Structural features of residue 109 in chain B

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Hydrophobic Interactions:
VAL A 34	LEU B 109	Dist=6.326	INTER-CHAIN
ILE B 21	LEU B 109	Dist=6.882	INTRA-CHAIN
ILE B 27	LEU B 109	Dist=6.897	INTRA-CHAIN
VAL B 34	LEU B 109	Dist=5.774	INTRA-CHAIN
VAL B 57	LEU B 109	Dist=4.439	INTRA-CHAIN
VAL B 108	LEU B 109	Dist=5.724	INTRA-CHAIN
LEU B 109	ALA B 110	Dist=5.808	INTRA-CHAIN

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Protrusion Index:
LEU B 109 N	0.03
LEU B 109 CA	-0.01
LEU B 109 C	0.02
LEU B 109 O	0.01
LEU B 109 CB	-0.10
LEU B 109 CG	-0.12
LEU B 109 CD1	-0.11
LEU B 109 CD2	-0.11

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Van der Waal's Interactions:
VAL A 34 CG2 267	LEU B 109 CD2 1952	-0.523	INTER-CHAIN
ILE B 21 CD1 1253	LEU B 109 CD2 1952	-0.031	INTRA-CHAIN
ILE B 27 CD1 1304	LEU B 109 CD2 1952	-0.060	INTRA-CHAIN
PHE B 29 CZ 1322	LEU B 109 CD2 1952	-0.017	INTRA-CHAIN
VAL B 34 CG2 1363	LEU B 109 CD2 1952	-0.277	INTRA-CHAIN
VAL B 57 CG2 1559	LEU B 109 CD2 1952	-0.011	INTRA-CHAIN