BMRB Entry 16722
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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/BMR16722
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Title: mPrP_D167S PubMed: 20460128
Deposition date: 2010-02-12 Original release date: 2010-05-18
Authors: Perez, Daniel; Damberger, Fred; Wuthrich, Kurt
Citation: Perez, Daniel; Damberger, Fred; Wuthrich, Kurt. "Horse prion protein NMR structure and comparisons with related variants of the mouse prion protein." J. Mol. Biol. 400, 121-128 (2010).
Assembly members:
mouse prion protein double mutant D167S, N173K, polymer, 113 residues, 13203.797 Da.
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):
mouse prion protein double mutant D167S, N173K: SVVGGLGGYMLGSAMSRPMI
HFGNDWEDRYYRENMYRYPN
QVYYRPVSQYSNQNNFVHDC
VNITIKQHTVTTTTKGENFT
ETDVKMMERVVEQMCVTQYQ
KESQAYYDGRRSS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 367 |
| 15N chemical shifts | 134 |
| 1H chemical shifts | 790 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | mouse prion protein double mutant D167S, N173K | 1 |
Entities:
Entity 1, mouse prion protein double mutant D167S, N173K 113 residues - 13203.797 Da.
| 1 | SER | VAL | VAL | GLY | GLY | LEU | GLY | GLY | TYR | MET | ||||
| 2 | LEU | GLY | SER | ALA | MET | SER | ARG | PRO | MET | ILE | ||||
| 3 | HIS | PHE | GLY | ASN | ASP | TRP | GLU | ASP | ARG | TYR | ||||
| 4 | TYR | ARG | GLU | ASN | MET | TYR | ARG | TYR | PRO | ASN | ||||
| 5 | GLN | VAL | TYR | TYR | ARG | PRO | VAL | SER | GLN | TYR | ||||
| 6 | SER | ASN | GLN | ASN | ASN | PHE | VAL | HIS | ASP | CYS | ||||
| 7 | VAL | ASN | ILE | THR | ILE | LYS | GLN | HIS | THR | VAL | ||||
| 8 | THR | THR | THR | THR | LYS | GLY | GLU | ASN | PHE | THR | ||||
| 9 | GLU | THR | ASP | VAL | LYS | MET | MET | GLU | ARG | VAL | ||||
| 10 | VAL | GLU | GLN | MET | CYS | VAL | THR | GLN | TYR | GLN | ||||
| 11 | LYS | GLU | SER | GLN | ALA | TYR | TYR | ASP | GLY | ARG | ||||
| 12 | ARG | SER | SER |
Samples:
sample_1: sodium acetate, [U-2H], 10 ± 1 mM; H2O 90%; D2O 10%; entity 1.3 mM
sample_conditions_1: ionic strength: 10 mM; pH: 4.5; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 1H-15N NOESY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCA | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-15N TOCSY | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D 1H-13C NOESY | sample_1 | isotropic | sample_conditions_1 |
Software:
ATHNOS-CANDID, Herrmann and Wuthrich - automatic peak picking and NOE assignment
NMR spectrometers:
- Bruker DRX 750 MHz
- Bruker DRX 600 MHz
- Bruker DRX 500 MHz
Related Database Links:
| BMRB | 15845 16071 16075 16076 16077 16078 16079 16080 16184 16185 16723 17081 17082 17084 17174 17213 17758 17759 |
| PDB | |
| DBJ | BAA08790 BAE28320 BAE28693 BAE29994 BAE34221 |
| EMBL | CAJ18553 |
| GB | AAA39996 AAA39997 AAA39998 AAA41947 AAB30728 |
| REF | NP_001265185 NP_035300 NP_036763 XP_006235124 |
| SP | P04925 P13852 Q9Z0T3 |
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