BMRB Entry 30421
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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/BMR30421
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Title: Solution structure of the Burkholderia thailandensis transcription antitermination protein NusB (BTH_I1529) - Seattle Structural Genomics Center for Infectious Disease target ButhA.17903.a
Deposition date: 2018-02-28 Original release date: 2018-03-29
Authors: Buchko, G.; Seattle Structural Genomics Center for Infectious Disease, SSGCID
Citation: Buchko, G.; SSGCID, SSGCID. "Solution structure of the Burkholderia thailandensis transcription antitermination protein NusB (BTH_I1529)." . ., .-..
Assembly members:
entity_1, polymer, 149 residues, 16301.551 Da.
Natural source: Common Name: Burkholderia thailandensis Taxonomy ID: 271848 Superkingdom: Bacteria Kingdom: not available Genus/species: Burkholderia thailandensis
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: GPGSMKKSARRQSRELATQG
LYQWLLSNAAPGEIDAQLRG
ALGYDKADKTLLDTILHGVI
REHATLAEAISPSLDRPIDQ
LSPVERAVLLIATYELTHQI
ETPYRVIINEAVELAKTFGG
SDGYKYVNGVLDKLAVKLRP
AETQARRGA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 543 |
| 15N chemical shifts | 147 |
| 1H chemical shifts | 825 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 149 residues - 16301.551 Da.
| 1 | GLY | PRO | GLY | SER | MET | LYS | LYS | SER | ALA | ARG | ||||
| 2 | ARG | GLN | SER | ARG | GLU | LEU | ALA | THR | GLN | GLY | ||||
| 3 | LEU | TYR | GLN | TRP | LEU | LEU | SER | ASN | ALA | ALA | ||||
| 4 | PRO | GLY | GLU | ILE | ASP | ALA | GLN | LEU | ARG | GLY | ||||
| 5 | ALA | LEU | GLY | TYR | ASP | LYS | ALA | ASP | LYS | THR | ||||
| 6 | LEU | LEU | ASP | THR | ILE | LEU | HIS | GLY | VAL | ILE | ||||
| 7 | ARG | GLU | HIS | ALA | THR | LEU | ALA | GLU | ALA | ILE | ||||
| 8 | SER | PRO | SER | LEU | ASP | ARG | PRO | ILE | ASP | GLN | ||||
| 9 | LEU | SER | PRO | VAL | GLU | ARG | ALA | VAL | LEU | LEU | ||||
| 10 | ILE | ALA | THR | TYR | GLU | LEU | THR | HIS | GLN | ILE | ||||
| 11 | GLU | THR | PRO | TYR | ARG | VAL | ILE | ILE | ASN | GLU | ||||
| 12 | ALA | VAL | GLU | LEU | ALA | LYS | THR | PHE | GLY | GLY | ||||
| 13 | SER | ASP | GLY | TYR | LYS | TYR | VAL | ASN | GLY | VAL | ||||
| 14 | LEU | ASP | LYS | LEU | ALA | VAL | LYS | LEU | ARG | PRO | ||||
| 15 | ALA | GLU | THR | GLN | ALA | ARG | ARG | GLY | ALA |
Samples:
sample_1: NusB, [U-99% 13C; U-99% 15N], 1 ± 0.3 mM; sodium chloride 100 ± 0.05 mM; TRIS 20 ± 0.05 mM; DTT 1 ± 0.02 mM
sample_conditions_1: ionic strength: 0.12 M; pH: 7; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-13C HSQC aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 2D Deltas | sample_1 | isotropic | sample_conditions_1 |
| deuterium exchange | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aromatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY aliphatic | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D C(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY v3.13, Goddard - data analysis
CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure calculation
CNS v1.1, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
PSVS v1.5, Bhattacharya and Montelione - peak picking
Felix v2007, Accelrys Software Inc. - processing
NMR spectrometers:
- Varian VXRS 600 MHz
- Agilent VXRS 750 MHz
- Agilent VXRS 800 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts