wwPDB validation report of PDB entry 4AV7

STRUCTURE DETERMINATION OF THE STEREOSELECTIVE INVERTING SEC-ALKYLSULFATASE PISA1 FROM PSEUDOMONAS SP.

STRUCTURE AND MECHANISM OF THE FIRST INVERTING ALKYLSULFATASE SPECIFIC FOR SECONDARY ALKYLSULFATASES

ENGINEERED RESIDUE IN CHAIN A, SER 233 TO TYR ENGINEERED RESIDUE IN CHAIN A, PHE 250 TO GLY ENGINEERED RESIDUE IN CHAIN B, SER 233 TO TYR ENGINEERED RESIDUE IN CHAIN B, PHE 250 TO GLY ENGINEERED RESIDUE IN CHAIN C, SER 233 TO TYR ENGINEERED RESIDUE IN CHAIN C, PHE 250 TO GLY ENGINEERED RESIDUE IN CHAIN D, SER 233 TO TYR ENGINEERED RESIDUE IN CHAIN D, PHE 250 TO GLY ENGINEERED RESIDUE IN CHAIN E, SER 233 TO TYR ENGINEERED RESIDUE IN CHAIN E, PHE 250 TO GLY

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT ALL CHAINS HAVE DISORDERED REGIONS WITH HIGH B-FACTOR DISORDERED REGIONS WERE MODELED VIA NCS
Structure determination of the double mutant S233Y F250G from the sec- alkyl sulfatase PisA1
The largest off-origin peak in the Patterson function is 1.87% 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)