TABLE 1.
Data collection and refinement statistics
r.m.s., root mean square.
| Data collection | |
| Resolution (Å)a | 20-2.1 (2.1-2.17) |
| Wavelength (Å) | 1.00 |
| Space group | P3121 |
| Unit cell dimensions (a = b, c) (Å) | 142.4, 217.1 |
| Measured reflections | 123276 |
| Completeness (%) | 83.4 (80.9) |
| Redundancy | 2.6 (2.6) |
| Mosaicity (°) | 0.32 |
| I/σ | 15.8 (1.9) |
| Rsym (%)b | 5.7 (23.3) |
| Wilson B factor | 37.6 |
| Refinement | |
| Rwork (%)c | 19.5 |
| Rfree (%)c | 23.3 |
| Number of residues/waters | 1438/1017 |
| R.m.s. bonds (Å)/angles (°) | 0.008/1.062 |
| Ramachandran plot (%)d | 87.9/11.2/0.5/0.6e |
| Average B values | 41.5 |
Values in parentheses correspond to the highest resolution bin.
Rsym = 100*ΣhΣi|li(h) — 〈l(h)〉|/ΣhΣili(h), where li(h) is the ith measurement of reflection h and 〈l(h)〉 is the average value of the reflection intensity.
Rwork = 100*Σ||Fobs| — |Fcalc||/|Fobs|, where Fobs and Fcalc are the structure factor amplitudes from the data and the model, respectively. Rfree is Rwork with 5% of the reflections set aside throughout refinement.
Numbers correspond to the percentage of amino acid residues in the favored, allowed, generously allowed, and disallowed regions, respectively. Calculated using PROCHECK (42).
Seven residues were observed in stereochemically strained conformations either due to crystal packing contacts (Tyr-219 in monomers A and C) or hydrogen bonding interactions (Asn-232 in monomers A—E).