data_862 ####################### # Entry information # ####################### save_entry_information _Entry.Sf_category entry_information _Entry.Sf_framecode entry_information _Entry.ID 862 _Entry.Title ; Hydrogen-1 Nuclear Magnetic Resonance Investigation of Bovine Cardiac Troponin C. Comparison of Tyrosyl Assignments and Calcium-Induced Structural Changes to Those of Two Homologous Proteins, Rabbit Skeletal Troponin C and Bovine Brain Calm ; _Entry.Type macromolecule _Entry.Version_type update _Entry.Submission_date 1995-07-31 _Entry.Accession_date 1996-04-12 _Entry.Last_release_date . _Entry.Original_release_date . _Entry.Origination BMRB _Entry.NMR_STAR_version 3.1.1.61 _Entry.Original_NMR_STAR_version . _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 Maxwell Hincke . T. . 862 2 Brian Sykes . D. . 862 3 Cyril Kay . M. . 862 stop_ loop_ _Data_set.Type _Data_set.Count _Data_set.Entry_ID assigned_chemical_shifts 1 862 stop_ loop_ _Datum.Type _Datum.Count _Datum.Entry_ID '1H chemical shifts' 12 862 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 6 . . 2010-06-11 . revision BMRB 'Complete natural source information' 862 5 . . 2008-09-30 . revision BMRB 'Updating non-standard residue' 862 4 . . 1999-06-14 . revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 862 3 . . 1996-04-12 . revision BMRB 'Error corrected in abrreviations given to non-polymers' 862 2 . . 1996-03-25 . reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 862 1 . . 1995-07-31 . original BMRB 'Last release in original BMRB flat-file format' 862 stop_ save_ ############### # Citations # ############### save_entry_citation _Citation.Sf_category citations _Citation.Sf_framecode entry_citation _Citation.Entry_ID 862 _Citation.ID 1 _Citation.Class 'entry citation' _Citation.CAS_abstract_code . _Citation.MEDLINE_UI_code . _Citation.DOI . _Citation.PubMed_ID . _Citation.Full_citation ; Hincke, Maxwell T., Sykes, Brian D., Kay, Cyril M., "Hydrogen-1 Nuclear Magnetic Resonance Investigation of Bovine Cardiac Troponin C. Comparison of Tyrosyl Assignments and Calcium-Induced Structural Changes to Those of Two Homologous Proteins, Rabbit Skeletal Troponin C and Bovine Brain Calm," Biochemistry 20, 3286-3294 (1981). ; _Citation.Title ; Hydrogen-1 Nuclear Magnetic Resonance Investigation of Bovine Cardiac Troponin C. Comparison of Tyrosyl Assignments and Calcium-Induced Structural Changes to Those of Two Homologous Proteins, Rabbit Skeletal Troponin C and Bovine Brain Calm ; _Citation.Status published _Citation.Type journal _Citation.Journal_abbrev Biochemistry _Citation.Journal_name_full . _Citation.Journal_volume 20 _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 3286 _Citation.Page_last 3294 _Citation.Year 1981 _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 Maxwell Hincke . T. . 862 1 2 Brian Sykes . D. . 862 1 3 Cyril Kay . M. . 862 1 stop_ save_ ############################################# # Molecular system (assembly) description # ############################################# save_system_troponin_C _Assembly.Sf_category assembly _Assembly.Sf_framecode system_troponin_C _Assembly.Entry_ID 862 _Assembly.ID 1 _Assembly.Name 'troponin C' _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 'troponin C' 1 $troponin_C . . . . . . . . . 862 1 stop_ loop_ _Assembly_common_name.Name _Assembly_common_name.Type _Assembly_common_name.Entry_ID _Assembly_common_name.Assembly_ID 'troponin C' system 862 1 stop_ save_ #################################### # Biological polymers and ligands # #################################### save_troponin_C _Entity.Sf_category entity _Entity.Sf_framecode troponin_C _Entity.Entry_ID 862 _Entity.ID 1 _Entity.BMRB_code . _Entity.Name 'troponin C' _Entity.Type polymer _Entity.Polymer_common_type . _Entity.Polymer_type polypeptide(L) _Entity.Polymer_type_details . _Entity.Polymer_strand_ID . _Entity.Polymer_seq_one_letter_code_can . _Entity.Polymer_seq_one_letter_code ; XDDIYKAAVEQLTEEQKNEF KAAFDIFVLGAEDGCISTKE LGKVMRMLGQNPTPEELQEM IDEVDEDGSGTVDFDEFLVM MVRCMKDDSKGKSEEELSDL FRMFDKNADGYIDLELKIML QATGETITEDDIEELMKDGD KNNDGRIDYDEFLEFMKGVE ; _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 160 _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 . _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 15385 . F104W . . . . . 99.38 161 97.50 98.13 1.65e-103 . . . . 862 1 2 no BMRB 15388 . F153W . . . . . 99.38 161 97.50 98.13 1.65e-103 . . . . 862 1 3 no BMRB 15400 . F153(FTR) . . . . . 99.38 161 97.50 97.50 7.12e-103 . . . . 862 1 4 no BMRB 15427 . F104(FTR) . . . . . 99.38 161 97.50 98.13 1.65e-103 . . . . 862 1 5 no BMRB 16190 . cNTnC . . . . . 54.66 89 97.73 97.73 8.57e-52 . . . . 862 1 6 no BMRB 16752 . TnC . . . . . 99.38 161 98.75 99.38 1.18e-105 . . . . 862 1 7 no BMRB 17103 . cNTnC . . . . . 54.66 89 100.00 100.00 3.92e-54 . . . . 862 1 8 no BMRB 19789 . cNTnC . . . . . 54.66 89 100.00 100.00 3.92e-54 . . . . 862 1 9 no BMRB 25034 . cChimera . . . . . 54.66 141 98.86 98.86 2.45e-53 . . . . 862 1 10 no BMRB 25035 . cChimeraX . . . . . 54.66 141 98.86 98.86 1.89e-53 . . . . 862 1 11 no BMRB 25120 . cTnC . . . . . 99.38 161 98.13 98.13 5.41e-104 . . . . 862 1 12 no BMRB 4822 . TnC . . . . . 55.90 93 100.00 100.00 1.18e-55 . . . . 862 1 13 no BMRB 4823 . TnC . . . . . 55.90 93 100.00 100.00 1.18e-55 . . . . 862 1 14 no BMRB 846 . troponin_C . . . . . 99.38 161 100.00 100.00 3.92e-106 . . . . 862 1 15 no BMRB 934 . troponin_C . . . . . 99.38 161 100.00 100.00 3.92e-106 . . . . 862 1 16 no PDB 1AJ4 . "Structure Of Calcium-Saturated Cardiac Troponin C, Nmr, 1 Structure" . . . . . 98.76 161 97.48 98.11 3.50e-103 . . . . 862 1 17 no PDB 1AP4 . "Regulatory Domain Of Human Cardiac Troponin C In The Calcium-Saturated State, Nmr, 40 Structures" . . . . . 54.66 89 100.00 100.00 3.92e-54 . . . . 862 1 18 no PDB 1DTL . "Crystal Structure Of Calcium-Saturated (3ca2+) Cardiac Troponin C Complexed With The Calcium Sensitizer Bepridil At 2.15 A Reso" . . . . . 99.38 161 98.13 98.13 4.69e-104 . . . . 862 1 19 no PDB 1FI5 . "Nmr Structure Of The C Terminal Domain Of Cardiac Troponin C Bound To The N Terminal Domain Of Cardiac Troponin I." . . . . . 50.31 81 97.53 98.77 1.04e-45 . . . . 862 1 20 no PDB 1J1D . "Crystal Structure Of The 46kda Domain Of Human Cardiac Troponin In The Ca2+ Saturated Form" . . . . . 99.38 161 98.13 98.13 4.69e-104 . . . . 862 1 21 no PDB 1J1E . "Crystal Structure Of The 52kda Domain Of Human Cardiac Troponin In The Ca2+ Saturated Form" . . . . . 99.38 161 98.13 98.13 4.69e-104 . . . . 862 1 22 no PDB 1LA0 . "Solution Structure Of Calcium Saturated Cardiac Troponin C In The Troponin C-Troponin I Complex" . . . . . 99.38 161 98.75 99.38 1.18e-105 . . . . 862 1 23 no PDB 1LXF . "Structure Of The Regulatory N-Domain Of Human Cardiac Troponin C In Complex With Human Cardiac Troponin-I(147- 163) And Bepridi" . . . . . 54.66 89 100.00 100.00 3.92e-54 . . . . 862 1 24 no PDB 1MXL . "Structure Of Cardiac Troponin C-troponin I Complex" . . . . . 54.66 89 100.00 100.00 3.92e-54 . . . . 862 1 25 no PDB 1SBJ . "Nmr Structure Of The Mg2+-Loaded C Terminal Domain Of Cardiac Troponin C Bound To The N Terminal Domain Of Cardiac Troponin I" . . . . . 50.31 81 97.53 98.77 1.04e-45 . . . . 862 1 26 no PDB 1SCV . "Nmr Structure Of The C Terminal Domain Of Cardiac Troponin C Bound To The N Terminal Domain Of Cardiac Troponin I" . . . . . 50.31 81 97.53 98.77 1.04e-45 . . . . 862 1 27 no PDB 1SPY . "Regulatory Domain Of Human Cardiac Troponin C In The Calcium-Free State, Nmr, 40 Structures" . . . . . 54.66 89 100.00 100.00 3.92e-54 . . . . 862 1 28 no PDB 1WRK . "Crystal Structure Of The N-Terminal Domain Of Human Cardiac Troponin C In Complex With Trifluoperazine (Orthrombic Crystal Form" . . . . . 54.04 88 97.70 97.70 4.84e-51 . . . . 862 1 29 no PDB 1WRL . "Crystal Structure Of The N-Terminal Domain Of Human Cardiac Troponin C In Complex With Trifluoperazine (Monoclinic Crystal Form" . . . . . 54.04 88 97.70 97.70 4.84e-51 . . . . 862 1 30 no PDB 2CTN . "Structure Of Calcium-Saturated Cardiac Troponin C, Nmr, 30 Structures" . . . . . 54.04 89 97.70 97.70 2.60e-51 . . . . 862 1 31 no PDB 2JT0 . "Solution Structure Of F104w Cardiac Troponin C" . . . . . 99.38 161 97.50 98.13 1.65e-103 . . . . 862 1 32 no PDB 2JT3 . "Solution Structure Of F153w Cardiac Troponin C" . . . . . 99.38 161 97.50 98.13 1.65e-103 . . . . 862 1 33 no PDB 2JT8 . "Solution Structure Of The F153-To-5-Flurotryptophan Mutant Of Human Cardiac Troponin C" . . . . . 99.38 161 97.50 97.50 7.12e-103 . . . . 862 1 34 no PDB 2JTZ . "Solution Structure And Chemical Shift Assignments Of The F104-To-5-Flurotryptophan Mutant Of Cardiac Troponin C" . . . . . 99.38 161 97.50 97.50 7.12e-103 . . . . 862 1 35 no PDB 2JXL . "Solution Structure Of Cardiac N-Domain Troponin C Mutant F77w-V82a" . . . . . 54.66 89 97.73 98.86 3.48e-53 . . . . 862 1 36 no PDB 2KFX . "Structure Of The N-Terminal Domain Of Human Cardiac Troponin C Bound To Calcium Ion And To The Inhibitor W7" . . . . . 54.66 89 97.73 97.73 8.57e-52 . . . . 862 1 37 no PDB 2KGB . "Nmr Solution Of The Regulatory Domain Cardiac F77w-Troponin C In Complex With The Cardiac Troponin I 144-163 Switch Peptide" . . . . . 54.66 89 98.86 100.00 8.58e-54 . . . . 862 1 38 no PDB 2KRD . "Solution Structure Of The Regulatory Domain Of Human Cardiac C In Complex With The Switch Region Of Cardiac Troponin I A" . . . . . 54.66 89 100.00 100.00 3.92e-54 . . . . 862 1 39 no PDB 2L1R . "The Structure Of The Calcium-Sensitizer, Dfbp-O, In Complex With The N-Domain Of Troponin C And The Switch Region Of Troponin I" . . . . . 54.66 89 100.00 100.00 3.92e-54 . . . . 862 1 40 no PDB 2MKP . "N Domain Of Cardiac Troponin C Bound To The Switch Fragment Of Fast Skeletal Troponin I At Ph 6" . . . . . 54.66 89 100.00 100.00 3.92e-54 . . . . 862 1 41 no PDB 3SD6 . "Crystal Structure Of The Amino-terminal Domain Of Human Cardiac Troponin C In Complex With Cadmium At 1.4 Resolution." . . . . . 54.66 89 100.00 100.00 3.92e-54 . . . . 862 1 42 no PDB 3SWB . "Crystal Structure Of The Amino-terminal Domain Of Human Cardiac Troponin C In Complex With Cadmium At 1.7 A Resolution" . . . . . 54.66 89 100.00 100.00 3.92e-54 . . . . 862 1 43 no PDB 4GJE . "Crystal Structure Of The Refolded Amino-terminal Domain Of Human Cardiac Troponin C In Complex With Cadmium" . . . . . 54.66 89 100.00 100.00 3.92e-54 . . . . 862 1 44 no DBJ BAA02369 . "cardiac troponin C [Gallus gallus]" . . . . . 99.38 161 98.75 99.38 1.18e-105 . . . . 862 1 45 no DBJ BAG36483 . "unnamed protein product [Homo sapiens]" . . . . . 99.38 161 99.38 99.38 5.32e-106 . . . . 862 1 46 no EMBL CAA30736 . "unnamed protein product [Homo sapiens]" . . . . . 99.38 161 99.38 99.38 5.32e-106 . . . . 862 1 47 no EMBL CAG46663 . "TNNC1 [Homo sapiens]" . . . . . 99.38 161 99.38 99.38 5.32e-106 . . . . 862 1 48 no EMBL CAG46683 . "TNNC1 [Homo sapiens]" . . . . . 99.38 161 99.38 99.38 5.32e-106 . . . . 862 1 49 no GB AAA36772 . "slow twitch skeletal/cardiac muscle troponin C [Homo sapiens]" . . . . . 99.38 161 99.38 99.38 5.32e-106 . . . . 862 1 50 no GB AAA37492 . "slow/cardiac troponin C, partial [Mus musculus]" . . . . . 99.38 161 98.75 99.38 1.85e-105 . . . . 862 1 51 no GB AAA37493 . "slow/cardiac troponin C [Mus musculus]" . . . . . 99.38 161 98.75 99.38 1.85e-105 . . . . 862 1 52 no GB AAA48654 . "slow muscle troponin C [Gallus gallus]" . . . . . 99.38 161 98.75 99.38 1.18e-105 . . . . 862 1 53 no GB AAB91994 . "cardiac ventricular troponin C [Homo sapiens]" . . . . . 99.38 160 98.75 98.75 1.24e-103 . . . . 862 1 54 no PIR TPHUCC . "troponin C, cardiac and slow skeletal muscle - human" . . . . . 99.38 161 99.38 99.38 5.32e-106 . . . . 862 1 55 no PRF 1510257A . "troponin C" . . . . . 99.38 161 99.38 99.38 4.42e-106 . . . . 862 1 56 no PRF 750650A . "troponin c,cardiac" . . . . . 99.38 161 99.38 99.38 4.42e-106 . . . . 862 1 57 no REF NP_001029277 . "troponin C, slow skeletal and cardiac muscles [Rattus norvegicus]" . . . . . 99.38 161 98.75 99.38 1.85e-105 . . . . 862 1 58 no REF NP_001029523 . "troponin C, slow skeletal and cardiac muscles [Bos taurus]" . . . . . 99.38 161 99.38 99.38 4.42e-106 . . . . 862 1 59 no REF NP_001123715 . "troponin C, slow skeletal and cardiac muscles [Sus scrofa]" . . . . . 99.38 161 99.38 99.38 4.42e-106 . . . . 862 1 60 no REF NP_001272501 . "troponin C type 1 (slow) [Capra hircus]" . . . . . 99.38 161 99.38 99.38 4.42e-106 . . . . 862 1 61 no REF NP_003271 . "troponin C, slow skeletal and cardiac muscles [Homo sapiens]" . . . . . 99.38 161 99.38 99.38 5.32e-106 . . . . 862 1 62 no SP P02591 . "RecName: Full=Troponin C, slow skeletal and cardiac muscles; Short=TN-C [Oryctolagus cuniculus]" . . . . . 99.38 161 99.38 99.38 5.32e-106 . . . . 862 1 63 no SP P09860 . "RecName: Full=Troponin C, slow skeletal and cardiac muscles; Short=TN-C [Gallus gallus]" . . . . . 99.38 161 98.75 99.38 1.18e-105 . . . . 862 1 64 no SP P19123 . "RecName: Full=Troponin C, slow skeletal and cardiac muscles; Short=TN-C [Mus musculus]" . . . . . 99.38 161 98.75 99.38 1.85e-105 . . . . 862 1 65 no SP P63315 . "RecName: Full=Troponin C, slow skeletal and cardiac muscles; Short=TN-C [Bos taurus]" . . . . . 99.38 161 99.38 99.38 4.42e-106 . . . . 862 1 66 no SP P63316 . "RecName: Full=Troponin C, slow skeletal and cardiac muscles; Short=TN-C [Homo sapiens]" . . . . . 99.38 161 99.38 99.38 5.32e-106 . . . . 862 1 67 no TPG DAA16908 . "TPA: troponin C, slow skeletal and cardiac muscles [Bos taurus]" . . . . . 99.38 161 99.38 99.38 4.42e-106 . . . . 862 1 stop_ loop_ _Entity_common_name.Name _Entity_common_name.Type _Entity_common_name.Entry_ID _Entity_common_name.Entity_ID 'troponin C' common 862 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 . AME . 862 1 2 . ASP . 862 1 3 . ASP . 862 1 4 . ILE . 862 1 5 . TYR . 862 1 6 . LYS . 862 1 7 . ALA . 862 1 8 . ALA . 862 1 9 . VAL . 862 1 10 . GLU . 862 1 11 . GLN . 862 1 12 . LEU . 862 1 13 . THR . 862 1 14 . GLU . 862 1 15 . GLU . 862 1 16 . GLN . 862 1 17 . LYS . 862 1 18 . ASN . 862 1 19 . GLU . 862 1 20 . PHE . 862 1 21 . LYS . 862 1 22 . ALA . 862 1 23 . ALA . 862 1 24 . PHE . 862 1 25 . ASP . 862 1 26 . ILE . 862 1 27 . PHE . 862 1 28 . VAL . 862 1 29 . LEU . 862 1 30 . GLY . 862 1 31 . ALA . 862 1 32 . GLU . 862 1 33 . ASP . 862 1 34 . GLY . 862 1 35 . CYS . 862 1 36 . ILE . 862 1 37 . SER . 862 1 38 . THR . 862 1 39 . LYS . 862 1 40 . GLU . 862 1 41 . LEU . 862 1 42 . GLY . 862 1 43 . LYS . 862 1 44 . VAL . 862 1 45 . MET . 862 1 46 . ARG . 862 1 47 . MET . 862 1 48 . LEU . 862 1 49 . GLY . 862 1 50 . GLN . 862 1 51 . ASN . 862 1 52 . PRO . 862 1 53 . THR . 862 1 54 . PRO . 862 1 55 . GLU . 862 1 56 . GLU . 862 1 57 . LEU . 862 1 58 . GLN . 862 1 59 . GLU . 862 1 60 . MET . 862 1 61 . ILE . 862 1 62 . ASP . 862 1 63 . GLU . 862 1 64 . VAL . 862 1 65 . ASP . 862 1 66 . GLU . 862 1 67 . ASP . 862 1 68 . GLY . 862 1 69 . SER . 862 1 70 . GLY . 862 1 71 . THR . 862 1 72 . VAL . 862 1 73 . ASP . 862 1 74 . PHE . 862 1 75 . ASP . 862 1 76 . GLU . 862 1 77 . PHE . 862 1 78 . LEU . 862 1 79 . VAL . 862 1 80 . MET . 862 1 81 . MET . 862 1 82 . VAL . 862 1 83 . ARG . 862 1 84 . CYS . 862 1 85 . MET . 862 1 86 . LYS . 862 1 87 . ASP . 862 1 88 . ASP . 862 1 89 . SER . 862 1 90 . LYS . 862 1 91 . GLY . 862 1 92 . LYS . 862 1 93 . SER . 862 1 94 . GLU . 862 1 95 . GLU . 862 1 96 . GLU . 862 1 97 . LEU . 862 1 98 . SER . 862 1 99 . ASP . 862 1 100 . LEU . 862 1 101 . PHE . 862 1 102 . ARG . 862 1 103 . MET . 862 1 104 . PHE . 862 1 105 . ASP . 862 1 106 . LYS . 862 1 107 . ASN . 862 1 108 . ALA . 862 1 109 . ASP . 862 1 110 . GLY . 862 1 111 . TYR . 862 1 112 . ILE . 862 1 113 . ASP . 862 1 114 . LEU . 862 1 115 . GLU . 862 1 116 . LEU . 862 1 117 . LYS . 862 1 118 . ILE . 862 1 119 . MET . 862 1 120 . LEU . 862 1 121 . GLN . 862 1 122 . ALA . 862 1 123 . THR . 862 1 124 . GLY . 862 1 125 . GLU . 862 1 126 . THR . 862 1 127 . ILE . 862 1 128 . THR . 862 1 129 . GLU . 862 1 130 . ASP . 862 1 131 . ASP . 862 1 132 . ILE . 862 1 133 . GLU . 862 1 134 . GLU . 862 1 135 . LEU . 862 1 136 . MET . 862 1 137 . LYS . 862 1 138 . ASP . 862 1 139 . GLY . 862 1 140 . ASP . 862 1 141 . LYS . 862 1 142 . ASN . 862 1 143 . ASN . 862 1 144 . ASP . 862 1 145 . GLY . 862 1 146 . ARG . 862 1 147 . ILE . 862 1 148 . ASP . 862 1 149 . TYR . 862 1 150 . ASP . 862 1 151 . GLU . 862 1 152 . PHE . 862 1 153 . LEU . 862 1 154 . GLU . 862 1 155 . PHE . 862 1 156 . MET . 862 1 157 . LYS . 862 1 158 . GLY . 862 1 159 . VAL . 862 1 160 . GLU . 862 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 . AME 1 1 862 1 . ASP 2 2 862 1 . ASP 3 3 862 1 . ILE 4 4 862 1 . TYR 5 5 862 1 . LYS 6 6 862 1 . ALA 7 7 862 1 . ALA 8 8 862 1 . VAL 9 9 862 1 . GLU 10 10 862 1 . GLN 11 11 862 1 . LEU 12 12 862 1 . THR 13 13 862 1 . GLU 14 14 862 1 . GLU 15 15 862 1 . GLN 16 16 862 1 . LYS 17 17 862 1 . ASN 18 18 862 1 . GLU 19 19 862 1 . PHE 20 20 862 1 . LYS 21 21 862 1 . ALA 22 22 862 1 . ALA 23 23 862 1 . PHE 24 24 862 1 . ASP 25 25 862 1 . ILE 26 26 862 1 . PHE 27 27 862 1 . VAL 28 28 862 1 . LEU 29 29 862 1 . GLY 30 30 862 1 . ALA 31 31 862 1 . GLU 32 32 862 1 . ASP 33 33 862 1 . GLY 34 34 862 1 . CYS 35 35 862 1 . ILE 36 36 862 1 . SER 37 37 862 1 . THR 38 38 862 1 . LYS 39 39 862 1 . GLU 40 40 862 1 . LEU 41 41 862 1 . GLY 42 42 862 1 . LYS 43 43 862 1 . VAL 44 44 862 1 . MET 45 45 862 1 . ARG 46 46 862 1 . MET 47 47 862 1 . LEU 48 48 862 1 . GLY 49 49 862 1 . GLN 50 50 862 1 . ASN 51 51 862 1 . PRO 52 52 862 1 . THR 53 53 862 1 . PRO 54 54 862 1 . GLU 55 55 862 1 . GLU 56 56 862 1 . LEU 57 57 862 1 . GLN 58 58 862 1 . GLU 59 59 862 1 . MET 60 60 862 1 . ILE 61 61 862 1 . ASP 62 62 862 1 . GLU 63 63 862 1 . VAL 64 64 862 1 . ASP 65 65 862 1 . GLU 66 66 862 1 . ASP 67 67 862 1 . GLY 68 68 862 1 . SER 69 69 862 1 . GLY 70 70 862 1 . THR 71 71 862 1 . VAL 72 72 862 1 . ASP 73 73 862 1 . PHE 74 74 862 1 . ASP 75 75 862 1 . GLU 76 76 862 1 . PHE 77 77 862 1 . LEU 78 78 862 1 . VAL 79 79 862 1 . MET 80 80 862 1 . MET 81 81 862 1 . VAL 82 82 862 1 . ARG 83 83 862 1 . CYS 84 84 862 1 . MET 85 85 862 1 . LYS 86 86 862 1 . ASP 87 87 862 1 . ASP 88 88 862 1 . SER 89 89 862 1 . LYS 90 90 862 1 . GLY 91 91 862 1 . LYS 92 92 862 1 . SER 93 93 862 1 . GLU 94 94 862 1 . GLU 95 95 862 1 . GLU 96 96 862 1 . LEU 97 97 862 1 . SER 98 98 862 1 . ASP 99 99 862 1 . LEU 100 100 862 1 . PHE 101 101 862 1 . ARG 102 102 862 1 . MET 103 103 862 1 . PHE 104 104 862 1 . ASP 105 105 862 1 . LYS 106 106 862 1 . ASN 107 107 862 1 . ALA 108 108 862 1 . ASP 109 109 862 1 . GLY 110 110 862 1 . TYR 111 111 862 1 . ILE 112 112 862 1 . ASP 113 113 862 1 . LEU 114 114 862 1 . GLU 115 115 862 1 . LEU 116 116 862 1 . LYS 117 117 862 1 . ILE 118 118 862 1 . MET 119 119 862 1 . LEU 120 120 862 1 . GLN 121 121 862 1 . ALA 122 122 862 1 . THR 123 123 862 1 . GLY 124 124 862 1 . GLU 125 125 862 1 . THR 126 126 862 1 . ILE 127 127 862 1 . THR 128 128 862 1 . GLU 129 129 862 1 . ASP 130 130 862 1 . ASP 131 131 862 1 . ILE 132 132 862 1 . GLU 133 133 862 1 . GLU 134 134 862 1 . LEU 135 135 862 1 . MET 136 136 862 1 . LYS 137 137 862 1 . ASP 138 138 862 1 . GLY 139 139 862 1 . ASP 140 140 862 1 . LYS 141 141 862 1 . ASN 142 142 862 1 . ASN 143 143 862 1 . ASP 144 144 862 1 . GLY 145 145 862 1 . ARG 146 146 862 1 . ILE 147 147 862 1 . ASP 148 148 862 1 . TYR 149 149 862 1 . ASP 150 150 862 1 . GLU 151 151 862 1 . PHE 152 152 862 1 . LEU 153 153 862 1 . GLU 154 154 862 1 . PHE 155 155 862 1 . MET 156 156 862 1 . LYS 157 157 862 1 . GLY 158 158 862 1 . VAL 159 159 862 1 . GLU 160 160 862 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 862 _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 $troponin_C . 9909 organism . 'Bos primigenius' cow . . Eukaryota Metazoa Bos primigenius . . . . heart . . . . . . . . . . . . . . . . 862 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 862 _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 $troponin_C . 'not available' . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 862 1 stop_ save_ ################################# # Polymer residues and ligands # ################################# save_chem_comp_AME _Chem_comp.Sf_category chem_comp _Chem_comp.Sf_framecode chem_comp_AME _Chem_comp.Entry_ID 862 _Chem_comp.ID AME _Chem_comp.Provenance PDB _Chem_comp.Name N-ACETYLMETHIONINE _Chem_comp.Type NON-POLYMER _Chem_comp.BMRB_code AME _Chem_comp.PDB_code AME _Chem_comp.Ambiguous_flag no _Chem_comp.Initial_date 2000-05-11 _Chem_comp.Modified_date 2011-12-14 _Chem_comp.Release_status REL _Chem_comp.Replaced_by . _Chem_comp.Replaces . _Chem_comp.One_letter_code . _Chem_comp.Three_letter_code AME _Chem_comp.Number_atoms_all 25 _Chem_comp.Number_atoms_nh 12 _Chem_comp.PubChem_code . _Chem_comp.Subcomponent_list . _Chem_comp.InChI_code InChI=1S/C7H13NO3S/c1-5(9)8-6(7(10)11)3-4-12-2/h6H,3-4H2,1-2H3,(H,8,9)(H,10,11)/t6-/m0/s1 _Chem_comp.Mon_nstd_flag . _Chem_comp.Mon_nstd_class . _Chem_comp.Mon_nstd_details . _Chem_comp.Mon_nstd_parent . _Chem_comp.Mon_nstd_parent_comp_ID . _Chem_comp.Std_deriv_one_letter_code . _Chem_comp.Std_deriv_three_letter_code . _Chem_comp.Std_deriv_BMRB_code . _Chem_comp.Std_deriv_PDB_code . _Chem_comp.Std_deriv_chem_comp_name . _Chem_comp.Synonyms . _Chem_comp.Formal_charge 0 _Chem_comp.Paramagnetic . _Chem_comp.Aromatic no _Chem_comp.Formula 'C7 H13 N O3 S' _Chem_comp.Formula_weight 191.248 _Chem_comp.Formula_mono_iso_wt_nat . _Chem_comp.Formula_mono_iso_wt_13C . _Chem_comp.Formula_mono_iso_wt_15N . _Chem_comp.Formula_mono_iso_wt_13C_15N . _Chem_comp.Image_file_name . _Chem_comp.Image_file_format . _Chem_comp.Topo_file_name . _Chem_comp.Topo_file_format . _Chem_comp.Struct_file_name . _Chem_comp.Struct_file_format . _Chem_comp.Stereochem_param_file_name . _Chem_comp.Stereochem_param_file_format . _Chem_comp.Model_details . _Chem_comp.Model_erf . _Chem_comp.Model_source . _Chem_comp.Model_coordinates_details . _Chem_comp.Model_coordinates_missing_flag no _Chem_comp.Ideal_coordinates_details . _Chem_comp.Ideal_coordinates_missing_flag no _Chem_comp.Model_coordinates_db_code 1SJA _Chem_comp.Processing_site EBI _Chem_comp.Vendor . _Chem_comp.Vendor_product_code . _Chem_comp.Details . _Chem_comp.DB_query_date . _Chem_comp.DB_last_query_revised_last_date . loop_ _Chem_comp_descriptor.Descriptor _Chem_comp_descriptor.Type _Chem_comp_descriptor.Program _Chem_comp_descriptor.Program_version _Chem_comp_descriptor.Entry_ID _Chem_comp_descriptor.Comp_ID CC(=O)NC(CCSC)C(=O)O SMILES 'OpenEye OEToolkits' 1.5.0 862 AME CC(=O)N[C@@H](CCSC)C(=O)O SMILES_CANONICAL 'OpenEye OEToolkits' 1.5.0 862 AME CSCC[C@H](NC(C)=O)C(O)=O SMILES_CANONICAL CACTVS 3.341 862 AME CSCC[CH](NC(C)=O)C(O)=O SMILES CACTVS 3.341 862 AME InChI=1S/C7H13NO3S/c1-5(9)8-6(7(10)11)3-4-12-2/h6H,3-4H2,1-2H3,(H,8,9)(H,10,11)/t6-/m0/s1 InChI InChI 1.03 862 AME O=C(NC(C(=O)O)CCSC)C SMILES ACDLabs 10.04 862 AME XUYPXLNMDZIRQH-LURJTMIESA-N InChIKey InChI 1.03 862 AME stop_ loop_ _Chem_comp_identifier.Identifier _Chem_comp_identifier.Type _Chem_comp_identifier.Program _Chem_comp_identifier.Program_version _Chem_comp_identifier.Entry_ID _Chem_comp_identifier.Comp_ID '(2S)-2-acetamido-4-methylsulfanyl-butanoic acid' 'SYSTEMATIC NAME' 'OpenEye OEToolkits' 1.5.0 862 AME N-acetyl-L-methionine 'SYSTEMATIC NAME' ACDLabs 10.04 862 AME stop_ loop_ _Chem_comp_atom.Atom_ID _Chem_comp_atom.BMRB_code _Chem_comp_atom.PDB_atom_ID _Chem_comp_atom.Alt_atom_ID _Chem_comp_atom.Auth_atom_ID _Chem_comp_atom.Type_symbol _Chem_comp_atom.Isotope_number _Chem_comp_atom.Chirality _Chem_comp_atom.Stereo_config _Chem_comp_atom.Charge _Chem_comp_atom.Partial_charge _Chem_comp_atom.Oxidation_number _Chem_comp_atom.Unpaired_electron_number _Chem_comp_atom.Align _Chem_comp_atom.Aromatic_flag _Chem_comp_atom.Leaving_atom_flag _Chem_comp_atom.Substruct_code _Chem_comp_atom.Ionizable _Chem_comp_atom.Drawing_2D_coord_x _Chem_comp_atom.Drawing_2D_coord_y _Chem_comp_atom.Model_Cartn_x _Chem_comp_atom.Model_Cartn_x_esd _Chem_comp_atom.Model_Cartn_y _Chem_comp_atom.Model_Cartn_y_esd _Chem_comp_atom.Model_Cartn_z _Chem_comp_atom.Model_Cartn_z_esd _Chem_comp_atom.Model_Cartn_x_ideal _Chem_comp_atom.Model_Cartn_y_ideal _Chem_comp_atom.Model_Cartn_z_ideal _Chem_comp_atom.PDBX_ordinal _Chem_comp_atom.Details _Chem_comp_atom.Entry_ID _Chem_comp_atom.Comp_ID CT2 CT2 CT2 CT2 . C . . N 0 . . . 1 no no . . . . 27.076 . 46.120 . 57.048 . -2.402 2.835 0.611 1 . 862 AME CT1 CT1 CT1 CT1 . C . . N 0 . . . 1 no no . . . . 25.688 . 45.572 . 57.270 . -1.987 1.579 -0.111 2 . 862 AME OT OT OT OT . O . . N 0 . . . 1 no no . . . . 24.978 . 45.268 . 56.223 . -2.480 1.306 -1.185 3 . 862 AME CB CB CB CB . C . . N 0 . . . 1 no no . . . . 23.260 . 43.949 . 59.549 . 0.741 -0.867 0.184 4 . 862 AME CG CG CG CG . C . . N 0 . . . 1 no no . . . . 23.043 . 42.994 . 58.383 . 1.744 0.202 -0.254 5 . 862 AME SD SD SD SD . S . . N 0 . . . 1 no no . . . . 23.323 . 41.240 . 58.772 . 3.411 -0.279 0.278 6 . 862 AME CE CE CE CE . C . . N 0 . . . 1 no no . . . . 23.317 . 40.535 . 57.114 . 4.362 1.129 -0.358 7 . 862 AME C C C C . C . . N 0 . . . 1 no no . . . . 23.545 . 46.185 . 60.212 . -1.633 -1.570 0.057 8 . 862 AME O O O O . O . . N 0 . . . 1 no no . . . . 22.617 . 45.822 . 61.055 . -2.566 -1.361 0.797 9 . 862 AME OXT OXT OXT OXT . O . . N 0 . . . 1 no yes . . . . 24.219 . 47.282 . 60.432 . -1.461 -2.789 -0.478 10 . 862 AME N N N N . N . . N 0 . . . 1 no no . . . . 25.189 . 45.384 . 58.629 . -1.068 0.759 0.437 11 . 862 AME CA CA CA CA . C . . S 0 . . . 1 no no . . . . 23.803 . 45.300 . 59.052 . -0.664 -0.462 -0.265 12 . 862 AME HT23 HT23 HT23 3HT2 . H . . N 0 . . . 0 no no . . . . 27.250 . 46.253 . 55.970 . -2.316 2.681 1.687 13 . 862 AME HT22 HT22 HT22 2HT2 . H . . N 0 . . . 0 no no . . . . 27.173 . 47.090 . 57.558 . -3.435 3.074 0.359 14 . 862 AME HT21 HT21 HT21 1HT2 . H . . N 0 . . . 0 no no . . . . 27.817 . 45.416 . 57.454 . -1.754 3.658 0.310 15 . 862 AME HB2 HB2 HB2 2HB . H . . N 0 . . . 1 no no . . . . 22.301 . 44.114 . 60.061 . 0.763 -0.962 1.269 16 . 862 AME HB1 HB1 HB1 1HB . H . . N 0 . . . 1 no no . . . . 23.993 . 43.505 . 60.239 . 1.006 -1.822 -0.270 17 . 862 AME HG2 HG2 HG2 2HG . H . . N 0 . . . 1 no no . . . . 22.000 . 43.101 . 58.052 . 1.723 0.297 -1.340 18 . 862 AME HG1 HG1 HG1 1HG . H . . N 0 . . . 1 no no . . . . 23.782 . 43.266 . 57.614 . 1.479 1.157 0.200 19 . 862 AME HE3 HE3 HE3 3HE . H . . N 0 . . . 1 no no . . . . 23.316 . 41.346 . 56.370 . 4.000 2.049 0.100 20 . 862 AME HE2 HE2 HE2 2HE . H . . N 0 . . . 1 no no . . . . 24.214 . 39.913 . 56.977 . 4.243 1.190 -1.439 21 . 862 AME HE1 HE1 HE1 1HE . H . . N 0 . . . 1 no no . . . . 22.417 . 39.916 . 56.982 . 5.417 0.994 -0.115 22 . 862 AME HO HO HO HO . H . . N 0 . . . 1 no no . . . . 23.912 . 47.687 . 61.235 . -2.083 -3.500 -0.271 23 . 862 AME HN1 HN1 HN1 1HN . H . . N 0 . . . 1 no no . . . . 25.879 . 45.304 . 59.349 . -0.673 0.978 1.296 24 . 862 AME HA HA HA HA . H . . N 0 . . . 1 no no . . . . 23.306 . 45.559 . 58.106 . -0.664 -0.280 -1.340 25 . 862 AME stop_ loop_ _Chem_comp_bond.ID _Chem_comp_bond.Type _Chem_comp_bond.Value_order _Chem_comp_bond.Atom_ID_1 _Chem_comp_bond.Atom_ID_2 _Chem_comp_bond.Aromatic_flag _Chem_comp_bond.Stereo_config _Chem_comp_bond.Ordinal _Chem_comp_bond.Details _Chem_comp_bond.Entry_ID _Chem_comp_bond.Comp_ID 1 . SING CT2 CT1 no N 1 . 862 AME 2 . SING CT2 HT23 no N 2 . 862 AME 3 . SING CT2 HT22 no N 3 . 862 AME 4 . SING CT2 HT21 no N 4 . 862 AME 5 . DOUB CT1 OT no N 5 . 862 AME 6 . SING CT1 N no N 6 . 862 AME 7 . SING CB CG no N 7 . 862 AME 8 . SING CB CA no N 8 . 862 AME 9 . SING CB HB2 no N 9 . 862 AME 10 . SING CB HB1 no N 10 . 862 AME 11 . SING CG SD no N 11 . 862 AME 12 . SING CG HG2 no N 12 . 862 AME 13 . SING CG HG1 no N 13 . 862 AME 14 . SING SD CE no N 14 . 862 AME 15 . SING CE HE3 no N 15 . 862 AME 16 . SING CE HE2 no N 16 . 862 AME 17 . SING CE HE1 no N 17 . 862 AME 18 . DOUB C O no N 18 . 862 AME 19 . SING C OXT no N 19 . 862 AME 20 . SING C CA no N 20 . 862 AME 21 . SING OXT HO no N 21 . 862 AME 22 . SING N CA no N 22 . 862 AME 23 . SING N HN1 no N 23 . 862 AME 24 . SING CA HA no N 24 . 862 AME stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Sample.Sf_category sample _Sample.Sf_framecode sample_one _Sample.Entry_ID 862 _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 862 _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 862 1 temperature 301 . K 862 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 862 _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 862 _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' . . 862 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 862 _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 . . . . . . . . . . . . . . . . 862 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 862 _Chem_shift_reference.ID 1 _Chem_shift_reference.Details . loop_ _Chem_shift_ref.Atom_type _Chem_shift_ref.Atom_isotope_number _Chem_shift_ref.Mol_common_name _Chem_shift_ref.Atom_group _Chem_shift_ref.Concentration_val _Chem_shift_ref.Concentration_units _Chem_shift_ref.Solvent _Chem_shift_ref.Rank _Chem_shift_ref.Chem_shift_units _Chem_shift_ref.Chem_shift_val _Chem_shift_ref.Ref_method _Chem_shift_ref.Ref_type _Chem_shift_ref.Indirect_shift_ratio _Chem_shift_ref.External_ref_loc _Chem_shift_ref.External_ref_sample_geometry _Chem_shift_ref.External_ref_axis _Chem_shift_ref.Indirect_shift_ratio_cit_ID _Chem_shift_ref.Indirect_shift_ratio_cit_label _Chem_shift_ref.Ref_correction_type _Chem_shift_ref.Correction_val _Chem_shift_ref.Correction_val_cit_ID _Chem_shift_ref.Correction_val_cit_label _Chem_shift_ref.Entry_ID _Chem_shift_ref.Chem_shift_reference_ID H . DSS CH3 . . . . ppm 0 . . . . . . 1 $entry_citation . . 1 $entry_citation 862 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 862 _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 . 862 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 5 5 TYR HD1 H 1 6.72 . . 1 . . . . . . . . 862 1 2 . 1 1 5 5 TYR HD2 H 1 6.72 . . 1 . . . . . . . . 862 1 3 . 1 1 5 5 TYR HE1 H 1 6.83 . . 1 . . . . . . . . 862 1 4 . 1 1 5 5 TYR HE2 H 1 6.83 . . 1 . . . . . . . . 862 1 5 . 1 1 111 111 TYR HD1 H 1 7.06 . . 1 . . . . . . . . 862 1 6 . 1 1 111 111 TYR HD2 H 1 7.06 . . 1 . . . . . . . . 862 1 7 . 1 1 111 111 TYR HE1 H 1 6.79 . . 1 . . . . . . . . 862 1 8 . 1 1 111 111 TYR HE2 H 1 6.79 . . 1 . . . . . . . . 862 1 9 . 1 1 149 149 TYR HD1 H 1 6.39 . . 1 . . . . . . . . 862 1 10 . 1 1 149 149 TYR HD2 H 1 6.39 . . 1 . . . . . . . . 862 1 11 . 1 1 149 149 TYR HE1 H 1 6.6 . . 1 . . . . . . . . 862 1 12 . 1 1 149 149 TYR HE2 H 1 6.6 . . 1 . . . . . . . . 862 1 stop_ save_