3o49

X-ray diffraction
1.45Å resolution

Crystal structure of Symfoil-1: de novo designed beta-trefoil architecture with symmetric primary structure

Released:
Source organism: synthetic construct
Primary publication:
Experimental support for the evolution of symmetric protein architecture from a simple peptide motif.
Proc Natl Acad Sci U S A 108 126-30 (2011)
PMID: 21173271

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
de novo designed beta-trefoil architecture with symmetric primary structure Chain: A
Molecule details ›
Chain: A
Length: 142 amino acids
Theoretical weight: 15.74 KDa
Source organism: synthetic construct
Expression system: Escherichia coli
Structure domains: Trefoil (Acidic Fibroblast Growth Factor, subunit A)

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-BM
Spacegroup: I222
Unit cell:
a: 50.365Å b: 53.351Å c: 85.175Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.196 0.227
Expression system: Escherichia coli