wwPDB validation report of PDB entry 1AFV

HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 CAPSID PROTEIN

LIGHT CHAIN RESIDUES 1 - 217, HEAVY CHAIN RESIDUES 1 - 220

THE CARBOXY-TERMINAL RESIDUES 152 - 231 OF THE HIV-1 CAPSID PROTEIN ARE DISORDERED AND NOT VISIBLE IN THE ELECTRON DENSITY MAPS.
MOLECULAR REPLACEMENT, MULTIPLE ISOMORPHOUS REPLACEMENT, ANOMALOUS DISPERSION

HUMAN IMMUNODEFICIENCY VIRUS TYPE 1 CAPSID PROTEIN, ANTIBODY FAB25.3 FRAGMENT
HIV-1 CAPSID PROTEIN (P24) COMPLEX WITH FAB25.3

The analyses of the Patterson function reveals a significant off-origin peak that is 48.98 % 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 7.9592e-05. 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