Measured ATPase activity in ADP molecules produced per KaiC monomer per day (24 hours), under different conditions.

First rows show results for parameters given in Tables 2 and 3. The last four rows show results for alternative models. When , the ATP hydrolysis in the CII domain is blocked when KaiA is bound to CII. When, , the CII domain has a higher relative affinity for ADP when the monomer is in the D state. The experimental values for the combined ATPase activity of the CI and CII domain, given in the last column, are taken from [25], and are shown for comparison.