BMRB Entry 4318

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR4318

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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:

Assignment of 1H, 13C, and 15N Resonances of Reduced Escherichia coli Glutaredoxin 2

Deposition date:

1999-03-12

Original release date:

1999-08-12

Authors:

Xia, Bin; Chung, John; Vlamis-Gardikas, Alexios; Holmgren, Arne; Wright, Peter; Dyson, H.

Citation:

Citation: Xia, Bin; Chung, John; Vlamis-Gardikas, Alexios; Holmgren, Arne; Wright, Peter; Dyson, H.. "Assignment of 1H, 13C, and 15N Resonances of Reduced Escherichia coli Glutaredoxin 2" J. Biomol. NMR 14, 197-198 (1999).

Assembly members:

Assembly members:
glutaredoxin 2, polymer, 215 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
glutaredoxin 2: MKLYIYDHCPYCLKARMIFG LKNIPVELHVLLNDDAETPT RMVGQKQVPILQKDDSRYMP ESMDIVHYVDKLDGKPLLTG KRSPAIEEWLRKVNGYANKL LLPRFAKSAFDEFSTPAARK YFVDKKEASAGNFADLLAHS DGLIKNISDDLRALDKLIVK PNAVNGELSEDDIQLFPLLR NLTLVAGINWPSRVADYRDN MAKQTQINLLSSMAI

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts

Data type	Count
13C chemical shifts	788
15N chemical shifts	193
1H chemical shifts	1199

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	glutaredoxin 2	1

Entities:

Entity 1, glutaredoxin 2 215 residues - Formula weight is not available

1

MET

LYS

LEU

TYR

ILE

TYR

ASP

HIS

CYS

PRO

2

TYR

CYS

LEU

LYS

ALA

ARG

MET

ILE

PHE

GLY

3

LEU

LYS

ASN

ILE

PRO

VAL

GLU

LEU

HIS

VAL

4

LEU

ASN

ASP

ALA

GLU

THR

PRO

THR

5

ARG

MET

VAL

GLY

GLN

LYS

GLN

VAL

PRO

ILE

6

LEU

GLN

LYS

ASP

SER

ARG

TYR

MET

PRO

7

GLU

SER

MET

ASP

ILE

VAL

HIS

TYR

VAL

ASP

8

LYS

LEU

ASP

GLY

LYS

PRO

LEU

THR

GLY

9

LYS

ARG

SER

PRO

ALA

ILE

GLU

TRP

LEU

10

ARG

LYS

VAL

ASN

GLY

TYR

ALA

ASN

LYS

LEU

11

LEU

PRO

ARG

PHE

ALA

LYS

SER

ALA

PHE

12

ASP

GLU

PHE

SER

THR

PRO

ALA

ARG

LYS

13

TYR

PHE

VAL

ASP

LYS

GLU

ALA

SER

ALA

14

GLY

ASN

PHE

ALA

ASP

LEU

ALA

HIS

SER

15

ASP

GLY

LEU

ILE

LYS

ASN

ILE

SER

ASP

16

LEU

ARG

ALA

LEU

ASP

LYS

LEU

ILE

VAL

LYS

17

PRO

ASN

ALA

VAL

ASN

GLY

GLU

LEU

SER

GLU

18

ASP

ILE

GLN

LEU

PHE

PRO

LEU

ARG

19

ASN

LEU

THR

LEU

VAL

ALA

GLY

ILE

ASN

TRP

20

PRO

SER

ARG

VAL

ALA

ASP

TYR

ARG

ASP

ASN

21

MET

ALA

LYS

GLN

THR

GLN

ILE

ASN

LEU

22

SER

MET

ALA

ILE

Samples:

sample_one: glutaredoxin 2, [U-13C; U-15N], 1.5 – 2.5 mM

sample_conditions: pH: 7.0 na; temperature: 293 K

Experiments:

Name	Sample	Sample state	Sample conditions

Software:

No software information available

NMR spectrometers:

unknown unknown 0 MHz

PDB	1G7O 4KSM 4KX4
DBJ	BAA35872 BAB34865 BAG76651 BAI24698 BAI29948
EMBL	CAA63058 CAP75556 CAQ31585 CAQ97963 CAR02405
GB	AAC74148 AAG55810 AAN42692 AAN79804 AAP16579
REF	NP_309469 NP_415582 NP_706985 WP_000780905 WP_000780906
SP	P0AC59 P0AC60 P0AC61
AlphaFold	P0AC59 P0AC60 P0AC61