Structural features of residue 158 in chain B

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Hydrophobic Interactions:
PHE B 154	TYR B 158	Dist=6.028	INTRA-CHAIN
ALA B 155	TYR B 158	Dist=5.986	INTRA-CHAIN
ALA B 157	TYR B 158	Dist=5.417	INTRA-CHAIN
TYR B 158	ALA B 159	Dist=5.461	INTRA-CHAIN
TYR B 158	ILE B 162	Dist=6.411	INTRA-CHAIN
TYR B 158	LEU B 255	Dist=6.342	INTRA-CHAIN

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Protrusion Index:
TYR B 158 N	0.50
TYR B 158 CA	0.43
TYR B 158 C	0.58
TYR B 158 O	0.54
TYR B 158 CB	0.25
TYR B 158 CG	0.20
TYR B 158 CD1	0.21
TYR B 158 CD2	0.20
TYR B 158 CE1	0.16
TYR B 158 CE2	0.18
TYR B 158 CZ	0.16
TYR B 158 OH	0.25

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Van der Waal's Interactions:
TYR B 158 OH 1229	TYR B 167 OH 1304	-0.065	INTRA-CHAIN
TYR B 158 OH 1229	LEU B 255 CD2 2000	-0.007	INTRA-CHAIN
TYR B 158 OH 1229	PRO A 272 CD 2117	-0.029	INTER-CHAIN
TYR B 158 OH 1229	VAL A 314 CG2 2460	-0.019	INTER-CHAIN