File:Structural-Basis-for-Functional-Tetramerization-of-Lentiviral-Integrase-ppat.1000515.s006.ogv

English: Simulation of transitions between the open and closed conformations of the MVV IN tetramer (side view). Experimentally determined structures CF1/CDEF, CF1/ABEF and CF2 correspond to the first, middle and the last frames of the animation, respectively. IN chains are shown as cartoons; residues discussed in the main text are shown in ball-and-stick style. The color code is preserved from Figure 1 of the main text. Running numbers show separation of the active sites (measured as distance between Cγ atoms of Glu154 residues in cyan and yellow chains). Asp66, Asp118 and Glu154 in the inner monomers are collectively indicated as DDE motifs. Residues 148–151 from the inner monomers (cyan and yellow) are omitted for clarity. Note a slight deformation of α4 helices and compression of the active sites towards the end of the animation. Transitions states were interpolated using Yale Morph Server (http://molmovdb.org/), and the movie was created with PyMOL (http://pymol.sourceforge.net/).