wwPDB validation report of PDB entry 3B82

EF-2, Translation elongation factor 2, Eukaryotic elongation factor 2, eEF2, Ribosomal translocase

ADP-ribosylated eEF2 in complex with catalytic fragment of ExoA

Structure of eEF2-ExoA in complex with PJ34

Structure of the eEF2-ExoA(R551H)-NAD+ complex

THERE ARE ILE->VAL AND GLY->SER SEQUCE CONFLICTS AT RESIDUES 432 AND 540 IN THE UNIPROT DATABASE.

Test set chosen from 1ZM9 and extended to 2.35A
Structure of the eEF2-ExoA(E546H)-NAD+ complex
The analyses of the Patterson function reveals a significant off-origin peak that is 40.05 % of the origin peak, indicating pseudo-translational symmetry. The chance of finding a peak of this or larger height by random in a structure without pseudo-translational symmetry is equal to 2.8973e-04. The detected translational NCS is most likely also responsible for the elevated intensity ratio. See the relevant section of the logfile for more details.
structure factor analysis and validation
geometric validation package for ligand chemistry in protein x-ray structures
20191225.v01 (using entries in the PDB archive December 25th 2019)