Table 3 Model parameter values

kG1₀

s^-1

Rate of binding of Gt to unphosphorylated R*

DO-13

3.28e-5

2.416e-2

Optimized

k RK1₀

s^-1

Rate of binding of RK to unphosphorylated R*

DO-2

7.543e-3

5.198e-2

Optimized

m _RK

Slope of the rate of decrease in RK affinity for R* with increasing phosphorylation events

DO-2

0.1

Manually tuned

k Arr

s^-1

Rate of binding of Arr to R* with a single phosphate attached

DO-5

6.092e-10

6.204e-8

Optimized

m _Arr

Slope of t The rate of increase of Arr-R* affinity with additional R* phosphorylations

DO-5

1.14e-8

Optimized

k A2

s ^-1

Rate constant of dissociation of R* from Arr · R* without R* deactivation

DO-5

3.232e-3

2.754e-4

Optimized

k A3

s^-1

Rate constant of dissociation of R* from Arr · R* after R* deactivation

DO-6

4.451e-2

2.649e-2

Optimized

k A4

s ^-1

Rate constant of Arr self-association

3, 4

1.787e-8

Optimized

k A5

s ^-1

Rate constant of Arr self-dissociation

3, 4

0.646

Manually tuned

k RGS1

s ^-1

Rate of binding RGS to an effector complex

DO-22, DO-24

1.57e-7

1.86e-7

Optimized

k PDE_shutoff

s ^-1

Rate constant of PDE-induced shutoff of an effector complex

DO-26, DO-27

3.3e-2

2e-2

Manually tuned

k Rec1

μM^-1 s^-1

Ca²⁺⁻dependent rate of Rec conformational change from “tense” to “relaxed” form

1

0.011

[43]

k Rec2

s ^-1

Rate of Rec conformational change from “relaxed” to “tense” form

1

0.05

[43]