wwPDB validation report of PDB entry 5VSE

Histone-lysine N-methyltransferase EHMT2

Euchromatic histone-lysine N-methyltransferase 2,HLA-B-associated transcript 8,Histone H3-K9 methyltransferase 3,H3-K9-HMTase 3,Lysine N-methyltransferase 1C,Protein G9a

chain 'B' and (resid 1022 through 1079 )

chain 'B' and (resid 1080 through 1110 )

chain 'B' and (resid 1111 through 1155 )

chain 'B' and (resid 1156 through 1190 )

chain 'A' and (resid 1006 through 1025 )

chain 'A' and (resid 1026 through 1062 )

chain 'A' and (resid 1063 through 1096 )

chain 'A' and (resid 1097 through 1140 )

chain 'A' and (resid 1141 through 1162 )

chain 'A' and (resid 1163 through 1190 )

Histone-lysine N-methyltransferase EHMT2 (E.C.2.1.1.-,2.1.1.43)
Structure of human G9a SET-domain (EHMT2) in complex with inhibitor 17: N~2~-cyclopentyl-6,7-dimethoxy-N~2~-methyl-N~4~-(1-methylpiperidin-4-yl)quinazoline-2,4-diamine

(chain A and (resid 919 through 1090 or resid 1095 through 1190))

The analyses of the Patterson function reveals a significant off-origin peak that is 23.16 % 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 4.9307e-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.

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)