Figure 3. Interresidue distances in the simulated FG domains.

(A) Plots of the probability distribution of inter-atomic distances in the wild-type and mutant FG domains. The distance distribution between the backbone β-carbons of phenylalanine (F) or alanine (A) residues in positions 84 and 93 (see Figure 1C) is shown as a representative example. The solid line in each plot corresponds to a Gaussian fit to the probability distribution. (B) Pearson squared correlation plots of the atomic distance between F–F or A–A pairs in the wild-type and mutant Nup116 FG domains. The numbers in the axes correspond to the various F–F or A–A pairs that result from all possible combinations (listed in Table S1). The correlation map shows how each of the pairs is related to the others. The insert depicts the contour level of the Pearson coefficient. (C) Schematic representations of Phe-to-Phe distances in the wild-type FG domain and Ala-to-Ala distances in the F>A mutant domain. The calculated average distance between the Phe or Ala residues in the pair-wise combinations is thickness and color coded. Thick red lines represent distances between 10 and 15 Å; medium blue lines represent distances between 15 and 20 Å; and thin green lines represent distances greater than 20 Å.