BMRB Entry 30194

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

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PDB ID: 5tn2
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30194
MolProbity Validation Chart

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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 C-terminal multimerization 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, 47 residues, 5722.338 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: GSHMEYDGQLDSEWEKLVRD AMTSGVSKKQFREFLDYQKW RKSQKEE

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	209
15N chemical shifts	54
1H chemical shifts	312

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	entity_1, chain 1	1
2	entity_1, chain 2	1
3	entity_1, chain 3	1
4	entity_1, chain 4	1

Entities:

Entity 1, entity_1, chain 1 47 residues - 5722.338 Da.

1

GLY

SER

HIS

MET

GLU

TYR

ASP

GLY

GLN

LEU

2

ASP

SER

GLU

TRP

GLU

LYS

LEU

VAL

ARG

ASP

3

ALA

MET

THR

SER

GLY

VAL

SER

LYS

GLN

4

PHE

ARG

GLU

PHE

LEU

ASP

TYR

GLN

LYS

TRP

5

ARG

LYS

SER

GLN

LYS

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 HN(CA)CO	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_2	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_3	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 30194

Additional metadata:

Assembly:

Entities:

Samples:

Experiments:

Software:

NMR spectrometers: