BMRB Entry 15378

Title:
NMR structure of the S. aureus VraR DNA binding domain
Deposition date:
2007-07-13
Original release date:
2008-03-13
Authors:
Donaldson, Logan
Citation:

Citation: Donaldson, Logan. "The NMR Structure of the Staphylococcus aureus Response Regulator VraR DNA Binding Domain Reveals a Dynamic Relationship between It and Its Associated Receiver Domain"  Biochemistry 47, 3379-3388 (2008).
PubMed: 18293926

Assembly members:

Assembly members:
VraR, polymer, 93 residues, 10625.2 Da.

Natural source:

Natural source:   Common Name: Staphylococcus aureus   Taxonomy ID: 1280   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Staphylococcus aureus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15b

Data sets:
Data typeCount
13C chemical shifts239
15N chemical shifts55
1H chemical shifts366

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1VraR1

Entities:

Entity 1, VraR 93 residues - 10625.2 Da.

The first 20 residues are a His6 affinity tag and thrombin protease recognition site derived from pET15b (Novagen). The next 6 residues are derived from the native protein but not included in the structure determination

1   GLYSERSERHISHISHISHISHISHISSER
2   SERGLYLEUVALPROARGGLYSERHISMET
3   LYSLYSARGALAGLULEUGLULEUTYRGLU
4   METLEUTHRGLUARGGLUMETGLUILELEU
5   LEULEUILEALALYSGLYTYRSERASNGLN
6   GLUILEALASERALASERHISILETHRILE
7   LYSTHRVALLYSTHRHISVALSERASNILE
8   LEUSERLYSLEUGLUVALGLNASPARGTHR
9   GLNALAVALILETYRALAPHEGLNHISASN
10   LEUILEGLN

Samples:

sample_1: VraR, [U-98% 15N], 0.3 mM; NaCl 750 mM; H2O 90%; D2O 10%

sample_2: VraR, [U-98% 13C; U-98% 15N], 0.3 mM; NaCl 750 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 750 mM; pH: 7.8; pressure: 1 atm; temperature: 308.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_1isotropicsample_conditions_1
2D (HB)CB(CGCDCE)HEsample_1isotropicsample_conditions_1

Software:

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

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

X-PLOR NIH v2.17, Schwieters, Kuszewski, Tjandra and Clore - refinement

NMRView v5, Johnson, One Moon Scientific - data analysis

NMR spectrometers:

  • Varian NMRS 600 MHz

Related Database Links:

GB 14247656 47208328 EUS58931
BMRB 11024
PDB

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