SER . 4865 2 124 . ALA . 4865 2 125 . SER . 4865 2 126 . ASP . 4865 2 127 . ASP . 4865 2 128 . PHE . 4865 2 129 . ALA . 4865 2 130 . ALA . 4865 2 131 . GLY . 4865 2 132 . THR . 4865 2 133 . THR . 4865 2 134 . CYS . 4865 2 135 . VAL . 4865 2 136 . THR . 4865 2 137 . THR . 4865 2 138 . GLY . 4865 2 139 . TRP . 4865 2 140 . GLY . 4865 2 141 . LEU . 4865 2 142 . THR . 4865 2 143 . ARG . 4865 2 144 . TYR . 4865 2 145 . ALA . 4865 2 146 . ASN . 4865 2 147 . THR . 4865 2 148 . PRO . 4865 2 149 . ASP . 4865 2 150 . ARG . 4865 2 151 . LEU . 4865 2 152 . GLN . 4865 2 153 . GLN . 4865 2 154 . ALA . 4865 2 155 . SER . 4865 2 156 . LEU . 4865 2 157 . PRO . 4865 2 158 . LEU . 4865 2 159 . LEU . 4865 2 160 . SER . 4865 2 161 . ASN . 4865 2 162 . THR . 4865 2 163 . ASN . 4865 2 164 . CYS . 4865 2 165 . LYS . 4865 2 166 . LYS . 4865 2 167 . TYR . 4865 2 168 . TRP . 4865 2 169 . GLY . 4865 2 170 . THR . 4865 2 171 . LYS . 4865 2 172 . ILE . 4865 2 173 . LYS . 4865 2 174 . ASP . 4865 2 175 . ALA . 4865 2 176 . MET . 4865 2 177 . ILE . 4865 2 178 . CYS . 4865 2 179 . ALA . 4865 2 180 . GLY . 4865 2 181 . ALA . 4865 2 182 . SER . 4865 2 183 . GLY . 4865 2 184 . VAL . 4865 2 185 . SER . 4865 2 186 . SER . 4865 2 187 . CYS . 4865 2 188 . MET . 4865 2 189 . GLY . 4865 2 190 . ASP . 4865 2 191 . SER . 4865 2 192 . GLY . 4865 2 193 . GLY . 4865 2 194 . PRO . 4865 2 195 . LEU . 4865 2 196 . VAL . 4865 2 197 . CYS . 4865 2 198 . LYS . 4865 2 199 . LYS . 4865 2 200 . ASN . 4865 2 201 . GLY . 4865 2 202 . ALA . 4865 2 203 . TRP . 4865 2 204 . THR . 4865 2 205 . LEU . 4865 2 206 . VAL . 4865 2 207 . GLY . 4865 2 208 . ILE . 4865 2 209 . VAL . 4865 2 210 . SER . 4865 2 211 . TRP . 4865 2 212 . GLY . 4865 2 213 . SER . 4865 2 214 . SER . 4865 2 215 . THR . 4865 2 216 . CYS . 4865 2 217 . SER . 4865 2 218 . THR . 4865 2 219 . SER . 4865 2 220 . THR . 4865 2 221 . PRO . 4865 2 222 . GLY . 4865 2 223 . VAL . 4865 2 224 . TYR . 4865 2 225 . ALA . 4865 2 226 . ARG . 4865 2 227 . VAL . 4865 2 228 . THR . 4865 2 229 . ALA . 4865 2 230 . LEU . 4865 2 231 . VAL . 4865 2 232 . ASN . 4865 2 233 . TRP . 4865 2 234 . VAL . 4865 2 235 . GLN . 4865 2 236 . GLN . 4865 2 237 . THR . 4865 2 238 . LEU . 4865 2 239 . ALA . 4865 2 240 . ALA . 4865 2 241 . ASN . 4865 2 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 4865 2 . GLY 2 2 4865 2 . VAL 3 3 4865 2 . PRO 4 4 4865 2 . ALA 5 5 4865 2 . ILE 6 6 4865 2 . GLN 7 7 4865 2 . PRO 8 8 4865 2 . VAL 9 9 4865 2 . LEU 10 10 4865 2 . SER 11 11 4865 2 . GLY 12 12 4865 2 . LEU 13 13 4865 2 . ILE 14 14 4865 2 . VAL 15 15 4865 2 . ASN 16 16 4865 2 . GLY 17 17 4865 2 . GLU 18 18 4865 2 . GLU 19 19 4865 2 . ALA 20 20 4865 2 . VAL 21 21 4865 2 . PRO 22 22 4865 2 . GLY 23 23 4865 2 . SER 24 24 4865 2 . TRP 25 25 4865 2 . PRO 26 26 4865 2 . TRP 27 27 4865 2 . GLN 28 28 4865 2 . VAL 29 29 4865 2 . SER 30 30 4865 2 . LEU 31 31 4865 2 . GLN 32 32 4865 2 . ASP 33 33 4865 2 . LYS 34 34 4865 2 . THR 35 35 4865 2 . GLY 36 36 4865 2 . PHE 37 37 4865 2 . HIS 38 38 4865 2 . PHE 39 39 4865 2 . CYS 40 40 4865 2 . GLY 41 41 4865 2 . GLY 42 42 4865 2 . SER 43 43 4865 2 . LEU 44 44 4865 2 . ILE 45 45 4865 2 . ASN 46 46 4865 2 . GLU 47 47 4865 2 . ASN 48 48 4865 2 . TRP 49 49 4865 2 . VAL 50 50 4865 2 . VAL 51 51 4865 2 . THR 52 52 4865 2 . ALA 53 53 4865 2 . ALA 54 54 4865 2 . HIS 55 55 4865 2 . CYS 56 56 4865 2 . GLY 57 57 4865 2 . VAL 58 58 4865 2 . THR 59 59 4865 2 . THR 60 60 4865 2 . SER 61 61 4865 2 . ASP 62 62 4865 2 . VAL 63 63 4865 2 . VAL 64 64 4865 2 . VAL 65 65 4865 2 . ALA 66 66 4865 2 . GLY 67 67 4865 2 . GLU 68 68 4865 2 . PHE 69 69 4865 2 . ASP 70 70 4865 2 . GLN 71 71 4865 2 . GLY 72 72 4865 2 . SER 73 73 4865 2 . SER 74 74 4865 2 . SER 75 75 4865 2 . GLU 76 76 4865 2 . LYS 77 77 4865 2 . ILE 78 78 4865 2 . GLN 79 79 4865 2 . LYS 80 80 4865 2 . LEU 81 81 4865 2 . LYS 82 82 4865 2 . ILE 83 83 4865 2 . ALA 84 84 4865 2 . LYS 85 85 4865 2 . VAL 86 86 4865 2 . PHE 87 87 4865 2 . LYS 88 88 4865 2 . ASN 89 89 4865 2 . SER 90 90 4865 2 . LYS 91 91 4865 2 . TYR 92 92 4865 2 . ASN 93 93 4865 2 . SER 94 94 4865 2 . LEU 95 95 4865 2 . THR 96 96 4865 2 . ILE 97 97 4865 2 . ASN 98 98 4865 2 . ASN 99 99 4865 2 . ASP 100 100 4865 2 . ILE 101 101 4865 2 . THR 102 102 4865 2 . LEU 103 103 4865 2 . LEU 104 104 4865 2 . LYS 105 105 4865 2 . LEU 106 106 4865 2 . SER 107 107 4865 2 . THR 108 108 4865 2 . ALA 109 109 4865 2 . ALA 110 110 4865 2 . SER 111 111 4865 2 . PHE 112 112 4865 2 . SER 113 113 4865 2 . GLN 114 114 4865 2 . THR 115 115 4865 2 . VAL 116 116 4865 2 . SER 117 117 4865 2 . ALA 118 118 4865 2 . VAL 119 119 4865 2 . CYS 120 120 4865 2 . LEU 121 121 4865 2 . PRO 122 122 4865 2 . SER 123 123 4865 2 . ALA 124 124 4865 2 . SER 125 125 4865 2 . ASP 126 126 4865 2 . ASP 127 127 4865 2 . PHE 128 128 4865 2 . ALA 129 129 4865 2 . ALA 130 130 4865 2 . GLY 131 131 4865 2 . THR 132 132 4865 2 . THR 133 133 4865 2 . CYS 134 134 4865 2 . VAL 135 135 4865 2 . THR 136 136 4865 2 . THR 137 137 4865 2 . GLY 138 138 4865 2 . TRP 139 139 4865 2 . GLY 140 140 4865 2 . LEU 141 141 4865 2 . THR 142 142 4865 2 . ARG 143 143 4865 2 . TYR 144 144 4865 2 . ALA 145 145 4865 2 . ASN 146 146 4865 2 . THR 147 147 4865 2 . PRO 148 148 4865 2 . ASP 149 149 4865 2 . ARG 150 150 4865 2 . LEU 151 151 4865 2 . GLN 152 152 4865 2 . GLN 153 153 4865 2 . ALA 154 154 4865 2 . SER 155 155 4865 2 . LEU 156 156 4865 2 . PRO 157 157 4865 2 . LEU 158 158 4865 2 . LEU 159 159 4865 2 . SER 160 160 4865 2 . ASN 161 161 4865 2 . THR 162 162 4865 2 . ASN 163 163 4865 2 . CYS 164 164 4865 2 . LYS 165 165 4865 2 . LYS 166 166 4865 2 . TYR 167 167 4865 2 . TRP 168 168 4865 2 . GLY 169 169 4865 2 . THR 170 170 4865 2 . LYS 171 171 4865 2 . ILE 172 172 4865 2 . LYS 173 173 4865 2 . ASP 174 174 4865 2 . ALA 175 175 4865 2 . MET 176 176 4865 2 . ILE 177 177 4865 2 . CYS 178 178 4865 2 . ALA 179 179 4865 2 . GLY 180 180 4865 2 . ALA 181 181 4865 2 . SER 182 182 4865 2 . GLY 183 183 4865 2 . VAL 184 184 4865 2 . SER 185 185 4865 2 . SER 186 186 4865 2 . CYS 187 187 4865 2 . MET 188 188 4865 2 . GLY 189 189 4865 2 . ASP 190 190 4865 2 . SER 191 191 4865 2 . GLY 192 192 4865 2 . GLY 193 193 4865 2 . PRO 194 194 4865 2 . LEU 195 195 4865 2 . VAL 196 196 4865 2 . CYS 197 197 4865 2 . LYS 198 198 4865 2 . LYS 199 199 4865 2 . ASN 200 200 4865 2 . GLY 201 201 4865 2 . ALA 202 202 4865 2 . TRP 203 203 4865 2 . THR 204 204 4865 2 . LEU 205 205 4865 2 . VAL 206 206 4865 2 . GLY 207 207 4865 2 . ILE 208 208 4865 2 . VAL 209 209 4865 2 . SER 210 210 4865 2 . TRP 211 211 4865 2 . GLY 212 212 4865 2 . SER 213 213 4865 2 . SER 214 214 4865 2 . THR 215 215 4865 2 . CYS 216 216 4865 2 . SER 217 217 4865 2 . THR 218 218 4865 2 . SER 219 219 4865 2 . THR 220 220 4865 2 . PRO 221 221 4865 2 . GLY 222 222 4865 2 . VAL 223 223 4865 2 . TYR 224 224 4865 2 . ALA 225 225 4865 2 . ARG 226 226 4865 2 . VAL 227 227 4865 2 . THR 228 228 4865 2 . ALA 229 229 4865 2 . LEU 230 230 4865 2 . VAL 231 231 4865 2 . ASN 232 232 4865 2 . TRP 233 233 4865 2 . VAL 234 234 4865 2 . GLN 235 235 4865 2 . GLN 236 236 4865 2 . THR 237 237 4865 2 . LEU 238 238 4865 2 . ALA 239 239 4865 2 . ALA 240 240 4865 2 . ASN 241 241 4865 2 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 4865 _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 $OMTKY3_CTR . 9103 . . 'Meleagris Gallopavo' Turkey . . Eukaryota Metazoa Meleagris Gallopavo . . . . . . . . . . . . . . . . . . . . . 4865 1 2 2 $BCAa . 9913 . . 'Bos taurus' Cow . . Eukaryota Metazoa Bos taurus . . . . . . . . . . . . . . . . . . . . . 4865 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 4865 _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 $OMTKY3_CTR . 'recombinant technology' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4865 1 2 2 $BCAa . 'purified from the natural source' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4865 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_Sample_1 _Sample.Sf_category sample _Sample.Sf_framecode Sample_1 _Sample.Entry_ID 4865 _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 . loop_ _Sample_component.ID _Sample_component.Mol_common_name _Sample_component.Isotopic_labeling _Sample_component.Assembly_ID _Sample_component.Assembly_label _Sample_component.Entity_ID _Sample_component.Entity_label _Sample_component.Product_ID _Sample_component.Type _Sample_component.Concentration_val _Sample_component.Concentration_val_min _Sample_component.Concentration_val_max _Sample_component.Concentration_val_units _Sample_component.Concentration_val_err _Sample_component.Vendor _Sample_component.Vendor_product_name _Sample_component.Vendor_product_code _Sample_component.Entry_ID _Sample_component.Sample_ID 1 'Ovomucoid Third Domain from Turkey' '[U-13C; U-15N]' . . 1 $OMTKY3_CTR . . 2 . . mM . . . . 4865 1 2 'bovine chymotrypsin Aa' . . . 2 $BCAa . . 2 . . mM . . . . 4865 1 stop_ save_ ####################### # Sample conditions # ####################### save_condition_1 _Sample_condition_list.Sf_category sample_conditions _Sample_condition_list.Sf_framecode condition_1 _Sample_condition_list.Entry_ID 4865 _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 7.3 0.2 n/a 4865 1 temperature 298 1 K 4865 1 stop_ save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer _NMR_spectrometer.Sf_category NMR_spectrometer _NMR_spectrometer.Sf_framecode NMR_spectrometer _NMR_spectrometer.Entry_ID 4865 _NMR_spectrometer.ID 1 _NMR_spectrometer.Details . _NMR_spectrometer.Manufacturer Bruker _NMR_spectrometer.Model DMX _NMR_spectrometer.Serial_number . _NMR_spectrometer.Field_strength 600 save_ save_spectrometer_list _NMR_spectrometer_list.Sf_category NMR_spectrometer_list _NMR_spectrometer_list.Sf_framecode spectrometer_list _NMR_spectrometer_list.Entry_ID 4865 _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 NMR_spectrometer Bruker DMX . 600 . . . 4865 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 4865 _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 HNCA . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4865 1 2 HN(CO)CA . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4865 1 3 HNCO . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 4865 1 stop_ save_ save_NMR_spec_expt__0_1 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_1 _NMR_spec_expt.Entry_ID 4865 _NMR_spec_expt.ID 1 _NMR_spec_expt.Name HNCA _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_2 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_2 _NMR_spec_expt.Entry_ID 4865 _NMR_spec_expt.ID 2 _NMR_spec_expt.Name HN(CO)CA _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ save_NMR_spec_expt__0_3 _NMR_spec_expt.Sf_category NMR_spectrometer_expt _NMR_spec_expt.Sf_framecode NMR_spec_expt__0_3 _NMR_spec_expt.Entry_ID 4865 _NMR_spec_expt.ID 3 _NMR_spec_expt.Name HNCO _NMR_spec_expt.Type . _NMR_spec_expt.Sample_volume . _NMR_spec_expt.Sample_volume_units . _NMR_spec_expt.NMR_tube_type . _NMR_spec_expt.Sample_spinning_rate . _NMR_spec_expt.Sample_angle . _NMR_spec_expt.NMR_spectrometer_ID . _NMR_spec_expt.NMR_spectrometer_label . _NMR_spec_expt.NMR_spectrometer_probe_ID . _NMR_spec_expt.NMR_spectrometer_probe_label . _NMR_spec_expt.Carrier_freq_switch_time . _NMR_spec_expt.Software_ID . _NMR_spec_expt.Software_label . _NMR_spec_expt.Method_ID . _NMR_spec_expt.Method_label . _NMR_spec_expt.Pulse_seq_accession_BMRB_code . _NMR_spec_expt.Details . save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference _Chem_shift_reference.Sf_category chem_shift_reference _Chem_shift_reference.Sf_framecode chemical_shift_reference _Chem_shift_reference.Entry_ID 4865 _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 1 DSS 'methyl protons' . . . . ppm 0.0 internal direct 1.0 . . . . . . . . . 4865 1 N 15 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.101329118 . . . . . . . . . 4865 1 C 13 DSS 'methyl protons' . . . . ppm 0.0 . indirect 0.251449530 . . . . . . . . . 4865 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_shifts_OMTKY3_pH7.3 _Assigned_chem_shift_list.Sf_category assigned_chemical_shifts _Assigned_chem_shift_list.Sf_framecode chemical_shifts_OMTKY3_pH7.3 _Assigned_chem_shift_list.Entry_ID 4865 _Assigned_chem_shift_list.ID 1 _Assigned_chem_shift_list.Sample_condition_list_ID 1 _Assigned_chem_shift_list.Sample_condition_list_label $condition_1 _Assigned_chem_shift_list.Chem_shift_reference_ID 1 _Assigned_chem_shift_list.Chem_shift_reference_label $chemical_shift_reference _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 HNCA 1 $Sample_1 . 4865 1 2 HN(CO)CA 1 $Sample_1 . 4865 1 3 HNCO 1 $Sample_1 . 4865 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 8 8 CYS C C 13 176.88 0.1 . 1 . . . . . . . . 4865 1 2 . 1 1 8 8 CYS H H 1 8.88 0.05 . 1 . . . . . . . . 4865 1 3 . 1 1 8 8 CYS N N 15 126.88 0.1 . 1 . . . . . . . . 4865 1 4 . 1 1 9 9 SER C C 13 175.63 0.1 . 1 . . . . . . . . 4865 1 5 . 1 1 9 9 SER CA C 13 62.30 0.1 . 1 . . . . . . . . 4865 1 6 . 1 1 9 9 SER H H 1 8.72 0.05 . 1 . . . . . . . . 4865 1 7 . 1 1 9 9 SER N N 15 120.51 0.1 . 1 . . . . . . . . 4865 1 8 . 1 1 10 10 GLU C C 13 174.32 0.1 . 1 . . . . . . . . 4865 1 9 . 1 1 10 10 GLU CA C 13 56.82 0.1 . 1 . . . . . . . . 4865 1 10 . 1 1 10 10 GLU H H 1 8.87 0.05 . 1 . . . . . . . . 4865 1 11 . 1 1 10 10 GLU N N 15 119.92 0.1 . 1 . . . . . . . . 4865 1 12 . 1 1 11 11 TYR CA C 13 58.19 0.1 . 1 . . . . . . . . 4865 1 13 . 1 1 11 11 TYR H H 1 7.50 0.05 . 1 . . . . . . . . 4865 1 14 . 1 1 11 11 TYR N N 15 119.83 0.1 . 1 . . . . . . . . 4865 1 15 . 1 1 12 12 PRO C C 13 175.51 0.1 . 1 . . . . . . . . 4865 1 16 . 1 1 12 12 PRO CA C 13 62.23 0.1 . 1 . . . . . . . . 4865 1 17 . 1 1 13 13 LYS CA C 13 53.88 0.1 . 1 . . . . . . . . 4865 1 18 . 1 1 13 13 LYS H H 1 9.52 0.05 . 1 . . . . . . . . 4865 1 19 . 1 1 13 13 LYS N N 15 120.66 0.1 . 1 . . . . . . . . 4865 1 20 . 1 1 14 14 PRO C C 13 175.06 0.1 . 1 . . . . . . . . 4865 1 21 . 1 1 14 14 PRO CA C 13 63.24 0.1 . 1 . . . . . . . . 4865 1 22 . 1 1 15 15 ALA C C 13 176.08 0.1 . 1 . . . . . . . . 4865 1 23 . 1 1 15 15 ALA CA C 13 50.02 0.1 . 1 . . . . . . . . 4865 1 24 . 1 1 15 15 ALA H H 1 7.29 0.05 . 1 . . . . . . . . 4865 1 25 . 1 1 15 15 ALA N N 15 123.93 0.1 . 1 . . . . . . . . 4865 1 26 . 1 1 16 16 CYS C C 13 175.52 0.1 . 1 . . . . . . . . 4865 1 27 . 1 1 16 16 CYS CA C 13 51.30 0.1 . 1 . . . . . . . . 4865 1 28 . 1 1 16 16 CYS H H 1 8.87 0.05 . 1 . . . . . . . . 4865 1 29 . 1 1 16 16 CYS N N 15 116.23 0.1 . 1 . . . . . . . . 4865 1 30 . 1 1 17 17 THR C C 13 176.41 0.1 . 1 . . . . . . . . 4865 1 31 . 1 1 17 17 THR CA C 13 62.62 0.1 . 1 . . . . . . . . 4865 1 32 . 1 1 17 17 THR H H 1 7.77 0.05 . 1 . . . . . . . . 4865 1 33 . 1 1 17 17 THR N N 15 111.47 0.1 . 1 . . . . . . . . 4865 1 34 . 1 1 18 18 LEU CA C 13 55.20 0.1 . 1 . . . . . . . . 4865 1 35 . 1 1 18 18 LEU H H 1 8.21 0.05 . 1 . . . . . . . . 4865 1 36 . 1 1 18 18 LEU N N 15 120.10 0.1 . 1 . . . . . . . . 4865 1 37 . 1 1 19 19 GLU C C 13 175.10 0.1 . 1 . . . . . . . . 4865 1 38 . 1 1 19 19 GLU H H 1 7.95 0.05 . 1 . . . . . . . . 4865 1 39 . 1 1 19 19 GLU N N 15 131.45 0.1 . 1 . . . . . . . . 4865 1 40 . 1 1 20 20 TYR CA C 13 57.02 0.1 . 1 . . . . . . . . 4865 1 41 . 1 1 20 20 TYR H H 1 9.11 0.05 . 1 . . . . . . . . 4865 1 42 . 1 1 20 20 TYR N N 15 123.99 0.1 . 1 . . . . . . . . 4865 1 43 . 1 1 21 21 ARG HE H 1 6.98 0.05 . 1 . . . . . . . . 4865 1 44 . 1 1 21 21 ARG NE N 15 116.38 0.1 . 1 . . . . . . . . 4865 1 45 . 1 1 23 23 LEU C C 13 173.68 0.1 . 1 . . . . . . . . 4865 1 46 . 1 1 24 24 CYS C C 13 175.63 0.1 . 1 . . . . . . . . 4865 1 47 . 1 1 24 24 CYS CA C 13 54.48 0.1 . 1 . . . . . . . . 4865 1 48 . 1 1 24 24 CYS H H 1 8.22 0.05 . 1 . . . . . . . . 4865 1 49 . 1 1 24 24 CYS N N 15 121.90 0.1 . 1 . . . . . . . . 4865 1 50 . 1 1 25 25 GLY C C 13 174.86 0.1 . 1 . . . . . . . . 4865 1 51 . 1 1 25 25 GLY CA C 13 45.38 0.1 . 1 . . . . . . . . 4865 1 52 . 1 1 25 25 GLY H H 1 9.39 0.05 . 1 . . . . . . . . 4865 1 53 . 1 1 25 25 GLY N N 15 116.69 0.1 . 1 . . . . . . . . 4865 1 54 . 1 1 26 26 SER C C 13 173.80 0.1 . 1 . . . . . . . . 4865 1 55 . 1 1 26 26 SER CA C 13 60.87 0.1 . 1 . . . . . . . . 4865 1 56 . 1 1 26 26 SER H H 1 9.36 0.05 . 1 . . . . . . . . 4865 1 57 . 1 1 26 26 SER N N 15 119.15 0.1 . 1 . . . . . . . . 4865 1 58 . 1 1 27 27 ASP C C 13 176.27 0.1 . 1 . . . . . . . . 4865 1 59 . 1 1 27 27 ASP CA C 13 53.11 0.1 . 1 . . . . . . . . 4865 1 60 . 1 1 27 27 ASP H H 1 8.44 0.05 . 1 . . . . . . . . 4865 1 61 . 1 1 27 27 ASP N N 15 122.47 0.1 . 1 . . . . . . . . 4865 1 62 . 1 1 28 28 ASN C C 13 173.74 0.1 . 1 . . . . . . . . 4865 1 63 . 1 1 28 28 ASN CA C 13 55.00 0.1 . 1 . . . . . . . . 4865 1 64 . 1 1 28 28 ASN H H 1 8.66 0.05 . 1 . . . . . . . . 4865 1 65 . 1 1 28 28 ASN N N 15 117.01 0.1 . 1 . . . . . . . . 4865 1 66 . 1 1 29 29 LYS C C 13 174.43 0.1 . 1 . . . . . . . . 4865 1 67 . 1 1 29 29 LYS CA C 13 55.00 0.1 . 1 . . . . . . . . 4865 1 68 . 1 1 29 29 LYS H H 1 7.89 0.05 . 1 . . . . . . . . 4865 1 69 . 1 1 29 29 LYS N N 15 120.80 0.1 . 1 . . . . . . . . 4865 1 70 . 1 1 30 30 THR C C 13 174.57 0.1 . 1 . . . . . . . . 4865 1 71 . 1 1 30 30 THR CA C 13 62.58 0.1 . 1 . . . . . . . . 4865 1 72 . 1 1 30 30 THR H H 1 8.19 0.05 . 1 . . . . . . . . 4865 1 73 . 1 1 30 30 THR N N 15 122.19 0.1 . 1 . . . . . . . . 4865 1 74 . 1 1 31 31 TYR C C 13 176.93 0.1 . 1 . . . . . . . . 4865 1 75 . 1 1 31 31 TYR CA C 13 58.14 0.1 . 1 . . . . . . . . 4865 1 76 . 1 1 31 31 TYR H H 1 9.75 0.05 . 1 . . . . . . . . 4865 1 77 . 1 1 31 31 TYR N N 15 131.16 0.1 . 1 . . . . . . . . 4865 1 78 . 1 1 32 32 GLY C C 13 171.36 0.1 . 1 . . . . . . . . 4865 1 79 . 1 1 32 32 GLY CA C 13 47.91 0.1 . 1 . . . . . . . . 4865 1 80 . 1 1 32 32 GLY H H 1 9.09 0.05 . 1 . . . . . . . . 4865 1 81 . 1 1 32 32 GLY N N 15 110.28 0.1 . 1 . . . . . . . . 4865 1 82 . 1 1 33 33 ASN C C 13 175.93 0.1 . 1 . . . . . . . . 4865 1 83 . 1 1 33 33 ASN CA C 13 51.83 0.1 . 1 . . . . . . . . 4865 1 84 . 1 1 33 33 ASN H H 1 7.77 0.05 . 1 . . . . . . . . 4865 1 85 . 1 1 33 33 ASN N N 15 109.99 0.1 . 1 . . . . . . . . 4865 1 86 . 1 1 33 33 ASN ND2 N 15 118.60 0.1 . 1 . . . . . . . . 4865 1 87 . 1 1 34 34 LYS C C 13 175.81 0.1 . 1 . . . . . . . . 4865 1 88 . 1 1 34 34 LYS CA C 13 60.22 0.1 . 1 . . . . . . . . 4865 1 89 . 1 1 34 34 LYS H H 1 9.01 0.05 . 1 . . . . . . . . 4865 1 90 . 1 1 34 34 LYS N N 15 119.93 0.1 . 1 . . . . . . . . 4865 1 91 . 1 1 35 35 CYS C C 13 175.84 0.1 . 1 . . . . . . . . 4865 1 92 . 1 1 35 35 CYS CA C 13 58.24 0.1 . 1 . . . . . . . . 4865 1 93 . 1 1 35 35 CYS H H 1 8.14 0.05 . 1 . . . . . . . . 4865 1 94 . 1 1 35 35 CYS N N 15 122.46 0.1 . 1 . . . . . . . . 4865 1 95 . 1 1 36 36 ASN C C 13 178.32 0.1 . 1 . . . . . . . . 4865 1 96 . 1 1 36 36 ASN CA C 13 56.41 0.1 . 1 . . . . . . . . 4865 1 97 . 1 1 36 36 ASN H H 1 8.40 0.05 . 1 . . . . . . . . 4865 1 98 . 1 1 36 36 ASN N N 15 118.95 0.1 . 1 . . . . . . . . 4865 1 99 . 1 1 37 37 PHE C C 13 175.94 0.1 . 1 . . . . . . . . 4865 1 100 . 1 1 37 37 PHE CA C 13 61.23 0.1 . 1 . . . . . . . . 4865 1 101 . 1 1 37 37 PHE H H 1 8.53 0.05 . 1 . . . . . . . . 4865 1 102 . 1 1 37 37 PHE N N 15 119.85 0.1 . 1 . . . . . . . . 4865 1 103 . 1 1 38 38 CYS C C 13 177.64 0.1 . 1 . . . . . . . . 4865 1 104 . 1 1 38 38 CYS CA C 13 55.34 0.1 . 1 . . . . . . . . 4865 1 105 . 1 1 38 38 CYS H H 1 9.13 0.05 . 1 . . . . . . . . 4865 1 106 . 1 1 38 38 CYS N N 15 117.91 0.1 . 1 . . . . . . . . 4865 1 107 . 1 1 39 39 ASN C C 13 177.48 0.1 . 1 . . . . . . . . 4865 1 108 . 1 1 39 39 ASN CA C 13 56.33 0.1 . 1 . . . . . . . . 4865 1 109 . 1 1 39 39 ASN H H 1 8.02 0.05 . 1 . . . . . . . . 4865 1 110 . 1 1 39 39 ASN N N 15 120.38 0.1 . 1 . . . . . . . . 4865 1 111 . 1 1 40 40 ALA C C 13 181.16 0.1 . 1 . . . . . . . . 4865 1 112 . 1 1 40 40 ALA CA C 13 54.82 0.1 . 1 . . . . . . . . 4865 1 113 . 1 1 40 40 ALA H H 1 7.44 0.05 . 1 . . . . . . . . 4865 1 114 . 1 1 40 40 ALA N N 15 125.30 0.1 . 1 . . . . . . . . 4865 1 115 . 1 1 41 41 VAL C C 13 181.44 0.1 . 1 . . . . . . . . 4865 1 116 . 1 1 41 41 VAL CA C 13 66.82 0.1 . 1 . . . . . . . . 4865 1 117 . 1 1 41 41 VAL H H 1 8.57 0.05 . 1 . . . . . . . . 4865 1 118 . 1 1 41 41 VAL N N 15 124.35 0.1 . 1 . . . . . . . . 4865 1 119 . 1 1 42 42 VAL C C 13 179.28 0.1 . 1 . . . . . . . . 4865 1 120 . 1 1 42 42 VAL CA C 13 66.00 0.1 . 1 . . . . . . . . 4865 1 121 . 1 1 42 42 VAL H H 1 7.94 0.05 . 1 . . . . . . . . 4865 1 122 . 1 1 42 42 VAL N N 15 120.29 0.1 . 1 . . . . . . . . 4865 1 123 . 1 1 43 43 GLU C C 13 177.04 0.1 . 1 . . . . . . . . 4865 1 124 . 1 1 43 43 GLU CA C 13 58.34 0.1 . 1 . . . . . . . . 4865 1 125 . 1 1 43 43 GLU H H 1 7.76 0.05 . 1 . . . . . . . . 4865 1 126 . 1 1 43 43 GLU N N 15 122.39 0.1 . 1 . . . . . . . . 4865 1 127 . 1 1 44 44 SER C C 13 175.55 0.1 . 1 . . . . . . . . 4865 1 128 . 1 1 44 44 SER CA C 13 59.13 0.1 . 1 . . . . . . . . 4865 1 129 . 1 1 44 44 SER H H 1 7.83 0.05 . 1 . . . . . . . . 4865 1 130 . 1 1 44 44 SER N N 15 114.43 0.1 . 1 . . . . . . . . 4865 1 131 . 1 1 45 45 ASN C C 13 175.51 0.1 . 1 . . . . . . . . 4865 1 132 . 1 1 45 45 ASN CA C 13 54.27 0.1 . 1 . . . . . . . . 4865 1 133 . 1 1 45 45 ASN H H 1 8.49 0.05 . 1 . . . . . . . . 4865 1 134 . 1 1 45 45 ASN N N 15 121.77 0.1 . 1 . . . . . . . . 4865 1 135 . 1 1 46 46 GLY C C 13 174.97 0.1 . 1 . . . . . . . . 4865 1 136 . 1 1 46 46 GLY CA C 13 45.71 0.1 . 1 . . . . . . . . 4865 1 137 . 1 1 46 46 GLY H H 1 8.01 0.05 . 1 . . . . . . . . 4865 1 138 . 1 1 46 46 GLY N N 15 104.48 0.1 . 1 . . . . . . . . 4865 1 139 . 1 1 47 47 THR CA C 13 63.19 0.1 . 1 . . . . . . . . 4865 1 140 . 1 1 47 47 THR H H 1 7.61 0.05 . 1 . . . . . . . . 4865 1 141 . 1 1 47 47 THR N N 15 111.88 0.1 . 1 . . . . . . . . 4865 1 142 . 1 1 48 48 LEU C C 13 174.58 0.1 . 1 . . . . . . . . 4865 1 143 . 1 1 48 48 LEU CA C 13 55.45 0.1 . 1 . . . . . . . . 4865 1 144 . 1 1 48 48 LEU H H 1 7.75 0.05 . 1 . . . . . . . . 4865 1 145 . 1 1 48 48 LEU N N 15 126.01 0.1 . 1 . . . . . . . . 4865 1 146 . 1 1 49 49 THR C C 13 173.22 0.1 . 1 . . . . . . . . 4865 1 147 . 1 1 49 49 THR CA C 13 59.31 0.1 . 1 . . . . . . . . 4865 1 148 . 1 1 49 49 THR H H 1 8.56 0.05 . 1 . . . . . . . . 4865 1 149 . 1 1 49 49 THR N N 15 117.18 0.1 . 1 . . . . . . . . 4865 1 150 . 1 1 50 50 LEU C C 13 176.59 0.1 . 1 . . . . . . . . 4865 1 151 . 1 1 50 50 LEU CA C 13 54.74 0.1 . 1 . . . . . . . . 4865 1 152 . 1 1 50 50 LEU H H 1 8.73 0.05 . 1 . . . . . . . . 4865 1 153 . 1 1 50 50 LEU N N 15 123.16 0.1 . 1 . . . . . . . . 4865 1 154 . 1 1 51 51 SER C C 13 174.98 0.1 . 1 . . . . . . . . 4865 1 155 . 1 1 51 51 SER CA C 13 60.35 0.1 . 1 . . . . . . . . 4865 1 156 . 1 1 51 51 SER H H 1 8.91 0.05 . 1 . . . . . . . . 4865 1 157 . 1 1 51 51 SER N N 15 124.02 0.1 . 1 . . . . . . . . 4865 1 158 . 1 1 52 52 HIS C C 13 173.06 0.1 . 1 . . . . . . . . 4865 1 159 . 1 1 52 52 HIS CA C 13 55.03 0.1 . 1 . . . . . . . . 4865 1 160 . 1 1 52 52 HIS H H 1 7.24 0.05 . 1 . . . . . . . . 4865 1 161 . 1 1 52 52 HIS N N 15 109.96 0.1 . 1 . . . . . . . . 4865 1 162 . 1 1 53 53 PHE C C 13 177.04 0.1 . 1 . . . . . . . . 4865 1 163 . 1 1 53 53 PHE CA C 13 60.18 0.1 . 1 . . . . . . . . 4865 1 164 . 1 1 53 53 PHE H H 1 8.94 0.05 . 1 . . . . . . . . 4865 1 165 . 1 1 53 53 PHE N N 15 120.69 0.1 . 1 . . . . . . . . 4865 1 166 . 1 1 54 54 GLY C C 13 170.64 0.1 . 1 . . . . . . . . 4865 1 167 . 1 1 54 54 GLY CA C 13 44.05 0.1 . 1 . . . . . . . . 4865 1 168 . 1 1 54 54 GLY H H 1 8.26 0.05 . 1 . . . . . . . . 4865 1 169 . 1 1 54 54 GLY N N 15 114.86 0.1 . 1 . . . . . . . . 4865 1 170 . 1 1 55 55 LYS C C 13 178.21 0.1 . 1 . . . . . . . . 4865 1 171 . 1 1 55 55 LYS CA C 13 56.19 0.1 . 1 . . . . . . . . 4865 1 172 . 1 1 55 55 LYS H H 1 7.81 0.05 . 1 . . . . . . . . 4865 1 173 . 1 1 55 55 LYS N N 15 114.02 0.1 . 1 . . . . . . . . 4865 1 174 . 1 1 56 56 CYS CA C 13 55.75 0.1 . 1 . . . . . . . . 4865 1 175 . 1 1 56 56 CYS H H 1 8.19 0.05 . 1 . . . . . . . . 4865 1 176 . 1 1 56 56 CYS N N 15 125.54 0.1 . 1 . . . . . . . . 4865 1 stop_ save_