Table 4. Number of salt bridges formed between ATP and surrounding residues.
| Label | K18-Oα | K18-Oβ | K137-Oγ | Total |
| 0.1 MPa | ||||
| Rab | 1.0±0.0 | 1.5±0.6 | – | 2.5±0.6 |
| Ac1W | 0.8±0.4 | 1.4±0.6 | – | 2.2±0.7 |
| Ac1Q | 0.7±0.6 | 1.1±0.6 | – | 1.8±0.8 |
| Ac2 | 1.0±0.1 | 1.4±0.6 | – | 2.4±0.6 |
| Arm | 1.0±0.2 | 0.6±0.6 | 1.1±0.4 | 2.7±0.8 |
| Yaq | 1.0±0.1 | 1.0±0.3 | 1.7±0.5 | 3.7±0.5 |
| 60 MPa | ||||
| Rab | 1.0±0.0 | 1.1±0.7 | – | 2.1±0.7 |
| Ac1W | 1.0±0.0 | 1.4±0.5 | – | 2.4±0.5 |
| Ac1Q | 1.0±0.0 | 1.3±0.5 | – | 2.3±0.5 |
| Ac2 | 0.3±0.5 | 1.0±0.1 | – | 1.3±0.5 |
| Arm | 1.0±0.0 | 0.9±0.3 | 1.4±0.5 | 3.3±0.6 |
| Yaq | 1.0±0.2 | 0.8±0.6 | 1.0±0.3 | 2.8±0.7 |
K18-Oα, K18-Oβ, and K137-Oγ represent salt bridges between K18 and α-oxygen, between K18 and β-oxygen, and between K137 and γ-oxygen of ATP, respectively. The value after “±” indicates standard deviation.