TABLE 2.
Surface area and residue composition of the OmpR/PhoB dimer interface
| Protein | PDB ID | Interface surface areaa | Interface residuesa |
||
|---|---|---|---|---|---|
| Non-polar | Polar | Charged | |||
| Å2 | % | ||||
| ChxR (atypical) | 3Q7R | 1095 | 52 | 26 | 22 |
| YycF (inactive) | 3F6P | 1087 | 36 | 11 | 53 |
| PhoP (BeF3-activated) | 2PL1 | 1027 | 32 | 32 | 36 |
| TorR (inactive) | 1ZGZ | 981 | 28 | 24 | 48 |
| DrrD (Inactive) | 3NNN | 978 | 39 | 13 | 48 |
| PhoB (BeF3-activated) | 1ZES | 977 | 36 | 8 | 56 |
| PhoP (inactive) | 2PKX | 936 | 35 | 25 | 39 |
| ArcA (BeF3-activated) | 1XHF | 887 | 27 | 23 | 50 |
| ArcA (inactive) | 1XHE | 876 | 30 | 22 | 48 |
| HP1043 (atypical) | 2PLN | 837 | 38 | 17 | 45 |
| DrrB (inactive) | 3NNS | 802 | 38 | 19 | 43 |
a The dimer interface surface area and residue composition were calculated using PROTORP (51).