Table 3. Energetic analysis of hydration sites where a water molecule is displaced by CDC25c phosphopeptide binding.

Residue	Site	Occupancy	Mean HBs	ΔH	−TΔS	ΔG	ResidueΔH	Residue −TΔS	ResidueΔG
Leu 1	A	0.30	2.60	1.57	0.85	2.42
Leu 1	B	0.30	3.18	−0.05	0.85	0.80
Leu 1	C	0.28	3.02	1.22	0.73	1.95	2.74	2.43	5.17
Leu 2	D	0.29	3.60	0.31	0.81	1.12
Leu 2	E	0.73	2.76	−2.50	2.46	−0.04
Leu 2	F	0.36	3.06	1.50	1.03	2.53	−0.69	4.30	3.61
Cys 3	G	0.33	3.06	2.01	0.85	2.86
Cys 3	H	0.58	2.64	−0.58	1.73	1.15	1.43	2.58	4.01
Ser 4	I	0.84	2.20	0.80	2.76	3.56	0.80	2.76	3.56
Asn 7	J	0.32	2.99	1.22	0.86	2.08
Asn 7	K	0.32	3.04	0.91	0.92	1.83	2.13	1.78	3.91
Total							6.41	13.85	20.26

Details of eleven hydration sites from the apo protein surface that overlap with sidechains of the bound phosphopeptide. The occupancy, mean number of hydrogen bonds (Mean HBs), change in enthalpy, entropy and free energy are relative to bulk water. The sites are labelled A–K and are displayed in Figure 6. The enthalpy, entropy and free energy are weighted by the occupancy of the site.