BMRB Entry 18301

Name: Metal binding repeat 2 of the Wilson disease protein (ATP7B)
Published: 2013-07-01

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PDB ID: 2lqb
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18301
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:

Metal binding repeat 2 of the Wilson disease protein (ATP7B)

Deposition date:

2012-02-28

Original release date:

2013-07-01

Authors:

Nokhrin, Sergiy; Dolgova, Nataliya; Yu, Corey; Dmitriev, Oleg

Citation:

Citation: Dolgova, Nataliya; Nokhrin, Sergiy; Yu, Corey; George, Graham; Dmitriev, Oleg. "Copper chaperone Atox1 interacts with the metal-binding domain of Wilson's disease protein in cisplatin detoxification." Biochem. J. 454, 147-156 (2013).
PubMed: 23751120

Assembly members:

Assembly members:
MBD2, polymer, 76 residues, 8427.775 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: pTYB12

Entity Sequences (FASTA):

Entity Sequences (FASTA):
MBD2: AGHMQEAVVKLRVEGMTCQS CVSSIEGKVRKLQGVVRVKV SLSNQEAVITYQPYLIQPED LRDHVNDMGFEAAIKS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	281
15N chemical shifts	69
1H chemical shifts	413

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	MBD2	1

Entities:

Entity 1, MBD2 76 residues - 8427.775 Da.

1

ALA

GLY

HIS

MET

GLN

GLU

ALA

VAL

LYS

2

LEU

ARG

VAL

GLU

GLY

MET

THR

CYS

GLN

SER

3

CYS

VAL

SER

ILE

GLU

GLY

LYS

VAL

ARG

4

LYS

LEU

GLN

GLY

VAL

ARG

VAL

LYS

VAL

5

SER

LEU

SER

ASN

GLN

GLU

ALA

VAL

ILE

THR

6

TYR

GLN

PRO

TYR

LEU

ILE

GLN

PRO

GLU

ASP

7

LEU

ARG

ASP

HIS

VAL

ASN

ASP

MET

GLY

PHE

8

GLU

ALA

ILE

LYS

SER

Samples:

sample_1: Tris-Cl, [U-2H], 50 mM; DSS 0.5 mM; sodium azide 0.05 mM; D2O, [U-2H], 5%; TCEP (tris(2-carboxyethyl)phosphine) 5 mM; H2O, [U-2H], 95%; MBD2, [U-2H], 0.9 mM

sample_conditions_1: ionic strength: 50 mM; pH: 7.4; pressure: 1 atm; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	not available
3D HNCO	sample_1	isotropic	not available
3D HNCA	sample_1	isotropic	not available
3D HNCACB	sample_1	isotropic	not available
3D HN(CO)CACB	sample_1	isotropic	not available
3D C(CO)NH	sample_1	isotropic	not available
3D H(CCO)NH	sample_1	isotropic	not available
3D 1H-15N TOCSY	sample_1	isotropic	not available
3D 1H-15N NOESY	sample_1	isotropic	not available
3D 1H-13C NOESY	sample_1	isotropic	not available
3D HN(CA)CO	sample_1	isotropic	not available

Software:

CYANA_3.0, Guntert, Mumenthaler and Wuthrich - structure solution

AutoAssign, Zimmerman, Moseley, Kulikowski and Montelione - chemical shift assignment

CARA v1.9.0, F. Damberger, R. Keller - chemical shift assignment

FELIX, Accelrys Software Inc. - peak picking, processing

NMR spectrometers:

Bruker Avance 600 MHz