Figure 10

Average number of water molecules within 3 Å of the mutating residue (Arg or Ser 211), D112, and D185. The error bars represent standard deviations. Hydration patterns are not always consistent in the vicinity of R211 during the R211S and S211R mutations. For example, in the apo state, the number of water molecules near D185 increases (left subplot, right group, blue \(\rightarrow\) orange bars). When mutating the system with S211 back to R211, the number of water molecules decrease near D112 instead of near D185 (left subplot, middle group, orange \(\rightarrow\) green bars). It might be expected that the blue bars (wild type protein with R211) and the green bars (twice mutated protein also with R211) should be the same in all three systems. Between the two R211 states of before and after mutation, both the apo and gbi1 systems differ by 1–2 water molecules in the specified vicinity of D112 and D185, whereas gbi2 is more consistent in hydration around the two acidic residues.