BMRB Entry 4944

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4944

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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:

1H, 13C and 15N backbone resonance assignment of the arsenate reductase from Staphylococcus aureus in its reduced state.

Deposition date:

2001-01-22

Original release date:

2001-05-17

Authors:

Jacobs, Doris; Messens, Joris; Wechselberger, Rainer; Brosens, Elke; Wyns, Lode; Willem, Rudolph; Martins, Jose

Citation:

Citation: Jacobs, Doris; Messens, Joris; Wechselberger, Rainer; Brosens, Elke; Willem, Rudolph; Wyns, Lode; Martins, Jose. "Letter to the Editor: 1H, 13C and 15N backbone resonance assignment of the arsenate reductase from Staphylococcus aureus in its reduced state" J. Biomol. NMR 20, 95-96 (2001).

Assembly members:

Assembly members:
Arsenate reductase, polymer, 131 residues, 14812 Da.

Natural source:

Natural source: Common Name: Staphylococcus aureus Taxonomy ID: 1280 Superkingdom: Eubacteria Kingdom: not available Genus/species: Staphylococcus aureus

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET11a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Arsenate reductase: MDKKTIYFICTGNSCRSQMA EGWGKEILGEGWNVYSAGIE THGVNPKAIEAMKEVDIDIS NHTSDLIDNDILKQSDLVVT LCSDADNNCPILPPNVKKEH WGFDDPAGKEWSEFQRVRDE IKLAIEKFKLR

Data sets:

assigned_chemical_shifts
- shift_set_1

Data type	Count
1H chemical shifts	244
13C chemical shifts	358
15N chemical shifts	122

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 - 14812 Da.

1

MET

ASP

LYS

THR

ILE

TYR

PHE

ILE

CYS

2

THR

GLY

ASN

SER

CYS

ARG

SER

GLN

MET

ALA

3

GLU

GLY

TRP

GLY

LYS

GLU

ILE

LEU

GLY

GLU

4

GLY

TRP

ASN

VAL

TYR

SER

ALA

GLY

ILE

GLU

5

THR

HIS

GLY

VAL

ASN

PRO

LYS

ALA

ILE

GLU

6

ALA

MET

LYS

GLU

VAL

ASP

ILE

ASP

ILE

SER

7

ASN

HIS

THR

SER

ASP

LEU

ILE

ASP

ASN

ASP

8

ILE

LEU

LYS

GLN

SER

ASP

LEU

VAL

THR

9

LEU

CYS

SER

ASP

ALA

ASP

ASN

CYS

PRO

10

ILE

LEU

PRO

ASN

VAL

LYS

GLU

HIS

11

TRP

GLY

PHE

ASP

PRO

ALA

GLY

LYS

GLU

12

TRP

SER

GLU

PHE

GLN

ARG

VAL

ARG

ASP

GLU

13

ILE

LYS

LEU

ALA

ILE

GLU

LYS

PHE

LYS

LEU

14

ARG

Samples:

sample_1: Arsenate reductase, [U-95% 13C; U-98% 15N], 1.8 mM; DTT 1.0 mM; EDTA 0.1 mM; K2SO4 50 mM; potassium phosphate buffer 50 mM

sample_2: Arsenate reductase, [U-98% 15N], 1.8 mM; DTT 1.0 mM; EDTA 0.1 mM; K2SO4 50 mM; potassium phosphate buffer 50 mM

Ex-cond_1: pH: 6.7; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
1H-15N HSQC	not available	not available	not available
1H-15N HSQC-TOCSY	not available	not available	not available
1H-15N HSQC-NOESY	not available	not available	not available
HNCA	not available	not available	not available
HNCO	not available	not available	not available
HN(CO)CA	not available	not available	not available
HN(CA)CO	not available	not available	not available
CBCA(CO)NH	not available	not available	not available
HNCACB	not available	not available	not available

Software:

FELIX v97.0 - processing, manual peak picking, manual assignment

NMR spectrometers:

Bruker AMX 500 MHz
Bruker DRX 600 MHz
Varian Inova 750 MHz

PDB	1JF8 1JFV 1LJL 1LJU 1LK0 1RXE 1RXI 2CD7 2FXI
DBJ	BAB43887 BAC54538 BAE18778 BAE92851 BAG12261
EMBL	CAG39708
GB	AAA25638 ACZ58845 ACZ68457 ACZ68855 ACZ68904
REF	NP_395554 WP_000358995 WP_002452591 WP_002508683 WP_003756625
SP	P0A005 P0A006 Q49WS7 Q6GIZ3
AlphaFold	P0A005 P0A006 Q49WS7 Q6GIZ3