PDBe 2lmo

Solid-state NMR

Structural Model for a 40-Residue Beta-Amyloid Fibril with Two-Fold Symmetry, Negative Stagger

Released:
Source organism: Homo sapiens
Primary publication:
Molecular structural basis for polymorphism in Alzheimer's beta-amyloid fibrils.
Proc. Natl. Acad. Sci. U.S.A. 105 18349-54 (2008)
PMID: 19015532

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo 12-mer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Amyloid-beta protein 40 Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 40 amino acids
Theoretical weight: 4.34 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P05067 (Residues: 672-711; Coverage: 5%)
Gene names: A4, AD1, APP

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 2%
Refinement method: simulated annealing
Chemical shifts: BMR18128  
Expression system: Not provided