Table 3.

The interactions of the binding site residues with the best inhibitor of the related receptor

Receptor-complex	Binding energy	Surrounding residues
CatB (4)	-7.29	GLY198B, GLU122A, GLY27A, GLN23A, CYS29A, GLY74B, TRP30A, VAL176B, GLY197B, HIS199B, MET196B, ALA200B, PRO76B, ALA173B
HDAC2 (8)	-7.09	HIS33, PRO34, LEU276, PHE155, ASP104, GLY154, PHE210, HIS183,
Kinase (2)	-8.19	CYS531, TRP530, LEU513, PHE582, PHE594, ASN580, ASP593, LYS482, GLY463, ILE462, VAL470, SER464, PHE467, THR528, ALA480, LEU504,
rHA (4)	-7.32	ASP127, LYS133, SER96, ASN97, ASN99, ASP98, THR250, TYR134, ILE135, PRO137
RNR (10)	-8.25	SER625, LEU207, SER206, ALA466, SER465, LEU464, PRO621, THR209, SER224, LY253, CYS225, ASN437, LEU438, CYS439, ILE518, MET620
TopII (12)	-7.91	ILE104, PHE121, ARG77, ASP63, THR138, ASN129, SER128, ASP73, ASN99, THR195, ASN70, SER127, ALA71, VAL197, ILE67, VAL76
TS (2)	-8.31	GLU60, ILE81, CYS196, ASN229, PHE228, LEU224, GLY225, ASP221, ALA220, HIS250, TRP82, LEU195, VAL314

The first column shows the receptor and the number of its best active complex. The last column shows the surrounding residues of the docked complexes. Residues, which form hydrophobic interaction with the complexes are highlighted in bold and residues, which form hydrogen bonds are written in italic.