Update wiki/pages/model.html

wiki/pages/model.html

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     <br>
     <p><strong> Table Summary </strong> </p>
     <table>
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         <th style = "text-align:center"> Protein and Ligand </th>
         <td style="text-align:center"> 1aq6 and PFOA </td>
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     </table>
     <br>
     <p> These binding sites in all four combinations all consist of hydrogen bonds, halogen bonds, and salt bridges(except for haloacid dehalogenase and perfluorooctanesulfonic acid). These types of bonds all contribute to oxidative reactions, which we are trying to achieve with these enzymes to break down PFAS.</p>
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     <p>  The binding energy for haloacid dehalogenase is lower than optimal, however, because there is not much free energy, we know that there is strong binding affinity. The larger torsional energy also indicates that the PFAS will not easily change conformations, indicating that the protein-ligand complex would not change easily. The large inhibition constant also means that the enzyme activity is likely not to be disrupted, which allows for PFAS to continuously be broken down. The low cluster RMSD also indicates that it is an effective binding site. The reference RMSD is particularly high, but this is because we docked without predetermining an active site, which resulted in this high value.</p>