1m93

X-ray diffraction
1.65Å resolution

1.65 A Structure of Cleaved Viral Serpin CRMA

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Serine proteinase inhibitor 2 Chain: A
Molecule details ›
Chain: A
Length: 55 amino acids
Theoretical weight: 6.08 KDa
Source organism: Cowpox virus
Expression system: Escherichia coli
UniProt:
  • Canonical: P07385 (Residues: 1-55; Coverage: 16%)
Gene names: CPXV207, CRMA, SPI-2
Structure domains: Helix hairpin bin
Serine proteinase inhibitor 2 Chain: B
Molecule details ›
Chain: B
Length: 245 amino acids
Theoretical weight: 27.4 KDa
Source organism: Cowpox virus
Expression system: Escherichia coli
UniProt:
  • Canonical: P07385 (Residues: 56-300; Coverage: 72%)
Gene names: CPXV207, CRMA, SPI-2
Structure domains:
Serine proteinase inhibitor 2 Chain: C
Molecule details ›
Chain: C
Length: 41 amino acids
Theoretical weight: 4.52 KDa
Source organism: Cowpox virus
Expression system: Escherichia coli
UniProt:
  • Canonical: P07385 (Residues: 301-341; Coverage: 12%)
Gene names: CPXV207, CRMA, SPI-2

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P212121
Unit cell:
a: 49.52Å b: 92.59Å c: 100.63Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.188 0.245
Expression system: Escherichia coli