BMRB Entry 11064
Click here to enlarge.
PDB ID: 2mus
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
MolProbity Validation Chart
NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
NMR-STAR v2.1 text file (deprecated)
XML gzip file.
RDF gzip file.
All files associated with the entry
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 |