X-ray diffraction
2.2Å resolution

Structural Determinants for Improved Thermal Stability of Designed Ankyrin Repeat Proteins With a Redesigned C-capping Module.


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
NI1C MUT4 Chain: A
Molecule details ›
Chain: A
Length: 91 amino acids
Theoretical weight: 9.73 KDa
Source organism: synthetic construct
Expression system: Escherichia coli
Structure domains: Ankyrin repeat-containing domain

Ligands and Environments

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: C2
Unit cell:
a: 77.15Å b: 35.33Å c: 32.4Å
α: 90° β: 114.43° γ: 90°
R R work R free
0.174 0.168 0.222
Expression system: Escherichia coli