BMRB Entry 26578

Name: NMR Assignment of Homo sapiens cytochrome c in its oxidized state
Published: 2017-08-24

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR26578

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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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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):

Entity Sequences (FASTA):
cytochrome_c_peptide: GDVEKGKKIFIMKCSQCHTV EKGGKHKTGPNLHGLFGRKT GQAPGYSYTAANKNKGIIWG EDTLMEYLENPKKYIPGTKM IFVGIKKKEERADLIAYLKK ATNE

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
15N chemical shifts	102
1H chemical shifts	109

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity	1
2	HEME C	2

Entities:

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

1

GLY

ASP

VAL

GLU

LYS

GLY

LYS

ILE

PHE

2

ILE

MET

LYS

CYS

SER

GLN

CYS

HIS

THR

VAL

3

GLU

LYS

GLY

LYS

HIS

LYS

THR

GLY

PRO

4

ASN

LEU

HIS

GLY

LEU

PHE

GLY

ARG

LYS

THR

5

GLY

GLN

ALA

PRO

GLY

TYR

SER

TYR

THR

ALA

6

ALA

ASN

LYS

ASN

LYS

GLY

ILE

TRP

GLY

7

GLU

ASP

THR

LEU

MET

GLU

TYR

LEU

GLU

ASN

8

PRO

LYS

TYR

ILE

PRO

GLY

THR

LYS

MET

9

ILE

PHE

VAL

GLY

ILE

LYS

GLU

10

ARG

ALA

ASP

LEU

ILE

ALA

TYR

LEU

LYS

11

ALA

THR

ASN

GLU

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:

Name	Sample	Sample state	Sample conditions
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_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

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