BMRB Entry 34089
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PDB ID:
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
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Title: Sigma1.1 domain of sigmaA from Bacillus subtilis PubMed: 28539362
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: 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).
Assembly members:
entity_1, polymer, 76 residues, 8977.562 Da.
Natural source: Common Name: Bacillus subtilis Taxonomy ID: 1423 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus subtilis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: ADKQTHETELTFDQVKEQLT
ESGKKRGVLTYEEIAERMSS
FEIESDQMDEYYEFLGEQGV
ELISENEETEDLEHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 329 |
| 15N chemical shifts | 79 |
| 1H chemical shifts | 504 |
Additional metadata:
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 | LYS | ARG | GLY | VAL | LEU | THR | ||||
| 4 | TYR | GLU | GLU | ILE | ALA | GLU | ARG | MET | SER | SER | ||||
| 5 | PHE | GLU | ILE | GLU | SER | ASP | GLN | MET | ASP | GLU | ||||
| 6 | TYR | TYR | GLU | PHE | LEU | GLY | GLU | GLN | GLY | VAL | ||||
| 7 | GLU | LEU | ILE | SER | GLU | ASN | GLU | GLU | THR | GLU | ||||
| 8 | ASP | LEU | GLU | HIS | HIS | 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 simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts