BMRB Entry 30192

Name: Solution Structure of SinI, antagonist to the master biofilm-regulator SinR in Bacillus subtilis
Published: 2017-10-19

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PDB ID: 5tmx
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR30192
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title: Solution Structure of SinI, antagonist to the master biofilm-regulator SinR in 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: Draughn, G.; Bobay, B.; Stowe, S.; Thompson, R.; Cavanagh, J.. "Solution Structure of SinI, antagonist to the master biofilm-regulator SinR in Bacillus subtilis" . ., .-..

Assembly members:
Protein SinI, polymer, 63 residues, 7184.149 Da.

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

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

Entity Sequences (FASTA):
Protein SinI: GSHMASMKNAKQEHFELDQE WVELMVEAKEANISPEEIRK YLLLNKKSAHPGPAARSHTV NPF

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	252
15N chemical shifts	51
1H chemical shifts	389

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

Entities:

Entity 1, entity_1, chain 1 63 residues - 7184.149 Da.

1

GLY

SER

HIS

MET

ALA

SER

MET

LYS

ASN

ALA

2

LYS

GLN

GLU

HIS

PHE

GLU

LEU

ASP

GLN

GLU

3

TRP

VAL

GLU

LEU

MET

VAL

GLU

ALA

LYS

GLU

4

ALA

ASN

ILE

SER

PRO

GLU

ILE

ARG

LYS

5

TYR

LEU

ASN

LYS

SER

ALA

HIS

6

PRO

GLY

PRO

ALA

ARG

SER

HIS

THR

VAL

7

ASN

PRO

PHE

Samples:

sample_1: MES 20 mM; NaCl 200 mM; SinI, [U-15N], 1 mM; H2O 90%; D2O 10%

sample_2: MES 20 mM; NaCl 200 mM; SinI, [U-13C; U-15N], 1 mM; H2O 90%; D2O 10%

sample_3: MES 20 mM; NaCl 200 mM; SinI, [U-13C; U-15N], 1 mM; D2O 100%

sample_conditions_1: ionic strength: 200 mM; pH: 6; pressure: 1 atm; temperature: 293 K

Experiments:

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

Software:

AMBER v14, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, and Kollman - refinement

CYANA v3.0, Guntert, Mumenthaler and Wuthrich - structure calculation

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

NMRView, Johnson, One Moon Scientific - chemical shift assignment, peak picking

NMR spectrometers:

Bruker Avance 700 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts