deletions | additions       diff --git a/subsubsection_Cathepsin_G_Cathepsin_G__.tex b/subsubsection_Cathepsin_G_Cathepsin_G__.tex  index 07a47c9..e27d278 100644  --- a/subsubsection_Cathepsin_G_Cathepsin_G__.tex  +++ b/subsubsection_Cathepsin_G_Cathepsin_G__.tex 
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\subsubsection*{Cathepsin \subsection*{Cathepsin  G} Cathepsin G with its best approach and SMARTS expression, FOMS performed significantly better than random performance (cite stats table). For VAMS however, Cathepsin G with its best approach and SMARTS expression performed slightly worse than random chance (cite table). This indicates that for Cathepsin G, FOMS was a better performing screening method.  According to the study on the crystal structure of Cathepsin G with its inhibitor, Cathepsin G has 4 hydrophobic pockets that can be optimized for binding, each potentially being filled by a napthol group. Both FOMS and VAMS were pre-aligned to the deepest pocket in the active site, S1, the region that contributes the most to stabilizing the crystal structure (cite cathg). Although this is the most important interaction for a Cathepsin G inhibitor, filling the other pocket located at S3/S4 as referenced can contribute as much as 50 fold for increasing stability (cite cathg).