Structural features of residue 110 in chain B

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Hydrophobic Interactions:
VAL B 110	LEU B 111	Dist=6.059	INTRA-CHAIN
VAL B 110	TYR B 118	Dist=6.099	INTRA-CHAIN
VAL B 110	LEU B 120	Dist=6.899	INTRA-CHAIN
VAL B 110	LEU A 128	Dist=6.999	INTER-CHAIN

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Protrusion Index:
VAL B 110 N	0.30
VAL B 110 CA	0.28
VAL B 110 C	0.35
VAL B 110 O	0.42
VAL B 110 CB	0.18
VAL B 110 CG1	0.13
VAL B 110 CG2	0.04

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Van der Waal's Interactions:
ILE B 85 CD1 1034	VAL B 110 CG2 1230	-0.132	INTRA-CHAIN
SER B 96 OG 1116	VAL B 110 CG2 1230	-0.016	INTRA-CHAIN
VAL B 110 CG2 1230	LEU B 120 CD2 1310	-0.204	INTRA-CHAIN
VAL B 110 CG2 1230	LEU A 128 CD2 587	-0.136	INTER-CHAIN
VAL B 110 CG2 1230	LEU A 131 CD2 612	-0.032	INTER-CHAIN