wwPDB validation report of PDB entry 4AGW

PROTO-ONCOGENE TYROSINE-PROTEIN KINASE SRC

3-{2-[(cyclopropylcarbonyl)amino][1,3]thiazolo[5,4-b]pyridin-5-yl}-N-{4-[(4-ethylpiperazin-1-yl)methyl]-3-(trifluoromet hyl)phenyl}benzamide

SRC KINASE, PROTO-ONCOGENE C-SRC, PP60C-SRC, P60-SRC

C-SRC (SH3 DOMAIN) COMPLEXED WITH THE PROLINE-RICH LIGAND PLR1 (AFAPPLPRR) (NMR, MINIMIZED AVERAGE STRUCTURE)

C-SRC (SH3 DOMAIN) COMPLEXED WITH THE PROLINE-RICH LIGAND PLR1 (AFAPPLPRR) (NMR, 16 STRUCTURES)

C-SRC (SH3 DOMAIN) COMPLEXED WITH THE PROLINE-RICH LIGAND RLP2 (RALPPLPRY) (NMR, MINIMIZED AVERAGE STRUCTURE)

SRC SH2 THREF1TRP MUTANT COMPLEXED WITH THE PHOSPHOPEPTIDE PYVNV

CRYSTAL STRUCTURE OF THE SRC SH2 DOMAIN COMPLEXED WITHPEPTIDE (SDPYANFK)

C-SRC (SH3 DOMAIN) COMPLEXED WITH THE PROLINE-RICH LIGAND RLP2 (RALPPLPRY) (NMR, 16 STRUCTURES)

STRUCTURE OF SIGNAL TRANSDUCTION PROTEIN, NMR, MINIMIZEDAVERAGE STRUCTURE

PROTO-ONCOGENE TYROSINE-PROTEIN KINASE SRC (E.C.2.7.10.2)
Discovery of a small molecule type II inhibitor of wild-type and gatekeeper mutants of BCR-ABL, PDGFRalpha, Kit, and Src kinases

CHAIN A AND (RESSEQ 335:405 OR RESSEQ 425:533 )

CHAIN B AND (RESSEQ 335:405 OR RESSEQ 425:533 )

The analyses of the Patterson function reveals a significant off-origin peak that is 20.53 % 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 8.5126e-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)