BMRB Entry 17651
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17651
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Title: Solution Structure of Histidine Phosphotransfer Domain of CheA PubMed: 21947914
Deposition date: 2011-05-16 Original release date: 2011-10-12
Authors: Vu, Anh; Hamel, Damon; Zhou, Hongjun; Dahlquist, Frederick
Citation: Vu, Anh; Hamel, Damon; Zhou, Hongjun; Dahlquist, Frederick. "The structure and dynamic properties of the complete histidine phosphotransfer domain of the chemotaxis specific histidine autokinase CheA from Thermotoga maritima." J. Biomol. NMR 51, 49-55 (2011).
Assembly members:
CheA, polymer, 133 residues, 14948.087 Da.
Natural source: Common Name: Thermotoga maritima Taxonomy ID: 2336 Superkingdom: Bacteria Kingdom: not available Genus/species: Thermotoga maritima
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
CheA: MMEEYLGVFVDETKEYLQNL
NDTLLELEKNPEDMELINEA
FRALHTLKGMAGTMGFSSMA
KLCHTLENILDKARNSEIKI
TSDLLDKIFAGVDMITRMVD
KIVSEGSDDIGENIDVFSDT
IKSFASSGKEKLE
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 420 |
| 15N chemical shifts | 130 |
| 1H chemical shifts | 869 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | CheA | 1 |
Entities:
Entity 1, CheA 133 residues - 14948.087 Da.
| 1 | MET | MET | GLU | GLU | TYR | LEU | GLY | VAL | PHE | VAL | ||||
| 2 | ASP | GLU | THR | LYS | GLU | TYR | LEU | GLN | ASN | LEU | ||||
| 3 | ASN | ASP | THR | LEU | LEU | GLU | LEU | GLU | LYS | ASN | ||||
| 4 | PRO | GLU | ASP | MET | GLU | LEU | ILE | ASN | GLU | ALA | ||||
| 5 | PHE | ARG | ALA | LEU | HIS | THR | LEU | LYS | GLY | MET | ||||
| 6 | ALA | GLY | THR | MET | GLY | PHE | SER | SER | MET | ALA | ||||
| 7 | LYS | LEU | CYS | HIS | THR | LEU | GLU | ASN | ILE | LEU | ||||
| 8 | ASP | LYS | ALA | ARG | ASN | SER | GLU | ILE | LYS | ILE | ||||
| 9 | THR | SER | ASP | LEU | LEU | ASP | LYS | ILE | PHE | ALA | ||||
| 10 | GLY | VAL | ASP | MET | ILE | THR | ARG | MET | VAL | ASP | ||||
| 11 | LYS | ILE | VAL | SER | GLU | GLY | SER | ASP | ASP | ILE | ||||
| 12 | GLY | GLU | ASN | ILE | ASP | VAL | PHE | SER | ASP | THR | ||||
| 13 | ILE | LYS | SER | PHE | ALA | SER | SER | GLY | LYS | GLU | ||||
| 14 | LYS | LEU | GLU |
Samples:
sample_1: H2O 90%; D2O, [U-99% 2H], 10%; P1, [U-99% 13C; U-99% 15N], 1 mM
sample_conditions_1: ionic strength: 0.05 M; pH: 7.4; pressure: 1 atm; temperature: 273 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 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 4D 15N,13C NOESY | sample_1 | isotropic | sample_conditions_1 |
| 4D 13C,13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
X-PLOR v3.851, Brunger - structure solution
ANSIG, Kraulis - data analysis
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Varian INOVA 600 MHz
Related Database Links:
| PDB | |
| GB | AAA96387 AAD35784 ABQ46257 ACB08586 ADA66595 |
| REF | NP_228511 WP_004081040 WP_008192691 WP_011942905 WP_012310403 |
| SP | Q56310 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts