5jzr

Solid-state NMR

Solid-state MAS NMR structure of Acinetobacter phage 205 (AP205) coat protein in assembled capsid particles

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Coat protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 131 amino acids
Theoretical weight: 14.02 KDa
Source organism: Acinetobacter phage AP205
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9AZ42 (Residues: 1-131; Coverage: 100%)

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 34%
Refinement method: torsion angle dynamics
Chemical shifts: BMR30094  
Expression system: Escherichia coli