BMRB Entry 17910
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17910
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Title: WT alpha-synuclein fibrils in the presence of phospholipid vesicles PubMed: 22352310
Deposition date: 2011-09-01 Original release date: 2012-02-28
Authors: Comellas, Gemma; Lemkau, Luisel; Zhou, Donghua; George, Julia; Rienstra, Chad
Citation: Comellas, Gemma; Lemkau, Luisel Rodriguez; Zhou, Donghua; George, Julia; Rienstra, Chad Michael. "Structural intermediates during -synuclein fibrillogenesis on phospholipid vesicles." J. Am. Chem. Soc. 134, 5090-5099 (2012).
Assembly members:
wild-type_alpha-synuclein_formed_in_phospholipid_vesicles, polymer, 140 residues, Formula weight is not available
Natural source: Common Name: not available Taxonomy ID: not available Superkingdom: not available Kingdom: not available Genus/species: not available not available
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
wild-type_alpha-synuclein_formed_in_phospholipid_vesicles: MDVFMKGKSKAKEGVVAAAE
KTKQGVAEAAGKTKEGVLYV
GSKTKEGVVHGVATVAEKTK
EQVTNVGGAVVTGVTAVAQK
TVEGAGSIAAATGFVKKDQL
GKNEEGAPQEGILEDMPVDP
DNEAYEMPSEEGYQDYEPEA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 180 |
| 15N chemical shifts | 51 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | alpha-synuclein | 1 |
Entities:
Entity 1, alpha-synuclein 140 residues - Formula weight is not available
| 1 | MET | ASP | VAL | PHE | MET | LYS | GLY | LYS | SER | LYS | |
| 2 | ALA | LYS | GLU | GLY | VAL | VAL | ALA | ALA | ALA | GLU | |
| 3 | LYS | THR | LYS | GLN | GLY | VAL | ALA | GLU | ALA | ALA | |
| 4 | GLY | LYS | THR | LYS | GLU | GLY | VAL | LEU | TYR | VAL | |
| 5 | GLY | SER | LYS | THR | LYS | GLU | GLY | VAL | VAL | HIS | |
| 6 | GLY | VAL | ALA | THR | VAL | ALA | GLU | LYS | THR | LYS | |
| 7 | GLU | GLN | VAL | THR | ASN | VAL | GLY | GLY | ALA | VAL | |
| 8 | VAL | THR | GLY | VAL | THR | ALA | VAL | ALA | GLN | LYS | |
| 9 | THR | VAL | GLU | GLY | ALA | GLY | SER | ILE | ALA | ALA | |
| 10 | ALA | THR | GLY | PHE | VAL | LYS | LYS | ASP | GLN | LEU | |
| 11 | GLY | LYS | ASN | GLU | GLU | GLY | ALA | PRO | GLN | GLU | |
| 12 | GLY | ILE | LEU | GLU | ASP | MET | PRO | VAL | ASP | PRO | |
| 13 | ASP | ASN | GLU | ALA | TYR | GLU | MET | PRO | SER | GLU | |
| 14 | GLU | GLY | TYR | GLN | ASP | TYR | GLU | PRO | GLU | ALA |
Samples:
sample_1: Alpha-synuclein fibrils, [U-100% 13C; U-100% 15N], 64%; Phosphate buffer 50 mM; H2O 36%
sample_conditions_1: ionic strength: 50 mM; pH: 7.4; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| NCACX | sample_1 | isotropic | sample_conditions_1 |
| NCOCX | sample_1 | isotropic | sample_conditions_1 |
| CANCO | sample_1 | isotropic | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment
VNMRJ, Varian - collection
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Varian VNMRS 500 MHz