2af5

X-ray diffraction
2.5Å resolution

2.5A X-ray Structure of Engineered OspA protein

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: 297 amino acids
Theoretical weight: 32.29 KDa
Source organism: Borreliella burgdorferi
Expression system: Escherichia coli BL21(DE3)
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 14-ID-B
Spacegroup: P21
Unit cell:
a: 48.547Å b: 55.33Å c: 70.361Å
α: 90° β: 104.08° γ: 90°
R-values:
R R work R free
0.246 0.242 0.276
Expression system: Escherichia coli BL21(DE3)