Structural features of residue 110 in chain B

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Hydrophobic Interactions:
LEU A 83	PHE B 110	Dist=3.904	INTER-CHAIN
VAL A 92	PHE B 110	Dist=5.173	INTER-CHAIN
VAL B 36	PHE B 110	Dist=5.987	INTRA-CHAIN
PHE B 110	TYR B 111	Dist=6.067	INTRA-CHAIN

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Protrusion Index:
PHE B 110 N	0.03
PHE B 110 CA	-0.00
PHE B 110 C	0.04
PHE B 110 O	0.04
PHE B 110 CB	0.02
PHE B 110 CG	0.01
PHE B 110 CD1	0.01
PHE B 110 CD2	-0.02
PHE B 110 CE1	0.04
PHE B 110 CE2	0.01
PHE B 110 CZ	0.01

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Van der Waal's Interactions:
VAL A 27 CG2 160	PHE B 110 CZ 1812	-0.043	INTER-CHAIN
ALA A 90 CB 655	PHE B 110 CZ 1812	-0.220	INTER-CHAIN
VAL A 92 CG2 669	PHE B 110 CZ 1812	-0.348	INTER-CHAIN
VAL B 36 CG2 1234	PHE B 110 CZ 1812	-0.012	INTRA-CHAIN
VAL B 39 CG2 1257	PHE B 110 CZ 1812	-0.317	INTRA-CHAIN
SER B 108 OG 1795	PHE B 110 CZ 1812	-0.014	INTRA-CHAIN