Structural features of residue 380 in chain K

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Hydrophobic Interactions:
VAL K 295	ALA K 380	Dist=4.391	INTRA-CHAIN
PHE K 378	ALA K 380	Dist=5.792	INTRA-CHAIN
LEU K 379	ALA K 380	Dist=4.927	INTRA-CHAIN
TYR L 199	ALA K 380	Dist=6.399	INTER-CHAIN

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Van der Waal's Interactions:
VAL K 295 CG2 5108	ALA K 380 CB 5755	-0.096	INTRA-CHAIN
PRO K 296 CD 5115	ALA K 380 CB 5755	-0.387	INTRA-CHAIN
LEU K 379 CD2 5750	ALA K 380 CB 5755	-0.009	INTRA-CHAIN
ALA K 380 CB 5755	GLY K 381 O 5759	-0.073	INTRA-CHAIN
ALA K 380 CB 5755	ASN K 385 ND2 5795	-0.058	INTRA-CHAIN
SER L 198 OG 7377	ALA K 380 CB 5755	-0.081	INTER-CHAIN
TYR L 199 OH 7389	ALA K 380 CB 5755	-0.101	INTER-CHAIN