Fig. 4

MD simulations of PfCBH1 and TrCBH1 catalytic domains. a The energy decomposition comparison between PfCBH1 and TrCBH1 in the presence of cellononaose (G-9), celloheptaose (G-7), and cellobiose (G-2). Binding energies were derived from Molecular Mechanics Generalized Born Surface Area (MMGBSA) calculations. The significance discovery between groups is determined using the Two-stage linear step-up procedure of Benjamini, Krieger, and Yekutieli. ****p < 0.0001, while ns: no significant difference at α = 0.05. b, d The cluster representations of PfCBH1 and TrCBH1 over a 100-ns trajectory at 5-ns intervals. The enzymes are colored by RMSF, where red represents the highest fluctuations, and blue represents the lowest fluctuations. c The root-mean-square fluctuation (RMSF) of the active site-bound cellononaose by binding subsite. The RMSF values were calculated based on the glucose-heavy atoms over the entire 100-ns MD simulation. The error bars were computed by block averaging. ****p < 0.0001, at α = 0.05