BMRB Entry 27011
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27011
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Title: Relaxation data for sigma1.1 from Bacillus subtilis PubMed: 28539362
Deposition date: 2017-01-20 Original release date: 2017-06-30
Authors: Zachrdla, Milan; Padrta, Petr; Rabatinova, Alzbeta; Sanderova, Hana; Barvik, Ivan; Krasny, Libor; Zidek, Lukas
Citation: Zachrdla, Milan; Padrta, Petr; Rabatinova, Alzbeta; Sanderova, Hana; Barvik, Ivan; Krasny, Libor; Zidek, Lukas. "Solution Structure of Domain 1.1 of the sigma(A) Factor from Bacillus subtilis is Preformed for Binding to the RNA Polymerase Core" J. Biol. Chem. 292, 11610-11617 (2017).
Assembly members:
sigma1.1, polymer, 79 residues, Formula weight is not available
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):
sigma1.1: ADKQTHETELTFDQVKEQLT
ESGKKRGVLTYEEIAERMSS
FEIESDQMDEYYEFLGEQGV
ELISENEETEDLEHHHHHH
- assigned_chemical_shifts
- heteronucl_NOEs
- heteronucl_T1_relaxation
- heteronucl_T2_relaxation
- order_parameters
| Data type | Count |
| T1 relaxation values | 204 |
| T2 relaxation values | 206 |
| heteronuclear NOE values | 204 |
| order parameters | 76 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | domain1.1 | 1 |
Entities:
Entity 1, domain1.1 79 residues - Formula weight is not available
| 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 | HIS | HIS | HIS |
Samples:
sample_1: sigma1.1, [U-100% 15N], 0.6 mM; sodium chloride 10 mM; sodium azide 6 mM; phosphate buffer 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 R1 15N,1H correlation | sample_1 | isotropic | sample_conditions_1 |
| 2D R2 15N,1H correlation | sample_1 | isotropic | sample_conditions_1 |
| 2D NOE 15N,1H correlation | sample_1 | isotropic | sample_conditions_1 |
| 2D 15N1H correlation - transverse cross-correlated cross-relaxation (symmetrical reconversion) | sample_1 | isotropic | sample_conditions_1 |
| 2D 15N1H correlation - longitudinal cross-correlated cross-relaxation (symmetrical reconversion) | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - peak picking
Relax, d'Auvergne - data analysis
Octave, Eaton - data analysis
NMR spectrometers:
- Bruker Avance 950 MHz
- Bruker Avance 850 MHz
- Bruker Avance 600 MHz