deletions | additions       diff --git a/subsection_ER_alpha_agonist_ER__.tex b/subsection_ER_alpha_agonist_ER__.tex  index f99ebe0..42a7799 100644  --- a/subsection_ER_alpha_agonist_ER__.tex  +++ b/subsection_ER_alpha_agonist_ER__.tex 
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\subsection{ER$\alpha$ agonist} \subsection{ER$\alpha$}  ER-a with its best approach and SMARTS expression did not perform significantly better than random performance for the FOMS or VAMS method (cite table). Although FOMS was significantly better performing than VAMS, it still did not perform well enough for ER-a agonists to be considered an effective screening method.   Similar to ER-a, the interaction with Glu353 and Arg394 is vital for agonism of ER-a (cite crystal ER-a). There is also an indication that the stereochemistry is an important consideration for ER-a agonism when trying to avoid steric clash with W383, L536, and L539. The study reporting the crystal structure of the ER-a agonist cites, “…dihydrobenzoxathiin SERAMs [are] highly dependent on size and location of side chain substituents” (cite part 9). For this reason, it makes sense that our SMARTS expressions and fragment pre-alignments did not perform significantly better than random chance (cite table).