BMRB Entry 30596
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR30596
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Title: S8 phosphorylated beta amyloid 40 fibrils
Deposition date: 2019-03-22 Original release date: 2019-05-31
Authors: Qiang, W.; Hu, Z.
Citation: Hu, Z.; Vugmeyster, L.; Au, D.; Ostrovsky, D.; Sun, Y.; Qiang, W.. "The molecular structure of a "seeding-prone" N-terminal phosphorylated b-amyloid fibril." . ., .-..
Assembly members:
entity_1, polymer, 40 residues, 4335.852 Da.
entity_2PO, non-polymer, 79.980 Da.
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: chemical synthesis
Entity Sequences (FASTA):
entity_1: DAEFRHDSGYEVHHQKLVFF
AEDVGSNKGAIIGLMVGGVV
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 123 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | entity_1, 1 | 1 |
| 2 | entity_1, 2 | 1 |
| 3 | entity_1, 3 | 1 |
| 4 | entity_1, 4 | 1 |
| 5 | entity_1, 5 | 1 |
| 6 | entity_1, 6 | 1 |
| 7 | entity_1, 7 | 1 |
| 8 | entity_1, 8 | 1 |
| 9 | entity_1, 9 | 1 |
| 10 | entity_1, 10 | 1 |
| 11 | entity_2, 1 | 2 |
| 12 | entity_2, 2 | 2 |
| 13 | entity_2, 3 | 2 |
| 14 | entity_2, 4 | 2 |
| 15 | entity_2, 5 | 2 |
| 16 | entity_2, 6 | 2 |
| 17 | entity_2, 7 | 2 |
| 18 | entity_2, 8 | 2 |
| 19 | entity_2, 9 | 2 |
| 20 | entity_2, 10 | 2 |
Entities:
Entity 1, entity_1, 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, entity_2, 1 - H O3 P - 79.980 Da.
| 1 | 2PO |
Samples:
sample_1: beta amyloid peptide, E3, G9, V18, F20, D23, S26, K28, 50 uM; beta amyloid peptide, A2, F4, D7, Y10, V24, G25, 50 uM; beta amyloid peptide, Q15, F19, A21, I31, L34, V36, G37, 50 uM; beta amyloid peptide, V12, E22, G29, A30, M35, 50 uM; beta amyloid peptide, E11, L17, N27, I32, G33, G38, V39, 50 uM; beta amyloid peptide, F19, L34, 50 uM; beta amyloid peptide, E3, F4, V24, G25, S26, 50 uM; beta amyloid peptide, V12, F20, E22, 50 uM; beta amyloid peptide, I31, G33, V39, 50 uM
sample_2: beta amyloid peptide, L17, 2H-CD3, 50 uM; beta amyloid peptide, F19, 2H-ring-D5, 50 uM; beta amyloid peptide, L34, 2H-CD3, 50 uM; beta amyloid peptide, M35, 2H-CD3, 50 uM; beta amyloid peptide, V36, 2H-CD3, 50 uM
sample_3: beta amyloid peptide, A2-CH3, V12-CO, 50 uM; beta amyloid peptide, V18-CO, A21-CH3, 50 uM; beta amyloid peptide, V24-CO, A30-CH3, 50 uM; beta amyloid peptide, G33-CO, V39-Ca, 50 uM; beta amyloid peptide, V36-Ca, G38-CO, 50 uM; beta amyloid peptide, G9-CO, 50 uM
sample_conditions_1: ionic strength: 10 mM; pH: 7.4; pressure: 1 atm; temperature: 280 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D spin diffusion | sample_1 | anisotropic | sample_conditions_1 |
| 1D PITHIRDs-CT | sample_3 | anisotropic | sample_conditions_1 |
| 1D 13C-31P REDOR | sample_3 | anisotropic | sample_conditions_1 |
| 2H relaxation | sample_2 | anisotropic | sample_conditions_1 |
| 2H static | sample_2 | anisotropic | sample_conditions_1 |
Software:
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - chemical shift assignment
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement, structure calculation
NMR spectrometers:
- Bruker AvanceIII 600 MHz
- Bruker AvanceIII 750 MHz