BMRB Entry 4641
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR4641
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Title: Human Prion Protein Mutant E200K Fragment 90-231
Deposition date: 2000-08-25 Original release date: 2001-05-17
Authors: Zhang, Y.; Swietnicki, W.; Zagorski, M.; Surewicz, W.; Soennichsen, F.
Citation: Zhang, Y.; Swietnicki, W.; Zagorski, M.; Surewicz, W.; Soennichsen, F.. "Solution structure of Human Prion Protein Mutant E200K Fragment 90-231" J. Biol. Chem. 275, 33650-33654 (2000).
Assembly members:
PRION PROTEIN, polymer, 146 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):
PRION PROTEIN: GSDPGQGGGTHSQWNKPSKP
KTNMKHMAGAAAAGAVVGGL
GGYMLGSAMSRPIIHFGSDY
EDRYYRENMHRYPNQVYYRP
MDEYSNQNNFVHDCVNITIK
QHTVTTTTKGENFTKTDVKM
MERVVEQMCITQYERESQAY
YQRGSS
- assigned_chemical_shifts
- coupling_constants
| Data type | Count |
| 13C chemical shifts | 593 |
| 1H chemical shifts | 929 |
| 15N chemical shifts | 162 |
| coupling constants | 44 |
Additional metadata:
Assembly:
| Entity Assembly ID | Entity Name | Entity ID |
|---|---|---|
| 1 | PRION PROTEIN | 1 |
Entities:
Entity 1, PRION PROTEIN 146 residues - Formula weight is not available
| 1 | GLY | SER | ASP | PRO | GLY | GLN | GLY | GLY | GLY | THR | ||||
| 2 | HIS | SER | GLN | TRP | ASN | LYS | PRO | SER | LYS | PRO | ||||
| 3 | LYS | THR | ASN | MET | LYS | HIS | MET | ALA | GLY | ALA | ||||
| 4 | ALA | ALA | ALA | GLY | ALA | VAL | VAL | GLY | GLY | LEU | ||||
| 5 | GLY | GLY | TYR | MET | LEU | GLY | SER | ALA | MET | SER | ||||
| 6 | ARG | PRO | ILE | ILE | HIS | PHE | GLY | SER | ASP | TYR | ||||
| 7 | GLU | ASP | ARG | TYR | TYR | ARG | GLU | ASN | MET | HIS | ||||
| 8 | ARG | TYR | PRO | ASN | GLN | VAL | TYR | TYR | ARG | PRO | ||||
| 9 | MET | ASP | GLU | TYR | SER | ASN | GLN | ASN | ASN | PHE | ||||
| 10 | VAL | HIS | ASP | CYS | VAL | ASN | ILE | THR | ILE | LYS | ||||
| 11 | GLN | HIS | THR | VAL | THR | THR | THR | THR | LYS | GLY | ||||
| 12 | GLU | ASN | PHE | THR | LYS | THR | ASP | VAL | LYS | MET | ||||
| 13 | MET | GLU | ARG | VAL | VAL | GLU | GLN | MET | CYS | ILE | ||||
| 14 | THR | GLN | TYR | GLU | ARG | GLU | SER | GLN | ALA | TYR | ||||
| 15 | TYR | GLN | ARG | GLY | SER | SER |
Samples:
sample_1: PRION PROTEIN, [U-15N; U-13C], 0.8 mM; acetate buffer 10 mM; H2O 90%; D2O 10%
sample_cond_1: pH: 4.6; temperature: 299 K; pressure: 1 atm
Experiments:
| Name | Sample | Sample state | Sample conditions |
|---|---|---|---|
| 3D 13C-separated NOESY | sample_1 | not available | sample_cond_1 |
| 3D 15N-separated NOESY | sample_1 | not available | sample_cond_1 |
| 2D NOESY | sample_1 | not available | sample_cond_1 |
| HNHA | sample_1 | not available | sample_cond_1 |
Software:
NMRPipe vsgi6x.m4 - processing
FELIX v98 - processing
PIPP v4.24 - data analysis
ARIA v0.9 - structure solution
CNS v0.9 - structure solution, refinement
NMR spectrometers:
- Bruker DRX 800 MHz
Related Database Links:
| BMRB | 15676 16743 16757 17714 17756 17757 17780 18426 18550 19268 4379 4402 4434 4620 4736 |
| PDB | |
| DBJ | BAF62360 BAG32276 BAG32278 BAG52189 BAG56832 |
| EMBL | CAA58442 CAG46836 |
| GB | AAA60182 AAA68632 AAB59442 AAB59443 AAC05365 |
| REF | NP_000302 NP_001009093 NP_001073590 NP_001073591 NP_001073592 |
| SP | P04156 P61766 P61767 P61768 |
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