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40
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27444436080
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-
note
-
In some of the docking poses the studied compounds were not located within the binding site but were docked to the surface of the protein. Consequently, the "best" docking pose in this study was defined as the pose with the most favorable docking score for compounds that were located inside the binding pocket. For all virtual compounds (i.e., those that were not readily synthesized when the docking study was carried out) a further constraint was added. Since the activated double bond of compound 6a was predicted to be in proximity to the active site Cys145 and since it was the working hypothesis that this double bond reacts with Cys145, only those docking poses were scrutinized where the double bond was close to Cys145.
-
-
-
-
41
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27444438348
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-
note
-
His163 N-H ↔ O=C: 1.76 Å, angle NHO 153.1. Glu166 C=O ↔ H-N: 1.97 Å, angle NHO 169.3. Gln189 N-H ↔ O=C: 1.94 Å, angle NHO 141.1.
-
-
-
-
42
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27444444921
-
-
note
-
Adding the van der Waals radii of the involved heavy atoms sulfur and carbon results in 3.4 Å. Hence, when only noncovalent interactions are modeled, the two atoms cannot move closer because clashes are penalized by the scoring function of the docking tool.
-
-
-
-
43
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27444445676
-
-
note
-
Glu166 C=O ↔ H-N: 1.66 Å, angle NHO 159.5. Gln189 N-H ↔ O=C: 2.03 Å, angle NHO 170.2.
-
-
-
-
44
-
-
27444434645
-
-
note
-
Thr190 C=O ↔ H-N: 1.70 Å, angle NHO 147.6. Gln192 N-H ↔ O=C: 2.03 Å, angle NHO 147.0.
-
-
-
-
45
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0032147022
-
Development of in vitro peptide substrates for human rhinovirus-12 2A protease
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Wang, Q. M.; Johnson, R. B.; Sommergruber, W.; Shepherd, T. A. Development of in vitro peptide substrates for human rhinovirus-12 2A protease. Arch. Biochem. Biophys. 1998, 356, 12-18.
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46
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27444434367
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-
note
-
The descriptors ortho and meta are used with respect to the phenolic hydroxyl group.
-
-
-
-
47
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0004121625
-
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Rang, H. P.; Dale, M. M.; Ritter, J. M.; Moore, P. K. Pharmacology, 5th ed.; Churchill Livingstone: Edinburgh, U.K., 2003; p 362.
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27444438649
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i values could be determined. Dialysis assays with the CAC1 cysteine protease cathepsin B showed the inhibitors to act reversibly (unpublished results).
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