BMRB Entry 15574
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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/BMR15574
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Title: NMR solution structure of KP-TerB, a tellurite resistance protein from Klebsiella pneumoniae PubMed: 18305192
Deposition date: 2007-11-30 Original release date: 2008-06-27
Authors: Sheng-Kuo, Chiang; Yuan-Chao, Lou; Chinpan, Chen
Citation: Chiang, Sheng-Kuo; Lou, Yuan-Chao; Chen, Chinpan. "NMR solution structure of KP-TerB, a tellurite-resistance protein from Klebsiella pneumoniae" Protein Sci. 17, 785-789 (2008).
Assembly members:
KP-TerB, polymer, 159 residues, 17753.1 Da.
Natural source: Common Name: Klebsiella pneumoniae Taxonomy ID: 573 Superkingdom: Bacteria Kingdom: not available Genus/species: Klebsiella pneumoniae
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
KP-TerB: MSFFDKVKGALTSGREELTR
QVGRYKNKKFMQGTVAVCAR
IAVASDGVSSEEKQKMIGFL
RSSEELKVFDTAEVIEFFNK
LVTSFDFDLEIGKGETMKYI
LALKDQPEAAQLALRVGIAV
AKSDGNFDDDEKSAVREIAR
SLGFDPAEFGLLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 684 |
| 15N chemical shifts | 156 |
| 1H chemical shifts | 1058 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | KP-TerB | 1 |
Entities:
Entity 1, KP-TerB 159 residues - 17753.1 Da.
Residues 152-159 are tag residues.
| 1 | MET | SER | PHE | PHE | ASP | LYS | VAL | LYS | GLY | ALA | ||||
| 2 | LEU | THR | SER | GLY | ARG | GLU | GLU | LEU | THR | ARG | ||||
| 3 | GLN | VAL | GLY | ARG | TYR | LYS | ASN | LYS | LYS | PHE | ||||
| 4 | MET | GLN | GLY | THR | VAL | ALA | VAL | CYS | ALA | ARG | ||||
| 5 | ILE | ALA | VAL | ALA | SER | ASP | GLY | VAL | SER | SER | ||||
| 6 | GLU | GLU | LYS | GLN | LYS | MET | ILE | GLY | PHE | LEU | ||||
| 7 | ARG | SER | SER | GLU | GLU | LEU | LYS | VAL | PHE | ASP | ||||
| 8 | THR | ALA | GLU | VAL | ILE | GLU | PHE | PHE | ASN | LYS | ||||
| 9 | LEU | VAL | THR | SER | PHE | ASP | PHE | ASP | LEU | GLU | ||||
| 10 | ILE | GLY | LYS | GLY | GLU | THR | MET | LYS | TYR | ILE | ||||
| 11 | LEU | ALA | LEU | LYS | ASP | GLN | PRO | GLU | ALA | ALA | ||||
| 12 | GLN | LEU | ALA | LEU | ARG | VAL | GLY | ILE | ALA | VAL | ||||
| 13 | ALA | LYS | SER | ASP | GLY | ASN | PHE | ASP | ASP | ASP | ||||
| 14 | GLU | LYS | SER | ALA | VAL | ARG | GLU | ILE | ALA | ARG | ||||
| 15 | SER | LEU | GLY | PHE | ASP | PRO | ALA | GLU | PHE | GLY | ||||
| 16 | LEU | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: KP-TerB, [U-99% 13C; U-99% 15N], 1 – 2 mM; D2O, [U-100% 2H], 10%; H2O 90%
sample_conditions_1: pH: 6; pressure: 1 atm; temperature: 298 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 C(CO)NH | 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 HBHA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HCCH-TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
AURELIA, Bruker Biospin, Neidig, Geyer, Gorler, Antz, Saffrich, Beneicke, Kalbitzer, Schwieters, Kuszewski, Tjandra and Clore - chemical shift assignment, collection, refinement
NMR spectrometers:
- Bruker Avance 800 MHz
Related Database Links:
| PDB | |
| DBJ | BAH66155 |
| EMBL | CDI26599 CDM79665 CEO83280 CEP33512 |
| GB | AAA98290 AAR07675 ACI12150 AFB82882 AHE47496 |
| REF | NP_943325 WP_004026604 WP_011154616 WP_014386550 WP_023287202 |
| SP | P18779 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts