1b10

Solution NMR

SOLUTION NMR STRUCTURE OF RECOMBINANT SYRIAN HAMSTER PRION PROTEIN RPRP(90-231) , 25 STRUCTURES

Released:

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-137558 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Major prion protein Chain: A
Molecule details ›
Chain: A
Length: 142 amino acids
Theoretical weight: 16.26 KDa
Source organism: Mesocricetus auratus
Expression system: Escherichia coli
UniProt:
  • Canonical: P04273 (Residues: 90-231; Coverage: 61%)
Gene names: 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: NMR-RESTRAINED SIMULATED ANNEALING, MOLECULAR DYNAMICS, AND ENERGY MINIMIZATION.
Expression system: Escherichia coli