data_243
#######################
# Entry information #
#######################
save_entry_information
_Saveframe_category entry_information
_Entry_title
;
Two-Dimensional 1H NMR Studies of Cytochrome c: Assignment of the N-Terminal
Helix
;
_BMRB_accession_number 243
_BMRB_flat_file_name bmr243.str
_Entry_type update
_Submission_date 1995-07-31
_Accession_date 1996-04-13
_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 Wand A. Joshua .
2 Englander S. Walter .
stop_
loop_
_Saveframe_category_type
_Saveframe_category_type_count
assigned_chemical_shifts 1
stop_
loop_
_Data_type
_Data_type_count
"1H chemical shifts" 47
stop_
loop_
_Revision_date
_Revision_keyword
_Revision_author
_Revision_detail
2010-06-10 revision BMRB 'Complete natural source information'
1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format'
1996-04-13 revision BMRB 'Link to the Protein Data Bank added'
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
;
Wand, A. Joshua, Englander, S. Walter,
"Two-Dimensional 1H NMR Studies of Cytochrome c: Assignment of the
N-Terminal Helix,"
Biochemistry 25, 1100-1106 (1986).
;
_Citation_title
;
Two-Dimensional 1H NMR Studies of Cytochrome c: Assignment of the N-Terminal
Helix
;
_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 Wand A. Joshua .
2 Englander S. Walter .
stop_
_Journal_abbreviation Biochemistry
_Journal_volume 25
_Journal_issue .
_Journal_CSD .
_Book_chapter_title .
_Book_volume .
_Book_series .
_Book_ISBN .
_Conference_state_province .
_Conference_abstract_number .
_Page_first 1100
_Page_last 1106
_Year 1986
_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'
_Molecular_mass .
_Mol_thiol_state .
_Details .
##############################
# Polymer residue sequence #
##############################
_Residue_count 104
_Mol_residue_sequence
;
GDVEKGKKIFVQKCAQCHTV
EKGGKHKTGPNLHGLFGRKT
GQAPGFTYTDANKNKGITWK
EETLMEYLENPKKYIPGTKM
IFAGIKKKTEREDLIAYLKK
ATNE
;
loop_
_Residue_seq_code
_Residue_label
1 GLY 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 CYS 15 ALA
16 GLN 17 CYS 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 2015-11-25
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 98.06 98.06 9.51e-65
BMRB 1107 "cytochrome c" 99.04 104 98.06 98.06 9.51e-65
BMRB 1108 "cytochrome c" 99.04 104 100.00 100.00 2.19e-67
BMRB 1109 "cytochrome c" 99.04 104 100.00 100.00 2.19e-67
BMRB 1110 "cytochrome c" 99.04 104 100.00 100.00 2.19e-67
BMRB 1111 "cytochrome c" 99.04 104 100.00 100.00 2.19e-67
BMRB 1112 "cytochrome c" 99.04 104 100.00 100.00 2.19e-67
BMRB 1113 "cytochrome c" 99.04 104 98.06 98.06 9.51e-65
BMRB 1114 "cytochrome c" 99.04 104 100.00 100.00 2.19e-67
BMRB 1116 "cytochrome c" 99.04 104 100.00 100.00 2.19e-67
BMRB 1170 "cytochrome c" 99.04 104 100.00 100.00 2.19e-67
BMRB 1171 "cytochrome c" 99.04 104 98.06 98.06 9.51e-65
BMRB 1404 "cytochrome c" 99.04 104 100.00 100.00 2.19e-67
BMRB 16759 cytochrome_c 100.00 104 100.00 100.00 4.35e-68
BMRB 17120 cytc 100.00 105 99.04 100.00 6.87e-68
BMRB 17340 cytc 100.00 104 100.00 100.00 4.35e-68
BMRB 1736 "cytochrome c" 99.04 104 98.06 98.06 9.51e-65
BMRB 1783 "cytochrome c" 99.04 104 98.06 98.06 9.51e-65
BMRB 17847 hCc 100.00 104 100.00 100.00 4.35e-68
BMRB 17848 hCc 100.00 104 100.00 100.00 4.35e-68
BMRB 1785 "cytochrome c" 99.04 104 98.06 98.06 9.51e-65
BMRB 1787 "cytochrome c" 99.04 104 98.06 98.06 9.51e-65
BMRB 1789 "cytochrome c" 99.04 104 98.06 98.06 9.51e-65
BMRB 216 "cytochrome c" 99.04 104 98.06 98.06 9.51e-65
BMRB 220 "cytochrome c" 99.04 104 98.06 98.06 9.51e-65
BMRB 224 "cytochrome c" 99.04 104 98.06 98.06 9.51e-65
BMRB 2366 "cytochrome c" 99.04 104 100.00 100.00 2.19e-67
BMRB 2367 "cytochrome c" 99.04 104 100.00 100.00 2.19e-67
BMRB 2368 "cytochrome c" 99.04 104 100.00 100.00 2.19e-67
BMRB 244 "cytochrome c" 100.00 104 100.00 100.00 4.35e-68
BMRB 25640 entity_1 100.00 105 99.04 99.04 8.72e-67
BMRB 274 "cytochrome c" 100.00 104 100.00 100.00 4.35e-68
BMRB 285 "cytochrome c" 99.04 104 100.00 100.00 2.19e-67
BMRB 286 "cytochrome c" 99.04 104 100.00 100.00 2.19e-67
BMRB 316 "cytochrome c" 99.04 104 100.00 100.00 2.19e-67
BMRB 317 "cytochrome c" 99.04 104 100.00 100.00 2.19e-67
BMRB 336 "cytochrome c" 99.04 104 98.06 98.06 9.51e-65
BMRB 4189 "cytochrome c" 100.00 104 100.00 100.00 4.35e-68
BMRB 436 "cytochrome c" 99.04 104 98.06 98.06 9.51e-65
BMRB 437 "cytochrome c" 99.04 104 98.06 98.06 9.51e-65
BMRB 438 "cytochrome c" 99.04 104 98.06 98.06 9.51e-65
BMRB 439 "cytochrome c" 99.04 104 98.06 98.06 9.51e-65
PDB 1AKK "Solution Structure Of Oxidized Horse Heart Cytochrome C, Nmr, Minimized Average Structure" 100.00 104 100.00 100.00 4.35e-68
PDB 1CRC "Cytochrome C At Low Ionic Strength" 100.00 105 100.00 100.00 4.49e-68
PDB 1FI7 "Solution Structure Of The Imidazole Complex Of Cytochrome C" 100.00 104 100.00 100.00 4.35e-68
PDB 1FI9 "Solution Structure Of The Imidazole Complex Of Cytochrome C" 100.00 104 100.00 100.00 4.35e-68
PDB 1GIW "Solution Structure Of Reduced Horse Heart Cytochrome C, Nmr, Minimized Average Structure" 99.04 104 100.00 100.00 2.19e-67
PDB 1HRC "High-Resolution Three-Dimensional Structure Of Horse Heart Cytochrome C" 100.00 105 100.00 100.00 4.49e-68
PDB 1I5T "Solution Structure Of Cyanoferricytochrome C" 100.00 104 100.00 100.00 4.35e-68
PDB 1LC1 "Solution Structure Of Reduced Horse Heart Cytochrome C In 30% Acetonitrile Solution, Nmr Minimized Average Structure" 100.00 104 100.00 100.00 4.35e-68
PDB 1LC2 "Solution Structure Of Reduced Horse Heart Cytochrome C In 30% Acetonitrile Solution, Nmr 30 Structures" 100.00 104 100.00 100.00 4.35e-68
PDB 1M60 "Solution Structure Of Zinc-Substituted Cytochrome C" 100.00 104 100.00 100.00 4.35e-68
PDB 1OCD "Cytochrome C (Oxidized) From Equus Caballus, Nmr, Minimized Average Structure" 100.00 104 100.00 100.00 4.35e-68
PDB 1U75 "Electron Transfer Complex Between Horse Heart Cytochrome C And Zinc- Porphyrin Substituted Cytochrome C Peroxidase" 100.00 104 100.00 100.00 4.35e-68
PDB 1WEJ "Igg1 Fab Fragment (Of E8 Antibody) Complexed With Horse Cytochrome C At 1.8 A Resolution" 100.00 105 100.00 100.00 4.49e-68
PDB 2B4Z "Crystal Structure Of Cytochrome C From Bovine Heart At 1.5 A Resolution." 100.00 104 97.12 98.08 8.45e-66
PDB 2FRC "Cytochrome C (Reduced) From Equus Caballus, Nmr, Minimized Average Structure" 100.00 104 100.00 100.00 4.35e-68
PDB 2GIW "Solution Structure Of Reduced Horse Heart Cytochrome C, Nmr, 40 Structures" 100.00 104 100.00 100.00 4.35e-68
PDB 2PCB "Crystal Structure Of A Complex Between Electron Transfer Partners, Cytochrome C Peroxidase And Cytochrome C" 100.00 104 100.00 100.00 4.35e-68
PDB 2YBB "Fitted Model For Bovine Mitochondrial Supercomplex I1iii2iv1 By Single Particle Cryo-Em (Emd-1876)" 100.00 104 97.12 98.08 8.45e-66
PDB 3J2T "An Improved Model Of The Human Apoptosome" 100.00 104 97.12 98.08 8.45e-66
PDB 3NBS "Crystal Structure Of Dimeric Cytochrome C From Horse Heart" 100.00 104 100.00 100.00 4.35e-68
PDB 3NBT "Crystal Structure Of Trimeric Cytochrome C From Horse Heart" 100.00 104 100.00 100.00 4.35e-68
PDB 3O1Y "Electron Transfer Complexes: Experimental Mapping Of The Redox- Dependent Cytochrome C Electrostatic Surface" 100.00 105 100.00 100.00 4.49e-68
PDB 3O20 "Electron Transfer Complexes:experimental Mapping Of The Redox- Dependent Cytochrome C Electrostatic Surface" 100.00 105 100.00 100.00 4.49e-68
PDB 3WC8 "Dimeric Horse Cytochrome C Obtained By Refolding With Desalting Method" 100.00 104 100.00 100.00 4.35e-68
PDB 3WUI "Dimeric Horse Cytochrome C Formed By Refolding From Molten Globule State" 100.00 104 100.00 100.00 4.35e-68
PDB 4NFG "K13r Mutant Of Horse Cytochrome C And Yeast Cytochrome C Peroxidase Complex" 100.00 104 97.12 100.00 4.02e-66
PDB 4RSZ "The X-ray Structure Of The Primary Adduct Formed In The Reaction Between Cisplatin And Cytochrome C" 100.00 104 100.00 100.00 4.35e-68
GB AAB33495 "apocytochrome c [horses, heart, Peptide, 104 aa]" 100.00 104 98.08 98.08 4.54e-66
GB AAI05398 "Cytochrome c, somatic [Bos taurus]" 100.00 105 97.12 98.08 6.93e-66
GB AAX77008 "cytochrome c-like protein [Sus scrofa]" 100.00 105 97.12 98.08 6.93e-66
GB ABA06541 "mitochondrial cytochrome c [Bubalus bubalis]" 100.00 104 97.12 98.08 8.45e-66
GB AEB61027 "cytochrome c-like protein, partial [Equus caballus]" 100.00 127 100.00 100.00 1.28e-68
PRF 610169A "cytochrome c" 100.00 104 100.00 100.00 4.35e-68
PRF 711086A "cytochrome c" 100.00 104 97.12 100.00 2.47e-67
REF NP_001039526 "cytochrome c [Bos taurus]" 100.00 105 97.12 98.08 6.93e-66
REF NP_001123442 "cytochrome c [Sus scrofa]" 100.00 105 97.12 98.08 6.93e-66
REF NP_001157486 "cytochrome c [Equus caballus]" 100.00 105 99.04 100.00 6.87e-68
REF XP_004007999 "PREDICTED: cytochrome c [Ovis aries]" 100.00 105 97.12 98.08 6.93e-66
REF XP_004418964 "PREDICTED: cytochrome c-like [Ceratotherium simum simum]" 100.00 105 98.08 99.04 2.60e-67
SP P00004 "RecName: Full=Cytochrome c" 100.00 105 100.00 100.00 3.45e-68
SP P62894 "RecName: Full=Cytochrome c" 100.00 105 97.12 98.08 6.93e-66
SP P62895 "RecName: Full=Cytochrome c" 100.00 105 97.12 98.08 6.93e-66
SP P62896 "RecName: Full=Cytochrome c" 100.00 105 97.12 98.08 6.93e-66
SP P68096 "RecName: Full=Cytochrome c" 100.00 105 99.04 100.00 6.87e-68
TPG DAA30512 "TPA: cytochrome c [Bos taurus]" 100.00 105 97.12 98.08 6.93e-66
stop_
save_
####################
# Natural source #
####################
save_natural_source
_Saveframe_category natural_source
loop_
_Mol_label
_Organism_name_common
_NCBI_taxonomy_ID
_Superkingdom
_Kingdom
_Genus
_Species
_Strain
_Tissue
$cytochrome_c 'domestic horse' 9796 Eukaryota Metazoa Equus caballus generic heart
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_list
_Saveframe_category NMR_spectrometer
_Manufacturer unknown
_Model unknown
_Field_strength 0
_Details 'spectrometer information not available'
save_
#############################
# NMR applied experiments #
#############################
save__1
_Saveframe_category NMR_applied_experiment
_Sample_label $sample_one
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 5.7 . na
temperature 313 . 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
DSS H . . 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_
_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 . 5 LYS H H 8.09 . 1
2 . 5 LYS HA H 4.01 . 1
3 . 5 LYS HB2 H 1.86 . 1
4 . 5 LYS HB3 H 1.86 . 1
5 . 6 GLY H H 8.84 . 1
6 . 6 GLY HA2 H 3.56 . 2
7 . 6 GLY HA3 H 4.2 . 2
8 . 7 LYS H H 8.06 . 1
9 . 7 LYS HA H 3.58 . 1
10 . 7 LYS HB2 H 1.9 . 1
11 . 7 LYS HB3 H 1.9 . 1
12 . 8 LYS H H 7.03 . 1
13 . 8 LYS HA H 3.96 . 1
14 . 8 LYS HB2 H 1.98 . 1
15 . 8 LYS HB3 H 1.98 . 1
16 . 9 ILE H H 7.77 . 1
17 . 9 ILE HA H 3.88 . 1
18 . 9 ILE HB H 2.18 . 1
19 . 9 ILE HG12 H 1.29 . 1
20 . 9 ILE HG13 H 1.29 . 1
21 . 9 ILE HG2 H 1.13 . 1
22 . 10 PHE H H 8.68 . 1
23 . 10 PHE HA H 4.07 . 1
24 . 10 PHE HB2 H 3.14 . 2
25 . 10 PHE HB3 H 3.02 . 2
26 . 11 VAL H H 8.78 . 1
27 . 11 VAL HA H 3.6 . 1
28 . 11 VAL HB H 2.21 . 1
29 . 11 VAL HG1 H .98 . 2
30 . 11 VAL HG2 H 1.16 . 2
31 . 12 GLN H H 7.95 . 1
32 . 12 GLN HA H 4.25 . 1
33 . 12 GLN HB2 H 2.33 . 1
34 . 12 GLN HB3 H 2.33 . 1
35 . 12 GLN HG2 H 2.71 . 1
36 . 12 GLN HG3 H 2.71 . 1
37 . 13 LYS H H 8.97 . 1
38 . 13 LYS HA H 5.07 . 1
39 . 13 LYS HB2 H 2.11 . 1
40 . 13 LYS HB3 H 2.11 . 1
41 . 14 CYS H H 8.35 . 1
42 . 14 CYS HA H 5.35 . 1
43 . 14 CYS HB2 H 1.15 . 1
44 . 14 CYS HB3 H 1.15 . 1
45 . 15 ALA H H 7.42 . 1
46 . 15 ALA HA H 3.94 . 1
47 . 15 ALA HB H 1.41 . 1
stop_
save_