BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 16264

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

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

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

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

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

Data typeCount
13C chemical shifts276
15N chemical shifts89
1H chemical shifts625

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1Glutaredoxin1

Entities:

Entity 1, Glutaredoxin 92 residues - 9956.430 Da.

1   GLYPROGLYSERMETVALASPVALILEILE
2   TYRTHRARGPROGLYCYSPROTYRCYSALA
3   ARGALALYSALALEULEUALAARGLYSGLY
4   ALAGLUPHEASNGLUILEASPALASERALA
5   THRPROGLULEUARGALAGLUMETGLNGLU
6   ARGSERGLYARGASNTHRPHEPROGLNILE
7   PHEILEGLYSERVALHISVALGLYGLYCYS
8   ASPASPLEUTYRALALEUGLUASPGLUGLY
9   LYSLEUASPSERLEULEULYSTHRGLYLYS
10   LEUILE

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D HN(CO)CAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_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

Related Database Links:

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

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