Backbone 1H, 13C, and 15N chemical shift assignments for the T686S variant of the ligand-binding domain of human ionotropic glutamate receptor 2 complexed with glutamate

separate tube (no insert) not similar to the experimental sample tube

Structural Mechanisms Underlying Activity Changes in an AMPA-type Glutamate Receptor Induced by Substitutions in Its Ligand-Binding Domain.

human T686S and flip variant form of GluR2-LBD complexed with glutamate

Functional Structure Biology Laboratory, Graduate School of Medical Life Science, Yokohama City University

Laboratory for Biomolecular Function Simulation, RIKEN Center for Biosystems Dynamics Research

human flip variant form of GluR2-LBD complexed with glutamate

human T686A and flip variant form of GluR2-LBD complexed with glutamate

human flip variant form of GluR2-LBD complexed with kainate

rat T686S and flop variant form of GluR2-LBD complexed with glutamate

Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax