All peptide-protein complexes were subjected to duplicate MD simulations using YASARA structure. Maleimide constraints were modelled in YASARA by swapping the pertinent amino acids for cysteines and connecting to maleimide fragments. In addition, N-Myc73-94 (residues 90-94 not resolved in the original crystal structure) were modelled prior to any analysis using helical dihedral angles and then minimised structures were generated using the energy minimization function with default settings. The modelled complexes were subjected to MD simulations using YASARA structure macro for fast MD run (www.yasara.org/md_runfast.mcr). Briefly, the AMBER14 forcefield was used and the temperature was set as 298.0 K with the timestep set as 1*2.50 fs. Each complex was run for 80 ns. Minimum energy and average structures were analysed from these experiments and figures created using the same software.