Structural features of residue 110 in chain E

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Hydrophobic Interactions:
VAL E 110	LEU E 111	Dist=6.111	INTRA-CHAIN
VAL E 110	TYR E 118	Dist=5.456	INTRA-CHAIN
VAL E 110	LEU E 120	Dist=6.733	INTRA-CHAIN

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

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