wwPDB validation report of PDB entry 3L2N

Single crystal Si(111) bent monochromator (horizontal focusing)

THIS CONSTRUCT WAS EXPRESSED WITH A PURIFICATION TAG MGSDKIHHHHHHENLYFQG.

1.HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 2.ATOM RECORDS CONTAIN 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 FOR THE REDUCED SCATTERING POWER DUE TO PARTIAL S-MET INCORPORATION. 4.CALCIUM (CA) HAS BEEN MODELED AT THE PUTATIVE ACTIVE SITE BASED ON ITS PRESENCE AS A CO-CRYSTALLIZATION COMPOUND AND A FLUORESCENCE BASED THERMAL SHIFT BINDING ASSAY. 5.AN UNIDENTIFIED LIGAND (UNL) RESEMBLING GLUTAMIC OR ASPARTIC ACID HAS BEEN MODELED AT THE PUTATIVE ACTIVE SITE. 6.ACETATE (ACT) AND GLYCEROL (GOL) FROM THE CRYSTALLIZATION SOLUTION HAVE BEEN MODELED IN THE SOLVENT STRUCTURE. 7.RAMACHANDRAN OUTLIERS AT RESIDUE 37 IN BOTH CHAINS ARE SUPPORTED BY ELECTRON DENSITY.

Crystal structure of Putative carboxypeptidase A (YP_562911.1) from SHEWANELLA DENITRIFICANS OS-217 at 2.39 A resolution

CRYSTAL PACKING ANALYSIS SUGGESTS THE ASSIGNMENT OF A TETRAMER AS THE SIGNIFICANT OLIGOMERIC FORM IN SOLUTION. ANALYTICAL SIZE-EXCLUSION CHROMATOGRAPHY COUPLED WITH STATIC LIGHT SCATTERING SUGGESTS A HEXAMER AS THE SOLUTION STATE OLIGOMERIC FORM.

The largest off-origin peak in the Patterson function is 4.83% 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)