BMRB Entry 15394
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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/BMR15394
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Title: NMR structure of rabbit prion protein mutation S173N PubMed: 20639199
Deposition date: 2007-07-19 Original release date: 2010-11-15
Authors: Li, Jun; Lin, Donghai
Citation: Wen, Yi; Li, Jun; Yao, Wenming; Xiong, Minqian; Hong, Jing; Peng, Yu; Xiao, Gengfu; Lin, Donghai. "Unique structural characteristics of the rabbit prion protein." J. Biol. Chem. 285, 31682-31693 (2010).
Assembly members:
rpp mutation S173N, polymer, 138 residues, 12512.979 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 mutation S173N: QGGTHNQWGKPSKPKTSMKH
VAPAAAAGAVVGGLGGYMLG
SAMSRPLIHFGNDYEDRYYR
ENMYRYPNQVYYRPVDQYSN
QNNFVHDCVNITVKQHTVTT
TTKGENFTETDIKIMERVVE
QMCITQYQQESQAAYQRA
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 317 |
| 15N chemical shifts | 125 |
| 1H chemical shifts | 715 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | single chain polymers | 1 |
Entities:
Entity 1, single chain polymers 138 residues - 12512.979 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 | PRO | 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 | ASN | 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 | ILE | THR | GLN | TYR | GLN | GLN | GLU | ||||
| 14 | SER | GLN | ALA | ALA | TYR | GLN | ARG | ALA |
Samples:
sample_1: rpp S173N, [U-13C; U-15N], 0.8 – 1 mM; sodium acetate 20 mM
sample_2: rpp S173N, [U-15N], 0.8 – 1 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 |
| 3D HNCACB | 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 | 15399 16328 16616 |
| PDB | |
| EMBL | CBK44083 |
| GB | AAC48697 AAD01554 AAQ81748 AAQ81756 ABL75505 |
| REF | NP_001075490 XP_008254357 XP_008254358 |
| SP | Q95211 |
Download simulated HSQC data in one of the following formats:
CSV: Backbone
or all simulated shifts
SPARKY: Backbone
or all simulated shifts