BMRB Entry 31068
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR31068
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Title: STRUCTURE OF ALPHA-SYNUCLEIN FIBRILS DERIVED FROM HUMAN LEWY BODY DEMENTIA TISSUE
Deposition date: 2023-01-05 Original release date: 2023-02-14
Authors: Barclay, A.; Dhavale, D.; Borcik, C.; Rau, M.; Basore, K.; Milchberg, M.; Warmuth, O.; Kotzbauer, P.; Rienstra, C.
Citation: Barclay, A.; Dhavale, D.; Borcik, C.; Milchberg, M.; Warmuth, O.; Kotzbauer, P.; Rienstra, C.. "STRUCTURE OF ALPHA-SYNUCLEIN FIBRILS DERIVED FROM HUMAN LEWY BODY DEMENTIA TISSUE" .
Assembly members:
entity_1, polymer, 140 residues, 14476.108 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 BL21(DE3) Vector: PET28A-AS
Entity Sequences (FASTA):
entity_1: MDVFMKGLSKAKEGVVAAAE
KTKQGVAEAAGKTKEGVLYV
GSKTKEGVVHGVATVAEKTK
EQVTNVGGAVVTGVTAVAQK
TVEGAGSIAAATGFVKKDQL
GKNEEGAPQEGILEDMPVDP
DNEAYEMPSEEGYQDYEPEA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 190 |
| 15N chemical shifts | 47 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | unit_1 | 1 |
| 2 | unit_2 | 1 |
| 3 | unit_3 | 1 |
| 4 | unit_4 | 1 |
| 5 | unit_5 | 1 |
| 6 | unit_6 | 1 |
| 7 | unit_7 | 1 |
| 8 | unit_8 | 1 |
| 9 | unit_9 | 1 |
| 10 | unit_10 | 1 |
Entities:
Entity 1, unit_1 140 residues - 14476.108 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 | 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-100% 13C; U-100% 15N], 66%
sample_2: ALPHA-SYNUCLEIN, [U-100% 2H; U-100% 13C; U-100% 15N], 66%
sample_3: ALPHA-SYNUCLEIN 80%; labelled ALPHA-SYNUCLEIN, [U-25% 2-13C GLYCEROL; U-100% 15N], 20%
sample_conditions_1: ionic strength: 100 mM; pH: 7.6; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D CC DARR | sample_1 | isotropic | sample_conditions_1 |
| 2D NCO | sample_3 | isotropic | sample_conditions_1 |
| 2D NCA | sample_3 | isotropic | sample_conditions_1 |
| 2D CC DARR | sample_3 | isotropic | sample_conditions_1 |
| 2D CC FPRFDR | sample_2 | isotropic | sample_conditions_1 |
| 2D CACO CTUC-COSY | sample_2 | isotropic | sample_conditions_1 |
| 4D HN[HH]NH RFDR | sample_2 | isotropic | sample_conditions_1 |
| 3D N[HH]NH RFDR | sample_2 | isotropic | sample_conditions_1 |
| 3D CA[HH]NH RFDR | sample_2 | isotropic | sample_conditions_1 |
| 3D CAN[H]H RFDR | sample_2 | isotropic | sample_conditions_1 |
| 3D CO[CA]NH RFDR | sample_2 | isotropic | sample_conditions_1 |
| 3D CA[CO]NH RFDR | sample_2 | isotropic | sample_conditions_1 |
| 3D CONH | sample_2 | isotropic | sample_conditions_1 |
| 3D CANH | sample_2 | isotropic | sample_conditions_1 |
| 1D C FSREDOR | sample_1 | isotropic | sample_conditions_1 |
| 3D NCACX PAR | sample_1 | isotropic | sample_conditions_1 |
| 3D CCC RFDR THEN PAR | sample_1 | isotropic | sample_conditions_1 |
| 2D CC PAR | sample_1 | isotropic | sample_conditions_1 |
| 3D CANCO | sample_1 | isotropic | sample_conditions_1 |
| 3D NCOCA SPC5 | sample_1 | isotropic | sample_conditions_1 |
| 3D NCOCX DARR | sample_1 | isotropic | sample_conditions_1 |
| 3D NCACX DARR | sample_1 | isotropic | sample_conditions_1 |
| 2D NCO | sample_1 | isotropic | sample_conditions_1 |
| 2D NCA | sample_1 | isotropic | sample_conditions_1 |
| 2D CC DARR | sample_1 | isotropic | sample_conditions_1 |
| 3D CANCO | sample_1 | isotropic | sample_conditions_1 |
| 3D NCOCX DARR | sample_1 | isotropic | sample_conditions_1 |
| 3D NCACX DARR | sample_1 | isotropic | sample_conditions_1 |
| 2D CC SPC7 | sample_1 | isotropic | sample_conditions_1 |
Software:
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation
NMRFAM-SPARKY, LEE, TONELLI and MARKLEY, LEE, TONELLI, and MARKLEY - chemical shift assignment, peak picking
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis, processing
NMR spectrometers:
- Agilent VNMRS 750 MHz
- Agilent VNMRS 500 MHz