Flexibility of the flap in the active site of BACE1 as revealed by crystal structures and molecular dynamics simulations

Xu, Y.; Li, M.; Greenblatt, H.; Chen, W.; Paz, A.; Dym, O.; Peleg, Y.; Chen, T.; Shen, X.; He, J.; Jiang, H.; Silman, I.; Sussman, J.L.

doi:10.1107/S0907444911047251

Figure 6
MD simulations of the BACE1 monomer and `dimer'. (a) Time-dependent r.m.s.d.s of the C atoms with respect to their starting positions in the trajectories of BACE1 in the monomer (black) and in the two copies of the `dimer' (red and green). (b) Time-dependence of the distances between the C atoms of flap residues 67-75 and the two carboxyl O atoms of Asp228 in the monomer (black) and in the two copies of BACE1 in the `dimer' (green and red).