wwPDB validation report of PDB entry 2C9O

RUVBL1,49-KDA TATA BOX-BINDING PROTEIN-INTERACTING PROTEIN, 49 KDA TBP-INTERACTING PROTEIN, TIP49A, PONTIN 52,NUCLEAR MATRIX PROTEIN 238,NMP 238,54 KDA ERYTHROCYTE CYTOSOLIC PROTEIN, ECP-54, TIP60-ASSOCIATED PROTEIN 54-ALPHA, TAP54-ALPHA

HAS SINGLE-STRANDED DNA-STIMULATED ATPASE AND ATP-DEPENDENT DNA HELICASE (3' TO 5') ACTIVITY.

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. BECAUSE THEIR ELECTRON DENSITY COULD NOT BE SEEN, THE FOLLOWING RESIDUES ARE MISSING FROM THE FINAL MODEL 1-8, 142-155, 248-276 AND 450-456 IN CHAIN A, 1-10, 142-154, 245-278 AND 449-456 IN CHAIN B, AND 1-7, 129-230, 247-276 AND 450-456 IN CHAIN C. ALSO, ZERO (0.01) OCCUPANCY WAS GIVEN TO 26 ATOMS IN CHAIN A, 48 IN CHAIN B AND 84 IN CHAIN C.

3D Structure of the human RuvB-like helicase RuvBL1

The analyses of the Patterson function reveals a significant off-origin peak that is 22.93 % of the origin peak, indicating pseudo-translational symmetry. The chance of finding a peak of this or larger height by random in a structure without pseudo-translational symmetry is equal to 5.1589e-03. The detected translational NCS is most likely also responsible for the elevated intensity ratio. See the relevant section of the logfile for more details.

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