BMRB Entry 16546
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR16546
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Title: Backbone 1H and 15N Chemical Shifts for Disordered A30P alpha-Synuclein PubMed: 20041693
Deposition date: 2009-10-07 Original release date: 2010-01-28
Authors: Bodner, Christina; Dobson, Christopher; Bax, Ad
Citation: Bodner, Christina; Maltsev, Alexander; Dobson, Christopher; Bax, Ad. "Differential phospholipid binding of alpha-synuclein variants implicated in Parkinson's disease revealed by solution NMR spectroscopy." Biochemistry 49, 862-871 (2010).
Assembly members:
A30P_alpha-synuclein, polymer, 140 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
Entity Sequences (FASTA):
A30P_alpha-synuclein: MDVFMKGLSKAKEGVVAAAE
KTKQGVAEAPGKTKEGVLYV
GSKTKEGVVHGVATVAEKTK
EQVTNVGGAVVTGVTAVAQK
TVEGAGSIAAATGFVKKDQL
GKNEEGAPQEGILEDMPVDP
DNEAYEMPSEEGYQDYEPEA
- assigned_chemical_shifts
| Data type | Count |
| 15N chemical shifts | 132 |
| 1H chemical shifts | 132 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | monomer A30P alpha-synuclein | 1 |
Entities:
Entity 1, monomer A30P alpha-synuclein 140 residues - Formula weight is not available
| 1 | MET | ASP | VAL | PHE | MET | LYS | GLY | LEU | SER | LYS | |
| 2 | ALA | LYS | GLU | GLY | VAL | VAL | ALA | ALA | ALA | GLU | |
| 3 | LYS | THR | LYS | GLN | GLY | VAL | ALA | GLU | ALA | PRO | |
| 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: sodium phosphate 20 mM; protein, [U-15N; U-2H], 0.6 mM; H2O 95%; D2O 5%
sample_conditions_1: ionic strength: 20 mM; pH: 6.0; pressure: 1 atm; temperature: 293 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - peak picking
NMR spectrometers:
- Bruker DMX 600 MHz
Related Database Links:
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts