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. 2021 Jul 1;12:100074. doi: 10.1016/j.mbplus.2021.100074

Table 2.

Crystallographic refinement statistics for our LATS1 (residues 69–91)-bound human Nf2/merlin (residues 1–339) structure.

Resolution (last shell) 63.28 Å–1.61 Å (1.62 Å–1.61 Å)
No. of reflections, working set 55,750 (1053)
No. of reflections, test set 2748 (62)
R-factor * 0.200 (0.233)
R-free, 5% of reflections omitted 0.227 (0.308)
No. of non-hydrogen atoms:
 protein 2944
 ligands 21
 solvent 426
Average B-factor:
 protein 30.35 Å2
 ligand 40.38 Å2
 solvent 42.66 Å2
Root-mean-square deviation from ideal values:
 bond lengths 0.008 Å
 bond angles 0.87°
 Ramachandran plot, favoured 99.41%
 Ramachandran plot, allowed 0.29%
 Ramachandran plot, outliers 0.30%

* R-factor =hklFobshkl-Fcalc(hkl)hklFobs(hkl).