BMRB Entry 25243

Name: AN ARSENATE REDUCTASE IN OXIDIZED STATE
Published: 2015-08-03

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PDB ID: 2myu
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25243
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:

AN ARSENATE REDUCTASE IN OXIDIZED STATE

Deposition date:

2014-09-23

Original release date:

2015-08-03

Authors:

Jin, Changwen; Hu, Cuiyun

Citation:

Citation: Jin, Changwen; Hu, Cuiyun. "A Hybrid Mechanism for the Synechocystis Arsenate Reductase Revealed by Structural Snapshots during Arsenate Reduction" J. Biol. Chem. 290, 22262-22273 (2015).
PubMed: 26224634

Assembly members:

Assembly members:
entity, polymer, 131 residues, 14409.351 Da.

Natural source:

Natural source: Common Name: Synechocystis Taxonomy ID: 1142 Superkingdom: Bacteria Kingdom: not available Genus/species: Synechocystis not available

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET21a(+)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: MKKVMFVSKRNSSRSQMAEG FAKTLGAGKIAVTSSGLESS RVHPTAIAMMEEVGIDISGQ TSDPIENFNADDYDVVISLC GCGVNLPPEWVTQEIFEDWQ LEDPDGQSLEVFRTVRGQVK ERVENLIAKIS

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	542
15N chemical shifts	138
1H chemical shifts	875

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Arsenate Reductase	1

Entities:

Entity 1, Arsenate Reductase 131 residues - 14409.351 Da.

1

MET

LYS

VAL

MET

PHE

VAL

SER

LYS

ARG

2

ASN

SER

ARG

SER

GLN

MET

ALA

GLU

GLY

3

PHE

ALA

LYS

THR

LEU

GLY

ALA

GLY

LYS

ILE

4

ALA

VAL

THR

SER

GLY

LEU

GLU

SER

5

ARG

VAL

HIS

PRO

THR

ALA

ILE

ALA

MET

6

GLU

VAL

GLY

ILE

ASP

ILE

SER

GLY

GLN

7

THR

SER

ASP

PRO

ILE

GLU

ASN

PHE

ASN

ALA

8

ASP

TYR

ASP

VAL

ILE

SER

LEU

CYS

9

GLY

CYS

GLY

VAL

ASN

LEU

PRO

GLU

TRP

10

VAL

THR

GLN

GLU

ILE

PHE

GLU

ASP

TRP

GLN

11

LEU

GLU

ASP

PRO

ASP

GLY

GLN

SER

LEU

GLU

12

VAL

PHE

ARG

THR

VAL

ARG

GLY

GLN

VAL

LYS

13

GLU

ARG

VAL

GLU

ASN

LEU

ILE

ALA

LYS

ILE

14

SER

Samples:

sample_1: protein, [U-15N], 0.3 mM; sodium phosphate 50 mM; sodium chloride 50 mM

sample_2: protein, [U-13C; U-15N], 0.3 mM; sodium phosphate 50 mM; sodium chloride 50 mM

sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_2	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 HCCH-COSY	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC aromatic	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
3D 1H-13C NOESY aromatic	sample_2	isotropic	sample_conditions_1

Software:

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

NMR spectrometers:

Bruker Avance 500 MHz
Bruker Avance 800 MHz

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