BMRB Entry 16734
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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/BMR16734
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Title: NMR structure of the PASTA domain 3 and 4 of Mycobacterium tuberculosis of PknB PubMed: 20462494
Deposition date: 2010-02-17 Original release date: 2010-05-18
Authors: Barthe, Philippe; Cohen-Gonsaud, Martin; Roumestand, Christian; Mukamolova, Galina
Citation: Barthe, Philippe; Mukamolova, Galina; Roumestand, Christian; Cohen-Gonsaud, Martin. "The structure of PknB extracellular PASTA domain from mycobacterium tuberculosis suggests a ligand-dependent kinase activation." Structure (Cambridge, MA, U. S.) 18, 606-615 (2010).
Assembly members:
PknB_PASTA34, polymer, 139 residues, 14203.956 Da.
Natural source: Common Name: Mycobacterium tuberculosis Taxonomy ID: 1773 Superkingdom: Bacteria Kingdom: not available Genus/species: Mycobacterium tuberculosis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
PknB_PASTA34: GHMGPATKDIPDVAGQTVDV
AQKNLNVYGFTKFSQASVDS
PRPAGEVTGTNPPAGTTVPV
DSVIELQVSKGNQFVMPDLS
GMFWVDAEPRLRALGWTGML
DKGADVDAGGSQHNRVVYQN
PPAGTGVNRDGIITLRFGQ
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 378 |
| 15N chemical shifts | 148 |
| 1H chemical shifts | 890 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 139 residues - 14203.956 Da.
| 1 | GLY | HIS | MET | GLY | PRO | ALA | THR | LYS | ASP | ILE | ||||
| 2 | PRO | ASP | VAL | ALA | GLY | GLN | THR | VAL | ASP | VAL | ||||
| 3 | ALA | GLN | LYS | ASN | LEU | ASN | VAL | TYR | GLY | PHE | ||||
| 4 | THR | LYS | PHE | SER | GLN | ALA | SER | VAL | ASP | SER | ||||
| 5 | PRO | ARG | PRO | ALA | GLY | GLU | VAL | THR | GLY | THR | ||||
| 6 | ASN | PRO | PRO | ALA | GLY | THR | THR | VAL | PRO | VAL | ||||
| 7 | ASP | SER | VAL | ILE | GLU | LEU | GLN | VAL | SER | LYS | ||||
| 8 | GLY | ASN | GLN | PHE | VAL | MET | PRO | ASP | LEU | SER | ||||
| 9 | GLY | MET | PHE | TRP | VAL | ASP | ALA | GLU | PRO | ARG | ||||
| 10 | LEU | ARG | ALA | LEU | GLY | TRP | THR | GLY | MET | LEU | ||||
| 11 | ASP | LYS | GLY | ALA | ASP | VAL | ASP | ALA | GLY | GLY | ||||
| 12 | SER | GLN | HIS | ASN | ARG | VAL | VAL | TYR | GLN | ASN | ||||
| 13 | PRO | PRO | ALA | GLY | THR | GLY | VAL | ASN | ARG | ASP | ||||
| 14 | GLY | ILE | ILE | THR | LEU | ARG | PHE | GLY | GLN |
Samples:
sample_1: PknB_PASTA34, [U-100% 15N], 0.6 ± 0.1 mM; sodium acetate 20 ± 0.1 mM; H2O 5.0 ± 0.1 %; D2O 95 ± 0.1 %
sample_2: PknB_PASTA34, [U-100% 13C; U-100% 15N], 0.6 ± 0.1 mM; sodium acetate 20 ± 0.1 mM; H2O 95 ± 0.1 %; D2O 5 ± 0.1 %
sample_conditions_1: ionic strength: 20 mM; pH: 4.6; pressure: 1 atm; temperature: 283 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_2 | isotropic | sample_conditions_1 |
| 3D HN(COCA)CB | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_2 | isotropic | sample_conditions_1 |
| 3D HNCACO | sample_2 | isotropic | sample_conditions_1 |
Software:
CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
NMR spectrometers:
- Bruker Avance III 700 MHz
- Bruker Avance III 500 MHz
Related Database Links:
| PDB |
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