wwPDB validation report of PDB entry 1GQE

ENGINEERED MUTATION: THR(246)ALA. RESIDUE 298 CORRESPONDS TO A LEUCINE IN THE SWISS-PROT SEQUENCE, BUT IS CLEARLY IDENTIFIED AS A VALINE IN ELECTRON DENSITY.
CRYSTALS FROM MUTANT T246A. RESIDUE 298 CORRESPONDS TO A LEUCINE IN THE SWISS-PROT SEQUENCE, BUT IS CLEARLY IDENTIFIED AS A VALINE IN ELECTRON DENSITY.

REFINEMENT RESTRAINED BY SAD PHASES REGION 247 - 257 WAS NOT VISIBLE IN THE ELECTRON DENSITY, BUT WAS MODELLED STEREOCHEMICALLY ACCORDING TO STRUCTURAL SIMILARITY WITH THE GGR MOTIF IN RIBOSOMAL PROTEIN S5 (1FJF) AND THE GGQ MOTIF IN ERF1 (1DT9)

Polypeptide Chain Release Factor 2 (RF2) from Escherichia coli

The largest off-origin peak in the Patterson function is 7.21% of the height of the origin peak. No significant pseudotranslation is detected.

20191225.v01 (using entries in the PDB archive December 25th 2019)

structure factor analysis and validation

geometric validation package for ligand chemistry in protein x-ray structures