Structural features of residue 109 in chain B

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Hydrophobic Interactions:
ALA B 80	TYR B 109	Dist=3.830	INTRA-CHAIN
ALA B 84	TYR B 109	Dist=4.842	INTRA-CHAIN
LEU B 105	TYR B 109	Dist=6.552	INTRA-CHAIN
LEU B 106	TYR B 109	Dist=6.401	INTRA-CHAIN
TYR B 109	ALA B 111	Dist=5.119	INTRA-CHAIN
TYR B 109	LEU A 262	Dist=6.625	INTER-CHAIN

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Protrusion Index:
TYR B 109 N	0.13
TYR B 109 CA	0.09
TYR B 109 C	0.13
TYR B 109 O	0.09
TYR B 109 CB	0.08
TYR B 109 CG	-0.02
TYR B 109 CD1	-0.02
TYR B 109 CD2	-0.04
TYR B 109 CE1	-0.06
TYR B 109 CE2	-0.10
TYR B 109 CZ	-0.06
TYR B 109 OH	-0.06

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Van der Waal's Interactions:
PHE A 36 CZ 293	TYR B 109 OH 845	-0.014	INTER-CHAIN
ALA B 40 CB 324	TYR B 109 OH 845	-0.499	INTRA-CHAIN
ASP B 45 OD2 362	TYR B 109 OH 845	-0.008	INTRA-CHAIN
MET B 81 CE 620	TYR B 109 OH 845	-0.027	INTRA-CHAIN
LEU B 105 CD2 809	TYR B 109 OH 845	-0.013	INTRA-CHAIN
TYR B 109 OH 845	LEU A 262 CD2 1975	-0.218	INTER-CHAIN
TYR B 109 OH 845	PHE A 295 CZ 2208	-0.250	INTER-CHAIN
TYR B 109 OH 845	ARG B 298 NH2 2232	-0.016	INTRA-CHAIN