Structural features of residue 110 in chain A

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Hydrophobic Interactions:
PHE A 95	VAL A 110	Dist=4.124	INTRA-CHAIN
VAL A 110	LEU A 111	Dist=6.001	INTRA-CHAIN
VAL A 110	TYR A 118	Dist=5.862	INTRA-CHAIN
VAL A 110	LEU A 120	Dist=6.840	INTRA-CHAIN
VAL A 110	LEU B 128	Dist=6.908	INTER-CHAIN

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Protrusion Index:
VAL A 110 N	0.26
VAL A 110 CA	0.23
VAL A 110 C	0.31
VAL A 110 O	0.36
VAL A 110 CB	0.16
VAL A 110 CG1	0.07
VAL A 110 CG2	0.08

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Van der Waal's Interactions:
SER A 96 OG 323	VAL A 110 CG2 437	-0.027	INTRA-CHAIN
VAL A 110 CG2 437	LEU A 120 CD2 517	-0.116	INTRA-CHAIN
VAL A 110 CG2 437	LEU B 128 CD2 1380	-0.077	INTER-CHAIN
VAL A 110 CG2 437	LEU B 131 CD2 1405	-0.024	INTER-CHAIN