Mechanism of PhosphoThreonine/Serine Recognition and Specificity for Modular Domains from All-atom Molecular Dynamics

Table 2 Global MM-PBSA energy calculations

domain	mutated site	mutation	ΔΔU_VDW	ΔΔU_Coul	ΔΔW_PB	ΔΔE_ele	ΔΔE_tot-np	ΔΔW_np	ΔΔE_tot
Rad53-FHA1	1	pT→pS	2.50	-34.34	37.83	3.49	5.99	0.75	6.74
Rad53-FHA1	1	pT→pS	0.44	-13.74	16.08	2.33	2.77	0.72	3.49
Dun1-FHA	1	pT→pS	-2.63	-13.70	18.84	5.15	2.52	2.34	4.86
Ki67-FHA	1	pT→pS	4.30	-8.77	7.79	-0.98	3.32	-0.84	2.48
Dun1-FHA	2	pT→pS	-2.54	-59.30	63.39	4.09	1.55	1.95	3.50
Ki67-FHA	2	pS→pT	0.94	19.77	-20.15	-0.38	0.55	0.36	0.91
BRCT	1	pS→pT	-3.33	28.77	-23.67	5.10	1.77	0.84	2.61
WW	1	pS→pT	-1.03	-39.75	36.78	-2.96	-3.99	-0.01	-4.00

ΔΔU_Coul and ΔΔU_vdw are the electrostatic and van der Waals interactions, respectively, between the wild-type and mutants; ΔΔW_PB and ΔΔW_np are the polar and non-polar contributions from the solvation energy. ΔΔE_ele represents the sum of ΔΔU_Coul and ΔΔW_PB. ΔΔ indicates the changes between two calculations of the mutated and non-mutated state. For example, ΔΔU_VDW = ΔU_VDW,pSer-ΔU_VDW,pThr, where ΔU_VDW is the interaction energy between the phosphopeptide and the domain.

ISSN: 2046-1682