wwPDB validation report of PDB entry 3E0Z

THE CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG. THE TAG WAS REMOVED WITH TEV PROTEASE LEAVING ONLY A GLYCINE (0) FOLLOWED BY THE TARGET SEQUENCE.

1.HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
2.ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY.
3.A MET-INHIBITION PROTOCOL WAS USED FOR SELENOMETHIONINE
INCORPORATION DURING PROTEIN EXPRESSION. THE OCCUPANCY
OF THE SE ATOMS IN THE MSE RESIDUES WAS REDUCED TO 0.75
TO ACCOUNT FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL
S-MET INCORPORATION.
4.PEG MOLECULES FROM CRYOPROTECTION CONDITIOIN ARE MODELED
INTO THIS STRUCTURE.

Crystal structure of a putative imidazole glycerol phosphate synthase homolog (eubrec_1070) from eubacterium rectale at 1.75 A resolution

The analyses of the Patterson function reveals a significant off-origin peak that is 87.59 % 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 6.5171e-08. 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