Table 1 Potential subsite cooperativity analysis for KLK7.

From: Mass spectrometry-based determination of Kallikrein-related peptidase 7 (KLK7) cleavage preferences and subsite dependency

Fixed residue

Affected residue(s)

Change (percentage-points)

Vice-Versa change

P3_A

P1prime_A

11.6

11.4

P3_A

P2_V

16.4

16

P3_K

P2_K

11.5

12.5

P3_N

P1prime_A

18.6

11.2

P3_Q

P1prime_R

13.4

12.4

P3_Q

P2_K

10.8

12.2

P3_Q

P3prime_D

17.1

14.6

P3_Q

P3prime_V

18.2

11.1

P3_V

P2_P

22

14.9

P3_V

P3prime_N

10.6

19.1

P2_K

P1prime_S

19.3

12.3

P2_K

P2prime_N

14.8

20.8

P2_V

P1_F

−12.7

−10.3

P2_V

P1prime_A

11.1

11.1

P1_Q

P3prime_I

15.6

11.3

P1prime_H

P2prime_M

21.3

19.7

P1prime_R

P3prime_V

15.9

10.5

P2prime_N

P3prime_I

25.1

13

  1. Potential subsite cooperativity analysis for 353 KLK7 cleavage sites detected in the GluC library was calculated using the CLIP-PICS web server (http://clipserve.clip.ubc.ca/pics)18. Minimum difference for subsite dependency was set to ±10 percentage-points. Subsite dependency was checked for all positional occurrences >1 × natural abundance and restricted to P3-P3′. Subsites with a change ≥15 percentage-point are bold.