TABLE 7.
Crystal data collection and structure refinement statistics
r.m.s.d. is root mean square deviation.
| Trypsin-G193R/BPTI | Trypsin-K97D/BPTI | |
|---|---|---|
| PDB code | 4WWY | 4WXV |
| Complexes per asymmetric unit | 2 | 2 |
| Space group | P21 | P212121 |
| Unit cell, Å | 52.95, 63.23, 90.53, 90, 94.74, 90 | 42.85, 56.58, 228.58 90,90,90 |
| Resolution, Å | 1.70a | 2.1 |
| Unique reflections | 56150 | 31212 |
| Completeness, % | 89.9 (45.7)a,b | 97.8 (85.3)b |
| Multiplicity | 4.7 (2.2)b | 5.5 (4.1)b |
| Mean I/σ | 17.0 (1.21)b | 15.9 (4.24)b |
| Rmerge | 0.068 (0.435)b | 0.077 (0.256)b |
| Rmeas | 0.096 (0.625)b | 0.110 (0.410)b |
| Rp.i.m. | 0.041 (0.378)b | 0.047 (0.203)b |
| Rcryst/Rfree (%) | 18.2/21.7 | 22.2/28.1 |
| Average B-factor, Å2 | 17.8 | 25 |
| Protein atoms | 4789 | 4345 |
| Water molecules | 390 | 75 |
| r.m.s.d. bonds, Å | 0.0198 | 0.0167 |
| r.m.s.d. angles, (°) | 1.956 | 1.799 |
| Φ, ψ angle distributionc | ||
| Favored regions (%) | 96 | 98 |
| Allowed regions (%) | 4 | 2 |
| Outliers (%) | 0 | 0 |
a For the trypsin-G193R/BPTI data, imposing a resolution cutoff of 1.83 Å results in 97.5% overall completeness (82.4% in the 1.87 to 1.83 Å shell).
b Values in parentheses are for the highest resolution shell.
c Ramachandran distributions are reported as defined by the PDB validation server/MolProbity.