BMRB Entry 17087
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17087
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Title: Mouse prion protein (121-231) with the mutations Y169A, Y225A, and Y226A.
Deposition date: 2010-07-28 Original release date: 2012-08-02
Authors: Christen, Barbara; Damberger, Fred; Perez, Daniel; Hornemann, Simone; Wuthrich, Kurt
Citation: Christen, Barbara; Damberger, Fred; Perez, Daniel; Hornemann, Simone; Wuthrich, Kurt. "Temperature-dependent conformational exchange in the cellular form of prion proteins" J. Mol. Biol. ., .-..
Assembly members:
Prion with Y169A, Y225A, Y226A mutation, polymer, 114 residues, Formula weight is not available
Natural source: Common Name: Mouse Taxonomy ID: 10090 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Mus musculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
Prion with Y169A, Y225A, Y226A mutation: GSVVGGLGGYMLGSAMSRPM
IHFGNDWEDRYYRENMYRYP
NQVYYRPVDQASNQNNFVHD
CVNITIKQHTVTTTTKGENF
TETDVKMMERVVEQMCVTQY
QKESQAAADGRRSS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 363 |
| 15N chemical shifts | 135 |
| 1H chemical shifts | 784 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | prion | 1 |
Entities:
Entity 1, prion 114 residues - Formula weight is not available
| 1 | GLY | SER | VAL | VAL | GLY | GLY | LEU | GLY | GLY | TYR | ||||
| 2 | MET | LEU | GLY | SER | ALA | MET | SER | ARG | PRO | MET | ||||
| 3 | ILE | HIS | PHE | GLY | ASN | ASP | TRP | GLU | ASP | ARG | ||||
| 4 | TYR | TYR | ARG | GLU | ASN | MET | TYR | ARG | TYR | PRO | ||||
| 5 | ASN | GLN | VAL | TYR | TYR | ARG | PRO | VAL | ASP | GLN | ||||
| 6 | ALA | SER | ASN | GLN | ASN | ASN | PHE | VAL | HIS | ASP | ||||
| 7 | CYS | VAL | ASN | ILE | THR | ILE | LYS | GLN | HIS | THR | ||||
| 8 | VAL | THR | THR | THR | THR | LYS | GLY | GLU | ASN | PHE | ||||
| 9 | THR | GLU | THR | ASP | VAL | LYS | MET | MET | GLU | ARG | ||||
| 10 | VAL | VAL | GLU | GLN | MET | CYS | VAL | THR | GLN | TYR | ||||
| 11 | GLN | LYS | GLU | SER | GLN | ALA | ALA | ALA | ASP | GLY | ||||
| 12 | ARG | ARG | SER | SER |
Samples:
sample_1: prion, [U-99% 13C; U-99% 15N], 1.4 mM; sodium acetate, [U-2H], 10 mM; sodium azide 0.02%; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0.01 M; pH: 4.5; pressure: 1 atm; temperature: 293.2 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
xwinnmr, Bruker Biospin - collection, processing
CARA, Keller and Wuthrich - chemical shift assignment, data analysis
ATHNOS-CANDID v1.2, Herrmann, Guntert and Wuthrich - chemical shift assignment, peak picking
DYANA v1.0.3, Guntert, Mumenthaler and Wuthrich - structure solution
OPALP, Luginbuhl, Guntert, Billeter and Wuthrich - refinement
Molmol, Koradi, Billeter and Wuthrich - data analysis
NMR spectrometers:
- Bruker DRX 500 MHz
- Bruker Avance 900 MHz
- Bruker DRX 750 MHz
- Bruker DRX 600 MHz
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts