wwPDB validation report of PDB entry 2XP3

PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1

PIN1, PEPTIDYL-PROLYL CIS-TRANS ISOMERASE PIN1, PPIASE PIN1, ROTAMASE PIN1

STRUCTURAL BASIS FOR THE PHOSPHOSERINE-PROLINE RECOGNITIONBY GROUP IV WW DOMAINS

SOLUTION STRUCTURE OF PIN1 WW DOMAIN COMPLEXED WITH CDC25PHOSPHOTHREONINE PEPTIDE

PIN1 PEPTIDYL-PROLYL CIS-TRANS ISOMERASE FROM HOMO SAPIENS

DISCOVERY OF CELL-ACTIVE PHENYL-IMIDAZOLE PIN1 INHIBITORS BY STRUCTURE-GUIDED FRAGMENT EVOLUTION

SOLUTION STRUCTURE OF THE PPIASE DOMAIN OF HUMAN PIN1

SOLUTION STRUCTURE OF PIN1 WW DOMAIN COMPLEXED WITH HUMANTAU PHOSPHOTHREONINE PEPTIDE

ENGINEERED RESIDUE IN CHAIN A, ARG 14 TO ALA

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.

PEPTIDYL-PROLYL CIS-TRANS ISOMERASE NIMA-INTERACTING 1 (E.C.5.2.1.8)

The largest off-origin peak in the Patterson function is 7.94% 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