BMRB Entry 30556

Name: Solution structure of human Coa6
Published: 2019-11-12

Click here to enlarge.

PDB ID: 6nl3
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30556
MolProbity Validation Chart

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

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

Select model:

I am color blind

Download raw data. Direct link to this display. Help

Title:

Solution structure of human Coa6

Deposition date:

2019-01-07

Original release date:

2019-11-12

Authors:

Naik, M.; Soma, S.; Gohil, V.

Citation:

Citation: Soma, Shivatheja; Morgada, Marcos; Naik, Mandar; Boulet, Aren; Roesler, Anna; Dziuba, Nathaniel; Ghosh, Alok; Yu, Qinhong; Lindahl, Paul; Ames, James; Leary, Scot; Vila, Alejandro; Gohil, Vishal. "COA6 Is Structurally Tuned to Function as a Thiol-Disulfide Oxidoreductase in Copper Delivery to Mitochondrial Cytochrome c Oxidase" Cell Rep. 29, 4114-44126 (2019).
PubMed: 31851937

Assembly members:

Assembly members:
entity_1, polymer, 81 residues, 9586.769 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 BL21(DE3) Vector: pGEX-4T1

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: GSMAAPSMKERQVCWGARDE YWKCLDENLEDASQCKKLRS SFESSCPQQWIKYFDKRRDY LKFKEKFEAGQFEPSETTAK S

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	275
15N chemical shifts	78
1H chemical shifts	441

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 81 residues - 9586.769 Da.

1

GLY

SER

MET

ALA

PRO

SER

MET

LYS

GLU

2

ARG

GLN

VAL

CYS

TRP

GLY

ALA

ARG

ASP

GLU

3

TYR

TRP

LYS

CYS

LEU

ASP

GLU

ASN

LEU

GLU

4

ASP

ALA

SER

GLN

CYS

LYS

LEU

ARG

SER

5

SER

PHE

GLU

SER

CYS

PRO

GLN

TRP

6

ILE

LYS

TYR

PHE

ASP

LYS

ARG

ASP

TYR

7

LEU

LYS

PHE

LYS

GLU

LYS

PHE

GLU

ALA

GLY

8

GLN

PHE

GLU

PRO

SER

GLU

THR

ALA

LYS

9

SER

Name	Sample	Sample state	Sample conditions
2D COSY	sample_3	isotropic	sample_conditions_1
2D TOCSY	sample_3	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HCCH-COSY	sample_2	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
3D H(CCO)NH	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HNCACO	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_2	isotropic	sample_conditions_1
2D NOESY	sample_3	isotropic	sample_conditions_1
2D-hbCBcgcdHD	sample_2	isotropic	sample_conditions_1

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

BMRB Entry 30556

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: