BMRB Entry 16922
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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/BMR16922
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Title: Backbone structure of the membrane domain of E. coli histidine kinase receptor KdpD PubMed: 20498088
Deposition date: 2010-05-11 Original release date: 2010-06-15
Authors: Maslennikov, Innokentiy; Klammt, Christian; Kefala, Georgia; Okamura, Mizuki; Esquivies, Luis; Kwiatkowski, Witek; Choe, Senyon
Citation: Maslennikov, Innokentiy; Klammt, Christian; Hwang, Eunha; Kefala, Georgia; Okamura, Mizuki; Esquivies, Luis; Mors, Karsten; Glaubitz, Clemens; Kwiatkowski, Witek; Jeon, Young Ho; Choe, Senyon. "Membrane domain structures of three classes of histidine kinase receptors by cell-free expression and rapid NMR analysis." Proc. Natl. Acad. Sci. U.S.A. 107, 10902-10907 (2010).
Assembly members:
histidine kinase receptor KdpD, polymer, 107 residues, 11442.749 Da.
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Eubacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: cell free synthesis Host organism: E. coli - cell free
Entity Sequences (FASTA):
histidine kinase receptor KdpD: MVQIQGSVVAAALSAVITLI
AMQWLMAFDAANLVMLYLLG
VVVVALFYGRWPSVVATVIN
VVSFDLFFIAPRGTLAVSDV
QYLLTFAVMLTVGLVIGNLT
AGVRYQA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 257 |
| 15N chemical shifts | 102 |
| 1H chemical shifts | 102 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | histidine kinase receptor KdpD | 1 |
Entities:
Entity 1, histidine kinase receptor KdpD 107 residues - 11442.749 Da.
| 1 | MET | VAL | GLN | ILE | GLN | GLY | SER | VAL | VAL | ALA | ||||
| 2 | ALA | ALA | LEU | SER | ALA | VAL | ILE | THR | LEU | ILE | ||||
| 3 | ALA | MET | GLN | TRP | LEU | MET | ALA | PHE | ASP | ALA | ||||
| 4 | ALA | ASN | LEU | VAL | MET | LEU | TYR | LEU | LEU | GLY | ||||
| 5 | VAL | VAL | VAL | VAL | ALA | LEU | PHE | TYR | GLY | ARG | ||||
| 6 | TRP | PRO | SER | VAL | VAL | ALA | THR | VAL | ILE | ASN | ||||
| 7 | VAL | VAL | SER | PHE | ASP | LEU | PHE | PHE | ILE | ALA | ||||
| 8 | PRO | ARG | GLY | THR | LEU | ALA | VAL | SER | ASP | VAL | ||||
| 9 | GLN | TYR | LEU | LEU | THR | PHE | ALA | VAL | MET | LEU | ||||
| 10 | THR | VAL | GLY | LEU | VAL | ILE | GLY | ASN | LEU | THR | ||||
| 11 | ALA | GLY | VAL | ARG | TYR | GLN | ALA |
Samples:
sample_1: DSS 0.5 mM; Mes-BisTris 20 mM; 1-myristoyl-2-hydroxy-sn-glycero-3-[phospho-rac-(1-glycerol)] 100 mM; histidine kinase receptor KdpD, [U-99% 13C; U-99% 15N], 0.3 mM
sample_conditions_1: pH: 6.0; pressure: 1 atm; temperature: 318 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | 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 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA v1.0.6, Guntert, Mumenthaler and Wuthrich - structure solution
CARA v2K.2, Keller and Wuthrich - data analysis, peak picking
CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Bruker Avance 700 MHz
Related Database Links:
| PDB | |
| DBJ | BAA35352 BAB34146 BAG76279 BAI24084 BAI29552 |
| EMBL | CAP75181 CAQ31160 CAQ97539 CAR06880 CAR11989 |
| GB | AAA24041 AAC73789 AAG55016 AAN79253 AAZ87404 |
| REF | NP_308750 NP_415223 WP_001295875 WP_001297245 WP_001298625 |
| SP | P21865 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts