1shm

X-ray diffraction
1.9Å resolution

Convergent solutions to VHH domain stabilization from natural and in vitro evolution

Released:
Source organism: Lama glama
Primary publication:
A structure-based database of antibody variable domain diversity.
J Mol Biol 348 699-709 (2005)
PMID: 15826665

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-213089 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ANTIBODY RIG Chains: A, B, D, E
Molecule details ›
Chains: A, B, D, E
Length: 127 amino acids
Theoretical weight: 13.68 KDa
Source organism: Lama glama
Expression system: Escherichia coli
Structure domains: Immunoglobulins

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P21
Unit cell:
a: 34.211Å b: 120.711Å c: 52.246Å
α: 90° β: 103.32° γ: 90°
R-values:
R R work R free
0.188 0.185 0.236
Expression system: Escherichia coli