BMRB Entry 17649
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17649
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Title: Partial 13C, 15N chemical shift assignments of A53T alpha-synuclein fibrils PubMed: 21718702
Deposition date: 2011-05-13 Original release date: 2011-07-07
Authors: Comellas, Gemma; Lemkau, Luisel; Nieuwkoop, Andrew; Kloepper, Kathryn; Ladror, Daniel; Ebisu, Reika; Woods, Wendy; Lipton, Andrew; George, Julia; Rienstra, Chad
Citation: Comellas, Gemma; Lemkau, Luisel; Nieuwkoop, Andrew; Kloepper, Kathryn; Ladror, Daniel; Ebisu, Reika; Woods, Wendy; Lipton, Andrew; George, Julia; Rienstra, Chad. "Structured Regions of -Synuclein Fibrils Include the Early-Onset Parkinson's Disease Mutation Sites." J. Mol. Biol. 411, 881-895 (2011).
Assembly members:
A53T_alpha-synuclein_fibrils, polymer, 140 residues, Formula weight is not available
Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
A53T_alpha-synuclein_fibrils: MDVFMKGKSKAKEGVVAAAE
KTKQGVAEAAGKTKEGVLYV
GSKTKEGVVHGVTTVAEKTK
EQVTNVGGAVVTGVTAVAQK
TVEGAGSIAAATGFVKKDQL
GKNEEGAPQEGILEDMPVDP
DNEAYEMPSEEGYQDYEPEA
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 44 |
15N chemical shifts | 14 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | A53T alpha-synuclein | 1 |
Entities:
Entity 1, A53T alpha-synuclein 140 residues - Formula weight is not available
1 | MET | ASP | VAL | PHE | MET | LYS | GLY | LYS | 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 | THR | 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: A53T alpha-synuclein fibrils, [U-13C; U-15N], mM; H2O 36%
sample_conditions_1: ionic strength: 0.05 M; pH: 7.5; pressure: 1 atm; temperature: 10 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
NCACX 50 ms DARR | sample_1 | isotropic | sample_conditions_1 |
NCOCX 50 ms DARR | sample_1 | isotropic | sample_conditions_1 |
CANcoCX 50 ms DARR | sample_1 | isotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY, Goddard - data analysis
NMR spectrometers:
- Varian UnityPlus 600 MHz
Related Database Links:
BMRB | 16300 16302 16342 16543 16546 16547 16548 16904 16939 17214 17498 17648 17654 17665 17910 18207 18208 18243 18857 18860 19257 19337 19338 19344 19345 19350 19351 25227 25228 |
PDB | |
DBJ | BAB29375 BAF82858 BAG73790 |
EMBL | CAG33339 CAG46454 |
GB | AAA16117 AAC02114 AAG30302 AAH13293 AAI08276 |
REF | NP_000336 NP_001009158 NP_001032222 NP_001129014 NP_001139526 |
SP | P37840 P61139 P61140 P61142 P61143 |