DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ fairman-2011-1 in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. DIP original experiment: DIP-218476X Nature structural & molecular biology 2011 IMEx Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. Only protein-protein interactions imex curation fairman-2011-2 ecolx Escherichia coli molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. DIP original experiment: DIP-218472X Nature structural & molecular biology 2011 IMEx Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. Only protein-protein interactions imex curation fairman-2011-3 in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. DIP original experiment: DIP-218479X Nature structural & molecular biology 2011 IMEx Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. Only protein-protein interactions imex curation fairman-2011-4 in vitro In vitro tem transmission electron microscopy tem predetermined predetermined participant predetermined Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. DIP original experiment: DIP-218481X Nature structural & molecular biology 2011 IMEx Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. Only protein-protein interactions imex curation fairman-2011-5 in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. DIP original experiment: DIP-218477X Nature structural & molecular biology 2011 IMEx Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. Only protein-protein interactions imex curation fairman-2011-6 ecolx Escherichia coli x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. DIP original experiment: DIP-218473X Nature structural & molecular biology 2011 IMEx Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. Only protein-protein interactions imex curation fairman-2011-7 in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. DIP original experiment: DIP-218474X Nature structural & molecular biology 2011 IMEx Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. Only protein-protein interactions imex curation fairman-2011-8 ecolx Escherichia coli pull down pull down predetermined predetermined participant predetermined Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. DIP original experiment: DIP-218480X Nature structural & molecular biology 2011 IMEx Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. Only protein-protein interactions imex curation fairman-2011-9 in vitro In vitro 3d-em 3D electron microscopy 3D-EM electron tomog predetermined predetermined participant predetermined Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. DIP original experiment: DIP-218478X Nature structural & molecular biology 2011 IMEx Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. Only protein-protein interactions imex curation fairman-2011-10 in vitro In vitro light scattering light scattering predetermined predetermined participant predetermined Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. DIP original experiment: DIP-218475X Nature structural & molecular biology 2011 IMEx Structural basis for allosteric regulation of human ribonucleotide reductase by nucleotide-induced oligomerization. Fairman JW., Wijerathna SR., Ahmad MF., Xu H., Nakano R., Jha S., Prendergast J., Welin RM., Flodin S., Roos A., Nordlund P., Li Z., Walz T., Dealwis CG. Only protein-protein interactions imex curation rir1_human Ribonucleoside-diphosphate reductase large subunit Ribonucleoside-diphosphate reductase subunit M1 Ribonucleotide reductase large subunit RRM1 RR1 protein protein human Homo sapiens Human MHVIKRDGRQERVMFDKITSRIQKLCYGLNMDFVDPAQITMKVIQGLYSGVTTVELDTLAAETAATLTTKHPDYAILAARIAVSNLHKETKKVFSDVMEDLYNYINPHNGKHSPMVAKSTLDIVLANKDRLNSAIIYDRDFSYNYFGFKTLERSYLLKINGKVAERPQHMLMRVSVGIHKEDIDAAIETYNLLSERWFTHASPTLFNAGTNRPQLSSCFLLSMKDDSIEGIYDTLKQCALISKSAGGIGVAVSCIRATGSYIAGTNGNSNGLVPMLRVYNNTARYVDQGGNKRPGAFAIYLEPWHLDIFEFLDLKKNTGKEEQRARDLFFALWIPDLFMKRVETNQDWSLMCPNECPGLDEVWGEEFEKLYASYEKQGRVRKVVKAQQLWYAIIESQTETGTPYMLYKDSCNRKSNQQNLGTIKCSNLCTEIVEYTSKDEVAVCNLASLALNMYVTSEHTYDFKKLAEVTKVVVRNLNKIIDINYYPVPEACLSNKRHRPIGIGVQGLADAFILMRYPFESAEAQLLNKQIFETIYYGALEASCDLAKEQGPYETYEGSPVSKGILQYDMWNVTPTDLWDWKVLKEKIAKYGIRNSLLIAPMPTASTAQILGNNESIEPYTSNIYTRRVLSGEFQIVNPHLLKDLTERGLWHEEMKNQIIACNGSIQSIPEIPDDLKQLYKTVWEISQKTVLKMAAERGAFIDQSQSLNIHIAEPNYGKLTSMHFYGWKQGLKTGMYYLRTRPAANPIQFTLNKEKLKDKEKVSKEEEEKERNTAAMVCSLENRDECLMCGS rir1_yeast Ribonucleoside-diphosphate reductase large chain 1 RNR1 RIR1 Ribonucleotide reductase R1 subunit 1 YER070W CRT7 SDS12 Ribonucleotide reductase large subunit 1 protein protein yeast Saccharomyces cerevisiae Baker's yeast MYVYKRDGRKEPVQFDKITARISRLCYGLDPKHIDAVKVTQRIISGVYEGVTTIELDNLAAETCAYMTTVHPDYATLAARIAISNLHKQTTKQFSKVVEDLYRYVNAATGKPAPMISDDVYNIVMENKDKLNSAIVYDRDFQYSYFGFKTLERSYLLRINGQVAERPQHLIMRVALGIHGRDIEAALETYNLMSLKYFTHASPTLFNAGTPKPQMSSCFLVAMKEDSIEGIYDTLKECALISKTAGGIGLHIHNIRSTGSYIAGTNGTSNGLIPMIRVFNNTARYVDQGGNKRPGAFALYLEPWHADIFDFIDIRKNHGKEEIRARDLFPALWIPDLFMKRVEENGTWTLFSPTSAPGLSDCYGDEFEALYTRYEKEGRGKTIKAQKLWYSILEAQTETGTPFVVYKDACNRKSNQKNLGVIKSSNLCCEIVEYSAPDETAVCNLASVALPAFIETSEDGKTSTYNFKKLHEIAKVVTRNLNRVIDRNYYPVEEARKSNMRHRPIALGVQGLADTFMLLRLPFDSEEARLLNIQIFETIYHASMEASCELAQKDGPYETFQGSPASQGILQFDMWDQKPYGMWDWDTLRKDIMKHGVRNSLTMAPMPTASTSQILGYNECFEPVTSNMYSRRVLSGEFQVVNPYLLRDLVDLGIWDEGMKQYLITQNGSIQGLPNVPQELKDLYKTVWEISQKTIINMAADRSVYIDQSHSLNLFLRAPTMGKLTSMHFYGWKKGLKTGMYYLRTQAASAAIQFTIDQKIADQATENVADISNLKRPSYMPSSASYAASDFVPAAVTANATIPSLDSSSEASREASPAPTGSHSLTKGMAELNVQESKVEVPEVPAPTKNEEKAAPIVDDEETEFDIYNSKVIACAIDNPEACEMCSG 56BE1B077916E419 rir4_yeast Ribonucleoside-diphosphate reductase small chain 2 RNR4 YGR180C CRT3 Ribonucleotide reductase small subunit 2 Ribonucleotide reductase R2 subunit 2 protein protein yeast Saccharomyces cerevisiae Baker's yeast MEAHNQFLKTFQKERHDMKEAEKDEILLMENSRRFVMFPIKYHEIWAAYKKVEASFWTAEEIELAKDTEDFQKLTDDQKTYIGNLLALSISSDNLVNKYLIENFSAQLQNPEGKSFYGFQIMMENIYSEVYSMMVDAFFKDPKNIPLFKEIANLPEVKHKAAFIERWISNDDSLYAERLVAFAAKEGIFQAGNYASMFWLTDKKIMPGLAMANRNICRDRGAYTDFSCLLFAHLRTKPNPKIIEKIITEAVEIEKEYYSNSLPVEKFGMDLKSIHTYIEFVADGLLQGFGNEKYYNAVNPFEFMEDVATAGKTTFFEKKVSDYQKASDMSKSATPSKEINFDDDF 712853F2D87D3972 rir2_yeast Ribonucleoside-diphosphate reductase small chain 1 RNR2 YJL026W J1271 CRT6 Ribonucleotide reductase small subunit 1 Ribonucleotide reductase R2 subunit 1 protein protein yeast Saccharomyces cerevisiae Baker's yeast MPKETPSKAAADALSDLEIKDSKSNLNKELETLREENRVKSDMLKEKLSKDAENHKAYLKSHQVHRHKLKEMEKEEPLLNEDKERTVLFPIKYHEIWQAYKRAEASFWTAEEIDLSKDIHDWNNRMNENERFFISRVLAFFAASDGIVNENLVENFSTEVQIPEAKSFYGFQIMIENIHSETYSLLIDTYIKDPKESEFLFNAIHTIPEIGEKAEWALRWIQDADALFGERLVAFASIEGVFFSGSFASIFWLKKRGMMPGLTFSNELICRDEGLHTDFACLLFAHLKNKPDPAIVEKIVTEAVEIEQRYFLDALPVALLGMNADLMNQYVEFVADRLLVAFGNKKYYKVENPFDFMENISLAGKTNFFEKRVSDYQKAGVMSKSTKQEAGAFTFNEDF DB98028408292042 rir2_human Ribonucleoside-diphosphate reductase subunit M2 RRM2 RR2 Ribonucleotide reductase small subunit Ribonucleotide reductase small chain protein protein human Homo sapiens Human MLSLRVPLAPITDPQQLQLSPLKGLSLVDKENTPPALSGTRVLASKTARRIFQEPTEPKTKAAAPGVEDEPLLRENPRRFVIFPIEYHDIWQMYKKAEASFWTAEEVDLSKDIQHWESLKPEERYFISHVLAFFAASDGIVNENLVERFSQEVQITEARCFYGFQIAMENIHSEMYSLLIDTYIKDPKEREFLFNAIETMPCVKKKADWALRWIGDKEATYGERVVAFAAVEGIFFSGSFASIFWLKKRGLMPGLTFSNELISRDEGLHCDFACLMFKHLVHKPSEERVREIIINAVRIEQEFLTEALPVKLIGMNCTLMKQYIEFVADRLMLELGFSKVFRVENPFDFMENISLEGKTNFFEKRVGEYQRMGVMSSPTENSFTLDADF rrm1-2 3222802 N/A 3222812 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction false false false scrr1-1 3222803 N/A 3222813 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction false false false scrr1-scrr2-1 3222804 N/A 3222814 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli N/A 3222815 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli N/A 3222813 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli physical association physical association false false false scrr1-scrr2-2 3222805 N/A 3222814 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli N/A 3222815 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli N/A 3222813 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli physical association physical association false false false rrm1-rrm2-2 3222806 N/A 3222816 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli N/A 3222812 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction false false false scrr1-2 3222807 N/A 3222813 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction false false false rrm1-3 3222808 N/A 3222812 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction false false false scrr2-scrr4-1 3222809 N/A 3222814 unspecified role unspecified role prey prey ecolx Escherichia coli N/A 3222815 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 false ecolx Escherichia coli physical association physical association false false false scrr1-scrr2-3 3222810 N/A 3222814 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli N/A 3222815 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli N/A 3222813 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli physical association physical association false false false rrm1-4 3222811 N/A 3222812 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction false false false