wwPDB validation report of PDB entry 4LR4

Flat mirror (vertical focusing); single crystal Si(111) bent monochromator (horizontal focusing)

THE CONSTRUCT (26-394) 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. 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. 2. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS. ANISOU RECORD CONTAINS SUM OF TLS AND RESIDUAL U FACTORS. 3. THE MAD PHASES WERE USED AS RESTRAINTS DURING REFINEMENT. 4. PHOSPHATE (PO4), GLYCEROL (GOL), AND CHLORIDE (CL) MODELED WERE PRESENT IN PROTEIN/CYRO CONDITIONS. 5.NCS RESTRAINTS WERE IMPOSED BY AUTOBUSTER'S LSSR PROCEDURE (-AUTONCS). 6. RAMACHANDRAN OUTLIERS (A,D/378, A-D/181) ARE SUPPORTED BY DENSITY.

Crystal structure of a putative secreted protein (EUBREC_3654) from Eubacterium rectale at 2.43 A resolution

The analyses of the Patterson function reveals a significant off-origin peak that is 32.31 % 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 9.5882e-04. The detected translational NCS is most likely also responsible for the elevated intensity ratio. See the relevant section of the logfile for more details.

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)