data_1113 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Studies of Individual Carbon Sites of Proteins in Solution by Natural Abundance Carbon 13 Nuclear Magnetic Resonance Spectroscopy ; _BMRB_accession_number 1113 _BMRB_flat_file_name bmr1113.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-04-12 _Entry_origination BMRB _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Oldfield Eric . . 2 Norton Raymond S. . 3 Allerhand Adam . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "13C chemical shifts" 5 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-14 revision BMRB 'Complete natural source information' 2008-09-30 revision BMRB 'Updating non-standard residue' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-04-12 revision BMRB 'Error corrected in abrreviations given to non-polymers' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; Oldfield, Eric, Norton, Raymond S., Allerhand, Adam, "Studies of Individual Carbon Sites of Proteins in Solution by Natural Abundance Carbon 13 Nuclear Magnetic Resonance Spectroscopy," J. Biol. Chem. 250 (16), 6381-6402 (1975). ; _Citation_title ; Studies of Individual Carbon Sites of Proteins in Solution by Natural Abundance Carbon 13 Nuclear Magnetic Resonance Spectroscopy ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Oldfield Eric . . 2 Norton Raymond S. . 3 Allerhand Adam . . stop_ _Journal_abbreviation 'J. Biol. Chem.' _Journal_volume 250 _Journal_issue 16 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 6381 _Page_last 6402 _Year 1975 _Details . save_ ################################## # Molecular system description # ################################## save_system_cytochrome_c _Saveframe_category molecular_system _Mol_system_name 'cytochrome c' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'cytochrome c' $cytochrome_c stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_cytochrome_c _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'cytochrome c' _Name_variant 1Ac_G-104 _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 104 _Mol_residue_sequence ; XDVEKGKKIFVQKXAQXHTV EKGGKHKTGPNLHGLFGRKT GQAPGFTYTDANKNKGITWK EETLMEYLENPKKYIPGTKM IFAGIKKKTEREDLIAYLKK ATNE ; loop_ _Residue_seq_code _Residue_label 1 AAC 2 ASP 3 VAL 4 GLU 5 LYS 6 GLY 7 LYS 8 LYS 9 ILE 10 PHE 11 VAL 12 GLN 13 LYS 14 C_heme_c 15 ALA 16 GLN 17 C_heme_c 18 HIS 19 THR 20 VAL 21 GLU 22 LYS 23 GLY 24 GLY 25 LYS 26 HIS 27 LYS 28 THR 29 GLY 30 PRO 31 ASN 32 LEU 33 HIS 34 GLY 35 LEU 36 PHE 37 GLY 38 ARG 39 LYS 40 THR 41 GLY 42 GLN 43 ALA 44 PRO 45 GLY 46 PHE 47 THR 48 TYR 49 THR 50 ASP 51 ALA 52 ASN 53 LYS 54 ASN 55 LYS 56 GLY 57 ILE 58 THR 59 TRP 60 LYS 61 GLU 62 GLU 63 THR 64 LEU 65 MET 66 GLU 67 TYR 68 LEU 69 GLU 70 ASN 71 PRO 72 LYS 73 LYS 74 TYR 75 ILE 76 PRO 77 GLY 78 THR 79 LYS 80 MET 81 ILE 82 PHE 83 ALA 84 GLY 85 ILE 86 LYS 87 LYS 88 LYS 89 THR 90 GLU 91 ARG 92 GLU 93 ASP 94 LEU 95 ILE 96 ALA 97 TYR 98 LEU 99 LYS 100 LYS 101 ALA 102 THR 103 ASN 104 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-11-05 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 1058 "cytochrome c" 99.04 104 100.00 100.00 1.46e-64 BMRB 1107 "cytochrome c" 99.04 104 100.00 100.00 1.46e-64 BMRB 1108 "cytochrome c" 99.04 104 98.06 98.06 8.49e-65 BMRB 1109 "cytochrome c" 99.04 104 98.06 98.06 8.49e-65 BMRB 1110 "cytochrome c" 99.04 104 98.06 98.06 8.49e-65 BMRB 1111 "cytochrome c" 99.04 104 98.06 98.06 8.49e-65 BMRB 1112 "cytochrome c" 99.04 104 98.06 98.06 8.49e-65 BMRB 1114 "cytochrome c" 99.04 104 98.06 98.06 8.49e-65 BMRB 1116 "cytochrome c" 99.04 104 98.06 98.06 8.49e-65 BMRB 1170 "cytochrome c" 99.04 104 98.06 98.06 8.49e-65 BMRB 1171 "cytochrome c" 99.04 104 100.00 100.00 1.46e-64 BMRB 1404 "cytochrome c" 99.04 104 98.06 98.06 8.49e-65 BMRB 16759 cytochrome_c 99.04 104 98.06 98.06 9.26e-65 BMRB 17120 cytc 99.04 105 97.09 98.06 1.70e-64 BMRB 17340 cytc 99.04 104 98.06 98.06 9.26e-65 BMRB 1736 "cytochrome c" 99.04 104 100.00 100.00 1.46e-64 BMRB 1783 "cytochrome c" 99.04 104 100.00 100.00 1.46e-64 BMRB 17847 hCc 99.04 104 98.06 98.06 9.26e-65 BMRB 17848 hCc 99.04 104 98.06 98.06 9.26e-65 BMRB 1785 "cytochrome c" 99.04 104 100.00 100.00 1.46e-64 BMRB 1787 "cytochrome c" 99.04 104 100.00 100.00 1.46e-64 BMRB 1789 "cytochrome c" 99.04 104 100.00 100.00 1.46e-64 BMRB 216 "cytochrome c" 99.04 104 100.00 100.00 1.46e-64 BMRB 220 "cytochrome c" 99.04 104 100.00 100.00 1.46e-64 BMRB 224 "cytochrome c" 99.04 104 100.00 100.00 1.46e-64 BMRB 2366 "cytochrome c" 99.04 104 98.06 98.06 8.49e-65 BMRB 2367 "cytochrome c" 99.04 104 98.06 98.06 8.49e-65 BMRB 2368 "cytochrome c" 99.04 104 98.06 98.06 8.49e-65 BMRB 243 "cytochrome c" 99.04 104 98.06 98.06 9.26e-65 BMRB 244 "cytochrome c" 99.04 104 98.06 98.06 9.26e-65 BMRB 25640 entity_1 99.04 105 97.09 97.09 1.72e-63 BMRB 274 "cytochrome c" 99.04 104 98.06 98.06 9.26e-65 BMRB 285 "cytochrome c" 99.04 104 98.06 98.06 8.49e-65 BMRB 286 "cytochrome c" 99.04 104 98.06 98.06 8.49e-65 BMRB 316 "cytochrome c" 99.04 104 98.06 98.06 8.49e-65 BMRB 317 "cytochrome c" 99.04 104 98.06 98.06 8.49e-65 BMRB 336 "cytochrome c" 99.04 104 100.00 100.00 1.46e-64 BMRB 4189 "cytochrome c" 99.04 104 98.06 98.06 9.26e-65 BMRB 436 "cytochrome c" 99.04 104 100.00 100.00 1.46e-64 BMRB 437 "cytochrome c" 99.04 104 100.00 100.00 1.46e-64 BMRB 438 "cytochrome c" 99.04 104 100.00 100.00 1.46e-64 BMRB 439 "cytochrome c" 99.04 104 100.00 100.00 1.46e-64 PDB 1AKK "Solution Structure Of Oxidized Horse Heart Cytochrome C, Nmr, Minimized Average Structure" 99.04 104 98.06 98.06 9.26e-65 PDB 1CRC "Cytochrome C At Low Ionic Strength" 99.04 105 98.06 98.06 9.55e-65 PDB 1FI7 "Solution Structure Of The Imidazole Complex Of Cytochrome C" 99.04 104 98.06 98.06 9.26e-65 PDB 1FI9 "Solution Structure Of The Imidazole Complex Of Cytochrome C" 99.04 104 98.06 98.06 9.26e-65 PDB 1GIW "Solution Structure Of Reduced Horse Heart Cytochrome C, Nmr, Minimized Average Structure" 99.04 104 98.06 98.06 8.49e-65 PDB 1HRC "High-Resolution Three-Dimensional Structure Of Horse Heart Cytochrome C" 99.04 105 98.06 98.06 9.55e-65 PDB 1I5T "Solution Structure Of Cyanoferricytochrome C" 99.04 104 98.06 98.06 9.26e-65 PDB 1LC1 "Solution Structure Of Reduced Horse Heart Cytochrome C In 30% Acetonitrile Solution, Nmr Minimized Average Structure" 99.04 104 98.06 98.06 9.26e-65 PDB 1LC2 "Solution Structure Of Reduced Horse Heart Cytochrome C In 30% Acetonitrile Solution, Nmr 30 Structures" 99.04 104 98.06 98.06 9.26e-65 PDB 1M60 "Solution Structure Of Zinc-Substituted Cytochrome C" 99.04 104 98.06 98.06 9.26e-65 PDB 1OCD "Cytochrome C (Oxidized) From Equus Caballus, Nmr, Minimized Average Structure" 99.04 104 98.06 98.06 9.26e-65 PDB 1U75 "Electron Transfer Complex Between Horse Heart Cytochrome C And Zinc- Porphyrin Substituted Cytochrome C Peroxidase" 99.04 104 98.06 98.06 9.26e-65 PDB 1WEJ "Igg1 Fab Fragment (Of E8 Antibody) Complexed With Horse Cytochrome C At 1.8 A Resolution" 99.04 105 98.06 98.06 9.55e-65 PDB 2FRC "Cytochrome C (Reduced) From Equus Caballus, Nmr, Minimized Average Structure" 99.04 104 98.06 98.06 9.26e-65 PDB 2GIW "Solution Structure Of Reduced Horse Heart Cytochrome C, Nmr, 40 Structures" 99.04 104 98.06 98.06 9.26e-65 PDB 2PCB "Crystal Structure Of A Complex Between Electron Transfer Partners, Cytochrome C Peroxidase And Cytochrome C" 99.04 104 98.06 98.06 9.26e-65 PDB 3NBS "Crystal Structure Of Dimeric Cytochrome C From Horse Heart" 99.04 104 98.06 98.06 9.26e-65 PDB 3NBT "Crystal Structure Of Trimeric Cytochrome C From Horse Heart" 99.04 104 98.06 98.06 9.26e-65 PDB 3O1Y "Electron Transfer Complexes: Experimental Mapping Of The Redox- Dependent Cytochrome C Electrostatic Surface" 99.04 105 98.06 98.06 9.55e-65 PDB 3O20 "Electron Transfer Complexes:experimental Mapping Of The Redox- Dependent Cytochrome C Electrostatic Surface" 99.04 105 98.06 98.06 9.55e-65 PDB 3WC8 "Dimeric Horse Cytochrome C Obtained By Refolding With Desalting Method" 99.04 104 98.06 98.06 9.26e-65 PDB 3WUI "Dimeric Horse Cytochrome C Formed By Refolding From Molten Globule State" 99.04 104 98.06 98.06 9.26e-65 PDB 4RSZ "The X-ray Structure Of The Primary Adduct Formed In The Reaction Between Cisplatin And Cytochrome C" 99.04 104 98.06 98.06 9.26e-65 GB AEB61027 "cytochrome c-like protein, partial [Equus caballus]" 99.04 127 98.06 98.06 2.36e-65 PRF 610169A "cytochrome c" 99.04 104 98.06 98.06 9.26e-65 REF NP_001157486 "cytochrome c [Equus caballus]" 99.04 105 97.09 98.06 1.70e-64 REF XP_005609231 "PREDICTED: cytochrome c isoform X1 [Equus caballus]" 99.04 105 97.09 98.06 1.70e-64 REF XP_008535094 "PREDICTED: cytochrome c [Equus przewalskii]" 99.04 105 98.06 98.06 8.85e-65 SP P00004 "RecName: Full=Cytochrome c" 99.04 105 98.06 98.06 8.85e-65 SP P68096 "RecName: Full=Cytochrome c" 99.04 105 97.09 98.06 1.70e-64 SP P68097 "RecName: Full=Cytochrome c" 99.04 105 97.09 98.06 1.70e-64 stop_ save_ ###################### # Polymer residues # ###################### save_chem_comp_AAC _Saveframe_category polymer_residue _Mol_type NON-POLYMER _Name_common 'ACETYLAMINO-ACETIC ACID' _BMRB_code AAC _PDB_code AAC _Standard_residue_derivative . _Molecular_mass 117.103 _Mol_paramagnetic . _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons C1 C1 C . 0 . ? C2 C2 C . 0 . ? C3 C3 C . 0 . ? C4 C4 C . 0 . ? N1 N1 N . 0 . ? O1 O1 O . 0 . ? O2 O2 O . 0 . ? O3 O3 O . 0 . ? HC21 HC21 H . 0 . ? HC22 HC22 H . 0 . ? HC41 HC41 H . 0 . ? HC42 HC42 H . 0 . ? HC43 HC43 H . 0 . ? HN1 HN1 H . 0 . ? HO1 HO1 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING C1 C2 ? ? SING C1 O1 ? ? DOUB C1 O2 ? ? SING C2 N1 ? ? SING C2 HC21 ? ? SING C2 HC22 ? ? SING C3 C4 ? ? SING C3 N1 ? ? DOUB C3 O3 ? ? SING C4 HC41 ? ? SING C4 HC42 ? ? SING C4 HC43 ? ? SING N1 HN1 ? ? SING O1 HO1 ? ? stop_ save_ save_C_heme_c _Saveframe_category polymer_residue _Mol_type non-polymer _Name_common 'L-cysteine-Sg-heme c' _Abbreviation_common C_heme_c _BMRB_code . _PDB_code . _Standard_residue_derivative . loop_ _Mol_label _Residue_seq_code $cytochrome_c 14 $cytochrome_c 17 stop_ _Molecular_mass . _Mol_paramagnetic . _Details . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $cytochrome_c Horse 9796 Eukaryota Metazoa Equus caballus stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $cytochrome_c 'not available' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save_unknown_1 _Saveframe_category NMR_applied_experiment _Experiment_name unknown _Sample_label $sample_one save_ save_NMR_spec_expt_dummy _Saveframe_category NMR_applied_experiment _Experiment_name unknown _BMRB_pulse_sequence_accession_number . _Details 'experiment information not available' save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.7 . na temperature 309 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio_citation_label _Correction_value_citation_label TMS C . . ppm 0 . . . . . $entry_citation $entry_citation 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 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label unknown stop_ loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_condition_set_one _Chem_shift_reference_set_label $chem_shift_reference_par_set_one _Mol_system_component_name 'cytochrome c' _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 . 18 HIS CG C 123.83 . 1 2 . 59 TRP CG C 109.51 . 1 3 . 59 TRP CD2 C 127.07 . 1 4 . 59 TRP CE2 C 137.2 . 1 5 . 67 TYR CZ C 160.45 . 1 stop_ save_