GPCR oligomerisation is known to play an important role in the receptor signalling. However, due to the technical challenges, the structural information of GPCR oligomerisation is still very limited, which hinders our understanding of GPCR signalling in a fuller picture. In this deposit, we provide the structural coordinates of various oligomeric assemblies of Adenosine A2a receptor that were sampled from unbiased MD simulations. For more information regarding the MD simulations and the findings on A2aR oligomerization, please refer to our paper on BioRxiv: https://www.biorxiv.org/content/10.1101/2020.06.24.168260v1 ** Simulation setup ** 9 copies of A2aR were randomly inserted into an in-vivo mimetic biomembrane to build the initial configuration of the simulations. 10 such systems were setup for A2aR in the inactive state and 10 for the active state. The systems were represented by MARTINI 2 coarse-grained model and simulated for 50 micro-seconds. Protein-protein associations were identified when any atoms from two protomers were getting closer than 0.75 nm. The oligomerisation process was monitored and the sampled oligomeric assemblies were stored. ** Coordinate file explained ** The coarse-grained oligomeric structures were converted back to atomistic model in CHARMM force field. Oligomeric assemblies of the same oligomeric state (OS) were clustered to identify the different arrangements. 100 oligomeric arrangements (or all of the sampled oligomers if the cluster contains less than 100 samples) were randomly taken from each cluster and stored as seperate models in a pdb coordinate file. The pdb coordinate files were named as {Conf. State}_OS{Oligomeric State}_cl{Cluster id}.pdb, and can be viewed by such visualization tools as PyMol, Chimera or JMol etc. A Excel file containing some statistics of the oligomeric assemblies were also provided.

{"references": ["Song et al (2020) GPCR Oligomerisation Modulation by Conformational State and Lipid Interactions Revealed by MD Simulations and Markov Models; bioRxiv 2020.06.24.168260; doi: https://doi.org/10.1101/2020.06.24.168260"]}