Structural features of residue 285 in chain B

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Hydrophobic Interactions:
TYR A 61	ALA B 285	Dist=5.597	INTER-CHAIN
ALA B 284	ALA B 285	Dist=5.321	INTRA-CHAIN
ALA B 285	PHE B 286	Dist=5.720	INTRA-CHAIN
ALA B 285	LEU B 288	Dist=5.944	INTRA-CHAIN

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Protrusion Index:
ALA B 285 N	0.20
ALA B 285 CA	0.18
ALA B 285 C	0.29
ALA B 285 O	0.23
ALA B 285 CB	0.20

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Van der Waal's Interactions:
TYR A 61 OH 452	ALA B 285 CB 4681	-0.030	INTER-CHAIN
ASP B 282 O 4658	ALA B 285 CB 4681	-0.133	INTRA-CHAIN
ALA B 284 CB 4676	ALA B 285 CB 4681	-0.046	INTRA-CHAIN
ALA B 285 CB 4681	SER B 287 OG 4698	-0.012	INTRA-CHAIN
ALA B 285 CB 4681	LEU B 288 CD2 4706	-0.011	INTRA-CHAIN
ALA B 285 CB 4681	VAL B 289 CG2 4713	-0.014	INTRA-CHAIN