Table 1. Protection of Residues from HR-HRPF upon b12 Binding.
| residuea | % HR-HRPF protection upon b12 bindingb | direct protection in MD upon b12 binding (Δ%)c |
|---|---|---|
| M95 | 31.9 | 0% |
| W96 | 81.8 | 0% |
| M100 | 84.6d | 0% |
| M104 | 66.0d | 0% |
| C157 | 100d | 64% |
| Y173, A174 | 100 | 53%, 76% |
| F176 | 100 | 70% |
| D180 | 64.5 | 35% |
| V182, P183 | 21.3 | 32%, 54% |
| I322a | 43.6 | 0% |
| I323 | 28.2 | 14% |
| W338 | 100 | 0% |
| V360 | 72.4 | 0% |
| F361 | 73.3 | 0% |
| H363 | 70.4 | 0% |
| P417, C418, R419 | 45 | 0%, 0%, 0% |
| M434 | 28.5 | 0% |
| Y435 | 28.2 | 0% |
| C445 | –35.7 | 0% |
| M475 | 11.3 | 0% |
a
The residue numbering used is based on the HXB2 numbering system.
b
The protection upon binding for each residue was calculated by the changesin oxidation extent between gp120 and the gp120–b12 complex divided by the oxidation extent of gp120.
c
The direct protection is calculated by measuring the change in solvent accessibility after alignment of b12. The values are averages from the MD simulation.
d
CID-based data were used in HR-HRPF results and should be considered semiquantitative.