Additionally, MD analyses of the number of contacts per-residue between TACC3522-536(4-I)525F and the protein over the course of the trajectory indicated increased and more sustained contacts between the iodinated amino acid and Aurora-A (see Fig. vs Fig. ). In their minimum energy structures, a shorter distance between Arg151Aurora-A and Phe525TACC3 (3.9 Å for (4-I)Phe525 vs 4.2 Å for Phe525) is consistent with a stronger cation-π interaction.