Table 2. Data collection and refinement statistics.
Data collection | |
Space Group | P1 |
Cell dimensions | |
a, b, c (Å) | 38.985 45.014 80.89 |
α, β, γ, (°) | 93.60, 102.16, 97.34 |
Resolution (Å) | 30.93–1.78 (1.84–1.78) |
Rmerge (%) | 0.077 (0.50) |
I / σI | 28.9 (2.75) |
Completeness (%) | 94.63 (92.97) |
Redundancy | 7.1 (6.8) |
Refinement | |
No. reflections | 48157 (4735) |
Rwork / Rfree (%) | 0.169/0.204 |
No. atoms | |
Protein | 4100 |
Water | 481 |
Average B-factor | 32.23 |
Protein | 31.32 |
Water | 40.06 |
R.m.s. deviations | |
Bond lengths (Å) | 0.016 |
Bond angles (°) | 1.35 |
Ramachandran plot statistics (%) | |
Most favoured | 97.52 |
Allowed | 2.48 |
Disallowed | 0.0 |
*Values in parentheses are for highest-resolution shell.
Values in parentheses are for the highest resolution shell. Rmerge = ΣhΣi|Ih,i-Ih|/ΣhΣiIh,i, where Ih is the mean intensity of the i observations of symmetry related reflections of h. R = Σ|Fobs-Fcalc|/ΣFobs, where Fcalc is the calculated protein structure factor from the atomic model (Rfree was calculated with 5% of the reflections selected randomly).