wwPDB validation report of PDB entry 3PNX

THIS 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. 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. SODIUM (NA) AND CHLORIDE (CL) IONS HAVE BEEN MODELED INTO THE STRUCTURE. 4. ELECTRON DENSITY SUPPORTS THE MODELING OF CYS 120 ON THE SIX SUBUNITS IN THE ASYMMETRIC UNIT AS CYSTEINESULFONIC ACID (OCS). 5. ATOM RECORD CONTAINS RESIDUAL B FACTORS ONLY 5. LEU 83 ON THE C AND E SUBUNITS AND ASN 82 ON THE E SUBUNIT ARE IN REGIONS WHERE ELECTRON DENSITIES ARE DISORDERED, AND THESE RESIDUES ARE RAMACHANDRAN OUTLIERS IN MOLPROBITY. 6. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS. 7. WATERS WERE EXCLUDED FROM AUTOMATIC TLS ASSIGNMENT.

Crystal structure of a putative sulfurtransferase dsrE (Swol_2425) from Syntrophomonas wolfei str. Goettingen at 1.92 A resolution

ANALYTICAL SIZE EXCLUSION CHROMATOGRAPHY WITH STATIC LIGHT SCATTERING SUPPORTS THE ASSIGNEMENT OF A TRIMER AS A SIGNIFICANT OLIGOMERIZATION STATE IN SOLUTION.

The largest off-origin peak in the Patterson function is 4.10% 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)