Structural features of residue 112 in chain A

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Hydrophobic Interactions:
PHE A 108	VAL A 112	Dist=6.538	INTRA-CHAIN
LEU A 111	VAL A 112	Dist=5.364	INTRA-CHAIN
VAL A 112	VAL B 150	Dist=5.965	INTER-CHAIN
VAL A 112	PHE A 161	Dist=6.139	INTRA-CHAIN
ILE B 100	VAL A 112	Dist=5.885	INTER-CHAIN

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Protrusion Index:
VAL A 112 N	0.05
VAL A 112 CA	0.07
VAL A 112 C	0.11
VAL A 112 O	0.12
VAL A 112 CB	0.05
VAL A 112 CG1	0.02
VAL A 112 CG2	-0.02

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Van der Waal's Interactions:
PHE A 108 CZ 884	VAL A 112 CG2 910	-0.078	INTRA-CHAIN
THR A 109 CG2 891	VAL A 112 CG2 910	-0.015	INTRA-CHAIN
GLY A 110 O 895	VAL A 112 CG2 910	-0.013	INTRA-CHAIN
LEU A 111 CD2 903	VAL A 112 CG2 910	-0.086	INTRA-CHAIN
VAL A 112 CG2 910	THR A 115 CG2 932	-0.010	INTRA-CHAIN
VAL A 112 CG2 910	VAL B 150 CG2 3240	-0.072	INTER-CHAIN
VAL A 112 CG2 910	ALA B 153 CB 3263	-0.022	INTER-CHAIN
VAL A 112 CG2 910	PHE A 161 CZ 1281	-0.240	INTRA-CHAIN
ILE B 100 CD1 2858	VAL A 112 CG2 910	-0.012	INTER-CHAIN