Replication Data for: The structure and dynamics of water molecule networks underlie catalytic efficiency in a glycoside exo-hydrolase

The data provided corresponds to the molecular dynamics simulations performed for the wild-type (WT) and E220A mutant of HvoExoI glycosyl hydrolase in covalent complex with glucose (reaction intermediate) and with laminaripentaose bound. The data was used to study the effect of the mutation and how this area affects the correct positioning of the catalytic water and, thus, catalysis.

Three repicates of 1 microsecond each were performed for each system using the AMBER program.
For each replicate (r0, r1 and r2), around 10,000 PDB files of the enzyme:substrate complexes are provided.