Structural features of residue 111 in chain B

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Hydrophobic Interactions:
LEU B 52	TYR B 111	Dist=5.891	INTRA-CHAIN
ALA B 56	TYR B 111	Dist=5.625	INTRA-CHAIN
VAL B 108	TYR B 111	Dist=5.893	INTRA-CHAIN
LEU B 110	TYR B 111	Dist=5.497	INTRA-CHAIN
TYR B 111	LEU B 115	Dist=6.335	INTRA-CHAIN

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Protrusion Index:
TYR B 111 N	0.10
TYR B 111 CA	0.10
TYR B 111 C	0.16
TYR B 111 O	0.17
TYR B 111 CB	0.09
TYR B 111 CG	0.20
TYR B 111 CD1	0.11
TYR B 111 CD2	0.29
TYR B 111 CE1	0.06
TYR B 111 CE2	0.23
TYR B 111 CZ	0.16
TYR B 111 OH	0.20

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Van der Waal's Interactions:
ILE A 28 CD1 39	TYR B 111 OH 1501	-0.263	INTER-CHAIN
LEU A 36 CD2 95	TYR B 111 OH 1501	-0.071	INTER-CHAIN
LEU B 49 CD2 1001	TYR B 111 OH 1501	-0.011	INTRA-CHAIN
SER B 53 OG 1034	TYR B 111 OH 1501	-0.134	INTRA-CHAIN
ALA B 56 CB 1055	TYR B 111 OH 1501	-0.048	INTRA-CHAIN
TYR B 111 OH 1501	GLN B 112 NE2 1510	-0.012	INTRA-CHAIN
TYR B 111 OH 1501	LEU B 115 CD2 1531	-0.262	INTRA-CHAIN