David Koes edited subsection_FXIa_The_best_SMARTS__.tex  over 8 years ago

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\subsection*{FXIa}  The best SMARTS expression and approach for FXIa performed significantly better than random performance Virtual screening results  for the FOMS, but not the VAMS method (cite table). Inhibition factor XIa (FXIA) are shown in Figure~\ref{fxia}. The optimizing shape alignment  of FXIa relies on hydrogen-bonding RDKit provides some enrichment  with many residues. Only one an AUC  of the pockets and its interaction with a His57 by hydrogen bonding and a stacking interaction are covered by our SMARTS expression 0.58. Although FOMS outperforms VAMS, both VAMS  and fragment pre-alignment (cite FXIa). There are many other hydrogen-bond interactions that include hydrogen bonding FOMS perform worse than random  with Asp189, Gly216, AUCs of 0.31  and Gly218 backbones that are not covered by our SMARTS expression 0.42 for VAMS  andfragment pre-alignment. Similar to most other protein targets in the MUV dataset,  FOMS would respectively. Shape constraints do  not fully capture select enriched subsets. These results suggest that although  the complete binding mode shape  ofcompounds screened, which most likely led to its poor performance (cite table).   Docking of 2FDA with active compounds from  the MUV dataset revealed 5 hydrophobic pockets, with only one being covered by our fragment pre-alignment. Many hydrogen-bonding interactions were revealed, including His57 and query molecule provides some information, neither  the inhibitor. Because our best SMARTS expression and fragment pre-alignment only covered the interaction with His57 and 1 placement  of5 potential pockets to be filled, it makes sense that FOMS did not yield high performance.   More specific SMARTS expressions led to higher performance for VAMS, whereas  the least specific SMARTS expression led to highest performance for FOMS (cite table). (explanation fragment nor the whole molecule provides useful information  for both?) pre-alignment.