BMRB Entry 27027
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR27027
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Title: N-terminally acetylated beta-Synuclein PubMed: 28820253
Deposition date: 2017-02-06 Original release date: 2017-08-23
Authors: Miotto, Marco; Pavese, Mayra; Quintanar, Liliana; Zweckstetter, Markus; Griesinger, Christian; Fernandez, Claudio
Citation: Miotto, Marco; Pavese, Mayra; Quintanar, Liliana; Zweckstetter, Markus; Griesinger, Christian; Fernandez, Claudio. "Bioinorganic Chemistry of Parkinson's Disease: Affinity and Structural Features of Cu(I) Binding to the Full-Length beta-Synuclein Protein" Inorg. Chem. 56, 10387-10395 (2017).
Assembly members:
AcBS, polymer, 135 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
Entity Sequences (FASTA):
AcBS: XMDVFMKGLSMAKEGVVAAA
EKTKQGVTEAAEKTKEGVLY
VGSKTREGVVQGVASVAEKT
KEQASHLGGAVFSGAGNIAA
ATGLVKREEFPTDLKPEEVA
QEAAEEPLIEPLMEPEGESY
EDPPQEEYQEYEPEA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 385 |
| 15N chemical shifts | 126 |
| 1H chemical shifts | 255 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | AcBS | 1 |
Entities:
Entity 1, AcBS 135 residues - Formula weight is not available
| 1 | ACE | MET | ASP | VAL | PHE | MET | LYS | GLY | LEU | SER | ||||
| 2 | MET | ALA | LYS | GLU | GLY | VAL | VAL | ALA | ALA | ALA | ||||
| 3 | GLU | LYS | THR | LYS | GLN | GLY | VAL | THR | GLU | ALA | ||||
| 4 | ALA | GLU | LYS | THR | LYS | GLU | GLY | VAL | LEU | TYR | ||||
| 5 | VAL | GLY | SER | LYS | THR | ARG | GLU | GLY | VAL | VAL | ||||
| 6 | GLN | GLY | VAL | ALA | SER | VAL | ALA | GLU | LYS | THR | ||||
| 7 | LYS | GLU | GLN | ALA | SER | HIS | LEU | GLY | GLY | ALA | ||||
| 8 | VAL | PHE | SER | GLY | ALA | GLY | ASN | ILE | ALA | ALA | ||||
| 9 | ALA | THR | GLY | LEU | VAL | LYS | ARG | GLU | GLU | PHE | ||||
| 10 | PRO | THR | ASP | LEU | LYS | PRO | GLU | GLU | VAL | ALA | ||||
| 11 | GLN | GLU | ALA | ALA | GLU | GLU | PRO | LEU | ILE | GLU | ||||
| 12 | PRO | LEU | MET | GLU | PRO | GLU | GLY | GLU | SER | TYR | ||||
| 13 | GLU | ASP | PRO | PRO | GLN | GLU | GLU | TYR | GLN | GLU | ||||
| 14 | TYR | GLU | PRO | GLU | ALA |
Samples:
sample_1: AcBS, [U-100% 13C; U-100% 15N], 0.2 mM; MES 20 mM; NaCl 100 mM
sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 288 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNHA | sample_1 | isotropic | sample_conditions_1 |
Software:
TOPSPIN v3.1, Bruker Biospin, Keller and Wuthrich - chemical shift assignment, collection, processing
NMR spectrometers:
- Bruker Avance 600 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts