wwPDB validation report of PDB entry 1YSZ

deletion of 287-327 replaced by 4 glycines
N-terminal Domain of GRP94 Residues (69-337)

Crystal Structure Of The N-Domain Of The Er Hsp90 Chaperone Grp94 In Complex With The Specific Ligand Neca

Crystal Structure Of The N-Domain Of Grp94 Lacking The Charged Domain In Complex With Neca

Ligand Induced Conformational Shift in the N-Terminal Domain of Grp94, Open Conformation

Ligand Induced Conformational Shift in the N-Terminal Domain of Grp94, Open Conformation Complexed with the Physiological Partner ATP

Ligand Induced Conformational Shift in the N-Terminal Domain of Grp94, Open Conformation ADP-Complex

ONLY FRAGMENTS OF PEG400 (PG4) WERE IDENTIFIED AND IN MANY CASES SEVERAL ATOMS WERE MISSING DUE TO LACK OF ELECTRON DENSITY.

Crystal Structure of the Unliganded Form of GRP94, the ER Hsp90: Basis for Nucleotide-Induced Conformational Change, GRP94N(DELTA)41 APO CRYSTAL SOAKED WITH NECA

The largest off-origin peak in the Patterson function is 7.42% 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)