BMRB Entry 15991
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15991
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Title: Structure of the Core Binding Domain of sigma54 PubMed: 19426742
Deposition date: 2008-10-19 Original release date: 2009-05-29
Authors: Hong, Eunmi; Wemmer, David E.
Citation: Hong, Eunmi; Douclaff, Michaeleen; Wemmer, David. "Structure of the RNA Polymerase Core-Binding Domain of sigma(54) Reveals a Likely Conformational Fracture Point." J. Mol. Biol. 390, 70-82 (2009).
Assembly members:
Core_Binding_Domain, polymer, 130 residues, Formula weight is not available
Natural source: Common Name: Aquifex aeolicus Taxonomy ID: 63363 Superkingdom: Bacteria Kingdom: not available Genus/species: Aquifex aeolicus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET21b3-2
Entity Sequences (FASTA):
Core_Binding_Domain: YTPSELEELQQNIKLELEGK
EQELALELLNYLNEKGFLSK
SVEEISDVLRCSVEELEKVR
QKVLRLEPLGVCSKDVWEFL
ELQIEEIYPEEEEILKKALR
DLKRGKKLKPEIKGKLSRLR
LFPLSSSAEK
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 419 |
15N chemical shifts | 126 |
1H chemical shifts | 975 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | subunit 1 | 1 |
Entities:
Entity 1, subunit 1 130 residues - Formula weight is not available
1 | TYR | THR | PRO | SER | GLU | LEU | GLU | GLU | LEU | GLN | |
2 | GLN | ASN | ILE | LYS | LEU | GLU | LEU | GLU | GLY | LYS | |
3 | GLU | GLN | GLU | LEU | ALA | LEU | GLU | LEU | LEU | ASN | |
4 | TYR | LEU | ASN | GLU | LYS | GLY | PHE | LEU | SER | LYS | |
5 | SER | VAL | GLU | GLU | ILE | SER | ASP | VAL | LEU | ARG | |
6 | CYS | SER | VAL | GLU | GLU | LEU | GLU | LYS | VAL | ARG | |
7 | GLN | LYS | VAL | LEU | ARG | LEU | GLU | PRO | LEU | GLY | |
8 | VAL | CYS | SER | LYS | ASP | VAL | TRP | GLU | PHE | LEU | |
9 | GLU | LEU | GLN | ILE | GLU | GLU | ILE | TYR | PRO | GLU | |
10 | GLU | GLU | GLU | ILE | LEU | LYS | LYS | ALA | LEU | ARG | |
11 | ASP | LEU | LYS | ARG | GLY | LYS | LYS | LEU | LYS | PRO | |
12 | GLU | ILE | LYS | GLY | LYS | LEU | SER | ARG | LEU | ARG | |
13 | LEU | PHE | PRO | LEU | SER | SER | SER | ALA | GLU | LYS |
Samples:
sample_1: Core Binding Domain, [U-100% 13C; U-100% 15N], 0.6-0.8 mM; Core Binding Domain, [U-100% 15N], 0.6-0.8 mM; H2O 90%; D2O 10%
sample_2: Core Binding Domain, [U-100% 13C; U-100% 15N], 0.6-0.8 mM; D2O 100%
sample_conditions_1: ionic strength: 0.1 M; pH: 7; pressure: 1 atm; temperature: 303 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HNCA | sample_1 | isotropic | sample_conditions_1 |
3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
3D HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
3D HCCH-TOCSY | sample_2 | isotropic | sample_conditions_1 |
3D 1H-13C NOESY | sample_2 | isotropic | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY v3.114, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker DRX 800 MHz
- Bruker DRX 900 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts