BMRB Entry 11028
Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR11028
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Title: Solid-state NMR assignment of the rigid core of the HET-s(218-289) prion protein in its amyloid conformation. PubMed: 18339938
Deposition date: 2008-01-25 Original release date: 2009-03-31
Authors: Siemer, Ansgar; Wasmer, Christian; Lange, Adam; Van Melckebeke, Helene; Ernst, Matthias; Ritter, Christiane; Steinmetz, Michel; Riek, Roland; Meier, Beat
Citation: Wasmer, Christian; Lange, Adam; Van Melckebeke, Helene; Siemer, Ansgar; Riek, Roland; Meier, Beat. "Amyloid fibrils of the HET-s(218-289) prion form a beta-solenoid with a triangular hydrophobic core." Science 319, 1523-1526 (2008).
Assembly members:
HET-s(218-289), polymer, 79 residues, 8667.732 Da.
Natural source: Common Name: Podospora anserina Taxonomy ID: 5145 Superkingdom: Eukaryota Kingdom: Fungi Genus/species: Podospora anserina
Experimental source: Production method: recombinant technology Host organism: Escherichia coli
Entity Sequences (FASTA):
HET-s(218-289): MKIDAIVGRNSAKDIRTEER
ARVQLGNVVTAAALHGGIRI
SDQTTNSVETVVGKGESRVL
IGNEYGGKGFWDNHHHHHH
- assigned_chemical_shifts
Data type | Count |
13C chemical shifts | 217 |
15N chemical shifts | 56 |
Additional metadata:
Assembly:
Entity Assembly ID | Entity Name | Entity ID |
---|---|---|
1 | HET-s(218-289) | 1 |
Entities:
Entity 1, HET-s(218-289) 79 residues - 8667.732 Da.
1 | MET | LYS | ILE | ASP | ALA | ILE | VAL | GLY | ARG | ASN | ||||
2 | SER | ALA | LYS | ASP | ILE | ARG | THR | GLU | GLU | ARG | ||||
3 | ALA | ARG | VAL | GLN | LEU | GLY | ASN | VAL | VAL | THR | ||||
4 | ALA | ALA | ALA | LEU | HIS | GLY | GLY | ILE | ARG | ILE | ||||
5 | SER | ASP | GLN | THR | THR | ASN | SER | VAL | GLU | THR | ||||
6 | VAL | VAL | GLY | LYS | GLY | GLU | SER | ARG | VAL | LEU | ||||
7 | ILE | GLY | ASN | GLU | TYR | GLY | GLY | LYS | GLY | PHE | ||||
8 | TRP | ASP | ASN | HIS | HIS | HIS | HIS | HIS | HIS |
Samples:
sample_1: HET-s(218-289), [U-100% 13C; U-100% 15N], 5 40 mg; H2O%
sample_conditions_1: ionic strength: 0 M; pH: 7.5; pressure: 1 atm; temperature: 278 K
Experiments:
Name | Sample | Sample state | Sample conditions |
---|---|---|---|
DREAM | sample_1 | solid | sample_conditions_1 |
TOBSY | sample_1 | solid | sample_conditions_1 |
PDSD | sample_1 | solid | sample_conditions_1 |
NCA | sample_1 | solid | sample_conditions_1 |
NCO | sample_1 | solid | sample_conditions_1 |
N(CO)CA | sample_1 | solid | sample_conditions_1 |
N(CO)CB | sample_1 | solid | sample_conditions_1 |
N(CA)CO | sample_1 | solid | sample_conditions_1 |
CA-CA | sample_1 | solid | sample_conditions_1 |
Software:
TOPSPIN, Bruker Biospin - processing
SPARKY, Goddard - data analysis
CARA, Rochus Keller - data analysis
xwinnmr, Bruker Biospin - processing
NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing
NMR spectrometers:
- Bruker Avance 600 MHz
- Bruker Avance 850 MHz