data_1839 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 1839 _Entry.Title ; Proton NMR Assignments of Heme Contacts and Catalytically Implicated Amino Acids in Cyanide-Ligated Cytochrome c Peroxidase Determined from One- and Two-Dimensional Nuclear Overhauser Effects ; _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 James Satterlee . D. . 1839 2 James Erman . E. . 1839 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 1839 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 29 1839 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 . . 2010-06-15 . revision BMRB 'Complete natural source information' 1839 3 . . 1999-06-14 . revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1839 2 . . 1996-03-25 . reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1839 1 . . 1995-07-31 . original BMRB 'Last release in original BMRB flat-file format' 1839 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 1839 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Satterlee, James D., Erman, James E., "Proton NMR Assignments of Heme Contacts and Catalytically Implicated Amino Acids in Cyanide-Ligated Cytochrome c Peroxidase Determined from One- and Two-Dimensional Nuclear Overhauser Effects," Biochemistry 30 (18), 4398-4405 (1991). ; _Citation.Title ; Proton NMR Assignments of Heme Contacts and Catalytically Implicated Amino Acids in Cyanide-Ligated Cytochrome c Peroxidase Determined from One- and Two-Dimensional Nuclear Overhauser Effects ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full . _Citation.Journal_volume 30 _Citation.Journal_issue 18 _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 4398 _Citation.Page_last 4405 _Citation.Year 1991 _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 James Satterlee . D. . 1839 1 2 James Erman . E. . 1839 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_glucose_oxidase _Assembly.Sf_category assembly _Assembly.Sf_framecode system_glucose_oxidase _Assembly.Entry_ID 1839 _Assembly.ID 1 _Assembly.Name 'glucose oxidase' _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 'glucose oxidase' 1 $glucose_oxidase . . . . . . . . . 1839 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'glucose oxidase' system 1839 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_glucose_oxidase _Entity.Sf_category entity _Entity.Sf_framecode glucose_oxidase _Entity.Entry_ID 1839 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'glucose oxidase' _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 ; TTPLVHVASVEKGRSYEDFQ KVYNAIALKLREDDEYDNYI GYGPVLVRLAWHTSGTWDKH DNTGGSYGGTYRFKKEFDNP SNAGLQNGFKFLEPIHKEFP WISSGDLFSLGGVTAVQEMQ GPKIPWRCGRVDTPEDTTPD NGRLPDADKDADYVRTFFQR LNMNDREVVALMGAHALGKT HLKNSGYEGPWGAANNVFTN EFYLNLLNEDWKLEKNDANN EQWDSKSGYMMLPTDYSLIQ DPKYLSIVKEYANDQDKFFK DFSKAFEKLLENGITFPKDA PSPFIFKTLEEQGL ; _Entity.Polymer_seq_one_letter_code ; TTPLVHVASVEKGRSYEDFQ KVYNAIALKLREDDEYDNYI GYGPVLVRLAWHTSGTWDKH DNTGGSYGGTYRFKKEFDNP SNAGLQNGFKFLEPIHKEFP WISSGDLFSLGGVTAVQEMQ GPKIPWRCGRVDTPEDTTPD NGRLPDADKDADYVRTFFQR LNMNDREVVALMGAHALGKT HLKNSGYEGPWGAANNVFTN EFYLNLLNEDWKLEKNDANN EQWDSKSGYMMLPTDYSLIQ DPKYLSIVKEYANDQDKFFK DFSKAFEKLLENGITFPKDA PSPFIFKTLEEQGL ; _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 294 _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 1.1.3.4 _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 2015-11-25 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 19004 . cytochrome_c_peroxidase . . . . . 98.98 300 99.31 100.00 0.00e+00 . . . . 1839 1 2 no BMRB 19005 . cytochrome_c_peroxidase . . . . . 98.98 300 99.31 100.00 0.00e+00 . . . . 1839 1 3 no BMRB 19075 . cytochrome_c_peroxidase . . . . . 98.98 300 99.31 100.00 0.00e+00 . . . . 1839 1 4 no BMRB 19076 . cytochrome_c_peroxidase . . . . . 98.98 300 99.31 100.00 0.00e+00 . . . . 1839 1 5 no BMRB 19884 . High_pH . . . . . 98.98 295 98.97 99.66 0.00e+00 . . . . 1839 1 6 no BMRB 25551 . CcP . . . . . 100.00 294 98.64 99.32 0.00e+00 . . . . 1839 1 7 no PDB 1A2F . "Probing The Strength And Character Of An Asp-His-X Hydrogen Bond By Introducing Buried Charges" . . . . . 98.64 291 98.28 98.97 0.00e+00 . . . . 1839 1 8 no PDB 1A2G . "Probing The Strength And Character Of An Asp-His-X Hydrogen Bond By Introducing Buried Charges" . . . . . 98.64 291 98.28 98.97 0.00e+00 . . . . 1839 1 9 no PDB 1AA4 . "Specificity Of Ligand Binding In A Buried Polar Cavity Of Cytochrome C Peroxidase" . . . . . 98.98 294 98.28 98.97 0.00e+00 . . . . 1839 1 10 no PDB 1AC4 . "Variation In The Strength Of A Ch To O Hydrogen Bond In An Artificial Protein Cavity (2,3,4-Trimethyl-1,3-Thiazole)" . . . . . 98.98 294 97.94 98.97 0.00e+00 . . . . 1839 1 11 no PDB 1AC8 . "Variation In The Strength Of A Ch To O Hydrogen Bond In An Artificial Protein Cavity (3,4,5-Trimethylthiazole)" . . . . . 98.98 294 97.94 98.97 0.00e+00 . . . . 1839 1 12 no PDB 1AEB . "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (3- Methylthiazole)" . . . . . 98.98 294 97.94 98.97 0.00e+00 . . . . 1839 1 13 no PDB 1AED . "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (3,4- Dimethylthiazole)" . . . . . 98.98 294 97.94 98.97 0.00e+00 . . . . 1839 1 14 no PDB 1AEE . "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (Aniline)" . . . . . 98.98 294 97.94 98.97 0.00e+00 . . . . 1839 1 15 no PDB 1AEF . "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (3- Aminopyridine)" . . . . . 98.98 294 97.94 98.97 0.00e+00 . . . . 1839 1 16 no PDB 1AEG . "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (4- Aminopyridine)" . . . . . 98.98 294 97.94 98.97 0.00e+00 . . . . 1839 1 17 no PDB 1AEH . "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (2-Amino-4- Methylthiazole" . . . . . 98.98 294 97.94 98.97 0.00e+00 . . . . 1839 1 18 no PDB 1AEJ . "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (1- Vinylimidazole)" . . . . . 98.98 294 97.94 98.97 0.00e+00 . . . . 1839 1 19 no PDB 1AEK . "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (Indoline)" . . . . . 98.98 294 97.94 98.97 0.00e+00 . . . . 1839 1 20 no PDB 1AEM . "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (Imidazo[1,2- A]pyridine)" . . . . . 98.98 294 97.94 98.97 0.00e+00 . . . . 1839 1 21 no PDB 1AEN . "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (2-Amino-5- Methylthiazole" . . . . . 98.98 294 97.94 98.97 0.00e+00 . . . . 1839 1 22 no PDB 1AEO . "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (2- Aminopyridine)" . . . . . 98.98 294 97.94 98.97 0.00e+00 . . . . 1839 1 23 no PDB 1AEQ . "Variation In The Strength Of A Ch To O Hydrogen Bond In An Artificial Protein Cavity (2-Ethylimidazole)" . . . . . 98.98 294 97.94 98.97 0.00e+00 . . . . 1839 1 24 no PDB 1AES . "Specificity Of Ligand Binding To A Buried Polar Cavity At The Active Site Of Cytochrome C Peroxidase (Imidazole)" . . . . . 98.98 294 97.94 98.97 0.00e+00 . . . . 1839 1 25 no PDB 1AET . "Variation In The Strength Of A Ch To O Hydrogen Bond In An Artificial Protein Cavity (1-Methylimidazole)" . . . . . 98.98 294 97.94 98.97 0.00e+00 . . . . 1839 1 26 no PDB 1AEU . "Specificity Of Ligand Binding In A Polar Cavity Of Cytochrome C Peroxidase (2-Methylimidazole)" . . . . . 98.98 294 97.94 98.97 0.00e+00 . . . . 1839 1 27 no PDB 1AEV . "Introduction Of Novel Substrate Oxidation Into Cytochrome C Peroxidase By Cavity Complementation: Oxidation Of 2- Aminothiazole" . . . . . 98.98 294 97.94 98.97 0.00e+00 . . . . 1839 1 28 no PDB 1BEJ . "Interaction Between Proximal And Distals Regions Of Cytochrome C Peroxidase" . . . . . 98.98 291 97.94 98.97 0.00e+00 . . . . 1839 1 29 no PDB 1BEK . "Effect Of Unnatural Heme Substitution On Kinetics Of Electron Transfer In Cytochrome C Peroxidase" . . . . . 98.98 291 97.94 98.97 0.00e+00 . . . . 1839 1 30 no PDB 1BEM . "Interaction Between Proximal And Distals Regions Of Cytochrome C Peroxidase" . . . . . 98.98 291 97.94 98.97 0.00e+00 . . . . 1839 1 31 no PDB 1BEP . "Effect Of Unnatural Heme Substitution On Kinetics Of Electron Transfer In Cytochrome C Peroxidase" . . . . . 98.98 291 98.28 99.31 0.00e+00 . . . . 1839 1 32 no PDB 1BEQ . "Interaction Between Proximal And Distals Regions Of Cytochrome C Peroxidase" . . . . . 98.98 291 97.94 99.31 0.00e+00 . . . . 1839 1 33 no PDB 1BES . "Interaction Between Proximal And Distals Regions Of Cytochrome C Peroxidase" . . . . . 98.98 291 97.94 99.31 0.00e+00 . . . . 1839 1 34 no PDB 1BJ9 . "Effect Of Unnatural Heme Substitution On Kinetics Of Electron Transfer In Cytochrome C Peroxidase" . . . . . 98.98 291 98.28 99.31 0.00e+00 . . . . 1839 1 35 no PDB 1BVA . "Manganese Binding Mutant In Cytochrome C Peroxidase" . . . . . 98.98 294 97.59 98.63 0.00e+00 . . . . 1839 1 36 no PDB 1CCA . "The Asp-His-Fe Triad Of Cytochrome C Peroxidase Controls The Reduction Potential, Electronic Structure, And Coupling Of The Try" . . . . . 100.00 297 98.64 99.32 0.00e+00 . . . . 1839 1 37 no PDB 1CCB . "The Asp-His-Fe Triad Of Cytochrome C Peroxidase Controls The Reduction Potential, Electronic Structure, And Coupling Of The Try" . . . . . 100.00 297 98.30 99.32 0.00e+00 . . . . 1839 1 38 no PDB 1CCC . "The Asp-His-Fe Triad Of Cytochrome C Peroxidase Controls The Reduction Potential, Electronic Structure, And Coupling Of The Try" . . . . . 100.00 297 98.30 98.98 0.00e+00 . . . . 1839 1 39 no PDB 1CCE . "Construction Of A Bis-Aquo Heme Enzyme And Replacement With Exogenous Ligand" . . . . . 98.64 291 98.28 98.97 0.00e+00 . . . . 1839 1 40 no PDB 1CCG . "Construction Of A Bis-Aquo Heme Enzyme And Replacement With Exogenous Ligand" . . . . . 98.64 291 98.28 98.97 0.00e+00 . . . . 1839 1 41 no PDB 1CCI . "How Flexible Are Proteins? Trapping Of A Flexible Loop" . . . . . 98.98 294 98.28 98.97 0.00e+00 . . . . 1839 1 42 no PDB 1CCJ . "Conformer Selection By Ligand Binding Observed With Protein Crystallography" . . . . . 98.98 294 98.28 98.97 0.00e+00 . . . . 1839 1 43 no PDB 1CCK . "Altering Substrate Specificity Of Cytochrome C Peroxidase Towards A Small Molecular Substrate Peroxidase By Substituting Tyrosi" . . . . . 98.64 291 98.28 99.31 0.00e+00 . . . . 1839 1 44 no PDB 1CCL . "Probing The Strength And Character Of An Asp-His-X Hydrogen Bond By Introducing Buried Charges" . . . . . 98.64 291 98.28 98.97 0.00e+00 . . . . 1839 1 45 no PDB 1CCP . "X-Ray Structures Of Recombinant Yeast Cytochrome C Peroxidase And Three Heme-Cleft Mutants Prepared By Site-Directed Mutagenesi" . . . . . 100.00 296 98.64 99.32 0.00e+00 . . . . 1839 1 46 no PDB 1CMP . "Small Molecule Binding To An Artificially Created Cavity At The Active Site Of Cytochrome C Peroxidase" . . . . . 98.98 294 98.28 98.97 0.00e+00 . . . . 1839 1 47 no PDB 1CMQ . "Small Molecule Binding To An Artificially Created Cavity At The Active Site Of Cytochrome C Peroxidase" . . . . . 98.98 294 98.28 98.97 0.00e+00 . . . . 1839 1 48 no PDB 1CMT . "The Role Of Aspartate-235 In The Binding Of Cations To An Artificial Cavity At The Radical Site Of Cytochrome C Peroxidase" . . . . . 98.98 294 98.28 98.97 0.00e+00 . . . . 1839 1 49 no PDB 1CMU . "The Role Of Aspartate-235 In The Binding Of Cations To An Artificial Cavity At The Radical Site Of Cytochrome C Peroxidase" . . . . . 98.98 294 97.94 98.97 0.00e+00 . . . . 1839 1 50 no PDB 1CPD . "A Cation Binding Motif Stabilizes The Compound I Radical Of Cytochrome C Peroxidase" . . . . . 100.00 296 98.30 98.98 0.00e+00 . . . . 1839 1 51 no PDB 1CPE . "A Cation Binding Motif Stabilizes The Compound I Radical Of Cytochrome C Peroxidase" . . . . . 100.00 296 98.30 98.98 0.00e+00 . . . . 1839 1 52 no PDB 1CPF . "A Cation Binding Motif Stabilizes The Compound I Radical Of Cytochrome C Peroxidase" . . . . . 100.00 296 98.30 98.98 0.00e+00 . . . . 1839 1 53 no PDB 1CPG . "A Cation Binding Motif Stabilizes The Compound I Radical Of Cytochrome C Peroxidase" . . . . . 98.98 296 98.28 98.97 0.00e+00 . . . . 1839 1 54 no PDB 1CYF . "Identifying The Physiological Electron Transfer Site Of Cytochrome C Peroxidase By Structure-Based Engineering" . . . . . 100.00 296 97.96 98.64 0.00e+00 . . . . 1839 1 55 no PDB 1DCC . "2.2 Angstrom Structure Of Oxyperoxidase: A Model For The Enzyme:peroxide Complex" . . . . . 100.00 296 98.30 99.32 0.00e+00 . . . . 1839 1 56 no PDB 1DJ1 . "Crystal Structure Of R48a Mutant Of Cytochrome C Peroxidase" . . . . . 98.98 291 98.28 98.97 0.00e+00 . . . . 1839 1 57 no PDB 1DJ5 . "Crystal Structure Of R48a Mutant Of Cytochrome C Peroxidase With N-Hydroxyguanidine Bound" . . . . . 98.98 291 98.28 98.97 0.00e+00 . . . . 1839 1 58 no PDB 1DS4 . "Cytochrome C Peroxidase H175g Mutant, Imidazole Complex, Ph 6, 100k" . . . . . 98.98 292 98.28 98.97 0.00e+00 . . . . 1839 1 59 no PDB 1DSE . "Cytochrome C Peroxidase H175g Mutant, Imidazole Complex, With Phosphate Bound, Ph 6, 100k" . . . . . 98.98 292 97.94 98.97 0.00e+00 . . . . 1839 1 60 no PDB 1DSG . "Cytochrome C Peroxidase H175g Mutant, Imidazole Complex At Ph 5, Room Temperature." . . . . . 98.98 292 98.28 98.97 0.00e+00 . . . . 1839 1 61 no PDB 1DSO . "Cytochrome C Peroxidase H175g Mutant, Imidazole Complex At Ph 6, Room Temperature." . . . . . 98.98 292 98.28 98.97 0.00e+00 . . . . 1839 1 62 no PDB 1DSP . "Cytochrome C Peroxidase H175g Mutant, Imidazole Complex At Ph 7, Room Temperature" . . . . . 98.98 292 98.28 98.97 0.00e+00 . . . . 1839 1 63 no PDB 1EBE . "Laue Diffraction Study On The Structure Of Cytochrome C Peroxidase Compound I" . . . . . 100.00 294 98.98 100.00 0.00e+00 . . . . 1839 1 64 no PDB 1JCI . "Stabilization Of The Engineered Cation-Binding Loop In Cytochrome C Peroxidase (Ccp)" . . . . . 100.00 294 97.28 97.96 0.00e+00 . . . . 1839 1 65 no PDB 1JDR . "Crystal Structure Of A Proximal Domain Potassium Binding Variant Of Cytochrome C Peroxidase" . . . . . 100.00 294 97.62 98.30 0.00e+00 . . . . 1839 1 66 no PDB 1KOK . "Crystal Structure Of Mesopone Cytochrome C Peroxidase (Mpccp)" . . . . . 100.00 294 99.32 100.00 0.00e+00 . . . . 1839 1 67 no PDB 1KRJ . "Engineering Calcium-Binding Site Into Cytochrome C Peroxidase (Ccp)" . . . . . 100.00 294 97.62 98.30 0.00e+00 . . . . 1839 1 68 no PDB 1KXM . "Crystal Structure Of Cytochrome C Peroxidase With A Proposed Electron Transfer Pathway Excised To Form A Ligand Binding Channel" . . . . . 98.98 290 97.59 98.28 0.00e+00 . . . . 1839 1 69 no PDB 1KXN . "Crystal Structure Of Cytochrome C Peroxidase With A Proposed Electron Transfer Pathway Excised To Form A Ligand Binding Channel" . . . . . 98.98 289 97.59 98.28 0.00e+00 . . . . 1839 1 70 no PDB 1MK8 . "Crystal Structure Of A Mutant Cytochrome C Peroxidase Showing A Novel Trp-Tyr Covalent Cross-Link" . . . . . 100.00 294 98.98 100.00 0.00e+00 . . . . 1839 1 71 no PDB 1MKQ . "Crystal Structure Of The Mutant Variant Of Cytochrome C Peroxidase In The 'open' Uncross-Linked Form" . . . . . 100.00 294 98.98 100.00 0.00e+00 . . . . 1839 1 72 no PDB 1MKR . "Crystal Structure Of A Mutant Variant Of Cytochrome C Peroxidase (Plate Like Crystals)" . . . . . 100.00 294 98.98 100.00 0.00e+00 . . . . 1839 1 73 no PDB 1ML2 . "Crystal Structure Of A Mutant Variant Of Cytochrome C Peroxidase With Zn(Ii)-(20-Oxo-Protoporphyrin Ix)" . . . . . 100.00 294 98.98 100.00 0.00e+00 . . . . 1839 1 74 no PDB 1RYC . "Cytochrome C Peroxidase W191g From Saccharomyces Cerevisiae" . . . . . 98.98 294 98.28 98.97 0.00e+00 . . . . 1839 1 75 no PDB 1S6V . "Structure Of A Cytochrome C Peroxidase-Cytochrome C Site Specific Cross-Link" . . . . . 100.00 294 98.64 99.32 0.00e+00 . . . . 1839 1 76 no PDB 1S73 . "Crystal Structure Of Mesopone Cytochrome C Peroxidase (R- Isomer) [mpccp-R]" . . . . . 100.00 294 99.32 100.00 0.00e+00 . . . . 1839 1 77 no PDB 1SBM . "Crystal Structure Of Reduced Mesopone Cytochrome C Peroxidase (R-Isomer)" . . . . . 100.00 294 99.32 100.00 0.00e+00 . . . . 1839 1 78 no PDB 1SDQ . "Structure Of Reduced-No Adduct Of Mesopone Cytochrome C Peroxidase" . . . . . 100.00 294 99.32 100.00 0.00e+00 . . . . 1839 1 79 no PDB 1SOG . "Cyrstal Structure Of Cytochrome C Peroxidase Mutant: Ccpk2m2" . . . . . 100.00 294 96.94 97.96 0.00e+00 . . . . 1839 1 80 no PDB 1U74 . "Electron Transfer Complex Between Cytochrome C And Cytochrome C Peroxidase" . . . . . 100.00 296 98.64 99.32 0.00e+00 . . . . 1839 1 81 no PDB 1U75 . "Electron Transfer Complex Between Horse Heart Cytochrome C And Zinc- Porphyrin Substituted Cytochrome C Peroxidase" . . . . . 100.00 296 98.64 99.32 0.00e+00 . . . . 1839 1 82 no PDB 1Z53 . "The 1.13 Angstrom Structure Of Iron-Free Cytochrome C Peroxidase" . . . . . 100.00 294 99.32 100.00 0.00e+00 . . . . 1839 1 83 no PDB 1ZBY . "High-resolution Crystal Structure Of Native (resting) Cytochrome C Peroxidase (ccp)" . . . . . 100.00 294 99.32 100.00 0.00e+00 . . . . 1839 1 84 no PDB 1ZBZ . "High-Resolution Crystal Structure Of Compound I Intermediate Of Cytochrome C Peroxidase (Ccp)" . . . . . 100.00 294 99.32 100.00 0.00e+00 . . . . 1839 1 85 no PDB 2ANZ . "Cytochrome C Peroxidase In Complex With 2,6-Diaminopyridine" . . . . . 98.98 294 97.94 98.97 0.00e+00 . . . . 1839 1 86 no PDB 2AQD . "Cytochrome C Peroxidase (Ccp) In Complex With 2,5- Diaminopyridine" . . . . . 98.98 294 98.28 98.97 0.00e+00 . . . . 1839 1 87 no PDB 2AS1 . "Cytochrome C Peroxidase In Complex With Thiopheneamidine" . . . . . 98.98 294 98.28 98.97 0.00e+00 . . . . 1839 1 88 no PDB 2AS2 . "Cytochrome C Peroxidase In Complex With 2-Iminopiperidine" . . . . . 98.98 294 98.28 98.97 0.00e+00 . . . . 1839 1 89 no PDB 2AS3 . "Cytochrome C Peroxidase In Complex With Phenol" . . . . . 98.98 294 98.28 98.97 0.00e+00 . . . . 1839 1 90 no PDB 2AS4 . "Cytochrome C Peroxidase In Complex With 3-Fluorocatechol" . . . . . 98.98 294 98.28 98.97 0.00e+00 . . . . 1839 1 91 no PDB 2AS6 . "Cytochrome C Peroxidase In Complex With Cyclopentylamine" . . . . . 98.98 294 98.28 98.97 0.00e+00 . . . . 1839 1 92 no PDB 2B0Z . "Crystal Structure Of The Protein-Protein Complex Between F82i Cytochrome C And Cytochrome C Peroxidase" . . . . . 100.00 294 99.32 100.00 0.00e+00 . . . . 1839 1 93 no PDB 2B10 . "Crystal Structure Of The Protein-Protein Complex Between F82s Cytochrome C And Cytochrome C Peroxidase" . . . . . 100.00 294 99.32 100.00 0.00e+00 . . . . 1839 1 94 no PDB 2B11 . "Crystal Structure Of The Protein-Protein Complex Between F82w Cytochrome C And Cytochrome C Peroxidase" . . . . . 100.00 294 99.32 100.00 0.00e+00 . . . . 1839 1 95 no PDB 2B12 . "Crystal Structure Of The Protein-Protein Complex Between F82y Cytochrome C And Cytochrome C Peroxidase" . . . . . 100.00 294 99.32 100.00 0.00e+00 . . . . 1839 1 96 no PDB 2BCN . "Solvent Isotope Effects On Interfacial Protein Electron Transfer Between Cytochrome C And Cytochrome C Peroxidase" . . . . . 100.00 296 98.64 99.32 0.00e+00 . . . . 1839 1 97 no PDB 2CCP . "X-Ray Structures Of Recombinant Yeast Cytochrome C Peroxidase And Three Heme-Cleft Mutants Prepared By Site-Directed Mutagenesi" . . . . . 100.00 296 98.30 99.32 0.00e+00 . . . . 1839 1 98 no PDB 2CEP . "Role Of Met-230 In Intramolecular Electron Transfer Between The Oxyferryl Heme And Trp 191 In Cytochrome C Peroxidase Compound " . . . . . 100.00 296 98.30 99.32 0.00e+00 . . . . 1839 1 99 no PDB 2CYP . "Crystal Structure Of Yeast Cytochrome C Peroxidase Refined At 1.7-Angstroms Resolution" . . . . . 100.00 294 99.32 100.00 0.00e+00 . . . . 1839 1 100 no PDB 2EUN . "Cytochrome C Peroxidase (ccp) In Complex With 2,4- Diaminopyrimidine" . . . . . 98.98 294 98.28 98.97 0.00e+00 . . . . 1839 1 101 no PDB 2EUO . "Cytochrome C Peroxidase (ccp) In Complex With 1-methyl-1- Lambda-5-pyridin-3-yl-amine" . . . . . 98.98 294 98.28 98.97 0.00e+00 . . . . 1839 1 102 no PDB 2EUP . "Cytochrome C Peroxidase (Ccp) In Complex With 2-Amino-5- Picoline" . . . . . 98.98 294 98.28 98.97 0.00e+00 . . . . 1839 1 103 no PDB 2EUQ . "Cytochrome C Peroxydase (Ccp) In Complex With 3- Thienylmethylamine" . . . . . 98.98 294 98.28 98.97 0.00e+00 . . . . 1839 1 104 no PDB 2EUR . "Cytochrome C Peroxidase (Ccp) In Complex With 4- Pyridylcarbinol" . . . . . 98.98 294 98.28 98.97 0.00e+00 . . . . 1839 1 105 no PDB 2EUS . "Cytochrome C Peroxidase (Ccp) In Complex With Benzylamine" . . . . . 98.98 294 98.28 98.97 0.00e+00 . . . . 1839 1 106 no PDB 2EUT . "Cytochrome C Peroxidase (Ccp) In Complex With 2-Amino-4- Picoline" . . . . . 98.98 294 98.28 98.97 0.00e+00 . . . . 1839 1 107 no PDB 2EUU . "Cytochrome C Peroxidase (Ccp) In Complex With 1h-Imidazol-2- Ylmethanol" . . . . . 98.98 294 98.28 98.97 0.00e+00 . . . . 1839 1 108 no PDB 2GB8 . "Solution Structure Of The Complex Between Yeast Iso-1- Cytochrome C And Yeast Cytochrome C Peroxidase" . . . . . 100.00 294 98.64 99.32 0.00e+00 . . . . 1839 1 109 no PDB 2IA8 . "Kinetic And Crystallographic Studies Of A Redesigned Manganese-Binding Site In Cytochrome C Peroxidase" . . . . . 98.98 291 97.59 98.63 0.00e+00 . . . . 1839 1 110 no PDB 2ICV . "Kinetic And Crystallographic Studies Of A Redesigned Manganese-Binding Site In Cytochrome C Peroxidase" . . . . . 98.98 291 97.59 98.63 0.00e+00 . . . . 1839 1 111 no PDB 2JTI . "Solution Structure Of The Yeast Iso-1-Cytochrome C (T12a) : Yeast Cytochrome C Peroxidase Complex" . . . . . 100.00 294 98.64 99.32 0.00e+00 . . . . 1839 1 112 no PDB 2N18 . "Dominant Form Of The Low-affinity Complex Of Yeast Cytochrome C And Cytochrome C Peroxidase" . . . . . 100.00 294 98.64 99.32 0.00e+00 . . . . 1839 1 113 no PDB 2PCB . "Crystal Structure Of A Complex Between Electron Transfer Partners, Cytochrome C Peroxidase And Cytochrome C" . . . . . 100.00 296 98.64 99.32 0.00e+00 . . . . 1839 1 114 no PDB 2PCC . "Crystal Structure Of A Complex Between Electron Transfer Partners, Cytochrome C Peroxidase And Cytochrome C" . . . . . 100.00 296 98.64 99.32 0.00e+00 . . . . 1839 1 115 no PDB 2RBT . "N-Methylbenzylamine In Complex With Cytochrome C Peroxidase W191g" . . . . . 98.98 292 97.94 98.97 0.00e+00 . . . . 1839 1 116 no PDB 2RBU . "Cytochrome C Peroxidase In Complex With Cyclopentane-Carboximidamide" . . . . . 98.98 292 97.94 98.97 0.00e+00 . . . . 1839 1 117 no PDB 2RBV . "Cytochrome C Peroxidase In Complex With (1-Methyl-1h-Pyrrol-2-Yl)- Methylamine" . . . . . 98.98 292 97.94 98.97 0.00e+00 . . . . 1839 1 118 no PDB 2RBW . "Cytochrome C Peroxidase W191g In Complex With 1,2-dimethyl-1h-pyridin- 5-amine" . . . . . 98.98 292 97.94 98.97 0.00e+00 . . . . 1839 1 119 no PDB 2RBX . "Cytochrome C Peroxidase W191g In Complex With Pyrimidine-2,4,6- Triamine." . . . . . 98.98 292 97.94 98.97 0.00e+00 . . . . 1839 1 120 no PDB 2RBY . "1-methyl-5-imidazolecarboxaldehyde In Complex With Cytochrome C Peroxidase W191g" . . . . . 98.98 292 97.94 98.97 0.00e+00 . . . . 1839 1 121 no PDB 2RBZ . "Cytochrome C Peroxidase W191g In Complex 3-Methoxypyridine" . . . . . 98.98 292 97.94 98.97 0.00e+00 . . . . 1839 1 122 no PDB 2RC0 . "Cytochrome C Peroxidase W191g In Complex With 2-Imino-4- Methylpiperdine" . . . . . 98.98 292 97.94 98.97 0.00e+00 . . . . 1839 1 123 no PDB 2RC1 . "Cytochrome C Peroxidase W191g In Complex With 2,4,5-Trimethyl-3- Oxazoline" . . . . . 98.98 292 97.94 98.97 0.00e+00 . . . . 1839 1 124 no PDB 2RC2 . "Cytochrome C Peroxidase W191g In Complex With 1-Methyl-2-Vinyl- Pyridinium" . . . . . 98.98 292 97.94 98.97 0.00e+00 . . . . 1839 1 125 no PDB 2V23 . "Structure Of Cytochrome C Peroxidase Mutant N184r Y36a" . . . . . 100.00 296 98.30 99.32 0.00e+00 . . . . 1839 1 126 no PDB 2V2E . "Structure Of Isoniazid (Inh) Bound To Cytochrome C Peroxidase Mutant N184r Y36a" . . . . . 98.98 294 98.28 99.31 0.00e+00 . . . . 1839 1 127 no PDB 2X07 . "Cytochrome C Peroxidase: Engineered Ascorbate Binding Site" . . . . . 99.66 293 97.95 99.32 0.00e+00 . . . . 1839 1 128 no PDB 2X08 . "Cytochrome C Peroxidase: Ascorbate Bound To The Engineered Ascorbate Binding Site" . . . . . 99.66 293 97.95 99.32 0.00e+00 . . . . 1839 1 129 no PDB 2XIL . "The Structure Of Cytochrome C Peroxidase Compound I" . . . . . 98.98 294 98.97 100.00 0.00e+00 . . . . 1839 1 130 no PDB 2XJ5 . "The Structure Of Cytochrome C Peroxidase Compound Ii" . . . . . 98.98 294 99.31 100.00 0.00e+00 . . . . 1839 1 131 no PDB 2XJ8 . "The Structure Of Ferrous Cytochrome C Peroxidase" . . . . . 98.98 294 99.31 100.00 0.00e+00 . . . . 1839 1 132 no PDB 2Y5A . "Cytochrome C Peroxidase (Ccp) W191g Bound To 3-Aminopyridine" . . . . . 98.98 294 98.28 98.97 0.00e+00 . . . . 1839 1 133 no PDB 2YCG . "Structure Of Unreduced Ferric Cytochrome C Peroxidase Obtained By Multicrystal Method" . . . . . 100.00 294 99.32 100.00 0.00e+00 . . . . 1839 1 134 no PDB 3CCP . "X-Ray Structures Of Recombinant Yeast Cytochrome C Peroxidase And Three Heme-Cleft Mutants Prepared By Site-Directed Mutagenesi" . . . . . 100.00 296 98.30 99.32 0.00e+00 . . . . 1839 1 135 no PDB 3CCX . "Altering Substrate Specificity At The Heme Edge Of Cytochrome C Peroxidase" . . . . . 98.98 294 98.28 98.97 0.00e+00 . . . . 1839 1 136 no PDB 3E2O . "Crystal Structure Of Cytochrome C Peroxidase, N184r Mutant" . . . . . 100.00 294 98.64 99.32 0.00e+00 . . . . 1839 1 137 no PDB 3EXB . "Crystal Structure Of Cytochrome C Peroxidase With A Proposed Electron Pathway Excised In A Complex With A Peptide Wire" . . . . . 100.00 295 97.62 98.30 0.00e+00 . . . . 1839 1 138 no PDB 3M23 . "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" . . . . . 98.98 291 98.97 99.66 0.00e+00 . . . . 1839 1 139 no PDB 3M25 . "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" . . . . . 98.98 291 98.97 99.66 0.00e+00 . . . . 1839 1 140 no PDB 3M26 . "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" . . . . . 98.98 291 98.97 99.66 0.00e+00 . . . . 1839 1 141 no PDB 3M27 . "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" . . . . . 98.98 291 98.97 99.66 0.00e+00 . . . . 1839 1 142 no PDB 3M28 . "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" . . . . . 98.98 291 98.97 99.66 0.00e+00 . . . . 1839 1 143 no PDB 3M29 . "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" . . . . . 98.98 291 98.97 99.66 0.00e+00 . . . . 1839 1 144 no PDB 3M2A . "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" . . . . . 98.98 291 98.97 99.66 0.00e+00 . . . . 1839 1 145 no PDB 3M2B . "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" . . . . . 98.98 291 98.97 99.66 0.00e+00 . . . . 1839 1 146 no PDB 3M2C . "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" . . . . . 98.98 291 98.97 99.66 0.00e+00 . . . . 1839 1 147 no PDB 3M2D . "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" . . . . . 98.98 291 98.97 99.66 0.00e+00 . . . . 1839 1 148 no PDB 3M2E . "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" . . . . . 98.98 291 98.97 99.66 0.00e+00 . . . . 1839 1 149 no PDB 3M2F . "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" . . . . . 98.98 291 98.97 99.66 0.00e+00 . . . . 1839 1 150 no PDB 3M2G . "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" . . . . . 98.98 291 98.97 99.66 0.00e+00 . . . . 1839 1 151 no PDB 3M2H . "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" . . . . . 98.98 291 98.97 99.66 0.00e+00 . . . . 1839 1 152 no PDB 3M2I . "Crystallographic And Single Crystal Spectral Analysis Of The Peroxidase Ferryl Intermediate" . . . . . 98.98 291 98.97 99.66 0.00e+00 . . . . 1839 1 153 no PDB 3R98 . "Joint Neutron And X-Ray Structure Of Cytochrome C Peroxidase" . . . . . 99.66 293 99.32 100.00 0.00e+00 . . . . 1839 1 154 no PDB 3R99 . "Joint Neutron And X-Ray Structure Of Cytochrome C Peroxidase" . . . . . 99.66 293 99.32 100.00 0.00e+00 . . . . 1839 1 155 no PDB 4A6Z . "Cytochrome C Peroxidase With Bound Guaiacol" . . . . . 100.00 296 98.30 99.32 0.00e+00 . . . . 1839 1 156 no PDB 4A71 . "Cytochrome C Peroxidase In Complex With Phenol" . . . . . 100.00 296 98.64 99.32 0.00e+00 . . . . 1839 1 157 no PDB 4A78 . "Cytochrome C Peroxidase M119w In Complex With Guiacol" . . . . . 100.00 296 98.64 99.32 0.00e+00 . . . . 1839 1 158 no PDB 4A7M . "Cytochrome C Peroxidase S81w Mutant" . . . . . 100.00 296 98.98 99.66 0.00e+00 . . . . 1839 1 159 no PDB 4CCP . "X-Ray Structures Of Recombinant Yeast Cytochrome C Peroxidase And Three Heme-Cleft Mutants Prepared By Site-Directed Mutagenesi" . . . . . 100.00 296 98.30 99.32 0.00e+00 . . . . 1839 1 160 no PDB 4CCX . "Altering Substrate Specificity At The Heme Edge Of Cytochrome C Peroxidase" . . . . . 98.98 294 98.28 98.97 0.00e+00 . . . . 1839 1 161 no PDB 4CVI . "Neutron Structure Of Ferric Cytochrome C Peroxidase - Deuterium Exchanged At Room Temperature" . . . . . 99.32 294 99.32 100.00 0.00e+00 . . . . 1839 1 162 no PDB 4CVJ . "Neutron Structure Of Compound I Intermediate Of Cytochrome C Peroxidase - Deuterium Exchanged 100 K" . . . . . 98.98 294 99.31 100.00 0.00e+00 . . . . 1839 1 163 no PDB 4JB4 . "Expression, Purification, Characterization, And Solution Nmr Study Of Highly Deuterated Yeast Cytochrome C Peroxidase With Enha" . . . . . 98.98 300 99.31 100.00 0.00e+00 . . . . 1839 1 164 no PDB 4JM5 . "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 2-amino-5-methylthiazole" . . . . . 98.98 289 97.59 98.28 0.00e+00 . . . . 1839 1 165 no PDB 4JM6 . "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 2,4-diaminopyrimidine" . . . . . 98.98 289 97.59 98.28 0.00e+00 . . . . 1839 1 166 no PDB 4JM8 . "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 2,6-diaminopyridine" . . . . . 98.98 289 97.59 98.28 0.00e+00 . . . . 1839 1 167 no PDB 4JM9 . "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 3-amino-1-methylpyridinium" . . . . . 98.98 289 97.59 98.28 0.00e+00 . . . . 1839 1 168 no PDB 4JMA . "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 3-fluorocatechol" . . . . . 98.98 289 97.59 98.28 0.00e+00 . . . . 1839 1 169 no PDB 4JMB . "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 5,6,7,8-tetrahydrothieno[2,3-b]quinolin-4-amine" . . . . . 98.98 289 97.59 98.28 0.00e+00 . . . . 1839 1 170 no PDB 4JMS . "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With Imidazo[1,2-a]pyridin-5-amine" . . . . . 98.98 289 97.59 98.28 0.00e+00 . . . . 1839 1 171 no PDB 4JMT . "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 1h-pyrrolo[3,2-b]pyridin-6-ylmethanol" . . . . . 98.98 289 97.59 98.28 0.00e+00 . . . . 1839 1 172 no PDB 4JMV . "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With Imidazo[1,2-a]pyridin-6-amine" . . . . . 98.98 289 97.59 98.28 0.00e+00 . . . . 1839 1 173 no PDB 4JMW . "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With Phenol" . . . . . 98.98 289 97.59 98.28 0.00e+00 . . . . 1839 1 174 no PDB 4JMZ . "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With N-methyl-1h-benzimidazol-2-amine" . . . . . 98.98 289 97.59 98.28 0.00e+00 . . . . 1839 1 175 no PDB 4JN0 . "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 1h-pyrrolo[3,2-b]pyridine-6-carbaldehyde" . . . . . 98.98 289 97.59 98.28 0.00e+00 . . . . 1839 1 176 no PDB 4JPL . "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 4-azaindole" . . . . . 98.98 289 97.59 98.28 0.00e+00 . . . . 1839 1 177 no PDB 4JPT . "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With Quinazoline-2,4-diamine" . . . . . 98.98 289 97.59 98.28 0.00e+00 . . . . 1839 1 178 no PDB 4JPU . "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With Benzamidine" . . . . . 98.98 289 97.59 98.28 0.00e+00 . . . . 1839 1 179 no PDB 4JQJ . "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 4-aminoquinoline" . . . . . 98.98 289 97.59 98.28 0.00e+00 . . . . 1839 1 180 no PDB 4JQK . "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 2-(2-aminopyridin-1-ium-1-yl)ethanol" . . . . . 98.98 289 97.59 98.28 0.00e+00 . . . . 1839 1 181 no PDB 4JQM . "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 4-aminoquinazoline" . . . . . 98.98 289 97.59 98.28 0.00e+00 . . . . 1839 1 182 no PDB 4JQN . "Crystal Structure Of Cytochrome C Peroxidase W191g-gateless In Complex With 4-hydroxybenzaldehyde" . . . . . 98.98 289 97.59 98.28 0.00e+00 . . . . 1839 1 183 no PDB 4NFG . "K13r Mutant Of Horse Cytochrome C And Yeast Cytochrome C Peroxidase Complex" . . . . . 98.98 294 98.97 99.66 0.00e+00 . . . . 1839 1 184 no PDB 4NVA . "Predicting Protein Conformational Response In Prospective Ligand Discovery" . . . . . 98.98 289 97.59 98.28 0.00e+00 . . . . 1839 1 185 no PDB 4NVB . "Predicting Protein Conformational Response In Prospective Ligand Discovery." . . . . . 98.98 289 97.59 98.28 0.00e+00 . . . . 1839 1 186 no PDB 4NVC . "Predicting Protein Conformational Response In Prospective Ligand Discovery" . . . . . 98.98 289 97.59 98.28 0.00e+00 . . . . 1839 1 187 no PDB 4NVD . "Predicting Protein Conformational Response In Prospective Ligand Discovery." . . . . . 98.98 289 97.59 98.28 0.00e+00 . . . . 1839 1 188 no PDB 4NVE . "Predicting Protein Conformational Response In Prospective Ligand Discovery" . . . . . 98.98 289 97.59 98.28 0.00e+00 . . . . 1839 1 189 no PDB 4NVF . "Predicting Protein Conformational Response In Prospective Ligand Discovery" . . . . . 98.98 289 97.59 98.28 0.00e+00 . . . . 1839 1 190 no PDB 4NVG . "Predicting Protein Conformational Response In Prospective Ligand Discovery" . . . . . 98.98 289 97.59 98.28 0.00e+00 . . . . 1839 1 191 no PDB 4NVH . "Predicting Protein Conformational Response In Prospective Ligand Discovery" . . . . . 98.98 289 97.59 98.28 0.00e+00 . . . . 1839 1 192 no PDB 4NVI . "Predicting Protein Conformational Response In Prospective Ligand Discovery." . . . . . 98.98 289 97.59 98.28 0.00e+00 . . . . 1839 1 193 no PDB 4NVJ . "Predicting Protein Conformational Response In Prospective Ligand Discovery." . . . . . 98.98 289 97.59 98.28 0.00e+00 . . . . 1839 1 194 no PDB 4NVK . "Predicting Protein Conformational Response In Prospective Ligand Discovery." . . . . . 98.98 289 97.59 98.28 0.00e+00 . . . . 1839 1 195 no PDB 4NVL . "Predicting Protein Conformational Response In Prospective Ligand Discovery." . . . . . 98.98 289 97.59 98.28 0.00e+00 . . . . 1839 1 196 no PDB 4NVM . "Predicting Protein Conformational Response In Prospective Ligand Discovery" . . . . . 98.98 289 97.59 98.28 0.00e+00 . . . . 1839 1 197 no PDB 4NVN . "Predicting Protein Conformational Response In Prospective Ligand Discovery" . . . . . 98.98 289 97.59 98.28 0.00e+00 . . . . 1839 1 198 no PDB 4NVO . "Predicting Protein Conformational Response In Prospective Ligand Discovery" . . . . . 98.98 289 97.59 98.28 0.00e+00 . . . . 1839 1 199 no PDB 4OQ7 . "Predicting Protein Conformational Response In Prospective Ligand Discovery." . . . . . 98.98 289 97.59 98.28 0.00e+00 . . . . 1839 1 200 no PDB 4P4Q . "Complex Of Yeast Cytochrome C Peroxidase (w191f) With Iso-1 Cytochrome C" . . . . . 100.00 294 98.30 99.32 0.00e+00 . . . . 1839 1 201 no PDB 4XV4 . "Ccp Gateless Cavity" . . . . . 98.98 289 97.59 98.28 0.00e+00 . . . . 1839 1 202 no PDB 4XV5 . "Ccp Gateless Cavity" . . . . . 98.98 292 97.59 98.28 0.00e+00 . . . . 1839 1 203 no PDB 4XV6 . "Ccp Gateless Cavity" . . . . . 98.98 289 97.59 98.28 0.00e+00 . . . . 1839 1 204 no PDB 4XV7 . "Ccp Gateless Cavity" . . . . . 98.98 292 97.59 98.28 0.00e+00 . . . . 1839 1 205 no PDB 4XV8 . "Ccp Gateless Cavity" . . . . . 98.98 292 97.59 98.28 0.00e+00 . . . . 1839 1 206 no PDB 4XVA . "Crystal Structure Of Wild Type Cytochrome C Peroxidase" . . . . . 99.66 293 99.32 100.00 0.00e+00 . . . . 1839 1 207 no PDB 5CCP . "Histidine 52 Is A Critical Residue For Rapid Formation Of Cytochrome C Peroxidase Compound I" . . . . . 100.00 296 98.30 98.98 0.00e+00 . . . . 1839 1 208 no PDB 6CCP . "Effect Of Arginine-48 Replacement On The Reaction Between Cytochrome C Peroxidase And Hydrogen Peroxide" . . . . . 100.00 296 98.30 99.32 0.00e+00 . . . . 1839 1 209 no PDB 7CCP . "Effect Of Arginine-48 Replacement On The Reaction Between Cytochrome C Peroxidase And Hydrogen Peroxide" . . . . . 100.00 296 98.30 98.98 0.00e+00 . . . . 1839 1 210 no DBJ GAA24787 . "K7_Ccp1p [Saccharomyces cerevisiae Kyokai no. 7]" . . . . . 100.00 363 99.32 100.00 0.00e+00 . . . . 1839 1 211 no EMBL CAA44288 . "Cytochrome c peroxidase [Saccharomyces cerevisiae]" . . . . . 100.00 361 99.32 100.00 0.00e+00 . . . . 1839 1 212 no EMBL CAA82145 . "CCP1 [Saccharomyces cerevisiae]" . . . . . 100.00 361 99.32 100.00 0.00e+00 . . . . 1839 1 213 no EMBL CAY81144 . "Ccp1p [Saccharomyces cerevisiae EC1118]" . . . . . 100.00 362 98.98 99.66 0.00e+00 . . . . 1839 1 214 no GB AAA88709 . "cytochrome c peroxidase [Saccharomyces cerevisiae]" . . . . . 100.00 362 98.64 99.32 0.00e+00 . . . . 1839 1 215 no GB AAS56247 . "YKR066C [Saccharomyces cerevisiae]" . . . . . 100.00 361 98.98 100.00 0.00e+00 . . . . 1839 1 216 no GB AHY76301 . "Ccp1p [Saccharomyces cerevisiae YJM993]" . . . . . 100.00 363 98.64 99.32 0.00e+00 . . . . 1839 1 217 no GB AJP40095 . "Ccp1p [Saccharomyces cerevisiae YJM1078]" . . . . . 100.00 362 98.98 99.66 0.00e+00 . . . . 1839 1 218 no GB AJS30293 . "Ccp1p [Saccharomyces cerevisiae YJM189]" . . . . . 100.00 362 98.64 99.32 0.00e+00 . . . . 1839 1 219 no REF NP_012992 . "Ccp1p [Saccharomyces cerevisiae S288c]" . . . . . 100.00 361 99.32 100.00 0.00e+00 . . . . 1839 1 220 no SP P00431 . "RecName: Full=Cytochrome c peroxidase, mitochondrial; Short=CCP; Flags: Precursor" . . . . . 100.00 361 99.32 100.00 0.00e+00 . . . . 1839 1 221 no TPG DAA09217 . "TPA: Ccp1p [Saccharomyces cerevisiae S288c]" . . . . . 100.00 361 99.32 100.00 0.00e+00 . . . . 1839 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'glucose oxidase' common 1839 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 . THR . 1839 1 2 . THR . 1839 1 3 . PRO . 1839 1 4 . LEU . 1839 1 5 . VAL . 1839 1 6 . HIS . 1839 1 7 . VAL . 1839 1 8 . ALA . 1839 1 9 . SER . 1839 1 10 . VAL . 1839 1 11 . GLU . 1839 1 12 . LYS . 1839 1 13 . GLY . 1839 1 14 . ARG . 1839 1 15 . SER . 1839 1 16 . TYR . 1839 1 17 . GLU . 1839 1 18 . ASP . 1839 1 19 . PHE . 1839 1 20 . GLN . 1839 1 21 . LYS . 1839 1 22 . VAL . 1839 1 23 . TYR . 1839 1 24 . ASN . 1839 1 25 . ALA . 1839 1 26 . ILE . 1839 1 27 . ALA . 1839 1 28 . LEU . 1839 1 29 . LYS . 1839 1 30 . LEU . 1839 1 31 . ARG . 1839 1 32 . GLU . 1839 1 33 . ASP . 1839 1 34 . ASP . 1839 1 35 . GLU . 1839 1 36 . TYR . 1839 1 37 . ASP . 1839 1 38 . ASN . 1839 1 39 . TYR . 1839 1 40 . ILE . 1839 1 41 . GLY . 1839 1 42 . TYR . 1839 1 43 . GLY . 1839 1 44 . PRO . 1839 1 45 . VAL . 1839 1 46 . LEU . 1839 1 47 . VAL . 1839 1 48 . ARG . 1839 1 49 . LEU . 1839 1 50 . ALA . 1839 1 51 . TRP . 1839 1 52 . HIS . 1839 1 53 . THR . 1839 1 54 . SER . 1839 1 55 . GLY . 1839 1 56 . THR . 1839 1 57 . TRP . 1839 1 58 . ASP . 1839 1 59 . LYS . 1839 1 60 . HIS . 1839 1 61 . ASP . 1839 1 62 . ASN . 1839 1 63 . THR . 1839 1 64 . GLY . 1839 1 65 . GLY . 1839 1 66 . SER . 1839 1 67 . TYR . 1839 1 68 . GLY . 1839 1 69 . GLY . 1839 1 70 . THR . 1839 1 71 . TYR . 1839 1 72 . ARG . 1839 1 73 . PHE . 1839 1 74 . LYS . 1839 1 75 . LYS . 1839 1 76 . GLU . 1839 1 77 . PHE . 1839 1 78 . ASP . 1839 1 79 . ASN . 1839 1 80 . PRO . 1839 1 81 . SER . 1839 1 82 . ASN . 1839 1 83 . ALA . 1839 1 84 . GLY . 1839 1 85 . LEU . 1839 1 86 . GLN . 1839 1 87 . ASN . 1839 1 88 . GLY . 1839 1 89 . PHE . 1839 1 90 . LYS . 1839 1 91 . PHE . 1839 1 92 . LEU . 1839 1 93 . GLU . 1839 1 94 . PRO . 1839 1 95 . ILE . 1839 1 96 . HIS . 1839 1 97 . LYS . 1839 1 98 . GLU . 1839 1 99 . PHE . 1839 1 100 . PRO . 1839 1 101 . TRP . 1839 1 102 . ILE . 1839 1 103 . SER . 1839 1 104 . SER . 1839 1 105 . GLY . 1839 1 106 . ASP . 1839 1 107 . LEU . 1839 1 108 . PHE . 1839 1 109 . SER . 1839 1 110 . LEU . 1839 1 111 . GLY . 1839 1 112 . GLY . 1839 1 113 . VAL . 1839 1 114 . THR . 1839 1 115 . ALA . 1839 1 116 . VAL . 1839 1 117 . GLN . 1839 1 118 . GLU . 1839 1 119 . MET . 1839 1 120 . GLN . 1839 1 121 . GLY . 1839 1 122 . PRO . 1839 1 123 . LYS . 1839 1 124 . ILE . 1839 1 125 . PRO . 1839 1 126 . TRP . 1839 1 127 . ARG . 1839 1 128 . CYS . 1839 1 129 . GLY . 1839 1 130 . ARG . 1839 1 131 . VAL . 1839 1 132 . ASP . 1839 1 133 . THR . 1839 1 134 . PRO . 1839 1 135 . GLU . 1839 1 136 . ASP . 1839 1 137 . THR . 1839 1 138 . THR . 1839 1 139 . PRO . 1839 1 140 . ASP . 1839 1 141 . ASN . 1839 1 142 . GLY . 1839 1 143 . ARG . 1839 1 144 . LEU . 1839 1 145 . PRO . 1839 1 146 . ASP . 1839 1 147 . ALA . 1839 1 148 . ASP . 1839 1 149 . LYS . 1839 1 150 . ASP . 1839 1 151 . ALA . 1839 1 152 . ASP . 1839 1 153 . TYR . 1839 1 154 . VAL . 1839 1 155 . ARG . 1839 1 156 . THR . 1839 1 157 . PHE . 1839 1 158 . PHE . 1839 1 159 . GLN . 1839 1 160 . ARG . 1839 1 161 . LEU . 1839 1 162 . ASN . 1839 1 163 . MET . 1839 1 164 . ASN . 1839 1 165 . ASP . 1839 1 166 . ARG . 1839 1 167 . GLU . 1839 1 168 . VAL . 1839 1 169 . VAL . 1839 1 170 . ALA . 1839 1 171 . LEU . 1839 1 172 . MET . 1839 1 173 . GLY . 1839 1 174 . ALA . 1839 1 175 . HIS . 1839 1 176 . ALA . 1839 1 177 . LEU . 1839 1 178 . GLY . 1839 1 179 . LYS . 1839 1 180 . THR . 1839 1 181 . HIS . 1839 1 182 . LEU . 1839 1 183 . LYS . 1839 1 184 . ASN . 1839 1 185 . SER . 1839 1 186 . GLY . 1839 1 187 . TYR . 1839 1 188 . GLU . 1839 1 189 . GLY . 1839 1 190 . PRO . 1839 1 191 . TRP . 1839 1 192 . GLY . 1839 1 193 . ALA . 1839 1 194 . ALA . 1839 1 195 . ASN . 1839 1 196 . ASN . 1839 1 197 . VAL . 1839 1 198 . PHE . 1839 1 199 . THR . 1839 1 200 . ASN . 1839 1 201 . GLU . 1839 1 202 . PHE . 1839 1 203 . TYR . 1839 1 204 . LEU . 1839 1 205 . ASN . 1839 1 206 . LEU . 1839 1 207 . LEU . 1839 1 208 . ASN . 1839 1 209 . GLU . 1839 1 210 . ASP . 1839 1 211 . TRP . 1839 1 212 . LYS . 1839 1 213 . LEU . 1839 1 214 . GLU . 1839 1 215 . LYS . 1839 1 216 . ASN . 1839 1 217 . ASP . 1839 1 218 . ALA . 1839 1 219 . ASN . 1839 1 220 . ASN . 1839 1 221 . GLU . 1839 1 222 . GLN . 1839 1 223 . TRP . 1839 1 224 . ASP . 1839 1 225 . SER . 1839 1 226 . LYS . 1839 1 227 . SER . 1839 1 228 . GLY . 1839 1 229 . TYR . 1839 1 230 . MET . 1839 1 231 . MET . 1839 1 232 . LEU . 1839 1 233 . PRO . 1839 1 234 . THR . 1839 1 235 . ASP . 1839 1 236 . TYR . 1839 1 237 . SER . 1839 1 238 . LEU . 1839 1 239 . ILE . 1839 1 240 . GLN . 1839 1 241 . ASP . 1839 1 242 . PRO . 1839 1 243 . LYS . 1839 1 244 . TYR . 1839 1 245 . LEU . 1839 1 246 . SER . 1839 1 247 . ILE . 1839 1 248 . VAL . 1839 1 249 . LYS . 1839 1 250 . GLU . 1839 1 251 . TYR . 1839 1 252 . ALA . 1839 1 253 . ASN . 1839 1 254 . ASP . 1839 1 255 . GLN . 1839 1 256 . ASP . 1839 1 257 . LYS . 1839 1 258 . PHE . 1839 1 259 . PHE . 1839 1 260 . LYS . 1839 1 261 . ASP . 1839 1 262 . PHE . 1839 1 263 . SER . 1839 1 264 . LYS . 1839 1 265 . ALA . 1839 1 266 . PHE . 1839 1 267 . GLU . 1839 1 268 . LYS . 1839 1 269 . LEU . 1839 1 270 . LEU . 1839 1 271 . GLU . 1839 1 272 . ASN . 1839 1 273 . GLY . 1839 1 274 . ILE . 1839 1 275 . THR . 1839 1 276 . PHE . 1839 1 277 . PRO . 1839 1 278 . LYS . 1839 1 279 . ASP . 1839 1 280 . ALA . 1839 1 281 . PRO . 1839 1 282 . SER . 1839 1 283 . PRO . 1839 1 284 . PHE . 1839 1 285 . ILE . 1839 1 286 . PHE . 1839 1 287 . LYS . 1839 1 288 . THR . 1839 1 289 . LEU . 1839 1 290 . GLU . 1839 1 291 . GLU . 1839 1 292 . GLN . 1839 1 293 . GLY . 1839 1 294 . LEU . 1839 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 . THR 1 1 1839 1 . THR 2 2 1839 1 . PRO 3 3 1839 1 . LEU 4 4 1839 1 . VAL 5 5 1839 1 . HIS 6 6 1839 1 . VAL 7 7 1839 1 . ALA 8 8 1839 1 . SER 9 9 1839 1 . VAL 10 10 1839 1 . GLU 11 11 1839 1 . LYS 12 12 1839 1 . GLY 13 13 1839 1 . ARG 14 14 1839 1 . SER 15 15 1839 1 . TYR 16 16 1839 1 . GLU 17 17 1839 1 . ASP 18 18 1839 1 . PHE 19 19 1839 1 . GLN 20 20 1839 1 . LYS 21 21 1839 1 . VAL 22 22 1839 1 . TYR 23 23 1839 1 . ASN 24 24 1839 1 . ALA 25 25 1839 1 . ILE 26 26 1839 1 . ALA 27 27 1839 1 . LEU 28 28 1839 1 . LYS 29 29 1839 1 . LEU 30 30 1839 1 . ARG 31 31 1839 1 . GLU 32 32 1839 1 . ASP 33 33 1839 1 . ASP 34 34 1839 1 . GLU 35 35 1839 1 . TYR 36 36 1839 1 . ASP 37 37 1839 1 . ASN 38 38 1839 1 . TYR 39 39 1839 1 . ILE 40 40 1839 1 . GLY 41 41 1839 1 . TYR 42 42 1839 1 . GLY 43 43 1839 1 . PRO 44 44 1839 1 . VAL 45 45 1839 1 . LEU 46 46 1839 1 . VAL 47 47 1839 1 . ARG 48 48 1839 1 . LEU 49 49 1839 1 . ALA 50 50 1839 1 . TRP 51 51 1839 1 . HIS 52 52 1839 1 . THR 53 53 1839 1 . SER 54 54 1839 1 . GLY 55 55 1839 1 . THR 56 56 1839 1 . TRP 57 57 1839 1 . ASP 58 58 1839 1 . LYS 59 59 1839 1 . HIS 60 60 1839 1 . ASP 61 61 1839 1 . ASN 62 62 1839 1 . THR 63 63 1839 1 . GLY 64 64 1839 1 . GLY 65 65 1839 1 . SER 66 66 1839 1 . TYR 67 67 1839 1 . GLY 68 68 1839 1 . GLY 69 69 1839 1 . THR 70 70 1839 1 . TYR 71 71 1839 1 . ARG 72 72 1839 1 . PHE 73 73 1839 1 . LYS 74 74 1839 1 . LYS 75 75 1839 1 . GLU 76 76 1839 1 . PHE 77 77 1839 1 . ASP 78 78 1839 1 . ASN 79 79 1839 1 . PRO 80 80 1839 1 . SER 81 81 1839 1 . ASN 82 82 1839 1 . ALA 83 83 1839 1 . GLY 84 84 1839 1 . LEU 85 85 1839 1 . GLN 86 86 1839 1 . ASN 87 87 1839 1 . GLY 88 88 1839 1 . PHE 89 89 1839 1 . LYS 90 90 1839 1 . PHE 91 91 1839 1 . LEU 92 92 1839 1 . GLU 93 93 1839 1 . PRO 94 94 1839 1 . ILE 95 95 1839 1 . HIS 96 96 1839 1 . LYS 97 97 1839 1 . GLU 98 98 1839 1 . PHE 99 99 1839 1 . PRO 100 100 1839 1 . TRP 101 101 1839 1 . ILE 102 102 1839 1 . SER 103 103 1839 1 . SER 104 104 1839 1 . GLY 105 105 1839 1 . ASP 106 106 1839 1 . LEU 107 107 1839 1 . PHE 108 108 1839 1 . SER 109 109 1839 1 . LEU 110 110 1839 1 . GLY 111 111 1839 1 . GLY 112 112 1839 1 . VAL 113 113 1839 1 . THR 114 114 1839 1 . ALA 115 115 1839 1 . VAL 116 116 1839 1 . GLN 117 117 1839 1 . GLU 118 118 1839 1 . MET 119 119 1839 1 . GLN 120 120 1839 1 . GLY 121 121 1839 1 . PRO 122 122 1839 1 . LYS 123 123 1839 1 . ILE 124 124 1839 1 . PRO 125 125 1839 1 . TRP 126 126 1839 1 . ARG 127 127 1839 1 . CYS 128 128 1839 1 . GLY 129 129 1839 1 . ARG 130 130 1839 1 . VAL 131 131 1839 1 . ASP 132 132 1839 1 . THR 133 133 1839 1 . PRO 134 134 1839 1 . GLU 135 135 1839 1 . ASP 136 136 1839 1 . THR 137 137 1839 1 . THR 138 138 1839 1 . PRO 139 139 1839 1 . ASP 140 140 1839 1 . ASN 141 141 1839 1 . GLY 142 142 1839 1 . ARG 143 143 1839 1 . LEU 144 144 1839 1 . PRO 145 145 1839 1 . ASP 146 146 1839 1 . ALA 147 147 1839 1 . ASP 148 148 1839 1 . LYS 149 149 1839 1 . ASP 150 150 1839 1 . ALA 151 151 1839 1 . ASP 152 152 1839 1 . TYR 153 153 1839 1 . VAL 154 154 1839 1 . ARG 155 155 1839 1 . THR 156 156 1839 1 . PHE 157 157 1839 1 . PHE 158 158 1839 1 . GLN 159 159 1839 1 . ARG 160 160 1839 1 . LEU 161 161 1839 1 . ASN 162 162 1839 1 . MET 163 163 1839 1 . ASN 164 164 1839 1 . ASP 165 165 1839 1 . ARG 166 166 1839 1 . GLU 167 167 1839 1 . VAL 168 168 1839 1 . VAL 169 169 1839 1 . ALA 170 170 1839 1 . LEU 171 171 1839 1 . MET 172 172 1839 1 . GLY 173 173 1839 1 . ALA 174 174 1839 1 . HIS 175 175 1839 1 . ALA 176 176 1839 1 . LEU 177 177 1839 1 . GLY 178 178 1839 1 . LYS 179 179 1839 1 . THR 180 180 1839 1 . HIS 181 181 1839 1 . LEU 182 182 1839 1 . LYS 183 183 1839 1 . ASN 184 184 1839 1 . SER 185 185 1839 1 . GLY 186 186 1839 1 . TYR 187 187 1839 1 . GLU 188 188 1839 1 . GLY 189 189 1839 1 . PRO 190 190 1839 1 . TRP 191 191 1839 1 . GLY 192 192 1839 1 . ALA 193 193 1839 1 . ALA 194 194 1839 1 . ASN 195 195 1839 1 . ASN 196 196 1839 1 . VAL 197 197 1839 1 . PHE 198 198 1839 1 . THR 199 199 1839 1 . ASN 200 200 1839 1 . GLU 201 201 1839 1 . PHE 202 202 1839 1 . TYR 203 203 1839 1 . LEU 204 204 1839 1 . ASN 205 205 1839 1 . LEU 206 206 1839 1 . LEU 207 207 1839 1 . ASN 208 208 1839 1 . GLU 209 209 1839 1 . ASP 210 210 1839 1 . TRP 211 211 1839 1 . LYS 212 212 1839 1 . LEU 213 213 1839 1 . GLU 214 214 1839 1 . LYS 215 215 1839 1 . ASN 216 216 1839 1 . ASP 217 217 1839 1 . ALA 218 218 1839 1 . ASN 219 219 1839 1 . ASN 220 220 1839 1 . GLU 221 221 1839 1 . GLN 222 222 1839 1 . TRP 223 223 1839 1 . ASP 224 224 1839 1 . SER 225 225 1839 1 . LYS 226 226 1839 1 . SER 227 227 1839 1 . GLY 228 228 1839 1 . TYR 229 229 1839 1 . MET 230 230 1839 1 . MET 231 231 1839 1 . LEU 232 232 1839 1 . PRO 233 233 1839 1 . THR 234 234 1839 1 . ASP 235 235 1839 1 . TYR 236 236 1839 1 . SER 237 237 1839 1 . LEU 238 238 1839 1 . ILE 239 239 1839 1 . GLN 240 240 1839 1 . ASP 241 241 1839 1 . PRO 242 242 1839 1 . LYS 243 243 1839 1 . TYR 244 244 1839 1 . LEU 245 245 1839 1 . SER 246 246 1839 1 . ILE 247 247 1839 1 . VAL 248 248 1839 1 . LYS 249 249 1839 1 . GLU 250 250 1839 1 . TYR 251 251 1839 1 . ALA 252 252 1839 1 . ASN 253 253 1839 1 . ASP 254 254 1839 1 . GLN 255 255 1839 1 . ASP 256 256 1839 1 . LYS 257 257 1839 1 . PHE 258 258 1839 1 . PHE 259 259 1839 1 . LYS 260 260 1839 1 . ASP 261 261 1839 1 . PHE 262 262 1839 1 . SER 263 263 1839 1 . LYS 264 264 1839 1 . ALA 265 265 1839 1 . PHE 266 266 1839 1 . GLU 267 267 1839 1 . LYS 268 268 1839 1 . LEU 269 269 1839 1 . LEU 270 270 1839 1 . GLU 271 271 1839 1 . ASN 272 272 1839 1 . GLY 273 273 1839 1 . ILE 274 274 1839 1 . THR 275 275 1839 1 . PHE 276 276 1839 1 . PRO 277 277 1839 1 . LYS 278 278 1839 1 . ASP 279 279 1839 1 . ALA 280 280 1839 1 . PRO 281 281 1839 1 . SER 282 282 1839 1 . PRO 283 283 1839 1 . PHE 284 284 1839 1 . ILE 285 285 1839 1 . PHE 286 286 1839 1 . LYS 287 287 1839 1 . THR 288 288 1839 1 . LEU 289 289 1839 1 . GLU 290 290 1839 1 . GLU 291 291 1839 1 . GLN 292 292 1839 1 . GLY 293 293 1839 1 . LEU 294 294 1839 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 1839 _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 $glucose_oxidase . 5061 organism . 'Aspergillus niger' . . . Eukaryota Fungi Aspergillus niger generic . . . . . . . . . . . . . . . . . . . . 1839 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 1839 _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 $glucose_oxidase . 'not available' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 1839 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Sample.Sf_category sample _Sample.Sf_framecode sample_one _Sample.Entry_ID 1839 _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 1839 _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 6.8 . na 1839 1 temperature 295 . K 1839 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 1839 _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 1839 _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' . . 1839 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 1839 _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 . . . . . . . . . . . . . . . . 1839 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 1839 _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 . H2O/HDO . . . . . ppm 4.7 . . . . . . 1 $entry_citation . . 1 $entry_citation 1839 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 1839 _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 . 1839 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 48 48 ARG HB2 H 1 3.99 . . 2 . . . . . . . . 1839 1 2 . 1 1 48 48 ARG HB3 H 1 3.28 . . 2 . . . . . . . . 1839 1 3 . 1 1 48 48 ARG HD2 H 1 1.52 . . 2 . . . . . . . . 1839 1 4 . 1 1 48 48 ARG HD3 H 1 4.66 . . 2 . . . . . . . . 1839 1 5 . 1 1 51 51 TRP HE1 H 1 18 . . 1 . . . . . . . . 1839 1 6 . 1 1 52 52 HIS HD1 H 1 16.4 . . 1 . . . . . . . . 1839 1 7 . 1 1 52 52 HIS HD2 H 1 9.6 . . 1 . . . . . . . . 1839 1 8 . 1 1 52 52 HIS HE1 H 1 14 . . 1 . . . . . . . . 1839 1 9 . 1 1 52 52 HIS HE2 H 1 28.6 . . 1 . . . . . . . . 1839 1 10 . 1 1 174 174 ALA H H 1 10 . . 1 . . . . . . . . 1839 1 11 . 1 1 174 174 ALA HA H 1 2.65 . . 1 . . . . . . . . 1839 1 12 . 1 1 174 174 ALA HB1 H 1 .3 . . 1 . . . . . . . . 1839 1 13 . 1 1 174 174 ALA HB2 H 1 .3 . . 1 . . . . . . . . 1839 1 14 . 1 1 174 174 ALA HB3 H 1 .3 . . 1 . . . . . . . . 1839 1 15 . 1 1 175 175 HIS H H 1 12.9 . . 1 . . . . . . . . 1839 1 16 . 1 1 175 175 HIS HA H 1 8.48 . . 1 . . . . . . . . 1839 1 17 . 1 1 175 175 HIS HB2 H 1 19.5 . . 2 . . . . . . . . 1839 1 18 . 1 1 175 175 HIS HB3 H 1 14.9 . . 2 . . . . . . . . 1839 1 19 . 1 1 175 175 HIS HE1 H 1 -22 . . 1 . . . . . . . . 1839 1 20 . 1 1 176 176 ALA H H 1 6.99 . . 1 . . . . . . . . 1839 1 21 . 1 1 180 180 THR HG21 H 1 2.8 . . 1 . . . . . . . . 1839 1 22 . 1 1 180 180 THR HG22 H 1 2.8 . . 1 . . . . . . . . 1839 1 23 . 1 1 180 180 THR HG23 H 1 2.8 . . 1 . . . . . . . . 1839 1 24 . 1 1 232 232 LEU HD11 H 1 2.78 . . 2 . . . . . . . . 1839 1 25 . 1 1 232 232 LEU HD12 H 1 2.78 . . 2 . . . . . . . . 1839 1 26 . 1 1 232 232 LEU HD13 H 1 2.78 . . 2 . . . . . . . . 1839 1 27 . 1 1 232 232 LEU HD21 H 1 1.24 . . 2 . . . . . . . . 1839 1 28 . 1 1 232 232 LEU HD22 H 1 1.24 . . 2 . . . . . . . . 1839 1 29 . 1 1 232 232 LEU HD23 H 1 1.24 . . 2 . . . . . . . . 1839 1 stop_ save_