An ATP-binding step with pseudo-first-order rate has survival probability and waiting density . It decreases from a finite value at zero, integrates to one and has mean . Its concentration dependence suggests binding-limited waiting before the large 80-degree substep.
Two independent sequential exponential steps of rates give the convolution
It begins at zero, rises to a maximum at and decays; its mean is . At equal rates it becomes . This supports at least two kinetic events during the waiting associated with the 40-degree substep, plausibly chemical transformation/product release and conformational changes. It does not uniquely identify which rate belongs to hydrolysis or a particular product: different hidden-state networks can have the same waiting distribution. Three 120-degree catalytic cycles per revolution, partitioned into 80 and 40 degrees in the assay, are consistent with three catalytic sites.

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