Structural features of residue 259 in chain A

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Hydrophobic Interactions:
TYR A 258	LEU A 259	Dist=6.047	INTRA-CHAIN
LEU A 259	VAL A 262	Dist=5.250	INTRA-CHAIN
LEU A 259	ALA A 310	Dist=3.928	INTRA-CHAIN
ALA B 257	LEU A 259	Dist=6.526	INTER-CHAIN
TYR B 258	LEU A 259	Dist=6.858	INTER-CHAIN

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Protrusion Index:
LEU A 259 N	-0.10
LEU A 259 CA	-0.12
LEU A 259 C	-0.14
LEU A 259 O	-0.12
LEU A 259 CB	-0.07
LEU A 259 CG	-0.04
LEU A 259 CD1	-0.08
LEU A 259 CD2	-0.04

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Van der Waal's Interactions:
GLY A 255 O 1893	LEU A 259 CD2 1926	-0.084	INTRA-CHAIN
LEU A 256 CD2 1901	LEU A 259 CD2 1926	-0.106	INTRA-CHAIN
LEU A 259 CD2 1926	ASP B 260 OD2 4416	-0.044	INTER-CHAIN
LEU A 259 CD2 1926	VAL A 262 CG2 1949	-0.010	INTRA-CHAIN
LEU A 259 CD2 1926	ILE A 275 CD1 2063	-0.018	INTRA-CHAIN
LEU A 259 CD2 1926	CYS A 306 SG 2303	-0.104	INTRA-CHAIN
LEU A 259 CD2 1926	MET A 307 CE 2311	-0.012	INTRA-CHAIN
LEU A 259 CD2 1926	ARG A 309 NH2 2331	-0.259	INTRA-CHAIN
LEU A 259 CD2 1926	ALA A 310 CB 2336	-0.120	INTRA-CHAIN
GLY B 255 O 4375	LEU A 259 CD2 1926	-0.011	INTER-CHAIN
ALA B 257 CB 4388	LEU A 259 CD2 1926	-0.132	INTER-CHAIN