BMRB Entry 30121
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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/BMR30121
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: Colvin, M.; Silvers, R.; Ni, Q.; Can, T.; Sergeyev, I.; Rosay, M.; Donovan, K.; Michael, B.; Wall, J.; Linse, S.; Griffin, R.; Colvin, M.; Silvers, R.; Frohm, B.; Su, Y.; Linse, S.; Griffin, R.. "Atomic Resolution Structure of Monomorphic AB42 Amyloid Fibrils." J. Am. Chem. Soc. 138, 9663-9674 (2016).
PubMed: 27355699
Assembly members:
entity_1, 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
IA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 123 |
| 15N chemical shifts | 29 |
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_1, 11 | 1 |
| 12 | entity_1, 12 | 1 |
| 13 | entity_1, 13 | 1 |
| 14 | entity_1, 14 | 1 |
| 15 | entity_1, 15 | 1 |
| 16 | entity_1, 16 | 1 |
| 17 | entity_1, 17 | 1 |
| 18 | entity_1, 18 | 1 |
Entities:
Entity 1, entity_1, 1 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_3: AB42-M01-42, [U-100% 13C; U-100% 15N], 1 g/L; EDTA 0.2 mM; sodium azide 0.02%; sodium phosphate 20 mM
sample_4: AB42-M01-42, [U-30% 13C; U-30% 15N], 1 g/L; EDTA 0.2 mM; sodium azide 0.02%; sodium phosphate 20 mM
sample_5: AB42-M01-42, [1,6-13C-glucose, U-100% 15N], 1 g/L; EDTA 0.2 mM; sodium azide 0.02%; sodium phosphate 20 mM
sample_6: AB42-M01-42, [2-13C-glycerol, U-100% 15N], 1 g/L; EDTA 0.2 mM; sodium azide 0.02%; sodium phosphate 20 mM
sample_conditions_1: ionic strength: 1 mM; pH: 8.0; pressure: 1 atm; temperature: 277 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| PAR 5 ms mixing | sample_3 | isotropic | sample_conditions_1 |
| PAR 10 ms mixing | sample_3 | isotropic | sample_conditions_1 |
| PAR 20 ms mixing | sample_3 | isotropic | sample_conditions_1 |
| PAIN 30 ms mixing | sample_3 | isotropic | sample_conditions_1 |
| DARR 25 ms mixing | sample_3 | isotropic | sample_conditions_1 |
| DARR 100 ms mixing | sample_4 | isotropic | sample_conditions_1 |
| ZF-TEDOR 6.4 ms mixing | sample_5 | isotropic | sample_conditions_1 |
| FS-REDOR | sample_4 | isotropic | sample_conditions_1 |
| FS-REDOR | sample_3 | isotropic | sample_conditions_1 |
| PAR 20 ms mixing | sample_4 | isotropic | sample_conditions_1 |
| DARR 400 ms mixing | sample_6 | isotropic | sample_conditions_1 |
| DARR 100 ms mixing | sample_5 | isotropic | sample_conditions_1 |
| ZF-TEDOR 12 ms mixing | sample_5 | isotropic | sample_conditions_1 |
| 3D CONCA | sample_3 | isotropic | sample_conditions_1 |
| 3D NCOCX | sample_3 | isotropic | sample_conditions_1 |
| 3D NCACX | sample_3 | isotropic | sample_conditions_1 |
Software:
CYANA v3.97, Guntert, Mumenthaler and Wuthrich - refinement
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
SPARKY v3.113, Goddard - chemical shift assignment
TOPSPIN v3.1, Bruker Biospin - collection, processing
NMR spectrometers:
- Bruker AvanceIII 800 MHz
- Home-built RUBEN750 750 MHz
- Bruker AvanceIII 600 MHz