wwPDB validation report of PDB entry 2YHA

RESIDUES 787-838 REPLACED BY THREE-RESIDUE LINKER
POST-TRANSCRIPTIONAL GENE SILENCING PROTEIN QDE-2
MID-PIWI DOMAINS, RESIDUES 506-786 AND 839-938

CRYSTAL STRUCTURE OF THE N. CRASSA QDE-2 MID DOMAIN RELATED ENTRIES

CRYSTAL STRUCTURE OF THE N. CRASSA QDE-2 AGO MID- PIWI DOMAINS

THE FIRST 4 AMINO ACIDS (GAMA) ARISE FROM THE CLONING SITE RESIDUES R787 TO R838 OF UNIPROT ENTRY Q9P8T1 WERE REPLACED BY A GSG LINKER (GIVEN RESIDUE NUMBERS 787, 837, AND 838 HERE).

THE FOLLOWING RESIDUES ARE DISORDERED, K786 TO A840, F873 TO I882. SIDE-CHAINS OF THE FOLLOWING RESIDUES WERE TRUNCATED AT CB ATOMS: H841, Y842, K857, D860, T861, L862, E863, Q864, T866, H867, Y871, L872. HYDROGENS WERE REFINED IN THE RIDING POSITIONS.

Crystal Structure of the N. crassa QDE-2 AGO MID-PIWI Domains

The largest off-origin peak in the Patterson function is 5.86% 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