BMRB Entry 16720
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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/BMR16720
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Title: Horse prion protein 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 mutant D167S, polymer, 113 residues, 13203.797 Da.
Natural source: Common Name: Horse Taxonomy ID: 9796 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Equus caballus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
mouse prion protein mutant D167S: GSVVGGLGGYMLGSAMSRPL
IHFGNDYEDRYYRENMYRYP
NQVYYRPVSEYSNQKNFVHD
CVNITVKQHTVTTTTKGENF
TETDVKIMERVVEQMCITQY
QKEYEAFQQRGAS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 366 |
| 15N chemical shifts | 131 |
| 1H chemical shifts | 424 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | mouse prion protein mutant D167S | 1 |
Entities:
Entity 1, mouse prion protein mutant D167S 113 residues - 13203.797 Da.
| 1 | GLY | SER | VAL | VAL | GLY | GLY | LEU | GLY | GLY | TYR | ||||
| 2 | MET | LEU | GLY | SER | ALA | MET | SER | ARG | PRO | LEU | ||||
| 3 | ILE | HIS | PHE | GLY | ASN | ASP | TYR | GLU | ASP | ARG | ||||
| 4 | TYR | TYR | ARG | GLU | ASN | MET | TYR | ARG | TYR | PRO | ||||
| 5 | ASN | GLN | VAL | TYR | TYR | ARG | PRO | VAL | SER | GLU | ||||
| 6 | TYR | SER | ASN | GLN | LYS | ASN | PHE | VAL | HIS | ASP | ||||
| 7 | CYS | VAL | ASN | ILE | THR | VAL | LYS | GLN | HIS | THR | ||||
| 8 | VAL | THR | THR | THR | THR | LYS | GLY | GLU | ASN | PHE | ||||
| 9 | THR | GLU | THR | ASP | VAL | LYS | ILE | MET | GLU | ARG | ||||
| 10 | VAL | VAL | GLU | GLN | MET | CYS | ILE | THR | GLN | TYR | ||||
| 11 | GLN | LYS | GLU | TYR | GLU | ALA | PHE | GLN | GLN | ARG | ||||
| 12 | GLY | ALA | SER |
Samples:
sample_1: sodium acetate, [U-2H], 10 ± 1 mM; H2O 90%; D2O 10%; entity 1.3 ± 1 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:
| PDB | |
| DBJ | BAD72795 |
| GB | AAD19983 AAD19988 AAD19989 AAD20000 AAN16505 |
| REF | NP_001137270 XP_008518008 XP_008518010 |