BMRB Entry 11028

Title:
Solid-state NMR assignment of the rigid core of the HET-s(218-289) prion protein in its amyloid conformation.
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:

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).
PubMed: 18339938

Assembly members:

Assembly members:
HET-s(218-289), polymer, 79 residues, 8667.732 Da.

Natural source:

Natural source:   Common Name: Podospora anserina   Taxonomy ID: 5145   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Podospora anserina

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts217
15N chemical shifts56

Additional metadata:

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  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
1HET-s(218-289)1

Entities:

Entity 1, HET-s(218-289) 79 residues - 8667.732 Da.

1   METLYSILEASPALAILEVALGLYARGASN
2   SERALALYSASPILEARGTHRGLUGLUARG
3   ALAARGVALGLNLEUGLYASNVALVALTHR
4   ALAALAALALEUHISGLYGLYILEARGILE
5   SERASPGLNTHRTHRASNSERVALGLUTHR
6   VALVALGLYLYSGLYGLUSERARGVALLEU
7   ILEGLYASNGLUTYRGLYGLYLYSGLYPHE
8   TRPASPASNHISHISHISHISHISHIS

Related Database Links:

BMRB 11064
PDB 2KJ3 2LBU 2RNM
GB AAB19707 AAB94631
PRF 1718317A
SP Q03689
AlphaFold Q03689