Structural features of residue 110 in chain A

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Hydrophobic Interactions:
PHE A 95	VAL A 110	Dist=3.826	INTRA-CHAIN
VAL A 110	LEU A 111	Dist=6.111	INTRA-CHAIN
VAL A 110	TYR A 118	Dist=5.456	INTRA-CHAIN
VAL A 110	LEU A 120	Dist=6.733	INTRA-CHAIN

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Protrusion Index:
VAL A 110 N	0.34
VAL A 110 CA	0.29
VAL A 110 C	0.36
VAL A 110 O	0.42
VAL A 110 CB	0.20
VAL A 110 CG1	0.13
VAL A 110 CG2	0.09

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Van der Waal's Interactions:
SER A 96 OG 322	VAL A 110 CG2 436	-0.023	INTRA-CHAIN
VAL A 110 CG2 436	LEU A 120 CD2 516	-0.165	INTRA-CHAIN
VAL A 110 CG2 436	LEU E 131 CD2 611	-0.022	INTER-CHAIN