BMRB Entry 17434

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17434
MolProbity Validation Chart

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Title:
solution structure of the C-terminal domain of H-NS like protein Bv3F
Deposition date:
2011-01-29
Original release date:
2015-06-23
Authors:
Li, Yifei; Xia, Bin
Citation:

Citation: Gordon, Blair; Li, Yifei; Cote, Atina; Weirauch, Matthew; Ding, Pengfei; Hughes, Timothy; Navarre, William; Xia, Bin; Liu, Jun. "Structural basis for recognition of AT-rich DNA by unrelated xenogeneic silencing proteins"  Proc. Natl. Acad. Sci. U. S. A. 108, 10690-10695 (2011).
PubMed: 21673140

Assembly members:

Assembly members:
Bv3F, polymer, 44 residues, 4828.533 Da.

Natural source:

Natural source:   Common Name: Burkholderia vietnamiensis   Taxonomy ID: 60552   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Burkholderia vietnamiensis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Bv3F: MSTVPKYRDPATGKTWSGRG RQPAWLGNDPAAFLIQPDLP AILE

Data sets:
Data typeCount
13C chemical shifts188
15N chemical shifts40
1H chemical shifts287

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1Bv3F1

Entities:

Entity 1, Bv3F 44 residues - 4828.533 Da.

1   METSERTHRVALPROLYSTYRARGASPPRO
2   ALATHRGLYLYSTHRTRPSERGLYARGGLY
3   ARGGLNPROALATRPLEUGLYASNASPPRO
4   ALAALAPHELEUILEGLNPROASPLEUPRO
5   ALAILELEUGLU

Samples:

sample_1: C-terminal domain of H-NS like protein Bv3F, [U-13C, >90%; U-15 N, >90%], 0.7 mM; sodium phosphate, [U-100% 13C; U-100% 15N], 50 mM

sample_conditions_1: ionic strength: 0.05 M; pH: 7.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1

Software:

AMBER, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - geometry optimization

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
GB ABO59125 ABO60030 KIP17029

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