data_532 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 532 _Entry.Title ; 1H NMR Studies on Bovine Cyclophilin: Preliminary Structural Characterization of Its Complex with Cyclosporin A ; _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 S. Heald . L. . 532 2 Matthew Harding . W. . 532 3 R. Handschumacher . E. . 532 4 Ian Armitage . M. . 532 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 532 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 10 532 stop_ loop_ _Release.Release_number _Release.Format_type _Release.Format_version _Release.Date _Release.Submission_date _Release.Type _Release.Author _Release.Detail _Release.Entry_ID 4 . . 2010-06-11 . revision BMRB 'Complete natural source information' 532 3 . . 1999-06-14 . revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 532 2 . . 1996-03-25 . reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 532 1 . . 1995-07-31 . original BMRB 'Last release in original BMRB flat-file format' 532 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 532 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Heald, S.L., Harding, Matthew W., Handschumacher, R.E., Armitage, Ian M., "1H NMR Studies on Bovine Cyclophilin: Preliminary Structural Characterization of Its Complex with Cyclosporin A," Biochemistry 29, 4466-4478 (1990). ; _Citation.Title ; 1H NMR Studies on Bovine Cyclophilin: Preliminary Structural Characterization of Its Complex with Cyclosporin A ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full . _Citation.Journal_volume 29 _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 4466 _Citation.Page_last 4478 _Citation.Year 1990 _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 S. Heald . L. . 532 1 2 Matthew Harding . W. . 532 1 3 R. Handschumacher . E. . 532 1 4 Ian Armitage . M. . 532 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_peptidylprolyl_isomerase _Assembly.Sf_category assembly _Assembly.Sf_framecode system_peptidylprolyl_isomerase _Assembly.Entry_ID 532 _Assembly.ID 1 _Assembly.Name 'peptidylprolyl isomerase' _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 'peptidylprolyl isomerase' 1 $peptidylprolyl_isomerase . . . . . . . . . 532 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'peptidylprolyl isomerase' system 532 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_peptidylprolyl_isomerase _Entity.Sf_category entity _Entity.Sf_framecode peptidylprolyl_isomerase _Entity.Entry_ID 532 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'peptidylprolyl isomerase' _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 ; VNPTVFFDIAVDGEPLGRVS FELFADKVPKTAENFRALST GEKGFGYKGSCFHRIIPGFM CQGGDFTRHNGTGGKSIYGE KFDDENFILKHTGPGILSMA NAGPNTNGSQFFICTAKTEW LDGKHVVFGKVKEGMNIVEA MERFGSRNGKTSKKITIADC GQI ; _Entity.Polymer_seq_one_letter_code ; VNPTVFFDIAVDGEPLGRVS FELFADKVPKTAENFRALST GEKGFGYKGSCFHRIIPGFM CQGGDFTRHNGTGGKSIYGE KFDDENFILKHTGPGILSMA NAGPNTNGSQFFICTAKTEW LDGKHVVFGKVKEGMNIVEA MERFGSRNGKTSKKITIADC GQI ; _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 163 _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 5.2.1.8 _Entity.Calc_isoelectric_point . _Entity.Formula_weight . _Entity.Formula_weight_exptl . _Entity.Formula_weight_exptl_meth . _Entity.Details . _Entity.DB_query_date . _Entity.DB_query_revised_last_date 2015-01-28 loop_ _Entity_db_link.Ordinal _Entity_db_link.Author_supplied _Entity_db_link.Database_code _Entity_db_link.Accession_code _Entity_db_link.Entry_mol_code _Entity_db_link.Entry_mol_name _Entity_db_link.Entry_experimental_method _Entity_db_link.Entry_structure_resolution _Entity_db_link.Entry_relation_type _Entity_db_link.Entry_details _Entity_db_link.Chimera_segment_ID _Entity_db_link.Seq_query_to_submitted_percent _Entity_db_link.Seq_subject_length _Entity_db_link.Seq_identity _Entity_db_link.Seq_positive _Entity_db_link.Seq_homology_expectation_val _Entity_db_link.Seq_align_begin _Entity_db_link.Seq_align_end _Entity_db_link.Seq_difference_details _Entity_db_link.Seq_alignment_details _Entity_db_link.Entry_ID _Entity_db_link.Entity_ID 1 no BMRB 17218 . CypA . . . . . 100.00 164 98.77 100.00 1.10e-113 . . . . 532 1 2 no BMRB 17461 . CypA . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 3 no BMRB 2208 . cyclophilin . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 4 no BMRB 25337 . CypA . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 5 no BMRB 531 . "peptidylprolyl isomerase" . . . . . 100.00 163 100.00 100.00 1.32e-114 . . . . 532 1 6 no PDB 1AK4 . "Human Cyclophilin A Bound To The Amino-Terminal Domain Of Hiv-1 Capsid" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 7 no PDB 1AWQ . "Cypa Complexed With Hagpia (Pseudo-Symmetric Monomer)" . . . . . 100.00 164 98.77 100.00 1.10e-113 . . . . 532 1 8 no PDB 1AWR . "Cypa Complexed With Hagpia" . . . . . 100.00 164 98.77 100.00 1.10e-113 . . . . 532 1 9 no PDB 1AWU . "Cypa Complexed With Hvgpia (Pseudo-Symmetric Monomer)" . . . . . 100.00 164 98.77 100.00 1.10e-113 . . . . 532 1 10 no PDB 1AWV . "Cypa Complexed With Hvgpia" . . . . . 100.00 164 98.77 100.00 1.10e-113 . . . . 532 1 11 no PDB 1BCK . "Human Cyclophilin A Complexed With 2-Thr Cyclosporin" . . . . . 100.00 165 98.77 100.00 1.14e-113 . . . . 532 1 12 no PDB 1CWA . "X-Ray Structure Of A Monomeric Cyclophilin A-Cyclosporin A Crystal Complex At 2.1 Angstroms Resolution" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 13 no PDB 1CWB . "The X-Ray Structure Of (Mebm2t)1-Cyclosporin Complexed With Cyclophilin A Provides An Explanation For Its Anomalously High Immu" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 14 no PDB 1CWC . "Improved Binding Affinity For Cyclophilin A By A Cyclosporin Derivative Singly Modified At Its Effector Domain" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 15 no PDB 1CWF . "Human Cyclophilin A Complexed With 2-Val Cyclosporin" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 16 no PDB 1CWH . "Human Cyclophilin A Complexed With 3-D-Ser Cyclosporin" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 17 no PDB 1CWI . "Human Cyclophilin A Complexed With 2-Val 3-(N-Methyl)-D-Alanine Cyclosporin" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 18 no PDB 1CWJ . "Human Cyclophilin A Complexed With 2-Val 3-S-Methyl-Sarcosine Cyclosporin" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 19 no PDB 1CWK . "Human Cyclophilin A Complexed With 1-(6,7-Dihydro)mebmt 2-Val 3-D-(2- S-Methyl)sarcosine Cyclosporin" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 20 no PDB 1CWL . "Human Cyclophilin A Complexed With 4 4-Hydroxy-Meleu Cyclosporin" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 21 no PDB 1CWM . "Human Cyclophilin A Complexed With 4 Meile Cyclosporin" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 22 no PDB 1CWO . "Human Cyclophilin A Complexed With Thr2, Leu5, D-Hiv8, Leu10 Cyclosporin" . . . . . 100.00 165 98.77 100.00 1.14e-113 . . . . 532 1 23 no PDB 1FGL . "Cyclophilin A Complexed With A Fragment Of Hiv-1 Gag Protein" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 24 no PDB 1M63 . "Crystal Structure Of Calcineurin-Cyclophilin-Cyclosporin Shows Common But Distinct Recognition Of Immunophilin-Drug Complexes" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 25 no PDB 1M9C . "X-Ray Crystal Structure Of Cyclophilin AHIV-1 Ca N- Terminal Domain (1-146) M-Type Complex." . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 26 no PDB 1M9D . "X-Ray Crystal Structure Of Cyclophilin AHIV-1 Ca N- Terminal Domain (1-146) O-Type Chimera Complex." . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 27 no PDB 1M9E . "X-Ray Crystal Structure Of Cyclophilin AHIV-1 Ca N- Terminal Domain (1-146) M-Type H87a Complex" . . . . . 100.00 164 98.77 100.00 7.58e-114 . . . . 532 1 28 no PDB 1M9F . "X-Ray Crystal Structure Of Cyclophilin AHIV-1 Ca N- Terminal Domain (1-146) M-Type H87a,A88m Complex." . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 29 no PDB 1M9X . "X-Ray Crystal Structure Of Cyclophilin AHIV-1 Ca N- Terminal Domain (1-146) M-Type H87a,A88m,G89a Complex." . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 30 no PDB 1M9Y . "X-Ray Crystal Structure Of Cyclophilin AHIV-1 Ca N- Terminal Domain (1-146) M-Type H87a,G89a Complex." . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 31 no PDB 1MF8 . "Crystal Structure Of Human Calcineurin Complexed With Cyclosporin A And Human Cyclophilin" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 32 no PDB 1MIK . "The Role Of Water Molecules In The Structure-Based Design Of (5- Hydroxynorvaline)-2-Cyclosporin: Synthesis, Biological Activit" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 33 no PDB 1NMK . "The Sanglifehrin-Cyclophilin Interaction: Degradation Work, Synthetic Macrocyclic Analogues, X-Ray Crystal Structure And Bindin" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 34 no PDB 1OCA . "Human Cyclophilin A, Unligated, Nmr, 20 Structures" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 35 no PDB 1RMH . "Recombinant Cyclophilin A From Human T Cell" . . . . . 100.00 164 98.77 100.00 1.10e-113 . . . . 532 1 36 no PDB 1VBS . "Structure Of Cyclophilin Complexed With (D)ala Containing Tetrapeptide" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 37 no PDB 1VBT . "Structure Of Cyclophilin Complexed With Sulfur-Substituted Tetrapeptide Aapf" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 38 no PDB 1W8L . "Enzymatic And Structural Characterization Of Non Peptide Ligand Cyclophilin Complexes" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 39 no PDB 1W8M . "Enzymatic And Structural Characterisation Of Non Peptide Ligand Cyclophilin Complexes" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 40 no PDB 1W8V . "Enzymatic And Structural Characterization Of Non Peptide Ligand Cyclophilin Complexes" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 41 no PDB 1YND . "Structure Of Human Cyclophilin A In Complex With The Novel Immunosuppressant Sanglifehrin A At 1.6a Resolution" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 42 no PDB 1ZKF . "Cyrstal Structure Of Human Cyclophilin-A In Complex With Suc-Agpf-Pna" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 43 no PDB 2ALF . "Crystal Structure Of Human Cypa Mutant K131a" . . . . . 100.00 164 97.55 99.39 2.82e-112 . . . . 532 1 44 no PDB 2CPL . "Similarities And Differences Between Human Cyclophilin A And Other Beta-Barrel Structures. Structural Refinement At 1.63 Angstr" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 45 no PDB 2CYH . "Cyclophilin A Complexed With Dipeptide Ala-Pro" . . . . . 100.00 164 98.77 100.00 1.10e-113 . . . . 532 1 46 no PDB 2RMA . "Crystal Structures Of Cyclophilin A Complexed With Cyclosporin A And N-Methyl-4-[(E)-2-Butenyl]-4,4-Dimethylthreonine Cyclospor" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 47 no PDB 2RMB . "Crystal Structures Of Cyclophilin A Complexed With Cyclosporin A And N-Methyl-4-[(E)-2-Butenyl]-4,4-Dimethylthreonine Cyclospor" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 48 no PDB 2WLW . "Structure Of The N-Terminal Capsid Domain Of Hiv-2" . . . . . 100.00 165 97.55 99.39 3.64e-112 . . . . 532 1 49 no PDB 2X25 . "Free Acetyl-Cypa Orthorhombic Form" . . . . . 100.00 169 97.55 99.39 3.70e-112 . . . . 532 1 50 no PDB 2X2A . "Free Acetyl-Cypa Trigonal Form" . . . . . 100.00 165 97.55 99.39 2.20e-112 . . . . 532 1 51 no PDB 2X2C . "Acetyl-Cypa:cyclosporine Complex" . . . . . 100.00 165 98.16 99.39 5.43e-113 . . . . 532 1 52 no PDB 2X2D . "Acetyl-Cypa:hiv-1 N-Term Capsid Domain Complex" . . . . . 100.00 165 98.16 99.39 5.43e-113 . . . . 532 1 53 no PDB 2X83 . "Evolutionary Basis Of Hiv Restriction By The Antiretroviral Trimcyp" . . . . . 100.00 163 97.55 99.39 4.09e-112 . . . . 532 1 54 no PDB 2XGY . "Complex Of Rabbit Endogenous Lentivirus (Relik)capsid With Cyclophilin A" . . . . . 100.00 173 98.77 100.00 1.88e-113 . . . . 532 1 55 no PDB 3CYH . "Cyclophilin A Complexed With Dipeptide Ser-Pro" . . . . . 100.00 164 98.77 100.00 1.10e-113 . . . . 532 1 56 no PDB 3CYS . "Determination Of The Nmr Solution Structure Of The Cyclophilin A- Cyclosporin A Complex" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 57 no PDB 3K0M . "Cryogenic Structure Of Cypa" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 58 no PDB 3K0N . "Room Temperature Structure Of Cypa" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 59 no PDB 3K0O . "Room Temperature Structure Of Cypa Mutant Ser99thr" . . . . . 100.00 165 98.16 100.00 1.76e-113 . . . . 532 1 60 no PDB 3K0P . "Cryogenic Structure Of Cypa Mutant Ser99thr" . . . . . 100.00 165 98.16 100.00 1.76e-113 . . . . 532 1 61 no PDB 3K0Q . "Cryogenic Structure Of Cypa Mutant Ser99thr (2)" . . . . . 100.00 165 98.16 100.00 1.76e-113 . . . . 532 1 62 no PDB 3K0R . "Cryogenic Structure Of Cypa Mutant Arg55lys" . . . . . 100.00 165 98.16 100.00 2.47e-113 . . . . 532 1 63 no PDB 3ODI . "Crystal Structure Of Cyclophilin A In Complex With Voclosporin E- Isa247" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 64 no PDB 3ODL . "Crystal Structure Of Cyclophilin A In Complex With Voclosporin Z- Isa247" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 65 no PDB 3RDD . "Human Cyclophilin A Complexed With An Inhibitor" . . . . . 100.00 184 98.77 100.00 1.16e-113 . . . . 532 1 66 no PDB 4CYH . "Cyclophilin A Complexed With Dipeptide His-Pro" . . . . . 100.00 164 98.77 100.00 1.10e-113 . . . . 532 1 67 no PDB 4DGA . "Trimcyp Cyclophilin Domain From Macaca Mulatta: Hiv-1 Ca(O-Loop) Complex" . . . . . 100.00 165 97.55 99.39 3.64e-112 . . . . 532 1 68 no PDB 4DGB . "Trimcyp Cyclophilin Domain From Macaca Mulatta: Hiv-2 Ca Cyclophilin- Binding Loop Complex" . . . . . 100.00 165 97.55 99.39 3.64e-112 . . . . 532 1 69 no PDB 4DGC . "Trimcyp Cyclophilin Domain From Macaca Mulatta: Cyclosporin A Complex" . . . . . 100.00 165 97.55 99.39 3.64e-112 . . . . 532 1 70 no PDB 4DGD . "Trimcyp Cyclophilin Domain From Macaca Mulatta: H70c Mutant" . . . . . 100.00 165 96.93 98.77 1.68e-110 . . . . 532 1 71 no PDB 4DGE . "Trimcyp Cyclophilin Domain From Macaca Mulatta: H70c Mutant, Hiv-1 Ca(O-Loop) Complex" . . . . . 100.00 165 96.93 98.77 1.68e-110 . . . . 532 1 72 no PDB 4IPZ . "Smbz Bound To Cyclophilin A" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 73 no PDB 5CYH . "Cyclophilin A Complexed With Dipeptide Gly-Pro" . . . . . 100.00 164 98.77 100.00 1.10e-113 . . . . 532 1 74 no DBJ BAE01146 . "unnamed protein product [Macaca fascicularis]" . . . . . 63.80 105 97.12 100.00 5.37e-67 . . . . 532 1 75 no DBJ BAE87660 . "unnamed protein product [Macaca fascicularis]" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 76 no DBJ BAF82774 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 77 no DBJ BAF83540 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 165 98.16 100.00 2.58e-113 . . . . 532 1 78 no DBJ BAF85692 . "unnamed protein product [Homo sapiens]" . . . . . 63.80 105 98.08 100.00 1.08e-67 . . . . 532 1 79 no EMBL CAA37039 . "peptidylprolyl isomerase [Homo sapiens]" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 80 no EMBL CAA68264 . "unnamed protein product [Homo sapiens]" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 81 no EMBL CAG32988 . "PPIA [Homo sapiens]" . . . . . 100.00 165 98.77 100.00 9.04e-114 . . . . 532 1 82 no EMBL CAH91833 . "hypothetical protein [Pongo abelii]" . . . . . 100.00 165 98.16 99.39 3.11e-113 . . . . 532 1 83 no EMBL CAZ64804 . "peptidylprolyl isomerase A (cyclophilin A) [Sus scrofa]" . . . . . 100.00 164 100.00 100.00 1.18e-114 . . . . 532 1 84 no GB AAB81959 . "cyclophilin A [Papio hamadryas]" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 85 no GB AAB81960 . "cyclophilin A [Chlorocebus aethiops]" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 86 no GB AAB81961 . "cyclophilin A [Macaca mulatta]" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 87 no GB AAF69142 . "cyclophilin I [Bos taurus]" . . . . . 57.06 94 100.00 100.00 8.89e-60 . . . . 532 1 88 no GB AAF78600 . "cyclophilin A [Canis lupus familiaris]" . . . . . 95.71 156 100.00 100.00 3.88e-109 . . . . 532 1 89 no PRF 1503232A . "peptidyl-Pro cis trans isomerase" . . . . . 100.00 164 100.00 100.00 1.18e-114 . . . . 532 1 90 no REF NP_001009370 . "peptidyl-prolyl cis-trans isomerase A [Felis catus]" . . . . . 100.00 164 98.16 98.77 2.06e-112 . . . . 532 1 91 no REF NP_001027981 . "peptidyl-prolyl cis-trans isomerase A [Macaca mulatta]" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 92 no REF NP_001126060 . "peptidyl-prolyl cis-trans isomerase A [Pongo abelii]" . . . . . 100.00 165 98.16 99.39 3.11e-113 . . . . 532 1 93 no REF NP_001270275 . "uncharacterized protein LOC101866023 [Macaca fascicularis]" . . . . . 63.80 105 97.12 100.00 5.37e-67 . . . . 532 1 94 no REF NP_001271703 . "uncharacterized protein LOC101925040 [Macaca fascicularis]" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 95 no SP P62935 . "RecName: Full=Peptidyl-prolyl cis-trans isomerase A; Short=PPIase A; AltName: Full=Cyclophilin A; AltName: Full=Cyclosporin A-b" . . . . . 100.00 164 100.00 100.00 1.18e-114 . . . . 532 1 96 no SP P62936 . "RecName: Full=Peptidyl-prolyl cis-trans isomerase A; Short=PPIase A; AltName: Full=Cyclophilin A; AltName: Full=Cyclosporin A-b" . . . . . 100.00 164 100.00 100.00 1.18e-114 . . . . 532 1 97 no SP P62937 . "RecName: Full=Peptidyl-prolyl cis-trans isomerase A; Short=PPIase A; AltName: Full=Cyclophilin A; AltName: Full=Cyclosporin A-b" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 98 no SP P62938 . "RecName: Full=Peptidyl-prolyl cis-trans isomerase A; Short=PPIase A; AltName: Full=Cyclophilin A; AltName: Full=Cyclosporin A-b" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 99 no SP P62940 . "RecName: Full=Peptidyl-prolyl cis-trans isomerase A; Short=PPIase A; AltName: Full=Cyclophilin A; AltName: Full=Cyclosporin A-b" . . . . . 100.00 165 98.77 100.00 6.73e-114 . . . . 532 1 100 no TPG DAA25853 . "TPA: TRIM5/cyclophilin A fusion protein-like [Bos taurus]" . . . . . 100.00 164 98.77 98.77 3.43e-113 . . . . 532 1 101 no TPG DAA25854 . "TPA: TRIM5/cyclophilin A fusion protein-like [Bos taurus]" . . . . . 100.00 164 98.77 98.77 3.43e-113 . . . . 532 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'major isoform (non N-acetylated)' variant 532 1 'peptidylprolyl isomerase' common 532 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 . VAL . 532 1 2 . ASN . 532 1 3 . PRO . 532 1 4 . THR . 532 1 5 . VAL . 532 1 6 . PHE . 532 1 7 . PHE . 532 1 8 . ASP . 532 1 9 . ILE . 532 1 10 . ALA . 532 1 11 . VAL . 532 1 12 . ASP . 532 1 13 . GLY . 532 1 14 . GLU . 532 1 15 . PRO . 532 1 16 . LEU . 532 1 17 . GLY . 532 1 18 . ARG . 532 1 19 . VAL . 532 1 20 . SER . 532 1 21 . PHE . 532 1 22 . GLU . 532 1 23 . LEU . 532 1 24 . PHE . 532 1 25 . ALA . 532 1 26 . ASP . 532 1 27 . LYS . 532 1 28 . VAL . 532 1 29 . PRO . 532 1 30 . LYS . 532 1 31 . THR . 532 1 32 . ALA . 532 1 33 . GLU . 532 1 34 . ASN . 532 1 35 . PHE . 532 1 36 . ARG . 532 1 37 . ALA . 532 1 38 . LEU . 532 1 39 . SER . 532 1 40 . THR . 532 1 41 . GLY . 532 1 42 . GLU . 532 1 43 . LYS . 532 1 44 . GLY . 532 1 45 . PHE . 532 1 46 . GLY . 532 1 47 . TYR . 532 1 48 . LYS . 532 1 49 . GLY . 532 1 50 . SER . 532 1 51 . CYS . 532 1 52 . PHE . 532 1 53 . HIS . 532 1 54 . ARG . 532 1 55 . ILE . 532 1 56 . ILE . 532 1 57 . PRO . 532 1 58 . GLY . 532 1 59 . PHE . 532 1 60 . MET . 532 1 61 . CYS . 532 1 62 . GLN . 532 1 63 . GLY . 532 1 64 . GLY . 532 1 65 . ASP . 532 1 66 . PHE . 532 1 67 . THR . 532 1 68 . ARG . 532 1 69 . HIS . 532 1 70 . ASN . 532 1 71 . GLY . 532 1 72 . THR . 532 1 73 . GLY . 532 1 74 . GLY . 532 1 75 . LYS . 532 1 76 . SER . 532 1 77 . ILE . 532 1 78 . TYR . 532 1 79 . GLY . 532 1 80 . GLU . 532 1 81 . LYS . 532 1 82 . PHE . 532 1 83 . ASP . 532 1 84 . ASP . 532 1 85 . GLU . 532 1 86 . ASN . 532 1 87 . PHE . 532 1 88 . ILE . 532 1 89 . LEU . 532 1 90 . LYS . 532 1 91 . HIS . 532 1 92 . THR . 532 1 93 . GLY . 532 1 94 . PRO . 532 1 95 . GLY . 532 1 96 . ILE . 532 1 97 . LEU . 532 1 98 . SER . 532 1 99 . MET . 532 1 100 . ALA . 532 1 101 . ASN . 532 1 102 . ALA . 532 1 103 . GLY . 532 1 104 . PRO . 532 1 105 . ASN . 532 1 106 . THR . 532 1 107 . ASN . 532 1 108 . GLY . 532 1 109 . SER . 532 1 110 . GLN . 532 1 111 . PHE . 532 1 112 . PHE . 532 1 113 . ILE . 532 1 114 . CYS . 532 1 115 . THR . 532 1 116 . ALA . 532 1 117 . LYS . 532 1 118 . THR . 532 1 119 . GLU . 532 1 120 . TRP . 532 1 121 . LEU . 532 1 122 . ASP . 532 1 123 . GLY . 532 1 124 . LYS . 532 1 125 . HIS . 532 1 126 . VAL . 532 1 127 . VAL . 532 1 128 . PHE . 532 1 129 . GLY . 532 1 130 . LYS . 532 1 131 . VAL . 532 1 132 . LYS . 532 1 133 . GLU . 532 1 134 . GLY . 532 1 135 . MET . 532 1 136 . ASN . 532 1 137 . ILE . 532 1 138 . VAL . 532 1 139 . GLU . 532 1 140 . ALA . 532 1 141 . MET . 532 1 142 . GLU . 532 1 143 . ARG . 532 1 144 . PHE . 532 1 145 . GLY . 532 1 146 . SER . 532 1 147 . ARG . 532 1 148 . ASN . 532 1 149 . GLY . 532 1 150 . LYS . 532 1 151 . THR . 532 1 152 . SER . 532 1 153 . LYS . 532 1 154 . LYS . 532 1 155 . ILE . 532 1 156 . THR . 532 1 157 . ILE . 532 1 158 . ALA . 532 1 159 . ASP . 532 1 160 . CYS . 532 1 161 . GLY . 532 1 162 . GLN . 532 1 163 . ILE . 532 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 . VAL 1 1 532 1 . ASN 2 2 532 1 . PRO 3 3 532 1 . THR 4 4 532 1 . VAL 5 5 532 1 . PHE 6 6 532 1 . PHE 7 7 532 1 . ASP 8 8 532 1 . ILE 9 9 532 1 . ALA 10 10 532 1 . VAL 11 11 532 1 . ASP 12 12 532 1 . GLY 13 13 532 1 . GLU 14 14 532 1 . PRO 15 15 532 1 . LEU 16 16 532 1 . GLY 17 17 532 1 . ARG 18 18 532 1 . VAL 19 19 532 1 . SER 20 20 532 1 . PHE 21 21 532 1 . GLU 22 22 532 1 . LEU 23 23 532 1 . PHE 24 24 532 1 . ALA 25 25 532 1 . ASP 26 26 532 1 . LYS 27 27 532 1 . VAL 28 28 532 1 . PRO 29 29 532 1 . LYS 30 30 532 1 . THR 31 31 532 1 . ALA 32 32 532 1 . GLU 33 33 532 1 . ASN 34 34 532 1 . PHE 35 35 532 1 . ARG 36 36 532 1 . ALA 37 37 532 1 . LEU 38 38 532 1 . SER 39 39 532 1 . THR 40 40 532 1 . GLY 41 41 532 1 . GLU 42 42 532 1 . LYS 43 43 532 1 . GLY 44 44 532 1 . PHE 45 45 532 1 . GLY 46 46 532 1 . TYR 47 47 532 1 . LYS 48 48 532 1 . GLY 49 49 532 1 . SER 50 50 532 1 . CYS 51 51 532 1 . PHE 52 52 532 1 . HIS 53 53 532 1 . ARG 54 54 532 1 . ILE 55 55 532 1 . ILE 56 56 532 1 . PRO 57 57 532 1 . GLY 58 58 532 1 . PHE 59 59 532 1 . MET 60 60 532 1 . CYS 61 61 532 1 . GLN 62 62 532 1 . GLY 63 63 532 1 . GLY 64 64 532 1 . ASP 65 65 532 1 . PHE 66 66 532 1 . THR 67 67 532 1 . ARG 68 68 532 1 . HIS 69 69 532 1 . ASN 70 70 532 1 . GLY 71 71 532 1 . THR 72 72 532 1 . GLY 73 73 532 1 . GLY 74 74 532 1 . LYS 75 75 532 1 . SER 76 76 532 1 . ILE 77 77 532 1 . TYR 78 78 532 1 . GLY 79 79 532 1 . GLU 80 80 532 1 . LYS 81 81 532 1 . PHE 82 82 532 1 . ASP 83 83 532 1 . ASP 84 84 532 1 . GLU 85 85 532 1 . ASN 86 86 532 1 . PHE 87 87 532 1 . ILE 88 88 532 1 . LEU 89 89 532 1 . LYS 90 90 532 1 . HIS 91 91 532 1 . THR 92 92 532 1 . GLY 93 93 532 1 . PRO 94 94 532 1 . GLY 95 95 532 1 . ILE 96 96 532 1 . LEU 97 97 532 1 . SER 98 98 532 1 . MET 99 99 532 1 . ALA 100 100 532 1 . ASN 101 101 532 1 . ALA 102 102 532 1 . GLY 103 103 532 1 . PRO 104 104 532 1 . ASN 105 105 532 1 . THR 106 106 532 1 . ASN 107 107 532 1 . GLY 108 108 532 1 . SER 109 109 532 1 . GLN 110 110 532 1 . PHE 111 111 532 1 . PHE 112 112 532 1 . ILE 113 113 532 1 . CYS 114 114 532 1 . THR 115 115 532 1 . ALA 116 116 532 1 . LYS 117 117 532 1 . THR 118 118 532 1 . GLU 119 119 532 1 . TRP 120 120 532 1 . LEU 121 121 532 1 . ASP 122 122 532 1 . GLY 123 123 532 1 . LYS 124 124 532 1 . HIS 125 125 532 1 . VAL 126 126 532 1 . VAL 127 127 532 1 . PHE 128 128 532 1 . GLY 129 129 532 1 . LYS 130 130 532 1 . VAL 131 131 532 1 . LYS 132 132 532 1 . GLU 133 133 532 1 . GLY 134 134 532 1 . MET 135 135 532 1 . ASN 136 136 532 1 . ILE 137 137 532 1 . VAL 138 138 532 1 . GLU 139 139 532 1 . ALA 140 140 532 1 . MET 141 141 532 1 . GLU 142 142 532 1 . ARG 143 143 532 1 . PHE 144 144 532 1 . GLY 145 145 532 1 . SER 146 146 532 1 . ARG 147 147 532 1 . ASN 148 148 532 1 . GLY 149 149 532 1 . LYS 150 150 532 1 . THR 151 151 532 1 . SER 152 152 532 1 . LYS 153 153 532 1 . LYS 154 154 532 1 . ILE 155 155 532 1 . THR 156 156 532 1 . ILE 157 157 532 1 . ALA 158 158 532 1 . ASP 159 159 532 1 . CYS 160 160 532 1 . GLY 161 161 532 1 . GLN 162 162 532 1 . ILE 163 163 532 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 532 _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 $peptidylprolyl_isomerase . 9909 organism . 'Bos primigenius' cow . . Eukaryota Metazoa Bos primigenius . . . . thymus . . . . . . . . . . . . . . . . 532 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 532 _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 $peptidylprolyl_isomerase . 'not available' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 532 1 stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Sample.Sf_category sample _Sample.Sf_framecode sample_one _Sample.Entry_ID 532 _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 532 _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 532 1 temperature 298 . K 532 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 532 _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 532 _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' . . 532 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 532 _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 . . . . . . . . . . . . . . . . 532 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 532 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details 'The chemical shift reference is not available at this time.' 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 . . . . . . . . . . . . . . . . 1 $entry_citation . . 1 $entry_citation 532 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 532 _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 . 532 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 1 120 120 TRP H H 1 7.34 . . 1 . . . . . . . . 532 1 2 . 1 1 120 120 TRP HA H 1 4.72 . . 1 . . . . . . . . 532 1 3 . 1 1 120 120 TRP HB2 H 1 3.48 . . 2 . . . . . . . . 532 1 4 . 1 1 120 120 TRP HB3 H 1 3.46 . . 2 . . . . . . . . 532 1 5 . 1 1 120 120 TRP HD1 H 1 7.02 . . 1 . . . . . . . . 532 1 6 . 1 1 120 120 TRP HE1 H 1 10.98 . . 1 . . . . . . . . 532 1 7 . 1 1 120 120 TRP HE3 H 1 7.07 . . 1 . . . . . . . . 532 1 8 . 1 1 120 120 TRP HZ2 H 1 7.84 . . 1 . . . . . . . . 532 1 9 . 1 1 120 120 TRP HZ3 H 1 7.43 . . 1 . . . . . . . . 532 1 10 . 1 1 120 120 TRP HH2 H 1 7.55 . . 1 . . . . . . . . 532 1 stop_ save_