BMRB Entry 15399
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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/BMR15399
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Title: NMR structure of rabbit prion protein mutation I214V PubMed: 20949107
Deposition date: 2007-07-20 Original release date: 2010-10-19
Authors: Li, Jun; Lin, Donghai
Citation: Wen, Yi; Li, Jun; Xiong, Minqian; Peng, Yu; Yao, Wenming; Hong, Jing; Lin, Donghai. "Solution Structure and Dynamics of the I214V Mutant of the Rabbit Prion Protein." PLoS ONE 5, e13273-. (2010).
Assembly members:
rpp I214V, polymer, 138 residues, 12471.928 Da.
Natural source: Common Name: rabbit Taxonomy ID: 9986 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Oryctolagus cuniculus
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
rpp I214V: QGGTHNQWGKPSKPKTSMKH
VAGAAAAGAVVGGLGGYMLG
SAMSRPLIHFGNDYEDRYYR
ENMYRYPNQVYYRPVDQYSN
QNSFVHDCVNITVKQHTVTT
TTKGENFTETDIKIMERVVE
QMCVTQYQQESQAAYQRA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 532 |
| 15N chemical shifts | 156 |
| 1H chemical shifts | 926 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | rpp I214V | 1 |
Entities:
Entity 1, rpp I214V 138 residues - 12471.928 Da.
| 1 | GLN | GLY | GLY | THR | HIS | ASN | GLN | TRP | GLY | LYS | ||||
| 2 | PRO | SER | LYS | PRO | LYS | THR | SER | MET | LYS | HIS | ||||
| 3 | VAL | ALA | GLY | ALA | ALA | ALA | ALA | GLY | ALA | VAL | ||||
| 4 | VAL | GLY | GLY | LEU | GLY | GLY | TYR | MET | LEU | GLY | ||||
| 5 | SER | ALA | MET | SER | ARG | PRO | LEU | ILE | HIS | PHE | ||||
| 6 | GLY | ASN | ASP | TYR | GLU | ASP | ARG | TYR | TYR | ARG | ||||
| 7 | GLU | ASN | MET | TYR | ARG | TYR | PRO | ASN | GLN | VAL | ||||
| 8 | TYR | TYR | ARG | PRO | VAL | ASP | GLN | TYR | SER | ASN | ||||
| 9 | GLN | ASN | SER | PHE | VAL | HIS | ASP | CYS | VAL | ASN | ||||
| 10 | ILE | THR | VAL | LYS | GLN | HIS | THR | VAL | THR | THR | ||||
| 11 | THR | THR | LYS | GLY | GLU | ASN | PHE | THR | GLU | THR | ||||
| 12 | ASP | ILE | LYS | ILE | MET | GLU | ARG | VAL | VAL | GLU | ||||
| 13 | GLN | MET | CYS | VAL | THR | GLN | TYR | GLN | GLN | GLU | ||||
| 14 | SER | GLN | ALA | ALA | TYR | GLN | ARG | ALA |
Samples:
sample_1: rpp I214V, [U-13C; U-15N], 0.7 – 0.8 mM; sodium acetate 20 mM
sample_conditions_1: pH: 4.5; pressure: 1 atm; temperature: 298.13 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
Software:
ARIA, Linge, O, . - structure solution
SPARKY, Goddard - chemical shift assignment
NMR spectrometers:
- Varian INOVA 600 MHz
Related Database Links:
| BMRB | 15394 16328 16616 |
| PDB | |
| GB | AAC48697 AAD01554 ABL75505 AEM44421 AEM44422 |
| REF | NP_001075490 XP_008254357 XP_008254358 |
| SP | Q95211 |
Download simulated HSQC data in one of the following formats:
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SPARKY: Backbone
or all simulated shifts