Table 1.
Crystallographic Data Collection and Refinement Statistics
| PRWT | PRI47V | PRV32I | |
|---|---|---|---|
| Space group | P21212 | P21212 | P21212 |
| Unit cell dimensions: (Å) | |||
| A | 58.41 | 58.08 | 58.06 |
| B | 86.20 | 86.30 | 86.14 |
| C | 46.36 | 46.35 | 46.30 |
| Resolution range (Å) | 10-1.2 | 10-1.31 | 50-1.4 |
| Unique reflections | 66188 | 55879 | 45833 |
| Rmerge (%) overall (final shell) | 9.7 (39) | 6.3 (51) | 7.2 (43) |
| I/σ(I) overall (final shell) | 15.03 (2.2) | 27.8 (2.1) | 18.3 (2.1) |
| Completeness (%) overall (final shell) | 94.3 (56.8) | 98.8 (90.6) | 93.0 (98.7) |
| Data range for refinement (Å) | 10-1.2 | 10-1.31 | 10-1.4 |
| R (%) | 0.14 | 0.15 | 0.17 |
| Rfree (%) | 0.18 | 0.18 | 0.23 |
| No. of solvent atoms (total occupancies) | 206 (191) | 181 (169.5) | 140 (134) |
| RMS deviation from ideality | |||
| Bonds (Å) | 0.015 | 0.012 | 0.010 |
| Angle distance (Å) | 0.034 | 0.031 | 0.029 |
| Average B-factors (Å2) | |||
| Main-chain atoms | 19.2 | 17.1 | 16.8 |
| Side-chain atoms | 24.9 | 20.4 | 23.3 |
| Peptide Intermediate | 54.1 | 53.5 | 32.2 |
| Solvent | 36.4 | 33.3 | 30.5 |
| Intermediate Peptide | (Y)a DQIIxIE | (D)(Q)II+IE | (Y)DQII |
| Peptide relative occupancy | 0.5/0.4 | 0.5/0.4 | 1.0 |
a
Parentheses indicate peptide residues refined as alanine due to poor electron density for the longer side chain.