BMRB Entry 34178
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR34178
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Title: Solid-state MAS NMR structure of the HELLF prion amyloid fibrils
Deposition date: 2017-09-25 Original release date: 2018-10-02
Authors: Martinez, D.; Daskalov, A.; Andreas, L.; Bardiaux, B.; Coustou, V.; Stanek, J.; Berbon, M.; Noubhani, M.; Kauffmann, B.; Wall, J.; Pintacuda, G.; Saupe, S.; Habenstein, B.; Loquet, A.
Citation: Martinez, D.; Daskalov, A.; Andreas, L.; Bardiaux, B.; Coustou, V.; Stanek, J.; Berbon, M.; Noubhani, A.; Kauffmann, B.; Wall, J.; Pintacuda, G.; Saupe, S.; Habenstein, B.; Loquet, A.. "Amyloid fold conservation in the twilight zone of sequence similarity" To Be published ., .-..
Assembly members:
entity_1, polymer, 78 residues, 8515.534 Da.
Natural source: Common Name: Pleurage anserina Taxonomy ID: 515849 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Podospora anserina
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
entity_1: MKTLSATRACRTGQKFGEMK
TDDHSIAMQGIVGVAQPGVD
QSFGSLTTTKSSRAFQGQMD
AGSFSNLFSKLEHHHHHH
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 179 |
| 15N chemical shifts | 45 |
| 1H chemical shifts | 258 |
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 |
Entities:
Entity 1, entity_1, 1 78 residues - 8515.534 Da.
| 1 | MET | LYS | THR | LEU | SER | ALA | THR | ARG | ALA | CYS | ||||
| 2 | ARG | THR | GLY | GLN | LYS | PHE | GLY | GLU | MET | LYS | ||||
| 3 | THR | ASP | ASP | HIS | SER | ILE | ALA | MET | GLN | GLY | ||||
| 4 | ILE | VAL | GLY | VAL | ALA | GLN | PRO | GLY | VAL | ASP | ||||
| 5 | GLN | SER | PHE | GLY | SER | LEU | THR | THR | THR | LYS | ||||
| 6 | SER | SER | ARG | ALA | PHE | GLN | GLY | GLN | MET | ASP | ||||
| 7 | ALA | GLY | SER | PHE | SER | ASN | LEU | PHE | SER | LYS | ||||
| 8 | LEU | GLU | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: HELLF protein, U-15N/13C labeled, 1 mM
sample_2: HELLF, (U-14N/13C)/(U-15N/12C)]), 1 mM
sample_conditions_1: pH: 7; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| HhCH | sample_1 | anisotropic | sample_conditions_1 |
| HhNH | sample_1 | anisotropic | sample_conditions_1 |
| HhNH | sample_2 | anisotropic | sample_conditions_1 |
Software:
CcpNMR, CCPN - chemical shift assignment, peak picking
ARIA v2.3.2, Rieping, Habeck, Bardiaux, Bernard, Malliavin, Nilges - structure calculation
CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement
TALOS, Cornilescu, Delaglio and Bax - data analysis
NMR spectrometers:
- Bruker AvanceIII 1000 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts