BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 11064

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

Data sets:
Data typeCount
13C chemical shifts260
15N chemical shifts66

Additional metadata:

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  • Samples and Experiments
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Related Database Links:

BMRB 11028
PDB 2KJ3 2LBU 2RNM
GB AAB19707 AAB94631
PRF 1718317A
SP Q03689