TABLE 2.
X-ray data collection and refinement statistics
| Data collection | |
| Space group | P212121 |
| Unit cell, Å, ° | a = 61.51, b = 75.29, c = 77.45 α = β = γ = 90.00 |
| Wavelength, Å | 1.54178 |
| Temperature (K) | 100 |
| Resolution, Å | 25-1.7 (1.8-1.7)a |
| Unique reflections | 40244 (6215) |
| Rintb | 0.071 (0.539) |
| Average redundancy | 8.2 (5.7) |
| 〈I〉/〈σ(I)〉 | 17.5 (2.4) |
| Completeness, % | 99.8 (98.8) |
| Structure refinement | |
| Resolution, Å | 25-1.7 (1.74-1.70) |
| R/Rfree | 0.150 (0.257)/ 0.194 (0.345) |
| Protein atoms | 2904 |
| Water molecules | 583 |
| Other atoms | 1 |
| r.m.s.d.c from ideal bond length, Å (51) | 0.019 |
| r.m.s.d. from ideal bond angles, ° (51) | 1.969 |
| Wilson B-factor | 14.3 |
| Average B-factor for protein atoms, Å2 | 19.2 |
| Average B-factor for water molecules, Å2 | 32.5 |
| Ramachandran plot statistics, % (50) | |
| Allowed | 99.8 |
| Favored | 96.5 |
| Outliers | 1 (Asn-562) |
a Statistics for the highest resolution bin are in parentheses.
b Rint = Σ| I − 〈I〉|/Σ|I|, where I is the intensity of an individual reflection and 〈I〉 is the mean intensity of a group of equivalents, and the sums are calculated over all reflections with more than one equivalent measured.
c r.m.s.d. means root mean square deviation.