Structural features of residue 289 in chain B

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Hydrophobic Interactions:
PHE B 286	VAL B 289	Dist=5.248	INTRA-CHAIN
LEU B 288	VAL B 289	Dist=5.397	INTRA-CHAIN
VAL B 289	ALA B 292	Dist=5.680	INTRA-CHAIN

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Protrusion Index:
VAL B 289 N	0.20
VAL B 289 CA	0.23
VAL B 289 C	0.16
VAL B 289 O	0.16
VAL B 289 CB	0.22
VAL B 289 CG1	0.18
VAL B 289 CG2	0.28

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Van der Waal's Interactions:
ASN A 14 ND2 92	VAL B 289 CG2 4713	-0.015	INTER-CHAIN
TYR A 16 OH 109	VAL B 289 CG2 4713	-0.011	INTER-CHAIN
GLN A 17 NE2 118	VAL B 289 CG2 4713	-0.230	INTER-CHAIN
PHE B 109 CZ 3396	VAL B 289 CG2 4713	-0.243	INTRA-CHAIN
ALA B 285 CB 4681	VAL B 289 CG2 4713	-0.014	INTRA-CHAIN
PHE B 286 CZ 4692	VAL B 289 CG2 4713	-0.035	INTRA-CHAIN
LEU B 288 CD2 4706	VAL B 289 CG2 4713	-0.017	INTRA-CHAIN
VAL B 289 CG2 4713	ALA B 292 CB 4734	-0.016	INTRA-CHAIN
VAL B 289 CG2 4713	THR B 293 CG2 4741	-0.015	INTRA-CHAIN