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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.