BMRB Entry 34089

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):

Data sets:
Data typeCount
13C chemical shifts329
15N chemical shifts79
1H chemical shifts504

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 76 residues - 8977.562 Da.

1   ALAASPLYSGLNTHRHISGLUTHRGLULEU
2   THRPHEASPGLNVALLYSGLUGLNLEUTHR
3   GLUSERGLYLYSLYSARGGLYVALLEUTHR
4   TYRGLUGLUILEALAGLUARGMETSERSER
5   PHEGLUILEGLUSERASPGLNMETASPGLU
6   TYRTYRGLUPHELEUGLYGLUGLNGLYVAL
7   GLULEUILESERGLUASNGLUGLUTHRGLU
8   ASPLEUGLUHISHISHIS

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:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
13Cali-NOESY-HSQCsample_2isotropicsample_conditions_1
15N-NOESY-HSQCsample_2isotropicsample_conditions_1
3D TOCSY-HSQCsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
1D 1Hsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
13Caro-NOESY-HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
3D (H)CC(CO)NHsample_2isotropicsample_conditions_1
3D H(CC)(CO)NHsample_2isotropicsample_conditions_1
1H, 15N-IPAPsample_3anisotropicsample_conditions_1
13C-detected (H)CACO-IPAPsample_2anisotropicsample_conditions_1
HN[C]-S3Esample_2anisotropicsample_conditions_1
1H, 15N-IPAPsample_2anisotropicsample_conditions_1
13C-detected (H)CACO-IPAPsample_3anisotropicsample_conditions_1
HN[C]-S3Esample_3anisotropicsample_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