wwPDB validation report of PDB entry 1GI3

the same protein complexes with a different inhibitor

Residues simultaneously refined in two or more conformations are:
Val53, Leu66, Ser86, Ser113, Ser130, Lys159, Asp165, Ser170,
Ser217, Lys230, Ser236
Note that HOH383 makes short H-bonds to OgSer195 and O6' of the inhibitor
Disordered waters are:
HOH304 which is close to HOH305;
HOH331 which is close to HOH332;
HOH398 which is close to HOH399;
HOH407 which is close to HOH408 which is close to HOH409;
HOH468 which is close to HOH469 which is close to HOH470;
HOH537 which is close to HOH538;
HOH618 which is close to HOH619;
HOH719 which is close to HOH720 which is close to HOH721;
HOH838 which is close to HOH839;
HOH917 which is close to HOH918;

His40 and HIS91 are MONOPROTONATED ON THE EPSILON NITROGEN.
His57 is doubly protonated.

A NOVEL SERINE PROTEASE INHIBITION MOTIF INVOLVING A MULTI-CENTERED SHORT HYDROGEN BONDING NETWORK AT THE ACTIVE SITE

The largest off-origin peak in the Patterson function is 8.17% 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)