BMRB Entry 11063
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11063
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Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments for KP-PmrD
Deposition date: 2008-12-30 Original release date: 2010-01-12
Authors: Luo, Shih-Chi
Citation: Luo, Shih-Chi; Chen, Chinpan. "Structural characterization of PmrD, which connects the PhoPQ and PmrAB two-component signal-transduction systems" .
Assembly members:
PmrD, polymer, 89 residues, Formula weight is not available
Natural source: Common Name: Klebsiella pneumoniae Taxonomy ID: 484021 Superkingdom: Bacteria Kingdom: not available Genus/species: Klebsiella pneumoniae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli BL21(DE3) Vector: pET 29b(+)
Entity Sequences (FASTA):
PmrD: MEWWVKKVQDNASASLCRVV
LQSGALEMIAEIEACRLRLR
EGDKLTPLADARYCLNNNPT
QTLKIRNATHYSSERWTNAD
KLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 330 |
| 15N chemical shifts | 75 |
| 1H chemical shifts | 510 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Polymyxin b resistant protein D | 1 |
Entities:
Entity 1, Polymyxin b resistant protein D 89 residues - Formula weight is not available
| 1 | MET | GLU | TRP | TRP | VAL | LYS | LYS | VAL | GLN | ASP | ||||
| 2 | ASN | ALA | SER | ALA | SER | LEU | CYS | ARG | VAL | VAL | ||||
| 3 | LEU | GLN | SER | GLY | ALA | LEU | GLU | MET | ILE | ALA | ||||
| 4 | GLU | ILE | GLU | ALA | CYS | ARG | LEU | ARG | LEU | ARG | ||||
| 5 | GLU | GLY | ASP | LYS | LEU | THR | PRO | LEU | ALA | ASP | ||||
| 6 | ALA | ARG | TYR | CYS | LEU | ASN | ASN | ASN | PRO | THR | ||||
| 7 | GLN | THR | LEU | LYS | ILE | ARG | ASN | ALA | THR | HIS | ||||
| 8 | TYR | SER | SER | GLU | ARG | TRP | THR | ASN | ALA | ASP | ||||
| 9 | LYS | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: Polymyxin b resistant protein D, [U-95% 13C; U-90% 15N], 0.4 mM; sodium phosphate 50 mM; H2O 90%; D2O 10%
sample_conditions_1: pH: 6.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution
NMR spectrometers:
- Bruker Avance 800 MHz
Related Database Links:
| PDB | |
| DBJ | BAH64168 |
| EMBL | CCI77623 CCM84637 CCM87409 CCM96230 CCN30508 |
| GB | ABR77864 AEJ98926 AEW62201 AFQ65083 AGT23550 |
| REF | WP_004141189 WP_004157936 WP_014907299 WP_015874957 WP_023284006 |
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts