wwPDB validation report of PDB entry 4G8M

(1S,2R)-2-[(S)-amino(carboxy)methyl]cyclobutanecarboxylic acid

GluR-2, AMPA-selective glutamate receptor 2, GluR-B, GluR-K2, Glutamate receptor ionotropic, AMPA 2, GluA2

THE PROTEIN CRYSTALLIZED IS THE EXTRACELLULAR LIGAND-BINDING DOMAIN OF GLUA2. TRANSMEMBRANE REGIONS WERE GENETICALLY REMOVED AND REPLACED WITH A GLY-THR LINKER (RESIDUES 115-116 IN THE PDB-FILE). THEREFORE THE SEQUENCE MATCHES DISCONTINUOUSLY WITH THE REFERENCE DATABASE (UNP RESIDUES 413-527 AND 653-796, NUMBERING WITH SIGNAL PEPTIDE OF 21 AMINO ACIDS). THE FIRST TWO RESIDUES (GLY, ALA) ARE CLONING REMNANTS

Crystal structure of the GluA2 ligand-binding domain (S1S2J) in complex with the agonist CBG-IV at 2.05A resolution

The analyses of the Patterson function reveals a significant off-origin peak that is 22.72 % 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 5.3879e-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)