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Table 1 List of residues pairs participating in hydrogen bond formation during the entire MD simulation run

From: Embelin inhibits TNF-α converting enzyme and cancer cell metastasis: molecular dynamics and experimental evidence

S. No. Donor Acceptor Occupancy (%)
1 Leu 348 (M) Embelin 92.81
2 Gly349 (M) Embelin 73.54
3 Gln406 (S) Embelin 96.74
4 Embelin Gly346(M) 43.43
5 Thr347 (S) Embelin 1.82
6 His405 (S) Embelin 3.79
7 Embelin Gly349 (M) 4.03
8 Val314 (M) Embelin 0.10
9 Embelin Val314 (M) 0.10
10 Embelin Thr347 (S) 1.87
11 Embelin Glh406 (S) 13.71
12 Embelin Pro437 (M) 21.33
13 Embelin Asp344 (M) 0.29
14 Leu348 (S) Embelin 4.94
15 Thr347 (M) Embelin 3.26
16 Embelin Asp313 (S) 0.10
17 His409 (S) Embelin 41.56
18 Met345 (S) Embelin 0.10
19 Embelin Met345 (S) 0.14
20 Embelin Ile438 (M) 0.05
21 Val314 (S) Embelin 0.10
22 Embelin Val314 (S) 0.10
23 Embelin Met345 (M) 5.90
24 Embelin His405 (S) 0.14
25 Pro437 (S) Embelin 6.14
26 Embelin Leu348 (M) 0.77
27 Embelin Leu348 (S) 0.43
28 Embelin His409 (S) 0.05
29 Embelin Tyr436 (S) 0.34
30 Tyr436 (S) Embelin 0.05
31 Embelin Tyr390 (S) 0.24
32 Embelin Pro437 (S) 0.05
33 Tyr390 (S) Embelin 0.05
34 Embelin Thr347 (M) 0.05
  1. (M) Main chain, (S) Side Chain. The residues in bold format are the ones that were involved in H-bond formation in the representative average structure of TACE-embelin complex, obtained subsequent to molecular dynamics simulations.