BMRB Entry 18712
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR18712
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Title: b-flap domain of RNA polymerase (B. subtilis)
Deposition date: 2012-09-12 Original release date: 2014-03-10
Authors: Mobli, Mehdi
Citation: Mobli, Mehdi; Yang, Xiao; Ma, Cong; Thomas, Rhiannon; King, Glenn; Lewis, Peter. "NusA binding to the b-flap tip of RNA polymerase determined by NMR." Not known ., .-..
Assembly members:
b-flap, polymer, 149 residues, 15446.424 Da.
Natural source: Common Name: B. 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):
b-flap: MDDVYTSIHIEEYESEARDT
KLGPEEITRDIPNVGEDALR
NLDDRGVIRIGAEVKDGDLL
VGKVTPKGVTELTAEERLLH
AIFGEKAREVRDTSLRVPHG
GGGIIHDVKVFNREDGDELP
PGVNQLVRVYIVQKRKISEG
DGTHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 409 |
| 15N chemical shifts | 138 |
| 1H chemical shifts | 902 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | b-flap domain of RNA polymerase (B. subtilis) | 1 |
Entities:
Entity 1, b-flap domain of RNA polymerase (B. subtilis) 149 residues - 15446.424 Da.
| 1 | MET | ASP | ASP | VAL | TYR | THR | SER | ILE | HIS | ILE | ||||
| 2 | GLU | GLU | TYR | GLU | SER | GLU | ALA | ARG | ASP | THR | ||||
| 3 | LYS | LEU | GLY | PRO | GLU | GLU | ILE | THR | ARG | ASP | ||||
| 4 | ILE | PRO | ASN | VAL | GLY | GLU | ASP | ALA | LEU | ARG | ||||
| 5 | ASN | LEU | ASP | ASP | ARG | GLY | VAL | ILE | ARG | ILE | ||||
| 6 | GLY | ALA | GLU | VAL | LYS | ASP | GLY | ASP | LEU | LEU | ||||
| 7 | VAL | GLY | LYS | VAL | THR | PRO | LYS | GLY | VAL | THR | ||||
| 8 | GLU | LEU | THR | ALA | GLU | GLU | ARG | LEU | LEU | HIS | ||||
| 9 | ALA | ILE | PHE | GLY | GLU | LYS | ALA | ARG | GLU | VAL | ||||
| 10 | ARG | ASP | THR | SER | LEU | ARG | VAL | PRO | HIS | GLY | ||||
| 11 | GLY | GLY | GLY | ILE | ILE | HIS | ASP | VAL | LYS | VAL | ||||
| 12 | PHE | ASN | ARG | GLU | ASP | GLY | ASP | GLU | LEU | PRO | ||||
| 13 | PRO | GLY | VAL | ASN | GLN | LEU | VAL | ARG | VAL | TYR | ||||
| 14 | ILE | VAL | GLN | LYS | ARG | LYS | ILE | SER | GLU | GLY | ||||
| 15 | ASP | GLY | THR | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: b-flap, [U-100% 13C; U-100% 15N], 500 ± 50 uM; potassium phosphate 20 mM; sodium chloride 150 mM; H2O 95%; D2O 5%
sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
RNMRTK v3, Jeff Hoch, Alan Stern - processing
TALOS v+, Cornilescu, Delaglio and Bax - Dihedral angle generation
TOPSPIN v3, Bruker Biospin - collection
CYANA v3, Guntert, Mumenthaler and Wuthrich - structure solution
NMR spectrometers:
- Bruker Avance 900 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts