› 5jzr

Solid-state NMR

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

Released:
DOI: 10.2210/pdb5jzr/pdb
PDB entry 5jzr coloured by chain, ensemble of 20 models, front view.
PDB entry 5jzr coloured by chain, ensemble of 20 models, side view.
PDB entry 5jzr coloured by chain, ensemble of 20 models, top view.
Source organism: Acinetobacter phage AP205
Primary publication:
Structure of fully protonated proteins by proton-detected magic-angle spinning NMR.
Andreas LB, Jaudzems K, Stanek J, Lalli D, Bertarello A, Le Marchand T, Cala-De Paepe D, Kotelovica S, Akopjana I, Knott B, Wegner S, Engelke F, Lesage A, Emsley L, Tars K, Herrmann T, Pintacuda G
Proc Natl Acad Sci U S A 113 9187-92 (2016)
PMID: 27489348

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189619 (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: 35%
Refinement method: torsion angle dynamics
Expression system: Escherichia coli

Quick links

Citations

15 review citations

Insights into protein misfolding and aggregation enabled by solid-state NMR spectroscopy.
van der Wel PCA. (2017)
14 more

8 mentions without citation

1H-Detected Biomolecular NMR under Fast Magic-Angle Spinning.
Le Marchand et al. (2022)
7 more