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\subsection*{Heat Shock Protein 90}  Virtual screening results heat shock protein 90 (HSP90) are shown in Figure~\ref{hsp90}. All three shape similarity methods perform poorly with AUCs from 0.38 (VAMS) to 0.51 0.49  (RDKit). The shape constraint queries can produce statistically significant enrichments and the pareto frontier matches or exceeds the ROC curve of RDKit. This suggests that this target benefits from a partial similarity search as opposed to a whole molecule similarity. % The best SMARTS expression and approach for Hsp90 performed significantly better than random performance for FOMS, but not for VAMS (cite table). Hsp 90 inhibitors interact with the ATP binding site. The most important interactions are with Asp93, Gly97, Lys58 , and Asn51 residues, with the study reporting the crystal structure highlighting Asp93 as the most important (cite HSP). Only the Asp93 interaction is covered by our SMARTS expressions and fragment pre-alignments, while the other interactions are also key for Hsp90 inhibition, with the Gly backbone being second in importance. As with other targets in the MUV dataset, the poor performance of FOMS relative to random performance can be partially attributed to the large number of interactions that are not covered by our fragment selection due to the nature of the ligand binding mode.