DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structures of the Carbon-Phosphorus Lyase Complex Reveal the Binding Mode of the NBD-like PhnK. Structures of the Carbon-Phosphorus Lyase Complex Reveal the Binding Mode of the NBD-like PhnK. Structure (London, England : 1993) 2016 imex curation Yang K., Ren Z., Raushel FM., Zhang J. Only protein-protein interactions ecolx Escherichia coli 3d-em 3D electron microscopy 3D-EM electron tomog predetermined predetermined participant predetermined Yang K., Ren Z., Raushel FM., Zhang J. DIP original experiment: DIP-268481X Structure (London, England : 1993) 2016 IMEx Structures of the Carbon-Phosphorus Lyase Complex Reveal the Binding Mode of the NBD-like PhnK. Structures of the Carbon-Phosphorus Lyase Complex Reveal the Binding Mode of the NBD-like PhnK. Structures of the Carbon-Phosphorus Lyase Complex Reveal the Binding Mode of the NBD-like PhnK. Structure (London, England : 1993) 2016 imex curation Yang K., Ren Z., Raushel FM., Zhang J. Only protein-protein interactions ecolx Escherichia coli 3d-em 3D electron microscopy 3D-EM electron tomog predetermined predetermined participant predetermined Yang K., Ren Z., Raushel FM., Zhang J. DIP original experiment: DIP-268480X Structure (London, England : 1993) 2016 IMEx Structures of the Carbon-Phosphorus Lyase Complex Reveal the Binding Mode of the NBD-like PhnK. Structures of the Carbon-Phosphorus Lyase Complex Reveal the Binding Mode of the NBD-like PhnK. Structures of the Carbon-Phosphorus Lyase Complex Reveal the Binding Mode of the NBD-like PhnK. Structure (London, England : 1993) 2016 imex curation Yang K., Ren Z., Raushel FM., Zhang J. 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 Yang K., Ren Z., Raushel FM., Zhang J. DIP original experiment: DIP-268479X Structure (London, England : 1993) 2016 IMEx Structures of the Carbon-Phosphorus Lyase Complex Reveal the Binding Mode of the NBD-like PhnK. Structures of the Carbon-Phosphorus Lyase Complex Reveal the Binding Mode of the NBD-like PhnK. Structures of the Carbon-Phosphorus Lyase Complex Reveal the Binding Mode of the NBD-like PhnK. Structure (London, England : 1993) 2016 imex curation Yang K., Ren Z., Raushel FM., Zhang J. Only protein-protein interactions ecolx Escherichia coli pull down pull down predetermined predetermined participant predetermined Yang K., Ren Z., Raushel FM., Zhang J. DIP original experiment: DIP-268478X Structure (London, England : 1993) 2016 IMEx Structures of the Carbon-Phosphorus Lyase Complex Reveal the Binding Mode of the NBD-like PhnK. 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 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 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 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 phng-phnh-10 4 8 unspecified role unspecified role prey prey ecolx Escherichia coli 9 unspecified role unspecified role prey prey ecolx Escherichia coli 5 unspecified role unspecified role prey prey ecolx Escherichia coli 6 unspecified role unspecified role bait bait His-tag His-tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecolx Escherichia coli 7 unspecified role unspecified role prey prey ecolx Escherichia coli association association phng-phnh-11 1 9 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 7 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli physical association physical association phng-phnh-12 2 8 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 9 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 7 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli physical association physical association phng-phnh-13 3 8 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 9 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 7 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli physical association physical association