Previous work suggested that the salt-bridge between E23 and R97 is critical to lock the lid in an ordered conformation. However, the present MD simulations suggested that a broad range of mutations at E23 (E23G, E23L, E23Q) cause only moderate loss of helicity and did not significantly increase lid flexibility. The double mutant E23R97:R23E97 was simulated to test the effect of swapping the residues involved in salt-bridge formation. This causes a moderate decrease in stability of the helical motifs. Other double mutants that included I19G were simulated to evaluate potential additive effects (I19G:E23G, V14G:I19G, T16G:I19G). These double mutants exhibited helical stability comparable to that observed in I19G, suggesting that mutations of I19 were key to destabilizing the ordered lid state.