# Title of Dataset: Molecular models of the FtsQ-FtsL-FtsB-FtsW-FtsI complex (FtsQLBWI) in mono- and diprotomeric configurations --- Predicted protomeric and diprotomeric models of the FtsQLBWI complex of the bacterial divisome that explore potential conformational changes involved in the activation of the complex. ## Description of the Data and file structure There are five predicted models of the FtsQ/FtsL/FtsB/FtsW/FtsI (FtsQLBWI) complex of the in Protein Data Bank (pdb) format. The FtsQLBWI_protomer* models are comprised of one chain of each protein in the subcomplex, while the FtsQLBWI_diprotomer* models contain two copies of each chain (i.e. a dimer of pentamers). Within the dataset, the five proteins are given the same identification letter or letters across each file: FtsQ: Chain A + F FtsL: Chain B + G FtsB: Chain C + H FtsW: Chain D + I FtsI: Chain E + J The FtsQLBWI_diprotomer* models have been oriented such that the membrane-embedded portion of the complex is centered about the origin and parallel to the Z-axis, with the periplasmic domains of the complex oriented towards positive Z-values. The FtsQLBWI_protomer* models are superimposed with chains A-E of the diprotomeric complexes, such that when all of the models are opened in a PDB visualization program (such as PyMOL), the structures are aligned. When using the molecular visualization program PyMOL, the default orientation is that the Z-axis points out of the screen towards the user. To view the models from the side (that is, perpendicular to the membrane plane), it is useful to first rotate the X-axis by 270 degrees. This can be accomplished using the following console command: turn x, 270 ### Description of individual models: # FtsQLBWI_protomer_original.pdb The original protomeric (1 chain of each protein) FtsQLBWI complex, predicted by AlphaFold2 using ColabFold. The chain letters (A-E) have been rearranged from the original prediction for clarity and the model has been aligned with the diprotomeric models, as explained above. # FtsQLBWI_protomer_compact.pdb A protomeric FtsQLBWI complex in which the FtsW/FtsI components have been remodeled into a "compact" configuration based on the crystal structure of their paralog RodA/PBP2. A homology model of FtsWI was created based on this crystal structure (PDB 6PL5) using SWISS-MODEL. The FtsWI model was then aligned to the ColabFold FtsQLBWI protomer. After alignment, the FtsI of the ColabFold model was replaced with the FtsI of the homology model to create the final structure. # FtsQLBWI_diprotomer_clash.pdb This model is the result of making the FtsQLBWI_protomer_original model diprotomeric via a C2-symmetry operation, with FtsB and FtsL forming the core of the higher-order structure. The orientation of FtsQ relative to the rest of the complex leads to severe clashes in the model, clashing with FtsB, FtsL, and FtsI of the opposite protomer. Notably, this diprotomeric arrangement is largely free of clashes if FtsQ is removed. # FtsQLBWI_diprotomer_extended.pdb We next used a docking approach to determine whether rearranging FtsQ could lead to a clash-free FtsQLBWI diprotomer. The core of the FtsLBWI diprotomer (above) was docked to two bodies of the periplasmic domain of FtsQ in complex with the C-terminal tails of FtsL and FtsB using HADDOCK. Docking solutions were filtered for proper FtsB and FtsL connectivity via loop reconstruction in Rosetta and the transmembrane domain (TMD) of FtsQ was added via superpositioning of FtsQ+TMD models created using the Rosetta Membrane Protein Domain Assembly program. # FtsQLBWI_diprotomer_compact.pdb A diprotomeric arrangement of the FtsQLBWI complex in the "compact" orentation was created as described above, but led to clashes between FtsQ and FtsL/FtsB of the opposite protomer. However, because of the dramatically different orientation of FtsI, there were no FtsQ/FtsI clashes. Because there was more space to accomodate FtsQ, we identified a ColabFold conformation of the FtsQLB subcomplex that was almost completely compatible with the compact configuration of the FtsQLBWI diprotomer. The only clash was between the TMD of FtsQ with FtsW, which was resolved via superpositioning of FtsQ+TMD models created using the rosetta Membrane Protein Domain Assembly program. ## Sharing/access Information Was data derived from another source? Diprotomeric arrangements were created based on a predicted tetrameric arrangement of the FtsLB complex from Craven et al., JBC 2022 (doi: 10.1016/j.jbc.2021.101460)