wwPDB validation report of PDB entry 3CBU

Single crystal Si(111) bent (horizontal focusing)

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

1. HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
2. 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
FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION.
3. ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY.
4. THERE IS UNMODELED DENSITY NEAR SER 10 IN EACH CHAIN, WHICH
IS THE PUTATIVE GLUTATHIONE BINDING SITE.
5. PO4 AND EDO WERE MODELED BASED ON CRYSTALLIZATION
AND CRYOPROTECTION CONDITIONS.

Crystal structure of a putative glutathione s-transferase (reut_a1011) from ralstonia eutropha jmp134 at 2.05 A resolution

The largest off-origin peak in the Patterson function is 4.20% of the height of the origin peak. No significant pseudotranslation is detected.

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)