Skip to main content

Table 1 Data Collection and Refinement Statistics

From: Structure of human aspartyl aminopeptidase complexed with substrate analogue: insight into catalytic mechanism, substrate specificity and M18 peptidase family

  hDNPEP·Zn2+·ABH
PDB accession code 4DYO
Data collection  
Beamline Diamond Light Source, I03
Wavelength (Å) 0.9763
Spacegroup F 432
Resolution rangea (Å) 56.11 – 2.20 (2.32 – 2.20)
Unit cell dimensions a = b = c = 224.60 Å; α = β = γ = 90.0°
No. unique reflectionsa 32,192 (4,486)
Completenessa (%) 99.6 (97.5)
I/σIa 10.4 (2.2)
Rmergea (%); Rpima (%) 17.9 (83.3); 5.5 (29.7)
Redundancya 10.8 (8.0)
Wilson B factor (Å2) 28.5
Refinement  
No. atoms in refinement (P/L/M/O)c 3585/10/2/358
Rfact (%) 15.5
Rfree (%) 19.5
Bf (P/L/M/O)c2) 26/30/28/28
rms deviation bond lengthb (Å) 0.015
rms deviation bond angleb (°) 1.5
Molprobity  
Ramachandran favoured 97.1
Ramachandran allowed 99.8
  1. a Values in brackets show the statistics for the highest resolution shells.
  2. b rms, root-mean-square.
  3. c P/L/M/O indicate protein, ligand molecules in the active sites, metal zinc ions and other molecules, respectively.