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. 2016 Jul 18;113(31):E4567–E4576. doi: 10.1073/pnas.1604936113

Table S2.

Data collection and refinement statistics for crystal structure of AtSAL1 (PDB 5ESY)

Space group P61
Data processing
 Cell dimensions (Å) a = b, c 137.1, 74.6
 Resolution range, Å 38.25–3.05 (3.24–3.05)*
 Total number of reflections 125243 (20978)
 Number of unique reflections 15341 (2522)
 Completeness, % 99.6 (92.8)
 Mean I/σ(I) 15.2 (2.2)
 Wilson B factor, Å2 83.6
CC1/2 0.999 (0.620)
Rmerge 0.104 (1.11)
Refinement
Rwork/Rfree, % 22.7/25.8 (33.5/41.8)
 Total number protein of atoms 5082
 RMSD for bonds, Å 0.004
 RMSD for angles, deg 1.00
 Ramachandran favored, % 86
 Ramachandran outliers, % 1.9
 Clashscore 12
 Average B factor, Å2 106.0
*

Values in parentheses are for the highest-resolution shell.

Pearson’s correlation coefficient calculated from two half-sets of the data (62, 63).