In that work, such motions were observed in simulations at both 298 and 310 K. Accordingly, to investigate whether MCR-1 might experience increased mobility in simulations at physiological (i.e. host) temperature, a further set of triplicate 500 ns simulations of MCR-1 in the mono-zinc form, without bound POPE, was undertaken. The results failed to identify any significant change in dynamic behavior in simulations at the two different temperatures, as evidenced by averaged C RMSDs for simulations of the complete protein (2.70 ± 0.29 Å, 3.43 ± 0.48 Å); catalytic (1.55 ± 0.17 Å, 1.60 ± 0.16 Å) and transmembrane domains (2.73 ± 0.35 Å, 3.08 ± 0.48 Å) at 300 K and 310 K, respectively. Similarly, no significant difference was evident in the interdomain distance (39.4 ± 0.87 Å at 300 K, and 40.1 ± 0.57 Å at 310 K).