Table 6. Binding Scores, Amino Acid Interactions, and Bond Lengths of the Selected Compounds within the Active Site of ecDHFR.

		Interacting residues
			Hydrophobic interaction
Compound	Binding score (S value) kcal/mol	H-bonding	π–π, π–σ, π–alkyl interactions	van der Waals interactions
9n	–12.37	Tyr59,	Ala7, Ala8, Leu54, Phe32, Met51, Phe48, Ile15, Tyr103,	Ala53, Gly52, Glyn29, Glu28, Ly26, Ala25, Ser24, Trp23, Ile21, Ser97, Val43, Thr47, Gly99, Gly98,
9o	–12.37	Tyr59	Ala7, Ala8, Leu54, Phe32, Met51, Phe48, Ile15, Tyr103,	Ala53, Gly52, Glyn29, Glu28, Ly26, Ala25, Ser24, Trp23, Ile21, Met6, Ser97, Val43, Thr47
TMP	–12.07	Glu28, Met6, Ser97, Tyr103	Ala8, Leu54, Val43, Phe32, Met51	Ala7, Leu64, Gly52, Met51, Met6, Glu28, Tyr59, Phe48, Thr47, Thr116, Ile21, Lys33, Gln29,