Table 4. Different Structural Properties and Number of NOE Distance Upper Bound Violations of the Generated Ensembles or Experimentally Determined Structures of the Bound Complexes.
| no. of interprotein H-bonds | buried surface area [nm2] | no. of NOE violations > 0.0 nm/> 0.3 nm | % DSSP α-helix/β-sheet | ||
|---|---|---|---|---|---|
| wt complex | straight MD | 7.4 | 13.8 | 245/9 | 26.1/20.9 |
| bound, unrestrained | 6.4 | 11.7 | 299/22 | 22.7/21.0 | |
| bound, restrained | 4.6 | 13.4 | 353/36 | 27.6/20.7 | |
| bound, binding (restrained) | 5.2 | 11.9 | 367/42 | 27.8/20.6 | |
| experimental bundle (PDB-ID 2KTF) | 3.5 | 15.5 | 4/0 | 29.3/23.8 | |
| P692A | straight MD | 7.6 | 12.1 | n/a | 24.6/20.7 |
| complex | bound, unrestrained | 8.6 | 12.9 | n/a | 24.3/20.7 |
| bound, restrained | 5.7 | 12.2 | n/a | 27.1/20.6 | |
| bound, binding (restrained) | 4.9 | 11.7 | n/a | 27.4/20.7 | |
| experimental bundle (PDB-ID 2L0F) | 4.0a | 14.2a | n/a | 29.5/23.2a |
a
As experimental structures contained additional N- and C-terminal residues in P692A UBM2 that were not simulated but were expected to influence the calculated properties, additional residues were removed prior to analysis.