Restricted domain mobility in the Candida albicans Ess1 prolyl isomerase.

The first three residues correspond to the residual sequence from the thrombin cleavage site

Peptidyl-Prolyl Isomerase Ess1 From Candida Albicans

peptidyl prolyl cis/trans isomerase, putative [Candida dubliniensis CD36]

peptidyl prolyl cis/trans isomerase [Candida albicans]

hypothetical protein CaO19.5196 [Candida albicans SC5314]

hypothetical protein CaO19.12663 [Candida albicans SC5314]

peptidyl-prolyl cis-trans isomerase 1 [Candida albicans WO-1]

peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 [Candida albicans P94015]

Backbone 1H, 13C and 15N chemical shift assignments for the prolyl isomerase Ess1 from Candida albicans

THE STRUCTURE OF THE CANDIDA ALBICANS ESS1 PROLYL ISOMERASE REVEALS A WELL-ORDERED LINKER THAT RESTRICTS DOMAIN MOBILITY

50 mM potassium phosphate + 5 mM dithiothreitol-d10