BMRB Entry 16264

Name: Solution structure of Glutaredoxin from Brucella melitensis. Seattle Structure Genomics Center for Infectious Disease (SSGCID) (Target ID BrabA.00079.a)
Published: 2009-07-14

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PDB ID: 2khp
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16264
MolProbity Validation Chart

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3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution structure of Glutaredoxin from Brucella melitensis. Seattle Structure Genomics Center for Infectious Disease (SSGCID) (Target ID BrabA.00079.a)

Deposition date:

2009-04-25

Original release date:

2009-07-14

Authors:

Zheng, Suxin; Leeper, Thomas; Varani, Gabriele

Citation:

Citation: Zheng, Suxin; Leeper, Thomas; Varani, Gabriele. "." .

Assembly members:

Assembly members:
Glutaredoxin, polymer, 92 residues, 9956.430 Da.

Natural source:

Natural source: Common Name: Brucella melitensis Taxonomy ID: 29459 Superkingdom: Bacteria Kingdom: not available Genus/species: Brucella melitensis

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Glutaredoxin: GPGSMVDVIIYTRPGCPYCA RAKALLARKGAEFNEIDASA TPELRAEMQERSGRNTFPQI FIGSVHVGGCDDLYALEDEG KLDSLLKTGKLI

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1
spectral_peak_list

Data type	Count
13C chemical shifts	276
15N chemical shifts	89
1H chemical shifts	625

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Glutaredoxin	1

Entities:

Entity 1, Glutaredoxin 92 residues - 9956.430 Da.

1

GLY

PRO

GLY

SER

MET

VAL

ASP

VAL

ILE

2

TYR

THR

ARG

PRO

GLY

CYS

PRO

TYR

CYS

ALA

3

ARG

ALA

LYS

ALA

LEU

ALA

ARG

LYS

GLY

4

ALA

GLU

PHE

ASN

GLU

ILE

ASP

ALA

SER

ALA

5

THR

PRO

GLU

LEU

ARG

ALA

GLU

MET

GLN

GLU

6

ARG

SER

GLY

ARG

ASN

THR

PHE

PRO

GLN

ILE

7

PHE

ILE

GLY

SER

VAL

HIS

VAL

GLY

CYS

8

ASP

LEU

TYR

ALA

LEU

GLU

ASP

GLU

GLY

9

LYS

LEU

ASP

SER

LEU

LYS

THR

GLY

LYS

10

LEU

ILE

Samples:

sample_1: Glutaredoxin, [U-100% 15N], 2.0 mM; KHPO4 20 mM; KCL 100 mM; H20 95%; D20 5%

sample_2: Glutaredoxin, [U-100% 13C; U-100% 15N], 2.0 mM; KHPO4 20 mM; KCL 100 mM; H20 95%; D20 5%

sample_conditions_1: ionic strength: 200 mM; pH: 7.5; pressure: 1.0 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	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
2D 1H-1H NOESY	sample_1	isotropic	sample_conditions_1

Software:

CYANA v2.1, P.GUNTERT ET AL. - refinement

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

ANALYSIS, Wayne Boucher,Tim Stevens and Wim Vranken - chemical shift assignment

NMR spectrometers:

Bruker Avance 500 MHz
Bruker Avance 600 MHz

PDB	2KHP
EMBL	CAJ11835 CDL77247
GB	AAL51366 AAN30771 AAX75168 ABQ61193 ABX62910
REF	WP_002964949 WP_004692121 WP_006173401 WP_008507665 WP_008934891