Structural features of residue 109 in chain A

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Hydrophobic Interactions:
TYR A 59	LEU A 109	Dist=5.989	INTRA-CHAIN
PHE A 107	LEU A 109	Dist=6.476	INTRA-CHAIN

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Protrusion Index:
LEU A 109 N	0.11
LEU A 109 CA	0.16
LEU A 109 C	0.28
LEU A 109 O	0.27
LEU A 109 CB	0.05
LEU A 109 CG	-0.00
LEU A 109 CD1	-0.04
LEU A 109 CD2	-0.01

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Van der Waal's Interactions:
ILE A 62 CD1 440	LEU A 109 CD2 800	-0.009	INTRA-CHAIN
CYS A 81 SG 570	LEU A 109 CD2 800	-0.021	INTRA-CHAIN
TRP A 83 CH2 596	LEU A 109 CD2 800	-0.013	INTRA-CHAIN
ASP A 88 OD2 635	LEU A 109 CD2 800	-0.109	INTRA-CHAIN
GLY A 108 O 792	LEU A 109 CD2 800	-0.044	INTRA-CHAIN
LYS B 60 NZ 420	LEU A 109 CD2 800	-0.049	INTER-CHAIN
ILE B 62 CD1 440	LEU A 109 CD2 800	-0.161	INTER-CHAIN