Table 3. Hydrogen bond and van der Waals contact residues in ANG and ANG-PD and ANG-ALS variants.
| Variant | Potential hydrogen bonding residues |
Potential van der Waals contact residues |
||||
|---|---|---|---|---|---|---|
| Retained | Gained | Lost | Retained | Gained | Lost | |
| H13R | F9, I46 | N43, Q117 | T44 | F9, L10, T11, K40, T44, F45, I46, L115, Q117 | ||
| K40R | L35, P38, Y94 | Q12 | I42, N43 | M30, P38, I42, N43, Y94 | Q12, L35 | H13 |
| K54R | K50, I56, C57 | Y6 | R51, S52, I56, C57, L111, P112 | Y6, K50 | ||
| K60E | E58 | A55, G62, K73 | E58 | |||
| Q77P | H47 | R21 | I46, H47, G99, F100 | R21 | ||
| T80S | T44, T97 | C26, N43, R95, A96, T97, F120 | I42, T44, K82 | |||
| R95Q | K82 | D23, C81, K82, T97 | H84 | |||
| F100I | S75, F76, Q77 | |||||
| V103I | S72 | R70, I71, V78, V105, I119, F120 | I46, I56, F76 | |||
| H114R | A106 | F9, V105, A106 | L69 | D116 | ||
| R121C | S118, I119, F120 | |||||
*Note- The electron density for R121C is not optimal while R122 shows poor density and P123 is not visible in the electron density map (i.e., disordered) in the R121C variant structure. Also, the cysteine residue with a glutathione molecule bound to the free cysteine was observed in the variant structure.