BMRB Entry 17821

Name: Human C30S/C59S-Cox17 mutant
Published: 2011-09-13

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PDB ID: 2lgq
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17821
MolProbity Validation Chart

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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 C30S/C59S-Cox17 mutant

Deposition date:

2011-08-01

Original release date:

2011-09-13

Authors:

Bertini, Ivano; Ciofi-Baffoni, Simone; Gallo, Angelo

Citation:

Citation: Banci, Lucia; Bertini, Ivano; Cefaro, Chiara; Ciofi-Baffoni, Simone; Gallo, Angelo. "Functional role of two interhelical disulfide bonds in human Cox17 protein from a structural perspective." J. Biol. Chem. 286, 34382-34390 (2011).
PubMed: 21816817

Assembly members:

Assembly members:
Human C30S/C59S-Cox17 mutant, polymer, 67 residues, 7288.475 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: pET-11c

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Human C30S/C59S-Cox17 mutant: GSFTMPGLVDSNPAPPESQE KKPLKPCCASPETKKARDAC IIEKGEEHCGHLIEAHKESM RALGFKI

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	244
15N chemical shifts	54
1H chemical shifts	221

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Human C30S/C59S-Cox17 mutant	1

Entities:

Entity 1, Human C30S/C59S-Cox17 mutant 67 residues - 7288.475 Da.

GSFT residues are present as cloning artifacts

1

GLY

SER

PHE

THR

MET

PRO

GLY

LEU

VAL

ASP

2

SER

ASN

PRO

ALA

PRO

GLU

SER

GLN

GLU

3

LYS

PRO

LEU

LYS

PRO

CYS

ALA

SER

4

PRO

GLU

THR

LYS

ALA

ARG

ASP

ALA

CYS

5

ILE

GLU

LYS

GLY

GLU

HIS

CYS

GLY

6

HIS

LEU

ILE

GLU

ALA

HIS

LYS

GLU

SER

MET

7

ARG

ALA

LEU

GLY

PHE

LYS

ILE

Samples:

sample_1: C30S/C59S-Cox17_mutant, [U-100% 15N], 0.5 mM; sodium phosphate 50 mM; EDTA 0.5 mM; DTT 1 mM; D2O 10%; H2O 90%

sample_2: C30S/C59S-Cox17_mutant, [U-99% 13C; U-99% 15N], 1 mM; sodium phosphate 50 mM; EDTA 0.5 mM; DTT 1 mM; D2O 10%; H2O 90%

sample_conditions_1: ionic strength: 50 mM; pH: 7.2; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_2	isotropic	sample_conditions_1
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, data analysis, processing

CARA v2.1, Keller and Wuthrich - chemical shift assignment

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

PECAN, Eghbalnia, Wang, Bahrami, Assadi, and Markley - data analysis

AMBER v11.0, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

NMR spectrometers:

Bruker Avance 900 MHz
Bruker Avance 500 MHz