Structural features of residue 110 in chain A

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Hydrophobic Interactions:
PHE A 95	VAL A 110	Dist=4.128	INTRA-CHAIN
VAL A 110	LEU A 111	Dist=5.946	INTRA-CHAIN
VAL A 110	TYR A 118	Dist=5.383	INTRA-CHAIN
VAL A 110	LEU A 120	Dist=6.634	INTRA-CHAIN
VAL A 110	LEU B 131	Dist=6.993	INTER-CHAIN

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Protrusion Index:
VAL A 110 N	0.29
VAL A 110 CA	0.23
VAL A 110 C	0.34
VAL A 110 O	0.42
VAL A 110 CB	0.16
VAL A 110 CG1	0.12
VAL A 110 CG2	0.07

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Van der Waal's Interactions:
SER A 96 OG 340	VAL A 110 CG2 454	-0.017	INTRA-CHAIN
VAL A 110 CG2 454	LEU A 120 CD2 534	-0.220	INTRA-CHAIN
VAL A 110 CG2 454	LEU B 128 CD2 604	-0.113	INTER-CHAIN
VAL A 110 CG2 454	LEU B 131 CD2 629	-0.042	INTER-CHAIN