BMRB Entry 18232
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR18232
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Title: Solid-state NMR assignments for mouse alpha-synuclein fibrils PubMed: 22516611
Deposition date: 2012-01-31 Original release date: 2012-04-23
Authors: Lv, Guohua; Kumar, Ashutosh; Giller, Karin; Orcellet, Maria; Riedel, Dietmar; Fernandez, Claudio; Becker, Stefan
Citation: Lv, Guohua; Kumar, Ashutosh; Giller, Karin; Orcellet, Maria; Riedel, Dietmar; Fernandez, Claudio; Becker, Stefan; Lange, Adam. "Structural Comparison of Mouse and Human -Synuclein Amyloid Fibrils by Solid-State NMR." J. Mol. Biol. 420, 99-111 (2012).
Assembly members:
mouse_alpha-synuclein, polymer, 140 residues, Formula weight is not available
Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
mouse_alpha-synuclein: MDVFMKGLSKAKEGVVAAAE
KTKQGVAEAAGKTKEGVLYV
GSKTKEGVVHGVTTVAEKTK
EQVTNVGGAVVTGVTAVAQK
TVEGAGNIAAATGFVKKDQM
GKGEEGYPQEGILEDMPVDP
GSEAYEMPSEEGYQDYEPEA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 213 |
| 15N chemical shifts | 60 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | mouse alpha-synuclein | 1 |
Entities:
Entity 1, mouse 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 | 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 | THR | 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 | ASN | ILE | ALA | ALA | |
| 10 | ALA | THR | GLY | PHE | VAL | LYS | LYS | ASP | GLN | MET | |
| 11 | GLY | LYS | GLY | GLU | GLU | GLY | TYR | PRO | GLN | GLU | |
| 12 | GLY | ILE | LEU | GLU | ASP | MET | PRO | VAL | ASP | PRO | |
| 13 | GLY | SER | GLU | ALA | TYR | GLU | MET | PRO | SER | GLU | |
| 14 | GLU | GLY | TYR | GLN | ASP | TYR | GLU | PRO | GLU | ALA |
Samples:
sample_1: mouse alpha-synuclein, [U-100% 13C; U-100% 15N], 10 mg; TRIS 25 mM
sample_2: mouse alpha-synuclein, [2-Glucose 13C; U-100% 15N], 10 mg; TRIS 25 mM; DSS 0.1-0.5 mg
sample_3: mouse alpha-synuclein, [1-Glucose 13C; U-100% 15N], 10 mg; TRIS 25 mM; DSS 0.1-0.5 mg
sample_4: mouse alpha-synuclein, mixed 1:1 13C:15N, 10 mg; TRIS 25 mM; DSS 0.1-0.5 mg
sample_conditions_1: pH: 7.5; temperature: 278 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D PDSD 20 ms | sample_1 | solid | sample_conditions_1 |
| 2D PDSD 150 ms | sample_1 | solid | sample_conditions_1 |
| 2D DREAM | sample_1 | solid | sample_conditions_1 |
| 2D NCACX PDSD | sample_1 | solid | sample_conditions_1 |
| 2D NCOCX PDSD | sample_1 | solid | sample_conditions_1 |
| 3D NCACX PDSD | sample_1 | solid | sample_conditions_1 |
| 3D NCOCX PDSD | sample_1 | solid | sample_conditions_1 |
| 2D NCA | sample_1 | solid | sample_conditions_1 |
| 2D NHHC | sample_1 | solid | sample_conditions_1 |
| 2D PDSD 500 ms | sample_2 | solid | sample_conditions_1 |
| 2D PDSD 700 ms | sample_2 | solid | sample_conditions_1 |
| 2D NCA | sample_2 | solid | sample_conditions_1 |
| 2D NCO | sample_2 | solid | sample_conditions_1 |
| 2D NHHC | sample_2 | solid | sample_conditions_1 |
| 2D PDSD 400 ms | sample_3 | solid | sample_conditions_1 |
| 2D NCA | sample_3 | solid | sample_conditions_1 |
| 2D NCO | sample_3 | solid | sample_conditions_1 |
| 2D NHHC | sample_4 | solid | sample_conditions_1 |
| 2D DQ-SQ SPC5 | sample_1 | solid | sample_conditions_1 |
| 2D NCACX DARR | sample_1 | solid | sample_conditions_1 |
| 2D NCOCX DARR | sample_1 | solid | sample_conditions_1 |
Software:
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker Avance 850 MHz
- Bruker Avance 800 MHz