Figure 5.

Differences in the structural stability of the E-loops of PTP1B and YopH from our PT-MetaD-WTE simulations. (A and B) Normalized histograms of the P-Loop arginine to the E-loop glutamic acid salt bridge distance from each our simulations of (A) PTP1B and (B) YopH for the unliganded, pNPP-bound, and phospho-enzyme intermediates states of both enzymes. The figures show representative conformations for each protein with and without the salt bridge formed. (C and D) RMSFs of the C_α atoms of the E-loop residues, obtained from our PT-MetaD-WTE simulations of (C) PTP1B and (D) YopH in all three states simulated. (E and F) Representative structures of the conformational sampling/diversity of the E-loops of (E) PTP1B and (F) YopH, in the unliganded states of each enzyme. E-loop residues are colored mapped from red (most flexible) through white and to blue (least flexible) according to their calculated C_α RMSF.