BMRB Entry 16942
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PDB ID: 2ky9
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR16942
MolProbity Validation Chart
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NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
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Citation: Eletsky, Alexander; Sukumaran, Dinesh; Lee, Hsiau-Wei; Lee, Dan; Ciccosanti, Colleen; Janjua, Haleema; Liu, Jinfeng; Rost, Burkhard; Acton, Thomas; Xiao, Rong; Everett, John; Prestegard, James; Montelione, Gaetano; Szyperski, Thomas. "Solution NMR Structure of ydhK C-terminal Domain from B.subtilis, Northeast Structural Genomics Consortium Target Target SR518" To be published ., .-..
Assembly members:
SR518, polymer, 132 residues, 14611.442 Da.
Natural source: Common Name: Bacillus subtilis Taxonomy ID: 1423 Superkingdom: Bacteria Kingdom: not available Genus/species: Bacillus subtilis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET21-23C
| Data type | Count |
| 13C chemical shifts | 542 |
| 15N chemical shifts | 135 |
| 1H chemical shifts | 862 |
| residual dipolar couplings | 195 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | SR518 | 1 |
Entities:
Entity 1, SR518 132 residues - 14611.442 Da.
Residues 2-124 correspond to the range 83-205 of the native protein. Residues 125-132 represent a non-native affinity tag, and residue one is due to the initiation codon.
| 1 | MET | LYS | VAL | GLY | SER | GLN | VAL | ILE | ILE | ASN | ||||
| 2 | THR | SER | HIS | MET | LYS | GLY | MET | LYS | GLY | ALA | ||||
| 3 | GLU | ALA | THR | VAL | THR | GLY | ALA | TYR | ASP | THR | ||||
| 4 | THR | ALA | TYR | VAL | VAL | SER | TYR | THR | PRO | THR | ||||
| 5 | ASN | GLY | GLY | GLN | ARG | VAL | ASP | HIS | HIS | LYS | ||||
| 6 | TRP | VAL | ILE | GLN | GLU | GLU | ILE | LYS | ASP | ALA | ||||
| 7 | GLY | ASP | LYS | THR | LEU | GLN | PRO | GLY | ASP | GLN | ||||
| 8 | VAL | ILE | LEU | GLU | ALA | SER | HIS | MET | LYS | GLY | ||||
| 9 | MET | LYS | GLY | ALA | THR | ALA | GLU | ILE | ASP | SER | ||||
| 10 | ALA | GLU | LYS | THR | THR | VAL | TYR | MET | VAL | ASP | ||||
| 11 | TYR | THR | SER | THR | THR | SER | GLY | GLU | LYS | VAL | ||||
| 12 | LYS | ASN | HIS | LYS | TRP | VAL | THR | GLU | ASP | GLU | ||||
| 13 | LEU | SER | ALA | LYS | LEU | GLU | HIS | HIS | HIS | HIS | ||||
| 14 | HIS | HIS |
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