PDBe 1a2p

X-ray diffraction
1.5Å resolution

BARNASE WILDTYPE STRUCTURE AT 1.5 ANGSTROMS RESOLUTION

Released:
Source organism: Bacillus amyloliquefaciens
Primary publication:
Refinement and structural analysis of barnase at 1.5 A resolution.
Acta Crystallogr. D Biol. Crystallogr. 55 386-98 (1999)
PMID: 10089345

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribonuclease Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 110 amino acids
Theoretical weight: 12.4 KDa
Source organism: Bacillus amyloliquefaciens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00648 (Residues: 48-157; Coverage: 89%)
Sequence domains: ribonuclease
Structure domains: Microbial ribonucleases

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: LURE BEAMLINE DW32
Spacegroup: P32
Unit cell:
a: 58.97Å b: 58.97Å c: 81.58Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.115 not available 0.174
Expression system: Escherichia coli