Structural features of residue 110 in chain B

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Hydrophobic Interactions:
TYR B 106	LEU B 110	Dist=6.935	INTRA-CHAIN
LEU B 110	LEU B 113	Dist=5.858	INTRA-CHAIN
LEU B 110	TYR A 175	Dist=5.214	INTER-CHAIN
LEU B 110	VAL A 176	Dist=6.209	INTER-CHAIN
LEU B 110	LEU A 181	Dist=5.796	INTER-CHAIN

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Protrusion Index:
LEU B 110 N	0.23
LEU B 110 CA	0.26
LEU B 110 C	0.22
LEU B 110 O	0.23
LEU B 110 CB	0.18
LEU B 110 CG	0.18
LEU B 110 CD1	0.13
LEU B 110 CD2	0.20

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Van der Waal's Interactions:
PRO B 104 CD 2547	LEU B 110 CD2 2599	-0.030	INTRA-CHAIN
LEU B 110 CD2 2599	VAL A 176 CG2 1396	-0.105	INTER-CHAIN