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Root-mean-square (rms) fluctuations calculated for the α-helices of HbI from the MD simulations. The rms fluctuations of each α-helix of the protein are colored black for WT HbI and red for F97Y-HbI; opaque and transparent bars are used for the liganded and unliganded states, respectively. The backbone N, C, and O atoms were used to calculate the rms fluctuations. The error bars were calculated from the standard deviation among the trajectories.
