1y15

Solution NMR

Mouse Prion Protein with mutation N174T

Released:
Source organism: Mus musculus
Primary publication:
Prion protein NMR structures of elk and of mouse/elk hybrids.
Proc Natl Acad Sci U S A 102 646-50 (2005)
PMID: 15647363

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-138267 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Major prion protein Chain: A
Molecule details ›
Chain: A
Length: 112 amino acids
Theoretical weight: 13.25 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P04925 (Residues: 120-231; Coverage: 48%)
Gene names: Prn-p, Prnp, Prp
Sequence domains: Prion/Doppel alpha-helical domain
Structure domains: Prion/Doppel protein, beta-ribbon domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Refinement method: torsion angle dynamics
Expression system: Escherichia coli BL21