Structural features of residue 295 in chain A

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Hydrophobic Interactions:
PHE A 283	VAL A 295	Dist=5.418	INTRA-CHAIN
LEU A 293	VAL A 295	Dist=5.999	INTRA-CHAIN
VAL A 295	ILE A 297	Dist=6.765	INTRA-CHAIN

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Protrusion Index:
VAL A 295 N	0.36
VAL A 295 CA	0.42
VAL A 295 C	0.39
VAL A 295 O	0.34
VAL A 295 CB	0.25
VAL A 295 CG1	0.21
VAL A 295 CG2	0.12

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Van der Waal's Interactions:
PHE A 283 CZ 200	VAL A 295 CG2 295	-0.389	INTRA-CHAIN
LEU A 285 CD2 213	VAL A 295 CG2 295	-0.016	INTRA-CHAIN
LEU A 293 CD2 279	VAL A 295 CG2 295	-0.010	INTRA-CHAIN
VAL A 295 CG2 295	ILE A 311 CD1 408	-0.304	INTRA-CHAIN
VAL A 295 CG2 295	ILE A 329 CD1 497	-0.018	INTRA-CHAIN
VAL A 295 CG2 295	PHE A 331 CZ 517	-0.009	INTRA-CHAIN
VAL A 295 CG2 295	CYS B 370 SG 1723	-0.088	INTER-CHAIN