PDBe 2l7b

Solution NMR

NMR Structure of full length apoE3

Released:
Source organism: Homo sapiens
Primary publication:
Topology of human apolipoprotein E3 uniquely regulates its diverse biological functions.
Proc. Natl. Acad. Sci. U.S.A. 108 14813-8 (2011)
PMID: 21873229

Function and Biology Details

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Apolipoprotein E Chain: A
Molecule details ›
Chain: A
Length: 307 amino acids
Theoretical weight: 35.3 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P02649 (Residues: 19-317; Coverage: 100%)
Gene name: APOE
Sequence domains: Apolipoprotein A1/A4/E domain

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 74%
Refinement method: simulated annealing, distance geometry
Chemical shifts: BMR15744  
Expression system: Escherichia coli