BMRB Entry 36185
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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/BMR36185
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Title: Solution structure of RRM domian of La protein from Trypanosoma brucei PubMed: 30993866
Deposition date: 2018-05-07 Original release date: 2019-05-13
Authors: Shan, F.
Citation: Shan, Fangzhen; Mei, Song; Zhang, Jiahai; Zhang, Xuecheng; Xu, Chao; Liao, Shanhui; Tu, Xiaoming. "A telomerase subunit homolog La protein from Trypanosoma brucei plays an essential role in ribosomal biogenesis" . ., .-..
Assembly members:
RNA binding protein La-like protein, polymer, 99 residues, 11282.726 Da.
Natural source: Common Name: Trypanosoma brucei Taxonomy ID: 5691 Superkingdom: Eukaryota Kingdom: not available Genus/species: Trypanosoma brucei
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
RNA binding protein La-like protein: TDHQTVYVKPVPPTATLEQL
TEFFSKHGTVQAVWRRYFAG
KKDAPPESRTKPSVFVVFNS
SEEAEAFQKAPPMYDDVQLT
AEMKTTYLERKAEEIAAKK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 195 |
| 15N chemical shifts | 91 |
| 1H chemical shifts | 611 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1 | 1 |
Entities:
Entity 1, entity_1 99 residues - 11282.726 Da.
| 1 | THR | ASP | HIS | GLN | THR | VAL | TYR | VAL | LYS | PRO | ||||
| 2 | VAL | PRO | PRO | THR | ALA | THR | LEU | GLU | GLN | LEU | ||||
| 3 | THR | GLU | PHE | PHE | SER | LYS | HIS | GLY | THR | VAL | ||||
| 4 | GLN | ALA | VAL | TRP | ARG | ARG | TYR | PHE | ALA | GLY | ||||
| 5 | LYS | LYS | ASP | ALA | PRO | PRO | GLU | SER | ARG | THR | ||||
| 6 | LYS | PRO | SER | VAL | PHE | VAL | VAL | PHE | ASN | SER | ||||
| 7 | SER | GLU | GLU | ALA | GLU | ALA | PHE | GLN | LYS | ALA | ||||
| 8 | PRO | PRO | MET | TYR | ASP | ASP | VAL | GLN | LEU | THR | ||||
| 9 | ALA | GLU | MET | LYS | THR | THR | TYR | LEU | GLU | ARG | ||||
| 10 | LYS | ALA | GLU | GLU | ILE | ALA | ALA | LYS | LYS |
Samples:
sample_1: RRM, [U-13C; U-15N], 0.5 mM; DTT 2 mM; EDTA 2 mM; sodium chloride 200 mM; sodium phosphate 20 mM; H2O 90%; D2O, [U-2H], 10%
sample_conditions_1: ionic strength: 200 mM; pH: 6.8; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
CYANA, Guntert P., Guntert, Mumenthaler and Wuthrich - refinement, structure calculation
SPARKY, Goddard - chemical shift assignment, peak picking
NMR spectrometers:
- Bruker DMX 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts