BMRB Entry 34089

Name: Sigma1.1 domain of sigmaA from Bacillus subtilis
Published: 2017-06-08

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PDB ID: 5mww
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34089
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:

Sigma1.1 domain of sigmaA from Bacillus subtilis

Deposition date:

2017-01-20

Original release date:

2017-06-08

Authors:

Zachrdla, M.; Padrta, P.; Rabatinova, A.; Sanderova, H.; Barvik, I.; Krasny, L.; Zidek, L.

Citation:

Citation: Zachrdla, M.; Padrta, P.; Rabatinova, A.; Sanderova, H.; Barvik, I.; Krasny, L.; Zidek, L.. "Solution structure of domain 1.1 of the sigmaA factor from Bacillus subtilis is preformed for binding to the RNA polymerase core" J. Biol. Chem. 292, 11610-11617 (2017).
PubMed: 28539362

Assembly members:

Assembly members:
entity_1, polymer, 76 residues, 8977.562 Da.

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity_1: ADKQTHETELTFDQVKEQLT ESGKKRGVLTYEEIAERMSS FEIESDQMDEYYEFLGEQGV ELISENEETEDLEHHH

Data sets:

assigned_chemical_shifts
- assigned_chemical_shifts_1

Data type	Count
13C chemical shifts	329
15N chemical shifts	79
1H chemical shifts	504

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 76 residues - 8977.562 Da.

1

ALA

ASP

LYS

GLN

THR

HIS

GLU

THR

GLU

LEU

2

THR

PHE

ASP

GLN

VAL

LYS

GLU

GLN

LEU

THR

3

GLU

SER

GLY

LYS

ARG

GLY

VAL

LEU

THR

4

TYR

GLU

ILE

ALA

GLU

ARG

MET

SER

5

PHE

GLU

ILE

GLU

SER

ASP

GLN

MET

ASP

GLU

6

TYR

GLU

PHE

LEU

GLY

GLU

GLN

GLY

VAL

7

GLU

LEU

ILE

SER

GLU

ASN

GLU

THR

GLU

8

ASP

LEU

GLU

HIS

Samples:

sample_1: sigma1.1, [U-15N], 0.6 mM; sodium azide 6 mM; sodium chloride 10 mM; sodium phosphate 20 mM

sample_2: sigma1.1, [U-13C; U-15N], 0.8 mM; sodium azide 6 mM; sodium chloride 10 mM; sodium phosphate 20 mM

sample_3: polyacrylamide gel 5%; sigma1.1, [U-13C; U-15N], 0.8 mM; sodium azide 6 mM; sodium chloride 10 mM; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 10 mM; pH: 6.6; pressure: 1 atm; temperature: 298.2 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_2	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_2	isotropic	sample_conditions_1
3D HNCACB	sample_2	isotropic	sample_conditions_1
3D HN(CO)CA	sample_2	isotropic	sample_conditions_1
13Cali-NOESY-HSQC	sample_2	isotropic	sample_conditions_1
15N-NOESY-HSQC	sample_2	isotropic	sample_conditions_1
3D TOCSY-HSQC	sample_2	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_2	isotropic	sample_conditions_1
1D 1H	sample_2	isotropic	sample_conditions_1
3D HNCO	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_2	isotropic	sample_conditions_1
3D HNHA	sample_1	isotropic	sample_conditions_1
13Caro-NOESY-HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
3D (H)CC(CO)NH	sample_2	isotropic	sample_conditions_1
3D H(CC)(CO)NH	sample_2	isotropic	sample_conditions_1
1H, 15N-IPAP	sample_3	anisotropic	sample_conditions_1
13C-detected (H)CACO-IPAP	sample_2	anisotropic	sample_conditions_1
HN[C]-S3E	sample_2	anisotropic	sample_conditions_1
1H, 15N-IPAP	sample_2	anisotropic	sample_conditions_1
13C-detected (H)CACO-IPAP	sample_3	anisotropic	sample_conditions_1
HN[C]-S3E	sample_3	anisotropic	sample_conditions_1

Software:

CNS, Brunger A. T. et.al. - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - data analysis

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

S3EPY, Novak et al. - data analysis

SPARKY, Goddard - chemical shift assignment

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

Bruker AvanceIII 850 MHz
Bruker AvanceIII 700 MHz

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