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. Author manuscript; available in PMC: 2010 Nov 12.
Published in final edited form as: J Phys Chem A. 2009 Nov 12;113(45):12439–12446. doi: 10.1021/jp902949f

Figure 1.

Figure 1

Comparison of the optimized active site of myosin motor domain with ATP bound to the (a) open (post-rigor) and (b) closed (pre-powerstroke) conformation state. The geometries have been optimized at the B3LYP/6-31G(d)/MM level (see text). Note the significant difference between the optimized Pγ-O3β bond distance in ATP; for reference, the equilibrium bond distance is ~1.69-1.70 Å in solution56,57.