BMRB Entry 30193

Name: Solution Structure of the N-terminal DNA-binding domain of the master biofilm-regulator SinR from Bacillus subtilis
Published: 2017-10-19

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PDB ID: 5tn0
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30193
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Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

Solution Structure of the N-terminal DNA-binding domain of the master biofilm-regulator SinR from Bacillus subtilis

Deposition date:

2016-10-13

Original release date:

2017-10-19

Authors:

Draughn, G.; Bobay, B.; Stowe, S.; Thompson, R.; Cavanagh, J.

Citation:

Citation: Milton, Morgan; Draughn, G Logan; Bobay, Benjamin; Stowe, Sean; Olson, Andrew; Feldmann, Erik; Thompson, Richele; Myers, Katherine; Santoro, Michael; Kearns, Daniel; Cavanagh, John. "The Solution Structures and Interaction of SinR and SinI: Elucidating the Mechanism of Action of the Master Regulator Switch for Biofilm Formation in Bacillus subtilis" J. Mol. Biol. 432, 343-357 (2020).
PubMed: 31493408

Assembly members:

Assembly members:
HTH-type transcriptional regulator SinR, polymer, 69 residues, 7847.908 Da.

Natural source:

Natural source: Common Name: firmicutes Taxonomy ID: 224308 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus subtilis

Experimental source:

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
HTH-type transcriptional regulator SinR: MIGQRIKQYRKEKGYSLSEL AEKAGVAKSYLSSIERNLQT NPSIQFLEKVSAVLDVSVHT LLDEKHETE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	309
15N chemical shifts	66
1H chemical shifts	465

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1	1

Entities:

Entity 1, entity_1 69 residues - 7847.908 Da.

1

MET

ILE

GLY

GLN

ARG

ILE

LYS

GLN

TYR

ARG

2

LYS

GLU

LYS

GLY

TYR

SER

LEU

SER

GLU

LEU

3

ALA

GLU

LYS

ALA

GLY

VAL

ALA

LYS

SER

TYR

4

LEU

SER

ILE

GLU

ARG

ASN

LEU

GLN

THR

5

ASN

PRO

SER

ILE

GLN

PHE

LEU

GLU

LYS

VAL

6

SER

ALA

VAL

LEU

ASP

VAL

SER

VAL

HIS

THR

7

LEU

ASP

GLU

LYS

HIS

GLU

THR

GLU

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_3	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_3	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_2	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HN(CA)CO	sample_2	isotropic	sample_conditions_1

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

BMRB Entry 30193

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: