2n0k

Solution NMR

Chemical shift assignments and structure of the alpha-crystallin domain from human, HSPB5

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-crystallin B chain Chains: A, B
Molecule details ›
Chains: A, B
Length: 89 amino acids
Theoretical weight: 10.2 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P02511 (Residues: 64-152; Coverage: 51%)
Gene names: CRYA2, CRYAB, HSPB5
Structure domains: Immunoglobulin-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 42%
Refinement method: simulated annealing
Chemical shifts: BMR25527  
Expression system: Escherichia coli BL21(DE3)