BMRB Entry 27348
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR27348
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Title: 1H, 13C and 15N assignment of C', CA, N and HN of intrinsically disordered alpha-synuclein near-phsysiological conditions PubMed: 29492731
Deposition date: 2017-12-22 Original release date: 2018-03-08
Authors: Schiavina, Marco; Murrali, Maria Grazia; Sainati, Valerio; Bermel, Wolfgang; Pierattelli, Roberta; Felli, Isabella
Citation: Murrali, Maria Grazia; Schiavina, Marco; Sainati, Valerio; Bermel, Wolfgang; Pierattelli, Roberta; Felli, Isabella. "13C APSY-NMR for sequential assignment of intrinsically disordered proteins" J. Biomol. NMR 70, 167-175 (2018).
Assembly members:
intrinsically_disordered_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 Vector: pT7-7
Entity Sequences (FASTA):
intrinsically_disordered_alpha-synuclein: MDVFMKGLSKAKEGVVAAAE
KTKQGVAEAAGKTKEGVLYV
GSKTKEGVVHGVATVAEKTK
EQVTNVGGAVVTGVTAVAQK
TVEGAGSIAAATGFVKKDQL
GKNEEGAPQEGILEDMPVDP
DNEAYEMPSEEGYQDYEPEA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 273 |
| 15N chemical shifts | 139 |
| 1H chemical shifts | 93 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | intrinsically disordered alpha-synuclein | 1 |
Entities:
Entity 1, intrinsically disordered 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 | 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: intrinsically disordered alpha-synuclein, [U-13C; U-15N], 1.0 mM; KPI 20 mM; EDTA 0.5 mM; NaCl 200 mM; H2O 90%; D2O, [U-2H], 10%
sample_conditions_1: pH: 6.5; temperature: 315 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 5D APSY-(HCA)CONCACON | sample_1 | isotropic | sample_conditions_1 |
| 3D APSY-HNCO | sample_1 | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 2D CON | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v4.0.1, Bruker Biospin - chemical shift assignment
NMR spectrometers:
- Bruker Avance NEO 700 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts