TABLE I.
Data collection and structure refinement statistics
| Structure | 3M1 | 3M2 |
|---|---|---|
| Data collection | ||
| Space group | P1 | P1 |
| Cell dimensions | ||
| a/b/c (Å) | 29.07/67.89/69.74 | 29.30/67.62/69.72 |
| α/β/γ (°) | 77.1/83.3/83.2 | 76.8/83.9/83.6 |
| Temperature (K) | 100 | 100 |
| X‐ray source | DESY X13 | BESSY BL14.2 |
| Wavelength (Å) | 0.81500 | 0.82657 |
| Resolution (Å) | 42.87–2.43 (2.58–2.43) a | 32.42–1.93 (2.05–1.93) |
| R int b | 0.062 (0.363) | 0.070 (0.637) |
| R meas c | 0.071 (0.421) | 0.095 (0.860) |
| <I/σI> | 15.51 (3.83) | 9.40 (1.49) |
| CC1/2 | 99.9 (93.1) | 99.7 (55.5) |
| Reflections | ||
| Measured | 75,102 (11,724) | 83,558 (13,381) |
| Unique | 19,062 (3,023) | 37,694 (6,043) |
| Multiplicity | 3.94 (3.79) | 2.22 (2.21) |
| Completeness (%) | 98.8 (97.7) | 97.0 (96.3) |
| Wilson B‐factor (Å2) | 39.9 | 27.2 |
| Refinement | ||
| No. reflections, work/test set | 18,089/954 | 36,685/999 |
| R/R free d | 0.1796/0.2362 | 0.1768/0.2110 |
| Protein molecules in ASU | 4 (two dimers) | 4 (two dimers) |
| No. atoms (non‐H) | ||
| Protein | 3,426 | 3,435 |
| Inhibitor | 124 | 128 |
| Water | 170 | 309 |
| PEG/acetate | 32/0 | 32/12 |
| <B > (Å2) | ||
| Protein | 49.0 | 35.9 |
| Inhibitor | 75.5 | 37.1 |
| Water | 47.8 | 43.6 |
| PEG/acetate | 73.4/− | 53.0/67.9 |
| Rmsd from ideal | ||
| Bond lengths (Å) | 0.008 | 0.008 |
| Bond angles (°) | 1.09 | 1.11 |
| Ramachandran statistics (%) | ||
| Favored/allowed/outliers | 96/4/0 | 98/2/0 |
| PDB code | 7bgu | 7bgt |
Values in parentheses are for the highest resolution shell.
R int = ΣhklΣi|I i(hkl) – <I(hkl)>|/ΣhklΣi I i(hkl), where I i(hkl) is the ith measurement of the intensity of reflection hkl and <I(hkl)> is the mean intensity of reflection hkl.
R meas = Σhkl [n/(n‐1)]0.5 Σi|I i(hkl) – <I(hkl)>|/ΣhklΣi I i(hkl), where I i(hkl) is the ith measurement of the intensity of reflection hkl, <I(hkl)> is the mean intensity of reflection hkl, and n is the number of observations of intensity I(hkl) (redundancy).
R = Σhkl║F o│‐│F c║/ Σhkl |F o│, where F o and F c are the observed and calculated structure factors, respectively. R free was calculated analogously for ~1000 randomly selected reflections excluded from refinement.