Table 1. Data collection and refinement statistics.
| FL Btk†,‡ | PHTH/KD complex*,‡ | KD with dasatinib†,‡ | |
|---|---|---|---|
| PDB codes | 8GMB | 8S93 | 8S9F |
| Data collection | |||
| Space group | P 31 2 1 | P 1 21 1 | P 1 21 1 |
| Cell dimensions | |||
| a, b, c (Å) | 125.72, 125.72, 110.09 | 38.38, 77.38, 82.32 | 55.24, 110.04, 61.14 |
| α, β, γ (°) | 90, 90, 120 | 90, 97.98, 90 | 90, 99.51, 90 |
| Resolution (Å)§ | 108.88–3.19 (3.53–3.19) | 81.53–2.00 (2.20–2.00) | 55.02–2.50 (2.79–2.50) |
| Spherical data completeness (%)§ | 67.7 (13.2) | 54.5 (13.6) | 69.7 (12.5) |
| Ellipsoidal data completeness (%)§ | 94.2 (70.4) | 84.1 (78.5) | 91.8 (52.0) |
| R merge § | 0.27 (>1) | 0.13 (0.80) | 0.26 (>1) |
| R meas § | 0.27 (>1) | 0.16 (0.95) | 0.396 (>1) |
| CC1/2§ | 0.998 (0.74) | 0.99 (0.54) | 0.99 (0.56) |
| Mean I /σ§ | 17.8 (2.0) | 7.1 (1.6) | 11.2 (1.4) |
| Multiplicity§ | 88.5 (82.2) | 3.7 (3.3) | 14.8 (14.9) |
| Refinement | |||
| Resolution (Å)§ | 19.58–3.40 (3.52–3.40) | 19.71–2.10 (2.18–2.10) | 19.96–2.60 (2.69–2.60) |
| Number of reflections§ | 11,205 (295) | 21,392 (572) | 17,286 (300) |
| Rwork / Rfree (%) | 27.63/28.93 | 19.95/24.86 | 24.34/28.95 |
| Number of non-hydrogen atoms | 3168 | 3759 | 4167 |
| Protein | 3119 | 3525 | 4034 |
| Ligand/ion | 93 | 108 | 118 |
| Water | 0 | 178 | 67 |
| Average B-factor | 157.69 | 39.89 | 78.30 |
| Protein | 158.15 | 40.15 | 78.73 |
| Ligand/ion | 128.60 | 36.73 | 74.73 |
| Water | 35.74 | 56.37 | |
| Ramachandran statistics | |||
| Favored (%) | 93.72 | 97.62 | 96.59 |
| Allowed (%) | 6.05 | 2.38 | 3.41 |
| Outliers (%) | 0.23 | 0.00 | 0.00 |
| Clashscore | 6.56 | 1.69 | 3.27 |
| R.m.s. deviations | |||
| Bond lengths (Å) | 0.002 | 0.002 | 0.002 |
| Bond angles (°) | 0.43 | 0.49 | 0.43 |
*
X-ray data from a single crystal.
†
X-ray data from multiple crystals.
‡
X-ray data anisotropically corrected with the STARANISO webserver (Global Phasing).
§
Statistics for the highest resolution shell are shown in parentheses.