2ms2

X-ray diffraction
2.8Å resolution

THE REFINED STRUCTURE OF BACTERIOPHAGE MS2 AT 2.8 ANGSTROMS RESOLUTION

Released:
Source organism: Enterobacteria phage MS2
Primary publication:
The refined structure of bacteriophage MS2 at 2.8 A resolution.
J. Mol. Biol. 234 620-39 (1993)
PMID: 8254664

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
homo 180-mer (preferred)
homo trimer
homo pentadecamer
homo octadecamer
homo 30-mer
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Capsid protein Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 129 amino acids
Theoretical weight: 13.74 KDa
Source organism: Enterobacteria phage MS2
Expression system: Not provided
UniProt:
  • Canonical: P03612 (Residues: 2-130; Coverage: 99%)
Sequence domains: Levivirus coat protein
Structure domains: MS2 Viral Coat Protein

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: R32
Unit cell:
a: 288Å b: 288Å c: 653Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.189 0.189 not available
Expression system: Not provided