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Table 1 Data collection and refinement statistics

From: Ternary complex structures of human farnesyl pyrophosphate synthase bound with a novel inhibitor and secondary ligands provide insights into the molecular details of the enzyme’s active site closure

Data sets
PDB ID 4H5C 4H5D 4H5E
Ligands YS0470, Pi YS0470, PPi YS0470, IPP
Data collection
Space group P 41212 P 41212 P 41212
Unit cell dimension (Å) a = b = 110.98, c = 66.79 a = b = 111.53, c = 66.24 a = b = 111.24, c = 65.65
Resolution range (Å) 50.0-2.02 (2.05-2.02) 50.0-2.02 (2.05-2.02) 50.0-2.05 (2.09-2.05)
Redundancy 26.4 (24.1) 28.2 (27.9) 27.3 (26.2)
Completeness (%) 99.9 (100) 100 (100) 100 (100)
I/σ(I) 36.9 (5.7) 59.9 (7.7) 47.7 (6.9)
R merge 0.061 (0.475) 0.043 (0.418) 0.043 (0.369)
Refinement
No. reflections 26,374 26,414 24,849
Rwork/Rfree 0.180/0.213 0.180/0.203 0.186/0.233
No. protein atoms 2,705 2,748 2,743
No. ligand atoms 31 35 40
No. ion atoms 3 3 3
No. solvent atoms 132 136 108
R.m.s. deviations
Bond length (Å) 0.018 0.019 0.020
Bond angle (°) 1.8 1.9 2.0