Table 2. Crystallographic data-collection and refinement statistics.
Values in parentheses are for the highest resolution shell.
| BRD2 BD1–NS5 | BRD2 BD2–NS5 | BRD2 BD2–L10a | |
|---|---|---|---|
| Data-collection parameters | |||
| Space group | C2 | P21212 | P22121 |
| a, b, c (Å) | 115.22, 55.89, 67.60 | 52.10, 71.12, 31.85 | 32.02, 52.67, 71.66 |
| α, β, γ (°) | 90, 94.85, 90 | 90, 90, 90 | 90, 90, 90 |
| Wavelength (Å) | 1.54056 | 1.54056 | 1.54056 |
| Resolution (Å) | 50.0–2.45 (2.49–2.45) | 50.0–1.72 (1.75–1.72) | 14.14–1.70 (1.73–1.70) |
| Unique reflections | 15805 (744) | 13233 (610) | 13875 (700) |
| R merge † (%) | 13.5 (53.0) | 7.8 (26.4) | 13.1 (35.0) |
| 〈I/σ(I)〉 | 10.82 (1.45) | 23.02 (2.72) | 7.6 (3.2) |
| Completeness (%) | 99.1 (92.8) | 98.5 (92.4) | 99.7 (100) |
| Multiplicity | 4.4 (2.3) | 3.3 (2.2) | 5.8 (5.4) |
| CC1/2 | 0.993 (0.593) | 0.981 (0.86) | 0.985 (0.874) |
| Refinement | |||
| Resolution (Å) | 31.6–2.45 | 29.07–2.00 | 14.14–1.70 |
| No. of reflections | 15798 | 8314 | 13834 |
| R work ‡/R free § (%) | 18.7/25.9 | 17.6/22.4 | 18.9/22.6 |
| No. of atoms | |||
| Total | 2841 | 1138 | 1217 |
| Protein atoms | 2699 | 974 | 972 |
| Water molecules | 140 | 133 | 218 |
| Ligand molecules | 1 | 1 | 1 |
| PEG molecules | — | 1 | 1 |
| Sulfate ions | 1 | — | 1 |
| Real-space CC (RSCC) for the ligand | 0.83 | 0.87 | 0.94 |
| Average B factor (Å2) | 37.47 | 19.47 | 13.15 |
| R.m.s.d., bonds (Å) | 0.008 | 0.007 | 0.007 |
| R.m.s.d., angles (°) | 0.937 | 0.877 | 0.813 |
†
R
merge =
, where I
i
(hkl) is the intensity of the ith measurement and 〈I(hkl)〉 is the mean intensity for that reflection.
‡
R
work =
, where |F
obs| and |F
calc| are the observed and calculated structure-factor amplitudes, respectively.
§
R free was calculated with 5.0% of reflections in the test set.