BMRB Entry 25083
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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/BMR25083
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Title: Backbone 1H, 13C, and 15N Chemical Shift Assignments and NMR structure for potential drug target from Burkholderia thailandensis E264'
Deposition date: 2014-07-09 Original release date: 2014-07-16
Authors: Barnwal, Ravi P; Varani, Gabriele
Citation: Barnwal, Ravi P; Varani, Gabriele. "Backbone 1H, 13C, and 15N Chemical Shift Assignments and NMR structure for potential drug target from Burkholderia thailandensis E264'" To be Published ., .-..
Assembly members:
entity, polymer, 72 residues, 8133.381 Da.
Natural source: Common Name: Burkholderia thailandensis Taxonomy ID: 57975 Superkingdom: Bacteria Kingdom: not available Genus/species: Burkholderia thailandensis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity: MDRIFMTRTEALEFLLKAHQ
TAVDKIGHPSHKQTPADHAA
IEALDRLLLDVRARRVDQFQ
INASAAQIIVTD
- assigned_chemical_shifts
| Data type | Count |
| 1H chemical shifts | 468 |
| 13C chemical shifts | 321 |
| 15N chemical shifts | 76 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity | 1 |
Entities:
Entity 1, entity 72 residues - 8133.381 Da.
| 1 | MET | ASP | ARG | ILE | PHE | MET | THR | ARG | THR | GLU | ||||
| 2 | ALA | LEU | GLU | PHE | LEU | LEU | LYS | ALA | HIS | GLN | ||||
| 3 | THR | ALA | VAL | ASP | LYS | ILE | GLY | HIS | PRO | SER | ||||
| 4 | HIS | LYS | GLN | THR | PRO | ALA | ASP | HIS | ALA | ALA | ||||
| 5 | ILE | GLU | ALA | LEU | ASP | ARG | LEU | LEU | LEU | ASP | ||||
| 6 | VAL | ARG | ALA | ARG | ARG | VAL | ASP | GLN | PHE | GLN | ||||
| 7 | ILE | ASN | ALA | SER | ALA | ALA | GLN | ILE | ILE | VAL | ||||
| 8 | THR | ASP |
Samples:
sample_1: Putative uncharacterized protein (BTH_I2711), [U-95% 13C; U-95% 15N], 7.2 mg/mL
sample_conditions_1: temperature: 298 K; pH: 7.0; pressure: 1 atm
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | 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 C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert, Mumenthaler and Wuthrich - refinement, structure solution
TALOS, Cornilescu, Delaglio and Bax - data analysis
CCPNMR, CCPN - chemical shift assignment, data analysis, peak picking
TOPSPIN, Bruker Biospin - collection, processing
NMR spectrometers:
- Bruker AMX 500 MHz
- Bruker Avance 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts