BMRB Entry 16912
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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/BMR16912
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Title: Delta subunit of RNA polymerase from Bacillus subtilis PubMed: 20890634
Deposition date: 2010-05-03 Original release date: 2010-10-05
Authors: Motackova, Veronika; Novacek, Jiri; Zawadska-Kazimierczuk, Anna; Kazimierczuk, Krzysztof; Zidek, Lukas; Sanderova, Hana; Krasny, Libor; Kozminski, Wiktor; Sklenar, Vladimir
Citation: Motakova, Veronika; Novaek, Jii; Zawadzka-Kazimierczuk, Anna; Kazimierczuk, Krzysztof; Zidek, Luka; Sanderova, Hana; Krasny, Libor; Komiski, Wiktor; Sklena, Vladimir. "Strategy for complete NMR assignment of disordered proteins with highly repetitive sequences based on resolution-enhanced 5D experiments." J. Biomol. NMR 48, 169-177 (2010).
Assembly members:
delta, polymer, 172 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):
delta: GIKQYSQEELKEMALVEIAH
ELFEEHKKPVPFQELLNEIA
SLLGVKKEELGDRIAQFYTD
LNIDGRFLALSDQTWGLRSW
YPYDQLDEETQPTVKAKKKK
AKKAVEEDLDLDEFEEIDED
DLDLDEVEEELDLEADDFDE
EDLDEDDDDLEIEEDIIDED
DEDYDDEEEEIK
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 752 |
15N chemical shifts | 183 |
1H chemical shifts | 1191 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | delta | 1 |
Entities:
Entity 1, delta 172 residues - Formula weight is not available
1 | GLY | ILE | LYS | GLN | TYR | SER | GLN | GLU | GLU | LEU | ||||
2 | LYS | GLU | MET | ALA | LEU | VAL | GLU | ILE | ALA | HIS | ||||
3 | GLU | LEU | PHE | GLU | GLU | HIS | LYS | LYS | PRO | VAL | ||||
4 | PRO | PHE | GLN | GLU | LEU | LEU | ASN | GLU | ILE | ALA | ||||
5 | SER | LEU | LEU | GLY | VAL | LYS | LYS | GLU | GLU | LEU | ||||
6 | GLY | ASP | ARG | ILE | ALA | GLN | PHE | TYR | THR | ASP | ||||
7 | LEU | ASN | ILE | ASP | GLY | ARG | PHE | LEU | ALA | LEU | ||||
8 | SER | ASP | GLN | THR | TRP | GLY | LEU | ARG | SER | TRP | ||||
9 | TYR | PRO | TYR | ASP | GLN | LEU | ASP | GLU | GLU | THR | ||||
10 | GLN | PRO | THR | VAL | LYS | ALA | LYS | LYS | LYS | LYS | ||||
11 | ALA | LYS | LYS | ALA | VAL | GLU | GLU | ASP | LEU | ASP | ||||
12 | LEU | ASP | GLU | PHE | GLU | GLU | ILE | ASP | GLU | ASP | ||||
13 | ASP | LEU | ASP | LEU | ASP | GLU | VAL | GLU | GLU | GLU | ||||
14 | LEU | ASP | LEU | GLU | ALA | ASP | ASP | PHE | ASP | GLU | ||||
15 | GLU | ASP | LEU | ASP | GLU | ASP | ASP | ASP | ASP | LEU | ||||
16 | GLU | ILE | GLU | GLU | ASP | ILE | ILE | ASP | GLU | ASP | ||||
17 | ASP | GLU | ASP | TYR | ASP | ASP | GLU | GLU | GLU | GLU | ||||
18 | ILE | LYS |
Samples:
sample_1: delta, [U-100% 13C; U-100% 15N], 0.7 mM; D2O, [U-2H], 10%; sodium chloride 10 mM; sodium azide 50 uM; phosphate buffer 20 mM; H2O 90%
sample_conditions_1: ionic strength: 30 mM; pH: 6.6; pressure: 1 atm; temperature: 301 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
2D CON | sample_1 | isotropic | sample_conditions_1 |
3D CBCACON | sample_1 | isotropic | sample_conditions_1 |
3D CBCANCO | sample_1 | isotropic | sample_conditions_1 |
3D HNCO | sample_1 | isotropic | sample_conditions_1 |
5D HN_CA_CONH | sample_1 | isotropic | sample_conditions_1 |
5D HabCabCONH | sample_1 | isotropic | sample_conditions_1 |
5D H_CCtocsy_CONH | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe v3.0, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker Avance 600 MHz
- Varian Uniform NMR System 700 MHz
Related Database Links:
BMRB | 16635 18903 19284 |
PDB | |
DBJ | BAM55799 BAM59811 |
EMBL | CAA89869 CAB15744 CCU60814 CEI59524 CEJ79381 |
GB | AAA22710 ADM39706 ADV94526 AEP92774 AFI30331 |
REF | NP_391597 WP_003221959 WP_003227609 WP_003235832 WP_003243661 |
SP | P12464 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts