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Table 2 Amino acid residues participating in interactions of conotoxin 1XGA with the α/γ receptor interface determined by docking simulation, as well as average occupancies of the main anchor point residues participating in interactions after 7 ns molecular dynamics simulation along the trajectory.

From: Binding of long-chain α-neurotoxin would stabilize the resting state of nAChR: A comparative study with α-conotoxin

  T.nAChR subunit interface
1-XGA Principal site (alpha 1) Complementary site (gamma) Average occupancy during MD
GLU 1    
CYS 2    
CYS 3    
ASN 4 Thr 191, Cys 192   Asn4 Thr191 0.9
    Asn4 Cys192 0.8
PRO 5    
ALA 6 Tyr 190, Val 188   Ala 6 Tyr190 0.5
    Ala 6 Val 188 0.4
CYS 7 Tyr 190   Cys 7 Tyr 190 0.8
GLY 8   Trp 54  
ARG 9* Trp 149, Val 91, Leu 92, Asp 99, Tyr 198 Leu 118, Trp 54, Thr 37, Asn 38 Arg9* Trp 149 0.7
    Arg9* Leu 92 0.9
    Arg9* Trp 54 0.9
    Arg9* Thr 37 0.8
    Arg9* Asn 38 0.8
HIS 10   Leu 118, Tyr 116, Leu 108, Arg 78 His10 Leu108 0.8
    His10 Arg 78 0.8
TYR 11   Trp 54, Thr 35, Asp 176 Tyr11 Trp54 0.9
    Tyr 11Asp 176 0.7
SER 12   Glu 56, Leu 118, Lys 33 Ser 12 Leu118 0.4
CYS 13   Tyr 116 Cys13 Tyr116 0.5
  1. The critical residue Arg 9 is marked with an asterix. Amino acids making hydrogen bonds are underlined.