Structural features of residue 110 in chain K

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Hydrophobic Interactions:
ALA K 109	PHE K 110	Dist=5.725	INTRA-CHAIN
PHE K 110	VAL K 111	Dist=5.908	INTRA-CHAIN
PHE K 110	VAL K 124	Dist=5.793	INTRA-CHAIN

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Van der Waal's Interactions:
GLN J 91 NE2 4885	PHE K 110 CZ 6485	-0.810	INTER-CHAIN
PHE K 110 CZ 6485	VAL K 124 CG2 6600	-0.071	INTRA-CHAIN
PHE K 110 CZ 6485	GLY K 125 O 6604	-0.014	INTRA-CHAIN