BMRB Entry 27334
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27334
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Ataxin7N10QT3N9 (Residues:1-62)
Deposition date: 2017-12-07 Original release date: 2018-02-07
Authors: Hu, Hongyu; Hong, Junye
Citation: Hu, Hongyu; Hong, Junye; Wang, Dongdong; Xue, Wei; Yue, Hongwei; Yang, Hui; Jiang, Leilei; Wang, Wenning. "Structural and dynamic studies reveal that the alanine-rich region in the N-terminus of ataxin-7 initiates -helix formation of the polyglutamine tract but inhibits its amyloid aggregation" J. Biol. Chem. ., .-..
Assembly members:
Atx7N10QT3N9, polymer, 62 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: E. coli - cell free Vector: pET-32M
Entity Sequences (FASTA):
Atx7N10QT3N9: MSERAADDVRGEPRRAAAAA
GGAAAAAARQQTQQQQQNQP
PPPQPQRQQHPPPPPRRTRP
ED
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 158 |
| 15N chemical shifts | 43 |
| 1H chemical shifts | 179 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Ataxin7N10QT3N9 | 1 |
Entities:
Entity 1, Ataxin7N10QT3N9 62 residues - Formula weight is not available
| 1 | MET | SER | GLU | ARG | ALA | ALA | ASP | ASP | VAL | ARG | ||||
| 2 | GLY | GLU | PRO | ARG | ARG | ALA | ALA | ALA | ALA | ALA | ||||
| 3 | GLY | GLY | ALA | ALA | ALA | ALA | ALA | ALA | ARG | GLN | ||||
| 4 | GLN | THR | GLN | GLN | GLN | GLN | GLN | ASN | GLN | PRO | ||||
| 5 | PRO | PRO | PRO | GLN | PRO | GLN | ARG | GLN | GLN | HIS | ||||
| 6 | PRO | PRO | PRO | PRO | PRO | ARG | ARG | THR | ARG | PRO | ||||
| 7 | GLU | ASP |
Samples:
sample_1: Atx7N10QT3N9, [U-13C; U-15N], 300 uM; Atx7N10QT3N9, [U-15N], 300 uM
sample_conditions_1: ionic strength: 70 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 CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker Uniform NMR System 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts