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Table 9 Interatomic interactions for the mutant hypothetical hsCENP-HIKM complex

From: Computer-aided molecular modeling and structural analysis of the human centromere protein–HIKM complex

Chain(s) Residue(s) VDW H-bond Hydrophobic
H ALA-219 H: PHE-216
H: GLN-217
H: LEU-221
H: SER-223
H: VAL-215
H: PHE-216
H: SER-223
K: PHE-183
K: PHE-188
H ALA-225 H: ILE-220 H: ILE-220 H: ILE-220
H ALA-233 H: GLU-235 H: ASP-230
H: ILE-236
H: VAL-237
H: TRP-227
H: ASP-230
H ALA-234 H: ASP-230; I: LEU-183
H: ALA-232
H: VAL-237
H: LEU-238
H: TRP-227; I: LEU-183
H: ASP-230
H: PRO-231
H: LEU-238
I: PHE-189
H ALA-238 H: GLU-235
H: LYS-242
H: LYS-234
H: GLU-235
H: VAL-237
I: LEU-183
I: PHE-187
M ALA-94 M: ALA-90
M: SER-91
M: PHE-92
M: LYS-96
M: LEU-166
M: ALA-90
M: SER-91
M: LYS-96
M: LEU-163
M: LEU-163; I: TRP-461
M: LEU-166
M GLU-163 M: SER-161
M: LEU-165
M: LEU-166
M: LEU-94; I: TRP-461
M: SER-161
M: LEU-166
M: LEU-94
  1. The first and second columns show the mutated chains and residues of interest, while the remaining columns represent the observed interaction types (van der Waals, hydrogen bond and hydrophobic interactions, respectively). Specific chains and residues that interact with the mutant residues are presented in the corresponding columns for each interaction type