2k1d

Solution NMR

NMR Studies of a Pathogenic Mutant (D178N) of the Human Prion Protein

Released:
Source organism: Homo sapiens
Entry authors: Mills JL, Surewicz K, Surewicz WK, Sonnichsen FD

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-137455 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Major prion protein Chain: A
Molecule details ›
Chain: A
Length: 146 amino acids
Theoretical weight: 16.49 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P04156 (Residues: 90-231; Coverage: 62%)
Gene names: ALTPRP, PRIP, 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
Chemical shift assignment: 76%
Refinement method: simulated annealing, TORSION ANGLE DYNAMICS
Expression system: Escherichia coli