BMRB Entry 52380
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR52380
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Title: Solid-state NMR backbone chemical shift assignments of a-synuclein amyloid fibrils at fast MAS regime
Deposition date: 2024-03-31 Original release date: 2024-04-03
Authors: Toleikis, Zigmantas; Paluch, Piotr; Kuc, Ewelina; Petkus, Jana; Sulskis, Darius; Org-Tago, Mai-Liis; Samoson, Ago; Smirnovas, Vytautas; Stanek, Jan; Lends, Alons
Citation: Toleikis, Zigmantas; Paluch, Piotr; Kuc, Ewelina; Petkus, Jana; Sulskis, Darius; Org-Tago, Mai-Liis; Samoson, Ago; Smirnovas, Vytautas; Stanek, Jan; Lends, Alons. "Solid-state NMR backbone chemical shift assignments of a-synuclein amyloid fibrils at fast MAS regime" Biomol. NMR Assignments ., .-..
Assembly members:
entity_1, 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: pRK172
Entity Sequences (FASTA):
entity_1: MDVFMKGLSKAKEGVVAAAE
KTKQGVAEAAGKTKEGVLYV
GSKTKEGVVHGVATVAEKTK
EQVTNVGGAVVTGVTAVAQK
TVEGAGSIAAATGFVKKDQL
GKNEEGAPQEGILEDMPVDP
DNEAYEMPSEEGYQDYEPEA
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 166 |
15N chemical shifts | 59 |
1H chemical shifts | 59 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | alpha-synuclein | 1 |
Entities:
Entity 1, 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: alpha-synuclein, [U-13C; U-15N; U-2H], 1 mg
sample_conditions_1: ionic strength: 0.137 M; pH: 7.4; pressure: 1 atm; temperature: 293 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
2D hNH | sample_1 | isotropic | sample_conditions_1 |
3D hCaNH | sample_1 | isotropic | sample_conditions_1 |
3D hCONH | sample_1 | isotropic | sample_conditions_1 |
3D hcaCbcaNH | sample_1 | isotropic | sample_conditions_1 |
3D hcoCacoNH | sample_1 | isotropic | sample_conditions_1 |
hcaCbcacoNH | sample_1 | isotropic | sample_conditions_1 |
Software:
CcpNMR v2.4.2 - chemical shift assignment
TOPSPIN v3.4.5 - collection
NMR spectrometers:
- Bruker Avance III HD 800 MHz 18.8 MHz
Download HSQC peak lists in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts