TABLE 1.
X-ray diffraction data and refinement statistics
| PBP 2 wild type | PBP 2-6140CT | |
|---|---|---|
| Data collection | ||
| Resolution range (Å) | 87.0-2.30 (2.36-2.30) | 50.0-2.4 (2.49-2.40) |
| Rmergea (%) | 6.1 (34.9) | 10.1 (52.0) |
| Redundancy | 6.2 (3.7) | 7.1 (4.3) |
| Completeness (%) | 90.3 (52.6) | 98.0 (83.5) |
| <I>/<σI> | 8.8 (2.0) | 29.9 (2.7) |
| Refinement | ||
| Resolution range (Å) | 66.6-2.40 | 48.1-2.40 |
| Completeness in range (%) | 94.6 (70.0) | 97.7 (80.4) |
| Total number of reflections | 68,535 | 72,265 |
| Number of non-hydrogen protein atoms | 6,522 | 6,639 |
| Number of sulfate molecules | 17 | 15 |
| Number of glycerol molecules | 2 | 2 |
| Number of water molecules | 146 | 86 |
| Rfactor (%) | 21.6 | 21.9 |
| Rfree (%) | 23.7 | 25.3 |
| r.m.s.d. from ideal stereochemistry | ||
| Bond lengths (Å) | 0.012 | 0.011 |
| Bond angles (°) | 1.45 | 1.39 |
| B factors | ||
| Mean B factor (main chain) (Å3) | 35.4 | 48.1 |
| r.m.s.d. in main chain B factor (Å3) | 0.48 | 0.44 |
| Mean B factor (side chains and waters) (Å3) | 38.1 | 49.4 |
| r.m.s.d. in side chain B factors (Å3) | 1.42 | 1.18 |
| Ramachandran plot | ||
| Residues in most favored region (%) | 93.0 | 91.7 |
| Residues in additionally allowed regions (%) | 7.0 | 8.3 |
| Residues in generously allowed regions (%) | 0.0 | 0.0 |
| residues in disallowed regions (%) | 0.0 | 0.0 |
| PDB code | 3EQU | 3EQV |
a
Rmerge = ∑|Ii - Im|/∑Ii, where Ii is the intensity of the measured reflection, and Im is the mean intensity for all observations of that reflection. Numbers within parentheses are for the outer resolution shell of data.