IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ The Min Oscillator Uses MinD-Dependent Conformational Changes in MinE to Spatially Regulate Cytokinesis. The Min Oscillator Uses MinD-Dependent Conformational Changes in MinE to Spatially Regulate Cytokinesis. Cell (0092-8674) 2011 imex curation Park K.T., Wu W., Battaile K.P., Lovell S., Holyoak T., Lutkenhaus J. jlutkenh@kumc.edu 23-Sept-2011: Contacted by JYOTI. Only protein-protein interactions ecolx Escherichia coli adenylate cyclase adenylate cyclase complementation bacterial two-hybrid bacterial two-hybrid adenylate cyclase predetermined predetermined participant predetermined Park K.T., Wu W., Battaile K.P., Lovell S., Holyoak T., Lutkenhaus J. jlutkenh@kumc.edu Accepted 2011-AUG-30 by MGT 23-Sept-2011: Contacted by JYOTI. Cell (0092-8674) 2011 Only protein-protein interactions imex curation I was trying to capture those MIND mutants which did not interact with the wild-type MINE "MinDM193L, MinDD198R, MinDG224C, and MinDN222A" and then just described the MINE mutants which rescued the interation - I decided mutants which only interact with other mutants but not with wild-type were just too complicated for the system. The Min Oscillator Uses MinD-Dependent Conformational Changes in MinE to Spatially Regulate Cytokinesis. The Min Oscillator Uses MinD-Dependent Conformational Changes in MinE to Spatially Regulate Cytokinesis. Cell (0092-8674) 2011 imex curation Park K.T., Wu W., Battaile K.P., Lovell S., Holyoak T., Lutkenhaus J. jlutkenh@kumc.edu 23-Sept-2011: Contacted by JYOTI. Only protein-protein interactions in vitro In vitro atpase assay atpase assay predetermined predetermined participant predetermined Park K.T., Wu W., Battaile K.P., Lovell S., Holyoak T., Lutkenhaus J. Data is taken from a graph in Supp. Fig. 4A, from which the key is missing. It has therefore been interpreted using data in the text. jlutkenh@kumc.edu Accepted 2011-AUG-30 by MGT 23-Sept-2011: Contacted by JYOTI. Cell (0092-8674) 2011 Only protein-protein interactions imex curation I was trying to capture those MIND mutants which did not interact with the wild-type MINE "MinDM193L, MinDD198R, MinDG224C, and MinDN222A" and then just described the MINE mutants which rescued the interation - I decided mutants which only interact with other mutants but not with wild-type were just too complicated for the system. The Min Oscillator Uses MinD-Dependent Conformational Changes in MinE to Spatially Regulate Cytokinesis. The Min Oscillator Uses MinD-Dependent Conformational Changes in MinE to Spatially Regulate Cytokinesis. Cell (0092-8674) 2011 imex curation Park K.T., Wu W., Battaile K.P., Lovell S., Holyoak T., Lutkenhaus J. jlutkenh@kumc.edu 23-Sept-2011: Contacted by JYOTI. Only protein-protein interactions ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Park K.T., Wu W., Battaile K.P., Lovell S., Holyoak T., Lutkenhaus J. jlutkenh@kumc.edu Accepted 2011-AUG-30 by MGT 23-Sept-2011: Contacted by JYOTI. Cell (0092-8674) 2011 Only protein-protein interactions imex curation I was trying to capture those MIND mutants which did not interact with the wild-type MINE "MinDM193L, MinDD198R, MinDG224C, and MinDN222A" and then just described the MINE mutants which rescued the interation - I decided mutants which only interact with other mutants but not with wild-type were just too complicated for the system. The Min Oscillator Uses MinD-Dependent Conformational Changes in MinE to Spatially Regulate Cytokinesis. The Min Oscillator Uses MinD-Dependent Conformational Changes in MinE to Spatially Regulate Cytokinesis. Cell (0092-8674) 2011 imex curation Park K.T., Wu W., Battaile K.P., Lovell S., Holyoak T., Lutkenhaus J. jlutkenh@kumc.edu 23-Sept-2011: Contacted by JYOTI. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Park K.T., Wu W., Battaile K.P., Lovell S., Holyoak T., Lutkenhaus J. jlutkenh@kumc.edu Accepted 2011-AUG-30 by MGT 23-Sept-2011: Contacted by JYOTI. Cell (0092-8674) 2011 Only protein-protein interactions imex curation I was trying to capture those MIND mutants which did not interact with the wild-type MINE "MinDM193L, MinDD198R, MinDG224C, and MinDN222A" and then just described the MINE mutants which rescued the interation - I decided mutants which only interact with other mutants but not with wild-type were just too complicated for the system. The Min Oscillator Uses MinD-Dependent Conformational Changes in MinE to Spatially Regulate Cytokinesis. The Min Oscillator Uses MinD-Dependent Conformational Changes in MinE to Spatially Regulate Cytokinesis. Cell (0092-8674) 2011 imex curation Park K.T., Wu W., Battaile K.P., Lovell S., Holyoak T., Lutkenhaus J. jlutkenh@kumc.edu 23-Sept-2011: Contacted by JYOTI. Only protein-protein interactions in vitro In vitro pull down pull down weight by comassie molecular weight estimation by coomasie staining weight by comassie Park K.T., Wu W., Battaile K.P., Lovell S., Holyoak T., Lutkenhaus J. jlutkenh@kumc.edu Accepted 2011-AUG-30 by MGT 23-Sept-2011: Contacted by JYOTI. Cell (0092-8674) 2011 Only protein-protein interactions imex curation I was trying to capture those MIND mutants which did not interact with the wild-type MINE "MinDM193L, MinDD198R, MinDG224C, and MinDN222A" and then just described the MINE mutants which rescued the interation - I decided mutants which only interact with other mutants but not with wild-type were just too complicated for the system. The Min Oscillator Uses MinD-Dependent Conformational Changes in MinE to Spatially Regulate Cytokinesis. The Min Oscillator Uses MinD-Dependent Conformational Changes in MinE to Spatially Regulate Cytokinesis. Cell (0092-8674) 2011 imex curation Park K.T., Wu W., Battaile K.P., Lovell S., Holyoak T., Lutkenhaus J. jlutkenh@kumc.edu 23-Sept-2011: Contacted by JYOTI. Only protein-protein interactions in vitro In vitro crosslink cross-linking study crosslink predetermined predetermined participant predetermined Park K.T., Wu W., Battaile K.P., Lovell S., Holyoak T., Lutkenhaus J. Formaldehyde was used fro crosslinking. jlutkenh@kumc.edu Accepted 2011-AUG-30 by MGT 23-Sept-2011: Contacted by JYOTI. Cell (0092-8674) 2011 Only protein-protein interactions imex curation I was trying to capture those MIND mutants which did not interact with the wild-type MINE "MinDM193L, MinDD198R, MinDG224C, and MinDN222A" and then just described the MINE mutants which rescued the interation - I decided mutants which only interact with other mutants but not with wild-type were just too complicated for the system. mind_ecoli Septum site-determining protein MinD Cell division inhibitor MinD minD b1175 JW1164 protein protein ecoli Escherichia coli (strain K12) MARIIVVTSGKGGVGKTTSSAAIATGLAQKGKKTVVIDFDIGLRNLDLIMGCERRVVYDFVNVIQGDATLNQALIKDKRTENLYILPASQTRDKDALTREGVAKVLDDLKAMDFEFIVCDSPAGIETGALMALYFADEAIITTNPEVSSVRDSDRILGILASKSRRAENGEEPIKEHLLLTRYNPGRVSRGDMLSMEDVLEILRIKLVGVIPEDQSVLRASNQGEPVILDINADAGKAYADTVERLLGEERPFRFIEEEKKGFLKRLFGG DIP protein P0AEZ3 original sequence version: 74 DIP protein P0AEZ3 original sequence version: 39 0D2C4C0976B77D2C mine_ecoli Cell division topological specificity factor minE b1174 JW1163 protein protein ecoli Escherichia coli (strain K12) MALLDFFLSRKKNTANIAKERLQIIVAERRRSDAEPHYLPQLRKDILEVICKYVQIDPEMVTVQLEQKDGDISILELNVTLPEAEELK 04DDFB4EA24F96C1 atp ATP Adenosine 5'-triphosphate Adenosine triphosphate ADENOSINE-5'-TRIPHOSPHATE Adephos Adetol Adynol Atipi ATP Atriphos Cardenosine Fosfobion Glucobasin H4atp Myotriphos Triadenyl Triphosphaden adenosine 5'-(tetrahydrogen triphosphate) small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) mind-mine-2 1 7 unspecified role unspecified role neutral component neutral component P0AEZ3:p.Asp192Tyr mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain D Y Wed May 02 17:13:29 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp192tyr' Tue Jun 30 16:03:21 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp192Tyr' P0AEZ3:p.Met193Leu mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain M L Wed May 02 15:07:28 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'met193leu' Tue Jun 30 16:59:48 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Met193Leu' P0AEZ3:p.Gly224Cys mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain G C Wed May 02 16:52:11 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'gly224cys' Tue Jun 30 20:08:34 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Gly224Cys' P0AEZ3:p.Asp198Arg mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain D R Wed May 02 20:22:52 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp198arg' Tue Jun 30 17:17:56 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp198Arg' P0AEZ3:p.Asn222Ala mutation disrupting mutation disrupting interaction mutation disrupting mutation analysis mutation analysis certain certain sequence position certain certain certain sequence position certain N A Wed May 02 17:02:33 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asn222ala' Tue Jun 30 17:10:22 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asn222Ala' 8 unspecified role unspecified role neutral component neutral component physical association physical association Fig. 2A MinE Ile24Asn retained the ability to interact with wild-type MinD and also interacted with MinD Asp198Arg but not with the other MinD mutants. MinD Asp198Arg Interacted with MinE Ile24Ser/Glu66Gly and MinE Ile24Ser/Asp45Glu. MinD Gly224Cys interacted with MinE Ile24Thr/Asn16Lys. mine-3 3 8 unspecified role unspecified role neutral component neutral component P0A734:p.Ile24Asn mutation mutation certain certain sequence position certain certain certain sequence position certain I N Wed May 02 17:18:11 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile24asn' Wed May 02 20:02:29 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile24asn' Tue Jun 30 19:35:01 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile24Asn' region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction Supp. Fig. 2A mine-mine-3 6 8 unspecified role unspecified role neutral component neutral component region his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 8 unspecified role unspecified role neutral component neutral component region his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 25 28 direct interaction direct interaction Supp. Fig. 2B atp-mind 2 7 enzyme enzyme unspecified role unspecified role ecoli Escherichia coli (strain K12) 9 enzyme target enzyme target substrate substrate unspecified role unspecified role atpase reaction atpase reaction Supp. Fig. 4A atp-mind-1 2 9 enzyme target enzyme target substrate substrate unspecified role unspecified role 8 stimulator stimulator ancillary ancillary c-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range P0A734:p.Ile24Asn mutation mutation certain certain sequence position certain certain certain sequence position certain I N Wed May 02 14:38:45 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile24asn' Tue Jun 30 19:19:31 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile24Asn' region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 7 enzyme enzyme unspecified role unspecified role ecoli Escherichia coli (strain K12) atpase reaction atpase reaction Supp. Fig. 4A mine-mind 5 7 unspecified role unspecified role prey prey region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P0AEZ3:p.Asp40Ala mutation mutation certain certain sequence position certain certain certain sequence position certain D A Wed May 02 16:23:55 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp40ala' Tue Jun 30 19:54:33 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp40Ala' ecoli Escherichia coli (strain K12) 8 unspecified role unspecified role bait bait c-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range P0A734:p.Ile24Asn mutation mutation certain certain sequence position certain certain certain sequence position certain I N Wed May 02 15:04:28 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile24asn' Tue Jun 30 18:53:22 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile24Asn' region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 41 46 direct interaction direct interaction Supp. Fig. 4B Interaction is ATP dependent mind-mine-3 4 7 unspecified role unspecified role neutral component neutral component P0AEZ3:p.Asp40Ala mutation mutation certain certain sequence position certain certain certain sequence position certain D A Wed May 02 18:20:56 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp40ala' Tue Jun 30 16:16:46 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp40Ala' region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 8 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P0A734:p.Ile24Asn mutation mutation certain certain sequence position certain certain certain sequence position certain I N Wed May 02 20:08:16 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'ile24asn' Tue Jun 30 20:23:27 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Ile24Asn' c-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag c-term range C-terminal range c-term range c-term range C-terminal range c-term range ecoli Escherichia coli (strain K12) 52 50 direct interaction direct interaction Table 1 Interaction is ATP dependent 4.3A Rworking 29.4%, Rfree 31.1% mind-mine-4 4 8 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain chemical synthesis Chemical synthesis (Chemical synthesis) 7 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain P0AEZ3:p.Asp40Ala mutation mutation certain certain sequence position certain certain certain sequence position certain D A Wed May 02 18:44:43 BST 2018 This feature has been corrected as a result of our quality control procedures. The original label was 'asp40ala' Tue Jun 30 19:48:48 BST 2020 This feature has been corrected as a result of our quality control procedures. The original label was 'p.Asp40Ala' ecoli Escherichia coli (strain K12) 59 57 direct interaction direct interaction Table 1 Interaction is ATP dependent 2.6A Rworking 20.1%, Rfree 24.3% mine-mine-2 3 8 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain direct interaction direct interaction Supp. Fig. 2A mine-mine-4 3 8 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 8 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain 66 68 direct interaction direct interaction Supp. Fig. 2A