wwPDB validation report of PDB entry 2ZIT

White beam slits, cryo-cooled first and sagittally bent second crystal of double crystal monochromator (DCM), vertically focusing mirror (VFM)

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 the eEF2-ExoA(E546A)-NAD+ complex

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

THIS SEQUENCE IS BASED ON UNIPROT DATABASE, P11439, REF. 1.

When refining TLS, the output PDB file always has the ANISOU records for the atoms involved in TLS groups. The anisotropic B-factor in ANISOU records is the total B-factor (B_tls + B_individual). The isotropic equivalent B-factor in ATOM records is the mean of the trace of the ANISOU matrix divided by 10000 and multiplied by 8*pi^2 and represents the isotropic equivalent of the total B-factor (B_tls + B_individual). To obtain the individual B-factors, one needs to compute the TLS component (B_tls) using the TLS records in the PDB file header and then subtract it from the total B-factors (on the ANISOU records).
Test set chosen from eEF2-ExoA(E546H)-NAD+

Elongation factor 2, Exotoxin A (E.C.2.4.2.-)

The analyses of the Patterson function reveals a significant off-origin peak that is 61.09 % 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 1.3798e-05. The detected translational NCS is most likely also responsible for the elevated intensity ratio. See the relevant section of the logfile for more details.
20191225.v01 (using entries in the PDB archive December 25th 2019)
structure factor analysis and validation
geometric validation package for ligand chemistry in protein x-ray structures