TABLE 3.
Dominant lipid/protein interactions
| Interaction | OMPT1 | OMPT2 | OMPT3a | OMPT3b | OMPT3c |
|---|---|---|---|---|---|
| Proposed site | |||||
| Arg138 | 97.0 | 85.4 | 67.5 | 95.2 | 88.9 |
| Arg175 | 26.1 | 33.3 | 93.7 | 99.2 | 13.5 |
| Lys226 | 0.0 | 91.0 | 90.5 | 100.0 | 85.7 |
| Tyr134 | 39.9 | 0.0 | 99.2 | 0.0 | 0.0 |
| E136-w | 62.6 | 92.2 | 98.2 | 97.6 | 95.6 |
| Vicinity | |||||
| Lys177 | 96.0 | 46.3 | 100.0 | 92.1 | 33.3 |
| 2nd site | |||||
| Arg77 | 100.0 | 95.4 | 69.0 | 83.3 | 93.7 |
| Arg255 | 60.1 | 76.8 | 84.9 | 0.0 | 7.1 |
| Asn47 | 94.0 | 100.0 | 48.4 | 95.2 | 10.3 |
| Lower belt | |||||
| Tyr189 | 77.8 | 94.2 | 100.0 | 8.7 | 33.3 |
| Tyr126 | 9.8 | 98.2 | 52.4 | 5.6 | 100.0 |
| Thr2 | 55.3 | 36.1 | 0.0 | 0.0 | 0.0 |
Protein-lipid interactions (given as percentage of total simulation time for which an H-bonding interaction is formed between the phosphate of DMPC and a protein side chain) are listed for proposed site, residues identified by analogy with the FhuA LPS binding site; vicinity, interactions with Lys177 which sits near to the proposed site; 2nd site, a putative second LPS-binding site; and lower belt, interactions with the lower (periplasmic) half of the protein.