Solution NMR

High resolution structure and dynamics of CsPinA parvulin at physiological temperature

Source organism: Cenarchaeum symbiosum
Entry authors: Jaremko L, Jaremko M, Zweckstetter M, Bayer P, Ejchart A

Function and Biology Details

Reaction catalysed:
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
PpiC domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 97 amino acids
Theoretical weight: 10.52 KDa
Source organism: Cenarchaeum symbiosum
Expression system: Escherichia coli
  • Canonical: O74049 (Residues: 1-92; Coverage: 100%)
Gene names: CENSYa_1183, pinA
Sequence domains: PPIC-type PPIASE domain
Structure domains: Chitinase A; domain 3

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 85%
Refinement method: simulated annealing
Chemical shifts: BMR18864  
Expression system: Escherichia coli