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 4225

Title: NMR structure of Escherichia coli glutaredoxin3-glutathione mixed disulfide complex

Deposition date: 1998-08-17 Original release date: 2000-03-09

Authors: Nordstrand, K.; Aslund, F.; Holmgren, A.; Otting, G.; Berndt, K.

Citation: Nordstrand, K.; Aslund, F.; Holmgren, A.; Otting, G.; Berndt, K.. "NMR Structure of Escherichia coli Glutaredoxin 3-glutathione Mixed Disulfide Complex: Implications for the Enzymatic Mechanism"  J. Mol. Biol. 286, 541-552 (1999).

Assembly members:
Glutaredoxin 3, polymer, 83 residues, Formula weight is not available

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

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-24D

Entity Sequences (FASTA):
Glutaredoxin 3: ANVEIYTKETCPYSHRAKAL LSSKGVSFQELPIDGNAAKR EEMIKRSGRTTVPQIFIDAQ HIGGYDDLYALDARGGLDPL LKX

Data sets:
Data typeCount
15N chemical shifts87
1H chemical shifts501

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Glutaredoxin 31

Entities:

Entity 1, Glutaredoxin 3 83 residues - Formula weight is not available

1   ALAASNVALGLUILETYRTHRLYSGLUTHR
2   CYSPROTYRSERHISARGALALYSALALEU
3   LEUSERSERLYSGLYVALSERPHEGLNGLU
4   LEUPROILEASPGLYASNALAALALYSARG
5   GLUGLUMETILELYSARGSERGLYARGTHR
6   THRVALPROGLNILEPHEILEASPALAGLN
7   HISILEGLYGLYTYRASPASPLEUTYRALA
8   LEUASPALAARGGLYGLYLEUASPPROLEU
9   LEULYSGSH

Samples:

sample_1: Glutaredoxin 3 2.8 mM

sample_2: Glutaredoxin 3, [U-15N], 5.0 mM

sample_cond_1: ionic strength: 0.05 M; pH: 6.0; pressure: 1 atm; temperature: 301 K

Experiments:

NameSampleSample stateSample conditions
not availablenot availablenot availablesample_cond_1

Software:

PROSA v3.6 - spectral FT-transformations; baseline correction

XEASY v1.2 - spectral analysis

NMR spectrometers:

  • Bruker . 600 MHz

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