Structural basis of RGD-hirudin binding to thrombin: Tyr3 and five C-terminal residues are crucial for inhibiting thrombin activity

Table 2 Calculate the effect of single-point mutations on the binding affinity

Residues	Mutation	VDW Term	Electrostatic Term	Entropy Term	Weighted Mutation Energy	Effect of Mutation
Tyr3	Ala	6.58	-1.92	0.12	2.2	destabilizing
Ser50	Ala	6.68	0.41	-0.58	2.71	destabilizing
Gln53	Ala	8.99	-0.47	-2.02	2.16	destabilizing
Asp55	Ala	8.7	3.15	-0.94	4.56	destabilizing
Glu57	Ala	0.72	1.78	-0.13	1.02	destabilizing
Ile59	Ala	3.19	-0.4	-0.58	0.78	destabilizing

VDW Term: The van der Waals contribution to the binding energy differences.
Electrostatic Term: The electrostatic contribution to the binding energy difference between wild type and mutated structures.
Entropy Term: The side-chain entropy contribution to the binding energy differences.
Non-polar Term: The non-polar (surface tension) contribution to the binding energy differences.
Weighted Mutation Energy: The total free energy difference between the wild type and mutated structures. It is calculated as a weighted sum of the VDW, Electrostatic, Entropy and Non-polar terms.

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