Structural features of residue 108 in chain A

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Hydrophobic Interactions:
ILE A 105	VAL A 108	Dist=5.591	INTRA-CHAIN
LEU A 107	VAL A 108	Dist=5.352	INTRA-CHAIN
VAL A 108	PHE A 165	Dist=6.756	INTRA-CHAIN
VAL A 108	LEU A 195	Dist=6.617	INTRA-CHAIN
TYR B 84	VAL A 108	Dist=6.461	INTER-CHAIN

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Protrusion Index:
VAL A 108 N	0.45
VAL A 108 CA	0.32
VAL A 108 C	0.34
VAL A 108 O	0.29
VAL A 108 CB	0.22
VAL A 108 CG1	0.15
VAL A 108 CG2	0.15

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Van der Waal's Interactions:
THR A 104 CG2 1315	VAL A 108 CG2 1344	-0.148	INTRA-CHAIN
ILE A 105 CD1 1323	VAL A 108 CG2 1344	-0.025	INTRA-CHAIN
LEU A 107 CD2 1337	VAL A 108 CG2 1344	-0.016	INTRA-CHAIN
VAL A 108 CG2 1344	PHE A 165 CZ 1799	-0.101	INTRA-CHAIN
VAL A 108 CG2 1344	ASN A 168 ND2 1822	-0.029	INTRA-CHAIN
VAL A 108 CG2 1344	LEU A 195 CD2 2046	-0.157	INTRA-CHAIN
TYR B 84 OH 1145	VAL A 108 CG2 1344	-0.014	INTER-CHAIN