BMRB Entry 50888
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR50888
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Title: 1H 15N 13C chemical shift assignment of the construct of human ataxin-3 including residues 182-291 PubMed: 34262938
Deposition date: 2021-04-10 Original release date: 2021-08-16
Authors: Invernizzi, Gaetano; Lambrughi, Matteo; Lindorff-Larsen, Kresten; Papaleo, Elena; Teilum, Kaare
Citation: Lambrughi, Matteo; Maiani, Emiliano; Fas, Burcu; Shaw, Gary; Kragelund, Birthe; Lindorff-Larsen, Kresten; Teilum, Kaare; Invernizzi, Gaetano; Papaleo, Elena. "Ubiquitin Interacting Motifs: duality between structured and disordered motifs" Front. Mol. Biosci. 8, 676235-676235 (2021).
Assembly members:
entity_1, polymer, 114 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: pGEX-6P-1
Entity Sequences (FASTA):
entity_1: GPLGSVQQMHRPKLIGEELA
QLKEQRVHKTDLERMLEAND
GSGMLDEDEEDLQRALALSR
QEIDMEDEEADLRRAIQLSM
QGSSRNISQDMTQTSGTNLT
SEELRKRREAYFEK
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 375 |
| 15N chemical shifts | 104 |
| 1H chemical shifts | 102 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | ataxin-3 | 1 |
Entities:
Entity 1, ataxin-3 114 residues - Formula weight is not available
Residues 1-5 are residuals from the glutathione S-transferase (GST) tag. The sequence includes the disordered region between the Josephin domain and the polyglutamine tract of ataxin-3.
| 1 | GLY | PRO | LEU | GLY | SER | VAL | GLN | GLN | MET | HIS | ||||
| 2 | ARG | PRO | LYS | LEU | ILE | GLY | GLU | GLU | LEU | ALA | ||||
| 3 | GLN | LEU | LYS | GLU | GLN | ARG | VAL | HIS | LYS | THR | ||||
| 4 | ASP | LEU | GLU | ARG | MET | LEU | GLU | ALA | ASN | ASP | ||||
| 5 | GLY | SER | GLY | MET | LEU | ASP | GLU | ASP | GLU | GLU | ||||
| 6 | ASP | LEU | GLN | ARG | ALA | LEU | ALA | LEU | SER | ARG | ||||
| 7 | GLN | GLU | ILE | ASP | MET | GLU | ASP | GLU | GLU | ALA | ||||
| 8 | ASP | LEU | ARG | ARG | ALA | ILE | GLN | LEU | SER | MET | ||||
| 9 | GLN | GLY | SER | SER | ARG | ASN | ILE | SER | GLN | ASP | ||||
| 10 | MET | THR | GLN | THR | SER | GLY | THR | ASN | LEU | THR | ||||
| 11 | SER | GLU | GLU | LEU | ARG | LYS | ARG | ARG | GLU | ALA | ||||
| 12 | TYR | PHE | GLU | LYS |
Samples:
sample_1: ataxin-3, [U-100% 13C; U-100% 15N], 0.5 mM; sodium chloride 150 mM; D2O 10%; Phosphate Buffered Saline buffer 90%
sample_conditions_1: pH: 7.4; pressure: 1 atm; temperature: 298.15 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CO)CA | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCANH | sample_1 | isotropic | sample_conditions_1 |
| 3D CC(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D H(CCO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe - processing
CcpNMR - chemical shift assignment
VNMRj - collection
NMR spectrometers:
- Varian INOVA 800 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts