attachment site
A structural model of the Pom34-152 transmembrane attachment site dimer was computed by integrative modeling based on the cryo-EM density maps (EMD-41117) and the AlphaFold2 structure predcition of the monomers. A model of the dimer Pom34-152 transmembrane domains (TMDs) was computed by satisfying this input information to the best possible degree using IMP.
data
All data used for integrative modeling, including the cross-links, EM density map, and the AlphaFold2 models.scripts
PMI modeling script (mod_TMDs.py
) to model the symmetric Pom34-152 dimer.analysis
Scripts to analyze the simulationsresults
All the relevant results from integrative modeling, including the distance statistics for the cross-links and clustering of the results.SI_table
Scripts to generate a table summarizing the integrative modeling protocols.utils
Template and code to generate the Supporting information table summarizing the integrative modeling protocol.
Author (s): Ignacia Echeverria
License: CC BY-SA 4.0 This work is licensed under the Creative Commons Attribution-ShareAlike 4.0 International License.
Publications: Implications of a multiscale structure of the yeast Nuclear Pore Complex. Akey CA, Echeverria I, Ouch C, Nudelman I, Shi Y, Wang J, Weiss TM, Shi Y, Chait BT, Sali A,Fernandez-Martinez J, Rout MP. Molecular Cell. 2023