TABLE 2.

Prediction of key amino acid residues during the docking of XaffOBP9 to different ligands.

No.	Ligand	Binding energy	Hydrophobic interactions	Van der Waals interactions	H-Bond
1	2-Phenyl-2-propanol	−6.5	Phe103 Phe55	Ile48 Met49 Ile53 Tyr106 Leu114 Val116	Tyr46 Ser50
2	Myrcene	−4.0	Leu2 Phe55 Lys70 Leu71 Ala74 Phe103 Tyr106 Leu114	Ile10 Val67 His113
3	Terpinolene	−6.9	Met 49 Phe55 Val67 Lys70 Lys71 Leu71 Tyr106 Leu114 Ser50
4	(S)-cis-Verbenol	−5.0	Lys15 Val18 Pro25 Ile28 Phe117	Ser19
5	Camphene	−6.9	Phe55 Val67 Lys70 Leu71 Ala74 Tyr106 Leu114	Leu2 Phe103
				His113
6	ɑ-Pinene	−6.7	Leu2 Phe55 Lys70 Leu71 Ala74 Phe103 Tyr106 Leu114	Val67 His113
7	3-Carene	−6.6	Leu2 Phe55 Lys70 Leu71 Ala74 Phe103 Tyr106 Leu114	Val67 His113
8	ɑ-Copaene	−6.8	Leu2 Ile10 Met49 Ile53 Phe55 Val67 Leu71 Phe103 Tyr106 Leu114	His113 Thr115
				Val116
9	(+)-Longifolene	−5.5	Phe55 Val67 Lys70 Leu71 Ala74 Phe103 Tyr106 His113 Leu114	Leu2 Ile10
				Ile53
10	Sabinene	−6.5	Phe55 Val67 Lys70 Leu71 Phe103 Tyr106 Leu114	His113 Thr115
11	(-)-β-Pinene	−6.6	Phe55 Lys70 Leu71 Ala74 Tyr106 Leu114	Phe103 Leu2 Val67 His113
12	Tetradecane	−3.0	Leu11 Cys17	Lys9 Ala12 Lys15 Ala16 Lys52 Ile53 Thy115 Val116 Phe117
13	m-Cymene	−6.7	Met49 Phe55 Val67 Leu71 Phe103 Tyr106 Leu114	Ser50
14	(S)- (-)-Limonene	−6.7	Met49 Phe55 Val67 Leu71 Phe103 Tyr106 Leu114	Ser50

Note: Key residues (overstriking) that bound to more than one ligand was selected as the object of subsequent site-directed mutation analysis.