BMRB Entry 36715
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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/BMR36715
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
All files associated with the entry
Citation: Liu, W.; Yang, J.; Chang, Z.. "Lipidic-Abeta40 fibril structure analyzed by Solid-state NMR" .
Assembly members:
Amyloid-beta protein 40, polymer, 234 residues, 2651.129 Da.
Natural source: Common Name: human Taxonomy ID: 9606 Superkingdom: not available Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Amyloid-beta protein 40: QKLVFFAEDVGSNKGAIIGL
MVGGVV
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 102 |
| 15N chemical shifts | 25 |
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 |
Entities:
Entity 1, entity_1_1 234 residues - 2651.129 Da.
| 1 | GLN | LYS | LEU | VAL | PHE | PHE | ALA | GLU | ASP | VAL | ||||
| 2 | GLY | SER | ASN | LYS | GLY | ALA | ILE | ILE | GLY | LEU | ||||
| 3 | MET | VAL | GLY | GLY | VAL | VAL |
Samples:
sample_1: Protein (abeta40 fibril), [U-13C; U-15N], 30 % w/w; H2O 50 % w/w
sample_2: Protein (abeta40 fibril), uniformly diluted labelled, 30 % w/w; H2O 50 % w/w
sample_3: Protein (abeta40 fibril), 15N uniformly and [2-13C]-Gly labelled, 30 % w/w; H2O 50 % w/w
sample_4: Protein (abeta40 fibril), 15N uniformly and [2-13C]-Gly diluted labelled, 30 % w/w; H2O 50 % w/w
sample_5: Protein (abeta40 fibril), [1, 3-13C2]-Gly labelled, 30 % w/w; H2O 50 % w/w
sample_6: Protein (abeta40 fibril), [1, 3-13C2]-Gly labelled, 30 % w/w; H2O 50 % w/w
sample_conditions_1: ionic strength: 10 mM; pH: 7.4; pressure: 1 atm; temperature: 273 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D DARR | sample_1 | isotropic | sample_conditions_1 |
| 2D DARR | sample_2 | isotropic | sample_conditions_1 |
| 2D DARR | sample_3 | isotropic | sample_conditions_1 |
| 2D DARR | sample_4 | isotropic | sample_conditions_1 |
| 2D DARR | sample_5 | isotropic | sample_conditions_1 |
| 2D TEDOR | sample_6 | isotropic | sample_conditions_1 |
| 2D NCA | sample_1 | isotropic | sample_conditions_1 |
| 3D NCACX | sample_1 | isotropic | sample_conditions_1 |
| 3D NCOCX | sample_1 | isotropic | sample_conditions_1 |
| 3D NCACX | sample_1 | isotropic | sample_conditions_1 |
Software:
Sparky, Goddard - chemical shift assignment
X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure calculation
Sparky, Goddard - peak picking
NMR spectrometers:
- Bruker AVANCE 800 MHz