BMRB Entry 11064
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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR11064
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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: 19504509
Deposition date: 2009-01-16 Original release date: 2009-06-25
Authors: Siemer, Ansgar; Wasmer, Christian; Lange, Adam; Van Melckebeke, Helene; Ernst, Matthias; Ritter, Christiane; Steinmetz, Michel; Riek, Roland; Meier, Beat
Citation: Lange, Adam; Gattin, Zrinka; Van Melckebeke, Helene; Wasmer, Christian; Soragni, Alice; Van Gunsteren, Wilfred; Meier, Beat. "A Combined Solid-State NMR and MD Characterization of the Stability and Dynamics of the HET-s(218-289) Prion in its Amyloid Conformation" ChemBioChem. 10, 1657-1665 (2009).
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 | 260 |
| 15N chemical shifts | 66 |
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 mg
sample_2: HET-s(218-289), [2-100% 13C; U-100% 15N], 5 – 40 mg; H2O mg
sample_3: HET-s(218-289), [U-10% 13C; U-100% 15N], 5 – 40 mg; H2O mg
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 No1 | 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 |
| PDSD No2 | sample_2 | solid | sample_conditions_1 |
| PDSD No3 | sample_3 | solid | sample_conditions_1 |
| DQSQ | sample_3 | 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