Ding patterns with the active site. By using iGEMDOCK post run analysis procedures, the compounds were clustered and scored on a generic evolutionary method. The clustering and building a dendrogram of the docked compounds is based on the interaction profiles including the atomic composition of the interacting partners (Fig. 2C). A dendrogram and interaction profiles of compounds is given in Fig. 3A. The figure summarizes the profile of interaction of 18325633 each compound with residues of PAZ domain. Electrostatic, hydrogen bonding and van der Waals Eliglustat price interactions of each compound with the main chain or side chain of each residue are assigned. The rule of each residue can be thoroughly assigned e.g. the most important van der Waals interactions is occurring with F669, Y681, I706 and LTable 2. The docking results by using the docking server.Compound 8.82 27.07 26.6 24.15 26.62 28.26 26.76 25.55 27.35 27.25 25.75 27.16 27.71 27.46 28.66 79.39 21.94 21.23 20.32 20.75 20.53 20.62 20.45 20.66 20.68 20.18 20.09 20.9 24.8 9.17 28.26 27.9 28.65 210.06 27.8 27.89 26.71 26.4 26.13 20.79 29.45 77.46 26.03 8.85 29.01 28.43 29.26 210.5 28.45 28.57 26.89 26.49 27.03 20.83 28.29 21.38 29.1 20.93 28.09 20.04 25.79 21.41 28.66 21 28.35 20.12 25.67 21.35 28.11 748.43 466.14 688 899 484 667 820 688 901.26 1188 995.45 1117 744 901.48 945.85 808.5 835.7 719 780.3 664 616.33 20.65 28.91 747.37 20.08 26.7 503.7 20.47 24.62 727.216 20.66 27.27 732.72 20.08 27.15 115.63 17.56 143.04 58.9 402.26 228.99 47.67 466.86 140.99 49.19 424.55 74.8 38.27 nd nd nd 49.61 4.8 12.75 3 42.37 48.57 57.82 21.8 60.14 572.Estimated free energyInhibition constant Ki Electrostatic energy Total intermolecular energy Interaction surface 0.48 0.29 0.28 0.48 0.37 0.4 0.42 0.32 0.34 0.3 0.32 0.36 0.2 0.37 0.6 0.65 1.1 0.58 0.7 0.78 1.05 0.74 0.26 0.3 0.28 0.vDw + Hbond + desolvation energyRL/FLt26.tt25.ttt22.U25.U25.U24.U24.U25.U24.U25.U25.U24.U10bbn25.U11btbt26.U174.5 siRNA Recognition by PAZ DomainU15.U57.U15BbBb25.U16BnBn27.U17BhBh26.U18ByBy27.u19bBBn25.u20BB25.Utd25.Utd26.U21RHRH25.The ligands are ordered as shown in Fig. 1). The output data included free energy (Kcal/mol), inhibition constant (mM),van der Waals interactions, Hydrogen bonding and desolvation energy (Kcal/mol), electrostatic energy (Kcal/ mol) and interaction surface. RL/FL indicates Renilla luciferace expression normalized by firefly luciferase data. doi:10.1371/journal.pone.0057140.tsiRNA Recognition by PAZ DomainTable 3. Correlation analysis for RNAi activity and the measured parameters produced by iGEMDOCK.RL/FL 1.00 20.2338 20.4163* 0.1918 0.2236 RL/FL 20.1681 20.5756* 20.1976 20.1478 *Pearson’s correlation Fexinidazole site coefficient is calculated by STATA. Data showing significant correlation at 0.05 level are marked by asterisk. doi:10.1371/journal.pone.0057140.t004 1.00 1.00 1.00 0.7744* 0.6443* 20.303 vDw + Hbond + desolvation energy Total intermolecular energy Estimated free energy Inhibition constant Ki Electrostatic energyTotal Energy Total Energy 1.00 VDW HBond energy Elec 0.833* 0.4091 0.VDWHBondElecAverConPair RL/FL Interaction surface1.00 20.08 20.0593 0.4168* 1.00 20.0198 0.2372 1.00 0.2036 1.00 0.1271 20.4681* 1.AverConPair 0.4799* RL/FL 20.20.4153* 0.*Pearson’s correlation coefficient is calculated by STATA. Data showing significant correlation at 0.05 level are marked by asterisk. doi:10.1371/journal.pone.0057140.tDissection of receptor-ligand binding forcesIn dissecting the forces accompanying the recognition of siRNAs.Ding patterns with the active site. By using iGEMDOCK post run analysis procedures, the compounds were clustered and scored on a generic evolutionary method. The clustering and building a dendrogram of the docked compounds is based on the interaction profiles including the atomic composition of the interacting partners (Fig. 2C). A dendrogram and interaction profiles of compounds is given in Fig. 3A. The figure summarizes the profile of interaction of 18325633 each compound with residues of PAZ domain. Electrostatic, hydrogen bonding and van der Waals interactions of each compound with the main chain or side chain of each residue are assigned. The rule of each residue can be thoroughly assigned e.g. the most important van der Waals interactions is occurring with F669, Y681, I706 and LTable 2. The docking results by using the docking server.Compound 8.82 27.07 26.6 24.15 26.62 28.26 26.76 25.55 27.35 27.25 25.75 27.16 27.71 27.46 28.66 79.39 21.94 21.23 20.32 20.75 20.53 20.62 20.45 20.66 20.68 20.18 20.09 20.9 24.8 9.17 28.26 27.9 28.65 210.06 27.8 27.89 26.71 26.4 26.13 20.79 29.45 77.46 26.03 8.85 29.01 28.43 29.26 210.5 28.45 28.57 26.89 26.49 27.03 20.83 28.29 21.38 29.1 20.93 28.09 20.04 25.79 21.41 28.66 21 28.35 20.12 25.67 21.35 28.11 748.43 466.14 688 899 484 667 820 688 901.26 1188 995.45 1117 744 901.48 945.85 808.5 835.7 719 780.3 664 616.33 20.65 28.91 747.37 20.08 26.7 503.7 20.47 24.62 727.216 20.66 27.27 732.72 20.08 27.15 115.63 17.56 143.04 58.9 402.26 228.99 47.67 466.86 140.99 49.19 424.55 74.8 38.27 nd nd nd 49.61 4.8 12.75 3 42.37 48.57 57.82 21.8 60.14 572.Estimated free energyInhibition constant Ki Electrostatic energy Total intermolecular energy Interaction surface 0.48 0.29 0.28 0.48 0.37 0.4 0.42 0.32 0.34 0.3 0.32 0.36 0.2 0.37 0.6 0.65 1.1 0.58 0.7 0.78 1.05 0.74 0.26 0.3 0.28 0.vDw + Hbond + desolvation energyRL/FLt26.tt25.ttt22.U25.U25.U24.U24.U25.U24.U25.U25.U24.U10bbn25.U11btbt26.U174.5 siRNA Recognition by PAZ DomainU15.U57.U15BbBb25.U16BnBn27.U17BhBh26.U18ByBy27.u19bBBn25.u20BB25.Utd25.Utd26.U21RHRH25.The ligands are ordered as shown in Fig. 1). The output data included free energy (Kcal/mol), inhibition constant (mM),van der Waals interactions, Hydrogen bonding and desolvation energy (Kcal/mol), electrostatic energy (Kcal/ mol) and interaction surface. RL/FL indicates Renilla luciferace expression normalized by firefly luciferase data. doi:10.1371/journal.pone.0057140.tsiRNA Recognition by PAZ DomainTable 3. Correlation analysis for RNAi activity and the measured parameters produced by iGEMDOCK.RL/FL 1.00 20.2338 20.4163* 0.1918 0.2236 RL/FL 20.1681 20.5756* 20.1976 20.1478 *Pearson’s correlation coefficient is calculated by STATA. Data showing significant correlation at 0.05 level are marked by asterisk. doi:10.1371/journal.pone.0057140.t004 1.00 1.00 1.00 0.7744* 0.6443* 20.303 vDw + Hbond + desolvation energy Total intermolecular energy Estimated free energy Inhibition constant Ki Electrostatic energyTotal Energy Total Energy 1.00 VDW HBond energy Elec 0.833* 0.4091 0.VDWHBondElecAverConPair RL/FL Interaction surface1.00 20.08 20.0593 0.4168* 1.00 20.0198 0.2372 1.00 0.2036 1.00 0.1271 20.4681* 1.AverConPair 0.4799* RL/FL 20.20.4153* 0.*Pearson’s correlation coefficient is calculated by STATA. Data showing significant correlation at 0.05 level are marked by asterisk. doi:10.1371/journal.pone.0057140.tDissection of receptor-ligand binding forcesIn dissecting the forces accompanying the recognition of siRNAs.

Ding patterns with the active site. By using iGEMDOCK post run

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