Figure 7
The effects of amino acid sequence for conformational ensembles of each EF-lobe. We made some mutants of calmodulin from native one and lobe-swapped one, and evaluated the effects of mutation by MD. The mutant structure was made by homology modeling with SWISS-MODEL. (a) F12I and L48V for N-lobe and I85F and V121L for C-lobe were mutated in 1CLL.pdb. (b) I12F and V48L for N-lobe and F85I and L121V for C-lobe were mutated in the lobe swapped calmodulin structure used in Fig. 6a. (c) F12I, I18V, T34H, P43L, L48V, V55A and P66E for N-lobe and I85F, V91I, H107T, L116P, V121L, A128V and E139P for C-lobe were mutated in 1CLL.pdb. (d) I12F, V18I, H34T, L43P, V48L, A55V and E66P for N-lobe and F85I, I91V, T107H, P116L, L121V, V128A and P139E for C-lobe were mutated in the lobe swapped calmodulin structure used in Fig. 6a. MD simulations were performed by using GROMACS 2016 on a Cray XC50. This figure summarizes six 100 ns MD results for each model. Squares show the peak position for each MD run. The dots are the conformations sampled at every 20 ps. Squares show the peak position for each MD run. The contour shows the free energy landscape of ensemble summed over six MD runs. The models generated by SWISS-MODEL are licensed under the CC BY-SA 4.0 Creative Commons Attribution-ShareAlike 4.0 International License.
