2fkg

X-ray diffraction
2.4Å resolution

The Crystal Structure of Engineered OspA

Released:
Source organism: Borreliella burgdorferi
Primary publication:
Atomic structures of peptide self-assembly mimics.
Proc Natl Acad Sci U S A 103 17753-8 (2006)
PMID: 17093048

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-143538 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Outer surface protein A Chain: A
Molecule details ›
Chain: A
Length: 320 amino acids
Theoretical weight: 34.94 KDa
Source organism: Borreliella burgdorferi
Expression system: Escherichia coli
UniProt:
  • Canonical: P0CL66 (Residues: 27-131, 132-273; Coverage: 96%)
Gene names: BB_A15, ospA
Sequence domains: Borrelia lipoprotein
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID
Spacegroup: C2
Unit cell:
a: 99.447Å b: 76.894Å c: 51.941Å
α: 90° β: 120° γ: 90°
R-values:
R R work R free
0.22 0.219 0.255
Expression system: Escherichia coli