Structural features of residue 112 in chain A

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Hydrophobic Interactions:
PHE A 109	LEU A 112	Dist=5.445	INTRA-CHAIN
LEU A 112	ALA A 115	Dist=5.292	INTRA-CHAIN
LEU A 112	VAL A 116	Dist=6.286	INTRA-CHAIN
LEU A 112	ALA A 292	Dist=5.918	INTRA-CHAIN
ALA B 20	LEU A 112	Dist=4.354	INTER-CHAIN
ALA B 21	LEU A 112	Dist=6.382	INTER-CHAIN
ALA B 24	LEU A 112	Dist=4.257	INTER-CHAIN

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Protrusion Index:
LEU A 112 N	0.26
LEU A 112 CA	0.16
LEU A 112 C	0.18
LEU A 112 O	0.15
LEU A 112 CB	0.04
LEU A 112 CG	0.02
LEU A 112 CD1	-0.00
LEU A 112 CD2	0.04

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Van der Waal's Interactions:
GLY A 108 O 824	LEU A 112 CD2 859	-0.016	INTRA-CHAIN
PHE A 109 CZ 835	LEU A 112 CD2 859	-0.030	INTRA-CHAIN
LEU A 112 CD2 859	ALA A 115 CB 876	-0.012	INTRA-CHAIN
LEU A 112 CD2 859	VAL A 116 CG2 883	-0.034	INTRA-CHAIN
LEU A 112 CD2 859	LEU A 288 CD2 2198	-0.282	INTRA-CHAIN
LEU A 112 CD2 859	LEU A 291 CD2 2221	-0.026	INTRA-CHAIN
LEU A 112 CD2 859	ALA A 292 CB 2226	-0.026	INTRA-CHAIN
ALA B 20 CB 2705	LEU A 112 CD2 859	-0.340	INTER-CHAIN
ALA B 21 CB 2710	LEU A 112 CD2 859	-0.170	INTER-CHAIN
ALA B 24 CB 2732	LEU A 112 CD2 859	-0.095	INTER-CHAIN
LEU B 58 CD2 2997	LEU A 112 CD2 859	-0.013	INTER-CHAIN