Three-dimensional image reconstruction of dephosphorylated smooth muscle heavy meromyosin reveals asymmetry in the interaction between myosin heads and placement of subfragment 2 -- Data Supplement - Supplemental Data -- Proceedings of the National Academy of Sciences

Supplementary material for Wendt et al. (April 3, 2001) Proc. Natl. Acad. Sci. USA, 10.1073/pnas.071051098

Fig. 6.
Stereoview of the heavy chain–heavy chain interactions. Top pair is for crosseyed stereo viewing; bottom pair is for normal stereo viewing. This view perpendicular to the crystal plane. Color scheme: the heavy chain of the "free" myosin head is magenta and that of the "blocked" head is red. For both myosin heads the converter domain is green, the essential light chains are blue, and the regulatory light chains, orange. In addition, loops involved in heavy chain–heavy chain interactions are in black on the "free" head and in yellow on the "blocked" head. "Free" head residues potentially involved in the interaction include 458 (at the end of a disordered loop), loop 167–170, and converter domain loop 746–749 and helix 727–732. "Blocked" head residues include loop 368–379, the myopathy loop 407–417, loop 615–618, and helix 392–398.