Comparison of the dynamics of substrate access channels in three cytochrome P450s reveals different opening mechanisms and a novel functional role for a buried arginine -- Data Supplement - Supporting Information -- Proceedings of the National Academy of Sciences

Supporting information for Winn et al. (2002) Proc. Natl. Acad. Sci. USA 99 (8), 5361–5366. (10.1073/pnas.082522999)

Supporting Figure 9 Fig. 9.
Snapshots at 10-s intervals along REMD traj\#5 (Table 2, main article), showing the rearrangement of residues around R185 immediately prior to DEB egress. The secondary structure is rendered with the helices represented as green tubes, the beta strands as yellow, planar arrows, and turns and coils as thin green ribbons. The heavy atoms of all side chains referred to in Fig. 8 are displayed as sticks colored by atom type. The heavy atoms and polar hydrogens of DEB are display as sticks, with carbon atoms colored blue, oxygen atoms colored red, and hydrogen atoms colored white. Hydrogen bonding interactions are represented by dotted black lines, with the distance at the instant of the snapshot, shown in Å.