Overexpression, purification and characterization of the acidic ribosomal P-proteins from Candida albicans

60S acidic ribosomal protein P1-B CaRP1B Q9HFQ6 Candida albicans 108 MSTEASVSYAALILADAEQEITSEKLLAITKAAGANVDQVWADVFAKAVEGKNLKELLFSFAAAAPASGAAAGSASGAAAGGEAAAEEAAEEEAAEESDDDMGFGLFD Disordered 1 108 MSTEASVSYAALILADAEQEITSEKLLAITKAAGANVDQVWADVFAKAVEGKNLKELLFSFAAAAPASGAAAGSASGAAAGGEAAAEEAAEEEAAEESDDDMGFGLFD Native Relationship to function unknown Molecular assembly Protein-protein binding Paper 15182941 Abramczyk D, Tchorzewski M, Krokowski D, Boguszewska A, Grankowski N Overexpression, purification and characterization of the acidic ribosomal P-proteins from Candida albicans 2004 Biochim Biophys Acta 1672 3 214-23 60S acidic ribosomal protein P2-beta L12EIA L45 YL44C YPA1 P02400 133071 A35109 Saccharomyces cerevisiae (Baker's yeast) 110 MKYLAAYLLLVQGGNAAPSAADIKAVVESVGAEVDEARINELLSSLEGKGSLEEIIAEGQKKFATVPTGGASSAAAGAAGAAAGGDAAEEEKEEEAKEESDDDMGFGLFD Disordered - Molten Globule 1 110 MKYLAAYLLLVQGGNAAPSAADIKAVVESVGAEVDEARINELLSSLEGKGSLEEIIAEGQKKFATVPTGGASSAAAGAAGAAAGGDAAEEEKEEEAKEESDDDMGFGLFD Native Function arises via a molten globule to order transition Molecular recognition effectors Protein-protein binding Far-UV circular dichroism (CD) Nuclear magnetic resonance (NMR) Analytical ultracentrifugation Hydrogen-deuterium Exchange Thermal stability Paper 9236009 Zurdo J, Sanz JM, Gonzalez C, Rico M, Ballesta JP The exchangeable yeast ribosomal acidic protein YP2beta shows characteristics of a partly folded state under physiological conditions 1997 Biochemistry 36 31 9625-35 10913306 Zurdo J, Gonzalez C, Sanz JM, Rico M, Remacha M, Ballesta JP Structural differences between Saccharomyces cerevisiae ribosomal stalk proteins P1 and P2 support their functional diversity 2000 Biochemistry 39 30 8935-43 Adenovirus ssDNA binding protein Early E2A DNA-binding protein P03265 P03265 118736 W7AD25 Human adenovirus type 5 529 MASREEEQRETTPERGRGAARRPPTMEDVSSPSPSPPPPRAPPKKRMRRRIESEDEEDSSQDALVPRTPSPRPSTSAADLAIAPKKKKKRPSPKPERPPSPEVIVDSEEEREDVALQMVGFSNPPVLIKHGKGGKRTVRRLNEDDPVARGMRTQEEEEEPSEAESEITVMNPLSVPIVSAWEKGMEAARALMDKYHVDNDLKANFKLLPDQVEALAAVCKTWLNEEHRGLQLTFTSNKTFVTMMGRFLQAYLQSFAEVTYKHHEPTGCALWLHRCAEIEGELKCLHGSIMINKEHVIEMDVTSENGQRALKEQSSKAKIVKNRWGRNVVQISNTDARCCVHDAACPANQFSGKSCGMFFSEGAKAQVAFKQIKAFMQALYPNAQTGHGHLLMPLRCECNSKPGHAPFLGRQLPKLTPFALSNAEDLDADLISDKSVLASVHHPALIVFQCCNPVYRNSRAQGGGPNCDFKISAPDLLNALVMVRSLWSENFTELPRMVVPEFKWSTKHQYRNVSLPVAHSDARQNPFDF Disordered - Extended Flexible Loop 297 331 IEMDVTSENGQRALKEQSSKAKIVKNRWGRNVVQI Native 1ADTA 1ADVA 1ADVB 1ANVA Function arises via a disorder to order transition Molecular recognition effectors DNA unwinding Protein-DNA binding X-ray crystallography 7.2 ethanol 5 NaCl 1.6 phosphate buffer 100 protein 0.5 Paper 8039495 Tucker, P., Tsernoglou, D., Tucker, A., Coenjaerts, F., Leenders, H., Vliet, P. Crystal structure of the adenovirus DNA binding protein reveals a hook-on model for cooperative DNA binding. 1994 13 13 2994-3002 9545375 Dekker, J. Kanellopoulos, P. N. van Oosterhout, J. A. Stier, G. Tucker, P. A. van der Vliet, P. C. ATP-independent DNA unwinding by the adenovirus single-stranded DNA binding protein requires a flexible DNA binding loop 1998 Journal of Molecular Biology 277 4 825-838 4040872 Tsernoglou D, Tsugita A, Tucker AD, van der Vliet PC Characterization of the chymotryptic core of the adenovirus DNA-binding protein 1985 FEBS Lett 188 2 248-52 This region is known as the flexible loop. It goes from disordered to ordered upon binding to DNA, helps to stabilize the binding complex and plays an important role in DNA replication. Disordered - Extended 401 406 KPGHAP Native 1ADTA 1ADVA 1ADVB 1ANVA Relationship to function unknown Unknown Unknown X-ray crystallography 7.2 ethanol 5 NaCl 1.6 phosphate buffer 100 protein 0.5 Paper 8039495 Tucker, P., Tsernoglou, D., Tucker, A., Coenjaerts, F., Leenders, H., Vliet, P. Crystal structure of the adenovirus DNA binding protein reveals a hook-on model for cooperative DNA binding. 1994 13 13 2994-3002 9545375 Dekker, J. Kanellopoulos, P. N. van Oosterhout, J. A. Stier, G. Tucker, P. A. van der Vliet, P. C. ATP-independent DNA unwinding by the adenovirus single-stranded DNA binding protein requires a flexible DNA binding loop 1998 Journal of Molecular Biology 277 4 825-838 4040872 Tsernoglou D, Tsugita A, Tucker AD, van der Vliet PC Characterization of the chymotryptic core of the adenovirus DNA-binding protein 1985 FEBS Lett 188 2 248-52 This region is part of the C-terminal portion of the protein which is important in chain formation and DNA replication. Disordered - Extended 453 464 PVYRNSRAQGGG Native 1ADTA 1ADVA 1ADVB 1ANVA Relationship to function unknown Unknown Unknown X-ray crystallography 7.2 ethanol 5 NaCl 1.6 phosphate buffer 100 protein 0.5 Paper 8039495 Tucker, P., Tsernoglou, D., Tucker, A., Coenjaerts, F., Leenders, H., Vliet, P. Crystal structure of the adenovirus DNA binding protein reveals a hook-on model for cooperative DNA binding. 1994 13 13 2994-3002 9545375 Dekker, J. Kanellopoulos, P. N. van Oosterhout, J. A. Stier, G. Tucker, P. A. van der Vliet, P. C. ATP-independent DNA unwinding by the adenovirus single-stranded DNA binding protein requires a flexible DNA binding loop 1998 Journal of Molecular Biology 277 4 825-838 4040872 Tsernoglou D, Tsugita A, Tucker AD, van der Vliet PC Characterization of the chymotryptic core of the adenovirus DNA-binding protein 1985 FEBS Lett 188 2 248-52 This region is part of the C-terminal portion of the protein which is important for chain formation and DNA replication. Ordered 332 400 SNTDARCCVHDAACPANQFSGKSCGMFFSEGAKAQVAFKQIKAFMQALYPNAQTGHGHLLMPLRCECNS 1ADTA 1ADVA 1ADVB 1ANVA Paper 9545375 Dekker J, Kanellopoulos PN, van Oosterhout JA, Stier G, Tucker PA, van der Vliet PC ATP-independent DNA unwinding by the adenovirus single-stranded DNA binding protein requires a flexible DNA binding loop 1998 J Mol Biol 277 4 825-38 8039495 Tucker PA, Tsernoglou D, Tucker AD, Coenjaerts FE, Leenders H, van der Vliet PC Crystal structure of the adenovirus DNA binding protein reveals a hook-on model for cooperative DNA binding 1994 Embo J 13 13 2994-3002 4040872 Tsernoglou D, Tsugita A, Tucker AD, van der Vliet PC Characterization of the chymotryptic core of the adenovirus DNA-binding protein 1985 FEBS Lett 188 2 248-52 Ordered 407 452 FLGRQLPKLTPFALSNAEDLDADLISDKSVLASVHHPALIVFQCCN 1ADTA 1ADVA 1ADVB 1ANVA Paper 9545375 Dekker J, Kanellopoulos PN, van Oosterhout JA, Stier G, Tucker PA, van der Vliet PC ATP-independent DNA unwinding by the adenovirus single-stranded DNA binding protein requires a flexible DNA binding loop 1998 J Mol Biol 277 4 825-38 8039495 Tucker PA, Tsernoglou D, Tucker AD, Coenjaerts FE, Leenders H, van der Vliet PC Crystal structure of the adenovirus DNA binding protein reveals a hook-on model for cooperative DNA binding 1994 Embo J 13 13 2994-3002 4040872 Tsernoglou D, Tsugita A, Tucker AD, van der Vliet PC Characterization of the chymotryptic core of the adenovirus DNA-binding protein 1985 FEBS Lett 188 2 248-52 Ordered 465 529 PNCDFKISAPDLLNALVMVRSLWSENFTELPRMVVPEFKWSTKHQYRNVSLPVAHSDARQNPFDF 1ADTA 1ADVA 1ADVB 1ANVA Paper 9545375 Dekker J, Kanellopoulos PN, van Oosterhout JA, Stier G, Tucker PA, van der Vliet PC ATP-independent DNA unwinding by the adenovirus single-stranded DNA binding protein requires a flexible DNA binding loop 1998 J Mol Biol 277 4 825-38 8039495 Tucker PA, Tsernoglou D, Tucker AD, Coenjaerts FE, Leenders H, van der Vliet PC Crystal structure of the adenovirus DNA binding protein reveals a hook-on model for cooperative DNA binding 1994 Embo J 13 13 2994-3002 4040872 Tsernoglou D, Tsugita A, Tucker AD, van der Vliet PC Characterization of the chymotryptic core of the adenovirus DNA-binding protein 1985 FEBS Lett 188 2 248-52 Antibacterial protein FALL-39 precursor Antibacterial protein LL-37 Antimicrobial protein CAP-18 CAP18 precursor FALL-39 peptide antibiotic hCAP-18 LL-37 P49913 P49913 1706745 I38932 Homo sapiens (Human) 170 MKTQRNGHSLGRWSLVLLLLGLVMPLAIIAQVLSYKEAVLRAIDGINQRSSDANLYRLLDLDPRPTMDGDPDTPKPVSFTVKETVCPRTTQQSPEDCDFKKDGLVKRCMGTVTLNQARGSFDISCDKDNKRFALLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES Disordered - Extended 134 170 LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES Engineered Function arises via a disorder to order transition Unknown Unknown Near-UV circular dichroism (CD) spectroscopy 298 6 magnesium sulfate salt 84 sodium chloride salt 160 Paper 9452503 Johansson, J. Gudmundsson, G. H. Rottenberg, M. E. Berndt, K. D. Agerberth, B. Conformation-dependent antibacterial activity of the naturally occurring human peptide LL-37. 1998 J Biol Chem 273 6 3718-3724 The disordered region became significantly more disordered below pH 5. At pH of 2, it was completely disordered. At pH of 13, it adopted a helical structure. Antitermination protein N Antitermination protein N of bacteriophage lambda Nucleocapsid protein PN Regulatory protein N P03045 P03045 132276 P03045 Bacteriophage lambda 107 MDAQTRRRERRAEKQAQWKAANPLLVGVSAKPVNLPILSLNRKPKSRVESALNPIDLTVLAEYHKQIESNLQRIERKNQRTWYSKPGERGITCSGRQKIKGKSIPLI Disordered 1 107 MDAQTRRRERRAEKQAQWKAANPLLVGVSAKPVNLPILSLNRKPKSRVESALNPIDLTVLAEYHKQIESNLQRIERKNQRTWYSKPGERGITCSGRQKIKGKSIPLI Paper 9659923 Mogridge J, Legault P, Li J, Van Oene MD, Kay LE, Greenblatt J Independent ligand-induced folding of the RNA-binding domain and two functionally distinct antitermination regions in the phage lambda N protein 1998 Mol Cell 1 2 265-75 Cytochrome c Apocytochrome c P00004 117995 A00005 Equus caballus (Horse) 104 GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFTYTDANKNKGITWKEETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE Disordered 1 104 GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFTYTDANKNKGITWKEETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE Paper 4344990 Stellwagen E, Rysavy R, Babul G The conformation of horse heart apocytochrome c 1972 J Biol Chem 247 24 8074-7 DNA-(apurinic or apyrimidinic site) lyase APE nuclease APEX nuclease Apurinic/apyrimidinic endonuclease HAP1 Major apurinic/apyrimidinic endonuclease Ref-1 P27695 Hs.73722 P27695 18375505 S23550 Homo sapiens (Human) 318 MPKRGKKGAVAEDGDELRTEPEAKKSKTAAKKNDKEAAGEGPALYEDPPDQKTSPSGKPATLKICSWNVDGLRAWIKKKGLDWVKEEAPDILCLQETKCSENKLPAELQELPGLSHQYWSAPSDKEGYSGVGLLSRQCPLKVSYGIGDEEHDQEGRVIVAEFDSFVLVTAYVPNAGRGLVRLEYRQRWDEAFRKFLKGLASRKPLVLCGDLNVAHEEIDLRNPKGNKKNAGFTPQERQGFGELLQAVPLADSFRHLYPNTPYAYTFWTYMMNARSKNVGWRLDYFLLSHSLLPALCDSKIRSKALGSDHCPITLYLAL Disordered - Extended 1 43 MPKRGKKGAVAEDGDELRTEPEAKKSKTAAKKNDKEAAGEGPA Complex Native 1HD7A Relationship to function unknown Unknown Disordered region is not essential for protein function Unknown X-ray crystallography 4.6 lead (II) acetate 1 polyethylene glycol 4000 25% (w/v) sodium acetate pH 4.6 0.1 Paper 11286553 Beernink PT, Segelke BW, Hadi MZ, Erzberger JP, Wilson DM 3rd, Rupp B Two divalent metal ions in the active site of a new crystal form of human apurinic/apyrimidinic endonuclease, Ape1: implications for the catalytic mechanism 2001 J Mol Biol 307 4 1023-34 This structure is refered to as 'form II' in Beernink (2001). Disordered - Extended 36 43 EAAGEGPA Complex Engineered Fragment 1BIX_ Relationship to function unknown Unknown Disordered region is not essential for protein function Unknown X-ray crystallography 6.2 1,4- Dioxane 5 percent w/v calcium acetate 292 Kelvin 200 crystals flash cooled 110 Kelvin HEPES pH 7.4 10 MES pH 6.2 100 PEG 8000 16 to 20 percent w/v samarium acetate 7.5-30 mM well solution 3 Paper 9351835 Gorman MA, Morera S, Rothwell DG, de La Fortelle E, Mol CD, Tainer JA, Hickson ID, Freemont PS The crystal structure of the human DNA repair endonuclease HAP1 suggests the recognition of extra-helical deoxyribose at DNA abasic sites 1997 Embo J 16 21 6548-58 This structure is refered to as 'form I' in Beernink (2001). The experimental sequence did not contain the N-terminal residues 1-35. Disordered - Extended 102 112 NKLPAELQELP Complex Native 1HD7A Relationship to function unknown Unknown Unknown X-ray crystallography 4.6 lead (II) acetate 1 polyethylene glycol 4000 25% (w/v) sodium acetate pH 4.6 0.1 Paper 11286553 Beernink PT, Segelke BW, Hadi MZ, Erzberger JP, Wilson DM 3rd, Rupp B Two divalent metal ions in the active site of a new crystal form of human apurinic/apyrimidinic endonuclease, Ape1: implications for the catalytic mechanism 2001 J Mol Biol 307 4 1023-34 This structure is refered to as 'form II' in Beernink (2001). Disordered - Extended 123 127 SDKEG Complex Native 1HD7A Relationship to function unknown Unknown Unknown X-ray crystallography 4.6 lead (II) acetate 1 polyethylene glycol 4000 25% (w/v) sodium acetate pH 4.6 0.1 Paper 11286553 Beernink PT, Segelke BW, Hadi MZ, Erzberger JP, Wilson DM 3rd, Rupp B Two divalent metal ions in the active site of a new crystal form of human apurinic/apyrimidinic endonuclease, Ape1: implications for the catalytic mechanism 2001 J Mol Biol 307 4 1023-34 This structure is refered to as 'form II' in Beernink (2001). Disordered 100 104 SENKL Complex Engineered Relationship to function unknown Unknown Unknown X-ray crystallography 6.2 1,4- Dioxane 5 percent w/v calcium acetate 292 Kelvin 200 crystals flash cooled 110 Kelvin HEPES pH 7.4 10 MES pH 6.2 100 PEG 8000 16 to 20 percent w/v samarium acetate 7.5-30 mM well solution 3 Paper 11286553 Beernink PT, Segelke BW, Hadi MZ, Erzberger JP, Wilson DM 3rd, Rupp B Two divalent metal ions in the active site of a new crystal form of human apurinic/apyrimidinic endonuclease, Ape1: implications for the catalytic mechanism 2001 J Mol Biol 307 4 1023-34 This structure is refered to as 'form I' in Beernink (2001). The experimental sequence did not contain the N-terminal residues 1-35. Disordered - Extended 1 42 MPKRGKKGAVAEDGDELRTEPEAKKSKTAAKKNDKEAAGEGP Complex Native 1E9NA 1E9NB Relationship to function unknown Unknown Disordered region is not essential for protein function Unknown X-ray crystallography 7.5 HECAMEG 19.5 lead (II) acetate 1 polyethylene glycol 4000 25% (w/v) sodium acetate 0.2 Tris-HCl pH 7.5 0.1 Paper 9351835 Gorman MA, Morera S, Rothwell DG, de La Fortelle E, Mol CD, Tainer JA, Hickson ID, Freemont PS The crystal structure of the human DNA repair endonuclease HAP1 suggests the recognition of extra-helical deoxyribose at DNA abasic sites 1997 Embo J 16 21 6548-58 This region is not essential for function (Gorman 1997). This structure is refered to as 'form III' in Beernink (2001) For forms I, II and III of this protein referenced in Beernick (2001) , there is relatively high thermal motion in the areas of residues 100-110, 145, 200 and 270. These areas also show large root-mean-square fluctuations. POU domain class 2, associating factor 1 B-cell-specific coactivator BOB.1/OBF.1 B cell-specific transcription co-activator BOB-1 OCA-B OCT binding factor 1 Q64693 1150493 Mus musculus (Mouse) 256 MLWQKSTAPEQAPAPPRPYQGVRVKEPVKELLRRKRGHTSVGAAGPPTAGVLPHQPLATYSTVGPSCLDMEVSASTVTEEGTLCAGWLSQPAPATLHALAPWTPYTEYVSHEAVSCPYSTDMYVQPVCPSYTVVGPSSVLTYASPPLITNVTPRSTATPAVGPQLEGPEHQAPLTYFPWPQPLSTLPTSSLQYQPPAPTLSGPQFVQLPISIPEPVLQDMDDPRRAISSLTIDKLLLEEEESNTYELNHTLSVEGF Disordered 1 256 MLWQKSTAPEQAPAPPRPYQGVRVKEPVKELLRRKRGHTSVGAAGPPTAGVLPHQPLATYSTVGPSCLDMEVSASTVTEEGTLCAGWLSQPAPATLHALAPWTPYTEYVSHEAVSCPYSTDMYVQPVCPSYTVVGPSSVLTYASPPLITNVTPRSTATPAVGPQLEGPEHQAPLTYFPWPQPLSTLPTSSLQYQPPAPTLSGPQFVQLPISIPEPVLQDMDDPRRAISSLTIDKLLLEEEESNTYELNHTLSVEGF Paper 10329190 Chang JF, Phillips K, Lundback T, Gstaiger M, Ladbury JE, Luisi B Oct-1 POU and octamer DNA co-operate to recognise the Bob-1 transcription co-activator via induced folding 1999 J Mol Biol 288 5 941-52 Transcription initiation factor IIA small chain TFIIA 13.5 kDa subunit TOA2 P32774 418109 Saccharomyces cerevisiae (Baker's yeast) 122 MAVPGYYELYRRSTIGNSLVDALDTLISDGRIEASLAMRVLETFDKVVAETLKDNTQSKLTVKGNLDTYGFCDDVWTFIVKNCQVTVEDSHRDASQNGSGDSQSVISVDKLRIVACNSKKSE Disordered 89 103 DSHRDASQNGSGDSQ Complex Molecular assembly Protein-protein binding Transactivation (transcriptional activation) X-ray crystallography 103 Paper 8610010 Tan S, Hunziker Y, Sargent DF, Richmond TJ Crystal structure of a yeast TFIIA/TBP/DNA complex 1996 Nature 381 6578 127-51 Monoamine-sulfating phenol sulfotransferase Catecholamine sulfotransferase EC 2.8.2.1 HAST3 M-PST Placental estrogen sulfotransferase Sulfotransferase, monoamine-preferring Thermolabile phenol sulfotransferase TL-PST P50224 Hs.458369 P50224 10835035 A55451 Homo sapiens (Human) 295 MELIQDTSRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLINTYPKSGTTWVSQILDMIYQGGDLEKCNRAPIYVRVPFLEVNDPGEPSGLETLKDTPPPRLIKSHLPLALLPQTLLDQKVKVVYVARNPKDVAVSYYHFHRMEKAHPEPGTWDSFLEKFMAGEVSYGSWYQHVQEWWELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETMDFMVQHTSFKEMKKNPMTNYTTVPQELMDHSISPFMRKGMAGDWKTTFTVAQNERFDADYAEKMAGCSLSFRSEL Disordered - Extended 216 261 PEETMDFMVQHTSFKEMKKNPMTNYTTVPQELMDHSISPFMRKGMA Fragment 1CJMA Function arises via a disorder to order transition Metal sponge Substrate/ligand binding X-ray crystallography 293 lithium sulfate 0.5 PAP at 277 K pre-incubation for 1-2 hours polyethylene glycol 8000 5-7% (w/v) Paper 10543947 Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL Crystal structure of human catecholamine sulfotransferase 1999 J Mol Biol 293 3 521-530 Disordered 1 7 MELIQDT Fragment 1CJMA Function arises via a disorder to order transition Unknown Substrate/ligand binding X-ray crystallography 293 lithium sulfate 0.5 PAP at 277 K pre-incubation for 1-2 hours polyethylene glycol 8000 5-7% (w/v) Paper 10543947 Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL Crystal structure of human catecholamine sulfotransferase 1999 J Mol Biol 293 3 521-530 Disordered 64 77 GGDLEKCNRAPIYV Fragment 1CJMA Function arises via a disorder to order transition Unknown Substrate/ligand binding X-ray crystallography 293 lithium sulfate 0.5 PAP at 277 K pre-incubation for 1-2 hours polyethylene glycol 8000 5-7% (w/v) Paper 10543947 Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL Crystal structure of human catecholamine sulfotransferase 1999 J Mol Biol 293 3 521-530 Disordered 91 93 SGL Fragment 1CJMA Function arises via a disorder to order transition Unknown Substrate/ligand binding X-ray crystallography 293 lithium sulfate 0.5 PAP at 277 K pre-incubation for 1-2 hours polyethylene glycol 8000 5-7% (w/v) Paper 10543947 Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL Crystal structure of human catecholamine sulfotransferase 1999 J Mol Biol 293 3 521-530 Disordered 294 295 EL Fragment 1CJMA Function arises via a disorder to order transition Unknown Substrate/ligand binding X-ray crystallography 293 lithium sulfate 0.5 PAP at 277 K pre-incubation for 1-2 hours polyethylene glycol 8000 5-7% (w/v) Paper 10543947 Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL Crystal structure of human catecholamine sulfotransferase 1999 J Mol Biol 293 3 521-530 Disordered 216 224 PEETMDFMV Fragment 1CJMA Function arises via a disorder to order transition Unknown Substrate/ligand binding X-ray crystallography 293 lithium sulfate 0.5 PAP at 277 K pre-incubation for 1-2 hours polyethylene glycol 8000 5-7% (w/v) Paper 10543947 Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL Crystal structure of human catecholamine sulfotransferase 1999 J Mol Biol 293 3 521-530 Ordered 8 63 SRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLINTYPKSGTTWVSQILDMIYQ 1CJMA Paper 10543947 Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL Crystal structure of human catecholamine sulfotransferase 1999 J Mol Biol 293 3 521-530 Ordered 78 90 RVPFLEVNDPGEP 1CJMA Paper 10543947 Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL Crystal structure of human catecholamine sulfotransferase 1999 J Mol Biol 293 3 521-530 Ordered 94 215 ETLKDTPPPRLIKSHLPLALLPQTLLDQKVKVVYVARNPKDVAVSYYHFHRMEKAHPEPGTWDSFLEKFMAGEVSYGSWYQHVQEWWELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSL 1CJMA Paper 10543947 Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL Crystal structure of human catecholamine sulfotransferase 1999 J Mol Biol 293 3 521-530 Ordered 262 293 GDWKTTFTVAQNERFDADYAEKMAGCSLSFRS 1CJMA Paper 10543947 Bidwell LM, McManus ME, Gaedigk A, Kakuta Y, Negishi M, Pedersen L, Martin JL Crystal structure of human catecholamine sulfotransferase 1999 J Mol Biol 293 3 521-530 Cystic fibrosis transmembrane conductance regulator cAMP-dependent chloride channel CFTR Cystic fibrosis transmembrane conductance regulator, ATP-binding cassette P13569 1705762 DVHUCF Homo sapiens (Human) 1480 MQRSPLEKASVVSKLFFSWTRPILRKGYRQRLELSDIYQIPSVDSADNLSEKLEREWDRELASKKNPKLINALRRCFFWRFMFYGIFLYLGEVTKAVQPLLLGRIIASYDPDNKEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQASAFCGLGFLIVLALFQAGLGRMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYVRYFNSSAFFFSGFFVVFLSVLPYALIKGIILRKIFTTISFCIVLRMAVTRQFPWAVQTWYDSLGAINKIQDFLQKQEYKTLEYNLTTTEVVMENVTAFWEEGFGELFEKAKQNNNNRKTSNGDDSLFFSNFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQNLQPDFSSKLMGCDSFDQFSAERRNSILTETLHRFSLEGDAPVSWTETKKQSFKQTGEFGEKRKNSILNPINSIRKFSIVQKTPLQMNGIEEDSDEPLERRLSLVPDSEQGEAILPRISVISTGPTLQARRRQSVLNLMTHSVNQGQNIHRKTTASTRKVSLAPQANLTELDIYSRRLSQETGLEISEEINEEDLKECFFDDMESIPAVTTWNTYLRYITVHKSLIFVLIWCLVIFLAEVAASLVVLWLLGNTPLQDKGNSTHSRNNSYAVIITSTSSYYVFYIYVGVADTLLAMGFFRGLPLVHTLITVSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYIFVATVPVIVAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFFIAVTFISILTTGEGEGRVGIILTLAMNIMSTLQWAVNSSIDVDSLMRSVSRVFKFIDMPTEGKPTKSTKPYKNGQLSKVMIIENSHVKKDDIWPSGGQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQAISPSDRVKLFPHRNSSKCKSKPQIAALKEETEEEVQDTRL Disordered 708 831 IRKFSIVQKTPLQMNGIEEDSDEPLERRLSLVPDSEQGEAILPRISVISTGPTLQARRRQSVLNLMTHSVNQGQNIHRKTTASTRKVSLAPQANLTELDIYSRRLSQETGLEISEEINEEDLKE Paper Ostedgaard Lynda S, Baldursson Olafur, Vermeer Daniel W, Welsh Michael J, Robertson Andrew W A functional R domain from cystic fibrosis transmembrane conductance regulator is predominantly unstructured in solution 2000 PNAS 97 10 5657-5662 The sequence contains a mismatch at amino acid 470 when compared to PIR and SwissProt. Choriogonadotropin beta chain [Precursor] CG-beta Chorionic gonadotropin beta subunit Hcg Human chorionic gonadotropin P01233 116184 KTHUB Homo sapiens (Human) 145 SKEPLRPRCRPINATLAVEKEGCPVCITVNTTICAGYCPTMTRVLQGVLPALPQVVCNYRDVRFESIRLPGCPRGVNPVVSYAVALSCQCALCRRSTTDCGGPKDHPLTCDDPRFQDSSSSKAPPPSLPSPSRLPGPSDTPILPQ Disordered 112 145 DPRFQDSSSSKAPPPSLPSPSRLPGPSDTPILPQ Paper 8202136 Lapthorn AJ, Harris DC, Littlejohn A, Lustbader JW, Canfield RE, Machin KJ, Morgan FJ, Isaacs NW Crystal structure of human chorionic gonadotropin 1994 Nature 369 6480 455-61 SwissProt and NCBI have a sequence of 165 amino acids. This includes a 20 amino acid signal region on the N-terminal. Clusterin [Precursor] DAG Dimeric acid glycoprotein SGP-2 Sulfated glycoprotein 2 Testosterone repressed prostate message-2 TRPM-2 P05371 461756 A27205 Rattus norvegicus (Rat) 447 MKILLLCVALLLTWDNGMVLGEQEFSDNELQELSTQGSRYVNKEIQNAVQGVKHIKTLIEKTNAERKSLLNSLEEAKKKKEGALDDTRDSEMKLKAFPEVCNETMMALWEECKPCLKHTCMKFYARVCRSGSGLVGRQLEEFLNQSSPFYFWMNGDRIDSLLESDRQQSQVLDAMQDSFTRASGIIDTLFQDRFFTHEPQDIHHFSPMGFPHKRPHFLYPKSRLVRSLMPLSHYGPLSFHNMFQPFFDMIHQAQQAMDVQLHSPALQFPDVDFLKEGEDDPTVCKEIRHNSTGCLKMKGQCEKCQEILSVDCSTNNPAQANLRQELNDSLQVAERLTQQYNELLHSLQSKMLNTSSLLEQLNDQFTWVSQLANLTQGDDQYLRVSTVTTHSSDSEVPSRVTEVVVKLFDSDPITVVLPEEVSKDNPKFMDTVAEKALQEYRRKSRME Disordered 22 41 EQEFSDNELQELSTQGSRYV Relationship to function unknown Unknown Protein detergent Far-UV circular dichroism (CD) 298 7 Clusterin protein prepared in PBS 4 Nuclear magnetic resonance (NMR) Sensitivity to proteolysis 310 Clusterin renatured or partially denatured Deionized H2O 200 uL Tris pH 7.3, 10 uL 1 Trypsin 4 ug Paper 11570883 Bailey RW, Dunker AK, Brown CJ, Garner EC, Griswold MD Clusterin, a binding protein with a molten globule-like region 2001 Biochemistry 40 39 11828-40 This protein has been determined disordered based on numerous experimental results that indicate it contains flexible loops. However, no exact amino acid locations of disorder are known and the domains specified were based on PONDR predictions. Disordered 66 97 RKSLLNSLEEAKKKKEGALDDTRDSEMKLKAF Relationship to function unknown Unknown Protein detergent Far-UV circular dichroism (CD) 298 7 Clusterin protein prepared in PBS 4 Nuclear magnetic resonance (NMR) Sensitivity to proteolysis 310 Clusterin renatured or partially denatured Deionized H2O 200 uL Tris pH 7.3, 10 uL 1 Trypsin 4 ug Paper 11570883 Bailey RW, Dunker AK, Brown CJ, Garner EC, Griswold MD Clusterin, a binding protein with a molten globule-like region 2001 Biochemistry 40 39 11828-40 This protein has been determined disordered based on numerous experimental results that indicate it contains flexible loops. However, no exact amino acid locations of disorder are known and the domains specified were based on PONDR predictions. Disordered 386 447 TVTTHSSDSEVPSRVTEVVVKLFDSDPITVVLPEEVSKDNPKFMDTVAEKALQEYRRKSRME Relationship to function unknown Unknown Protein detergent Far-UV circular dichroism (CD) 298 7 Clusterin protein prepared in PBS 4 Nuclear magnetic resonance (NMR) Sensitivity to proteolysis 310 Clusterin renatured or partially denatured Deionized H2O 200 uL Tris pH 7.3, 10 uL 1 Trypsin 4 ug Paper 11570883 Bailey RW, Dunker AK, Brown CJ, Garner EC, Griswold MD Clusterin, a binding protein with a molten globule-like region 2001 Biochemistry 40 39 11828-40 This protein has been determined disordered based on numerous experimental results that indicate it contains flexible loops. However, no exact amino acid locations of disorder are known and the domains specified were based on PONDR predictions. This protein has been determined disordered based on numerous experimental results that indicate it contains flexible loops. However, no exact amino acid locations of disorder are known and the domains specified were based on PONDR predictions. cAMP-dependent protein kinase inhibitor, alpha cAMP-dependent protein kinase inhibitor, muscle/brain isoform PKI-alpha P61926 Oryctolagus cuniculus (Rabbit) 76 MTDVETTYADFIASGRTGRRNAIHDILVSSASGNSNELALKLAGLDINKTEGEEDAQRSSTEQSGEAQGEAAKSES Disordered 1 75 MTDVETTYADFIASGRTGRRNAIHDILVSSASGNSNELALKLAGLDINKTEGEEDAQRSSTEQSGEAQGEAAKSE Paper 1862343 Knighton DR, Zheng JH, Ten Eyck LF, Xuong NH, Taylor SS, Sowadski JM Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase 1991 Science 253 5018 414-20 2040607 Thomas J, Van Patten SM, Howard P, Day KH, Mitchell RD, Sosnick T, Trewhella J, Walsh DA, Maurer RA Expression in Escherichia coli and characterization of the heat-stable inhibitor of the cAMP-dependent protein kinase 1991 J Biol Chem 266 17 10906-11 Cyclin-dependent kinase inhibitor 1 CDK-interacting protein 1 Cyclin-dependent kinase inhibitor p21 MDA-6 Melanoma differentiation associated protein 6 p21 P38936 Hs.370771 P38936 2134956 I68674 Homo sapiens 164 MSEPAGDVRQNPCGSKACRRLFGPVDSEQLSRDCDALMAGCIQEARERWNFDFVTETPLEGDFAWERVRGLGLPKLYLPTGPRRGRDELGGGRRPGTSPALLQGTAEEDHVDLSLSCTLVPRSGEQAEGSPGGPGDSQGRKRRQTSMTDFYHSKRRLIFSKRKP Disordered - Extended p21-F (full length) 1 164 MSEPAGDVRQNPCGSKACRRLFGPVDSEQLSRDCDALMAGCIQEARERWNFDFVTETPLEGDFAWERVRGLGLPKLYLPTGPRRGRDELGGGRRPGTSPALLQGTAEEDHVDLSLSCTLVPRSGEQAEGSPGGPGDSQGRKRRQTSMTDFYHSKRRLIFSKRKP Native Function arises via a disorder to order transition Molecular assembly Protein-protein binding Aberrant mobility on SDS-PAGE gel Far-UV circular dichroism (CD) Gel filtration/size exclusion chromatography Insensitivity to pH extremes Mass spectrometry-based high resolution hydrogen-deuterium exchange Nuclear magnetic resonance (NMR) Sensitivity to proteolysis Paper 8876165 Kriwacki RW, Hengst L, Tennant L, Reed SI, Wright PE Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity 1996 Proc Natl Acad Sci U S A 93 21 11504-9 9297835 Kriwacki RW, Wu J, Tennant L, Wright PE, Siuzdak G Probing protein structure using biochemical and biophysical methods. Proteolysis, matrix-assisted laser desorption/ionization mass spectrometry, high-performance liquid chromatography and size-exclusion chromatography of p21Waf1/Cip1/Sdi1 1997 J Chromatogr A 777 1 23-30 Cyclin-dependent kinase inhibitor 1C Cyclin-dependent kinase inhibitor p57 p57KIP2 P49918 Hs.106070 P49918 4557441 G02424 Homo sapiens 316 MSDASLRSTSTMERLVARGTFPVLVRTSACRSLFGPVDHEELSRELQARLAELNAEDQNRWDYDFQQDMPLRGPGRLQWTEVDSDSVPAFYRETVQVGRCRLLLAPRPVAVAVAVSPPLEPAAESLDGLEEAPEQLPSVPVPAPASTPPPVPVLAPAPAPAPAPVAAPVAAPVAVAVLAPAPAPAPAPAPAPAPVAAPAPAPAPAPAPAPAPAPAPDAAPQESAEQGANQGQRGQEPLADQLHSGISGRPAAGTAAASANGAAIKKLSGPLISDFFAKRKRSAPEKSSGDVPAPCPSPSAAPGVGSVEQTPRKRLR Disordered - Extended 1 316 MSDASLRSTSTMERLVARGTFPVLVRTSACRSLFGPVDHEELSRELQARLAELNAEDQNRWDYDFQQDMPLRGPGRLQWTEVDSDSVPAFYRETVQVGRCRLLLAPRPVAVAVAVSPPLEPAAESLDGLEEAPEQLPSVPVPAPASTPPPVPVLAPAPAPAPAPVAAPVAAPVAVAVLAPAPAPAPAPAPAPAPVAAPAPAPAPAPAPAPAPAPAPDAAPQESAEQGANQGQRGQEPLADQLHSGISGRPAAGTAAASANGAAIKKLSGPLISDFFAKRKRSAPEKSSGDVPAPCPSPSAAPGVGSVEQTPRKRLR Native Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Analytical ultracentrifugation 278 Far-UV circular dichroism (CD) 7 DTT 0.001 NaCl salt 50 sodium phosphate salt 10 Gel filtration/size exclusion chromatography 7 DTT 1 NaCl salt 150 sodium phosphate salt 10 Intrinsic fluorescence 7 DTT 1 NaCl salt 50 sodium phosphate salt 10 Nuclear magnetic resonance (NMR) 303 6.6 DTT 1 NaCl salt 50 sodium phosphate salt 10 Paper 11746698 Adkins JN, Lumb KJ Intrinsic structural disorder and sequence features of the cell cycle inhibitor p57Kip2 2002 Proteins 46 1 1-7 9251023 Dynlacht BD, Ngwu C, Winston J, Swindell EC, Elledge SJ, Harlow E, Harper JW Purification and analysis of CIP/KIP proteins 1997 Methods Enzymol 283 230-44 Disordered - Extended inhibition domain 27 91 TSACRSLFGPVDHEELSRELQARLAELNAEDQNRWDYDFQQDMPLRGPGRLQWTEVDSDSVPAFY Fragment Native Function arises via a disorder to order transition Molecular recognition effectors Protein-protein binding Analytical ultracentrifugation 278 Far-UV circular dichroism (CD) 7 DTT 0.001 NaCl salt 50 sodium phosphate salt 10 Paper 11746698 Adkins JN, Lumb KJ Intrinsic structural disorder and sequence features of the cell cycle inhibitor p57Kip2 2002 Proteins 46 1 1-7 9251023 Dynlacht BD, Ngwu C, Winston J, Swindell EC, Elledge SJ, Harlow E, Harper JW Purification and analysis of CIP/KIP proteins 1997 Methods Enzymol 283 230-44 This fragment had 90% inhibition activity towards A-CDK2. Cyclin-dependent kinase inhibitor 1B Cyclin-dependent kinase inhibitor p27 p27Kip1 P46527 1168871 Homo sapiens (Human) 198 MSNVRVSNGSPSLERMDARQAEHPKPSACRNLFGPVDHEELTRDLEKHCRDMEEASQRKWNFDFQNHKPLEGKYEWQEVEKGSLPEFYYRPPRPPKGACKVPAQESQDVSGSRPAAPLIGAPANSEDTHLVDPKTDPSDSQTGLAEQCAGIRKRPATDDSSTQNKRANRTEENVSDGSPNAGSVEQTPKKPGLRRRQT Disordered 22 106 EHPKPSACRNLFGPVDHEELTRDLEKHCRDMEEASQRKWNFDFQNHKPLEGKYEWQEVEKGSLPEFYYRPPRPPKGACKVPAQES Paper 15024385 Lacy ER, Filippov I, Lewis WS, Otieno S, Xiao L, Weiss S, Hengst L, Kriwacki RW p27 binds cyclin-CDK complexes through a sequential mechanism involving binding-induced protein folding 2004 Nat Struct Mol Biol 11 4 358-64 8684460 Russo AA, Jeffrey PD, Patten AK, Massague J, Pavletich NP Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex 1996 Nature 382 6589 325-31 Ubiquinol-cytochrome c reductase iron-sulfur subunit, mitochondrial [Precursor] Cytochrome Bc1 Complex Ubiquinol Cytochrome C Oxidoreductase, Complex III P13272 1351360 A34660 Bos taurus (Bovine) 274 MLSVAARSGPFAPVLSATSRGVAGALRPLVQAAVPATSESPVLDLKRSVLCRESLRGQAAGRPLVASVSLNVPASVRYSHTDIKVPDFSDYRRPEVLDSTKSSKESSEARKGFSYLVTATTTVGVAYAAKNVVSQFVSSMSASADVLAMSKIEIKLSDIPEGKNMAFKWRGKPLFVRHRTKKEIDQEAAVEVSQLRDPQHDLERVKKPEWVILIGVCTHLGCVPIANAGDFGGYYCPCHGSHYDASGRIRKGPAPLNLEVPSYEFTSDDMVIVG Disordered 1 45 MLSVAARSGPFAPVLSATSRGVAGALRPLVQAAVPATSESPVLDL Paper 9651245 Iwata S, Lee JW, Okada K, Lee JK, Iwata M, Rasmussen B, Link TA, Ramaswamy S, Jap BK Complete structure of the 11-subunit bovine mitochondrial cytochrome bc1 complex 1998 Science 281 5373 64-71 DNA-binding protein RAP1 Repressor/activator site binding protein SBF-E TUF P11938 730473 S50714 Saccharomyces cerevisiae (Baker's yeast) 827 MSSPDDFETAPAEYVDALDPSMVVVDSGSAAVTAPSDSAAEVKANQNEENTGATAAETSEKVDQTEVEKKDDDDTTEVGVTTTTPSIADTAATANIASTSGASVTEPTTDDTAADEKKEQVSGPPLSNMKFYLNRDADAHDSLNDIDQLARLIRANGGEVLDSKPRESKENVFIVSPYNHTNLPTVTPTYIKACCQSNSLLNMENYLVPYDNFREVVDSRLQEESHSNGVDNSNSNSDNKDSIRPKTEIISTNTNGATEDSTSEKVMVDAEQQARLQEQAQLLRQHVSSTASITSGGHNDLVQIEQPQKDTSNNNNSNVNDEDNDLLTQDNNPQTADEGNASFQAQRSMISRGALPSHNKASFTDEEDEFILDVVRKNPTRRTTHTLYDEISHYVPNHTGNSIRHRFRVYLSKRLEYVYEVDKFGKLVRDDDGNLIKTKVLPPSIKRKFSADEDYTLAIAVKKQFYRDLFQIDPDTGRSLITDEDTPTAIARRNMTMDPNHVPGSEPNFAAYRTQSRRGPIAREFFKHFAEEHAAHTENAWRDRFRKFLLAYGIDDYISYYEAEKAQNREPEPMKNLTNRPKRPGVPTPGNYNSAAKRARNYSSQRNVQPTANAASANAAAAAAAAASNSYAIPENELLDEDTMNFISSLKNDLSNISNSLPFEYPHEIAEAIRSDFSNEDIYDNIDPDTISFPPKIATTDLFLPLFFHFGSTRQFMDKLHEVISGDYEPSQAEKLVQDLCDETGIRKNFSTSILTCLSGDLMVFPRYFLNMFKDNVNPPPNVPGIWTHDDDESLKSNDQEQIRKLVKKHGTGRMEMRKRFFEKDLL Disordered 482 512 TDEDTPTAIARRNMTMDPNHVPGSEPNFAAY Paper 8620531 Konig P, Giraldo R, Chapman L, Rhodes D The crystal structure of the DNA-binding domain of yeast RAP1 in complex with telomeric DNA 1996 Cell 85 1 125-36 Elongation factor G Elongation Factor G Without Nucleotide P13551 1827912 Thermus thermophilus 691 MAVKVEYDLKRLRNIGIAAHIDAGKTTTTERILYYTGRIHKIGEVHEGAATMDFMEQERERGITITAAVTTCFWKDHRINIIDTPGHVDFTIEVERSMRVLDGAIVVFDSSQGVEPQSETVWRQAEKYKVPRIAFANKMDKTGADLWLVIRTMQERLGARPVVMQLPIGREDTFSGIIDVLRMKAYTYGNDLGTDIREIPIPEEYLDQAREYHEKLVEVAADFDENIMLKYLEGEEPTEEELVAAIRKGTIDLKITPVFLGSALKNKGVQLLLDAVVDYLPSPLDIPPIKGTTPEGEVVEIHPDPNGPLAALAFKIMADPYVGRLTFIRVYSGTLTSGSYVYNTTKGRKERVARLLRMHANHREEVEELKAGDLGAVVGLKETITGDTLVGEDAPRVILESIEVPEPVIDVAIEPKTKADQEKLSQALARLAEEDPTFRVSTHPETGQTIISGMGELHLEIIVDRLKREFKVDANVGKPQVAYRETITKPVDVEGKFIRQTGGRGQYGHVKIKVEPLPRGSGFEFVNAIVGGVIPKEYIPAVQKGIEEAMQSGPLIGFPVVDIKVTLYDGSYHEVDSSEMAFKIAGSMAIKEAVQKGDPVILEPIMRVEVTTPEEYMGDVIGDLNARRGQILGMEPRGNAQVIRAFVPLAEMFGYATDLRSKTQGRGSFVMFFDHYQEVPKQVQEKLIKGQ Disordered 40 67 HKIGEVHEGAATMDFMEQERERGITITA Paper 11054294 Laurberg M, Kristensen O, Martemyanov K, Gudkov AT, Nagaev I, Hughes D, Liljas A Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site 2000 J Mol Biol 303 4 593-603 Disordered 400 475 ESIEVPEPVIDVAIEPKTKADQEKLSQALARLAEEDPTFRVSTHPETGQTIISGMGELHLEIIVDRLKREFKVDAN Paper 11054294 Laurberg M, Kristensen O, Martemyanov K, Gudkov AT, Nagaev I, Hughes D, Liljas A Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site 2000 J Mol Biol 303 4 593-603 EMB-1 protein Embryonic abundant protein from carrot P17639 119316 JQ2273 Daucus carota (Carrot) 92 MASQQEKKELDARARQGETVVPGGTGGKSLEAQQHLAEGRSKGGQTRKEQLGGEGYHEMGRKGGLSNNDMSGGERAEQEGIDIDESKFRTKK Disordered 1 92 MASQQEKKELDARARQGETVVPGGTGGKSLEAQQHLAEGRSKGGQTRKEQLGGEGYHEMGRKGGLSNNDMSGGERAEQEGIDIDESKFRTKK Paper Eom J, Baker WR, Kintanar A, Wurtele ES The embryo-specific EMB-1 protein of Daucus carota is flexible and unstructured in solution 1996 Plant Science 115 17-24 Estradiol 17 beta-dehydrogenase 1 17-beta-HSD 1 20-alpha-HSD 20 alpha-hydroxysteroid dehydrogenase E2DH EC 1.1.1.62 Placental 17-beta-hydroxysteroid dehydrogenase P14061 Hs.448861 P14061 4504501 DEHUE7 Homo sapiens (Human) 327 ARTVVLITGCSSGIGLHLAVRLASDPSQSFKVYATLRDLKTQGRLWEAARALACPPGSLETLQLDVRDSKSVAAARERVTEGRVDVLVCNAGLGLLGPLEALGEDAVASVLDVNVVGTVRMLQAFLPDMKRRGSGRVLVTGSVGGLMGLPFNDVYCASKFALEGLCESLAVLLLPFGVHLSLIECGPVHTAFMEKVLGSPEEVLDRTDIHTFHRFYQYLAHSKQVFREAAQNPEEVAEVFLTALRAPKPTLRYFTTERFLPLLRMRLDDPSGSNYVTAMHREVFGDVPAKAEAGAEAGGGAGPGAEDEAGRSAVGDPELGDPPAAPQ Disordered - Extended 285 327 GDVPAKAEAGAEAGGGAGPGAEDEAGRSAVGDPELGDPPAAPQ Native 1BHS_ 1DHTA 1EQUA 1EQUB 1IOL_ 3DHEA Relationship to function unknown Unknown Unknown X-ray crystallography Mass spectrometry-based high resolution hydrogen-deuterium exchange Paper 8756321 Azzi A, Rehse PH, Zhu DW, Campbell RL, Labrie F, Lin SX Crystal structure of human estrogenic 17 beta-hydroxysteroid dehydrogenase complexed with 17 beta-estradiol 1996 Nat Struct Biol 3 8 665-668 7663947 Ghosh D, Pletnev VZ, Zhu DW, Wawrzak Z, Duax WL, Pangborn W, Labrie F, Lin SX Structure of human estrogenic 17 beta-hydroxysteroid dehydrogenase at 2.20 A resolution 1995 Structure 3 5 503-513 10625652 Han Q, Campbell RL, Gangloff A, Huang YW, Lin SX Dehydroepiandrosterone and dihydrotestosterone recognition by human estrogenic 17beta-hydroxysteroid dehydrogenase. C-18/c-19 steroid discrimination and enzyme-induced strain 2000 J Biol Chem 275 2 1105-1111 9927655 Sawicki MW, Erman M, Puranen T, Vihko P, Ghosh D Structure of the ternary complex of human 17beta-hydroxysteroid dehydrogenase type 1 with 3-hydroxyestra-1,3,5,7-tetraen-17-one (equilin) and NADP+ 1999 Proc Natl Acad Sci U S A 96 3 840-845 The 3DHE:A PDB file gives this protein fragment as complexed with Dehydroepiandrosterone. The 1DHT:A PDB file gives this protein fragment as complexed with Dihydrotestosterone. The 1EQU:A and B PDB files, give this protein fragment as complexed with NADP+ and 3-hydroxyestra-1,3,5,7-tetraen-17-one, (equilin). The 1IOL PDB file gives this protein fragment as complexed with Estradiol. The 1BHS PDB file gives the amino acid sequence for the uncomplexed, unmutated crystal structure of this protein. Disordered - Extended 190 207 TAFMEKVLGSPEEVLDRT Complex Native 1IOL_ Relationship to function unknown Molecular recognition effectors Unknown Substrate/ligand binding X-ray crystallography Paper 8756321 Azzi A, Rehse PH, Zhu DW, Campbell RL, Labrie F, Lin SX Crystal structure of human estrogenic 17 beta-hydroxysteroid dehydrogenase complexed with 17 beta-estradiol 1996 N