› 2mzu

Solution NMR

Extending the eNOE data set of large proteins by evaluation of NOEs with unresolved diagonals

Released:
DOI: 10.2210/pdb2mzu/pdb
PDB entry 2mzu coloured by chain, ensemble of 20 models, front view.
PDB entry 2mzu coloured by chain, ensemble of 20 models, side view.
PDB entry 2mzu coloured by chain, ensemble of 20 models, top view.
Source organism: Homo sapiens
Primary publication:
Extending the eNOE data set of large proteins by evaluation of NOEs with unresolved diagonals.
Chi CN, Strotz D, Riek R, Vögeli B
J Biomol NMR 62 63-9 (2015)
PMID: 25749872

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158766 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase A Chain: A
Molecule details ›
Chain: A
Length: 165 amino acids
Theoretical weight: 18.04 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P62937 (Residues: 1-165; Coverage: 100%)
Gene names: CYPA, PPIA
Sequence domains: Cyclophilin type peptidyl-prolyl cis-trans isomerase/CLD
Structure domains: Cyclophilin-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Chemical shift assignment: 83%
Refinement method: DGSA-distance geometry simulated annealing
Expression system: Escherichia coli

Quick links

Citations

3 review citations

The Exact Nuclear Overhauser Enhancement: Recent Advances.
Nichols et al. (2017)
2 more

3 mentions without citation

Assemble-And-Match: A Novel Hybrid Tool for Enhancing Education and Research in Rational Structure Based Drug Design.
Tavousi et al. (2018)
2 more