BMRB Entry 17586
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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/BMR17586
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Title: Rv0020c_FHA 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_FHA, polymer, 100 residues, 10888.060 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_FHA: GHGSAGTSVTLQLDDGSGRT
YQLREGSNIIGRGQDAQFRL
PDTGVSRRHLEIRWDGQVAL
LADLNSTNGTTVNNAPVQEW
QLADGDVIRLGHSEIIVRMH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 287 |
| 15N chemical shifts | 114 |
| 1H chemical shifts | 673 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Rv0020c_FHA | 1 |
Entities:
Entity 1, Rv0020c_FHA 100 residues - 10888.060 Da.
| 1 | GLY | HIS | GLY | SER | ALA | GLY | THR | SER | VAL | THR | |
| 2 | LEU | GLN | LEU | ASP | ASP | GLY | SER | GLY | ARG | THR | |
| 3 | TYR | GLN | LEU | ARG | GLU | GLY | SER | ASN | ILE | ILE | |
| 4 | GLY | ARG | GLY | GLN | ASP | ALA | GLN | PHE | ARG | LEU | |
| 5 | PRO | ASP | THR | GLY | VAL | SER | ARG | ARG | HIS | LEU | |
| 6 | GLU | ILE | ARG | TRP | ASP | GLY | GLN | VAL | ALA | LEU | |
| 7 | LEU | ALA | ASP | LEU | ASN | SER | THR | ASN | GLY | THR | |
| 8 | THR | VAL | ASN | ASN | ALA | PRO | VAL | GLN | GLU | TRP | |
| 9 | GLN | LEU | ALA | ASP | GLY | ASP | VAL | ILE | ARG | LEU | |
| 10 | GLY | HIS | SER | GLU | ILE | ILE | VAL | ARG | MET | HIS |
Samples:
15N: Rv0020c_FHA, [U-15N], 0.5 ± 0.01 mM
13C-15N: Rv0020c_FHA, [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 BAN29123 BAQ03850 |
| EMBL | CAL70034 CCC25094 CCC42360 CCC62613 CCE35563 |
| GB | AAK44245 AAS02340 ABK67403 ABQ71740 ABR04363 |
| REF | NP_214534 NP_853690 WP_003400376 WP_003872107 WP_003876793 |
| SP | P71590 |
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