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Table 1 X-ray data collection and refinement statistics

From: Structural analysis of inhibition of E. coli methionine aminopeptidase: implication of loop adaptability in selective inhibition of bacterial enzymes

Inhibitor 4 5 6 7 8
Inhibitor code B23 B21 A04 A05 B18
PDB code 2Q92 2Q93 2Q94 2Q95 2Q96
Cell Parameters      
Space group P 21 P 21 P 21 P 21 P 21
a (Å) 38.1 39.1 38.2 38.8 39.3
b (Å) 61.0 62.3 60.6 62.4 62.0
c (Å) 50.7 52.4 50.6 52.4 52.4
β (deg) 104.9 108.8 104.8 108.4 108.8
X-ray Data Collection      
Resolution range (Å)      
   Overall 30-1.9 20-1.6 20-1.6 24-1.7 20-1.6
   Outer shell 2.0-1.9 1.7-1.6 1.7-1.6 1.8-1.7 1.7-1.6
Collected reflections 63,846 108,452 100,161 93,908 112,816
Unique reflections 17,799 29,294 27,719 26,219 31,502
Completeness (%) a 100 (100) 93 (89) 99 (98) 100 (100) 100 (100)
I/σ (I)a 18.1 (4.7) 23.6 (11.1) 20.8 (2.5) 17.3 (2.8) 23.5 (7.2)
Rmerge (%) a 5.4 (22.1) 3.0 (9.9) 4.4 (36.3) 5.5 (38.9) 3.8 (13.8)
Refinement Statistics      
R (%) 20.3 22.6 21.3 21.4 21.1
Rfree (%) 23.8 25.1 23.8 23.9 23.5
RMSD bonds (Å) 0.006 0.005 0.005 0.005 0.004
RMSD angles (deg) 1.32 1.32 1.32 1.33 1.30
No. of solvent molecules 133 224 194 195 234
<B> enzyme (Å 2) 21.4 11.3 20.9 19.0 11.8
<B> inhibitor (Å 2) 25.8 13.3 18.4 16.3 12.1
<B> water (Å 2) 27.0 18.6 28.9 25.8 18.8
  1. a Numbers given in parentheses corresponding to the outer shell of data.