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The binding constants were obtained using a 1 1 Langmuir model.

As can be seen from Fig. 4A,B and B,C there was no significant difference in DCoA binding to the enzyme in the presence or absence of ATPγS and similar values of change in enthalpy and binding constant were obtained.

The lowest binding constant was obtained with phenylbutazone as site probe suggesting site I (sub-domain IIA) as the principal binding site for rivaroxaban (Fig. 3d).

Dissociation constants were obtained from equilibrium binding analysis, therefore no rate constants are given.

Inhibition constants were obtained by fitting to a simple binding curve (Stambach and Taylor 2003) using SigmaPlot.

The kinetic rate constants were obtained by fitting the curves to 1∶1 Langmuir binding model using BIAevaluation software.

Different kinetic constants were obtained with different primer-templates.

When the binding of the peptide to various other cyanine dyes (AF750, Cy5.5, Cy3.5) is investigated, varied affinity constants are obtained.

Apparent binding constants (KD) were obtained from the dose dependency of equilibrium binding and/or from the kinetic rate constants for complex formation (kon) and dissociation (koff) respectively.

The decay constant was obtained for each experiment.

The binding sites number, n and binding constant, K were obtained at various temperatures.