BMRB Entry 25228
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR25228
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: 1H, 13C, and 15N chemical shift assignments for alpha-synuclein (H50Q) PubMed: 25505181
Deposition date: 2014-09-15 Original release date: 2015-09-04
Authors: Waudby, Christopher; Proukakis, Christos; Porcari, Riccardo; Bellotti, Vittorio; Shapira, Anthony; Christodoulou, John; Camilloni, Carlo; Tartaglia, Gian Gaetano; Stoppini, Monica; Verona, Guglielmo; Vendruscolo, Michele; Relini, Annalisa; Penco, Amanda; Cabrita, Lisa; Mullin, Stephen; Paton, Jack; Mangione, Patrizia; Bolognesi, Benedetta
Citation: Porcari, Riccardo; Proukakis, Christos; Waudby, Christopher; Bolognesi, Benedetta; Mangione, Patrizia; Paton, Jack; Mullin, Stephen; Cabrita, Lisa; Penco, Amanda; Relini, Annalisa; Verona, Guglielmo; Vendruscolo, Michele; Stoppini, Monica; Tartaglia, Gian Gaetano; Camilloni, Carlo; Christodoulou, John; Shapira, Anthony; Bellotti, Vittorio. "The H50Q mutation induces a 10-fold decrease in the solubility of alpha-synuclein" J. Biol. Chem. 290, 2395-2404 (2015).
Assembly members:
H50Q, polymer, 140 residues, 14442.0329 Da.
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):
H50Q: MDVFMKGLSKAKEGVVAAAE
KTKQGVAEAAGKTKEGVLYV
GSKTKEGVVQGVATVAEKTK
EQVTNVGGAVVTGVTAVAQK
TVEGAGSIAAATGFVKKDQL
GKNEEGAPQEGILEDMPVDP
DNEAYEMPSEEGYQDYEPEA
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 399 |
15N chemical shifts | 131 |
1H chemical shifts | 275 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | H50Q | 1 |
Entities:
Entity 1, H50Q 140 residues - 14442.0329 Da.
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 | GLN | |
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: H50Q, [U-13C; U-15N], 0.7 mM; sodium phosphate 10.0 mM; NaCl 100.0 mM; NaN3 1e-07 kg/m3; DSS 1e-08 kg/m3; H2O 95%; D2O 5%
sample_conditions_1: pH: 7.500; pressure: 1.000 atm; temperature: 283.000 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
3D HA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
3D BEST-HNCACB | sample_1 | isotropic | sample_conditions_1 |
3D BEST-HNCOCACB | sample_1 | isotropic | sample_conditions_1 |
3D HNHA | sample_1 | isotropic | sample_conditions_1 |
3D BEST-HNCO | sample_1 | isotropic | sample_conditions_1 |
3D BEST-iHNCO | sample_1 | isotropic | sample_conditions_1 |
2D 1H-15N HSQC/HMQC | sample_1 | isotropic | sample_conditions_1 |
Software:
CcpNmr_Analysis v2.4, CCPN - assignment, peak picking
TopSpin v2.1, Bruker - acquisition
nmrPipe v7.5, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker Avance 700 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