Structural features of residue 110 in chain A

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Hydrophobic Interactions:
ALA A 106	VAL A 110	Dist=6.363	INTRA-CHAIN
ALA A 109	VAL A 110	Dist=5.295	INTRA-CHAIN
VAL A 110	ALA A 111	Dist=5.422	INTRA-CHAIN
VAL A 110	ALA B 157	Dist=4.460	INTER-CHAIN

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Protrusion Index:
VAL A 110 N	0.31
VAL A 110 CA	0.46
VAL A 110 C	0.81
VAL A 110 O	1.04
VAL A 110 CB	0.47
VAL A 110 CG1	0.75
VAL A 110 CG2	0.31

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Van der Waal's Interactions:
ARG A 78 NH2 606	VAL A 110 CG2 852	-0.008	INTRA-CHAIN
ALA A 106 CB 820	VAL A 110 CG2 852	-0.033	INTRA-CHAIN
ALA A 109 CB 845	VAL A 110 CG2 852	-0.059	INTRA-CHAIN
VAL A 110 CG2 852	ALA A 111 CB 857	-0.010	INTRA-CHAIN
VAL A 110 CG2 852	GLY B 150 O 2534	-0.012	INTER-CHAIN
VAL A 110 CG2 852	LEU B 153 CD2 2556	-0.076	INTER-CHAIN
VAL A 110 CG2 852	ALA B 157 CB 2589	-0.278	INTER-CHAIN
VAL A 110 CG2 852	GLU B 158 OE2 2598	-0.011	INTER-CHAIN