Fig. 1. Molecular visualization of the wild-type (WT) (left) and variant (right) amino acid using the FoldX function of SNPeffect 4.0. If the mutation destabilizes the structure, ddG (ΔΔG) is increased, whereas stabilizing mutations decrease ddG. Since the FoldX error margin is approximately 0.5 kcal/mol, changes in this range are considered insignificant. (A, B) The mutation from Ile (red in A) to Met (red in B) at position 220 resulted in a ddG of -0.38 kcal/mol. This implies that the mutation had no effect on protein stability. (C, D) The mutation from Gly (red in C) to Ser (red in D) at position 306 resulted in a ddG of 2.81 kcal/mol. This implies that the mutation reduced protein stability. (E, F) The mutation from Ile (red in E) to Thr (red in F) at position 380 resulted in a ddG of 0.56 kcal/mol. This implies that the mutation slightly reduced protein stability. (G, H) The mutation from Cys (red in G) to Gly (red in H) at position 385 resulted in a ddG of 0.65 kcal/mol. This implies that the mutation slightly reduced protein stability. (I, J) The mutation from Arg (red in I) to Cys (red in J) at position 387 resulted in a ddG of 2.18 kcal/mol. This implies that the mutation reduced protein stability. (K, L) The mutation from Pro (red in K) to Arg (red in L) at position 396 resulted in a ddG of 3.19 kcal/mol. This implies that the mutation reduced protein stability. (M and N) The mutation from Glu (red in M) to Lys (red in N) at position 416 resulted in a ddG of -0.86 kcal/mol. This implies that the mutation slightly enhanced protein stability.