Structural features of residue 104 in chain B

********************************* Electrostatic Interactions: GLU B 28 OE1 LYS B 104 NZ -1.103 INTRA-CHAIN GLU B 28 OE2 LYS B 104 NZ -1.121 INTRA-CHAIN LYS B 100 NZ LYS B 104 NZ 0.564 INTRA-CHAIN LYS B 101 NZ LYS B 104 NZ 0.945 INTRA-CHAIN LYS B 104 NZ GLU B 28 OE2 -1.121 INTRA-CHAIN LYS B 104 NZ LYS B 100 NZ 0.564 INTRA-CHAIN LYS B 104 NZ LYS B 101 NZ 0.945 INTRA-CHAIN LYS B 104 NZ GLU B 106 OE2 -1.297 INTRA-CHAIN LYS B 104 NZ LYS B 111 NZ 0.530 INTRA-CHAIN LYS B 104 NZ LYS B 112 NZ 0.574 INTRA-CHAIN LYS B 104 NZ GLU B 115 OE2 -1.078 INTRA-CHAIN GLU B 106 OE1 LYS B 104 NZ -1.369 INTRA-CHAIN GLU B 106 OE2 LYS B 104 NZ -1.297 INTRA-CHAIN LYS B 111 NZ LYS B 104 NZ 0.530 INTRA-CHAIN LYS B 112 NZ LYS B 104 NZ 0.574 INTRA-CHAIN GLU B 115 OE1 LYS B 104 NZ -1.167 INTRA-CHAIN GLU B 115 OE2 LYS B 104 NZ -1.078 INTRA-CHAIN ********************************* Protrusion Index: LYS B 104 N 0.31 LYS B 104 CA 0.41 LYS B 104 C 0.49 LYS B 104 O 0.51 LYS B 104 CB 0.62 LYS B 104 CG 0.65 LYS B 104 CD 0.98 LYS B 104 CE 1.51 LYS B 104 NZ 1.57 ********************************* Van der Waal's Interactions: LYS B 101 NZ 1216 LYS B 104 NZ 1242 -0.011 INTRA-CHAIN LYS B 104 NZ 1242 VAL B 105 CG2 1249 -0.076 INTRA-CHAIN LYS B 104 NZ 1242 ASP B 108 OD2 1274 -0.447 INTRA-CHAIN