BMRB Entry 25325
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR25325
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Title: NMR Chemical Shifts of the hybrid protein Beta-Synuclien HC
Deposition date: 2014-11-10 Original release date: 2015-09-03
Authors: Allison, Jane; Rivers, Robert; Christodoulou, John; Vendruscolo, Michele; Dobson, Christopher
Citation: Allison, Jane; Rivers, Robert; Christodoulou, John; Vendruscolo, Michele; Dobson, Christopher. "A relationship between the transient structure in the monomeric state and the aggregation propensities" Biochemistry ., .-..
Assembly members:
beta-synuclein_HC, polymer, 145 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):
beta-synuclein_HC: MDVFMKGLSMAKEGVVAAAE
KTKQGVTEAAEKTKEGVLYV
GSKTREGVVQGVASVAEKTK
EQASHLGGAVFSGVTAVAQK
TVEGAGNIAAATGLVKREEF
PTDLKPEEVAQEAAEEPLIE
PLMEPEGESYEDPPQEEYQE
YEPEA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 260 |
| 15N chemical shifts | 133 |
| 1H chemical shifts | 133 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | Beta-synuclein HC | 1 |
Entities:
Entity 1, Beta-synuclein HC 145 residues - Formula weight is not available
| 1 | MET | ASP | VAL | PHE | MET | LYS | GLY | LEU | SER | MET | ||||
| 2 | ALA | LYS | GLU | GLY | VAL | VAL | ALA | ALA | ALA | GLU | ||||
| 3 | LYS | THR | LYS | GLN | GLY | VAL | THR | GLU | ALA | ALA | ||||
| 4 | GLU | LYS | THR | LYS | GLU | GLY | VAL | LEU | TYR | VAL | ||||
| 5 | GLY | SER | LYS | THR | ARG | GLU | GLY | VAL | VAL | GLN | ||||
| 6 | GLY | VAL | ALA | SER | VAL | ALA | GLU | LYS | THR | LYS | ||||
| 7 | GLU | GLN | ALA | SER | HIS | LEU | GLY | GLY | ALA | VAL | ||||
| 8 | PHE | SER | GLY | VAL | THR | ALA | VAL | ALA | GLN | LYS | ||||
| 9 | THR | VAL | GLU | GLY | ALA | GLY | ASN | ILE | ALA | ALA | ||||
| 10 | ALA | THR | GLY | LEU | VAL | LYS | ARG | GLU | GLU | PHE | ||||
| 11 | PRO | THR | ASP | LEU | LYS | PRO | GLU | GLU | VAL | ALA | ||||
| 12 | GLN | GLU | ALA | ALA | GLU | GLU | PRO | LEU | ILE | GLU | ||||
| 13 | PRO | LEU | MET | GLU | PRO | GLU | GLY | GLU | SER | TYR | ||||
| 14 | GLU | ASP | PRO | PRO | GLN | GLU | GLU | TYR | GLN | GLU | ||||
| 15 | TYR | GLU | PRO | GLU | ALA |
Samples:
sample: beta-synuclein HC, [U-99% 13C; U-99% 15N], 150 uM; NaCl 100 mM; Phosphate Buffer 10 mM; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 100 mM; pH: 7.4; pressure: 1 atm; temperature: 283 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D CBCA(CO)NH | sample | isotropic | sample_conditions_1 |
| 3D HNCO | sample | isotropic | sample_conditions_1 |
| 2D 1H-15N HSQC | sample | isotropic | sample_conditions_1 |
Software:
SPARKY v3.114, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax, Goddard - chemical shift assignment
NMR spectrometers:
- Bruker Avance 700 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts