In comparison to the hydrophobic interaction described above, our second example shows a hydrogen bond/salt bridge interaction between the residues Arg and Gln in TEM1. Interestingly, two of these alternate interactions show a rather substantial conformational difference in which one of the helices is now a loop, and the interaction formed is now between the sidechain and the backbone instead of between the two sidechains (Figure ). candidate single point mutations to test as compared to the 365 from the X-ray structure alone. As depicted in Figure , there was not an increase in the mean fitness values from the inclusion of MD simulation data. It should be noted that the MD-based networks include more potential mutations (which could be subsequently filtered and/or combined in subsequent steps), so the denominator to the mean fitness value increases. We also performed a sensitivity analysis with regard to per-trajectory cutoff score (Figure ). The shape of the distributions and mean values for the distributions obtained were very similar for both "strict" and "relaxed" cutoffs, with the only notable (and expected) difference being that using a stricter cutoff reduces the number of possible mutations to try.