Table 1.
X-ray crystallography data collection and refinement statistics.
| PPARγ LBD-Y473E- GW1929 | PPARγ LBDGW1929 | PPARγ LBD-Y473E- Darglitazone | PPARγ LBDY473E | PPARγ LBD-Apo Delipidated | |
|---|---|---|---|---|---|
| Data collection | |||||
| Space group | C 1 2 1 | C 1 2 1 | C 1 2 1 | C 1 2 1 | C 1 2 1 |
| Cell dimensions | |||||
| a, b, c (Å) | 92.70, 61.62, 118.66 | 92.84, 62.13, 119.12 | 93.07, 61.59, 120.53 | 92.64, 61.75, 118.78 | 93.04, 62.10, 118.85 |
| α, β, γ (°) | 90, 102.44, 90 | 90, 102.16, 90 | 90, 102.16, 90 | 90, 101.93, 90 | 90, 102.22, 90 |
| Resolution | 36.15–2.15 (2.23–2.15) | 51.27–2.07 (2.14–2.07) | 33.41–2.40 (2.49–2.40) | 33.01–2.3 (2.38–2.3) | 58.08–2.27 (2.35–2.27) |
| Rmerge | 0.0134 (0.196) | 0.0511 (1.374) | 0.0245 (0.362) | 0.0163 (0.360) | 0.0367 (0.341) |
| I / σ(I) | 22.00 (3.49) | 13.59 (1.22) | 13.59 (2.06) | 19.42 (1.94) | 8.43 (1.58) |
| CC1/2 in highest shell | 0.934 | 0.727 | 0.774 | 0.877 | 0.862 |
| Completeness (%) | 98.19 (98.62) | 98.75 (97.88) | 98.16 (98.76) | 97.89 (94.32) | 99.50 (97.78) |
| Redundancy | 2.0 (2.0) | 6.4 (6.4) | 2.0 (2.0) | 2.0 (2.0) | 2.0 (1.9) |
| Refinement | |||||
| Resolution (Å) | 2.15 | 2.07 | 2.40 | 2.30 | 2.27 |
| No. of unique reflections | 35158 | 40606 | 25861 | 28880 | 30849 |
| Rwork/Rfree (%) | 23.0/26.5 | 25.3/28.6 | 22.2/27.3 | 22.4/27.5 | 22.3/26.7 |
| No. of atoms | |||||
| Protein | 3999 | 4012 | 4075 | 4050 | 4122 |
| Water | 90 | 335 | 205 | 122 | 270 |
| B-factors | |||||
| Protein | 58.40 | 29.54 | 32.78 | 54.96 | 31.34 |
| Ligand | 81.00 | 53.92 | 43.47 | n/a | n/a |
| Water | 54.06 | 31.37 | 31.70 | 50.39 | 31.84 |
| Root mean square deviations | |||||
| Bond lengths (Å) | 0.016 | 0.010 | 0.010 | 0.010 | 0.011 |
| Bond angles (°) | 1.30 | 1.12 | 1.18 | 1.08 | 1.18 |
| Ramachandran favored (%) | 96.91 | 96.92 | 96.96 | 97.76 | 96.61 |
| Ramachandran outliers (%) | 0.82 | 0.41 | 0.40 | 0.20 | 0.40 |
*
Values in parentheses indicate highest resolution shell.