BMRB Entry 26578

Title:
NMR Assignment of Homo sapiens cytochrome c in its oxidized state
Deposition date:
2015-05-18
Original release date:
2017-08-24
Authors:
Moreno-Beltran, Blas; Diaz-Quintana, Antonio; De la Rosa, Miguel; Diaz-Moreno, Irene
Citation:

Citation: Gonzalez-Arzola, Katiuska; Diaz-Moreno, Irene; Cano-Gonzalez, Ana; Diaz-Quintana, Antonio; Velazquez-Campoy, Adrian; Moreno-Beltran, Blas; Lopez-Rivas, Abelardo; De la Rosa, Miguel. "Structural basis for inhibition of the histone chaperone activity of SET/TAF-Ibeta by cytochrome c"  Proc. Natl. Acad. Sci. U.S.A. 112, 9908-9913 (2015).
PubMed: 26216969

Assembly members:

Assembly members:
cytochrome_c_peptide, polymer, 104 residues, Formula weight is not available
HEME C, non-polymer, 618.503 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pBTR1

Entity Sequences (FASTA):

Data sets:
Data typeCount
15N chemical shifts102
1H chemical shifts109

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1
2HEME C2

Entities:

Entity 1, entity 104 residues - Formula weight is not available

1   GLYASPVALGLULYSGLYLYSLYSILEPHE
2   ILEMETLYSCYSSERGLNCYSHISTHRVAL
3   GLULYSGLYGLYLYSHISLYSTHRGLYPRO
4   ASNLEUHISGLYLEUPHEGLYARGLYSTHR
5   GLYGLNALAPROGLYTYRSERTYRTHRALA
6   ALAASNLYSASNLYSGLYILEILETRPGLY
7   GLUASPTHRLEUMETGLUTYRLEUGLUASN
8   PROLYSLYSTYRILEPROGLYTHRLYSMET
9   ILEPHEVALGLYILELYSLYSLYSGLUGLU
10   ARGALAASPLEUILEALATYRLEULYSLYS
11   ALATHRASNGLU

Entity 2, HEME C - C34 H34 Fe N4 O4 - 618.503 Da.

1   HEC

Samples:

sample_1: entity, [U-100% 15N], 0.900 ± 0.001 mM; H2O 90%; D2O 10%; phosphate buffer 5 mM

sample_conditions_1: ionic strength: 0.005 M; pH: 6.3; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1

Software:

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

TOPSPIN, Bruker Biospin - collection, processing

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMR spectrometers:

  • Bruker Avance 750 MHz

Related Database Links:

EMBL BT007646.1
GB M22877.1
UNP P99999
AlphaFold Q96BV4

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks