Table 2.
AtMTAN1-SAH | |
---|---|
Diffraction statistics | |
Space group | P21 |
Unit cell dimensions (Å) | |
a | 45.9 |
b | 126.4 |
c | 83.8 |
β (°) | 101.7 |
No. observed reflections | 173,922 |
No. unique reflections | 46,037 |
Resolution range (Å) | 23.12–2.20 |
Rmerge(%)a | 8.4 (28.9) |
Redundancy | 3.8 |
Completeness (%) | 97.2 (95.2) |
Average (I/σI) | 7.4 (3.0) |
Refinement statistics | |
No. of protein atoms | 7524 |
No. of ligand atoms | 68 |
No. of water molecules | 519 |
Resolution range (Å) | 23.12–2.20 |
No. reflections in test set | 4627 |
Test set size (%) | 10 |
Rcryst(%)b | 20.8 |
Rfree(%)c | 26.2 |
Overall B factor (Å2) | 22.6 |
Ligands | 20.0 |
Water | 23.1 |
R.m.s. deviation | |
Bonds (Å) | 0.012 |
Angles (°) | 1.4 |
Dihedral angles (°) | 24.5 |
Improper angles (°) | 3.0 |
Molprobity output scores (%)e | |
Ramachandran favored | 98.1 |
Ramachandran outliers | 0.0 |
Cruickshank’s DPI based on Rfreed | 0.26 |
Values given in parentheses refer to reflections in the outer resolution shell: (2.28–2.20 Å).
Rmerge = ΣΣ| I(k) − 〈I〉|/ΣI(k), where I(k) and 〈I〉 represent the diffraction intensity values of the individual measurements and the corresponding mean values. The summation is over all unique measurements.
, where Fobs and Fcalc are the observed and calculated structure factors, respectively.
Rfree is the sum extended over a subset of reflections (10%) excluded from all stages of the refinement.
Cruickshank’s diffraction component precision index (DPI) as an estimate of coordinate error (Cruickshank, 1999).
As calculated using Molprobity (Lovell et al., 2003).