Table 1. Crystal parameters, data-collection and structure-refinement statistics.
Values in parentheses are for the highest resolution bin.
| Data processing | |
| Resolution range () | 27.082.40 (2.462.40) |
| Space group | P41 |
| Unit-cell parameters (, ) | a = b = 96.77, c = 44.31, = = = 90.00 |
| Unique reflections | 14385 (765) |
| Completeness (%) | 92.7 (90.2) |
| Mean I/(I) | 14.4 (1.7) |
| R merge † (%) | 8.3 (32.9) |
| Refinement statistics | |
| Resolution range () | 27.082.40 |
| R factor‡/R free § (%) | 23.11/27.31 |
| Mean B factor (2) | 48.69 |
| No. of protein atoms | 1949 |
| No. of water atoms | 69 |
| R.m.s.d.¶ bond lengths () | 0.015 |
| R.m.s.d.¶ bond angles () | 1.448 |
| Ramachandran plot†† | |
| Residues in most favoured regions (%) | 95.15 |
| Residues in additional allowed regions (%) | 4.85 |
| Residues in disallowed regions (%) | 0 |
†
R
merge = 
, where I
i(hkl) is the intensity of an observation and I(hkl) is the mean value for its unique reflection; summations are over all reflections.
‡
R factor = 
, where F
obs and F
calc are the observed and calculated structure-factor amplitudes, respectively.
§
R free was calculated with 5% of the data excluded from the refinement.
¶
Root-mean-square deviation from ideal values.
††
Categories were defined by MolProbity.