BMRB Entry 25418

Name: Human Cytochrome c WT ferric form (oxidized)
Published: 2015-10-07

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR25418

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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:

Human Cytochrome c WT ferric form (oxidized)

Deposition date:

2015-01-07

Original release date:

2015-10-07

Authors:

Karsisiotis, Andreas Ioannis; Worrall, Jonathan; Deacon, Oliver

Citation:

Citation: Karsisiotis, Andreas Ioannis; Deacon, Oliver; Rajagopal, Badri; Macdonald, Colin; Blumenschein, Tharin; Moore, Geoffrey; Worrall, Jonathan. "Backbone resonance assignments of ferric human cytochrome c and the pro-apoptotic G41S mutant in the ferric and ferrous states" Biomol. NMR Assign. 9, 415-419 (2015).
PubMed: 26123826

Assembly members:

Assembly members:
hCyt_c_WT, 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: pUC19Amp

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	193
15N chemical shifts	99
1H chemical shifts	101

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	human Cyt c	1
2	human Cyt c	2

Entities:

Entity 1, human Cyt c 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, human Cyt c - C34 H34 Fe N4 O4 - 618.503 Da.

1

HEC

Samples:

HCC_WT_293K: sodium phosphate 20 mM; sodium chloride 50 mM; hCyt c WT, [U-100% 15N], 1 mM; HEME C 1 mM; H2O 90%; D2O, U-2H, 10%

293K: ionic strength: 70 mM; pH: 6.8; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	HCC_WT_293K	isotropic	293K
3D HNCACB	HCC_WT_293K	isotropic	293K
3D CBCA(CO)NH	HCC_WT_293K	isotropic	293K

Software:

TOPSPIN, Bruker Biospin - collection

SPARKY, Goddard - chemical shift assignment, data analysis, processing

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

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

Analysis, CCPN - chemical shift assignment, data analysis, peak picking

NMR spectrometers:

Bruker UltraShield Plus 800 MHz

BMRB	25420 25422
PDB	1J3S 3NWV 3ZCF 3ZOO
DBJ	BAG34778 BAH24118
EMBL	CAD28485 CAG46972 CAH89483 CAL38091 CAL38301
GB	AAA35732 AAH05299 AAH08475 AAH08477 AAH09578
PRF	630485A
REF	NP_001065289 NP_001124639 NP_061820 XP_001110791 XP_001140708
SP	P00002 P99998 P99999 Q52V08 Q5RFH4
AlphaFold	P00002 P99998 P99999 Q52V08 Q5RFH4