BMRB Entry 34454
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR34454
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Title: A New Structural Model of Abeta(1-40) Fibrils PubMed: 32749391
Deposition date: 2019-11-21 Original release date: 2020-07-18
Authors: Bertini, I.; Gonnelli, L.; Luchinat, C.; Mao, J.; Nesi, A.
Citation: Cerofolini, L.; Ravera, E.; Bologna, S.; Wiglenda, T.; Boddrich, A.; Bettina, P.; Benilova, I.; Korsak, M.; Gallo, G.; Rizzo, D.; Gonnelli, L.; Fragai, M.; De Strooper, B.; Wanker, E.; Luchinat, C.. "Mixing Abeta(1-40) and Abeta(1-42) peptides generates unique amyloid fibrils" Chem. Commun. (Camb.) 56, 8830-8833 (2020).
Assembly members:
entity_1, polymer, 40 residues, 4335.852 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
Entity Sequences (FASTA):
entity_1: DAEFRHDSGYEVHHQKLVFF
AEDVGSNKGAIIGLMVGGVV
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 159 |
| 15N chemical shifts | 38 |
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 |
| 11 | unit_11 | 1 |
| 12 | unit_12 | 1 |
| 13 | unit_13 | 1 |
| 14 | unit_14 | 1 |
| 15 | unit_15 | 1 |
| 16 | unit_16 | 1 |
Entities:
Entity 1, unit_1 40 residues - 4335.852 Da.
| 1 | ASP | ALA | GLU | PHE | ARG | HIS | ASP | SER | GLY | TYR | |
| 2 | GLU | VAL | HIS | HIS | GLN | LYS | LEU | VAL | PHE | PHE | |
| 3 | ALA | GLU | ASP | VAL | GLY | SER | ASN | LYS | GLY | ALA | |
| 4 | ILE | ILE | GLY | LEU | MET | VAL | GLY | GLY | VAL | VAL |
Samples:
sample_1: Amyloid beta peptide 1-40, [U-100% 13C; U-100% 15N], 100 uM; ammonium acetate 50 mM
sample_conditions_1: pH: 8.5; pressure: 1 atm; temperature: 283 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 15N-13C NCA | sample_1 | anisotropic | sample_conditions_1 |
| 2D 15N-13C NCO | sample_1 | anisotropic | sample_conditions_1 |
| 3D NCACX | sample_1 | anisotropic | sample_conditions_1 |
| 3D NCOCX | sample_1 | anisotropic | sample_conditions_1 |
| 3D CANCO | sample_1 | anisotropic | sample_conditions_1 |
| 2D 13C-13C DARR (<100 ms) | sample_1 | anisotropic | sample_conditions_1 |
| 2D 15N-13C PAIN | sample_1 | anisotropic | sample_conditions_1 |
| 2D 13C-13C DARR/PDSD (>100 ms) | sample_1 | anisotropic | sample_conditions_1 |
| 2D 13C-13C PAR (10-15 ms) | sample_1 | anisotropic | sample_conditions_1 |
Software:
TopSpin, Bruker Biospin - processing
CARA, Keller and Wuthrich - chemical shift assignment
Sparky, Goddard - chemical shift assignment
HADDOCK, Bonvin - structure calculation
NMR spectrometers:
- Bruker AVANCE II 700 MHz
- Bruker AVANCE III 850 MHz