water molecule were constructed/placed manually into the active site in order to optimize the position of the water molecule for nucleophilic attack on the phosphate. In Chimera 3, the catalytic aspartic was found in the crystal structure in an unproductive conformation and thus was rotated into a productive conformation taking the highest probability rotamer from the Dynameomics rotamer library 72 (probability 0.66, top-ranked out of 9 possible rotamers) as implemented in UCSF Chimera, v. 1.14. In addition, the side chain of Gln261 was rotated to match the rotamer found in PDB ID: 3I80, which is the conformation it is expected to take during the hydrolytic step of catalysis.