BMRB Entry 16536

Name: Structure of the E1064A mutant of the N-domain of Wilson Disease Associated Protein
Published: 2012-08-03

Click here to enlarge.

PDB ID: 2koy
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16536
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:

Structure of the E1064A mutant of the N-domain of Wilson Disease Associated Protein

Deposition date:

2009-10-03

Original release date:

2012-08-03

Authors:

Dmitriev, Oleg

Citation:

Citation: Dmitriev, Oleg; Lutsenko, Svetlana; Uhelmann, Eva-Maria. "The structure of the E1064A mutant reveals ATP-dependent conformational changes in the ATP7B N-domain." Biochemistry ., .-..

Assembly members:

Assembly members:
E1064A mutant, polymer, 141 residues, 14752.269 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):
E1064A mutant: AGHMVPRVMRVLLLGDVATL PLRKVLAVVGTAAASSEHPL GVAVTKYCKEELGTETLGYC TDFQAVPGCGIGCKVSNVEG ILAAVPQTFSVLIGNREWLR RNGLTISSDVSDAMTDHEMK GQTAILVAIDGVLCGMIAIA D

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	523
15N chemical shifts	141
1H chemical shifts	865

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	E1064A mutant	1

Entities:

Entity 1, E1064A mutant 141 residues - 14752.269 Da.

1

ALA

GLY

HIS

MET

VAL

PRO

ARG

VAL

MET

ARG

2

VAL

LEU

GLY

ASP

VAL

ALA

THR

LEU

3

PRO

LEU

ARG

LYS

VAL

LEU

ALA

VAL

GLY

4

THR

ALA

SER

GLU

HIS

PRO

LEU

5

GLY

VAL

ALA

VAL

THR

LYS

TYR

CYS

LYS

GLU

6

GLU

LEU

GLY

THR

GLU

THR

LEU

GLY

TYR

CYS

7

THR

ASP

PHE

GLN

ALA

VAL

PRO

GLY

CYS

GLY

8

ILE

GLY

CYS

LYS

VAL

SER

ASN

VAL

GLU

GLY

9

ILE

LEU

ALA

VAL

PRO

GLN

THR

PHE

SER

10

VAL

LEU

ILE

GLY

ASN

ARG

GLU

TRP

LEU

ARG

11

ARG

ASN

GLY

LEU

THR

ILE

SER

ASP

VAL

12

SER

ASP

ALA

MET

THR

ASP

HIS

GLU

MET

LYS

13

GLY

GLN

THR

ALA

ILE

LEU

VAL

ALA

ILE

ASP

14

GLY

VAL

LEU

CYS

GLY

MET

ILE

ALA

ILE

ALA

15

ASP

Samples:

sample_1: sodium phosphate 50 mM; DTT 5 mM; DSS 0.3 mM; H2O 95%; D2O 5%; protein, [13C; 15N], 0.8 mM

sample_conditions_1: ionic strength: 0.1 M; pH: 6.0; pressure: 1 atm; temperature: 300 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(COCA)CB	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_1	isotropic	sample_conditions_1

Software:

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

FELIX v2007, Accelrys Software Inc. - peak picking

TALOS, Cornilescu, Delaglio and Bax - refinement

NMR spectrometers:

Bruker DRX 600 MHz