BMRB Entry 34455
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full
BMRB Entry DOI: doi:10.13018/BMR34455
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry
Citation: Cerofolini, L.; Ravera, E.; Bologna, S.; Wiglenda, T.; Boddrich, A.; Purfurst, B.; Benilova, A.; 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).
PubMed: 32749391
Assembly members:
entity_1, polymer, 40 residues, 4335.852 Da.
entity_2, polymer, 42 residues, 4520.087 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
entity_2: DAEFRHDSGYEVHHQKLVFF
AEDVGSNKGAIIGLMVGGVV
IA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 373 |
| 15N chemical shifts | 82 |
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 | 2 |
| 10 | unit_10 | 2 |
| 11 | unit_11 | 2 |
| 12 | unit_12 | 2 |
| 13 | unit_13 | 2 |
| 14 | unit_14 | 2 |
| 15 | unit_15 | 2 |
| 16 | unit_16 | 2 |
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 |
Entity 2, unit_9 42 residues - 4520.087 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 | ||||
| 5 | ILE | ALA |
Samples:
sample_1: Amyloid-beta peptide 1-40, [U-100% 13C; U-100% 15N], 50 uM; Amyloid-beta peptide 1-42 50 uM; ammonium acetate 50 mM
sample_2: Amyloid-beta peptide 1-40, [U-100% 13C; U-100% 15N], 70 uM; Amyloid-beta peptide 1-42 30 uM; ammonium acetate 50 mM
sample_3: Amyloid-beta peptide 1-40 50 uM; Amyloid-beta peptide 1-42, [U-100% 13C; U-100% 15N], 50 uM; ammonium acetate 50 mM
sample_4: Amyloid-beta peptide 1-40, [U-100% 13C], 50 uM; Amyloid-beta peptide 1-42, [U-100% 15N], 50 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 NCACB | sample_1 | anisotropic | sample_conditions_1 |
| 3D N(CO)CACB | sample_1 | anisotropic | sample_conditions_1 |
| 3D CANCO | sample_1 | anisotropic | sample_conditions_1 |
| 2D 13C 13C SHANGHAI (15-300 ms) | sample_1 | anisotropic | sample_conditions_1 |
| 2D 13C-13C PDSD (400, 800 ms) | sample_1 | anisotropic | sample_conditions_1 |
| 2D 13C-15N PAIN (10 ms) | sample_1 | anisotropic | sample_conditions_1 |
| 2D 15N-13C NCA | sample_2 | anisotropic | sample_conditions_1 |
| 2D 13C-13C DARR (100 ms) | sample_2 | anisotropic | sample_conditions_1 |
| 2D 15N-13C NCA | sample_3 | anisotropic | sample_conditions_1 |
| 2D 15N-13C NCO | sample_3 | anisotropic | sample_conditions_1 |
| 2D 13C-13C SHANGHAI (15-300 ms) | sample_3 | anisotropic | sample_conditions_1 |
| 2D 15N-13C hNhhC | sample_4 | anisotropic | sample_conditions_1 |
Software:
TopSpin, Bruker Biospin - processing
CARA, Keller and Wuthrich - chemical shift assignment
HADDOCK v2.2, Bonvin - structure calculation
MODELLER, Fiser and Sali - structure calculation
NMR spectrometers:
- Bruker AVANCE II 700 MHz
- Bruker AVANCE III 850 MHz
- Bruker AVANCE III 800 MHz