Structural features of residue 109 in chain B

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Hydrophobic Interactions:
TYR B 109	ALA B 110	Dist=5.183	INTRA-CHAIN
TYR B 109	ALA B 113	Dist=6.733	INTRA-CHAIN
TYR B 109	VAL B 159	Dist=6.285	INTRA-CHAIN

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Protrusion Index:
TYR B 109 N	0.18
TYR B 109 CA	0.10
TYR B 109 C	-0.00
TYR B 109 O	-0.04
TYR B 109 CB	0.07
TYR B 109 CG	0.19
TYR B 109 CD1	0.26
TYR B 109 CD2	0.22
TYR B 109 CE1	0.41
TYR B 109 CE2	0.32
TYR B 109 CZ	0.47
TYR B 109 OH	0.91

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Van der Waal's Interactions:
ASN A 58 ND2 455	TYR B 109 OH 2163	-0.010	INTER-CHAIN
ARG B 105 NE 2127	TYR B 109 OH 2163	-0.101	INTRA-CHAIN
TYR B 109 OH 2163	CYS B 145 SG 2418	-0.026	INTRA-CHAIN
TYR B 109 OH 2163	CYS B 160 SG 2529	-0.097	INTRA-CHAIN