wwPDB validation report of PDB entry 2VOM

HIGH-RESOLUTION DOUBLE- CRYSTAL SI(220) SAGITTAL FOCUSING, ROSENBAUM-ROCK VERTICAL FOCUSING MIRROR

HUMAN TRIOSEPHOSPHATE ISOMERASE OF NEW CRYSTAL FORM

TRIOSEPHOSPHATE ISOMERASE (TIM) COMPLEXED WITH 2-PHOSPHOGLYCOLIC ACID

ENGINEERED RESIDUE IN CHAIN A, GLU 105 TO ASP ENGINEERED RESIDUE IN CHAIN B, GLU 105 TO ASP ENGINEERED RESIDUE IN CHAIN C, GLU 105 TO ASP ENGINEERED RESIDUE IN CHAIN D, GLU 105 TO ASP
THE STRUCTURE CORRESPONDS TO THE MUTANT E104D

CHAIN D IS MORE DISORDERED THAN CHAINS A, B AND C ON RESIDUES 1 THIS IS PROBABLY DUE TO LACK OF CRYSTALLOGRAPHIC CONTACTS

Structural basis of human triosephosphate isomerase deficiency. Mutation E104D and correlation to solvent perturbation.

The largest off-origin peak in the Patterson function is 4.44% 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)