DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structural insights into the bacterial carbon-phosphorus lyase machinery. Structural insights into the bacterial carbon-phosphorus lyase machinery. Nature 2015 imex curation Seweryn P., Van LB., Kjeldgaard M., Russo CJ., Passmore LA., Hove-Jensen B., Jochimsen B., Brodersen DE. 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 Seweryn P., Van LB., Kjeldgaard M., Russo CJ., Passmore LA., Hove-Jensen B., Jochimsen B., Brodersen DE. DIP original experiment: DIP-267082X Nature 2015 IMEx Structural insights into the bacterial carbon-phosphorus lyase machinery. Structural insights into the bacterial carbon-phosphorus lyase machinery. Structural insights into the bacterial carbon-phosphorus lyase machinery. Nature 2015 imex curation Seweryn P., Van LB., Kjeldgaard M., Russo CJ., Passmore LA., Hove-Jensen B., Jochimsen B., Brodersen DE. Only protein-protein interactions ecolx Escherichia coli tem transmission electron microscopy tem predetermined predetermined participant predetermined Seweryn P., Van LB., Kjeldgaard M., Russo CJ., Passmore LA., Hove-Jensen B., Jochimsen B., Brodersen DE. DIP original experiment: DIP-267083X Nature 2015 IMEx Structural insights into the bacterial carbon-phosphorus lyase machinery. Structural insights into the bacterial carbon-phosphorus lyase machinery. Structural insights into the bacterial carbon-phosphorus lyase machinery. Nature 2015 imex curation Seweryn P., Van LB., Kjeldgaard M., Russo CJ., Passmore LA., Hove-Jensen B., Jochimsen B., Brodersen DE. 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 Seweryn P., Van LB., Kjeldgaard M., Russo CJ., Passmore LA., Hove-Jensen B., Jochimsen B., Brodersen DE. DIP original experiment: DIP-267080X Nature 2015 IMEx Structural insights into the bacterial carbon-phosphorus lyase machinery. Structural insights into the bacterial carbon-phosphorus lyase machinery. Structural insights into the bacterial carbon-phosphorus lyase machinery. Nature 2015 imex curation Seweryn P., Van LB., Kjeldgaard M., Russo CJ., Passmore LA., Hove-Jensen B., Jochimsen B., Brodersen DE. Only protein-protein interactions ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Seweryn P., Van LB., Kjeldgaard M., Russo CJ., Passmore LA., Hove-Jensen B., Jochimsen B., Brodersen DE. DIP original experiment: DIP-267081X Nature 2015 IMEx Structural insights into the bacterial carbon-phosphorus lyase machinery. phni_ecoli Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnI Ribose 1-methylphosphonate 5-triphosphate synthase nucleosidase subunit JW4060 b4099 phnI protein protein ecoli Escherichia coli (strain K12) MYVAVKGGEKAIDAAHALQESRRRGDTDLPELSVAQIEQQLNLAVDRVMTEGGIADRELAALALKQASGDNVEAIFLLRAYRTTLAKLAVSEPLDTTGMRLERRISAVYKDIPGGQLLGPTYDYTHRLLDFTLLANGEAPTLTTADSEQQPSPHVFSLLARQGLAKFEEDSGAQPDDITRTPPVYPCSRSSRLQQLMRGDEGYLLALAYSTQRGYGRNHPFAGEIRSGYIDVSIVPEELGFAVNVGELLMTECEMVNGFIDPPGEPPHFTRGYGLVFGMSERKAMAMALVDRALQAPEYGEHATGPAQDEEFVLAHADNVEAAGFVSHLKLPHYVDFQAELELLKRLQQEQNHG DIP protein P16687 original sequence version: 68 DIP protein P16687 original sequence version: 105 DIP protein P16687 original sequence version: 107 9E974F01B85CCE81 phng_ecoli Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnG JW4062 b4101 phnG protein protein ecoli Escherichia coli (strain K12) MHADTATRQHWMSVLAHSQPAELAARLNALNITADYEVIRAAETGLVQIQARMGGTGERFFAGDATLTRAAVRLTDGTLGYSWVQGRDKQHAERCALIDALMQQSRHFQNLSETLIAPLDADRMARIAARQAEVNASRVDFFTMVRGDNA DIP protein P16685 original sequence version: 66 DIP protein P16685 original sequence version: 105 DIP protein P16685 original sequence version: 107 818A95526FAD0817 phnj_ecoli Alpha-D-ribose 1-methylphosphonate 5-phosphate C-P lyase phnJ b4098 JW4059 protein protein ecoli Escherichia coli (strain K12) MANLSGYNFAYLDEQTKRMIRRAILKAVAIPGYQVPFGGREMPMPYGWGTGGIQLTASVIGESDVLKVIDQGADDTTNAVSIRNFFKRVTGVNTTERTDDATVIQTRHRIPETPLTEDQIIIFQVPIPEPLRFIEPRETETRTMHALEEYGVMQVKLYEDIARFGHIATTYAYPVKVNGRYVMDPSPIPKFDNPKMDMMPALQLFGAGREKRIYAVPPFTRVESLDFDDHPFTVQQWDEPCAICGSTHSYLDEVVLDDAGNRMFVCSDTDYCRQQSEAKNQ DIP protein P16688 original sequence version: 102 DIP protein P16688 original sequence version: 105 241F6AF140995468 phnk_ecoli Putative phosphonates utilization ATP-binding protein PhnK JW5727 b4097 phnK protein protein ecoli Escherichia coli (strain K12) MNQPLLSVNNLTHLYAPGKGFSDVSFDLWPGEVLGIVGESGSGKTTLLKSISARLTPQQGEIHYENRSLYAMSEADRRRLLRTEWGVVHQHPLDGLRRQVSAGGNIGERLMATGARHYGDIRATAQKWLEEVEIPANRIDDLPTTFSGGMQQRLQIARNLVTHPKLVFMDEPTGGLDVSVQARLLDLLRGLVVELNLAVVIVTHDLGVARLLADRLLVMKQGQVVESGLTDRVLDDPHHPYTQLLVSSVLQN DIP protein P16678 original sequence version: 127 DIP protein P16678 original sequence version: 129 3B8677F22C472A9F phnh_ecoli Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnH JW4061 b4100 phnH protein protein ecoli Escherichia coli (strain K12) MTLETAFMLPVQDAQHSFRRLLKAMSEPGVIVALHQLKRGWQPLNIATTSVLLTLADNDTPVWLSTPLNNDIVNQSLRFHTNAPLVSQPEQATFAVTDEAISSEQLNALSTGTAVAPEAGATLILQVASLSGGRMLRLTGAGIAEERMIAPQLPECILHELTERPHPFPLGIDLILTCGERLLAIPRTTHVEVC DIP protein P16686 original sequence version: 108 DIP protein P16686 original sequence version: 110 69F068F78EF44EF3 phng-phnh-6 3 7 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 5 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 9 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli physical association physical association phng-phnh-7 2 8 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 7 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 5 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 9 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli physical association physical association phng-phnh-8 1 8 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 7 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 5 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 9 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli physical association physical association phng-phnh-9 4 7 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 5 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 6 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 9 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli physical association physical association