BMRB Entry 17585
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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/BMR17585
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Title: Rv0020c_Nter structure PubMed: 22000520
Deposition date: 2011-04-11 Original release date: 2011-10-26
Authors: Barthe, Philippe; Cohen-Gonsaud, Martin; Roumestand, Christian
Citation: Roumestand, Christian; Leiba, Jade; Galophe, Nathalie; Margeat, Emmanuel; Padilla, Andre; Bessin, Yannick; Barthe, Philippe; Molle, Virginie; Cohen-Gonsaud, Martin. "Structural Insight into the Mycobacterium tuberculosis Rv0020c Protein and Its Interaction with the PknB Kinase." Structure 19, 1525-1534 (2011).
Assembly members:
Rv0020c_Nter, polymer, 132 residues, 14773.583 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):
Rv0020c_Nter: MGSQKRLVQRVERKLEQTVG
DAFARIFGGSIVPQEVEALL
RREAADGIQSLQGNRLLAPN
EYIITLGVHDFEKLGADPEL
KSTGFARDLADYIQEQGWQT
YGDVVVRFEQSSNLHTGQFR
ARGTVNPDVETH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 342 |
| 15N chemical shifts | 140 |
| 1H chemical shifts | 844 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Rv0020c_Nter | 1 |
Entities:
Entity 1, Rv0020c_Nter 132 residues - 14773.583 Da.
| 1 | MET | GLY | SER | GLN | LYS | ARG | LEU | VAL | GLN | ARG | ||||
| 2 | VAL | GLU | ARG | LYS | LEU | GLU | GLN | THR | VAL | GLY | ||||
| 3 | ASP | ALA | PHE | ALA | ARG | ILE | PHE | GLY | GLY | SER | ||||
| 4 | ILE | VAL | PRO | GLN | GLU | VAL | GLU | ALA | LEU | LEU | ||||
| 5 | ARG | ARG | GLU | ALA | ALA | ASP | GLY | ILE | GLN | SER | ||||
| 6 | LEU | GLN | GLY | ASN | ARG | LEU | LEU | ALA | PRO | ASN | ||||
| 7 | GLU | TYR | ILE | ILE | THR | LEU | GLY | VAL | HIS | ASP | ||||
| 8 | PHE | GLU | LYS | LEU | GLY | ALA | ASP | PRO | GLU | LEU | ||||
| 9 | LYS | SER | THR | GLY | PHE | ALA | ARG | ASP | LEU | ALA | ||||
| 10 | ASP | TYR | ILE | GLN | GLU | GLN | GLY | TRP | GLN | THR | ||||
| 11 | TYR | GLY | ASP | VAL | VAL | VAL | ARG | PHE | GLU | GLN | ||||
| 12 | SER | SER | ASN | LEU | HIS | THR | GLY | GLN | PHE | ARG | ||||
| 13 | ALA | ARG | GLY | THR | VAL | ASN | PRO | ASP | VAL | GLU | ||||
| 14 | THR | HIS |
Samples:
15N: Rv0020c_Nter, [U-15N], 0.5 ± 0.01 mM
13C-15N: Rv0020c_Nter, [U-13C; U-15N], 0.5 ± 0.01 mM
sample_conditions_1: ionic strength: 100 mM; pH: 6.8; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | 15N | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | 15N | isotropic | sample_conditions_1 |
| 3D HNCA | 13C-15N | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | 13C-15N | isotropic | sample_conditions_1 |
| 3D HNCACB | 13C-15N | isotropic | sample_conditions_1 |
| 3D HNCO | 13C-15N | isotropic | sample_conditions_1 |
| 3D HCACO | 13C-15N | isotropic | sample_conditions_1 |
Software:
GIFA v4.44, Delsuc - processing
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution
CNS v1.2, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
TALOS+ v1.2009.0721.18, Cornilescu, Delaglio and Bax - angle prediction
NMR spectrometers:
- Bruker Avance 700 MHz
- Bruker Avance 500 MHz
Related Database Links:
| PDB | |
| DBJ | BAH24322 BAL63843 BAQ03850 |
| EMBL | CAL70034 CCC25094 CCC42360 CCC62613 CCE35563 |
| GB | AAK44245 ABQ71740 ABR04363 ACT23041 AEB02149 |
| REF | NP_214534 NP_853690 WP_003400376 WP_003899777 WP_003905210 |
| SP | P71590 |
Download simulated HSQC data in one of the following formats:
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or all simulated shifts