BMRB Entry 16636

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16636
MolProbity Validation Chart

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Title:
NMR solution structure of the DNA binding domain of Competence protein A
Deposition date:
2009-12-16
Original release date:
2010-05-05
Authors:
Hobbs, Carey; Bobay, Benjamin; Thompson, Richele; Perego, Marta; Cavanagh, John
Citation:

Citation: Hobbs, Carey; Bobay, Benjamin; Thompson, Richele; Perego, Marta; Cavanagh, John. "NMR solution structure and DNA-binding model of the DNA-binding domain of competence protein A."  J. Mol. Biol. 398, 248-263 (2010).
PubMed: 20302877

Assembly members:

Assembly members:
ComAC, polymer, 73 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: Bacillus subtilis   Taxonomy ID: 1423   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus subtilis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pet28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
ComAC: GSHMSSQKEQDVLTPRECLI LQEVEKGFTNQEIADALHLS KRSIEYSLTSIFNKLNVGSR TEAVLIAKSDGVL

Data sets:
Data typeCount
13C chemical shifts294
15N chemical shifts69
1H chemical shifts398

Additional metadata:

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

Entity Assembly IDEntity NameEntity ID
1ComAC 11
2ComAC 21

Entities:

Entity 1, ComAC 1 73 residues - Formula weight is not available

1   GLYSERHISMETSERSERGLNLYSGLUGLN
2   ASPVALLEUTHRPROARGGLUCYSLEUILE
3   LEUGLNGLUVALGLULYSGLYPHETHRASN
4   GLNGLUILEALAASPALALEUHISLEUSER
5   LYSARGSERILEGLUTYRSERLEUTHRSER
6   ILEPHEASNLYSLEUASNVALGLYSERARG
7   THRGLUALAVALLEUILEALALYSSERASP
8   GLYVALLEU

Samples:

ComAC_1: sodium phosphate 25 mM; sodium chloride 100 mM; DTT 1 mM; EDTA 2 mM; ComAC, [U-13C; U-15N], 1 mM; H2O 90%; D2O 10%

ComAC_2: sodium phosphate 25 mM; sodium chloride 100 mM; DTT 1 mM; EDTA 2 mM; ComAC, [U-13C; U-15N], 1 mM; D2O 100%

sample_conditions_1: pH: 6.5; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCComAC_1isotropicsample_conditions_1
2D 1H-13C HSQCComAC_1isotropicsample_conditions_1
3D CBCA(CO)NHComAC_1isotropicsample_conditions_1
3D C(CO)NHComAC_1isotropicsample_conditions_1
3D HNCOComAC_1isotropicsample_conditions_1
3D HNCACBComAC_1isotropicsample_conditions_1
3D HN(CO)CAComAC_1isotropicsample_conditions_1
3D H(CCO)NHComAC_1isotropicsample_conditions_1
3D HCCH-TOCSYComAC_2isotropicsample_conditions_1
3D 1H-15N NOESYComAC_1isotropicsample_conditions_1
3D 1H-13C NOESYComAC_1isotropicsample_conditions_1
3D 1H-15N TOCSYComAC_1isotropicsample_conditions_1

Software:

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

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

NMRView, Johnson, One Moon Scientific - data analysis, peak picking

ARIA v1.2, Linge, O'Donoghue and Nilges - structure solution

CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

VNMRJ, Varian - collection

NMR spectrometers:

  • Varian INOVA 600 MHz

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