BMRB Entry 17757
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR17757
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Title: Backbone 1H and 13C Chemical Shift Assignments of human prion protein (residues 121-230) in its reduced state PubMed: 19882604
Deposition date: 2011-07-05 Original release date: 2011-07-14
Authors: Schwalbe, Harald; Schlepckow, Kai
Citation: Gerum, Christian; Silvers, Robert; Wirmer-Bartoschek, Julia; Schwalbe, Harald. "Unfolded-state Structure and Dynamics Influence Fibril Formation of Human Prion Protein" Angew. Chem. Int. Ed. 48, 9452-9456 (2009).
Assembly members:
hPrP(121-230), polymer, 113 residues, Formula weight is not available
Natural source: Common Name: Human Taxonomy ID: 9606 Superkingdom: Eukaryota Kingdom: Metazoa Genus/species: Homo sapiens
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
hPrP(121-230): GHMVVGGLGGYMLGSAMSRP
IIHFGSDYEDRYYRENMHRY
PNQVYYRPMDEYSNQNNFVH
DXVNITIKQHTVTTTTKGEN
FTETDVKMMERVVEQMXITQ
YERESQAYYQRGS
- assigned_chemical_shifts
| Data type | Count |
| 13C chemical shifts | 257 |
| 1H chemical shifts | 174 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | human prion protein (residues 121-230) | 1 |
Entities:
Entity 1, human prion protein (residues 121-230) 113 residues - Formula weight is not available
Construct constitutes C-terminal domain (residues 121-230). First three residues are a remnant of the N-terminal (his)6 tag.
| 1 | GLY | HIS | MET | VAL | VAL | GLY | GLY | LEU | GLY | GLY | ||||
| 2 | TYR | MET | LEU | GLY | SER | ALA | MET | SER | ARG | PRO | ||||
| 3 | ILE | ILE | HIS | PHE | GLY | SER | ASP | TYR | GLU | ASP | ||||
| 4 | ARG | TYR | TYR | ARG | GLU | ASN | MET | HIS | ARG | TYR | ||||
| 5 | PRO | ASN | GLN | VAL | TYR | TYR | ARG | PRO | MET | ASP | ||||
| 6 | GLU | TYR | SER | ASN | GLN | ASN | ASN | PHE | VAL | HIS | ||||
| 7 | ASP | SMC | VAL | ASN | ILE | THR | ILE | LYS | GLN | HIS | ||||
| 8 | THR | VAL | THR | THR | THR | THR | LYS | GLY | GLU | ASN | ||||
| 9 | PHE | THR | GLU | THR | ASP | VAL | LYS | MET | MET | GLU | ||||
| 10 | ARG | VAL | VAL | GLU | GLN | MET | SMC | ILE | THR | GLN | ||||
| 11 | TYR | GLU | ARG | GLU | SER | GLN | ALA | TYR | TYR | GLN | ||||
| 12 | ARG | GLY | SER |
Samples:
sample_1: hPrP(121-230), [U-13C; U-15N], 0.2 – 0.5 mM; TSP 1 mM; urea 8 M; H2O 90%; D2O 10%
sample_conditions_1: ionic strength: 0 M; pH: 2.0; pressure: 1 atm; temperature: 298 K
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 2D 1H-15N HSQC | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCO | sample_1 | isotropic | sample_conditions_1 |
| 3D CBCA(CO)NH | sample_1 | isotropic | sample_conditions_1 |
| 3D HNCACB | sample_1 | isotropic | sample_conditions_1 |
| 3D HN(CA)CO | sample_1 | isotropic | sample_conditions_1 |
| 3D HNN | sample_1 | isotropic | sample_conditions_1 |
Software:
CARA, Keller and Wuthrich - chemical shift assignment
NMR spectrometers:
- Bruker DRX 600 MHz
- Bruker Avance 600 MHz
- Bruker Avance 700 MHz
- Bruker Avance 800 MHz