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.