BMRB Entry 16636

Name: NMR solution structure of the DNA binding domain of Competence protein A
Published: 2010-05-05

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PDB ID: 2krf
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
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: NMR solution structure of the DNA binding domain of Competence protein A PubMed: 20302877

Deposition date: 2009-12-16 Original release date: 2010-05-05

Authors: Hobbs, Carey; Bobay, Benjamin; Thompson, Richele; Perego, Marta; Cavanagh, John

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).

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

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

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

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	294
15N chemical shifts	69
1H chemical shifts	398

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	ComAC 1	1
2	ComAC 2	1

Entities:

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

1

GLY

SER

HIS

MET

SER

GLN

LYS

GLU

GLN

2

ASP

VAL

LEU

THR

PRO

ARG

GLU

CYS

LEU

ILE

3

LEU

GLN

GLU

VAL

GLU

LYS

GLY

PHE

THR

ASN

4

GLN

GLU

ILE

ALA

ASP

ALA

LEU

HIS

LEU

SER

5

LYS

ARG

SER

ILE

GLU

TYR

SER

LEU

THR

SER

6

ILE

PHE

ASN

LYS

LEU

ASN

VAL

GLY

SER

ARG

7

THR

GLU

ALA

VAL

LEU

ILE

ALA

LYS

SER

ASP

8

GLY

VAL

LEU

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	ComAC_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	ComAC_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	ComAC_1	isotropic	sample_conditions_1
3D C(CO)NH	ComAC_1	isotropic	sample_conditions_1
3D HNCO	ComAC_1	isotropic	sample_conditions_1
3D HNCACB	ComAC_1	isotropic	sample_conditions_1
3D HN(CO)CA	ComAC_1	isotropic	sample_conditions_1
3D H(CCO)NH	ComAC_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	ComAC_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	ComAC_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	ComAC_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	ComAC_1	isotropic	sample_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 simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts