BMRB Entry 27071
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27071
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NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Dilworth, David; Upadhyay, Santosh; Bonnafous, Pierre; Edoo, Amiirah Bibi; Bourbigot, Sarah; Pesek-Jardim, Francy; Gudavicius, Geoff; Serpa, Jason; Petrotchenko, Evgeniy; Borchers, Christoph; Nelson, Christopher; Mackereth, Cameron. "The basic tilted helix bundle domain of the prolyl isomerase FKBP25 is a novel double-stranded RNA binding module." Nucleic Acids Res. 45, 11989-12004 (2017).
PubMed: 29036638
Assembly members:
BTHB, polymer, 76 residues, Formula weight is not available
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-His1a
Entity Sequences (FASTA):
BTHB: GAMAAAVPQRAWTVEQLRSE
QLPKKDIIKFLQEHGSDSFL
AEHKLLGNIKNVAKTANKDH
LVTAYNHLFETKRFKG
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 210 |
| 15N chemical shifts | 80 |
| 1H chemical shifts | 90 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | BTHB | 1 |
Entities:
Entity 1, BTHB 76 residues - Formula weight is not available
| 1 | GLY | ALA | MET | ALA | ALA | ALA | VAL | PRO | GLN | ARG | ||||
| 2 | ALA | TRP | THR | VAL | GLU | GLN | LEU | ARG | SER | GLU | ||||
| 3 | GLN | LEU | PRO | LYS | LYS | ASP | ILE | ILE | LYS | PHE | ||||
| 4 | LEU | GLN | GLU | HIS | GLY | SER | ASP | SER | PHE | LEU | ||||
| 5 | ALA | GLU | HIS | LYS | LEU | LEU | GLY | ASN | ILE | LYS | ||||
| 6 | ASN | VAL | ALA | LYS | THR | ALA | ASN | LYS | ASP | HIS | ||||
| 7 | LEU | VAL | THR | ALA | TYR | ASN | HIS | LEU | PHE | GLU | ||||
| 8 | THR | LYS | ARG | PHE | LYS | GLY |
Samples:
sample_1: BTHB, [U-99% 13C; U-99% 15N], 310 uM; sodium phosphate 20 mM; sodium chloride 150 mM; D2O, [U-99% 2H], 10 % v/v
sample_conditions_1: ionic strength: 170 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - chemical shift assignment, data analysis, peak picking
TOPSPIN v3.5, Bruker Biospin - collection
NMR spectrometers:
- Bruker Avance 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated peaks
SPARKY: Backbone
or all simulated peaks