<p>Sequence prediction of the cNBH domain around the β9-strand for (A) WT (i) and AAA mutant (ii). (B) RMSD (i) and RMSF (ii) of WT (red) and AAA mutant (black) from the 60 ns of MD simulations. The blue box highlights the most significant difference between WT and AAA mutant in the backbone fluctuation. (C) The structures that have the lowest structural fluctuation to the centroid structure in the most populated cluster from the last 10 ns for WT (i) and AAA mutant (ii). Residues involved in hydrophobic interactions, defined by being within 4 Å of residues 860, 861 and 862 (cyan), are highlighted in magenta for WT (i) and AAA mutant (ii). There are reduced hydrophobic interactions in the AAA mutant. (D) Summary of residues that participate in hydrogen bonds with residues 860, 861 and 862 in WT (i) and the AAA mutant (ii) that are present for more than 5% of the 60 ns of MD simulation (see <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0077032#pone-0077032-t001" target="_blank">Table 1</a> for details).</p
