wwPDB validation report of PDB entry 5N6S

Beta-D-glucoside glucohydrolase,Cellobiase,Gentiobiase

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
THE DATA ARE HIGHLY ANISOTROPIC.
THERE ARE UNMODELLED REGIONS FOR C212-213, C359-363, C372, C423-427,
D233, D361-364, D425-427 and D430-432. THE LIGAND MOLECULES IN THE PROTEIN ACTIVE SITES ARE MODELLED AS FOLLOWS: CHAIN A, IN 2 CONFORMATIONS AT OCCUPANCIES 0.6/0.4, CHAIN B, IN 1 CONFORMATION, CHAIN C, WITH THE CARBA-CYCLOPHELLITOL AND AMIDE GROUPS AT OCCUPANCY 1, AND AZIDOBUTYL GROUP AT OCCUPANCY 0.5, CHAIN D, WITH ONLY THE CARBA-CYCLOPHELLITOL AND AMIDE MOIETIES PRESENT, AT OCCUPANCY 1.

Thermotoga maritima family 1 Glycoside hydrolase complexed with Carba-Cyclophellitol transition state mimic

binding site for residues PEG B 513 and PGE B 514

The largest off-origin peak in the Patterson function is 6.24% 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