Table II. Native data collection and refinement statistics.
| Form A | Form B | Form C | |
|---|---|---|---|
| Space group | P21 | P21 | P21 |
| Unit cell dimensions | a = 75.30, b = 130.18, | a = 74.58, b = 171.20, | a = 73.92, b = 172.63, |
| c = 92.55 Å, β = 106.48° | c = 80.37 Å, β = 116.49° | c = 73.99 Å, β = 117.50° | |
| Resolution range (Å) | 38.0–2.1 | 25.0–2.8 | 44.0–2.0 |
| Wavelength (Å) | 1.012 | 1.5418 | 1.083 |
| No. of unique reflections | 101 445 | 37 393 | 109 778 |
| Average multiplicity | 3.1 | 2.5 | 3.9 |
| Completeness (%) | 99.1 (97.5) | 85.6 (41.0) | 100.0 (100.0) |
| <I>/σI | 16.0 (2.5) | 13.3 (1.9) | 27.4 (7.2) |
| Rmerge (I> –3σI) | 5.9 (38.5) | 7.3 (39.8) | 5.0 (19.3) |
| R/Rfreea | 0.199/0.239 | 0.209/0.253 | 0.168/0.197 |
| Residues | |||
| monomer 1α | 439–451, 460–863 | 461–865 | 462–870 |
| monomer 1β | 461–865 | 460–864 | 462–866 |
| monomer 2α | 464–865 | 460–866 | 468–871 |
| monomer 2β | 458–864 | 453–865 | 477–872 |
| Ligands | 4 HMG, 4 CoA | 4 HMG-CoA | 4 HMG, 4 CoA, 4 NADP+ |
| Waters | 282 | 472 | |
| Other molecules | 2 DTT | ||
| No. of atoms in refinement | 12 669 | 12 351 | 12 911 |
| Deviation from ideality | 0.0105/1.51 | 0.0157/1.62 | 0.0120/1.58 |
| R.m.s.d. bonds (Å)/angles (°) | |||
| average protein B–factors | 56.3/30.3/36.0 | 71.0/46.6/52.44 | 34.8/16.3/19.3 |
| N/L/S domain (Å2)b | |||
| average ligand B–factors (Å2) | 41.6 | 58.6 | 23.0 |
| B–factor r.m.s.d. of bonded atoms main/side chain | 1.190/2.035 | N/Ac | 1.39/2.54 |
aR = (Σ∣Fobs – Fcalc∣)/(ΣFobs), where Fobs and Fcalc are observed and calculated structure factors, respectively.
bThe three domains are indicated in Figure 1.
cB–factors were grouped for residues.