Table 2.
Statistics of X-ray data collection and structure refinement
Number of crystals for both data sets, 1. The values in parentheses are for the highest resolution shell.
| COX-2·compound 1 | COX-2·compound 2 | |
|---|---|---|
| Data collection | ||
| PDB code | 6BL4 | 6BL3 |
| Wavelength (Å) | 0.9792 | 0.9792 |
| Resolution range (Å) | 112–2.22 (2.30–2.22) | 103.3–2.22 (2.30–2.22) |
| Space group | C2 | C2 |
| Unit cell | ||
| a, b, c (Å) | 214.8, 120.4, 134.4 | 215.5, 121.8, 134.8 |
| α, β, γ (°) | 90, 123.6, 90 | 90, 123.5, 90 |
| Total reflections | 324,375 (32,417) | 480,554 (45,327) |
| Unique reflections | 138,412 (13,682) | 141,148 (13,090) |
| Multiplicity | 2.3 (2.4) | 3.4 (3.3) |
| Completeness (%) | 98.49 (97.71) | 97.83 (91.40) |
| Mean I/σ(I/σ) | 9.55 (1.58) | 5.97 (1.09) |
| Wilson B-factor (Å2) | 29.05 | 39.05 |
| Rmergea | 0.109 (0.715) | 0.1535 (1.424) |
| CC1/2b | 0.986 (0.507) | 0.989 (0.458) |
| CC*c | 0.996 (0.820) | 0.997 (0.792) |
| Refinement | ||
| Rwork/Rfreed (%) | 18.9/22.0 (28.3/33.9) | 20.5/22.9 (30.2/32.9) |
| Number of atoms | 20,177 | 19,075 |
| Protein/ligands/water | 17,896/652/1,629 | 17,932/676/467 |
| Protein residues | 2,208 | 2,236 |
| r.m.s.e (bonds/angles) | 0.01/1.22 | 0.007/1.09 |
| Ramachandran favored/outlier (%) | 97.0/0.18 | 97.0/0 |
| Average B-factor | 34.2 | 41.8 |
| Protein/ligands/solvent | 33.6/41.8/37.5 | 41.5/51.5/42.4 |
aRmerge = (ΣhklΣi|Ii(hkl) − Ii(hkl)|)/(ΣhklΣIi(hkl)) 100%; R = (Σhkl‖Fo| − |Fc‖)/(Σhkl|Fo|) 100% where Fo and Fc are the observed and calculated structure factors.
bCC1/2 = (Σ(xi − x̄)(yi − ȳ))/(Σ(xi − x)2 Σ(yi − ȳ)2) where xi and yi are the intensities of unique reflections merged across the observations randomly and evenly split into subsets X and Y and where x̄ and ȳ are the averages of the subset X,Y, respectively.
cCC* = √(2CC1/2)/(1 + CC1/2).
dRfree is the value from the test set (3.0% of all reflections).
er.m.s., root mean square.