Structural features of residue 110 in chain A

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Hydrophobic Interactions:
VAL A 36	PHE A 110	Dist=5.865	INTRA-CHAIN
PHE A 110	TYR A 111	Dist=6.069	INTRA-CHAIN
LEU B 83	PHE A 110	Dist=3.926	INTER-CHAIN
VAL B 84	PHE A 110	Dist=6.576	INTER-CHAIN
VAL B 92	PHE A 110	Dist=5.166	INTER-CHAIN

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Protrusion Index:
PHE A 110 N	-0.00
PHE A 110 CA	-0.03
PHE A 110 C	0.00
PHE A 110 O	0.02
PHE A 110 CB	-0.02
PHE A 110 CG	0.02
PHE A 110 CD1	0.00
PHE A 110 CD2	-0.02
PHE A 110 CE1	0.03
PHE A 110 CE2	0.03
PHE A 110 CZ	0.03

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Van der Waal's Interactions:
VAL A 36 CG2 228	PHE A 110 CZ 806	-0.010	INTRA-CHAIN
VAL A 39 CG2 251	PHE A 110 CZ 806	-0.269	INTRA-CHAIN
SER A 108 OG 789	PHE A 110 CZ 806	-0.014	INTRA-CHAIN
CYS A 109 SG 795	PHE A 110 CZ 806	-0.032	INTRA-CHAIN
VAL B 27 CG2 1166	PHE A 110 CZ 806	-0.039	INTER-CHAIN
ASP B 85 OD2 1630	PHE A 110 CZ 806	-0.126	INTER-CHAIN
ALA B 90 CB 1661	PHE A 110 CZ 806	-0.188	INTER-CHAIN
VAL B 92 CG2 1675	PHE A 110 CZ 806	-0.295	INTER-CHAIN