Structural features of residue 109 in chain B

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Hydrophobic Interactions:
TYR A 16	PHE B 109	Dist=6.384	INTER-CHAIN
PHE B 109	ALA B 292	Dist=5.063	INTRA-CHAIN

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Protrusion Index:
PHE B 109 N	0.23
PHE B 109 CA	0.15
PHE B 109 C	0.20
PHE B 109 O	0.27
PHE B 109 CB	0.15
PHE B 109 CG	0.13
PHE B 109 CD1	0.11
PHE B 109 CD2	0.13
PHE B 109 CE1	0.12
PHE B 109 CE2	0.11
PHE B 109 CZ	0.15

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Van der Waal's Interactions:
TYR A 16 OH 109	PHE B 109 CZ 3396	-0.051	INTER-CHAIN
TYR A 61 OH 452	PHE B 109 CZ 3396	-0.010	INTER-CHAIN
GLY B 108 O 3385	PHE B 109 CZ 3396	-0.014	INTRA-CHAIN
PHE B 109 CZ 3396	LEU B 288 CD2 4706	-0.096	INTRA-CHAIN
PHE B 109 CZ 3396	VAL B 289 CG2 4713	-0.243	INTRA-CHAIN
PHE B 109 CZ 3396	ALA B 292 CB 4734	-0.371	INTRA-CHAIN
PHE B 109 CZ 3396	THR B 293 CG2 4741	-0.036	INTRA-CHAIN