The exchangeable yeast ribosomal acidic protein YP2beta shows characteristics of a partly folded state under physiological conditions

60S acidic ribosomal protein P1-beta Acidic ribosomal stalk protein P1 133069 P10622 106 MSDSIISFAAFILADAGLEITSDNLLTITKAAGANVDNVWADVYAKALEGKDLKEILSGFHNAGPVAGAGAASGAAAAGGDAAAEEEKEEEAAEESDDDMGFGLFD Circular dichroism Limited proteolysis Nuclear magnetic resonance spectroscopy Other techniques 1 106 106 Disordered Function arises from the disordered (extended) state Function arises from the molten globule (collapsed) state Phosphorylation Protein-protein binding Protein-rRNA binding Regulation of proteolysis in vivo Substrate/ligand binding Zurdo, J., Sanz, J. M., Gonzalez, C., Rico, M., and Ballesta, J. P. The exchangeable yeast ribosomal acidic protein YP2beta shows characteristics of a partly folded state under physiological conditions 1997 Biochemistry 36 9625 9635 Zurdo, J., Gonzalez, C., Sanz, J. M., Rico, M., Remacha, M., and Ballesta, J. P. Structural differences between Saccharomyces cerevisiae ribosomal stalk proteins P1 and P2 support their functional diversity 2000 Biochemistry 39 8935 8943 Nusspaumer, G., Remacha, M., and Ballesta, J. P. Phosphorylation and N-terminal region of yeast ribosomal protein P1 mediate its degradation, which is prevented by protein P2 2000 EMBO J. 19 6075 6084 Ballesta, J. P. Personal communication 60S acidic ribosomal protein P2-beta Acidic ribosomal stalk protein P2 133071 P02400 110 MKYLAAYLLLVQGGNAAPSAADIKAVVESVGAEVDEARINELLSSLEGKGSLEEIIAEGQKKFATVPTGGASSAAAGAAGAAAGGDAAEEEKEEEAKEESDDDMGFGLFD Circular dichroism Limited proteolysis Nuclear magnetic resonance spectroscopy Other techniques 1 110 110 Disordered Function arises from the disordered (extended) state Function arises from the molten globule (collapsed) state Phosphorylation Protein-protein binding Protein-rRNA binding Regulation of proteolysis in vivo Substrate/ligand binding Zurdo, J., Sanz, J. M., Gonzalez, C., Rico, M., and Ballesta, J. P. The exchangeable yeast ribosomal acidic protein YP2beta shows characteristics of a partly folded state under physiological conditions 1997 Biochemistry 36 9625 9635 Zurdo, J., Gonzalez, C., Sanz, J. M., Rico, M., Remacha, M., and Ballesta, J. P. Structural differences between Saccharomyces cerevisiae ribosomal stalk proteins P1 and P2 support their functional diversity 2000 Biochemistry 39 8935 8943 Nusspaumer, G., Remacha, M., and Ballesta, J. P. Phosphorylation and N-terminal region of yeast ribosomal protein P1 mediate its degradation, which is prevented by protein P2 2000 EMBO J. 19 6075 6084 Ballesta, J. P. Personal communication Early E2a Dna-Binding Protein Adenovirus ssDNA binding protein 1633461 P03265 LADT 356 SVPIVSAWEKGMEAARALMDKYHVDNDLKANFKLLPDQVEALAAVCKTWLNEEHRGLQLTFTSNKTFVTMMGRFLQAYLQSFAEVTYKHHEPTGCALWLHRCAEIEGELKCLHGSIMINKEHVIEMDVTSENGQRALKEQSSKAKIVKNRWGRNVVQISNTDARCCVHDAACPANQFSGKSCGMFFSEGAKAQVAFKQIKAFMQALYPNAQTGHGHLLMPLRCECNSKPGHAPFLGRQLPKLTPFALSNAEDLDADLISDKSVLASVHHPALIVFQCCNPVYRNSRAQGGGPNCDFKISAPDLLNALVMVRSLWSENFTELPRMVVPQFKWSTKHQYRNVSLPVAHSDARQNPFDF Other techniques X-ray crystallography 124 158 35 Disordered Function arises via a disorder to order transition DNA unwinding Flexible linkers/spacers Protein-DNA binding Tucker, P. A., Tsernoglou, D., Tucker, A. D., Coenjaerts, F. E., Leenders, H., and van der Vliet, P. C. Crystal structure of the adenovirus DNA binding protein reveals a hook-on model for cooperative DNA binding 1994 EMBO J. 13 2994 3002 Dekker, J., Kanellopoulos, P. N., van Oosterhout, J. A., Stier, G., Tucker, P. A., and van der Vliet, P. C. ATP-independent DNA unwinding by the adenovirus single-stranded DNA binding protein requires a flexible DNA binding loop 1998 J. Mol. Biol. 277 825 838 van Breukelen, B., Kanellopoulos, P. N., Tucker, P. A., and van der Vliet, P. C. The formation of a flexible DNA-binding protein chain is required for efficient DNA unwinding and adenovirus DNA chain elongation 2000 J. Biol. Chem. 275 40897 40903 Antibacterial protein FALL-39 precursor Antibacterial protein LL-37 1706745 P49913 170 MKTQRDGHSLGRWSLVLLLLGLVMPLAIIAQVLSYKEAVLRAIDGINQRSSDANLYRLLDLDPRPTMDGDPDTPKPVSFTVKETVCPRTTQQSPEDCDFKKDGLVKRCMGTVTLNQARGSFDISCDKDNKRFALLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES Circular dichroism 134 170 37 Disordered Function arises via a disorder to order transition Polymerization Protein-protein binding Johansson, J., Gudmundsson, G. H., Rottenberg, M. E., Berndt, K. D., and Agerberth, B. Conformation-dependent antibacterial activity of the naturally occurring human peptide LL-37 1998 J. Biol. Chem. 273 3718 3724 ANTITERMINATION PROTEIN N NUCLEOCAPSID PROTEIN PN REGULATORY PROTEIN N Antitermination protein N of bacteriophage lambda 132276 P03045 107 MDAQTRRRERRAEKQAQWKAANPLLVGVSAKPVNLPILSLNRKPKSRVESALNPIDLTVLAEYHKQIESNLQRIERKNQRTWYSKPGERGITCSGRQKIKGKSIPLI Circular dichroism Nuclear magnetic resonance spectroscopy 1 107 107 Disordered Function arises via a disorder to order transition Protein-mRNA binding Protein-protein binding Mogridge, J., Legault, P., Li, J., Van Oene, M. D., Kay, L. E., and 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 1 265 275 Legault, P., Li, L., Mogridge, J., Kay, L. E., and Greenblatt, J. NMR structure of the bacteriophage lambda N peptide/boxB RNA complex: recognition of a GNRA fold by an arginine-rich motif 1998 Cell 93 289 299 Cytochrome c Apocytochrome c 117995 P00004 1CRC 104 GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFTYTDANKNKGITWKEETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE Circular dichroism 1 104 104 Disordered Function arises via a disorder to order transition Cofactor/heme binding Stellwagen, E., Rysavy, R., and Babul, G. The conformation of horse heart apocytochrome c 1972 J. Biol. Chem. 247 8074 8077 APEX nuclease Major apurinic/apyrimidinic endonuclease Apurinic/apyrimidinic endonuclease 299037 P27695 1DEW 317 PKRGKKGAVAEDGDELRTEPEAKKSKTAAKKNDKEAAGEGPALYEDPPDHKTSPSGKPATLKICSWNVDGLRAWIKKKGLDWVKEEAPDILCLQETKCSENKLPAELQELPGLSHQYWSAPSDKEGYSGVGLLSRQCPLKVSYGIGDEEHDQEGRVIVAEFDSFVLVTAYVPNAGRGLVRLEYRQRWDEAFRKFLKGLASRKPLVLCGDLNVAHEEIDLRNPKGNKKNAGFTPQERQGFGELLQAVPLADSFRHLYPNTPYAYTFWTYMMNARSKNVGWRLDYFLLSHSLLPALCDSKIRSKALGSDHCPITLYLAL Limited proteolysis X-ray crystallography 1 40 40 Disordered Known to exist in disordered state, relationship to function unknown Unknown Strauss, P. R., and Holt, C. M. Domain mapping of human apurinic/apyrimidinic endonuclease. Structural and functional evidence for a disordered amino terminus and a tight globular carboxyl domain 1998 J. Biol. Chem. 273 14435 14441 Gorman, M. A., Morera, S., Rothwell, D. G., de La Fortelle, E., Mol, C. D., Tainer, J. A., Hickson, I. D., and Freemont, P. S. 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 6548 6558 Mol, C. D., Izumi, T., Mitra, S., and Tainer, J. A. DNA-bound structures and mutants reveal abasic DNA binding by APE1 and DNA repair coordination 2000 Nature 403 451 456 GenBank AAB26054.1 B-cell-specific coactivator BOB.1/OBF.1 B cell-specific transcription co-activator 1150493 Q64693 256 MLWQKSTAPEQAPAPPRPYQGVRVKEPVKELLRRKRGHTSVGAAGPPTAGVLPHQPLATYSTVGPSCLDMEVSASTVTEEGTLCAGWLSQPAPATLHALAPWTPYTEYVSHEAVSCPYSTDMYVQPVCPSYTVVGPSSVLTYASPPLITNVTPRSTATPAVGPQLEGPEHQAPLTYFPWPQPLSTLPTSSLQYQPPAPTLSGPQFVQLPISIPEPVLQDMDDPRRAISSLTIDKLLLEEEESNTYELNHTLSVEGF Circular dichroism Limited proteolysis 1 256 256 Disordered Function arises via a disorder to order transition Protein-DNA binding Protein-protein binding Chang, J. F., Phillips, K., Lundback, T., Gstaiger, M., Ladbury, J. E., and 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. 288 941 952 Rat Bcl-Xl An Apoptosis Inhibitory Protein Bcl-xL antiapoptotic protein 2392082 P53563 1AF3 196 MSQSNRELVVDFLSYKLSQKGYSWSQFSDVEENRTEAPEETEPERETPSAINGNPSWHLADSPAVNGATGHSSSLDAREVIPMAAVKQALREAGDEFELRYRRAFSDLTSQLHITPGTAYQSFEQVVNELFRDGVNWGRIVAFFSFGGALCVESVDKEMQVLVSRIASWMATYLNDHLEPWIQENGGWDTFVDLYG Limited proteolysis X-ray crystallography 31 80 50 Disordered Function arises from the disordered (extended) state Phosphorylation Regulation of proteolysis in vivo Yamamoto, K., Ichijo, H., and Korsmeyer, S. J. BCL-2 is phosphorylated and inactivated by an ASK1/Jun N-terminal protein kinase pathway normally activated at G(2)/M 1999 Mol. Cell. Biol. 19 8469 8478 Cheng, E. H., Kirsch, D. G., Clem, R. J., Ravi, R., Kastan, M. B., Bedi, A., Ueno, K., and Hardwick, J. M. Conversion of Bcl-2 to a Bax-like death effector by caspases 1997 Science 278 1966 1968 Chang, B. S., Minn, A. J., Muchmore, S. W., Fesik, S. W., and Thompson, C. B. Identification of a novel regulatory domain in Bcl-X(L) and Bcl-2 1997 EMBO J. 16 968 977 Alpha-s1-casein precursor - bovine Alpha s-Casein 1070620 P02662 214 MKLLILTCLVAVALARPKHPIKHQGLPQEVLNENLLRFFVAPFPEVFGKEKVNELSKDIGSESTEDQAMEDIKQMEAESISSSEEIVPNSVEQKHIQKEDVPSERYLGYLEQLLRLKKYKVPQLEIVPNSAEERLHSMKEGIHAQQKEPMIGVNQELAYFYPELFRQFYQLDAYPSGAWYYVPLGTQYTDAPSFSDIPNPIGSENSEKTTMPLW Circular dichroism 1 15 15 Undetermined 16 214 199 Disordered Bhattacharyya, J., and Das, K. P. Molecular chaperone-like properties of an unfolded protein, alpha(s)-casein 1999 J. Biol. Chem. 274 15505 15509 Monoamine-sulfating phenol sulfotransferase Sulfotransferase, monoamine-preferring Catecholamine sulfotransferase 1711609 P50224 1CJM A 295 MELIQDTSRPPLEYVKGVPLIKYFAEALGPLQSFQARPDDLLINTYPKSGTTWVSQILDMIYQGGDLEKCNRAPIYVRVPFLEVNDPGEPSGLETLKDTPPPRLIKSHLPLALLPQTLLDQKVKVVYVARNPKDVAVSYYHFHRMEKAHPEPGTWDSFLEKFMAGEVSYGSWYQHVQEWWELSRTHPVLYLFYEDMKENPKREIQKILEFVGRSLPEETMDFMVQHTSFKEMKKNPMTNYTTVPQELMDHSISPFMRKGMAGDWKTTFTVAQNERFDADYAEKMAGCSLSFRSEL X-ray crystallography 216 261 46 Disordered Function arises via a disorder to order transition Substrate/ligand binding Bidwell, L. M., McManus, M. E., Gaedigk, A., Kakuta, Y., Negishi, M., Pedersen, L., and Martin, J. L. Crystal structure of human catecholamine sulfotransferase 1999 J. Mol. Biol. 293 521 530 Dajani, R., Cleasby, A., Neu, M., Wonacott, A. J., Jhoti, H., Hood, A. M., Modi, S., Hersey, A., Taskinen, J., Cooke, R. M., Manchee, G. R., and Coughtrie, M. W. X-ray crystal structure of human dopamine sulfotransferase, SULT1A3. Molecular modeling and quantitative structure-activity relationship analysis demonstrate a molecular basis for sulfotransferase substrate specificity 1999 J. Biol. Chem. 274 37862 37868 Cystic fibrosis transmembrane conductance regulator, ATP-binding cassette CFTR 14753227 P13569 1480 MQRSPLEKASVVSKLFFSWTRPILRKGYRQRLELSDIYQIPSVDSADNLSEKLEREWDRELASKKNPKLINALRRCFFWRFMFYGIFLYLGEVTKAVQPLLLGRIIASYDPDNKEERSIAIYLGIGLCLLFIVRTLLLHPAIFGLHHIGMQMRIAMFSLIYKKTLKLSSRVLDKISIGQLVSLLSNNLNKFDEGLALAHFVWIAPLQVALLMGLIWELLQASAFCGLGFLIVLALFQAGLGRMMMKYRDQRAGKISERLVITSEMIENIQSVKAYCWEEAMEKMIENLRQTELKLTRKAAYVRYFNSSAFFFSGFFVVFLSVLPYALIKGIILRKIFTTISFCIVLRMAVTRQFPWAVQTWYDSLGAINKIQDFLQKQEYKTLEYNLTTTEVVMENVTAFWEEGFGELFEKAKQNNNNRKTSNGDDSLFFSNFSLLGTPVLKDINFKIERGQLLAVAGSTGAGKTSLLMVIMGELEPSEGKIKHSGRISFCSQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDISKFAEKDNIVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILHEGSSYFYGTFSELQNLQPDFSSKLMGCDSFDQFSAERRNSILTETLHRFSLEGDAPVSWTETKKQSFKQTGEFGEKRKNSILNPINSIRKFSIVQKTPLQMNGIEEDSDEPLERRLSLVPDSEQGEAILPRISVISTGPTLQARRRQSVLNLMTHSVNQGQNIHRKTTASTRKVSLAPQANLTELDIYSRRLSQETGLEISEEINEEDLKECFFDDMESIPAVTTWNTYLRYITVHKSLIFVLIWCLVIFLAEVAASLVVLWLLGNTPLQDKGNSTHSRNNSYAVIITSTSSYYVFYIYVGVADTLLAMGFFRGLPLVHTLITVSKILHHKMLHSVLQAPMSTLNTLKAGGILNRFSKDIAILDDLLPLTIFDFIQLLLIVIGAIAVVAVLQPYIFVATVPVIVAFIMLRAYFLQTSQQLKQLESEGRSPIFTHLVTSLKGLWTLRAFGRQPYFETLFHKALNLHTANWFLYLSTLRWFQMRIEMIFVIFFIAVTFISILTTGEGEGRVGIILTLAMNIMSTLQWAVNSSIDVDSLMRSVSRVFKFIDMPTEGKPTKSTKPYKNGQLSKVMIIENSHVKKDDIWPSGGQMTVKDLTAKYTEGGNAILENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGEIQIDGVSWDSITLQQWRKAFGVIPQKVFIFSGTFRKNLDPYEQWSDQEIWKVADEVGLRSVIEQFPGKLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLDPVTYQIIRRTLKQAFADCTVILCEHRIEAMLECQQFLVIEENKVRQYDSIQKLLNERSLFRQAISPSDRVKLFPHRNSSKCKSKPQIAALKEETEEEVQDTRL Circular dichroism Limited proteolysis 1 707 707 Undetermined 708 831 124 Disordered Function arises from the disordered (extended) state Autoregulatory Phosphorylation 832 1480 649 Undetermined Ostedgaard, L. S., Baldursson, O., Vermeer, D. W., Welsh, M. J., and Robertson, A. D. A functional R domain from cystic fibrosis transmembrane conductance regulator is predominantly unstructured in solution 2000 Proc. Natl. Acad. Sci. USA 97 5657 5662 Human Chorionic Gonadotropin Hcg Chorionic gonadotropin 116184 P01233 1hrp B 145 SKEPLRPRCRPINATLAVEKEGCPVCITVNTTICAGYCPTMTRVLQGVLPALPQVVCNYRDVRFESIRLPGCPRGVNPVVSYAVALSCQCALCRRSTTDCGGPKDHPLTCDDPRFQDSSSSKAPPPSLPSPSRLPGPSDTPILPQ X-ray crystallography 112 145 34 Disordered Function arises from the disordered (extended) state Disordered region is not essential for protein function Glycosylation Lapthorn, A. J., Harris, D. C., Littlejohn, A., Lustbader, J. W., Canfield, R. E., Machin, K. J., Morgan, F. J., and Isaacs, N. W. Crystal structure of human chorionic gonadotropin 1994 Nature 369 455 461 Clusterin precursor Clusterin Sulfated glycoprotein 2 SGP-2 Dimeric acid glycoprotein DAG Testosterone repressed prostate message-2 TRPM-2 461756 P05371 447 MKILLLCVALLLTWDNGMVLGEQEFSDNELQELSTQGSRYVNKEIQNAVQGVKHIKTLIEKTNAERKSLLNSLEEAKKKKEGALDDTRDSEMKLKAFPEVCNETMMALWEECKPCLKHTCMKFYARVCRSGSGLVGRQLEEFLNQSSPFYFWMNGDRIDSLLESDRQQSQVLDAMQDSFTRASGIIDTLFQDRFFTHEPQDIHHFSPMGFPHKRPHFLYPKSRLVRSLMPLSHYGPLSFHNMFQPFFDMIHQAQQAMDVQLHSPALQFPDVDFLKEGEDDPTVCKEIRHNSTGCLKMKGQCEKCQEILSVDCSTNNPAQANLRQELNDSLQVAERLTQQYNELLHSLQSKMLNTSSLLEQLNDQFTWVSQLANLTQGDDQYLRVSTVTTHSSDSEVPSRVTEVVVKLFDSDPITVVLPEEVSKDNPKFMDTVAEKALQEYRRKSRME Limited proteolysis 66 97 32 Disordered Function arises from the disordered (extended) state Function arises from the molten globule (collapsed) state Protein detergent 386 445 60 Disordered Function arises from the disordered (extended) state Function arises from the molten globule (collapsed) state Protein detergent Bailey, R. W., Yang, J., Dunker, A. K., and Griswold, M. D. 2000 Biophysical J. 78 152 cAMP-dependent protein kinase inhibitor, alpha form PKI-alpha cAMP-dependent protein kinase inhibitor, muscle/brain isoform cAMP-dependent protein kinase inhibitor 417194 P04541 1APM 76 MTDVETTYADFIASGRTGRRNAIHDILVSSASGNSNELALKLAGLDINKTEGEEDAQRSSTEQSGEAQGEAAKSES Circular dichroism X-ray crystallography 1 76 76 Disordered Function arises via a disorder to order transition Protein-protein binding Wu, H., Lustbader, J. W., Liu, Y., Canfield, R. E., and Hendrickson, W. A. Structure of human chorionic gonadotropin at 2.6 A resolution from MAD analysis of the selenomethionyl protein 1994 Structure 2 545 558 Thomas, J., Van Patten, S. M., Howard, P., Day, K. H., Mitchell, R. D., Sosnick, T., Trewhella, J., Walsh, D. A., and Maurer, R. A. Expression in Escherichia coli and characterization of the heat-stable inhibitor of the cAMP-dependent protein kinase 1991 J. Biol. Chem. 266 10906 10911 Knighton, D. R., Zheng, J. H., Ten Eyck, L. F., Xuong, N. H., Taylor, S. S., and Sowadski, J. M. Structure of a peptide inhibitor bound to the catalytic subunit of cyclic adenosine monophosphate-dependent protein kinase 1991 Science 253 414 420 Cyclin-dependent kinase inhibitor 1 p21 CDK-interacting protein 1 Melanoma differentiation associated protein 6 MDA-6 Cyclin-dependent kinase inhibitor p21 729143 P38936 164 MSEPAGDVRQNPCGSKACRRLFGPVDSEQLSRDCDALMAGCIQEARERWNFDFVTETPLEGDFAWERVRGLGLPKLYLPTGPRRGRDELGGGRRPGTSPALLQGTAEEDHVDLSLSCTLVPRSGEQAEGSPGGPGDSQGRKRRQTSMTDFYHSKRRLIFSKRKP Circular dichroism Limited proteolysis Nuclear magnetic resonance spectroscopy 1 164 164 Disordered Function arises via a disorder to order transition Known to exist in disordered state, relationship to function unknown Protein-protein binding Kriwacki, R. W., Hengst, L., Tennant, L., Reed, S. I., and Wright, P. E. Structural studies of p21Waf1/Cip1/Sdi1 in the free and Cdk2-bound state: conformational disorder mediates binding diversity 1996 Proc. Natl. Acad. Sci. USA 93 11504 11509 cyclin-dependent kinase inhibitor 1C Cyclin-dependent kinase inhibitor p57 11440665 P49918 316 MSDASLRSTSTMERLVARGTFPVLVRTSACRSLFGPVDHEELSRELQARLAELNAEDQNRWDYDFQQDMPLRGPGRLQWTEVDSDSVPAFYRETVQVGRCRLLLAPRPVAVAVAVSPPLEPAAESLDGLEEAPEQLPSVPVPAPASTPPPVPVLAPAPAPAPAPVAAPVAAPVAVAVLAPAPAPAPAPAPAPAPVAARAPAPARARAPAPAPAPAPDAAPQESAEQGANQGQRGQEPLADQLHSGISGRPAAGTAAASANGAAIKKLSGPLISDFFAKRKRSAPEKSSGDVPAPCPSPSAAPGVGSVEQTPRKRLR Circular dichroism Other techniques 1 316 316 Disordered Function arises from the disordered (extended) state Protein-protein binding Adkins, J. N., and Lumb, K. J. Intrinsic structural disorder and sequence features of the cell cycle inhibitor p57Kip2 2002 Proteins 46 1 7 Cyclin-dependent kinase inhibitor 1B Cyclin-dependent kinase inhibitor p27 p27Kip1 1168871 P46527 1JSU 198 MSNVRVSNGSPSLERMDARQAEHPKPSACRNLFGPVDHEELTRDLEKHCRDMEEASQRKWNFDFQNHKPLEGKYEWQEVEKGSLPEFYYRPPRPPKGACKVPAQESQDVSGSRPAAPLIGAPANSEDTHLVDPKTDPSDSQTGLAEQCAGIRKRPATDDSSTQNKRANRTEENVSDGSPNAGSVEQTPKKPGLRRRQT Circular dichroism Other techniques X-ray crystallography 1 21 21 Undetermined 22 106 85 Disordered Function arises via a disorder to order transition Protein-protein binding 107 198 92 Undetermined Russo, A. A., Jeffrey, P. D., Patten, A. K., Massague, J., and Pavletich, N. P. Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A-Cdk2 complex 1996 Nature 381 325 331 Flaugh, S. L., and Lumb, K. J. Effects of macromolecular crowding on the intrinsically disordered proteins c-Fos and p27(Kip1) 2001 Biomacromolecules 2 538 540 Engineered in PDB: 1jsu Cytochrome Bc1 Complex Ubiquinol Cytochrome C Oxidoreductase, Complex III 1351360 P13272 1be3 I 274 MLSVAARSGPFAPVLSATSRGVAGALRPLVQAAVPATSESPVLDLKRSVLCRESLRGQAAGRPLVASVSLNVPASVRYSHTDIKVPDFSDYRRPEVLDSTKSSKESSEARKGFSYLVTATTTVGVAYAAKNVVSQFVSSMSASADVLAMSKIEIKLSDIPEGKNMAFKWRGKPLFVRHRTKKEIDQEAAVEVSQLRDPQHDLERVKKPEWVILIGVCTHLGCVPIANAGDFGGYYCPCHGSHYDASGRIRKGPAPLNLEVPSYEFTSDDMVIVG X-ray crystallography 1 45 45 Disordered Known to exist in disordered state, relationship to function unknown Unknown Iwata, S., Lee, J. W., Okada, K., Lee, J. K., Iwata, M., Rasmussen, B., Link, T. A., Ramaswamy, S., and Jap, B. K. Complete structure of the 11-subunit bovine mitochondrial cytochrome bc1 complex 1998 Science 281 64 71 DNA-binding protein RAP1 SBF-E Repressor/activator site binding protein TUF 730473 P11938 1IGN 827 MSSPDDFETAPAEYVDALDPSMVVVDSGSAAVTAPSDSAAEVKANQNEENTGATAAETSEKVDQTEVEKKDDDDTTEVGVTTTTPSIADTAATANIASTSGASVTEPTTDDTAADEKKEQVSGPPLSNMKFYLNRDADAHDSLNDIDQLARLIRANGGEVLDSKPRESKENVFIVSPYNHTNLPTVTPTYIKACCQSNSLLNMENYLVPYDNFREVVDSRLQEESHSNGVDNSNSNSDNKDSIRPKTEIISTNTNGATEDSTSEKVMVDAEQQARLQEQAQLLRQHVSSTASITSGGHNDLVQIEQPQKDTSNNNNSNVNDEDNDLLTQDNNPQTADEGNASFQAQRSMISRGALPSHNKASFTDEEDEFILDVVRKNPTRRTTHTLYDEISHYVPNHTGNSIRHRFRVYLSKRLEYVYEVDKFGKLVRDDDGNLIKTKVLPPSIKRKFSADEDYTLAIAVKKQFYRDLFQIDPDTGRSLITDEDTPTAIARRNMTMDPNHVPGSEPNFAAYRTQSRRGPIAREFFKHFAEEHAAHTENAWRDRFRKFLLAYGIDDYISYYEAEKAQNREPEPMKNLTNRPKRPGVPTPGNYNSAAKRARNYSSQRNVQPTANAASANAAAAAAAAASNSYAIPENELLDEDTMNFISSLKNDLSNISNSLPFEYPHEIAEAIRSDFSNEDIYDNIDPDTISFPPKIATTDLFLPLFFHFGSTRQFMDKLHEVISGDYEPSQAEKLVQDLCDETGIRKNFSTSILTCLSGDLMVFPRYFLNMFKDNVNPPPNVPGIWTHDDDESLKSNDQEQIRKLVKKHGTGRMEMRKRFFEKDLL Limited proteolysis X-ray crystallography 482 512 31 Disordered Known to exist in disordered state, relationship to function unknown Unknown Konig, P., Giraldo, R., Chapman, L., and Rhodes, D. The crystal structure of the DNA-binding domain of yeast RAP1 in complex with telomeric DNA 1996 Cell 85 125 136 Elongation Factor G Without Nucleotide Elongation factor G 1827912 P13551 1elo 691 MAVKVEYDLKRLRNIGIAAHIDAGKTTTTERILYYTGRIHKIGEVHEGAATMDFMEQERERGITITAAVTTCFWKDHRINIIDTPGHVDFTIEVERSMRVLDGAIVVFDSSQGVEPQSETVWRQAEKYKVPRIAFANKMDKTGADLWLVIRTMQERLGARPVVMQLPIGREDTFSGIIDVLRMKAYTYGNDLGTDIREIPIPEEYLDQAREYHEKLVEVAADFDENIMLKYLEGEEPTEEELVAAIRKGTIDLKITPVFLGSALKNKGVQLLLDAVVDYLPSPLDIPPIKGTTPEGEVVEIHPDPNGPLAALAFKIMADPYVGRLTFIRVYSGTLTSGSYVYNTTKGRKERVARLLRMHANHREEVEELKAGDLGAVVGLKETITGDTLVGEDAPRVILESIEVPEPVIDVAIEPKTKADQEKLSQALARLAEEDPTFRVSTHPETGQTIISGMGELHLEIIVDRLKREFKVDANVGKPQVAYRETITKPVDVEGKFIRQTGGRGQYGHVKIKVEPLPRGSGFEFVNAIVGGVIPKEYIPAVQKGIEEAMQSGPLIGFPVVDIKVTLYDGSYHEVDSSEMAFKIAGSMAIKEAVQKGDPVILEPIMRVEVTTPEEYMGDVIGDLNARRGQILGMEPRGNAQVIRAFVPLAEMFGYATDLRSKTQGRGSFVMFFDHYQEVPKQVQEKLIKGQ X-ray crystallography 40 67 28 Disordered 400 475 76 Disordered Known to exist in disordered state, relationship to function unknown Autoregulatory Flexible linkers/spacers Protein-rRNA binding AEvarsson, A., Brazhnikov, E., Garber, M., Zheltonosova, J., Chirgadze, Y., al-Karadaghi, S., Svensson, L. A., and Liljas, A. Three-dimensional structure of the ribosomal translocase: elongation factor G from Thermus thermophilus 1994 EMBO Journal 13 3669 3677 Laurberg, M., Kristensen, O., Martemyanov, K., Gudkov, A. T., Nagaev, I., Hughes, D., and Liljas, A. Structure of a mutant EF-G reveals domain III and possibly the fusidic acid binding site 2000 J. Mol. Biol. 303 593 603 Martemyanov, K. A., and Gudkov, A. T Domain III of elongation factor G from Thermus thermophilus is essential for induction of GTP hydrolysis on the ribosome 2000 J. Biol. Chem. 275 35820 35824 EMB-1 PROTEIN Embryonic abundant protein from carrot 119316 P17639 92 MASQQEKKELDARARQGETVVPGGTGGKSLEAQQHLAEGRSKGGQTRKEQLGGEGYHEMGRKGGLSNNDMSGGERAEQEGIDIDESKFRTKK Nuclear magnetic resonance spectroscopy 1 92 92 Disordered Known to exist in disordered state, relationship to function unknown Substrate/ligand binding Eom, J., Baker, W., Kintanar, A., and Wurtele, E. 1996 Plant Sci. 115 17 17 Estrogenic 17-Beta Hydroxysteroid Dehydrogenase Complexed 17-Beta-Estradiol 2392375 P14061 1IOL 327 ARTVVLITGCSSGIGLHLAVRLASDPSQSFKVYATLRDLKTQGRLWEAARALACPPGSLETLQLDVRDSKSVAAARERVTEGRVDVLVCNAGLGLLGPLEALGEDAVASVLEVNVVGTVRMLQAFLPDMKRRGSGRVLVTGSVGGLMGLPFNDVYCASKFALEGLCESLAVLLLPFGVHLSLIECGPVHTAFMEKVLGSPEEVLDRTDIHTFHRFYQYLAHSKQVFREAAQNPEEVAEVFLTALRAPKPTLRYFTTERFLPLLRMRLDDPSGSNYVTAMHREVFGDVPAKAEAGAEAGGGAGPGAEDEAGRSAVGDPELGDPPAAPQ X-ray crystallography 285 327 43 Disordered Known to exist in disordered state, relationship to function unknown Disordered region is not essential for protein function Protein-lipid interaction Ghosh, D., Pletnev, V. Z., Zhu, D. W., Wawrzak, Z., Duax, W. L., Pangborn, W., Labrie, F., and Lin, S. X. Structure of human estrogenic 17 beta-hydroxysteroid dehydrogenase at 2.20 A resolution 1995 Structure 3 503 513 E7 protein E7 protein from HPV16 6469700 P03129 93 MHGDTPTLHEYMLDLQPETTDLYCYEQLSDSSEEEDEIDGPAGQAEPDRAHYNIVTFCCKCDSTLRLCVQSTHVDIRTLEDLLMGTLGIVCPI Circular dichroism 1 93 93 Disordered Function arises via a disorder to order transition Metal binding Protein-protein binding Pahel, G., Aulabaugh, A., Short, S. A., Barnes, J. A., Painter, G. R., Ray, P., and Phelps, W. C. Structural and functional characterization of the HPV16 E7 protein expressed in bacteria 1993 J. Biol. Chem. 268 26018 26025 Fibronectin-binding protein precursor FNBP Fibronectin binding protein 120457 P14738 1018 MKNNLRYGIRKHKLGAASVFLGTMIVVGMGQDKEAAASEQKTTTVEENGNSATDNKTSETQTTATNVNHIEETQSYNATVTEQPSNATQVTTEEAPKAVQAPQTAQPANIETVKEEVVKEEAKPQVKETTQSQDNSGDQRQVDLTPKKATQNQVAETQVEVAQPRTASESKPRVTRSADVAEAKEASNAKVETGTDVTSKVTVEIGSIEGHNNTNKVEPHAGQRAVLKYKLKFENGLHQGDYFDFTLSNNVNTHGVSTARKVPEIKNGSVVMATGEVLEGGKIRYTFTNDIEDKVDVTAELEINLFIDPKTVQTNGNQTITSTLNEEQTSKELDVKYKDGIGNYYANLNGSIETFNKANNRFSHVAFIKPNNGKTTSVTVTGTLMKGSNQNGNQPKVRIFEYLGNNEDIAKSVYANTTDTSKFKEVTSNMSGNLNLQNNGSYSLNIENLDKTYVVHYDGEYLNGTDEVDFRTQMVGHPEQLYKYYYDRGYTLTWDNGLVLYSNKANGNEKNGPIIQNNKFEYKEDTIKETLTGQYDKNLVTTVEEEYDSSTLDIDYHTAIDGGGGYVDGYIETIEETDSSAIDIDYHTAVDSEAGHVGGYTESSEESNPIDFEESTHENSKHHADVVEYEEDTNPGGGQVTTESNLVEFDEESTKGIVTGAVSDHTTVEDTKEYTTESNLIELVDELPEEHGQAQGPVEEITKNNHHISHSGLGTENGHGNYDVIEEIEENSHVDIKSELGYEGGQNSGNQSFEEDTEEDKPKYEQGGNIVDIDFDSVPQIHGQNKGNQSFEEDTEKDKPKYEHGGNIIDIDFDSVPHIHGFNKHTEIIEEDTNKDKPSYQFGGHNSVDFEEDTLPKVSGQNEGQQTIEEDTTPPIVPPTPPTPEVPSEPETPTPPTPEVPSEPETPTPPTPEVPSEPETPTPPTPEVPAEPGKPVPPAKEEPKKPSKPVEQGKVVTPVIEINEKVKAVAPTKKPQSKKSELPETGGEESTNKGMLFGGLFSILGLALLRRNKKNHKA Nuclear magnetic resonance spectroscopy 1 744 744 Undetermined 745 873 129 Disordered Function arises via a disorder to order transition Protein-protein binding 874 1018 145 Undetermined Penkett, C. J., Redfield, C., Dodd, I., Hubbard, J., McBay, D. L., Mossakowska, D. E., Smith, R. A., Dobson, C. M., and Smith, L. J. NMR analysis of main-chain conformational preferences in an unfolded fibronectin-binding protein 1997 J. Mol. Biol. 274 152 159 Penkett, C. J., Redfield, C., Jones, J. A., Dodd, I., Hubbard, J., Smith, R. A., Smith, L. J., and Dobson, C. M. Structural and dynamical characterization of a biologically active unfolded fibronectin-binding protein from Staphylococcus aureus 1998 Biochemistry 37 17054 17067 Penkett, C. J., Dobson, C. M., Smith, L. J., Bright, J. R., Pickford, A. R., Campbell, I. D., and Potts, J. R. Identification of residues involved in the interaction of Staphylococcus aureus fibronectin-binding protein with the (4)F1(5)F1 module pair of human fibronectin using heteronuclear NMR spectroscopy 2000 Biochemistry 39 2887 2893 Flagellin - Salmonella typhimurium Flagellin 96744 S16121 1io1 494 AQVINTNSLSLLTQNNLNKSQSALGTAIERLSSGLRINSAKDDAAGQAIANRFTANIKGLTQASRNANDGISIAQTTEGALNEINNNLQRVRELAVQSANSTNSQSDLDSIQAEITQRLNEIDRVSGQTQFNGVKVLAQDNTLTIQVGANDGETIDIDLKQINSQTLGLDTLNVQQKYKVSDTAATVTGYADTTIALDNSTFKASATGLGGTDQKIDGDLKFDDTTGKYYAKVTVTGGTGKDGYYEVSVDKTNGEVTLAGGATSPLTGGLPATATEDVKNVQVANADLTEAKAALTAAGVTGTASVVKMSYTDNNGKTIDGGLAVKVGDDYYSATQNKDGSISINTTKYTADDGTSKTALNKLGGADGKTEVVSIGGKTYAASKAEGHNFKAQPDLAEAAATTTENPLQKIDAALAQVDTLRSDLGAVQNRFNSAITNLGNTVNNLTSARSRIEDSDYATEVSNMSRAQILQQAGTSVLAQANQVPQNVLSLLR Circular dichroism Nuclear magnetic resonance spectroscopy Other techniques X-ray crystallography 1 55 55 Disordered Function arises from the disordered (extended) state Function arises via a disorder to order transition Polymerization Protein-protein binding Self-transport through channel 451 494 44 Disordered Function arises from the disordered (extended) state Function arises via a disorder to order transition Polymerization Protein-protein binding Self-transport through channel Vonderviszt, F., Kanto, S., Aizawa, S., and Namba, K. Terminal regions of flagellin are disordered in solution 1989 J. Mol. Biol. 209 127 133 Aizawa, S. I., Vonderviszt, F., Ishima, R., and Akasaka, K. Termini of Salmonella flagellin are disordered and become organized upon polymerization into flagellar filament 1990 J. Mol. Biol. 211 673 677 Mimori-Kiyosue, Y., Yamashita, I., Fujiyoshi, Y., Yamaguchi, S., and Namba, K. Role of the outermost subdomain of Salmonella flagellin in the filament structure revealed by electron cryomicroscopy 1998 J. Mol. Biol. 284 521 530 Mimori-Kiyosue, Y., Vonderviszt, F., and Namba, K. Locations of terminal segments of flagellin in the filament structure and their roles in polymerization and polymorphism 1997 J. Mol. Biol. 270 (2) 222 237 Samatey, F. A., Imada, K., Nagashima, S., Vonderviszt, F., Kumasaka, T., Yamamoto, M., and Namba, K. Structure of the bacterial flagellar protofilament and implications for a switch for supercoiling 2001 Nature 410 331 337 PIR: S16121 Negative regulator of flagellin synthesis Anti-sigma-28 factor Flagellum specific sigma factor 120306 P26477 97 MSIDRTSPLKPVSTVQTRETSDTPVQKTRQEKTSAATSASVTLSDAQAKLMQPGVSDINMERVEALKTAIRNGELKMDTGKIADSLIREAQSYLQSK Nuclear magnetic resonance spectroscopy 1 97 97 Disordered Function arises from the disordered (extended) state Function arises via a disorder to order transition Protein-protein binding Self-transport through channel Daughdrill, G. W., Chadsey, M. S., Karlinsey, J. E., Hughes, K. T., and Dahlquist, F. W. The C-terminal half of the anti-sigma factor, FlgM, becomes structured when bound to its target, sigma 28 1997 Nat. Struct. Biol. 4 285 291 Daughdrill, G. W., Hanely, L. J., and Dahlquist, F. W. The C-terminal half of the anti-sigma factor FlgM contains a dynamic equilibrium solution structure favoring helical conformations 1998 Biochemistry 37 1076 1082 Eukaryotic translation initiation factor 4E binding protein 1 4E-binding protein 1 4758258 Q13541 118 MSGGSSCSQTPSRAIPATRRVVLGDGVQLPPGDYSTTPGGTLFSTTPGGTRIIYDRKFLMECRNSPVTKTPPRDLPTIPGVTSPSSDEPPMEASQSHLRNSPEDKRAGGEESQFEMDI Circular dichroism Nuclear magnetic resonance spectroscopy X-ray crystallography 1 118 118 Disordered Function arises from the disordered (extended) state Function arises via a disorder to order transition Phosphorylation Protein-protein binding Fletcher, C. M., McGuire, A. M., Gingras, A. C., Li, H., Matsuo, H., Sonenberg, N., and Wagner, G. 4E binding proteins inhibit the translation factor eIF4E without folded structure 1998 Biochemistry 37 9 15 Fletcher, C. M., and Wagner, G. The interaction of eIF4E with 4E-BP1 is an induced fit to a completely disordered protein 1998 Protein Sci. 7 1639 1642 Gingras, A. C., Gygi, S. P., Raught, B., Polakiewicz, R. D., Abraham, R. T., Hoekstra, M. F., Aebersold, R., and Sonenberg, N. Regulation of 4E-BP1 phosphorylation: a novel two-step mechanism 1999 Genes Dev. 13 1422 1437 Glycine N-Methyltransferase Glial cell-derived neurotrophic factor 729568 Q07731 1agq A 135 MSPDKQAAALPRRERNRQAAAASPENSRGKGRRGQRGKNRGCVLTAIHLNVTDLGLGYETKEELIFRYCSGSCEAAETMYDKILKNLSRSRRLTSDKVGQACCRPVAFDDDLSFLDDSLVYHILRKHSAKRCGCI X-ray crystallography 1 38 38 Disordered Function arises via a disorder to order transition Protein-protein binding Eigenbrot, C., and Gerber, N. X-ray structure of glial cell-derived neurotrophic factor at 1.9 A resolution and implications for receptor binding 1997 Nat. Struct. Biol. 4 435 438 Eketjall, S., Fainzilber, M., Murray-Rust, J., and Ibanez, C. F. Distinct structural elements in GDNF mediate binding to GFRalpha1 and activation of the GFRalpha1-c-Ret receptor complex 1999 EMBO Journal 18 5901 5910 Ibanez, C. F. Personal communication Part of GI: 729568 Part of SP: Q07731 glucocorticoid receptor DNA binding factor 1 [Homo sapiens] Glucocorticoid receptor 4758482 Q9NRY4 834 DATSHIDNMENERIPFDLMDTVPAEALYEAHLEKLRNERKRVEMRRAFKENLETSPFITPGKPWEEARSFIMNEDFYQWLEESVYTDIYGKHQKQIIDKAKEEFQELLLEYSELFYELELDAKPSKEKMGVIQDVLGEEQRFKAIYKSSKQSVDALILKHIHFVYHPTKETCPSCPACVDAKIEHLISSRFIRPSDRNQKNSLSDPNIDRINLVILGKDALPESWPMEIRALCTNDDKYVIDGKMYELSLRPIEGNVRLPVNSFQTPTFQPHGCLCLYNSKESLSYVVESIEKSRESTLGRRDNHLVHLPLTLILVNKRGDTSGETLHSLIQQGQQIASKLQCVFLDPASAGIGYGRNINEKQISQVLKGLLDSKRNLNLVSSTASIKDLADVDLRIVMCLMCGDPFSADDILFPVLQSQTCKSSHCGSNNSVLLELPIGLHKKRIELSVLSYHSSFSIRKSRLVHGYIVFYSAKRKASLAMLRAFLCEVQDIIPIQLVALTDGAVDVLDNDLSREQLTEGEEIAQEIDGRFTSIPCSQPQHKLEIFHPFFKDVVEKKNIIEATHMYDNAAEACSTTEEVFNSPRAGSPLCNSNLQDSEEDIEPSYSLFREDTSLPSLSKDHSKLSMELEGNDGLSFIMSNFESKLNNKVPPPVKPKPPVHFEITKGDLSYLDQGHRDGQRKSVSSSPWLPQDGFDPSDYAEPMDAVVKPRNEEENIYSVPHDSTQGKIITIRNINKAQSNGSGNGSDSEMDTSSLERGRKVSIVSKPVLYRTRCTRLGGLLVTGPASAWGVMMSWGPSGRKRRIRHPRVIKGTMLSFHTKQTKTRGGGIFFAA Circular dichroism Other techniques 1 76 76 Undetermined 77 262 186 Disordered Function arises via a disorder to order transition Protein-protein binding 263 835 573 Undetermined Baskakov, I. V., Kumar, R., Srinivasan, G., Ji, Y. S., Bolen, D. W., and Thompson, E. B. Trimethylamine N-oxide-induced cooperative folding of an intrinsically unfolded transcription-activating fragment of human glucocorticoid receptor 1999 J. Biol. Chem. 274 10693 10696 Glycine N-Methyltransferase 121328 P13255 1d2h A 292 VDSVYRTRSLGVAAEGIPDQYADGEAARVWQLYIGDTRSRTAEYKAWLLGLLRQHGCHRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYALKERWNRRKEPAFDKWVIEEANWLTLDKDVPAGDGFDAVICLGNSFAHLPDSKGDQSEHRLALKNIASMVRPGGLLVIDHKNYDYILSTGCAPPGKNIYYKSDLTKDITTSVLTVNNKAHMVTLDYTVQVPGAGRDGAPGFSKFRLSYYPHCLASFTELVQEAFGGRCQHSVLGDFKPYRPGQAYVPCYFIHVLKKTG X-ray crystallography 1 40 40 Disordered Function arises via a disorder to order transition Known to exist in disordered state, relationship to function unknown Substrate/ligand binding Huang, Y., Komoto, J., Konishi, K., Takata, Y., Ogawa, H., Gomi, T., Fujioka, M., and Takusagawa, F. Mechanisms for auto-inhibition and forced product release in glycine N-methyltransferase: crystal structures of wild-type, mutant R175K and S-adenosylhomocysteine-bound R175K enzymes 2000 J. Mol. Biol. 298 149 162 Takusagawa, F. Personal communication Part of GI: 121328 Part of SP: P13255 Glycyl-tRNA Synthetase Glycyl-tRNA Ligase 2829475 P56206 1ggm A 442 AASSLDELVALCKRRGFIFQSSEIYGGLQGVYDYGPLGVELKNNLKQAWWRRNVYERDDMEGLDASVLTHRLVLHYSGHEATFADPMVDNAKARYWTPPRYFNMMFQDLRGPRGGRGLLAYLRPETAQGIFVNFKNVLDATSRKLGFGIAQIGKAFRNEITPRNFIFRVREFEQMEIEYFVRPGEDEYWHRYWVEERLKWWQEMGLSRENLVPYQQPPESSAHYAKATVDILYRFPHGSLELEGIAQRTDFDLGSHTKDQEALGITARVLRNEHSTQRLAYRDPETGKWFVPYVIEPSAGVDRGVLALLAEAFTREELPNGEERIVLKLKPQLAPIKVAVIPLVKNRPEITEYAKRLKARLLALGLGRVLYEDTGNIGKAYRRHDEVGTPFAVTVDYDTIGQSKDGTTRLKDTVTVRDRDTMEQIRLHVDELEGFLRERLRW X-ray crystallography 96 158 63 Disordered Known to exist in disordered state, relationship to function unknown Unknown Logan, D. T., Mazauric, M. H., Kern, D., and Moras, D. Crystal structure of glycyl-tRNA synthetase from Thermus thermophilus 1995 EMBO Journal 14 4156 4167 Arnez, J. G., Dock-Bregeon, A. C., and Moras, D. Glycyl-tRNA synthetase uses a negatively charged pit for specific recognition and activation of glycine 1999 J. Mol. Biol. 286 1449 1459 Growth Hormone Receptor 121180 P10912 1a22 B 238 FSGSEATAAILSRAPWSLQSVNPGLKTNSSKEPKFTKCRSPERETFSCHWTDEVHHGTKNLGPIQLFYTRRNTQEWTQEWKECPDYVSAGENSCYFNSSFTSIWIPYCIKLTSNGGTVDEKCFSVDEIVQPDPPIALNWTLLNVSLTGIHADIQVRWEAPRNADIQKGWMVLEYELQYKEVNETKWKMMDPILTTSVPVYSLKVDKEYEVRVRSKQRNSGNYGEFSEVLYVTLPQMSQ X-ray crystallography 1 32 32 Disordered Function arises via a disorder to order transition Disordered region is not essential for protein function Protein-protein binding Clackson, T., Ultsch, M. H., Wells, J. A., and de Vos, A. M. Structural and functional analysis of the 1:1 growth hormone:receptor complex reveals the molecular basis for receptor affinity 1998 J. Mol. Biol. 277 1111 1128 Clackson, T., and Wells, J. A. A hot spot of binding energy in a hormone-receptor interface 1995 Science 267 383 386 Coat protein A [Precursor] G3P g3p (fd phage minor coat protein) 5822481 P03661 2G3P 424 MKKLLFAIPLVVPFYSHSAETVESCLAKPHTENSFTNVWKDDKTLDRYANYEGCLWNATGVVVCTGDETQCYGTWVPIGLAIPENEGGGSEGGGSEGGGSEGGGTKPPEYGDTPIPGYTYINPLDGTYPPGTEQNPANPNPSLEESQPLNTFMFQNNRFRNRQGALTVYTGTVTQGTDPVKTYYQYTPVSSKAMYDAYWNGKFRDCAFHSGFNEDPFVCEYQGQSSDLPQPPVNAGGGSGGGSGGGSEGGGSEGGGSEGGGSEGGGSGGGSGSGDFDYEKMANANKGAMTENADENALQSDAKGKLDSVATDYGAAIDGFIGDVSGLANGNGATGDFAGSNSQMAQVGDGDNSPLMNNFRQYLPSLPQSVECRPYVFGAGKPYEFSIDCDKINLFRGVFAFLLYVATFMYVFSTFANILRNKES 236 274 39 Disordered Function arises from the disordered (extended) state Flexible linkers/spacers Holliger, P., Riechmann, L., and Williams, R. L. Crystal structure of the two N-terminal domains of g3p from filamentous phage fd at 1.9 A: evidence for conformational lability 1999 J. Mol. Biol. 288 649 657 Nilsson, N., Malmborg, A. C., and Borrebaeck, C. A. The phage infection process: a functional role for the distal linker region of bacteriophage protein 3 2000 J. Virol. 74 4229 4235 Mutant in PDB: 2g3p Guanine Nucleotide-Binding Protein Alpha-1 Subunit Gia1, Guanine Nucleotide-Binding Protein G(I), Alpha-1 Subunit G protein Gi Alpha 1 121020 P10824 1cip A 353 GCTLSAEDKAAVERSKMIDRNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDAARADDARQLFVLAGAAEEGFMTAELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAAAYIQCQFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF X-ray crystallography 1 31 31 Disordered Function arises from the disordered (extended) state Function arises via a disorder to order transition Fatty acylation (myristolation and palmitoylation) Protein-lipid interaction Protein-protein binding Coleman, D. E., Berghuis, A. M., Lee, E., Linder, M. E., Gilman, A. G., and Sprang, S. R. Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis 1994 Science 265 1405 1412 Coleman, D. E., and Sprang, S. R. Structure of Gialpha1.GppNHp, autoinhibition in a galpha protein-substrate complex 1999 J. Biol. Chem. 274 16669 16672 Heat shock factor protein HSF Heat shock transcription factor HSTF 123686 P22121 1FBQ 677 MGHNDSVETMDEISNPNNILLPHDGTGLDATGISGSQEPYGMVDVLNPDSLKDDSNVDEPLIEDIVNPSLDPEGVVSAEPSNEVGTPLLQQPISLDHVITRPASAGGVYSIGNSSTSSAAKLSDGDLTNATDPLLNNAHGHGQPSSESQSHSNGYHKQGQSQQPLLSLNKRKLLAKAHVDKHHSKKKLSTTRARPAFVNKLWSMVNDKSNEKFIHWSTSGESIVVPNRERFVQEVLPKYFKHSNFASFVRQLNMYGWHKVQDVKSGSMLSNNDSRWEFENENFKRGKEYLLENIVRQKSNTNILGGTTNAEVDIHILLNELETVKYNQLAIAEDLKRITKDNEMLWKENMMARERHQSQQQVLEKLLRFLSSVFGPNSAKTIGNGFQPDLIHELSDMQVNHMSNNNHNNTGNINPNAYHNETDDPMANVFGPLTPTDQGKVPLQDYKLRPRLLLKNRSMSSSSSSNLNQRQSPQNRIVGQSPPPQQQQQQQQQQGQPQGQQFSYPIQGGNQMMNQLGSPIGTQVGSPVGSQYGNQYGNQYSNQFGNQLQQQTSRPALHHGSNGEIRELTPSIVSSDSPDPAFFQDLQNNIDKQEESIQEIQDWITKLNPGPGEDGNTPIFPELNMPSYFANTGGSGQSEQPSDYGDSQIEELRNSRLHEPDRSFEEKNNGQKRRRAA Circular dichroism Nuclear magnetic resonance spectroscopy 1 196 196 Disordered Function arises from the disordered (extended) state Protein-protein binding 219 223 5 Disordered 261 276 16 Disordered 280 282 3 Disordered 283 677 395 Undetermined Cho, H. S., Liu, C. W., Damberger, F. F., Pelton, J. G., Nelson, H. C., and Wemmer, D. E. Yeast heat shock transcription factor N-terminal activation domains are unstructured as probed by heteronuclear NMR spectroscopy 1996 Protein Science 5 262 269 Part in PDB: 3hsf Heparin-Binding Epidermal Growth Factor Hbegf Heparin-binding EGF-like growth factor 544477 Q99075 1xdt R 79 GSHMRVTLSSKPQALATPNKEEHGKRKKKGKGLGKKRDPCLRKYKDFCIHGECKYVKELRAPSCICHPGYHGERCHGLS X-ray crystallography 1 38 38 Disordered Louie, G. V., Yang, W., Bowman, M. E., and Choe, S. Crystal structure of the complex of diphtheria toxin with an extracellular fragment of its receptor 1997 Mol. Cell 1 67 78 Higashiyama, S., Lau, K., Besner, G. E., Abraham, J. A., and Klagsbrun, M. Structure of heparin-binding EGF-like growth factor. Multiple forms, primary structure, and glycosylation of the mature protein 1992 J Biol Chem 267 6205 6212 high-mobility group (nonhistone chromosomal) protein 14 Nonhistone chromosomal protein HMG-14 human non-histone chromosomal protein HMG-14 [Homo sapiens] High mobility group - 14 4826758 P05114 100 MPKRKVSSAEGAAKEEPKRRSARLSAKPPAKVEAKPKKAAAKDKSSDKKVQTKGKRGAKGKQAEVANQETKEDLPAENGETKTEESPASDEAGEKEAKSD Circular dichroism Nuclear magnetic resonance spectroscopy Other techniques 1 100 100 Disordered Function arises from the disordered (extended) state Function arises via a disorder to order transition Acetylation Phosphorylation Protein-DNA binding Protein-protein binding Cary, P. D., King, D. S., Crane-Robinson, C., Bradbury, E. M., Rabbani, A., Goodwin, G. H., and Johns, E. W. Structural studies on two high-mobility-group proteins from calf thymus, HMG-14 and HMG-20 (ubiquitin), and their interaction with DNA 1980 Eur. J. Biochem. 112 577 580 Abercrombie, B. D., Kneale, G. G., Crane-Robinson, C., Bradbury, E. M., Goodwin, G. H., Walker, J. M., and Johns, E. W. Studies on the conformational properties of the high-mobility-group chromosomal protein HMG 17 and its interaction with DNA 1978 Eur. J. Biochem. 84 173 177 Louie, D. F., Gloor, K. K., Galasinski, S. C., Resing, K. A., and Ahn, N. G. Phosphorylation and subcellular redistribution of high mobility group proteins 14 and 17, analyzed by mass spectrometry 2000 Protein Science 9 170 179 Bergel, M., Herrera, J. E., Thatcher, B. J., Prymakowska-Bosak, M., Vassilev, A., Nakatani, Y., Martin, B., and Bustin, M. Acetylation of novel sites in the nucleosomal binding domain of chromosomal protein HMG-14 by p300 alters its interaction with nucleosomes 2000 J. Biol. Chem. 275 11514 11520 high-mobility group nucleosomal binding domain 2 nonhistone chromosomal protein HMG-17 high mobility group protein N2 high-mobility group (nonhistone chromosomal) protein 17 [Homo sapiens] High mobility group - 17 5031749 P05204 90 MPKRKAEGDAKGDKAKVKDEPQRRSARLSAKPAPPKPEPKPKKAPAKKGEKVPKGKKGKADAGKEGNNPAENGDAKTDQAQKAEGAGDAK Circular dichroism Nuclear magnetic resonance spectroscopy Other techniques 1 90 90 Disordered Function arises from the disordered (extended) state Function arises via a disorder to order transition Acetylation Phosphorylation Protein-DNA binding Protein-protein binding Cary, P. D., King, D. S., Crane-Robinson, C., Bradbury, E. M., Rabbani, A., Goodwin, G. H., and Johns, E. W. Structural studies on two high-mobility-group proteins from calf thymus, HMG-14 and HMG-20 (ubiquitin), and their interaction with DNA 1980 Eur. J. Biochem. 112 577 580 Abercrombie, B. D., Kneale, G. G., Crane-Robinson, C., Bradbury, E. M., Goodwin, G. H., Walker, J. M., and Johns, E. W. Studies on the conformational properties of the high-mobility-group chromosomal protein HMG 17 and its interaction with DNA 1978 Eur. J. Biochem. 84 173 177 Louie, D. F., Gloor, K. K., Galasinski, S. C., Resing, K. A., and Ahn, N. G. Phosphorylation and subcellular redistribution of high mobility group proteins 14 and 17, analyzed by mass spectrometry 2000 Protein Science 9 170 179 Bergel, M., Herrera, J. E., Thatcher, B. J., Prymakowska-Bosak, M., Vassilev, A., Nakatani, Y., Martin, B., and Bustin, M. Acetylation of novel sites in the nucleosomal binding domain of chromosomal protein HMG-14 by p300 alters its interaction with nucleosomes 2000 J. Biol. Chem. 275 11514 11520 High mobility group protein HMG-I/HMG-Y HMG-I(Y) High mobility group AT-hook 1 High mobility group - I(Y) 123377 P17096 2EZD 107 MSESSSKSSQPLASKQEKDGTEKRGRGRPRKQPPVSPGTALVGSQKEPSEVPTPKRPRGRPKGSKNKGAAKTRKTTTTPGRKPRGRPKKLEKEEEEGISQESSEEEQ Nuclear magnetic resonance spectroscopy 1 107 107 Disordered Function arises from the disordered (extended) state Function arises via a disorder to order transition Acetylation Phosphorylation Protein-DNA binding Protein-protein binding Huth, J. R., Bewley, C. A., Nissen, M. S., Evans, J. N., Reeves, R., Gronenborn, A. M., and Clore, G. M. The solution structure of an HMG-I(Y)-DNA complex defines a new architectural minor groove binding motif 1997 Nat. Struct. Biol. 4 657 665 Pierantoni, G. M., Fedele, M., Pentimalli, F., Benvenuto, G., Pero, R., Viglietto, G., Santoro, M., Chiariotti, L., and Fusco, A. High mobility group I (Y) proteins bind HIPK2, a serine-threonine kinase protein which inhibits cell growth 2001 Oncogene 20 6132 6141 Munshi, N., Agalioti, T., Lomvardas, S., Merika, M., Chen, G., and Thanos, D. Coordination of a transcriptional switch by HMGI(Y) acetylation 2001 Science 293 1133 1136 High mobility group-T protein HMG-T HMG-T1 HMG-1 123382 P07746 204 MGKDPRKPRGKMSSYAYFVQTRREEHKKKHPEASVNFSEFSKKCSERWKTMSAKEKGKFEDLAKLDKVRYEREMRSYIPPKGEKKKRFKDPNAPKRPSSAFFIFCADFRPQVKGETPGLSIGDVAKKLGEKWNNLTAEDKVPYEKKASRLKEKYEKDITAYRNKGKVPVSMPAKAAAPAKDDDDDDDDDDDDEDDDDDDDEDDE Circular dichroism Nuclear magnetic resonance spectroscopy 1 204 204 Disordered Function arises via a disorder to order transition Protein-DNA binding Cary, P. D., Crane-Robinson, C., Bradbury, E. M., and Dixon, G. H. Structural studies of the non-histone chromosomal proteins HMG-T and H6 from trout testis 1981 Eur. J. Biochem. 119 545 551 NONHISTONE CHROMOSOMAL PROTEIN H6 HISTONE T High mobility group - H6 462245 P02315 70 MPKRKSATKGDEPARRSARLSARPVPKPAAKPKKAAAPKKAVKGKKAAENGDAKAEAKVQAAGDGAGNAK Circular dichroism Nuclear magnetic resonance spectroscopy 1 70 70 Disordered Function arises via a disorder to order transition Protein-DNA binding Cary, P. D., Crane-Robinson, C., Bradbury, E. M., and Dixon, G. H. Structural studies of the non-histone chromosomal proteins HMG-T and H6 from trout testis 1981 Eur. J. Biochem. 119 545 551 Histone H3 211857 Q92068 136 MARTKQTARKSTGGKAPRKQLATKAARKSAPATGGVKKPHRYRPGTVALREIRRYQKSTELLIRKLPFQRLVREIAQDFKTDLRFQSSAVMALQEASEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA X-ray crystallography 1 40 40 Disordered Function arises from the disordered (extended) state Acetylation Methylation Phosphorylation Lambert, S. J., Nicholson, J. M., Chantalat, L., Reid, A. J., Donovan, M. J., and Baldwin, J. P. Purification of histone core octamers and 2.15 A X-ray analysis of crystals in KCl/phosphate 1999 Acta. Crystallogr. D. Biol. Crystallogr. 55 1048 1051 Nakayama, J., Rice, J. C., Strahl, B. D., Allis, C. D., and Grewal, S. I. Role of histone H3 lysine 9 methylation in epigenetic control of heterochromatin assembly 2001 Science 292 110 113 histone H5 - chicken 70678 P02259 1HST 189 TESLVLSPAPAKPKRVKASRRSASHPTYSEMIAAAIRAEKSRGGSSRQSIQKYIKSHYKVGHNADLQIKLSIRRLLAAGVLKQTKGVGASGSFRLAKSDKAKRSPGKKKKAVRRSTSPKKAARPRKARSPAKKPKATARKARKKSRASPKKAKKPKTVKAKSRKASKAKKVKRSKPRAKSGARKSPKKK Limited proteolysis X-ray crystallography 1 21 21 Disordered 101 185 85 Disordered Function arises via a disorder to order transition Protein-DNA binding Aviles, F. J., Chapman, G. E., Kneale, G. G., Crane-Robinson, C., and Bradbury, E. M. A nuclear-magnetic-resonance study of the globular structure of the H5 histone 1978 Eur. J. Biochem. 88 363 371 Ramakrishnan, V., Finch, J. T., Graziano, V., Lee, P. L., and Sweet, R. M. Crystal structure of globular domain of histone H5 and its implications for nucleosome binding 1993 Nature 362 219 223 Graziano, V., Gerchman, S. E., Wonacott, A. J., Sweet, R. M., Wells, J. R., White, S. W., and Ramakrishnan, V. Crystallization of the globular domain of histone H5 1990 J. Mol. Biol. 212 253 257 Crane-Robinson, C. Personal communication PIR: HSCH5 Hypoxanthine Phosphoribosyltransferase 6435814 Q27796 1tc1 B 220 PREYEFAEKILFTEEEIRTRIKEVAKRIADDYKGKGLRPYVNPLVLISVLKGSFMFTADLCRALCDFNVPVRMEFICVSSYGEGLTSSGQVRMLLDTRHSIEGHHVLIVEDIVDTALTLNYLYHMYFTRRPASLKTVVLLDKREGRRVPFSADYVVANIPNAFVIGYGLDYDDTYRELRDIVVLRPEVYAEREAARQKKQRAIGSADTDRDAKREFHSKY X-ray crystallography 190 220 31 Disordered Known to exist in disordered state, relationship to function unknown Unknown Focia, P. J., Craig, S. P., 3rd, Nieves-Alicea, R., Fletterick, R. J., and Eakin, A. E. A 1.4 A crystal structure for the hypoxanthine phosphoribosyltransferase of Trypanosoma cruzi 1998 Biochemistry 37 15066 15075 lymphoid enhancer factor-1 [Rattus sp.] 6537322 Q9QXN1 2lef 397 MPQLSGGGGGGDPELCATDEMIPFKDEGDPQKEKIFAEISHPEEEGDLADIKSSLVNESEIIPASNGHEVVGQTQSSQEPYHDKAREHPDDGKHPDGGLYNKGPSYSSYSGYIMMPNMNSDPYMSNGSLSPPIPRTSNKVPVVQPSHAVHPLTPLITYSDEHFSPGSHPSHIPSEVNPKQGMSRHPPAPEMPTFYPLSPGGVGQITPPLGWQGQPVYPITGGFRQAYPSSLSGDTSMSRFSHHMIPGPPGPHTTGIPHPAIVTPQVKQEHPHTDSDLMHVKPEHEQRKEQEPKRPHIKKPLNAFMLYMKEMRANVVAECTLKESAAINQILGRRWHALSREEQAKYYELARKERQLHMQLYPGWSARDNYGKKKKRKREKLQESTSGTGPRMTAAYI 1 295 295 Undetermined 296 397 102 Disordered Function arises via a disorder to order transition DNA bending Protein-DNA binding Love, J. J., Li, X., Case, D. A., Giese, K., Grosschedl, R., and Wright, P. E. Structural basis for DNA bending by the architectural transcription factor LEF-1 1995 Nature 376 791 795 Myelin basic protein MBP Myelin A1 protein 20 kDa microtubule stabilizing protein 126796 P02687 169 AAQKRPSQRSKYLASASTMDHARHGFLPRHRDTGILDSLGRFFGSDRGAPKRGSGKDGHHAARTTHYGSLPQKAQGHRPQDENPVVHFFKNIVTPRTPPPSQGKGRGLSLSRFSWGAEGQKPGFGYGGRASDYKSAHKGLKGHDAQGTLSKIFKLGGRDSRSGSPMARR Circular dichroism 1 169 169 Disordered Function arises via a disorder to order transition Protein-lipid interaction Polverini, E., Fasano, A., Zito, F., Riccio, P., and Cavatorta, P. Conformation of bovine myelin basic protein purified with bound lipids 1999 Eur. Biophys. J. 28 351 355 Negative factor F-protein 27 kDa protein 3'ORF Negative factor, HIV1 128023 P03406 1avv 206 MGGKWSKSSVVGWPTVRERMRRAEPAADGVGAASRDLEKHGAITSSNTAATNAACAWLEAQEEEEVGFPVTPQVPLRPMTYKAAVDLSHFLKEKGGLEGLIHSQRRQDILDLWIYHTQGYFPDWQNYTPGPGVRYPLTFGWCYKLVPVEPDKVEEANKGENTSLLHPVSLHGMDDPEREVLEWRFDSRLAFHHVARELHPEYFKNC Nuclear magnetic resonance spectroscopy X-ray crystallography 1 73 73 Disordered Function arises from the disordered (extended) state Function arises via a disorder to order transition Fatty acylation (myristolation and palmitoylation) Phosphorylation Protein-lipid interaction Protein-protein binding Regulation of proteolysis in vivo 149 178 30 Disordered Known to exist in disordered state, relationship to function unknown Protein-protein binding 204 206 3 Disordered Lee, C. H., Saksela, K., Mirza, U. A., Chait, B. T., and Kuriyan, J. Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain 1996 Cell 85 931 942 Arold, S., Franken, P., Strub, M. P., Hoh, F., Benichou, S., Benarous, R., and Dumas, C. The crystal structure of HIV-1 Nef protein bound to the Fyn kinase SH3 domain suggests a role for this complex in altered T cell receptor signaling 1997 Structure 5 1361 1372 Geyer, M., Munte, C. E., Schorr, J., Kellner, R., and Kalbitzer, H. R Structure of the anchor-domain of myristoylated and non-myristoylated HIV-1 Nef protein 1999 J. Mol. Biol. 289 123 138 Arold, S. T., and Baur, A. S. Dynamic Nef and Nef dynamics: how structure could explain the complex activities of this small HIV protein 2001 Trends Biochem. Sci. 26 356 363 neural zinc finger factor-1 1511632 P70475 1187 MDVDAEEKRHRTRSKGVRVPVEPAIQELFSCPTPGCDGTGHVSGKYARHRSVYGCPLAKKRKTQDKQPQEPAPKRKPFAVKADSSSVDECYESDGTEDMDDKEEDDDEEFSEDNDEQGDDDDEDEVDREDEEEIEEEDDEDDEDDDDGDDVEEEEDDDDEEEEEEEEEEENEDHQMSCTRIMQDPEKDDNNNDEYDNYDELVAKSLLNLGKIAEDAAYRARTESEVNSNTSNSLEDHSSKNENLGRKSELSLDLDSDVVRETVDSLKLLAQGHGVVLSENISDRSYAEGMSQQDSRNMNYVMLGKPMNNGLMEKMVEESDEEVCLSSLECLRNQCFDLARKLSETNPQDRSQPPNMSVRQHVRQEDDFPGRTPDRSYSDMMNLMRLEEQLSPRSRTFSSCAKEDGCHERDDDTTTVNSDRSEEVFDMTKGNLTLLEKAIALETERAKAMREKMAMDAGRRDNLRSYEDQSPRQLAGEDRKSKSSDSHVKKPYYDPSRTEKRESKCPTPGCDGTGHVNGLYPHHRSLSGCPHKDRVPPEILAMHENVLKCPTPGCTGRGHVNSNRNSHRSLSGCPIAAAEKLAKAQEKHQSCDVSKSNQASDRVLRPMCFVKQLEIPQYGYRNNVPTTTPRSNLAKELEKYSKTSFEYNSYDNHTYGKRAIAPRCKPGTYPPKDMTMPSGTGKNASPSSSTTSSYAPSSSSNLSCGGGSSASSTCSKSSFDYTHDMEAAHMAATAILNLSTRCREMPQNLSTKPQDLCTARNPDMEVDENGTLDLSMNKQRPRDSCCPVLTPLEPMSPQQQAVMSSRCFQLSEGDCWDLPVDYTKMKPRRVDEEDPKEITPEDLDPFQEALEERRYPGEVTIPSPKPKYPQCKESKKDLITLSGCPLADKSIRSMLATSSQELKCPTPGCDGSGHITGNYASHRSLSGCPRAKKSGIRIAQSKEDKEDQEPIRCPVPGCDGQGHITGKYASHRSASGCPLAAKRQKDGYLNGSQFSWKSVKTEGMSCPTPGCDGSGHVSGSFLTHRSLSGCPRATSAMKKAKLSGEQMLTIKQRASNGIENDEEIKQLDEEIKELNESNSQMEADMIKLRTQVTITTMESNLKTIEEENKVIEQQNESLLHELANLSQSLIHSLANIQLPHMDPINEQNFDAYVTTLTEMYTNQDRYQSPENKALLENIKQAVRGIQV Nuclear magnetic resonance spectroscopy 1 486 486 Undetermined 487 606 120 Disordered 607 1187 581 Undetermined Berkovits, H. J., and Berg, J. M. Metal and DNA binding properties of a two-domain fragment of neural zinc finger factor 1, a CCHC-type zinc binding protein 1999 Biochemistry 38 16826 168230 Neurofilament triplet H protein 200 kDa neurofilament protein Neurofilament heavy polypeptide NF-H Neurofilament H 128127 P19246 1087 MSFGSADALLGAPFAPLHGGGSLHYSLSRKAGPGGTRSAAGSSSGFHSWARTSVSSVSASPSRFRGAASSTDSLDTLSNGPEGCVVAAVAARSEKEQLQALNDRFAGYIDKVRQLEAHNRSLEGEAAALRQQKGRAAMGELYEREVREMRGAVLRLGAARGQLRLEQEHLLEDIAHVRQRLDEEARQREEAEAAARALAFAQEAEAARVELQKKAQALQEECGYLRRHHQEEVGELLGQIQGCGAAQAQAQAEARDALKCDVTSALREIRAQLEGHAVQSSLQSEEWFRVRLDRLSEAAKVNTDAMRSAQEEITEYRRQLQARTTELEALKSTKESLERQRSELEDRHQADIASYQDAIQQLDSELRNTKWEMAAQLREYQDLLNVKMALDIEIAAYRKLLEGEECRIGFGPSPFSLTEGLPKIPSISTHIKVKSEEMIKVVEKSEKETVIVEGQTEEIRVTEGVTEEEDKEAQGQEGEEAEEGEEKEEEELAAATSPPAEEAASPEKETKSRVKEEAKSPGEAKSPGEAKSPAEAKSPGEAKSPGEAKSPGEAKSPAEPKSPAEPKSPAEAKSPAEPKSPATVKSPGEAKSPSEAKSPAEAKSPAEAKSPAEAKSPAEAKSPAEAKSPAEAKSPATVKSPGEAKSPSEAKSPAEAKSPAEAKSPAEAKSPAEVKSPGEAKSPAEPKSPAEAKSPAEVKSPAEAKSPAEVKSPGEAKSPAAVKSPAEAKSPAAVKSPGEAKSPGEAKSPAEAKSPAEAKSPIEVKSPEKAKTPVKEGAKSPAEAKSPEKAKSPVKEDIKPPAEAKSPEKAKSPVKEGAKPPEKAKPLDVKSPEAQTPVQEEATVPTDIRPPEQVKSPAKEKAKSPEKEEAKTSEKVAPKKEEVKSPVKEEVKAKEPPKKVEEEKTLPTPKTEAKESKKDEAPKEAPKPKVEEKKETPTEKPKDSTAEAKKEEAGEKKKAVASEEETPAKLGVKEEAKPKEKTETTKTEAEDTKAKEPSKPTETEKPKKEEMPAAPEKKDTKEEKTTESRKPEEKPKMEAKVKEDDKSLSKEPSKPKTEKAEKSSSTDQKESQPPEKTTEDKATKGEK Other techniques 409 1087 679 Disordered Function arises from the disordered (extended) state Entropic bristle Glycosylation Phosphorylation Brown, H. G., and Hoh, J. H. Entropic exclusion by neurofilament sidearms: a mechanism for maintaining interfilament spacing 1997 Biochemistry 36 15035 15040 Hoh, J. H. Functional protein domains from the thermally driven motion of polypeptide chains: a proposal 1998 Proteins 32 223 228 Ornithine Decarboxylase 7404357 P07805 2tod B 425 GAMDIVVNDDLSCRFLEGFNTRDALCKKISMNTCDEGDPFFVADLGDIVRKHETWKKCLPRVTPFYAVACNDDWRVLGTLAALGTGFDCASNTEIQRVRGIGVPPEKIIYANPCKQISHIRYARDSGVDVMTFDCVDELEKVAKTHPKAKMVLRISTDDSLARCRLSVKFGAKVEDCRFILEQAKKLNIDVTGVSFHVGSGSTDASTFAQAISDSRFVFDMGTELGFNMHILDIGGGFPGTRDAPLKFEEIAGVINNALEKHFPPDLKLTIVAEPGRYYVASAFTLAVNVIAKKVTPGVQTDVGAHAESNAQSFMYYVNDGVYGSFNCILYDHAVVRPLPQREPIPNEKLYPSSVWGPTCDGLDQIVERYYLPEMQVGEWLLFEDMGAYTVVGTSSFNGFQSPTIYYVVSGLPDHVVRELKSQKS X-ray crystallography 1 36 36 Disordered Known to exist in disordered state, relationship to function unknown Unknown Grishin, N. V., Osterman, A. L., Brooks, H. B., Phillips, M. A., and Goldsmith, E. J. X-ray structure of ornithine decarboxylase from Trypanosoma brucei: the native structure and the structure in complex with alpha-difluoromethylornithine 1999 Biochemistry 38 15174 15184 SPARC precursor Secreted protein acidic and rich in cysteine Osteonectin ON Basement membrane protein BM-40 129284 P07214 302 MRAWIFFLLCLAGRALAAPQQTEVAEEIVEEETVVEETGVPVGANPVQVEMGEFEDGAEETVEEVVADNPCQNHHCKHGKVCELDESNTPMCVCQDPTSCPAPIGEFEKVCSNDNKTFDSSCHFFATKCTLEGTKKGHKLHLDYIGPCKYIAPCLDSELTEFPLRMRDWLKNVLVTLYERDEGNNLLTEKQKLRVKKIHENEKRLEAGDHPVELLARDFEKNYNMYIFPVHWQFGQLDQHPIDGYLSHTELAPLRAPLIPMEHCTTRFFETCDLDNDKYIALEEWAGCFGIKEQDINKDLVI Circular dichroism 1 17 17 Undetermined 18 302 285 Disordered Engel, J., Taylor, W., Paulsson, M., Sage, H., and Hogan, B. Calcium binding domains and calcium-induced conformational transition of SPARC/BM-40/osteonectin, an extracellular glycoprotein expressed in mineralized and nonmineralized tissues 1987 Biochemistry 26 6958 6965 Phenylalanyl-tRNA synthetase alpha chain Phenylalanine--tRNA ligase alpha chain PheRS 135112 P27001 1b70 A 350 MLEEALAAIQNARDLEELKALKARYLGKKGLLTQEMKGLSALPLEERRKRGQELNAIKAALEAALEAREKALEEAALKEALERERVDVSLPGASLFSGGLHPITLMERELVEIFRALGYQAVEGPEVESEFFNFDALNIPEHHPARDMWDTFWLTGEGFRLEGPLGEEVEGRLLLRTHTSPMQVRYMVAHTPPFRIVVPGRVFRFEQTDATHEAVFHQLEGLVVGEGIAMAHLKGAIYELAQALFGPDSKVRFQPVYFPFVEPGAQFAVWWPEGGKWLELGGAGMVHPKVFQAVDAYRERLGLPPAYRGVTGFAFGLGVERLAMLRYGIPDIRYFFGGRLKFLEQFKGVL X-ray crystallography 1 85 85 Disordered Function arises via a disorder to order transition Protein-tRNA binding Mosyak, L., Reshetnikova, L., Goldgur, Y., Delarue, M., and Safro, M. G. Structure of phenylalanyl-tRNA synthetase from Thermus thermophilus 1995 Nat. Struct. Biol. 2 537 547 Goldgur, Y., Mosyak, L., Reshetnikova, L., Ankilova, V., Lavrik, O., Khodyreva, S., and Safro, M. The crystal structure of phenylalanyl-tRNA synthetase from thermus thermophilus complexed with cognate tRNAPhe 1997 Structure 5 59 68 Chain A, Phosphatidylinositol Phosphate Kinase Type Ii Beta 3745771 P78356 1bo1 A 416 MSSNCTSTTAVAVAPLSASKTKTKKKHFVCQKVKLFRASEPILSVLMWGVNHTINELSNVPVPVMLMPDDFKAYSKIKVDNHLFNKENLPSRFKFKEYCPMVFRNLRERFGIDDQDYQNSVTRSAPINSDSQGRCGTRFLTTYDRRFVIKTVSSEDVAEMHNILKKYHQFIVECHGNTLLPQFLGMYRLTVDGVETYMVVTRNVFSHRLTVHRKYDLKGSTVAREASDKEKAKDLPTFKDNDFLNEGQKLHVGEESKKNFLEKLKRDVEFLAQLKIMDYSLLVGIHDVDRAEQEEMEVEERAEDEECENDGVGGNLLCSYGTPPDSPGNLLSFPRFFGPGEFDPSVDVYAMKSHESSPKKEVYFMAIIDILTPYDTKKKAAHAAKTVKHGAGAEISTVNPEQYSKRFNEFMSNILT X-ray crystallography 1 33 33 Disordered Known to exist in disordered state, relationship to function unknown Unknown 307 341 35 Disordered Known to exist in disordered state, relationship to function unknown Unknown Rao, V. D., Misra, S., Boronenkov, I. V., Anderson, R. A., and Hurley, J. H. Structure of type IIbeta phosphatidylinositol phosphate kinase: a protein kinase fold flattened for interfacial phosphorylation 1998 Cell 94 829 839 Phospholipase C Delta-1 PLC-Delta-1 130228 P10688 1qat A 622 MDQRQKLQHWIHSCLRKADKNKDNKMNFKELKDFLKELNIQVDDGYARKIFRECDHSQTDSLEDEEIETFYKMLTQRAEIDRAFEEAAGSAETLSVERLVTFLQHQQREEEAGPALALSLIERYEPSETAKAQRQMTKDGFLMYLLSADGNAFSLAHRRVYQDMDQPLSHYLVSSSHNTYLLEDQLTGPSSTEAYIRALCKGCRCLELDCWDGPNQEPIIYHGYTFTSKILFCDVLRAIRDYAFKASPYPVILSLENHCSLEQQRVMARHLRAILGPILLDQPLDGVTTSLPSPEQLKGKILLKGKKLGGLLPAGGENGSEATDVSDEVEAAEMEDEAVRSQVQHKPKEDKLKLVPELSDMIIYCKSVHFGGFSSPGTSGQAFYEMASFSESRALRLLQESGNGFVRHNVSCLSRIYPAGWRTDSSNYSPVEMWNGGCQIVALNFQTPGPEMDVYLGCFQDNGGCGYVLKPAFLRDPNTTFNSRALTQGPWWRPERLRVRIISGQQLPKVNKNKNSIVDPKVIVEIHGVGRDTGSRQTAVITNNGFNPRWDMEFEFEVTVPDLALVRFMVEDYDSSSKNDFIGQSTIPWNSLKQGYRHVHLLSKNGDQHPSATLFVKISIQD 1 71 71 Disordered 311 352 42 Disordered Grobler, J. A., Essen, L. O., Williams, R. L., and Hurley, J. H. C2 domain conformational changes in phospholipase C-delta 1 1996 Nat. Struct. Biol. 3 788 795 Essen, L. O., Perisic, O., Cheung, R., Katan, M., and Williams, R. L. Crystal structure of a mammalian phosphoinositide-specific phospholipase C delta 1996 Nature 380 595 602 prion protein 200527 P04925 254 MANLGYWLLALFVTMWTDVGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGTWGQPHGGGWGQPHGGSWGQPHGGSWGQPHGGGWGQGGGTHNQWNKPSKPKTNLKHVAGAAAAGAVVGGLGGYMLGSAVSRPMIHFGNDWEDRYYRENMYRYPNQVYYRPVDQYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCVTQYQKESQAYYDGRRSSSTVLFSSPPVILLISFLIFLIVG Nuclear magnetic resonance spectroscopy 1 22 22 Undetermined 23 119 97 Disordered Function arises via a disorder to order transition Metal binding 231 254 24 Undetermined Lopez Garcia, F., Zhan, R., Riek, R., and Wulthrich, K. NMR structure of the bovine prion protein 2000 Proc Natl. Acad. Sci. USA 97 8334 8339 Also, GI: 130914 Sperm histone Protamine Galline 123705 P15340 62 MARYRRSRTRSRSPRSRRRRRRSGRRRSPRRRRRYGSARRSRRSVGGRRRRYGSRRRRRRRY Circular dichroism 1 62 62 Disordered Function arises via a disorder to order transition Metal binding Protein-DNA binding Gatewood, J. M., Schroth, G. P., Schmid, C. W., and Bradbury, E. M. Zinc-induced secondary structure transitions in human sperm protamines 1990 J. Biol. Chem. 265 20667 20672 Prothymosin alpha 135836 P06302 112 MSDAAVDTSSEITTKDLKEKKEVVEEAENGRDAPANGNAQNEENGEQEADNEVDEEEEEGGEEEEEEEEGDGEEEDGDEDEEAEAPTGKRVAEDDEDDDVETKKQKKTDEDD Circular dichroism 1 112 112 Disordered Known to exist in disordered state, relationship to function unknown Protein-protein binding Gast, K., Damaschun, H., Eckert, K., Schulze-Forster, K., Maurer, H. R., Muller-Frohne, M., Zirwer, D., Czarnecki, J., and Damaschun, G. Prothymosin alpha: a biologically active protein with random coil conformation 1995 Biochemistry 34 13211 13218 Myc proto-oncogene protein c-myc 127619 P01106 1A93 439 MPLNVSFTNRNYDLDYDSVQPYFYCDEEENFYQQQQQSELQPPAPSEDIWKKFELLPTPPLSPSRRSGLCSPSYVAVTPFSLRGDNDGGGGSFSTADQLEMVTELLGGDMVNQSFICDPDDETFIKNIIIQDCMWSGFSAAAKLVSEKLASYQAARKDSGSPNPARGHSVCSTSSLYLQDLSAAASECIDPSVVFPYPLNDSSSPKSCASQDSSAFSPSSDSLLSSTESSPQGSPEPLVLHEETPPTTSSDSEEEQEDEEEIDVVSVEKRQAPGKRSESGSPSAGGHSKPPHSPLVLKRCHVSTHQHNYAAPPSTRKDYPAAKRVKLDSVRVLRQISNNRKCTSPRSSDTEENVKRRTHNVLERQRRNELKRSFFALRDQIPELENNEKAPKVVILKKATAYILSVQAEEQKLISEEDLLRKRREQLKHKLEQLRNSCA Circular dichroism 1 143 143 Disordered Function arises via a disorder to order transition Protein-protein binding 144 439 296 Undetermined McEwan, I. J., Dahlman-Wright, K., Ford, J., and Wright, A. P. Functional interaction of the c-Myc transactivation domain with the TATA binding protein: evidence for an induced fit model of transactivation domain folding 1996 Biochemistry 35 9584 9593 Chain A, PvuII Dna Methyltransferase Cytosine-N4-Specific 6729995 P11409 1boo A 323 MLNFGKKPAYTTSNGSMYIGDSLELLESFPEESISLVMTSPPFALQRKKEYGNLEQHEYVDWFLSFAKVVNKKLKPDGSFVVDFGGAYMKGVPARSIYNFRVLIRMIDEVGFFLAEDFYWFNPSKLPSPIEWVNKRKIRVKDAVNTVWWFSKTEWPKSDITKVLAPYSDRMKKLIEDPDKFYTPKTRPSGHDIGKSFSKDNGGSIPPNLLQISNSESNGQYLANCKLMGIKAHPARFPAKLPEFFIRMLTEPDDLVVDIFGGSNTTGLVAERESRKWISFEMKPEYVAASAFRFLDNNISEEKITDIYNRILNGESLDLNSII X-ray crystallography 166 203 38 Disordered Function arises via a disorder to order transition Protein-DNA binding Regulation of proteolysis in vivo Gong, W., O'Gara, M., Blumenthal, R. M., and Cheng, X. Structure of pvu II DNA-(cytosine N4) methyltransferase, an example of domain permutation and protein fold assignment 1997 Nucleic Acids Research 25 2702 2715 Replication protein A 70 kDa DNA-binding subunit RP-A RF-A Replication factor-A protein 1 Single-stranded DNA-binding protein 1350579 P27694 1ewi 616 MVGQLSEGAIAAIMQKGDTNIKPILQVINIRPITTGNSPPRYRLLMSDGLNTLSSFMLATQLNPLVEEEQLSSNCVCQIHRFIVNTLKDGRRVVILMELEVLKSAEAVGVKIGNPVPYNEGLGQPQVAPPAPAASPAASSRPQPQNGSSGMGSTVSKAYGASKTFGKAAGPSLSHTSGGTQSKVVPIASLTPYQSKWTICARVTNKSQIRTWSNSRGEGKLFSLELVDESGEIRATAFNEQVDKFFPLIEVNKVYYFSKGTLKIANKQFTAVKNDYEMTFNNETSVMPCEDDHHLPTVQFDFTGIDDLENKSKDSLVDIIGICKSYEDATKITVRSNNREVAKRNIYLMDTSGKVVTATLWGEDADKFDGSRQPVLAIKGARVSDFGGRSLSVLSSSTIIANPDIPEAYKLRGWFDAEGQALDGVSISDLKSGGVGGSNTNWKTLYEVKSENLGQGDKPDYFSSVATVVYLRKENCMYQACPTQDCNKKVIDQQNGLYRCEKCDTEFPNFKYRMILSVNIADFQENQWVTCFQESAEAILGQNAAYLGELKDKNEQAFEEVFQNANFRSFIFRVRVKVETYNDESRIKATVMDVKPVDYREYGRRLVMSIRRSALM Nuclear magnetic resonance spectroscopy 115 168 54 Disordered Function arises from the disordered (extended) state Flexible linkers/spacers Jacobs, D. M., Lipton, A. S., Isern, N. G., Daughdrill, G. W., Lowry, D. F., Gomes, X., and Wold, M. S. Human replication protein A: global fold of the N-terminal RPA-70 domain reveals a basic cleft and flexible C-terminal linker 1999 J. Biomol. NMR 14 321 331 Also, PDB: 1fgu retinoid X receptor, alpha [Homo sapiens] 4506755 P19793 1lbd 462 MDTKHFLPLDFSTQVNSSLTSPTGRGSMAAPSLHPSLGPGIGSPGQLHSPISTLSSPINGMGPPFSVISSPMGPHSMSVPTTPTLGFSTGSPQLSSPMNPVSSSEDIKPPLGLNGVLKVPAHPSGNMASFTKHICAICGDRSSGKHYGVYSCEGCKGFFKRTVRKDLTYTCRDNKDCLIDKRQRNRCQYCRYQKCLAMGMKREAVQEERQRGKDRNENEVESTSSANEDMPVERILEAELAVEPKTETYVEANMGLNPSSPNDPVTNICQAADKQLFTLVEWAKRIPHFSELPLDDQVILLRAGWNELLIASFSHRSIAVKDGILLATGLHVHRNSAHSAGVGAIFDRVLTELVSKMRDMQMDKTELGCLRAIVLFNPDSKGLSNPAEVEALREKVYASLEAYCKHKYPEQPGRFAKLLLRLPALRSIGLKCLEHLFFFKLIGDTPIDTFLMEMLEAPHQMT Nuclear magnetic resonance spectroscopy 1 129 129 Undetermined 130 224 95 Disordered Function arises via a disorder to order transition Metal binding Protein-DNA binding Holmbeck, S. M., Foster, M. P., Casimiro, D. R., Sem, D. S., Dyson, H. J., and Wright, P. E. High-resolution solution structure of the retinoid X receptor DNA-binding domain 1998 J. Mol. Biol. 281 271 284 Also, PDB: 1rxr Regulator of G-protein signaling 4 RGS4 RGP4 Signal transduction inhibitor RGS4 1710149 P49799 1agr E 205 MCKGLAGLPASCLRSAKDMKHRLGFLLQKSDSCEHSSSHSKKDKVVTCQRVSQEEVKKWAESLENLINHECGLAAFKAFLKSEYSEENIDFWISCEEYKKIKSPSKLSPKAKKIYNEFISVQATKEVNLDSCTREETSRNMLEPTITCFDEAQKKIFNLMEKDSYRRFLKSRFYLDLTNPSSCGAEKQKGAKSSADCTSLVPQCA X-ray crystallography 1 50 50 Disordered Known to exist in disordered state, relationship to function unknown Protein-protein binding 179 205 27 Disordered Known to exist in disordered state, relationship to function unknown Unknown Tesmer, J. J., Berman, D. M., Gilman, A. G., and Sprang, S. R Structure of RGS4 bound to AlF4--activated G(i alpha1): stabilization of the transition state for GTP hydrolysis 1997 Cell 89 251 261 Moy, F. J., Chanda, P. K., Cockett, M. I., Edris, W., Jones, P. G., Mason, K., Semus, S., and Powers, R. NMR structure of free RGS4 reveals an induced conformational change upon binding Galpha 2000 Biochemistry 39 7063 7073 Chatterjee, T. K., and Fisher, R. A. Novel alternative splicing and nuclear localization of human RGS12 gene products 2000 J. Biol. Chem. 275 24013 24021 Southern Bean Mosaic Virus Coat Protein Southern bean mosaic virus capsid 116795 P03607 4sbv C 261 MATRLTKKQLAQAIQNTLPNPPRRKRRAKRRAAQVPKPTQAGVSMAPIAQGTMVKLRPPMLRSSMDVTILSHCELSTELAVTVTIVVTSELVMPFTVGTWLRGVAQNWSKYAWVAIRYTYLPSCPTTTSGAIHMGFQYDMADTLPVSVNQLSNLKGYVTGPVWEGQSGLCFVNNTKCPDTSRAITIALDTNEVSEKRYPFKTATDYATAVGVNANIGNILVPARLVTAMEGGSSKTAVNTGRLYASYTIRLIEPIAAALNL X-ray crystallography 1 39 39 Disordered Function arises via a disorder to order transition Protein-genomic RNA binding Silva, A. M., and Rossmann, M. G. 1985 ACTA Cryst. B41 147 157 Rossmann, M. G., Chandrasekaran, R., Abad-Zapatero, C., Erickson, J. W., and Arnott, S. RNA-protein binding in southern bean mosaic virus 1983 J. Mol. Biol. 166 73 80 sdrD [Staphylococcus aureus] Serine aspartamine repeat protein D 3550594 O86488 1315 MLNRENKTAITRKGMVSNRLNKFSIRKYTVGTASILVGTTLIFGLGNQEAKAAESTNKELNEATTSASDNQSSDKVDMQQLNQEDNTKNDNQKEMVSSQGNETTSNGNKLIEKESVQSTTGNKVEVSTAKSDEQASPKSTNEDLNTKQTISNQEALQPDLQENKSVVNVQPTNEENKKVDAKTESTTLNVKSDAIKSNDETLVDNNSNSNNENNADIILPKSTAPKRLNTRMRIAAVQPSSTEAKNVNDLITSNTTLTVVDADKNNKIVPAQDYLSLKSQITVDDKVKSGDYFTIKYSDTVQVYGLNPEDIKNIGDIKDPNNGETIATAKHDTANNLITYTFTDYVDRFNSVQMGINYSIYMDADTIPVSKNDVEFNVTIGNTTTKTTANIQYPDYVVNEKNSIGSAFTETVSHVGNKENPGYYKQTIYVNPSENSLTNAKLKVQAYHSSYPNNIGQINKDVTDIKIYQVPKGYTLNKGYDVNTKELTDVTNQYLQKITYGDNNSAVIDFGNADSAYVVMVNTKFQYTNSESPTLVQMATLSSTGNKSVSTGNALGFTNNQSGGAGQEVYKIGNYVWEDTNKNGVQELGEKGVGNVTVTVFDNNTNTKVGEAVTKEDGSYLIPNLPNGDYRVEFSNLPKGYEVTPSKQGNNEELDSNGLSSVITVNGKDNLSADLGIYKPKYNLGDYVWEDTNKNGIQDQDEKGISGVTVTLKDENGNVLKTVTTDADGKYKFTDLDNGNYKVEFTTPEGYTPTTVTSGSDIEKDSNGLTTTGVINGADNMTLDSGFYKTPKYNLGNYVWEDTNKDGKQDSTEKGISGVTVTLKNENGEVLQTTKTDKDGKYQFTGLENGTYKVEFETPSGYTPTQVGSGTDEGIDSNGTSTTGVIKDKDNDTIDSGFYKPTYNLGDYVWEDTNKNGVQDKDEKGISGVTVTLKDENDKVLKTVTTDENGKYQFTDLNNGTYKVEFETPSGYTPTSVTSGNDTEKDSNGLTTTGVIKDADNMTLDSGFYKTPKYSLGDYVWYDSNKDGKQDSTEKGIKDVKVTLLNEKGEVIGTTKTDENGKYCFDNLDSGKYKVIFEKPAGLTQTGTNTTEDDKDADGGEVDVTITDHDDFTLDNGYYEEETSDSDSDSDSDSDSDRDSDSDSDSDSDSDSDSDSDSDSDSDSDSDRDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDAGKHTPVKPMSTTKDHHNKAKALPETGNENSGSNNATLFGGLFAALGSLLLFGRRKKQNK Circular dichroism 1 568 568 Undetermined 569 1123 555 Disordered Function arises via a disorder to order transition Flexible linkers/spacers Metal binding 1124 1315 192 Undetermined Josefsson, E., O'Connell, D., Foster, T. J., Durussel, I., and Cox, J. A. The binding of calcium to the B-repeat segment of SdrD, a cell surface protein of Staphylococcus aureus 1998 J. Biol. Chem. 273 31145 31152 Sindbis Virus Capsid, (Wild-Type) Residues 1-264, Tetragonal Crystal Form (Form Ii). 1942972 P27285 1snw 264 MNRGFFNMLGRRPFPAPTAMWRPRRRRQAAPMPARNGLASQIQQLTTAVSALVIGQATRPQNPRPRPPPRQKKQAPKQPPKPKKPKPQEKKKKQPAKTKPGKRQRMALKLEADRLFDVKNEDGDVIGHALAMEGKVMKPLHVKGTIDHPVLSKLKFTKSSAYDMEFAQLPVNMRSEAFTYTSEHPEGFYNWHHGAVQYSGGRFTIPRGVGGRGDSGRPIMDNSGRVVAIVLGGADEGTRTALSVVTWNSKGKTIKTTPEGTEEW X-ray crystallography 1 106 106 Disordered Function arises via a disorder to order transition Protein-genomic RNA binding Choi, H. K., Tong, L., Minor, W., Dumas, P., Boege, U., Rossmann, M. G., and Wengler, G. Structure of Sindbis virus core protein reveals a chymotrypsin-like serine proteinase and the organization of the virion 1991 Nature 354 37 43 Choi, H. K., Lee, S., Zhang, Y. P., McKinney, B. R., Wengler, G., Rossmann, M. G., and Kuhn, R. J. Structural analysis of Sindbis virus capsid mutants involving assembly and catalysis 1996 J. Mol. Biol. 262 151 167 Small Heat Shock Protein Small heat-shock protein HSP16.5 2495337 Q57733 1shs A 147 MFGRDPFDSLFERMFKEFFATPMTGTTMIQSSTGIQISGKGFMPISIIEGDQHIKVIAWLPGVNKEDIILNAVGDTLEIRAKRSPLMITESERIIYSEIPEEEEIYRTIKLPATVKEENASAKFENGVLSVILPKAESSIKKGINIE X-ray crystallography 1 32 32 Disordered Known to exist in disordered state, relationship to function unknown Protein-protein binding Kim, K. K., Kim, R., and Kim, S. H. Crystal structure of a small heat-shock protein 1998 Nature 394 595 599 Kim, R., Kim, K. K., Yokota, H., and Kim, S. H. Small heat shock protein of Methanococcus jannaschii, a hyperthermophile 1998 Proc. Natl. Acad. Sci. USA 95 9129 9133 Synaptosomal-associated protein 25 SNAP-25 Super protein SUP 134583 P13795 1SFC 206 MAEDADMRNELEEMQRRADQLADESLESTRRMLQLVEESKDAGIRTLVMLDEQGEQLERIEEGMDQINKDMKEAEKNLTDLGKFCGLCVCPCNKLKSSDAYKKAWGNNQDGVVASQPARVVDEREQMAISGGFIRRVTNDARENEMDENLEQVSGIIGNLRHMALDMGNEIDTQNRQIDRIMEKADSNKTRIDEANQRATKMLGSG Circular dichroism Limited proteolysis Other techniques X-ray crystallography 1 206 206 Disordered Fasshauer, D., Bruns, D., Shen, B., Jahn, R., and Brunger, A. T. A structural change occurs upon binding of syntaxin to SNAP-25 1997 J. Biol. Chem. 272 4582 4590 Fasshauer, D., Otto, H., Eliason, W. K., Jahn, R., and Brunger, A. T. Structural changes are associated with soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor complex formation 1997 J. Biol. Chem. 272 28036 28041 Fasshauer, D., Eliason, W. K., Brunger, A. T., and Jahn, R. Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly 1998 Biochemistry 37 10354 10362 Canaves, J. M., and Montal, M. Assembly of a ternary complex by the predicted minimal coiled-coil-forming domains of syntaxin, SNAP-25, and synaptobrevin. A circular dichroism study 1998 J. Biol. Chem. 273 34214 32221 Sutton, R. B., Fasshauer, D., Jahn, R., and Brunger, A. T. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution 1998 Nature 395 347 353 Vesicle-associated membrane protein 1 VAMP-1 Synaptobrevin 1 135093 P23763 118 MSAPAQPPAEGTEGTAPGGGPPGPPPNMTSNRRLQQTQAQVEEVVDIIRVNVDKVLERDQKLSELDDRADALQAGASQFESSAAKLKRKYWWKNCKMMIMLGAICAIIVVVIVIYFFT Circular dichroism Limited proteolysis Nuclear magnetic resonance spectroscopy Other techniques X-ray crystallography 1 96 96 Disordered Function arises via a disorder to order transition Protein-protein binding Fasshauer, D., Otto, H., Eliason, W. K., Jahn, R., and Brunger, A. T. Structural changes are associated with soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor complex formation 1997 J. Biol. Chem. 272 28036 28041 Fasshauer, D., Eliason, W. K., Brunger, A. T., and Jahn, R. Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly 1998 Biochemistry 37 10354 10362 Canaves, J. M., and Montal, M. Assembly of a ternary complex by the predicted minimal coiled-coil-forming domains of syntaxin, SNAP-25, and synaptobrevin. A circular dichroism study 1998 J. Biol. Chem. 273 34214 32221 Sutton, R. B., Fasshauer, D., Jahn, R., and Brunger, A. T. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 A resolution 1998 Nature 395 347 353 Hazzard, J., Sudhof, T. C., and Rizo, J. NMR analysis of the structure of synaptobrevin and of its interaction with syntaxin 1999 J. Biomol. NMR 14 203 207 Alpha-synuclein Non-A beta component of AD amyloid Non-A4 component of amyloid precursor NACP 586067 P37840 140 MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPEA Circular dichroism 1 140 140 Disordered Metal binding Polymerization Protein-protein binding Weinreb, P. H., Zhen, W., Poon, A. W., Conway, K. A., and Lansbury, P. T., Jr. NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded 1996 Biochemistry 35 13709 13715 Nielsen, M. S., Vorum, H., Lindersson, E., and Jensen, P. H. Ca2+ binding to alpha-synuclein regulates ligand binding and oligomerization 2001 J. Biol. Chem. 18 18 Thyroid transcription factor 1 Thyroid nuclear factor 1 TTF-1 Homeobox protein Nkx-2.1 136462 P23441 1ftt 372 MSMSPKHTTPFSVSDILSPLEESYKKVGMEGGGLGAPLAAYRQGQAAPPAAAMQQHAVGHHGAVTAAYHMTAAGVPQLSHSAVGGYCNGNLGNMSELPPYQDTMRNSASGPGWYGANPDPRFPAISRFMGPASGMNMSGMGGLGSLGDVSKNMAPLPSAPRRKRRVLFSQAQVYELERRFKQQKYLSAPEREHLASMIHLTPTQVKIWFQNHRYKMKRQAKDKAAQQQLQQDSGGGGGGGGGAGCPQQQQAQQQSPRRVAVPVLVKDGKPCQAGAPAPGAASLQGHAQQQAQQQAQAAQAAAAAISVGSGGAGLGAHPGHQPGSAGQSPDLAHHAASPAALQGQVSSLSHLNSSGSDYGAMSCSTLLYGRTW Limited proteolysis 1 166 166 Disordered Function arises via a disorder to order transition Protein-protein binding 217 226 10 Disordered 228 372 145 Undetermined Tell, G., Perrone, L., Fabbro, D., Pellizzari, L., Pucillo, C., De Felice, M., Acquaviva, R., Formisano, S., and Damante, G. Structural and functional properties of the N transcriptional activation domain of thyroid transcription factor-1: similarities with the acidic activation domains 1998 Biochem. J. 329 395 403 elastic titin [Homo sapiens] Titin, skeletal 1017427 Q10465 7962 PDQEMPVYPPAIITPLQDTVTSEGQPARFQCRVSGTDLKVSWYSKDKKIKPSRFFRMTQFEDTYQLEIAEAYPEDEGTYTFVANNAVGQVSSTANLSLEAPESILHERIEQEIEMEMKAAPVIKRKIEPLEVALGHLAKFTCEIQSAPNVRFQWFKAGREIYESDKCSIRSSKYISSLEILRTQVVDCGEYTCKASNEYGSVSCTATLTVTEAYPPTFLSRPKSLTTFVGKAAKFICTVTGTPVIETIWQKDGAALSPSPNWRISDAENKHILELSNLTIQDRGVYSCKASNKFGADICQAELIIIDKPHFIKELEPVQSAINKKVHLECQVDEDRKVTVTWSKDGQKLPPGKDYKICFEDKIATLEIPLAKLKDSGTYVCTASNEAGSSSCSATVTVREPPSFVKKVDPSYLMLPGESARLHCKLKGSPVIQVTWFKNNKELSESNTVRMYFVNSEAILDITDVKVEDSGSYSCEAVNDVGSDSCSTEIVIKEPPSFIKTLEPADIVRGTNALLQCEVSGTGPFEISWFKDKKQIRSSKKYRLFSQKSLVCLEIFSFNSADVGEYECVVANEVGKCGCMATHLLKEPPTFVKKVDDLIALGGQTVTLQAAVRGSEPISVTWMKGQEVIREDGKIKMSFSNGVAVLIIPDVQISFGGKYTCLAENEAGSQTSVGELIVKEPAKIIERAELIQVTAGDPATLEYTVAGTPELKPKWYKDGRPLVASKKYRISFKNNVAQLKFYSAELHDSGQYTFEISNEVGSSSCETTFTVLDRDIAPFFTKPLRNVDSVVNGTCRLDCKIAGSLPMRVSWFKDGKEIAASDRYRIAFVEGTASLEIIRVDMNDAGNFTCRATNSVGSKDSSGALIVQEPPSFVTKPGSKDVLPGSAVCLKSTFQGSTPLTIRWFKGNKELVSGGSCYITKEALESSLELYLVKTSDSGTYTCKVSNVAGGVECSANLFVKEPATFVEKLEPSQLLKKGDATQLACKVTGTPPIKITWFANDREIKESSKHRMSFVESTAVLRLTDVGIEDSGEYMCEAQNEAGSDHCSSIVIVKESPYFTKEFKPIEVLKEYDVMLLAEVAGTPPFEITWFKDNTILRSGRKYKTFIQDHLVSLQILKFVAADAGEYQCRVTNEVGSSICSARVTLREPPSFIKKIESTSSLRGGTAAFQATLKGSLPITVTWLKDSDEITEDDNIRMTFENNVASLYLSGIEVKHDGKYVCQAKNDAGIQRCSALLSVKEPATITEEAVSIDVTQGDPATLQVKFSGTKEITAKWFKDGQELTLGSKYKISVTDTVSILKIISTEKKDSGEYTFEVQNDVGRSSCKARINVLDLIIPPSFTKKLKKMDSIKGSFIDLECIVAGSHPISIQWFKDDQEISASEKYKFSFHDNTAFLEISQLEGTDSGTYTCSATNKAGHNQCSGHLTVKEPPYFVEKPQSQDVNPNTRVQLKALVGGTAPMTIKWFKDNKELHSGAARSVWKDDTSTSLELFAAKATDSGTYICQLSNDVGTATSKATLFVKEPPQFIKKPSPVLVLRNGQSTTFECQITGTPKIRVSWYLDGNEITAIQKHGISFIDGLATFQISGARVENSGTYVCEARNDAGTASCSIELKVKEPPTFIRELKPVEVVKYSDVELECEVTGTPPFEVTWLKNNREIRSSKKYTLTDRVSVFNLHITKCDPSDTGEYQCIVSNEGGSCSCSTRVALKEPPSFIKKIENTTTVLKSSATFQSTVAGSPPISITWLKDDQILDEDDNVYISFVDSVATLQIRSVDNGHSGRYTCQAKNESGVERCYAFLLVQEPAQIVEKAKSVDVTEKDPMTLECVVAGTPELKVKWLKDGKQIVPSRYFSMSFENNVASFRIQSVMKQDSGQYTFKVENDFGSSSCDAYLRVLDQNIPPSFTKKLTKMDKVLGSSIHMECKVSGSLPISAQWFKDGKEISTSAKYRLVCHERSVSLEVNNLELEDTANYTCKVSNVAGDDACSGILTVKEPPSFLVKPGRQQAIPDSTVEFKAILKGTPPFKIKWFKDDVELVSGPKCFIGLEGSTSFLNLYSVDASKTGQYTCHVTNDVGSDSCTTMLLVTEPPKFVKKLEASKIVKAGDSSRLECKIAGSPEIRVVWFRNEHELPASDKYRMTFIDSVAVIQMNNLSTEDSGDFICEAQNPAGSTSCSTKVIVKEPPVFSSFPPIVETLKNAEVSLECELSGTPPFEVVWYKDKRQLRSSKKYKIASKNFHTSIHILNVDTSDIGEYHCKAQNEVGSDTCVCTVKLKEPPRFVSKLNSLTVVAGEPAELQASIEGAQPIFVQWLKEKEEVIRESENIRITFVENVATLQFAKAEPANAGKYICQIKNDGGMRENMATLMVLEPAVIVEKAGPMTVTVGETCTLECKVAGTPELSVEWYKDGKLLTSSQKHKFSFYNKISSLRILSVERQDAGTYTFQVQNNVGKSSCTAVVDVSDRAVPPSFTRRLKNTGGVLGASCILECKVAGSSPISVAWFHEKTKIVSGAKYQTTFSDNVCTLQLNSLDSSDMGNYTCVAANVAGSDECRAVLTVQEPPSFVKEPEPLEVLPGKNVTFTSVIRGTPPFKVNWFRGARELVKGDRCNIYFEDTVAELELFNIDISQSGEYTCVVSNNAGQASCTTRLFVKEPAAFLKRLSDHSVEPGKSIILESTYTGTLPISVTWKKDGFNITTSEKCNIVTTEKTCILEILNSTKRDAGQYSCEIENEAGRDVCGALVSTLEPPYFVTELEPLEAAVGDSVSLQCQVAGTPEITVSWYKGDTKLRPTPEYRTYFTNNVATLVFNKVNINDSGEYTCKAENSIGTASSKTVFRIQERQLPPSFARQLKDIEQTVGLPVTLTCRLNGSAPIQVCWYRDGVLLRDHENLQTSFVDNVATLKILQTDLSHSGQYSCSASNPLGTASSSARLTAREPKKSPFFDIKPVSIDVIAGESADFECHVTGAQPMRITWSKDNKEIRPGGNYTITCVGNTPHLRILKVGKGDSGQYTCQATNDVGKDMCSAQLSVKEPPKFVKKLEASKVAKQGESIQLECKISGSPEIKVSWFRNDSELHESWKYNMSFINSVALLTINEASAEDSGDYICEAHNGVGDASCSTALTVKAPPVFTQKPSPVGALKGSDVILQCEISGTPPFEVVWVKDRKQVRNSKKFKITSKHFDTNLHILNLEASDVGEYHCKATNEVGSDTCSCSVKFKEPPRFVKKLSDTSTLIGDAVELRAIVEGFQPISVVWLKDRGEVIRESENTRISFIDNIATLQLGSPEASNSGKYICQIKNDAGMRECSAVLTVLEPARIIEKPEPMTVTTGNPFALECVVTGTPELSAKWFKDGRELSADSKHHITFINKVASLKIPCAEMSDKGLYSFEVKNSVGKSNCTVSVHVSDRIVPPSFIRKLKDVNAILGASVVLECRVSGSAPISVGWFQDGNEIVSGPKCQSSFSENVCTLNLSLLEPSDTGIYTCVAANVAGSDECSAVLTVQEPPSFEQTPDSVEVLPGMSLTFTSVIRGTPPFKVKWFKGSRELVPGESCNISLEDFVTELELFEVQPLESGDYSCLVTNDAGSASCTTHLFVKEPATFVKRLADFSVETGSPIVLEATYTGTPPISVSWIKDEYLISQSERCSITMTEKSTILEILESTIEDYAQYSCLIENEAGQDICEALVSVLEPPYFIEPLEHVEAVIGEPATLQCKVDGTPEIRISWYKEHTKLRSAPAYKMQFKNNVASLVINKVDHSDVGEYSCKADNSVGAVASSAVLVIKARKLPPFFARKLKDVHETLGFPVAFECRINGSEPLQVSWYKDGVLLKDDANLQTSFVHNVATLQILQTDQSHIGQYNCSASNPLGTASSSAKLILSEHEVPPFFDLKPVSVDLALGESGTFKCHVTGTAPIKITWAKDNREIRPGGNYKMTLVENTATLTVLKVGKGDAGQYTCYASNIAGKDSCSAQLGVQEPPRFIKKLEPSRIVKQDEFTRYECKIGGSPEIKVLWYKDETEIQESSKFRMSFVDSVAVLEMHNLSVEDSGDYTCEAHNAAGSASSSTSLKVKEPPIFRKKPHPIETLKGADVHLECELQGTPPFHVSWYKDKRELRSGKKYKIMSENFLTSIHILNVDAADIGEYQCKATNDVGSDTCVGSIALKAPPRFVKKLSDISTVVGKEVQLQTTIEGAEPISVVWFKDKGEIVRESDNIWISYSENIATLQFSRVEPANAGKYTCQIKNDAGMQECFATLSVLEPATIVEKPESIKVTTGDTCTLECTVAGTPELSTKWFKDGKELTSDNKYKISFFNKVSGLKIINVAPSDSGVYSFEVQNPVGKDSCTASLQVSDRTVPPSFTRKLKETNGLSGSSVVMECKVYGSPPISVSWFHEGNEISSGRKYQTTLTDNTCALTVNMLEESDSGDYTCIATNMAGSDECSAPLTVREPPSFVQKPDPMDVLTGTNVTFTSIVKGTPPFSVSWFKGSSELVPGDRCNVSLEDSVAELELFDVDTSQSGEYTCIVSNEAGKASCTTHLYIKAPAKFVKRLNDYSIEKGKPLILEGTFTGTPPISVTWKKNGINVTPSQRCNITTTEKSPILEIPSSTVEDAGQYNCYIENASGKDSCSAQILILEPPYFVKQLEPVKVSVGDSASLQCQLAGTPEIGVSWYKGDTKLRPTTTYKMHFRNNVATLVFNQVDINDSGEYICKAENSVGEVSASTFLTVQEQKLPPSFSRQLRDVQETVGLPVVFDCAISGSEPISVSWYKDGKPLKDSPNVQTSFLDNTATLNIFKTDRSLAGQYSCTATNPIGSASSSARLILTEGKNPPFFDIRLAPVDAVVGESADFECHVTGTQPIKVSWAKDSREIRSGGKYQISYLENSAHLTVLKVDKGDSGQYTCYAVNEVGKDSCTAQLNIKERLIPPSFTKRLSETVEETEGNSFKLEGRVAGSQPITVAWYKNNIEIQPTSNCEITFKNNTLVLQVRKAGMNDAGLYTCKVSNDAGSALCTSSIVIKEPKKPPVFDQHLTPVTVSEGEYVQLSCHVQGSEPIRIQWLKAGREIKPSDRCSFSFASGTAVLELRDVAKADSGDYVCKASNVAGSDTTKSKVTIKDKPAVAPATKKAAVDGRLFFVSEPQSIRVVEKTTATFIAKVGGDPIPNVKWTKGKWRQLNQGGRVFIHQKGDEAKLEIRDTTKTDSGLYRCVAFNEHGEIESNVNLQVDERKKQEKIEGDLRAMLKKTPILKKGAGEEEEIDIMELLKNVDPKEYEKYARMYGITDFRGLLQAFELLKQSQEEETHRLEIEEIERSERDEKEFEELVSFIQQRLSQTEPVTLIKDIENQTVLKDNDAVFEIDIKINYPEIKLSWYKGTEKLEPSDKFEISIDGDRHTLRVKNCQLKDQGNYRLVCGPHIASAKLTVIEPAWERHLQDVTLKEGQTCTMTVQFSVPNVKSEWFRNGRILKPQGRHKTEVEHKVHKLTIADVRAEDQGQYTCKYEDLETSAELRIEAEPIQFTKRIQNIVVSEHQSATFECEVSFDDAIVTWYKGPTELTESQKYNFRNDGRCHYMTIHNVTPDDEGVYSVIARLEPRGEARSTAELYLTTKEIKLELKPPDIPDSRVPIPTMPIRAVPPEEIPPVVAPPVPLLLPTPEEKKPPPKRIEVTKKAVKKDAKKVVAKPKEMTPREEIVKKPPPPTTLIPAKAPEIIDVSSKAEEVKIMTITRKKEVQKEKEAVYEKKQAVHKEKRVFIESFEEPYDELEVEPYTEPFEQPYYEEPDEDYEEIKVEAKKEVHEEWEEDFEEGQEYYEREEGYDEGEEEWEEAYQEREVIQVQKEVYEESHERKVPAKVPEKKAPPPPKVIKKPVIEKIEKTSRRMEEEKVQVTKVPEVSKKIVPQKPSRTPVQEEVIEVKVPAVHTKKMVISEEKMFFASHTEEEVSVTVPEVQKEIVTEEKIHVAVSKRVEPPPKVPELPEKPAPEEVAPVPIPKKVEPPAPKVPEVPKKPVPEEKKPVPVPKKEPAAPPKVPEVPKKPVPEEKIPVPVAKKKEAPPAKVPEVQKGVVTEEKITIVTQREESPPPAVPEIPKKKVPEERKPVPRKEEEVPPPPKVPALPKKPVPEEKVAVPVPVAKKAPPPRAEVSKKTVVEEKRFVAEEKLSFAVPQRVEVTRHEVSAEEEWSYSEEEEGVSISVYREEEREEEEEAEVTEYEVMEEPEEYVVEEKLHIISKRVEAEPAEVTERQEKKIVLKPKIPAKIEEPPPAKVPEAPKKIVPEKKVPAPVPKKEKVPPPKVPEEPKKPVPEKKVPPKVIKMEEPLPAKVTEKHMQITQEEKVLVAVTKKEAPPKARVPEEPKRAVPEEKVLKLKPKREEEPPAKVTEFRKRVVKEEKVSIEAPKREPQPIKEVTIMEEKERAYTLEEEAVSVQREEEYEEYEEYDYKEFEEYEPTEEYDQYEEYEEREYERYEEHEEYITEPEKPIPVKPVPEEPVPTKPKAPPAKVLKKAVPEEKVPVPIPKKLKPPPPKVPEEPKKVFEEKIHISITKREKEQVTEPAAKVPMKPKRVVAEEKVPVPRKEVAPPVRVPEVPKELEPEEVAFEEEVVTHVEEYLVEEEEEYIHEEEEFITEEEVVPVIPVKVPEVPRKPVPEEKKPVPVPKKKEAPPAKVPEVPKKPEEKVPVLIPKKEKPPPAKVPEVPKKPVPEEKVPVPVPKKVEAPPAKVPEVPKKPVPEKKVPVPAPKKVEAPPAKVPEVPKKLIPEEKKPTPVPKKVEAPPPKVPKKREPVPVPVALPQEEEVLFEEEIVPEEEVLPEEEEVLPEEEEVLPEEEEVLPEEEEIPPEEEEVPPEEEYVPEEEEFVPEEEVLPEVKPKVPVPAPVPEIKKKVTEKKVVIPKKEEAPPAKVPEVPKKVEEKRIILPKEEEVLPVEVTEEPEEEPISEEEIPEEPPSIEEVEEVAPPRVPEVIKKAVPEAPTPVPKKVEAPPAKVSKKIPEEKVPVPVQKKEAPPAKVPEVPKKVPEKKVLVPKKEAVPPAKGRTVLEEKVSVAFRQEVVVKERLELEVVEAEVEEIPEEEEFHEVEEYFEEGEFHEVEEFIKLEQHRVEEEHRVEKVHRVIEVFEAEEVEVFEKPKAPPKGPEISEKIIPPKKPPTKVVPRKEPPAKVPEVPKKIVVEEKVRVPEEPRVPPTKVPEVLPPKEVVPEKKVPVPPAKKPEAPPPKVPEAPKEVVPEKKVPVPPPKKPEVPPTKVPEVPKAAVPEKKVPEAIPPKPESPPPEVFEEPEESPSAPPKKPEVPPVRVPEVPKEVVPEKKVPAAPPKKPEVTPVKVPEAPKEVVPEKKVPVPPPKKPEVPPTKVPEVPKVAVPEKKVPEAIPPKPESPPPEVFEEPEEVALEEPPAEVVEEPEPAAPPQVTVPPKNPVPEKKAPAVVAKKPELPPVKVPEVPKEVVPEKKVPLVVPKKPEAPPAKVPEVPKEVVPEKKVAVPKKPEVPPAKVPEVPKKPVLEEKPAVPVPERAESPPPEVYEEPEEIAPEEEIAPEEEKPVPVAEEEEPEVPPPAVPEEPKKIIPEKKVPVIKKPEAPPPKEPEPEKVIEKPKLKPRPPPPPPAPPKEDVKEKIFQLKAIPKKKVPENPQVPEKVELTPLKVPGGEKKVRKLLPERKPEPKEEVVLKSVLRKRPEEEEPKVEPKKLEKVKKPAVPEPPPPKPVEEVEVPTVTKRERKIPEPTKVPEIKPAIPLPAPEPKPKPEAEVKTIKPPPVEPEPTPIAAPVTVPVVGKKAEAKAPKEEAAKPKGPIKGVPKKTPSPIEAERRKLRPGSGGEKPPDEAPFTYQLKAVPLKFVKEIKDIILTESEFVGSSAIFECLVSPSTAITTWMKDGSNIRESPKHRFIADGKDRKLHIIDVQLSDAGEYTCVLRLGNKEKTSTAKLVVEELPVRFVKTLEEEVTVVKGQPLYLSCELNKERDVVWRKDGKIVVEKPGRIVPGVIGLMRALTINDAD Circular dichroism Other techniques 1 5617 5617 Undetermined 5618 7791 2174 Disordered 7792 7962 171 Undetermined Trombitas, K., Greaser, M., Labeit, S., Jin, J. P., Kellermayer, M., Helmes, M., and Granzier, H. Titin extensibility in situ: entropic elasticity of permanently folded and permanently unfolded molecular segments 1998 J. Cell Biol. 140 853 859 Labeit, S., and Kolmerer, B. Titins: giant proteins in charge of muscle ultrastructure and elasticity 1995 Science 270 293 296 Kellermayer, M. S., Smith, S. B., Granzier, H. L., and Bustamante, C. Folding-unfolding transitions in single titin molecules characterized with laser tweezers 1997 Science 276 1112 1116 Helmes, M., Trombitas, K., Centner, T., Kellermayer, M., Labeit, S., Linke, W. A., and Granzier, H. Mechanically driven contour-length adjustment in rat cardiac titin's unique N2B sequence: titin is an adjustable spring 1999 Circ. Res. 84 1339 1352 titin, cardiac muscle [validated] - human Titin, cardiac 2136280 Q10466 26925 MTTQAPTFTQPLQSVVVLEGSTATFEAHISGFPVPEVSWFRDGQVISTSTLPGVQISFSDGRAKLTIPAVTKANSGRYSLKATNGSGQATSTAELLVKAETAPPNFVQRLQSMTVRQGSQVRLQVRVTGIPNPVVKFYRDGAEIQSSLDFQISQEGDLYSLLIAEAYPEDSGTYSVNATNSVGRATSTAELLVQGEEEVPAKKTKTIVSTAQISESRQTRIEKKIEAHFDARSIATVEMVIDGAAGQQLPHKTPPRIPPKPKSRSPTPPSIAAKAQLARQQSPSPIRHSPSPVRHVRAPTPSPVRSVSPAARISTSPIRSVRSPLLMRKTQASTVATGPEVPPPWKQEGYVASSSEAEMRETTLTTSTQIRTEERWEGRYGVQEQVTISGAAGAAASVSASASYAAEAVATGAKEVKQDADKSAAVATVVAAVDMARVREPVISAVEQTAQRTTTTAVHIQPAQEQVRKEAEKTAVTKVVVAADKAKEQELKSRTKEIITTKQEQMHVTHEQIRKETEKTFVPKVVISAAKAKEQETRISEEITKKQKQVTQEAIMKETRKTVVPKVIVATPKVKEQDLVSRGREGITTKREQVQITQEKMRKEAEKTALSTIAVATAKAKEQETILRTRETMATRQEQIQVTHGKVDVGKKAEAVATVVAAVDQARVREPREPGHLEESYAQQTTLEYGYKERISAAKVAEPPQRPASEPHVVPKAVKPRVIQAPSETHIKTTDQKGMHISSQIKKTTDLTTERLVHVDKRPRTASPHFTVSKISVPKTEHGYEASIAGSAIATLQKELSATSSAQKITKSVKAPTVKPSETRVRAEPTPLPQFPFADTPDTYKSEAGVEVKKEVGVSITGTTVREERFEVLHGREAKVTETARVPAPVEIPVTPPTLVSGLKNVTVIEGESVTLECHISGYPSPTVTWYREDYQIESSIDFQITFQSGIARLMIREAFAEDSGRFTCSAVNEAGTVSTSCYLAVQVSEEFEKETTAVTEKFTTEEKRFVESRDVVMTDTSLTEEQAGPGEPAAPYFITKPVVQKLVEGGSVVFGCQVGGNPKPHVYWKKSGVPLTTGYRYKVSYNKQTGECKLVISMTFADDAGEYTIVVRNKHGETSASASLLEEADYELLMKSQQEMLYQTQVTAFVQEPEVGETAPGFVYSEYEKEYEKEQALIRKKMAKDTVVVRTYVEDQEFHISSFEERLIKEIEYRIIKTTLEELLEEDGEEKMAVDISESEAVESGFDLRIKNYRILEGMGVTFHCKMSGYPLPKIAWYKDGKRIKHGERYQMDFLQDGRASLRIPVVLPEDEGIYTAFASNIKGNAICSGKLYVEPAAPLGAPTYIPTLEPVSRIRSLSPRSVSRSPIRMSPARMSPARMSPARMSPARMSPGRRLEETDESQLERLYKPVFVLKPVSFKCLEGANCRFDLKVVGRPMPETFWFHDGQQIVNDYTHKVVIKEDGTQSLIIVPATPSDSGEWTVVAQNRAGRSSISVILTVEAVEHQVKPMFVEKLKNVNIKEGSRLEMKVRATGNPNPDIVWLKNSDIIVPHKYPKIRIEGTKGEAALKIDSTVSQDSAWYTATAINKAGRDTTRCKVNVEVEFAEPEPERKLIIPRGTYRAKEIAAPELEPLHLRYGQEQWEEGDLYDKEKQQKPFFKKKLTSLRLKRFGPAHFECRLTPISDPTMVVEWLHDGKPLEAANRLRMINEFGYCSLDYGVAYSRDSGIITCRATNKYGTDHTSATLIVKDEKSLVEESQLPEGRKGLQRIEELERMAHEGALTGVTTDQKEKQKPDIVLYPEPVRVLEGETARFRCRVTGYPQPKVNWYLNGQLIRKSKRFRVRYDGIHYLDIVDCKSYDTGEVKVTAENPEGVIEHKVKLEIQQREDFRSVLRRAPEPRPEFHVHEPGKLQFEVQKVDRPVDTTETKEVVKLKRAERITHEKVPEESEELRSKFKRRTEEGYYEAITAVELKSRKKDESYEELLRKTKDELLHWTKELTEEEKKALAEEGKITIPTFKPDKIELSPSMEAPKIFERIQSQTVGQGSDAHFRVRVVGKPDPECEWYKNGVKIERSDRIYWYWPEDNVCELVIRDVTAEDSASIMVKAINIAGETSSHAFLLVQAKQLITFTQELQDVVAKEKDTMATFECETSEPFVKVKWYKDGMEVHEGDKYRMHSDRKVHFLSILTIDTSDAEDYSCVLVEDENVKTTAKLIVEGAVVEFVKELQDIEVPESYSGELCIVSPENIEGKWYHNDVELKSNGKYTITSRRGRQNLTVKDVTKEDQGEYSFVIDGKKTTCKLKMKPRPIAILQGLSDQKVCEGDIVQLEVKVSLESVEGVWMKDGQEVQPSDRVHIVIDKQSHMLLIEDMTKEDAGNYSFTIPALGLSTSGRVSVYSVDVITPLKDVNVIEGTKAVLECKVSVPDVTSVKWYLNDEQIKPDDRVQAIVKGTKQRLVINRTHASDEGPYKLIVGRVETNCNLSVEKIKIIRGLRDLTCTETQNVVFEVELSHSGIDVLWNFKDKEIKPSSKYKIEAHGKIYKLTVLNMMKDDEGKYTFYAGENMTSGKLTVAGGAISKPLTDQTVAESQEAVFECEVANPDSKGEWLRDGKHLPLTNNIRSESDGHKRRLIIAATKLDDIGEYTYKVATSKTSAKLKVEAVKIKKTLKNLTVTETQDAVFTVELTHPNVKGVQWIKNGVVLESNEKYAISVKGTIYSLRIKNCAIVDESVYGFRLGRLGASARLHVETVKIIKKPKDVTALENATVAFEVSVSHDTVPVKWFHKSVEIKPSDKHRLVSERKVHKLMLQNISPSDAGEYTAVVGQLECKAKLFVETLHITKTMKNIEVPETKTASFECEVSHFNVPSMWLKNGVEIEMSEKFKIVVQGKLHQLIIMNTSTEDSAEYTFVCGNDQVSATLTVTPIMITSMLKDINAEEKDTITFEVTVNYEGISYKWLKNGVEIKSTDKCQMRTKKLTHSLNIRNVHFGDAADYTFVAGKATSTATLYVEARHIEFRKHIKDIKVLEKKRAMFECEVSEPDITVQWMKDDQELQITDRIKIQKEKYVHRLLIPSTRMSDAGKYTVVAGGNVSTAKLFVEGRDVRIRSIKKEVQVIEKQRAVVEFEVNEDDVDAHWYKDGIEINFQVQERHKYVVERRIHRMFISETRQSDAGEYTFVAGRNRSSVTLYVNAPEPPQVLQELQPVTVQSGKPARFCAMISGRPQPKISWYKEEQLLSTGFKCKFLHDGQEYTLLLIEAFPEDAAVYTCEAKNDYGVATTSASLSVEVPEVVSPDQEMPVYPPAIITPLQDTVTSEGQPARFQCRVSGTDLKVSWYSKDKKIKPSRFFRMTQFEDTYQLEIAEAYPEDEGTYTFVANNAVGQVSSTANLSLEAPESILHERIEQEIEMEMKEFSSSFLSAEEEGLHSAELQLSKINETLELLSESPVYPTKFDSEKEGTGPIFIKEVSNADISMGDVATLSVTVIGIPKPKIQWFFNGVLLTPSADYKFVFDGDDHSLIILFTKLEDEGEYTCMASNDYGKTICSAYLKINSKGEGHKDTETESAVAKSLEKLGGPCPPHFLKELKPIRCAQGLPAIFEYTVVGEPAPTVTWFKENKQLCTSVYYTIIHNPNGSGTFIVNDPQREDSGLYICKAENMLGESTCAAELLVLLEDTDMTDTPCKAKSTPEAPEDFPQTPLKGPAVEALDSEQEIATFVKDTILKAALITEENQQLSYEHIAKANELSSQLPLGAQELQSILEQDKLTPESTREFLCINGSIHFQPLKEPSPNLQLQIVQSQKTFSKEGILMPEEPETQAVLSDTEKIFPSAMSIEQINSLTVEPLKTLLAEPEGNYPQSSIEPPMHSYLTSVAEEVLSLKEKTVSDTNREQRVTLQKQEAQSALILSQSLAEGHVESLQSPDVMISQVNYEPLVPSEHSCTEGGKILIESANPLENAGQDSAVRIEEGKSLRFPLALEEKQVLLKEEHSDNVVMPPDQIIESKREPVAIKKVQEVQGRDLLSKESLLSGIPEEQRLNLKIQICRALQAAVASEQPGLFSEWLRNIEKVEVEAVNITQEPRHIMCMYLVTSAKSVTEEVTIIIEDVDPQMANLKMELRDALCAIIYEEIDILTAEGPRIQQGAKTSLQEEMDSFSGSQKVEPITEPEVESKYLISTEEVSYFNVQSRVKYLDATPVTKGVASAVVSDEKQDESLKPSEEKEESSSESGTEEVATVKIQEAEGGLIKEDGPMIHTPLVDTVSEEGDIVHLTTSITNAKEVNWYFENKLVPSDEKFKCLQDQNTYTLVIDKVNTEDHQGEYVCEALNDSGKTATSAKLTVVKRAAPVIKRKIEPLEVALGHLAKFTCEIQSAPNVRFQWFKAGREIYESDKCSIRSSKYISSLEILRTQVVDCGEYTCKASNEYGSVSCTATLTVTVPGGEKKVRKLLPERKPEPKEEVVLKSVLRKRPEEEEPKVEPKKLEKVKKPAVPEPPPPKPVEEVEVPTVTKRERKIPEPTKVPEIKPAIPLPAPEPKPKPEAEVKTIKPPPVEPEPTPIAAPVTVPVVGKKAEAKAPKEEAAKPKGPIKGVPKKTPSPIEAERRKLRPGSGGEKPPDEAPFTYQLKAVPLKFVKEIKDIILTESEFVGSSAIFECLVSPSTAITTWMKDGSNIRESPKHRFIADGKDRKLHIIDVQLSDAGEYTCVLRLGNKEKTSTAKLVVEELPVRFVKTLEEEVTVVKGQPLYLSCELNKERDVVWRKDGKIVVEKPGRIVPGVIGLMRALTINDADDTDAGTYTVTVENANNLECSSCVKVVEVIRDWLVKPIRDQHVKPKGTAIFACDIAKDTPNIKWFKGYDEIPAEPNDKTEILRDGNHLYLKIKNAMPEDIAEYAVEIEGKRYPAKLTLGEREVELLKPIEDVTIYEKESASFDAEISEADIPGQWKLKGELLRPSPTCEIKAEGGKRFLTLHKVKLDQAGEVLYQALNAITTAILTVKEIELDFAVPLKDVTVPERRQARFECVLTREANVIWSKGPDIIKSSDKFDIIADGKKHILVINDSQFDDEGVYTAEVEGKKTSARLFVTGIRLKFMSPLEDQTVKEGETATFVCELSHEKMHVVWFKNDAKLHTSRTVLISSEGKTHKLEMKEVTLDDISQIKAQVKELSSTAQLKVLEADPYFTVKLHDKTAVEKDEITLKCEVSKDVPVKWFKDGEEIVPSPKYSIKADGLRRILKIKKADLKDKGEYVCDCGTDKTKANVTVEARLIEVEKPLYGVEVFVGETAHFEIELSEPDVHGQWKLKGQPLTASPDCEIIEDGKKHILILHNCQLGMTGEVSFQAANAKSAANLKVKELPLIFITPLSDVKVFEKDEAKFECEVSREPKTFRWLKGTQEITGDDRFELIKDGTKHSMVIKSAAFEDEAKYMFEAEDKHTSGKLIIEGIRLKFLTPLKDVTAKEKESAVFTVELSHDNIRVKWFKNDQRLHTTRSVSMQDEGKTHSITFKDLSIDDTSQIRVEAMGMSSEAKLTVLEGDPYFTGKLQDYTGVEKDEVILQCEISKADAPVKWFKDGKEIKPSKNAVIKTDGKKRMLILKKALKSDIGQYTCDCGTDKTSGKLDIEDREIKLVRPLHSVEVMETETARFETEISEDDIHANWKLKGEALLQTPDCEIKEEGKIHSLVLHNCRLDQTGGVDFQAANVKSSAHLRVKPRVIGLLRPLKDVTVTAGETATFDCELSYEDIPVEWYLKGKKLEPSDKVVPRSEGKVHTLTLRDVKLEDAGEVQLTAKDFKTHANLFVKEPPVEFTKPLEDQTVEEGATAVLECEVSRENAKVKWFKNGTEILKSKKYEIVADGRVRKLVIHDCTPEDIKTYTCDAKDFKTSCNLNVVPPHVEFLRPLTDLQVREKEMARFECELSRENAKVKWFKDGAEIKKGKKYDIISKGAVRILVINKCLLDDEAEYSCEVRTARTSGMLTVLEEEAVFTKNLANIEVSETDTIKLVCEVSKPGAEVIWYKGDEEIIETGRYEILTEGRKRILVIQNAHLEDAGNYNCRLPSSRTDGKVKVHELAAEFISKPQNLEILEGEKAEFVCSISKESFPVQWKRDDKTLESGDKYDVIADGKKRVLVVKDATLQDMGTYVVMVGAARAAAHLTVIEKLRIVVPLKDTRVKEQQEVVFNCEVNTEGAKAKWFRNEEAIFDSSKYIILQKDLVYTLRIRDAHLDDQANYNVSLTNHRGENVKSAANLIVEEEDLRIVEPLKDIETMEKKSVTFWCKVNRLNVTLKWTKNGEEVPFDNRVSYRVDKYKHMLTIKDCGFPDEGEYIVTAGQDKSVAELLIIEAPTEFVEHLEDQTVTEFDDAVFSCQLSREKANVKWYRNGREIKEGKKYKFEKDGSIHRLIIKDCRLDDECEYACGVEDRKSRARLFVEEIPVEIIRPPQDILEAPGADVVFLAELNKDKVEVQWLRNNMVVVQGDKHQMMSEGKIHRLQICDIKPRDQGEYRFIAKDKEARAKLELAAAPKIKTADQDLVVDVGKPLTMVVPYDAYPKAEAEWFKENEPLSTKTIDTTAEQTSFRILEAKKGDKGRYKIVLQNKHGKAEGFINLKVIDVPGPVRNLEVTETFDGEVSLAWEEPLTDGGSKIIGYVVERRDIKRKTWVLATDRAESCEFTVTGLQKGGVEYLFRVSARNRVGTGEPVETDNPVEARSKYDVPGPPLNVTITDVNRFGVSLTWEPPEYDGGAEITNYVIELRDKTSIRWDTAMTVRAEDLSATVTDVVEGQEYSFRVRAQNRIGVGKPSAATPFVKVADPIERPSPPVNLTSSDQTQSSVQLKWEPPLKDGGSPILGYIIERCEEGKDNWIRCNMKLVPELTYKVTGLEKGNKYLYRVSAENKAGVSDPSEILGPLTADDAFVEPTMDLSAFKDGLEVIVPNPITILVPSTGYPRPTATWCFGDKVLETGDRVKMKTLSAYAELVISPSERSDKGIYTLKLENRVKTISGEIDVNVIARPSAPKELKFGDITKDSVHLTWEPPDDDGGSPLTGYVVEKREVSRKTWTKVMDFVTDLEFTVPDLVQGKEYLFKVCARNKCGPGEPAYVDEPVNMSTPATVPDPPENVKWRDRTANSIFLTWDPPKNDGGSRIKGYIVERCPRGSDKWVACGEPVAETKMEVTGLEEGKWYAYRVKTLNRQGASKPSRPTEEIQAVDTQEAPEIFLDVKLLAGLTVKAGTKIELPATVTGKPEPKITWTKADMILKQDKRITIENVPKKSTVTIVDSKRSDTGTYIIEAVNVCGRATAVVEVNVLDKPGPPAAFDITDVTNESCLLTWNPPRDDGGSKITNYVVERRATDSEVWHKLSSTVKDTNFKATKLIPNKEYIFRVAAENMYGAGEPVQASPITAKYQFDPPGPPTRLEPSDITKDAVTLTWCEPDDDGGSPITGYWVERLDPDTDKWVRCNKMPVKDTTYRVKGLTNKKKYRFRVLAENLAGPGKPSKSTEPILIKDPIDPPWPPGKPTVKDVGKTSVRLNWTKPEHDGGAKIESYVIEMLKTGTDEWVRVAEGVPTTQHLLPGLMEGQEYSFRVRAVNKAGESEPSEPSDPVLCREKLYPPSPPRWLEVINITKNTADLKWTVPEKDGGSPITNYIVEKRDVRRKGWQTVDTTVKDTKCTVTPLTEGSLYVFRVAAENAIGQSDYTEIEDSVLAKDTFTTPGPPYALAVVDVTKRHVDLKWEPPKNDGGRPIQRYVIEKKERLGTRWVKAGKTAGPDCNFRVTDVIEGTEVQFQVRAENEAGVGHPSEPTEILSIEDPTSPPSPPLDLHVTDAGRKHIAIAWKPPEKNGGSPIIGYHVEMCPVGTEKWMRVNSRPIKDLKFKVEEGVVPDKEYVLRVRAVNAIGVSEPSEISENVVAKDPDCKPTIDLETHDIIVIEGEKLSIPVPFRAVPVPTVSWHKDGKEVKASDRLTMKNDHISAHLEVPKSVRADAGIYTITLENKLGSATASINVKVIGLPGPCKDIKASDITKSSCKLTWEPPEFDGGTPILHYVLERREAGRRTYIPVMSGENKLSWTVKDLIPNGEYFFRVKAVNKVGGGEYIELKNPVIAQDPKQPPDPPVDVEVHNPTAEAMTITWKPPLYDGGSKIMGYIIEKIAKGEERWKRCNEHLVPILTYTAKGLEEGKEYQFRVRAENAAGISEPSRATPPTKAVDPIDAPKVILRTSLEVKRGDEIALDASISGSPYPTITWIKDENVIVPEEIKKRAAPLVRRRKGEVQEEEPFVLPLTQRLSIDNSKKGESQLRVRDSLRPDHGLYMIKVENDHGIAKAPCTVSVLDTPGPPINFVFEDIRKTSVLCKWEPPLDDGGSEIINYTLEKKDKTKPDSEWIVVTSTLRHCKYSVTKLIEGKEYLFRVRAENRFGPGPPCVSKPLVAKDPFGPPDAPDKPIVEDVTSNSMLVKWNEPKDNGSPILGYWLEKREVNSTHWSRVNKSLLNALKANVDGLLEGLTYVFRVCAENAAGPGKFSPPSDPKTAHDPISPPGPPIPRVTDTSSTTIELEWEPPAFNGGGEIVGYFVDKQLVGTNKWSRCTEKMIKVRQYTVKEIREGADYKLRVSAVNAAGEGPPGETQPVTVAEPQEPPAVELDVSVKGGIQIMAGKTLRIPAVVTGRPVPTKVWTKEEGELDKDRVVIDNVGTKSELIIKDALRKDHGRYVITATNSCGSKFAAARVEVFDVPGPVLDLKPVVTNRKMCLLNWSDPEDDGGSEITGFIIERKDAKMHTWRQPIETERSKCDITGLLEGQEYKFRVIAKNKFGCGPPVEIGPILAVDPLGPPTSPERLTYTERQRSTITLDWKEPRSNGGSPIQGYIIEKRRHDKPDFERVNKRLCPTTSFLVENLDEHQMYEFRVKAVNEIGESEPSLPLNVVIQDDEVPPTIKLRLSVRGDTIKVKAGEPVHIPADVTGLPMPKIEWSKNETVIEKPTDALQITKEEVSRSEAKTELSIPKAVREDKGTYTVTASNRLGSVFRNVHVEVYDRPSPPRNLAVTDIKAESCYLTWDAPLDNGGSEITHYVIDKRDASRKKAEWEEVTNTAVEKRYGIWKLIPNGQYEFRVRAVNKYGISDECKSDKVVIQDPYRLPGPPGKPKVLARTKGSMLVSWTPPLDNGGSPITGYWLEKREEGSPYWSRVSRAPITKVGLKGVEFNVPRLLEGVKYQFRAMAINAAGIGPPSEPSDPEVAGDPIFPPGPPSCPEVKDKTKSSISLGWKPPAKDGGSPIKGYIVEMQEEGTTDWKRVNEPDKLITTCECVVPNLKELRKYRFRVKAVNEAGESEPSDTTGEIPATDIQEEPEVFIDIGAQDCLVCKAGSQIRIPAVIKGRPTPKSSWEFDGKAKKAMKDGVHDIPEDAQLETAENSSVIIIPECKRSHTGKYSITAKNKAGQKTANCRVKVMDVPGPPKDLKVSDITRGSCRLSWKMPDDDGGDRIKGYVIEKRTIDGKAWTKVNPDCGSTTFVVPDLLSEQQYFFRVRAENRFGIGPPVETIQRTTARDPIYPPDPPIKLKIGLITKNTVHLSWKPPKNDGGSPVTHYIVECLAWDPTGTKKEAWRQCNKRDVEELQFTVEDLVEGGEYEFRVKAVNAAGVSKPSATVGPCDCQRPDMPPSIDLKEFMEVEEGTNVNIVAKIKGVPFPTLTWFKAPPKKPDNKEPVLYDTHVNKLVVDDTCTLVIPQSRRSDTGLYTITAVNNLGTASKEMRLNVLGRPGPPVGPIKFESVSADQMTLSWFPPKDDGGSKITNYVIEKREANRKTWVHVSSEPKECTYTIPKLLEGHEYVFRIMAQNKYGIGEPLDSEPETARNLFSVPGAPDKPTVSSVTRNSMTVNWEEPEYDGGSPVTGYWLEMKDTTSKRWKRVNRDPIKAMTLGVSYKVTGLIEGSDYQFRVYAINAAGVGPASLPSDPATARDPIAPPGPPFPKVTDWTKSSADLEWSPPLKDGGSKVTGYIVEYKEEGKEEWEKGKDKEVRGTKLVVTGLKEGAFYKFRVSAVNIAGIGEPGEVTDVIEMKDRLVSPDLQLDASVRDRIVVHAGGVIRIIAYVSGKPPPTVTWNMNERTLPQEATIETTAISSSMVIKNCQRSHQGVYSLLAKNEAGERKKTIIVDVLDVPGPVGTPFLAHNLTNESCKLTWFSPEDDGGSPITNYVIEKRESDRRAWTPVTYTVTRQNATVQGLIQGKAYFFRIAAENSIGMGPFVETSEALVIREPITVPERPEDLEVKEVTKNTVTLTWNPPKYDGGSEIINYVLESRLIGTEKFHKVTNDNLLSRKYTVKGLKEGDTYEYRVSAVNIVGQGKPSFCTKPITCKDELAPPTLHLDFRDKLTIRVGEAFALTGRYSGKPKPKVSWFKDEADVLEDDRTHIKTTPATLALEKIKAKRSDSGKYCVVVENSTGSRKGFCQVNVVDHPGPPVGPVSFDEVTKDYMVISWKPPLDDGGSKITNYIIEKKEVGKDVWMPVTSASAKTTCKVSKLLEGKDYIFRIHAENLYGISDPLVSDSMKAKDRFRVPDAPDQPIVTEVTKDSALVTWNKPHDGGKPITNYILEKRETMSKRWARVTKDPIHPYTKFRVPDLLEGCQYEFRVSAENEIGIGDPSPPSKPVFAKDPIAKPSPPVNPEAIDTTCNSVDLTWQPPRHDGGSKILGYIVEYQKVGDEEWRRANHTPESCPETKYKVTGLRDGQTYKFRVLAVNAAGESDPAHVPEPVLVKDRLEPPELILDANMAREQHIKVGDTLRLSAIIKGVPFPKVTWKKEDRDAPTKARIDVTPVGSKLEIRNAAHEDGGIYSLTVENPAGSKTVSVKVLVLDKPGPPRDLEVSEIRKDSCYLTWKEPLDDGGSVITNYVVERRDVASAQWSPLSATSKKKSHFAKHLNEGNQYLFRVAAENQYGRGPFVETPKPIKALDPLHPPGPPKDLHHVDVDKTEVSLVWNKPDRDGGSPITGYLVEYQEEGTQDWIKFKTVTNLECVVTGLQQGKTYRFRVKAENIVGLGLPDTTIPIECQEKLVPPSVELDVKLIEGLVVKAGTTVRFPAIIRGVPVPTAKWTTDGSEIKTDEHYTVETDNFSSVLTIKNCLRRDTGEYQITVSNAAGSKTVAVHLTVLDVPGPPTGPINILDVTPEHMTISWQPPKDDGGSPVINYIVEKQDTRKDTWGVVSSGSSKTKLKIPHLQKGCEYVFRVRAENKIGVGPPLDSTPTVAKHKFSPPSPPGKPVVTDITENAATVSWTLPKSDGGSPITGYYMERREVTGKWVRVNKTPIADLKFRVTGLYEGNTYEFRVFAENLAGLSKPSPSSDPIKACRPIKPPGPPINPKLKDKSRETADLVWTKPLSDGGSPILGYVVECQKPGTAQWNRINKDELIRQCAFRVPGLIEGNEYRFRIKAANIVGEGEPRELAESVIAKDILHPPEVELDVTCRDVITVRVGQTIRILARVKGRPEPDITWTKEGKVLVREKRVDLIQDLPRVELQIKEAVRADHGKYIISAKNSSGHAQGSAIVNVLDRPGPCQNLKVTNVTKENCTISWENPLDNGGSEITNFIVEYRKPNQKGWSIVASDVTKRLIKANLLANNEYYFRVCAENKVGVGPTIETKTPILAINPIDRPGEPENLHIADKGKTFVYLKWRRPDYDGGSPNLSYHVERRLKGSDDWERVHKGSIKETHYMVDRCVENQIYEFRVQTKNEGGESDWVKTEEVVVKEDLQKPVLDLKLSGVLTVKAGDTIRLEAGVRGKPFPEVAWTKDKDATDLTRSPRVKIDTRADSSKFSLTKAKRSDGGKYVVTATNTAGSFVAYATVNVLDKPGPVRNLKIVDVSSDRCTVCWDPPEDDGGCEIQNYILEKCETKRMVWSTYSATVLTPGTTVTRLIEGNEYIFRVRAENKIGTGPPTESKPVIAKTKYDKPGRPDPPEVTKVSKEEMTVVWNPPEYDGGKSITGYFLEKKEKHSTRWVPVNKSAIPERRMKVQNLLPDHEYQFRVKAENEIGIGEPSLPSRPVVAKDPIEPPGPPTNFRVVDTTKHSITLGWGKPVYDGGAPIIGYVVEMRPKIADASPDEGWKRCNAAAQLVRKEFTVTSLDENQEYEFRVCAQNQVGIGRPAELKEAIKPKEILEPPEIDLDASMRKLVIVRAGCPIRLFAIVRGRPAPKVTWRKVGIDNVVRKGQVDLVDTMAFLVIPNSTRDDSGKYSLTLVNPAGEKAVFVNVRVLDTPGPVSDLKVSDVTKTSCHVSWAPPENDGGSQVTHYIVEKREADRKTWSTVTPEVKKTSFHVTNLVPGNEYYFRVTAVNEYGPGVPTDVPKPVLASDPLSEPDPPRKLEATEMTKNSATLAWLPPLRDGGAKIDGYIISYREEEQPADRWTEYSVVKDLSLVVTGLKEGKKYKFRVAARNAVGVSLPREAEGVYEAKEQLLPPKILMPEQITIKAGKKLRIEAHVYGKPHPTCKWKKGEDEVVTSSHLAVHKADSSSILIIKDVTRKDSGYYSLTAENSSGTDTQKIKVVVMDAPGPPQPPFDISDIDADACSLSWHIPLEDGGSNITNYIVEKCDVSRGDWVTALASVTKTSCRVGKLIPGQEYIFRVRAENRFGISEPLTSPKMVAQFPFGVPSEPKNARVTKVNKDCIFVAWDRPDSDGGSPIIGYLIERKERNSLLWVKANDTLVRSTEYPCAGLVEGLEYSFRIYALNKAGSSPPSKPTEYVTARMPVDPPGKPEVIDVTKSTVSLIWARPKHDGGSKIIGYFVEACKLPGDKWVRCNTAPHQIPQEEYTATGLEEKAQYQFRAIARTAVNISPPSEPSDPVTILAENVPPRIDLSVAMKSLLTVKAGTNVCLDATVFGKPMPTVSWKKDGTLLKPAEGIKMAMQRNLCTLELFSVNRKDSGDYTITAENSSGSKSATIKLKVLDKPGPPASVKINKMYSDRAMLSWEPPLEDGGSEITNYIVDKRETSRPNWAQVSATVPITSCSVEKLIEGHEYQFRICAENKYGVGDPVFTEPAIAKNPYDPPGRCDPPVISNITKDHMTVSWKPPADDGGSPITGYLLEKRETQAVNWTKVNRKPIIERTLKATGLQEGTEYEFRVTAINKAGPGKPSDASKAAYARDPQYPPAPPAFPKVYDTTRSSVSLSWGKPAYDGGSPIIGYLVEVKRADSDNWVRCNLPQNLQKTRFEVTGLMEDTQYQFRVYAVNKIGYSDPSDVPDKHYPKDILIPPEGEHDADLRKTLILRAGVTMRLYVPVKGRPPPKITWSKPNVNLRDRIGLDIKSTDFDTFLRCENVNKYDAGKYILTLENSCGKKEYTIVVKVLDTPGPPINVTVKEISKDSAYVTWEPPIIDGGSPIINYVVQKRDAERKSWSTVTTECSKTSFRVPNLEEGKSYFFRVFAENEYGIGDPGETRDAVKASQTPGPVVDLKVRSVSKSSCSIGWKKPHSDGGSRIIGYVVDFLTEENKWQRVMKSLSLQYSAKDLTEGKEYTFRVSAENENGEGTPSEITVVARDDVVAPDLDLKGLPDLCYLAKENSNFRLKIPIKGKPAPSVSWKKGEDPLATDTRVSVESSAVNTTLIVYDCQKSDAGKYTITLKNVAGTKEGTISIKVVGKPGIPTGPIKFDEVTAEAMTLKWAPPKDDGGSEITNYILEKRDSVNNKWVTCASAVQKTTFRVTRLHEGMEYTFRVSAENKYGVGEGLKSEPIVARHPFDVPDAPPPPNIVDVRHDSVSLTWTDPKKTGGSPITGYHLEFKERNSLLWKRANKTPIRMRDFKVTGLTEGLEYEFRVMAINLAGVGKPSLPSEPVVALDPIDPPGKPEVINITRNSVTLIWTEPKYDGGHKLTGYIVEKRDLPSKSWMKANHVNVPECAFTVTDLVEGGKYEFRIRAKNTAGAISAPSESTETIICKDEYEAPTIVLDPTIKDGLTIKAGDTIVLNAISILGKPLPKSSWSKAGKDIRPSDITQITSTPTSSMLTIKYATRKDAGEYTITATNPFGTKVEHVKVTVLDVPGPPGPVEISNVSAEKATLTWTPPLEDGGSPIKSYILEKRETSRLLWTVVSEDIQSCRHVATKLIQGNEYIFRVSAVNHYGKGEPVQSEPVKMVDRFGPPGPPEKPEVSNVTKNTATVSWKRPVDDGGSEITGYHVERREKKSLRWVRAIKTPVSDLRCKVTGLQEGSTYEFRVSAENRAGIGPPSEASDSVLMKDAAYPPGPPSNPHVTDTTKKSASLAWGKPHYDGGLEITGYVVEHQKVGDEAWIKDTTGTALRITQFVVPDLQTKEKYNFRISAINDAGVGEPAVIPDVEIVEREMAPDFELDAELRRTLVVRAGLSIRIFVPIKGRPAPEVTWTKDNINLKNRANIENTESFTLLIIPECNRYDTGKFVMTIENPAGKKSGFVNVRVLDTARPSPQLRPTDITKDSVTLHWDLPLIDGGSRITNYIVEKREATRKSYSTATTKCHKCTYKVTGLSEGCEYFFRVMAENEYGIGEPTETTEPVKASEAPSPPDSLNIMDITKSTVSLAWPKPKHDGGSKITGYVIEAQRKGSDQWTHITTVKGLECVVRNLTEGEEYTFQVMAVNSAGRSAPRESRPVIVKEQTMLPELDLRGIYQKLVIAKAGDNIKVEIPVLGRPKPTVTWKKGDQILKQTQRVNFETTATSTILNINECVRSDSGPYPLTARNIVGEVGDVITIQVHDIPGPPTGPIKFDEVSSDFVTFSWDPPENDGGVPISNYVVEMRQTDSTTWVELATTVIRTTYKATRLTTGLEYQFRVKAQNRYGVGPGITSAWIVANYPFKVPGPPGTPQVTAVTKDSMTISWHEPLSDGGSPILGYHVERKERNGILWQTVSKALVPGNIFKSSGLTDGIAYEFRVIAENMAGKSKPSKPSEPMLALDPIDPPGKPVPLNITRHTVTLKWAKPEYTGGFKITSYIVEKRDLPNGRWLKANFSNILENEFTVSGLTEDAAYEFRVIAKNAAGAISPPSEPSDAITCRDDVEAPKIKVDVKFKDTVILKAGEAFRLEADVSGRPPPTMEWSKDGKELEGTAKLEIKIADFSTNLVNKDSTRRDSGAYTLTATNPGGFAKHIFNVKVLDRPGPPEGPLAVTEVTSEKCVLSWFPPLDDGGAKIDHYIVQKRETSRLAWTNVASEVQVTKLKVTKLLKGNEYIFRVMAVNKYGVGEPLESEPVLAVNPYGPPDPPKNPEVTTITKDSMVVCWGHPDSDGGSEIINYIVERRDKAGQRWIKCNKKTLTDLRYKVSGLTEGHEYEFRIMAENAAGISAPSPTSPFYKACDTVFKPGPPGNPRVLDTSRSSISIAWNKPIYDGGSEITGYMVEIALPEEDEWQIVTPPAGLKATSYTITGLTENQEYKIRIYAMNSEGLGEPALVPGTPKAEDRMLPPEIELDADLRKVVTIRACCTLRLFVPIKGRPDPEVKWARDHGESLDKASIESASSYTLLIVGNVNRFDSGKYILTVENSSGSKSAFVNVRVLDTPGPPQDLKVKEVTKTSVTLTWDPPLLDGGSKIKNYIVEKRESTRKAYSTVATNCHKTSWKVDQLQEGCSYYFRVLAENEYGIGLPAETAESVKASERPLPPGKITLMDVTRNSVSLSWEKPEHDGGSRILGYIVEMQTKGSDKWATCATVKVTEATITGLIQGEEYSFRVSAQNEKGISDPRQLSVPVIAKDLVIPPAFKLLFNTFTVLAGEDLKVDVPFIGRPTPAVTWHKDNVPLKQTTRVNAESTENNSLLTIKDACREDVGHYVVKLTNSAGEAIETLNVIVLDKPGPPTGPVKMDEVTADSITLSWGPPKYDGGSSINNYIVEKRDTSTTTWQIVSATVARTTIKACRLKTGCEYQFRIAAENRYGKSTYLNSEPTVAQYPFKVPGPPGTPVVTLSSRDSMEVQWNEPISDGGSRVIGYHLERKERNSILWVKLNKTPIPQTKFKTTGLEEGVEYEFRVSAENIVGIGKPSKVSECYVARDPCDPPGRPEAIIVTRNSVTLQWKKPTYDGGSKITGYIVEKKELPEGRWMKASFTNIIDTHFEVTGLVEDHRYEFRVIARNAAGVFSEPSESTGAITARDEVDPPRISMDPKYKDTIVVHAGESFKVDADIYGKPIPTIQWIKGDQELSNTARLEIKSTDFATSLSVKDAVRVDSGNYILKAKNVAGERSVTVNVKVLDRPGPPEGPVVISGVTAEKCTLAWKPPLQDGGSDIINYIVERRETSRLVWTVVDANVQTLSCKVTKLLEGNEYTFRIMAVNKYGVGEPLESEPVVAKNPFVVPDAPKAPEVTTVTKDSMIVVWERPASDGGSEILGYVLEKRDKEGIRWTRCHKRLIGELRLRVTGLIENHDYEFRVSAENAAGLSEPSPPSAYQKACDPIYKPGPPNNPKVIDITRSSVFLSWSKPIYDGGCEIQGYIVEKCDVNVGEWTMCTPPTGINKTNIEVEKLLEKHEYNFRICAINKAGVGEHADVPGPIIVEEKLEAPDIDLDLELRKIINIRAGGSLRLFVPIKGRPTPEVKWGKVDGEIRDAAIIDVTSSFTSLVLDNVNRYDSGKYTLTLENSSGTKSAFVTVRVLDTPSPPVNLKVTEITKDSVSITWEPPLLDGGSKIKNYIVEKREATRKSYAAVVTNCHKNSWKIDQLQEGCSYYFRVTAENEYGIGLPAQTADPIKVAEVPQPPGKITVDDVTRNSVSLSWTKPEHDGGSKIIQYIVEMQAKHSEKWSECARVKSLQAVITNLTQGEEYLFRVVAVNEKGRSDPRSLAVPIVAKDLVIEPDVKPAFSSYSVQVGQDLKMEVPISGRPKPTITWTKDGLPLKQTTRINVTDSLDLTTLSIKETHKDDGGQYGITVANVVGQKTASIEIVTLDKPDPPKGPVKFDDVSAESITLSWNPPLYTGGCQITNYIVQKRDTTTTVWDVVSATVARTTLKVTKLKTGTEYQFRIFAENRYGQSFALESDPIVAQYPYKEPGPPGTPFATAISKDSMVIQWHEPVNNGGSPVIGYHLERKERNSILWTKVNKTIIHDTQFKAQNLEEGIEYEFRVYAENIVGVGKASKNSECYVARDPCDPPGTPEPIMVKRNEITLQWTKPVYDGGSMITGYIVEKRDLPDGRWMKASFTNVIETQFTVSGLTEDQRYEFRVIAKNAAGAISKPSDSTGPITAKDEVELPRISMDPKFRDTIVVNAGETFRLEADVHGKPLPTIEWLRGDKEIEESARCEIKNTDFKALLIVKDAIRIDGGQYILRASNVAGSKSFPVNVKVLDRPGPPEGPVQVTGVTSEKCSLTWSPPLQDGGSDISHYVVEKRETSRLAWTVVASEVVTNSLKVTKLLEGNEYVFRIMAVNKYGVGEPLESAPVLMKNPFVLPGPPKSLEVTNIAKDSMTVCWNRPDSDGGSEIIGYIVEKRDRSGIRWIKCNKRRITDLRLRVTGLTEDHEYEFRVSAENAAGVGEPSPATVYYKACDPVFKPGPPTNAHIVDTTKNSITLAWGKPIYDGGSEILGYVVEICKADEEEWQIVTPQTGLRVTRFEISKLTEHQEYKIRVCALNKVGLGEATSVPGTVKPEDKLEAPELDLDSELRKGIVVRAGGSARIHIPFKGRPMPEITWSREEGEFTDKVQIEKGVNYTQLSIDNCDRNDAGKYILKLENSSGSKSAFVTVKVLDTPGPPQNLAVKEVRKDSAFLVWEPPIIDGGAKVKNYVIDKRESTRKAYANVSSKCSKTSFKVENLTEGAIYYFRVMAENEFGVGVPVETVDAVKAAEPPSPPGKVTLTDVSQTSASLMWEKPEHDGGSRVLGYVVEMQPKGTEKWSIVAESKVCNAVVTGLSSGQEYQFRVKAYNEKGKSDPRVLGVPVIAKDLTIQPSLKLPFNTYSIQAGEDLKIEIPVIGRPRPNISWVKDGEPLKQTTRVNVEETATSTVLHIKEGNKDDFGKYTVTATNSAGTATENLSVIVLEKPGPPVGPVRFDEVSADFVVISWEPPAYTGGCQISNYIVEKRDTTTTTWHMVSATVARTTIKITKLKTGTEYQFRIFAENRYGKSAPLDSKAVIVQYPFKEPGPPGTPFVTSISKDQMLVQWHEPVNDGGTKIIGYHLEQKEKNSILWVKLNKTPIQDTKFKTTGLDEGLEYEFKVSAENIVGIGKPSKVSECFVARDPCDPPGRPEAIVITRNNVTLKWKKPAYDGGSKITGYIVEKKDLPDGRWMKASFTNVLETEFTVSGLVEDQRYEFRVIARNAAGNFSEPSDSSGAITARDEIDAPNASLDPKYKDVIVVHAGETFVLEADIRGKPIPDVVWSKDGKELEETAARMEIKSTIQKTTLVVKDCIRTDGGQYILKLSNVGGTKSIPITVKVLDRPGSPEGPLKVTGVTAEKCYLAWNPPLQDGGANISHYIIEKRETSRLSWTQVSTEVQALNYKVTKLLPGNEYIFRVMAVNKYGIGEPLESGPVTACNPYKPPGPPSTPEVSAITKDSMVVTWARPVDDGGTEIEGYILEKRDKEGVRWTKCNKKTLTDLRLRVTGLTEGHSYEFRVAAENAAGVGEPSEPSVFYRACDALYPPGPPSNPKVTDTSRSSVSLAWSKPIYDGGAPVKGYVVEVKEAAADEWTTCTPPTGLQGKQFTVTKLKENTEYNFRICAINSEGVGEPATLPGSVVAQERIEPPEIELDADLRKVVVLRASATLRLFVTIKGRPEPEVKWEKAEGILTDRAQIEVTSSFTMLVIDNVTRFDSGRYNLTLENNSGSKTAFVNVRVLDSPSAPVNLTIREVKKDSVTLSWEPPLIDGGAKITNYIVEKRETTRKAYATITNNCTKTTFRIENLQEGCSYYFRVLASNEYGIGLPAETTEPVKVSEPPLPPGRVTLVDVTRNTATIKWEKPESDGGSKITGYVVEMQTKGSEKWSTCTQVKTLEATISGLTAGEEYVFRVAAVNEKGRSDPRQLGVPVIARDIEIKPSVELPFHTFNVKAREQLKIDVPFKGRPQATVNWRKDGQTLKETTRVNVSSSKTVTSLSIKEASKEDVGTYELCVSNSAGSITVPITIIVLDRPGPPGPIRIDEVSCDSITISWNPPEYDGGCQISNYIVEKKETTSTTWHIVSQAVARTSIKIVRLTTGSEYQFRVCAENRYGKSSYSESSAVVAEYPFSPPGPPGTPKVVHATKSTMLVTWQVPVNDGGSRVIGYHLEYKERSSILWSKANKILIADTQVKVSGLDEGLMYEYRVYAENIAGIGKCSKSCEPVPARDPCDPPGQPEVTNITRKSVSLKWSKPHYDGGAKITGYIVERRELPDGRWLKCNYTNIQETYFEVTELTEDQRYEFRVFARNAADSVSEPSESTGPIIVKDDVEPPRVMMDVKFRDVIVVKAGEVLKINADIAGRPLPVISWAKDGIEIEERARTEIISTDNHTLLTVKDCIRRDTGQYVLTLKNVAGTRSVAVNCKVLDKPGPPAGPLEINGLTAEKCSLSWGRPQEDGGADIDYYHRKKRETSHLAWTICEGELQMTSCKVTKLLKGNEYIFRVTGVNKYGVGEPLESVAIKALDPFTVPSPPTSLEITSVTKESMTLCWSRPESDGGSEISGYIIERREKNSLRWVRVNKKPVYDLRVKSTGLREGCEYEYRVYAENAAGLSLPSETSPLIRAEDPVFLPSPPSKPKIVDSGKTTITIAWVKPLFDGGAPITGYTVEYKKSDDTDWKTSIQSLRGTEYTISGLTTGAEYVFRVKSVNKVGASDPSDSSDPQIAKEREEEPLFDIDSEMRKTLIVKAGASFTMTVPFRGRPVPNVLWSKPDTDLRTRAYVDTTDSRTSLTIENANRNDSGKYTLTIQNVLSAASLTLVVKVLDTPGPPTNITVQDVTKESAVLSWDVPENDGGAPVKNYHIEKREASKKAWVSVTNNCNRLSYKVTNLQEGAIYYFRVSGENEFGVGIPAETKEGVKITEKPSPPEKLGVTSISKDSVSLTWLKPEHDGGSRIVHYVVEALEKGQKNWVKCAVAKSTHHVVSGLRENSEYFFRVFAENQAGLSDPRELLLPVLIKEQLEPPEIDMKNFPSHTVYVRAGSNLKVDIPISGKPLPKVTLSRDGVPLKATMRFNTEITAENLTINLKESVTADAGRYEITAANSSGTTKAFINIVVLDRPGPPTGPVVISDITEESVTLKWEPPKYDGGSQVTNYILLKRETSTAVWTEVSATVARTMMKVMKLTTGEEYQFRIKAENRFGISDHIDSACVTVKLPYTTPGPPSTPWVTNVTRESITVGWHEPVSNGGSAVVGYHLEMKDRNSILWQKANKLVIRTTHFKVTTISAGLIYEFRVYAENAAGVGKPSHPSEPVLAIDACEPPRNVRITDISKNSVSLSWQQPAFDGGSKITGYIVERRDLPDGRWTKASFTNVTETQFTISGLTQNSQYEFRVFARNAVGSISNPSEVVGPITCIDSYGGPVIDLPLEYTEVVKYRAGTSVKLRAGISGKPAPTIEWYKDDKELQTNALVCVENTTDLASILIKDADRLNSGCYELKLRNAMASASATIRVQILDKPGPPGGPIEFKTVTAEKITLLWRPPADDGGAKITHYIVEKRETSRVVWSMVSEHLEECIITTTKIIKGNEYIFRVRAVNKYGIGEPLESDSVVAKNAFVTPGPPGIPEVTKITKNSMTVVWSRPIADGGSDISGYFLEKRDKKSLGWFKVLKETIRDTRQKVTGLTENSDYQYRVCAVNAAGQGPFSEPSEFYKAADPIDPPGPPAKIRIADSTKSSITLGWSKPVYDGGSAVTGYVVEIRQGEEEEWTTVSTKGEVRTTEYVVSNLKPGVNYYFRVSAVNCAGQGEPIEMNEPVQAKDILEAPEIDLDVALRTSVIAKAGEDVQVLIPFKGRPPPTVTWRKDEKNLGSDARYSIENTDSSSLLTIPQVTRNDTGKYILTIENGVGEPKSSTVSVKVLDTPAACQKLQVKHVSRGTVTLLWDPPLIDGGSPIINYVIEKRDATKRTWSVVSHKCSSTSFKLIDLSEKTPFFFRVLAENEIGIGEPCETTEPVKAAEVPAPIRDLSMKDSTKTSVILSWTKPDFDGGSVITEYVVERKGKGEQTWSHAGISKTCEIEVSQLKEQSVLEFRVFAKNEKGLSDPVTIGPITVKELIITPEVDLSDIPGAQVTVRIGHNVHLELPYKGKPKPSISWLKDGLPLKESEFVRFSKTENKITLSIKNAKKEHGGKYTVILDNAVCRIAVPITVITLGPPSKPKGPIRFDEIKADSVILSWDVPEDNGGGEITCYSIEKRETSQTNWKMVCSSVARTTFKVPNLVKDAEYQFRVRAENRYGVSQPLVSSIIVAKHQFRIPGPPGKPVIYNVTSDGMSLTWDAPVYDGGSEVTGFHVEKKERNSILWQKVNTSPISGREYRATGLVEGLDYQFRVYAENSAGLSSPSDPSKFTLAVSPVDPPGTPDYIDVTRETITLKWNPPLRDGGSKIVGYSIEKRQGNERWVRCNFTDVSECQYTVTGLSPGDRYEFRIIARNAVGTISPPSQSSGIIMTRDENVPPIVEFGPEYFDGLIIKSGESLRIKALVQGRPVPRVTWFKDGVEIEKRMNMEITNVLGSTSLFVRDATRDHRGVYTVEAKNASGSAKAEIKVKVQDTPGKVVGPIRFTNITGEKMTLWWDAPLNDGCAPITHYIIEKRETSRLAWALIEDKCEAQSYTAIKLINGNEYQFRVSAVNKFGVGRPLDSDPVVAQIQYTVPDAPGIPEPSNITGNSITLTWARPESDGGSEIQQYILERREKKSTRWVKVISKRPISETRFKVTGLTEGNEYEFHVMAENAAGVGPASGISRLIKCREPVNPPGPPTVVKVTDTSKTTVSLEWSKPVFDGGMEIIGYIIEMCKTDLGDWHKVNAEACVKTRYTVTDLQAGEEYKFRVSAINGAGKGDSCEVTGTIKAVDRLTAPELDIDANFKQTHVVRAGASIRLFIAYQGRPTPTAVWSKPDSNLSLRADIHTTDSFSTLTVENCNRNDAGKYTLTVENNSGSKSITFTVKVLDTPGPPGPITFKDVTRGSATLMWDAPLLDGGARIHHYVVEKREASRRSWQVISEKCTRQIFKVNDLAEGVPYYFRVSAVNEYGVGEPYEMPEPIVATEQPAPPRRLDVVDTSKSSAVLAWLKPDHDGGSRITGYLLEMRQKGSDLWVEAGHTKQLTFTVERLVEKTEYEFRVKAKNDAGYSEPREAFSSVIIKEPQIEPTADLTGITNQLITCKAGSPFTIDVPISGRPAPKVTWKLEEMRLKETDRVSITTTKDRTTLTVKDSMRGDSGRYFLTLENTAGVKTFSVTVVVIGRPGPVTGPIEVSSVSAESCVLSWGEPKDGGGTEITNYIVEKRESGTTAWQLVNSSVKRTQIKVTHLTKYMEYSFRVSSENRFGVSKPLESAPIIAEHPFVPPSAPTRPEVYHVSANAMSIRWEEPYHDGGSKIIGYWVEKKERNTILWVKENKVPCLECNYKVTGLVEGLEYQFRTYALNAAGVSKASEASRPIMAQNPVDAPGRPEVTDVTRSTVSLIWSAPAYDGGSKVVGYIIERKPVSEVGDGRWLKCNYTIVSDNFFTVTALSEGDTYEFRVLAKNAAGVISKGSESTGPVTCRDEYAPPKAELDARLHGDLVTIRAGSDLVLDAAVGGKPEPKIIWTKGDKELDLCEKVSLQYTGKRATAVIKFCDRSDSGKYTLTVKNASGTKAVSVMVKVLDSPGPCGKLTVSRVTQEKCTLAWSLPQEDGGAEITHYIVERRETSRLNWVIVEGECPTLSYVVTRLIKNNEYIFRVRAVNKYGPGVPVESEPIVARNSFTIPSPPGIPEEVGTGKEHIIIQWTKPESDGGNEISNYLVDKREKESLRWTRVNKDYVVYDTRLKVTSLMEGCDYQFRVTAVNAAGNSEPSERSNFISCREPSYTPGPPSAPRVVDTTKHSISLAWTKPMYDGGTDIVGYVLEMQEKDTDQWYRVHTNATIRNTEFTVPDLKMGQKYSFRVAAVNVKGMSEYSESIAEIEPVERIEIPDLELADDLKKTVTIRAGASLRLMVSVSGRPPPVITWSKQGIDLASRAIIDTTESYSLLIVDKVNRYDAGKYTIEAENQSGKKSATVLVKVYDTPGPCPSVKVKEVSRDSVTITWEIPTIDGGAPINNYIVEKREAAMRAFKTVTTKCSKTLYRISGLVEGTMHYFRVLPENIYGIGEPCETSDAVLVSEVPLVPAKLEVVDVTKSTVTLAWEKPLYDGGSRLTGYVLEACKAGTERWMKVVTLKPTVLEHTVTSLNEGEQYLFRIRAQNEKGVSEPRETVTAVTVQDLRVLPTIDLSTMPQKTIHVPAGRPVELVIPIAGRPPPAASWFFAGSKLRESERVTVETHTKVAKLTIRETTIRDTGEYTLELKNVTGTTSETIKVIILDKPGPPTGPIKIDEIDATSITISWEPPELDGGAPLSGYVVEQRDAHRPGWLPVSESVTRSTFKFTRLTEGNEYVFRVAATNRFGIGSYLQSEVIECRSSIRIPGPPETLQIFDVSRDGMTLTWYPPEDDGGSQVTGYIVERKEVRADRWVRVNKVPVTMTRYRSTGLTEGLEYEHRVTAINARGSGKPSRPSKPIVAMDPIAPPGKPQNPRVTDTTRTSVSLAWSVPEDEGGSKVTGYLIEMQKVDQHEWTKCNTTPTKIREYTLTHLPQGAEYRFRVLACNAGGPGEPAEVPGTVKVTEMLEYPDYELDERYQEGIFVRQGGVIRLTIPIKGKPFPICKWTKEGQDISKRAMIATSETHTELVIKEADRGDSGTYDLVLENKCGKKAVYIKVRVIGSPNSPEGPLEYDDIQVRSVRVSWRPPADDGGADILGYILERREVPKAAWYTIDSRVRGTSLVVKGLKENVEYHFRVSAENQFGISKPLKSEEPVTPKTPLNPPEPPSNPPEVLDVTKSSVSLSWSRPKDDGGSRVTGYYIERKETSTDKVVRHNKTQITTTMYTVTGLVPDAEYQFRIIAQNDVGLSETSPASEPVVCKDPFDKPSQPGELEILSISKDSVTLQWEKPECDGGKEILGYWVEYRQSGDSAWKKSNKERIKDKQFTIGGLLEATEYEFRVFAENETGLSRPRRTAMSIKTKLTSGEAPGIRKEMKDVTTKLGEAAQLSCQIVGRPLPDIKWYRFGKELIQSRKYKMSSDGRTHTLTVMTEEQEDEGVYTCIATNEVGEVETSSKLLLQATPQFHPGYPLKEKYYGAVGSTLRLHVMYIGRPVPAMTWFHGQKLLQNSENITIENTEHYTHLVMKNVQRKTHAGKYKVQLSNVFGTVDAILDVEIQDKPDKPTGPIVIEALLKNSAVISWKPPADDGGSWITNYVVEKCEAKEGAEWQLVSSAISVTTCRIVNLTENAGYYFRVSAQNTFGISDPLEVSSVVIIKSPFEKPGAPGKPTITAVTKDSCVVAWKPPASDGGAKIRNYYLEKREKKQNKWISVTTEEIRETVFSVKNLIEGLEYEFRVKCENLGGESEWSEISEPITPKSDVPIQAPHFKEELRNLNVRYQSNATLVCKVTGHPKPIVKWYRQGKEIIADGLKYRIQEFKGGYHQLIIASVTDDDATVYQVRATNQGGSVSGTASLEVEVPAKIHLPKTLEGMGAVHALRGEVVSIKIPFSGKPDPVITWQKGQDLIDNNGHYQVIVTRSFTSLVFPNGVERKDAGFYVVCAKNRFGIDQKTVELDVADVPDPPRGVKVSDASRDSVNLTWTEPASDGGSKITNYIVEKCATTAERWLRVGQARETRYTVINLFGKTSYQFRVIAENKFGLSKPSEPSEPTITKEDKTRAMNYDEEVDETREVSMTKASHSSTKELYEKYMIAEDLGRGEFGIVHRCVETSSKKTYMAKFVKVKGTDQVLVKKEISILNIARHRNILHLHESFESMEELVMIFEFISGLDIFERINTSAFELNEREIVSYVHQVCEALQFLHSHNIGHFDIRPENIIYQTRRSSTIKIIEFGQARQLKPGDNFRLLFTAPEYYAPEVHQHDVVSTATDMWSLGTLVYVLLSGINPFLAETNQQIIENIMNAEYTFDEEAFKEISIEAMDFVDRLLVKERKSRMTASEALQHPWLKQKIERVSTKVIRTLKHRRYYHTLIKKDLNMVVSAARISCGGAIRSQKGVSVAKVKVASIEIGPVSGQIMHAVGEEGGHVKYVCKIENYDQSTQVTWYFGVRQLENSEKYEITYEDGVAILYVKDITKLDDGTYRCKVVNDYGEDSSYAELFVKGVREVYDYYCRRTMKKIKRRTDTMRLLERPPEFTLPLYNKTAYVGENVRFGVTITVHPEPHVTWYKSGQKIKPGDNDKKYTFESDKGLYQLTINSVTTDDDAEYTVVARNKYGEDSCKAKLTVTLHPPPTDSTLRPMFKRLLANAECQEGQSVCFEIRVSGIPPPTLKWEKDGQPLSLGPNIEIIHEGLDYYALHIRDTLPEDTGYYRVTATNTAGSTSCQAHLQVERLRYKKQEFKSKEEHERHVQKQIDKTLRMAEILSGTESVPLTQVAKEALREAAVLYKPAVSTKTVKGEFRLEIEEKKEERKLRMPYDVPEPRKYKQTTIEEDQRIKQFVPMSDMKWYKKIRDQYEMPGKLDRVVQKRPKRIRLSRWEQFYVMPLPRITDQYRPKWRIPKLSQDDLEIVRPARRRTPSPDYDFYYRPRRRSLGDISDEELLLPIDDYLAMKRTEEERLRLEEELELGFSASPPSRSPPHFELSSLRYSSPQAHVKVEETRKNFRYSTYHIPTKAEASTSYAELRERHAQAAYRQPKQRQRIMAEREDEELLRPVTTTQHLSEYKSELDFMSKEEKSRKKSRRQREVTEITEIEEEYEISKHAQRESSSSASRLLRRRRSLSPTYIELMRPVSELIRSRPQPAEEYEDDTERRSPTPERTRPRSPSPVSSERSLSRFERSARFDIFSRYESMKAALKTQKTSERKYEVLSQQPFTLDHAPRITLRMRSHRVPCGQNTRFILNVQSKPTAEVKWYHNGVELQESSKIHYTNTSGVLTLEILDCHTDDSGTYRAVCTNYKGEASDYATLDVTGGDYTTYASQRRDEEVPRSVFPELTRTEAYAVPSFKKTSEMEASSSVREVKSQMTETRESLSSYEHSASAEMKSAALEEKSLEEKSTTRKIKTTLAARILTKPRSMTVYEGESARFSCDTDGEPVPTVTWLRKGQVLSTSARHQVTTTKYKSTFEISSVQASDEGNYSVVVENSEGKQEAEFTLTIQKARVTEKAVTSPPRVKSPEPRVKSPEAVKSPKRVKSPEPSHPKAVSPTETKPTPIEKVQHLPVSAPPKITQFLKAEASKEIAKLTCVVESSVLRAKEVTWYKDGKKLKENGHFQFHYSADGTYELKINNLTESDQGEYVCEISGEGGTSKTNLQFMGQAFKSIHEKVSKISETKKSDQKTTESTVTRKTEPKAPEPISSKPVIVTGLQDTTVSSDSVAKFAVKATGEPRPTAIWTKDGKAITQGGKYKLSEDKGGFFLEIHKTDTSDSGLYTCTVKNSAGSVSSSCKLTIKAIKDTEAQKVSTQKTSEITPQKKAVVQEEISQKALRSEEIKMSEAKSQEKLALKEEASKVLISEEVKKSAATSLEKSIVHEEITKTSQASEEVRTHAEIKAFSTQMSINEGQRLVLKANIAGATDVKWVLNGVELTNSEEYRYGVSGSDQTLTIKQASHRDEGILTCISKTKEGIVKCQYDLTLSKELSDAPAFISQPRSQNINEGQNVLFTREISGEPSPEIEWFKNNLPISISSNVSISRSRNVYSLEIRNASVSDSGKYTIKAKNFRGQCSATASLMVLPLVEEPSREVVLRTSGDTSLQGSFSSQSVQMSASKQEASFSSFSSSSASSMTEMKFASMSAQSMSSMQESFVEMSSSSFMGISNMTQLESSTSKMLKAGIRGIPPKIEALPSDISIDEGKVLTVACAFTGEPTPEVTWSCGGRKIHSQEQGRFHIENTDDLTTLIIMDVQKQDGGLYTLSLGNEFGSDSATVNIHIRSI Other techniques 1 3670 3670 Undetermined 3671 4242 572 Disordered 4243 26926 22684 Undetermined Trombitas, K., Greaser, M., Labeit, S., Jin, J. P., Kellermayer, M., Helmes, M., and Granzier, H. Titin extensibility in situ: entropic elasticity of permanently folded and permanently unfolded molecular segments 1998 J. Cell Biol. 140 853 859 Labeit, S., and Kolmerer, B. Titins: giant proteins in charge of muscle ultrastructure and elasticity 1995 Science 270 293 296 Kellermayer, M. S., Smith, S. B., Granzier, H. L., and Bustamante, C. Folding-unfolding transitions in single titin molecules characterized with laser tweezers 1997 Science 276 1112 1116 Helmes, M., Trombitas, K., Centner, T., Kellermayer, M., Labeit, S., Linke, W. A., and Granzier, H. Mechanically driven contour-length adjustment in rat cardiac titin's unique N2B sequence: titin is an adjustable spring 1999 Circ. Res. 84 1339 1352 PIR: I38344 http://www.embl-heidelberg.de/ExternalInfo/Titin/old_stuff/annotation.html Coat protein Tomato bushy stunt virus coat protein 116805 P11795 1tbv C 389 AMTTRNNNNVLAVSKKQLGVLAASAAVGALRNYIGESSPALLQSAVGLGKKALNKVRNRRKQGNQQIITHVGGVGGSIMAPVAVSRQLVGSKPKFTGRTSGSVTVTGHREYLTQVNNSSGFVVNGGIVGNSLQLNPSNGTLFSWLPALASNFDQYSFNSV VLDYVPLCGTTEVGRVALYFDKDSQDPEPADRVELANFGVLKETAPWAEAMLRIPTDKVKRYCNDSATVDQKLIDLGQLGIATYGGAGADAVGELFLARSVTLYFPQPTNTLLSSKRLDLTGSLADATGPGYLVLTRTPTVLTHTFRATGTFNLSGGLRC LTSLTLGATGAVVINDILAIDNVGTASDYFLNCTVSSLPATVTFTVSGVAAGILLVGRARANVVNLL X-ray crystallography 1 66 66 Disordered Function arises via a disorder to order transition Protein-genomic RNA binding Hopper, P., Harrison, S. C., and Sauer, R. T. Structure of tomato bushy stunt virus. V. Coat protein sequence determination and its structural implications 1984 J. Mol. Biol. 177 701 713 DNA TOPOISOMERASE I 135989 P11387 1A31 765 MSGDHLHNDSQIEADFRLNDSHKHKDKHKDREHRHKEHKKEKDREKSKHSNSEHKDSEKKHKEKEKTKHKDGSSEKHKDKHKDRDKEKRKEEKVRASGDAKIKKEKENGFSSPPQIKDEPEDDGYFVPPKEDIKPLKRPRDEDDVDYKPKKIKTEDTKKEKKRKLEEEEDGKLKKPKNKDKDKKVPEPDNKKKKPKKEEEQKWKWWEEERYPEGIKWKFLEHKGPVFAPPYEPLPENVKFYYDGKVMKLSPKAEEVATFFAKMLDHEYTTKEIFRKNFFKDWRKEMTNEEKNIITNLSKCDFTQMSQYFKAQTEARKQMSKEEKLKIKEENEKLLKEYGFCIMDNHKERIANFKIEPPGLFRGRGNHPKMGMLKRRIMPEDIIINCSKDAKVPSPPPGHKWKEVRHDNKVTWLVSWTENIQGSIKYIMLNPSSRIKGEKDWQKYETARRLKKCVDKIRNQYREDWKSKEMKVRQRAVALYFIDKLALRAGNEKEEGETADTVGCCSLRVEHINLHPELDGQEYVVEFDFLGKDSIRYYNKVPVEKRVFKNLQLFMENKQPEDDLFDRLNTGILNKHLQDLMEGLTAKVFRTYNASITLQQQLKELTAPDENIPAKILSYNRANRAVAILCNHQRAPPKTFEKSMMNLQTKIDAKKEQLADARRDLKSAKADAKVMKDAKTKKVVESKKKAVQRLEEQLMKLEVQATDREENKQIALGTSKLNYLDPRITVAWCKKWGVPIEKIYNKTQREKFAWAIDMADEDYEF Circular dichroism 1 197 197 Disordered Known to exist in disordered state, relationship to function unknown Disordered region is not essential for protein function Protein-protein binding Regulation of proteolysis in vivo 652 696 45 Disordered Stewart, L., Ireton, G. C., Parker, L. H., Madden, K. R., and Champoux, J. J. Biochemical and biophysical analyses of recombinant forms of human topoisomerase I 1996 J. Biol. Chem. 271 7593 7601 Shaiu, W. L., Hu, T., and Hsieh, T. S. The hydrophilic, protease-sensitive terminal domains of eucaryotic DNA topoisomerases have essential intracellular functions 1999 Pacific Symp. Biocomputing 4 578 589 DNA topoisomerase II 1351262 P06786 1BGW 1428 MSTEPVSASDKYQKISQLEHILKRPDTYIGSVETQEQLQWIYDEETDCMIEKNVTIVPGLFKIFDEILVNAADNKVRDPSMKRIDVNIHAEEHTIEVKNDGKGIPIEIHNKENIYIPEMIFGHLLTSSNYDDDEKKVTGGRNGYGAKLCNIFSTEFILETADLNVGQKYVQKWENNMSICHPPKITSYKKGPSYTKVTFKPDLTRFGMKELDNDILGVMRRRVYDINGSVRDINVYLNGKSLKIRNFKNYVELYLKSLEKKRQLDNGEDGAAKSDIPTILYERINNRWEVAFAVSDISFQQISFVNSIATTMGGTHVNYITDQIVKKISEILKKKKKKSVKSFQIKNNMFIFINCLIENPAFTSQTKEQLTTRVKDFGSRCEIPLEYINKIMKTDLATRMFEIADANEENALKKSDGTRKSRITNYPKLEDANKAGTKEGYKCTLVLTEGDSALSLAVAGLAVVGRDYYGCYPLRGKMLNVREASADQILKNAEIQAIKKIMGLQHRKKYEDTKSLRYGHLMIMTDQDHDGSHIKGLIINFLESSFPGLLDIQGFLLEFITPIIKVSITKPTKNTIAFYNMPDYEKWREEESHKFTWKQKYYKGLGTSLAQEVREYFSNLDRHLKIFHSLQGNDKDYIDLAFSKKKADDRKEWLRQYEPGTVLDPTLKEIPISDFINKELILFSLADNIRSIPNVLDGFKPGQRKVLYGCFKKNLKSELKVAQLAPYVSECTAYHHGEQSLAQTIIGLAQNFVGSNNIYLLLPNGAFGTRATGGKDAAAARYIYTELNKLTRKIFHPADDPLYKYIQEDEKTVEPEWYLPILPMILVNGAEGIGTGWSTYIPPFNPLEIIKNIRHLMNDEELEQMHPWFRGWTGTIEEIEPLRYRMYGRIEQIGDNVLEITELPARTWTSTIKEYLLLGLSGNDKIKPWIKDMEEQHDDNIKFIITLSPEEMAKTRKIGFYERFKLISPISLMNMVAFDPHGKIKKYNSVNEILSEFYYVRLEYYQKRKDHMSERLQWEVEKYSFQVKFIKMIIEKELTVTNKPRNAIIQELENLGFPRFNKEGKPYYGSPNDEIAEQINDVKGATSDEEDEESSHEDTENVINGPEELYGTYEYLLGMRIWSLTKERYQKLLKQKQEKETELENLLKLSAKDIWNTDLKAFEVGYQEFLQRDAEARGGNVPNKGSKTKGKGKRKLVDDEDYDPSKKNKKSTARKGKKIKLEDKNFERILLEQKLVTKSKAPTKIKKEKTPSVSETKTEEEENAPSSTSSSSIFDIKKEDKDEGELSKISNKFKKISTIFDKMGSTSATSKENTPEQDDVATKKNQTTAKKTAVKPKLAKKPVRKQQKVVELSGESDLEILDSYTDREDSNKDEDDAIPQRSRRQRSSRAASVPKKSYVETLELSDDSFIEDDEEENQGSDVSFNEED Limited proteolysis X-ray crystallography 1 632 632 Undetermined 633 681 49 Disordered Function arises from the disordered (extended) state Flexible linkers/spacers Protein-DNA binding 1077 1106 30 Disordered Known to exist in disordered state, relationship to function unknown Autoregulatory Phosphorylation 1178 1428 251 Disordered Known to exist in disordered state, relationship to function unknown Autoregulatory Disordered region is not essential for protein function Phosphorylation Protein-protein binding Shaiu, W. L., Hu, T., and Hsieh, T. S. The hydrophilic, protease-sensitive terminal domains of eucaryotic DNA topoisomerases have essential intracellular functions 1999 Pacific Symp. Biocomputing 4 578 589 Berger, J. M., Gamblin, S. J., Harrison, S. C., and Wang, J. C. Structure and mechanism of DNA topoisomerase II 1996 Nature 379 225 232 Caron, P. R., Watt, P., and Wang, J. C. The C-terminal domain of Saccharomyces cerevisiae DNA topoisomerase II 1994 Mol. Cell Biol. 14 3197 3207 Berger, J. M. Personal communication From residue 410, GI: 633273 From residue 410, PDB: 1bgw Regulatory protein ADR1 Transcription factor ADR1 113450 P07248 1323 MANVEKPNDCSGFPVVDLNSCFSNGFNNEKQEIEMETDDSPILLMSSSASRENSNTFSVIQRTPDGKIITTNNNMNSKINKQLDKLPENLRLNGRTPSGKLRSFVCEVCTRAFARQEHLKRHYRSHTNEKPYPCGLCNRCFTRRDLLIRHAQKIHSGNLGETISHTKKVSRTITKARKNSASSVKFQTPTYGTPDNGNFLNRTTANTRRKASPEANVKRKYLKKLTRRASFSAQSASSYALPDQSSLEQHPKDRVKFSTPELVPLDLKNPELDSSFDLNMNLDLNLNLDSNFNIALNRSDSSGSTMNLDYKLPESANNYTYSSGSPTRAYVGANTNSKNASFNDADLLSSSYWIKAYNDHLFSVSESDETSPMNSELNDTKLIVPDFKSTIHHLKDSRSSSWTVAIDNNSNNNKVSDNQPDFVDFQELLDNDTLGNDLLETTAVLKEFELLHDDSVSATATSNEIDLSHLNLSNSPISPHKLIYKNKEGTNDDMLISFGLDHPSNREDDLDKLCNMTRDVQAIFSQYLKGEESKRSLEDFLSTSNRKEKPDSGNYTFYGLDCLTLSKISRALPASTVNNNQPSHSIESKLFNEPMRNMCIKVLRYYEKFSHDSSESVMDSNPNLLSKELLMPAVSELNEYLDLFKNNFLPHFPIIHPSLLDLDLDSLQRYTNEDGYDDAENAQLFDRLSQGTDKEYDYEHYQILSISKIVCLPLFMATFGSLHKFGYKSQTIELYEMSRRILHSFLETKRRCRSTTVNDSYQNIWLMQSLILSFMFALVADYLEKIDSSLMKRQLSALCSTIRSNCLPTISANSEKSINNNNEPLTFGSPLQYIIFESKIRCTLMAYDFCQFLKCFFHIKFDLSIKEKDVETIYIPDNESKWASESIICNGHVVQKQNFYDFRNFYYSFTYGHLHSIPEFLGSSMIYYEYDLRKGTKSHVFLDRIDTKRLERSLDTSSYGNDNMAATNKNIAILIDDTIILKNNLMSMRFIKQIDRSFTEKVRKGQIAKIYDSFLNSVRLNFLKNYSVEVLCEFLVALNFSIRNISSLYVEEESDCSQRMNSPELPRIHLNNQALSVFNLQGYYYCFILIIKFLLDFEATPNFKLLRIFIELRSLANSILLPTLSRLYPQEFSGFPDVVFTQQFINKDNGMLVPGLSANEHHNGASAAVKTKLAKKINVEGLAMFINEILVNSFNDTSFLNMEDPIRNEFSFDNGHRAVTDLPRSAHFLSDTGLEGINFSGLNDSHQTVSTLNLLRYGENHSSKHKNGGKGQGFAEKYQLSLKYVTIAKLFFTNVKENYIHCHMLDKMASDFHTLENHLKGNS Nuclear magnetic resonance spectroscopy 75 159 85 Disordered Function arises via a disorder to order transition Metal binding Protein-DNA binding Parraga, G., Horvath, S. J., Eisen, A., Taylor, W. E., Hood, L., Young, E. T., and Klevit, R. E. Zinc-dependent structure of a single-finger domain of yeast ADR1 1988 Science 241 1489 1492 Klevit, R. E., Herriott, J. R., and Horvath, S. J. Solution structure of a zinc finger domain of yeast ADR1 1990 Proteins 7 215 226 Hyre, D. E., and Klevit, R. E. A disorder-to-order transition coupled to DNA binding in the essential zinc-finger DNA-binding domain of yeast ADR1 1998 J. Mol. Biol. 279 929 943 Bowers, P. M., Schaufler, L. E., and Klevit, R. E. A folding transition and novel zinc finger accessory domain in the transcription factor ADR1 1999 Nat. Struct. Biol. 6 478 485 cfos [Homo sapiens] Transcription factor c-Fos 4063509 P01100 380 MMFSGFNADYEASSSRCSSASPAGDSLSYYHSPADSFSSMGSPVNAQDFCTDLAVSSANFIPTVTAISTSPDLQWLVQPALVSSVAPSQTRAPHPFGVPAPSAGAYSRAGVVKTMTGGRAQSIGRRGKVEQLSPEEEEKRRIRRERNKMAAAKCRNRRRELTDTLQAETDQLEDEKSALQTEIANLLKEKEKLEFILAAHRPACKIPDDLGFPEEMSVASLDLTGGLPEVATPESEEAFTLPLLNDPEPKPSVEPVKSISSMELKTEPFDDFLFPASSRPSGSETARSVPDMDLSGSFYAADWEPLHSGSLGMGPMATELEPLCTPVVTCTPSCTAYTSSFVFTYPEADSFPSCAAAHRKGSSSNEPSSDSLSSPTLLAL Circular dichroism Nuclear magnetic resonance spectroscopy 216 380 165 Disordered Function arises via a disorder to order transition Protein-protein binding Campbell, K. M., Terrell, A. R., Laybourn, P. J., and Lumb, K. J. Intrinsic structural disorder of the C-terminal activation domain from the bZIP transcription factor Fos 2000 Biochemistry 39 2708 2713 Transcription factor AP-1 Activator protein 1 AP1 Proto-oncogene c-jun V-jun avian sarcoma virus 17 oncogene homolog p39 Transcription factor c-Jun 135298 P05412 1ao2 331 MTAKMETTFYDDALNASFLPSESGPYGYSNPKILKQSMTLNLADPVGSLKPHLRAKNSDLLTSPDVGLLKLASPELERLIIQSSNGHITTTPTPTQFLCPKNVTDEQEGFAEGFVRALAELHSQNTLPSVTSAAQPVNGAGMVAPAVASVAGGSGSGGFSASLHSEPPVYANLSNFNPGALSSGGGAPSYGAAGLAFPAQPQQQQQPPHHLPQQMPVQHPRLQALKEEPQTVPEMPGETPPLSPIDMESQERIKAERKRMRNRIAASKCRKRKLERIARLEEKVKTLKAQNSELASTANMLREQVAQLKQKVMNHVNSGCQLMLTQQLQTF Circular dichroism Nuclear magnetic resonance spectroscopy Other techniques X-ray crystallography 1 60 60 Undetermined 61 98 38 Disordered Function arises via a disorder to order transition Unknown 99 256 158 Undetermined 257 314 58 Disordered Function arises via a disorder to order transition Protein-DNA binding Protein-protein binding 315 331 17 Undetermined John, M., Briand, J. P., and Schnarr, M. A c-Jun activation domain peptide and its corresponding phosphopeptide have potential to adopt alpha-helical conformation 1996 Pept Res 9 71 78 Krebs, D., Dahmani, B., el Antri, S., Monnot, M., Convert, O., Mauffret, O., Troalen, F., and Fermandjian, S. The basic subdomain of the c-Jun oncoprotein. A joint CD, Fourier-transform infrared and NMR study 1995 Eur. J. Biochem. 231 370 380 Glover, J. N., and Harrison, S. C. Crystal structure of the heterodimeric bZIP transcription factor c-Fos-c-Jun bound to DNA 1995 Nature 373 257 261 Junius, F. K., O'Donoghue, S. I., Nilges, M., Weiss, A. S., and King, G. F. High resolution NMR solution structure of the leucine zipper domain of the c-Jun homodimer 1996 J. Biol. Chem. 271 13663 13667 Chen, L., Glover, J. N., Hogan, P. G., Rao, A., and Harrison, S. C. Structure of the DNA-binding domains from NFAT, Fos and Jun bound specifically to DNA 1998 Nature 392 42 48 Also, PDB: 1jun cAMP response element binding protein CREB Transcription factor CREB 117435 P15337 1KDX 341 MTMDSGADNQQSGDAAVTEAESQQMTVQAQPQIATLAQVSMPAAHATSSAPTVTLVQLPNGQTVQVHGVIQAAQPSVIQSPQVQTVQSSCKDLKRLFSGTQISTIAESEDSQESVDSVTDSQKRREILSRRPSYRKILNDLSSDAPGVPRIEEEKSEEETSAPAITTVTVPTPIYQTSSGQYIAITQGGAIQLANNGTDGVQGLQTLTMTNAAATQPGTTILQYAQTTDGQQILVPSNQVVVQAASGDVQTYQIRTAPTSTIAPGVVMASSPALPTQPAEEAARKREVRLMKNREAARECRRKKKEYVKCLENRVAVLENQNKTLIEELKALKDLYCHKSD Circular dichroism 1 265 265 Disordered Function arises via a disorder to order transition Phosphorylation Protein-protein binding Richards, J. P., Bachinger, H. P., Goodman, R. H., and Brennan, R. G. Analysis of the structural properties of cAMP-responsive element-binding protein (CREB) and phosphorylated CREB 1996 J. Biol. Chem. 271 13716 13723 Transcription initiation factor TFIID 230 kDa subunit TAFII-230 TAFII250 TBP-associated factor 230 kDa P230 Transcription factor dTAFII230 1705691 P51123 1tba 2067 MEMESDNSDDEGSIGNGLDLTGILFGNIDSEGRLLQDDDGEGRGGTGFDAELRENIGSLSKLGLDSMLLEVIDLKEAEPPSDDEEEEDARPSAVSASGGMSAFDALKAGVKREEREDGAVKAQDDAIDYSDITELSEDCPRTPPEETSTYDDLEDAIPASKVEAKLTKDDKELMPPPSAPMRSGSGGGIEEPAKSNDASSPSDDSKSTDSKDADRKLDTPLADILPSKYQNVDVRELFPDFRPQKVLRFSRLFGPGKPTSLPQIWRHVRQSRRKRNQSRDQKTTNTGGSDSPSDTEEPRKRGFSLHYAAEPTPAECMSDDEDKLLGDFNSEDVRPEGPDNGENSDQKPKVADWRFGPAQIWYDILEVPDSGEGFNYGFKTKAASTSSQQQLKDERRVKSPEDDVEDPSIADDAFLMVSQLHWEDDVVWDGNDIKAKVLQKLNSKTNAAGWLPSSGSRTAGAFSQPGKPSMPVGSGSSKQGSGASSKKAQQNAQAKPAEAPDDTWYSLFPVENEELIYYKWEDEVIWDAQQVSKVPKPKVLTLDPNDENIILGIPDDIDPSKINKSTGPPPKIKIPHPHVKKSKILLGKAGVINVLAEDTPPPPPKSPDRDPFNISNDTYYTPKTEPTLRLKVGGNLIQHSTPVVELRAPFVPTHMGPMNVRAFHRPPLKKYSHGPMAQSIPHPVFPLLKTIAKKAKQREVERIASGGGDVFFMRNPEDLSGRDGDIVLAEFCEEHPPLINQVGMCSKIKNYYKRKAEKDSGPQDYVYGEVAFAHTSPFLGILHPGQCIQAIENNMYRAPIYPHKMAHNDFLVIRTRNNYWIRSVNSIYTVGQECPLYEVPGPNSKRANNFTRDFLQVFIYRLFWKSRDNPRRIRMDDIKQAFPAHSESSIRKRLKQCADFKRTGMDSNWWVIKPEFRLPSEEEIRAMVSPEQCCAYFSMIAAEQRLKDAGYGEKFLFAPQEDDDEEAQLKLDDEVKVAPWNTTRAYIQAMRGKCLLQLSGPADPTGCGEGFSYVRVPNKPTQTKEEQESQPKRSVTGTDADLRRLPLQRAKELLRQFKVPEEEIKKLSRWEVIDVVRTLSTEKAKAGEEGMDKFSRGNRFSIAEHQERYKEECQRIFDLQNRVLASSEVLSTDEAESSASEESDLEELGKNLENMLSNKKTSTQLSREREELERQELLRQLDEEHGGPSGSGGAKGAKGKDDPGQQMLATNNQGRILRITRTFRGNDGKEYTRVETVRRQPVIDAYIKIRTTKDEQFIKQFATLDEQQKEEMKREKRRIQEQLRRIKRNQERERLAQLAQNQKLQPGGMPTSLGDPKSSGGHSHKERDSGYKEVSPSRKKFKLKPDLKLKCGACGQVGHMRTNKACPLYSGMQSSLSQSNPSLADDFDEQSEKEMTMDDDDLVNVDGTKVTLSSKILKRHGGDDGKRRSGSSSGFTLKVPRDAMGKKKRRVGGDLHCDYLQRHNKTANRRRTDPVVVLSSILEIIHNELRSMPDVSPFLFPVSAKKVPDYYRVVTKPMDLQTMREYIRQRRYTSREMFLEDLKQIVDNSLIYNGPQSAYTLAAQRMFSSCFELLAEREDKLMRLEKAINPLLDDDDQVALSFIFDKLHSQIKQLPESWPFLKPVNKKQVKDYYTVIKRPMDLETIGKNIEAHRYHSRAEYLADIELIATNCEQYNGSDTRYTKFSKKILEYAQTQLIEFSEHCGQLENNIAKTQERARENAPEFDEAWGNDDYNFDRGSRASSPGDDYIDVEGHGGHASSSNSIHRSMGAEAGSSHTAPAVRKPAPPGPGEVKRGRGRPRKQRDPVEEDLQCSTDDEDDDEEEDFQEVSEDENNAASILDQGERINAPADAMDGMFDPKNIKTEIDLEAHQMADESMDVDPNYDPSDFLAMHKQRQSLGEPSSLQGAFTNFLSHEQDDNGPYNPAEASTSAASGADLGMDASMAMQMAPEMPVNTMNNGMGIDDDLDISESDEEDDGSRVRIKKEVFDDGDYALQHQQMGQAASQSQIYMVDSSNEPTTLDYQQPPQLDFQQVQEMEQLHQVMPPMQSEQLQQQQTPQGDNDYAWTF Nuclear magnetic resonance spectroscopy 1 10 10 Undetermined 11 77 67 Disordered Function arises via a disorder to order transition Protein-protein binding 78 2068 1991 Undetermined Liu, D., Ishima, R., Tong, K. I., Bagby, S., Kokubo, T., Muhandiram, D. R., Kay, L. E., Nakatani, Y., and Ikura, M. Solution structure of a TBP-TAF(II)230 complex: protein mimicry of the minor groove surface of the TATA box unwound by TBP 1998 Cell 94 573 583 Eukaryotic translation initiation factor 4 gamma eIF-4-gamma eIF-4G eIF4G P220 Transcription factor eIF-4G 1170510 Q04637 1396 MSGARTASTPTPPQTGGSLEPQANGETPQVAVIVRPDDRSQGAIIADRPGLPGPEHSPSESQPSSPSPTPSPSPVLEPGSEPNLAVLSIPGDTMTTIQMSVEESTPISRETGEPYRLSPEPTPLAEPILEVEVTLSKPVPESEFSSSPLQAPTPLASHTVEIHEPNGMVPSEDLEPEVESSPELAPPPACPSESPVPIAPTAQPEELLNGAPSPPAVDLSPVSEPEEQAKEVTASVAPPTIPSATPATAPSATSPAQEEEMEEEEDEEEGEVGEAGEGESEKRGEELLPPESTPIPANLSQNLEAAAATQVAVSVPKRRRKIKELNKKEAVGDLLDAFKEANPAVPEVENQPPAGSNPGPESEGSGVPPRPEEADETWDSKEDKIHNAENIQPGEQKYEYKSDQWKPPNLEEKKRYDREFLLGFQFIFCQMQKPEGLPHISDVVLDKANKTPLRPLDPTRLQGINCGPDFTPSFANLGRTTLSTRGPPRGGPGGELPRGPAGLGPRRSQQGPRKEPRKIIATVLMTEDIKLNKAEKAWKPSSKRTAADKDRGEEDADGSKTQDLFRRWRSILNKLTPQMFQQLMKQVTQLAIDTEDASKGSLTSFLRRPFQSPTSLWPIQHVPLPHGAESAHYGKPTVTVNFRKLLLNRCQKEFEKDKDDDEVFEKKQKEMDEAATAEERERLKEELEEARDIARRCSLGNIKFIGELFKLKMLTEAIMHDCVVKLLKNHDEESLECLCRLLTTIGKDLDFEKAKPRMDQYFNQMEKIIKEKKTSSRIRFMLQDVLDLRGSNWVPRRGDQGPRPLTRSIRRLRWKTSRAHQSAAAHARAVTSVGAVLQALPSAVDFPLWMMVADTVPISKGSRPIDTSRLTKITKPGSIDSNNQLFAPGGRLSWGKGSSGGSGAQPSDAASEAARPATSTLIRFSALQQAVPTESTDNRRVVQRSSLSRERGEKAGDRGDRLERVNGEGTVGTGLIVSRTPATKRTFSKEVEERSRERPSQPEGLRKAASLTEDRDRGRDAVKREAALPPVSPLKAALSEEELEKKSKAIIEEYLHLNDMKEAVQCVQELASPSLLFIFVRHGVESTLERSAIAREHMGQLLHQLLCAGHLSTAQYYQGLYEILELAEDMEIDIPHVWLYLAELVTPILQEGGVPMGELFREITKPLRPLGKAASLLLEILGLLCKSMGPKKVGTLWREAGLSWKEFLPEGQDIGAFVAEQKVEYTLGEESEAPGQRALPSEELNRQLEKLLKEGSSNQRVFDWIEANLSEQIVSNTLVR ALMTAVCYSAIIFETPLRVDVAVLKGDIVLQKYLCDEAEGATGALRLQALVVTLEQPPNLLRMFFDALYDEDVVKEDAFYSWESSKDPAEQQGKGVALKSVTAFFKWLREVRGGV Nuclear magnetic resonance spectroscopy 1 380 380 Undetermined 381 506 126 Disordered Function arises via a disorder to order transition Protein-protein binding 507 1395 889 Undetermined Hershey, P. E., McWhirter, S. M., Gross, J. D., Wagner, G., Alber, T., and Sachs, A. B. The Cap-binding protein eIF4E promotes folding of a functional domain of yeast translation initiation factor eIF4G1 1999 J. Biol.Chem. 274 21297 21304 General control protein GCN4 Amino acid biosynthesis regulatory protein Transcription factor GCN4 121066 P03069 2ZTA 281 MSEYQPSLFALNPMGFSPLDGSKSTNENVSASTSTAKPMVGQLIFDKFIKTEEDPIIKQDTPSNLDFDFALPQTATAPDAKTVLPIPELDDAVVESFFSSSTDSTPMFEYENLEDNSKEWTSLFDNDIPVTTDDVSLADKAIESTEEVSLVPSNLEVSTTSFLPTPVLEDAKLTQTRKVKKPNSVVKKSHHVGKDDESRLDHLGVVAYNRKQRSIPLSPIVPESSDPAALKRARNTEAARRSRARKLQRMKQLEDKVEELLSKNYHLENEVARLKKLVGER Nuclear magnetic resonance spectroscopy 1 224 224 Undetermined 225 281 57 Disordered Weiss, M. A., Ellenberger, T., Wobbe, C. R., Lee, J. P., Harrison, S. C., and Struhl, K. Folding transition in the DNA-binding domain of GCN4 on specific binding to DNA 1990 Nature 347 575 578 Max protein Transcription factor MAX 126776 P25912 1AN2 160 MSDNDDIEVESDEEQPRFQSAADKRAHHNALERKRRDHIKDSFHSLRDSVPSLQGEKASRAQILDKATEYIQYMRRKNHTHQQDIDDLKRQNALLEQQVRALEKARSSAQLQTNYPSSDNSLYTNAKGSTISAFDGGSDSSSESEPEEPQSRKKLRMEAS Circular dichroism Other techniques 1 110 110 Disordered Function arises via a disorder to order transition Protein-DNA binding Protein-protein binding Horiuchi, M., Kurihara, Y., Katahira, M., Maeda, T., Saito, T., and Uesugi, S. Dimerization and DNA binding facilitate alpha-helix formation of Max in solution 1997 J. Biochem. (Tokyo) 122 711 716 Transcription factor p65 Nuclear factor NF-kappa-B p65 subunit Transcription factor NF-kappa B p65 417924 Q04206 1NFI 551 MDELFPLIFPAEPAQASGPYVEIIEQPKQRGMRFRYKCEGRSAGSIPGERSTDTTKTHPTIKINGYTGPGTVRISLVTKDPPHRPHPHELVGKDCRDGFYEAELCPDRCIHSFQNLGIQCVKKRDLEQAISQRIQTNNNPFQVPIEEQRGDYDLNAVRLCFQVTVRDPSGRPLRLPPVLPHPIFDNRAPNTAELKICRVNRNSGSCLGGDEIFLLCDKVQKEDIEVYFTGPGWEARGSFSQADVHRQVAIVFRTPPYADPSLQAPVRVSMQLRRPSDRELSEPMEFQYLPDTDDRHRIEEKRKRTYETFKSIMKKSPFSGPTDPRPPPRRIAVPSRSSASVPKPAPQPYPFTSSLSTINYDEFPTMVFPSGQISQASALAPAPPQVLPQAPAPAPAPAMVSALAQAPAPVPVLAPGPPQAVAPPAPKPTQAGEGTLSEALLQLQFDDEDLGALLGNSTDPAVFTDLASVDNSEFQQLLNQGIPVAPHTTEPMLMEYPEAITRLVTGAQRPPDPAPAPLGAPGLPNGLLSGDEDFSSIADMDFSALLSQISS Nuclear magnetic resonance spectroscopy 1 427 427 Undetermined 428 551 124 Disordered Function arises via a disorder to order transition Protein-protein binding Schmitz, M. L., dos Santos Silva, M. A., Altmann, H., Czisch, M., Holak, T. A., and Baeuerle, P. A. Structural and functional analysis of the NF-kappa B p65 C terminus. An acidic and modular transactivation domain with the potential to adopt an alpha-helical conformation 1994 J. Biol. Chem. 269 25613 25620 Cellular tumor antigen p53 Tumor suppressor p53 Phosphoprotein p53 Antigen NY-CO-13 Transcription factor p53 129369 P04637 1A1U 393 MEEPQSDPSVEPPLSQETFSDLWKLLPENNVLSPLPSQAMDDLMLSPDDIEQWFTEDPGPDEAPRMPEAAPPVAPAPAAPTPAAPAPAPSWPLSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVVRRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILTIITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNTSSSPQPKKKPLDGEYFTLQIRGRERFEMFRELNEALELKDAQAGKEPGGSRAHSSHLKSKKGQSTSRHKKLMFKTEGPDSD Circular dichroism 1 70 70 Disordered Function arises via a disorder to order transition Protein-protein binding 71 98 28 Undetermined 285 324 40 Undetermined 357 366 10 Undetermined 367 388 22 Disordered 389 393 5 Undetermined Chang, J., Kim, D. H., Lee, S. W., Choi, K. Y., and Sung, Y. C. Transactivation ability of p53 transcriptional activation domain is directly related to the binding affinity to TATA-binding protein 1995 J. Biol. Chem. 270 25014 25019 Kussie, P. H., Gorina, S., Marechal, V., Elenbaas, B., Moreau, J., Levine, A. J., and Pavletich, N. P. Structure of the MDM2 oncoprotein bound to the p53 tumor suppressor transactivation domain 1996 Science 274 948 953 ALPHA TRANS-INDUCING PROTEIN VMW65 ALPHA TRANS-INDUCING PROTEIN ICP25 VP16 PROTEIN ALPHA-TIF Transcription factor VP16 2827761 P23990 16vp 490 MDLLVDDLFADADGVSPPPPRPAGGPKNTPAAPPLYATGRLSQAQLMPSPPMPVPPAALFNRLLDDLGFSAGPALCTMLDTWNEDLFSGFPTNADMYRECKFLSTLPSDVIDWGDAHVPERSPIDIRAHGDVAFPTLPATRDELPSYYEAMAQFFRGELRAREESYRTVLANFCSALYRYLRASVRQLHRQAHMRGRNRDLREMLRTTIADRYYRETARLARVLFLHLYLFLSREILWAAYAEQMMRPDLFDGLCCDLESWRQLACLFQPLMFINGSLTVRGVPVEARRLRELNHIREHLNLPLVRSAAAEEPGAPLTTPPVLQGNQARSSGYFMLLIRAKLDSYSSVATSEGESVMREHAYSRGRTRNNYGSTIEGLLDLPDDDDAPAEAGLVAPRMSFLSAGQRPRRLSTTAPITDVSLGDELRLDGEEVDMTPADALDDFDLEMLGDVESPSPGMTHDPVSYGALDVDDFEFEQMFTDAMGIDDFGG Circular dichroism Limited proteolysis Nuclear magnetic resonance spectroscopy Other techniques X-ray crystallography 1 48 48 Undetermined 350 394 45 Disordered Function arises via a disorder to order transition Protein-DNA binding Protein-protein binding 403 490 88 Disordered Function arises via a disorder to order transition Protein-protein binding Shen, F., Triezenberg, S. J., Hensley, P., Porter, D., and Knutson, J. R. Critical amino acids in the transcriptional activation domain of the herpesvirus protein VP16 are solvent-exposed in highly mobile protein segments. An intrinsic fluorescence study 1996 J. Biol. Chem. 271 4827 4837 Uesugi, M., Nyanguile, O., Lu, H., Levine, A. J., and Verdine, G. L. Induced alpha helix in the VP16 activation domain upon binding to a human TAF 1997 Science 277 1310 1313 Liu, Y., Gong, W., Huang, C. C., Herr, W., and Cheng, X. Crystal structure of the conserved core of the herpes simplex virus transcriptional regulatory protein VP16 1999 Genes Dev. 13 1692 1703 Hayes, S., and O'Hare, P. Mapping of a major surface-exposed site in herpes simplex virus protein Vmw65 to a region of direct interaction in a transcription complex assembly 1993 J. Virol. 67 852 862 O'Hare, P., and Williams, G. Structural studies of the acidic transactivation domain of the Vmw65 protein of herpes simplex virus using 1H NMR 1992 Biochemistry 31 4150 4156 Donaldson, L., and Capone, J. P. Purification and characterization of the carboxyl-terminal transactivation domain of Vmw65 from herpes simplex virus type 1 1992 J. Biol. Chem. 267 1411 1414 Ubiquinol oxidase polypeptide I Cytochrome O subunit 1 Oxidase BO(3) subunit 1 Cytochrome O ubiquinol oxidase subunit 1 Ubiquinol oxidase chain A 118072 P18401 1FFT 663 MFGKLSLDAVPFHEPIVMVTIAGIILGGLALVGLITYFGKWTYLWKEWLTSVDHKRLGIMYIIVAIVMLLRGFADAIMMRSQQALASAGEAGFLPPHHYDQIFTAHGVIMIFFVAMPFVIGLMNLVVPLQIGARDVAFPFLNNLSFWFTVVGVILVNVSLGVGEFAQTGWLAYPPLSGIEYSPGVGVDYWIWSLQLSGIGTTLTGINFFVTILKMRAPGMTMFKMPVFTWASLCANVLIIASFPILTVTVALLTLDRYLGTHFFTNDMGGNMMMYINLIWAWGHPEVYILILPVFGVFSEIAATFSRKRLFGYTSLVWATVCITVLSFIVWLHHFFTMGAGANVNAFFGITTMIIAIPTGVKIFNWLFTMYQGRIVFHSAMLWTIGFIVTFSVGGMTGVLLAVPGADFVLHNSLFLIAHFHNVIIGGVVFGCFAGMTYWWPKAFGFKLNETWGKRAFWFWIIGFFVAFMPLYALGFMGMTRRLSQQIDPQFHTMLMIAASGAVLIALGILCLVIQMYVSIRDRDQNRDLTGDPWGGRTLEWATSSPPPFYNFAVVPHVHERDAFWEMKEKGEAYKKPDHYEEIHMPKNSGAGIVIAAFSTIFGFAMIWHIWWLAIVGFAGMIITWIVKSFDEDVDYYVPVAEIEKLENQHFDEITKAGLKNGN X-ray crystallography 1 51 51 Disordered Known to exist in disordered state, relationship to function unknown Unknown 553 663 111 Disordered Known to exist in disordered state, relationship to function unknown Unknown Wilmanns, M., Lappalainen, P., Kelly, M., Sauer-Eriksson, E., and Saraste, M. Crystal structure of the membrane-exposed domain from a respiratory quinol oxidase complex with an engineered dinuclear copper center 1995 Proc. Natl. Acad. Sci. USA 92 11955 11959 Abramson, J., Riistama, S., Larsson, G., Jasaitis, A., Svensson-Ek, M., Laakkonen, L., Puustinen, A., Iwata, S., and Wikstrom, M. The structure of the ubiquinol oxidase from Escherichia coli and its ubiquinone binding site 2000 Nat. Struct. Biol. 7 910 917 Ubiquinol oxidase polypeptide II precursor Cytochrome O subunit 2 Oxidase BO(3) subunit 2 Cytochrome O ubiquinol oxidase subunit 2 Ubiquinol oxidase chain B 118071 P18400 1FFT 315 MRLRKYNKSLGWLSLFAGTVLLSGCNSALLDPKGQIGLEQRSLILTAFGLMLIVVIPAILMAVGFAWKYRASNKDAKYSPNWSHSNKVEAVVWTVPILIIIFLAVLTWKTTHALEPSKPLAHDEKPITIEVVSMDWKWFFIYPEQGIATVNEIAFPANTPVYFKVTSNSVMNSFFIPRLGSQIYAMAGMQTRLHLIANEPGTYDGISASYSGPGFSGMKFKAIATPDRAAFDQWVAKAKQSPNTMSDMAAFEKLAAPSEYNQVEYFSNVKPDLFADVINKFMAHGKSMDMTQPEGEHSAHEGMEGMDMSHAESAH X-ray crystallography 1 26 26 Disordered 284 315 32 Disordered Known to exist in disordered state, relationship to function unknown Unknown PDB: 1cyw is part of the sequence potassium voltage-gated channel, shaker-related subfamily, member 1 [Homo sapiens] Voltage-gated potassium channel 4557685 Q09470 495 MTVMSGENVDEASAAPGHPQDGSYPRQADHDDHECCERVVINISGLRFETQLKTLAQFPNTLLGNPKKRMRYFDPLRNEYFFDRNRPSFDAILYYYQSGGRLRRPVNVPLDMFSEEIKFYELGEEAMEKFREDEGFIKEEERPLPEKEYQRQVWLLFEYPESSGPARVIAIVSVMVILISIVIFCLETLPELKDDKDFTGTVHRIDNTTVIYNSNIFTDPFFIVETLCIIWFSFELVVRFFACPSKTDFFKNIMNFIDIVAIIPYFITLGTEIAEQEGNQKGEQATSLAILRVIRLVRVFRIFKLSRHSKGLQILGQTLKASMRELGLLIFFLFIGVILFSSAVYFAEAEEAESHFSSIPDAFWWAVVSMTTVGYGDMYPVTIGGKIVGSLCAIAGVLTIALPVPVIVSNFNYFYHRETEGEEQAQLLHVSSPNLASDSDLSRRSSSTMSKYEYMEIEEDMNNSIAHYRQVNIRTANCTTANQNCVNKSKLLTDV Nuclear magnetic resonance spectroscopy 1 62 62 Disordered Function arises from the disordered (extended) state Autoregulatory Entropic clock Wissmann, R., Baukrowitz, T., Kalbacher, H., Kalbitzer, H. R., Ruppersberg, J. P., Pongs, O., Antz, C., and Fakler, B. NMR structure and functional characteristics of the hydrophilic N terminus of the potassium channel beta-subunit Kvbeta1.1 1999 J. Biol. Chem. 274 35521 35525 DNA-repair protein complementing XP-A cells homolog Xeroderma pigmentosum group A complementing protein homolog 139817 P27088 265 MEPEPEPEANKEEEKILSAAVRAKIERNRQRALMLRQARLACRPYPTGEGISTVKAPPKVIDSGGGFFIEEEEAEEQHVENVVRQPGPVLECDYLICEECGKDFMDSYLSNHFDLAVCDSCRDAEEKHKLITRTEAKQEYLLKDCDIDKREPVLKFILKKNPHNTHWGDMKLYLKAQVIKRSLEVWGSEEALEEAKEVRKDNRDKMKQKKFDKKVKELRRTVRSSLWKKEASGHQHEYGPEEHVEEDSYKKTCITCGYEMNYEKM 1 84 84 Disordered Function arises from the disordered (extended) state Protein-protein binding 181 265 85 Disordered Function arises from the disordered (extended) state Protein-protein binding Iakoucheva, L. M., Kimzey, A. L., Masselon, C. D., Bruce, J. E., Garner, E. C., Brown, C. J., Dunker, A. K., Smith, R. D., and Ackerman, E. J. Identification of intrinsic order and disorder in the DNA repair protein XPA 2001 Prot. Sci. 10 560 571 Serine/threonine protein phosphatase 2B catalytic subunit A1 EC 3.1.3.16 Calcineurin A1 Calmodulin-binding protein 1 171149 P23287 553 MSKDLNSSRIKIIKPNDSYIKVDRKKDLTKYELENGKVISTKDRPIASVPAITGKIPSDEEVFDSKTGLPNHSFLREHFFHEGRLSKEQAIKILNMSTVALSKEPNLLKLKAPITICGDIHGQYYDLLKLFEVGGDPAEIDYLFLGDYVDRGAFSFECLIYLYSLKLNNLGRFWMLRGNHECKHLTSYFTFKNEMLHKYDMEVYDACCRSFNVLPLAALMNGQYFCVHGGISPELKSVEDVNKINRFREIPSRGLMCDLLWADPVENYDDARDGSEFDQSEDEFVPNSLRGCSFAFTFKASCKFLKANGLLSIIRAHEAQDAGYRMYKNNKVTGFPSLITMFSAPNYLDTYHNKAAVLKYEENVMNIRQFHMSPHPYWLPDFMDVFTWSLPFVGEKVTSMLVSILNICSEQELDPESEPKAAEETVKARANATKETGTPSDEKASSAILEDETRRKALRNKILAIAKVSRMFSVLREESEKVEYLKTMNAGVLPRGALARGTEGLNETLSTFEKARKEDLINEKLPPSLSEVEQEKIKYYEKILKGAEKKPQL 409 510 102 Disordered Chain D, Complex Between Human T-Cell Receptor, Viral Peptide 2554793 1ao7 D 204 KEVEQNSGPLSVPEGAIASLNCTYSDRGSQSFFWYRQYSGKSPELIMSIYSNGDKEDGRFTAQLNKASQYVSLLIRDSQPSDSATYLCAVTTDSWGKLQFGAGTQVVVTPDIQNPDPAVYQLRDSKSSDKSVCLFTDFDSQTNVSQSKDSDVYITDKTVLDMRSMDFKSNSAVAWSNKSDFACANAFNNSIIPEDTFFPSPESS 125 204 80 Disordered Tyrosine 3-monooxygenase Tyrosine 3-hydroxylase TH 136577 P04177 498 MPTPSAPSPQPKGFRRAVSEQDAKQAEAVTSPRFIGRRQSLIEDARKEREAAAAAAAAAVASSEPGNPLEAVVFEERDGNAVLNLLFSLRGTKPSSLSRAVKVFETFEAKIHHLETRPAQRPLAGSPHLEYFVRFEVPSGDLAALLSSVRRVSDDVRSAREDKVPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQVYRQRRKLIAEIAFQYKHGEPIPHVEYTAEEIATWKEVYVTLKGLYATHACREHLEGFQLLERYCGYREDSIPQLEDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASSPMHSPEPDCCHELLGHVPMLADRTFAQFSQDIGLASLGASDEEIEKLSTVYWFTVEFGLCKQNGELKAYGAGLLSSYGELLHSLSEEPEVRAFDPDTAAVQPYQDQTYQPVYFVSESFNDAKDKLRNYASRIQRPFSVKFDPYTLAIDVLDSPHTIQRSLEGVQDELHTLAHALSAIS 1 155 155 Disordered Tyrosyl-tRNA synthetase Tyrosine--tRNA ligase TyrRS 135197 P00952 419 MDLLAELQWRGLVNQTTDEDGLRKLLNEERVTLYCGFDPTADSLHIGHLATILTMRRFQQAGHRPIALVGGATGLIGDPSGKKSERTLNAKETVEAWSARIKEQLGRFLDFEADGNPAKIKNNYDWIGPLDVITFLRDVGKHFSVNYMMAKESVQSRIETGISFTEFSYMMLQAYDFLRLYETEGCRLQIGGSDQWGNITAGLELIRKTKGEARAFGLTIPLVTKADGTKFGKTESGTIWLDKEKTSPYEFYQFWINTDDRDVIRYLKYFTFLSKEEIEALEQELREAPEKRAAQKTLAEEVTKLVHGEEALRQAIRISEALFSGDIANLTAAEIEQGFKDVPSFVHEGGDVPLVELLVSAGISPSKRQAREDIQNGAIYVNGERLQDVGAILTAEHRLEGRFTVIRRGKKKYYLIRYA 321 419 99 Disordered Dhp1 4hb1 108 SSEELLKQALQQAQQLLQQAQELAKKGGGEELLKQALQQAQQLLQQAQELAKKGGGGEELLKQALQQAQQLLQQAQELAKKGGGEELLKQALQQAQQLLQQAQELAKK 51 108 58 Disordered Amphiphysin 2 2145469 O08839 1bb9 115 MGSSHHHHHHSSGLVPRGSHMATVNGAVEGSTTTGRLDLPPGFMFKVQAQHDYTATDTDELQLKAGDVVLVIPFQNPEEQDEGWLMGVKESDWNQHKELEKCRGVFPENFTERVQ 1 32 32 Disordered Collagen Adhesin 1amx 180 MRGSHHHHHHGSITSGNKSTNVTVHKSEAGTSSVFYYKTGDMLPEDTTHVRWFLNINNEKSYVSKDITIKDQIQGGQQLDLSTLNINVTGTHSNYYSGQSAITDFEKAFPGSKITVDNTKNTIDVTIPQGYGSYNSFSINYKTKITNEQQKEFVNNSQAWYQEHGKEEVNGKSFNHTVHN 1 30 30 Disordered L-Arginine: Glycine Amidinotransferase 545385 P50440 1jdw 423 MLRVRCLRGGSRGAEAVHYIGSRLGRTLTGWVQRTFQSTQAATASSRNSCAADDKATEPLPKDCPVSSYNEWDPLEEVIVGRAENACVPPFTIEVKANTYEKYWPFYQKQGGHYFPKDHLKKAVAEIEEMCNILKTEGVTVRRPDPIDWSLKYKTPDFESTGLYSAMPRDILIVVGNEIIEAPMAWRSRFFEYRAYRSIIKDYFHRGAKWTTAPKPTMADELYNQDYPIHSVEDRHKLAAQGKFVTTEFEPCFDAADFIRAGRDIFAQRSQVTNYLGIEWMRRHLAPDYRVHIISFKDPNPMHIDATFNIIGPGIVLSNPDRPCHQIDLFKKAGWTIITPPTPIIPDDHPLWMSSKWLSMNVLMLDEKRVMVDANEVPIQKMFEKLGITTIKVNIRNANSLGGGFHCWTCDVRRRGTLQSYLD 1 63 63 Disordered Heat Shock Locus U 12518837 P32168 1do0 A 442 SEMTPREIVSELDKHIIGQDNAKRSVAIALRNRWRRMQLNEELRHEVTPKNILMIGPTGVGKTEIARRLAKLANAPFIKVEATKFTEVGYVGKEVDSIIRDLTDAAVKMVRVQAIEKNRYRAEELAEERILDVLIPPAKNNWGQTEQQQEPSAARQAFRKKLREGQLDDKEIEIDLAAAPMGVEIMAPPGMEEMTSQLQSMFQNLGGQKQKARKLKIKDAMKLLIEEEAAKLVNPEELKQDAIDAVEQHGIVFIDEIDKICKRGESSGPDVSREGVQRDLLPLVEGCTVSTKHGMVKTDHILFIASGAFQIAKPSDLIPELQGRLPIRVELQALTTSDFERILTEPNASITVQYKALMATEGVNIEFTDSGIKRIAEAAWQVNESTENIGARRLHTVLERLMEEISYDASDLSGQNITIDADYVSKHLDALVADEDLSRFIL 176 211 36 Disordered Factor Xa 1fax L 96 YKDGDQCETSPCQNQGKCKDGLGEYTCTCLEGFEGKNCELFTRKLCSLDNGDCDQFCHEEQASVVCSCARGYTLADNGKACIPTGPYPCGKQTLER 1 41 41 Disordered Myosin 1br2 A 791 AQKPLSDDEKFLFVDKNFVNNPLAQADWSAKKLVWVPSEKHGFEAASIKEEKGDEVTVELQENGKKVTLSKDDIQKMNPPKFSKVEDMAELTCLNEASVLHNLRERYFSGLIYTYSGLFCVVINPYKQLPIYSEKIIDMYKGKKRHEMPPHIYAIADTAYRSMLQDREDQSILCTGESGAGKTENTKKVIQYLAVVASSHKGKKDTSITQGPSFSYGELEKQLLQANPILEAFGNAKTVKNDNSSRFGKFIRINFDVTGYIVGANIETYLLEKSRAIRQAKDERTFHIFYYLIAGASEQMRNDLLLEGFNNYTFLSNGHVPIPAQQDDEMFQETLEAMTIMGFTEEEQTSILRVVSSVLQLGNIVFKKERNTDQASMPDNTAAQKVCHLMGINVTDFTRSILTPRIKVGRDVVQKAQTKEQADFAIEALAKAKFERLFRWILTRVNKALDKTKRQGASFLGILDIAGFEIFEINSFEQLCINYTNEKLQQLFNHTMFILEQEEYQREGIEWNFIDFGLDLQPCIELIERPTNPPGVLALLDEECWFPKATDTSFVEKLIQEQGNHAKFQKSKQLKDKTEFCILHYAGKVTYNASAWLTKNMDPLNDNVTSLLNQSSDKFVADLWKDVDRIVGLDQMAKMTESSLPSASKTKKGMFRTVGQLYKEQLTKLMTTLRNTNPNFVRCIIPNHEKRAGKLDAHLVLEQLRCNGVLEGIRICRQGFPNRIVFQEFRQRYEILAANAIPKGFMDGKQACILMIKALELDPNLYRIGQSKIFFRTGVLAHLEEERDLKI 1 32 32 Disordered 199 216 18 Disordered 626 655 30 Disordered Nucleotide Exchange Factor Grpe 1dkg B 197 MSSKEQKTPEGQAPEEIIMDQHEEIEAVEPEASAEQVDPRDEKVANLEAQLAEAQTRERDGILRVKAEMENLRRRTELDIEKAHKFALEKFINELLPVIDSLDRALEVADKANPDMSAMVEDIELTLKSMLDVVRKFGVEVIAETNVPLDPNVHQAIAMVESDDVAPGNVLGIMQKGYTLNGRTIRAAMVTVAKAKA 1 37 37 Disordered Yeast Tata-Box Binding Protein Ytbp 1ytf C 79 GSSALLDTDEVGSELDDSDDDYLISEGEEDGPDENLMLCLYDKVTRTKARWKCSLKDGVVTINRNDYTFQKAQVEAEWV 1 33 33 Disordered Diol Dehydratase 1dio B 224 MEINEKLLRQIIEDVLSEMKGSDKPVSFNAPAASAAPQATPPAGDGFLTEVGEARQGTQQDEVIIAVGPAFGLAQTVNIVGIPHKSILREVIAGIEEEGIKARVIRCFKSSDVAFVAVEGNRLSGSGISIGIQSKGTTVIHQQGLPPLSNLELFPQAPLLTLETYRQIGKNAARYAKRESPQPVPTLNDQMARPKYQAKSAILHIKETKYVVTGKNPQELRVAL 1 45 45 Disordered Diol Dehydratase 1dio G 173 MNTDAIESMVRDVLSRMNSLQGEAPAAAPAAGGASRSARVSDYPLANKHPEWVKTATNKTLDDFTLENVLSNKVTAQDMRITPETLRLQASIAKDAGRDRLAMNFERAAELTAVPDDRILEIYNALRPYRSTKEELLAIADDLESRYQAKICAAFVREAATLYVERKKLKGDD 1 36 36 Disordered Protein R2 Of Ribonucleotide Reductase 1xik A 375 AYTTFSQTKNDQLKEPMFFGQPVNVARYDQQKYDIFEKLIEKQLSFFWRPEEVDVSRDRIDYQALPEHEKHIFISNLKYQTLLDSIQGRSPNVALLPLISIPELETWVETWAFSETIHSRSYTHIIRNIVNDPSVVFDDIVTNEQIQKRAEGISSYYDELIEMTSYWHLLGEGTHTVNGKTVTVSLRELKKKLYLCLMSVNALEAIRFYVSFACSFAFAERELMEGNAKIIRLIARDEALHLTGTQHMLNLLRSGADDPEMAEIAEECKQECYDLFVQAAQQEKDWADYLFRDGSMIGLNKDILCQYVEYITNIRMQAVGLDLPFQTRSNPIPWINTWLVSDNVQVAPQEVEVSSYLVGQIDSEVDTDDLSNFQL 341 375 35 Disordered Fe-Only Hydrogenase (Larger Subunit) 1hfe L 421 MSRTVMERIEYEMHTPDPKADPDKLHFVQIDEAKCIGCDTCSQYCPTAAIFGEMGEPHSIPHIEACINCGQCLTHCPENAIYEAQSWVPEVEKKLKDGKVKCIAMPAPAVRYALGDAFGMPVGSVTTGKMLAALQKLGFAHCWDTEFTADVTIWEEGSEFVERLTKKSDMPLPQFTSCCPGWQKYAETYYPELLPHFSTCKSPIGMNGALAKTYGAERMKYDPKQVYTVSIMPCIAKKYEGLRPELKSSGMRDIDATLTTRELAYMIKKAGIDFAKLPDGKRDSLMGESTGGATIFGVTGGVMEAALRFAYEAVTGKKPDSWDFKAVRGLDGIKEATVNVGGTDVKVAVVHGAKRFKQVCDDVKAGKSPYHFIEYMACPGGCVCGGGQPVMPGVLEAMDRTTTRLYAGLKKRLAMASANKA 398 421 24 Disordered ADP-Ribosyltransferase 1qs1 A 462 MKRMEGKLFMVSKKLQVVTKTVLLSTVFSISLLNNEVIKAEQLNINSQSKYTNLQNLKITDKVEDFKEDKEKAKEWGKEKEKEWKLTATEKGKMNNFLDNKNDIKTNYKEITFSMAGSFEDEIKDLKEIDKMFDKTNLSNSIITYKNVEPTTIGFNKSLTEGNTINSDAMAQFKEQFLDRDIKFDSYLDTHLTAQQVSSKERVILKVTVPSGKGSTTPTKAGVILNNSEYKMLIDNGYMVHVDKVSKVVKKGVECLQIEGTLKKSLDFKNDINAEAHSWGMKNYEEWAKDLTDSQREALDGYARQDYKEINNYLRNQGGSGNEKLDAQIKNISDALGKKPIPENITVYRWCGMPEFGYQISDPLPSLKDFEEQFLNTIKEDKGYMSTSLSSERLAAFGSRKIILRLQVPKGSTGAYLSAIGGFASEKEILLDKDSKYHIDKVTEVIIKGVKRYVVDATLLTN 1 59 59 Disordered Carbonic Anhydrase 1qre A 247 MMFNKQIFTILILSLSLALAGSGCISEGAEDNVAQEITVDEFSNIRENPVTPWNPEPSAPVIDPTAYIDPQASVIGEVTIGANVMVSPMASIRSDEGMPIFVGDRSNVQDGVVLHALETINEEGEPIEDNIVEVDGKEYAVYIGNNVSLAHQSQVHGPAAVGDDTFIGMQAFVFKSKVGNNCVLEPRSAAIGVTIPDGRYIPAGMVVTSQAEADKLPEVTDDYAYSHTNEAVVYVNVHLAEGYKETS 1 37 37 Disordered Staphylococcal Nuclease Ob-Subdomain Sn-Ob 2sob 103 ATSTKKLHKEPATLIKAIDGDTVKLMYKGQPMTFRLLLVDTPETKHPKKGVEKYGPEASAFTKKMLENAKKIEVEFDKGQRTDKYGRVLAYIYADGKMVNEAL 1 103 103 Disordered dessication-related protein [Craterostigma plantagineum] 167473 155 MAQFGGEKYGGRHTDEYGNPIQQGAGAHRGGGIMGGGQQAGQHGTTGVLGHGTAGQHGTTGGGLGHGTAGTGGALGGQHRRSGSSSSSSSSESDGEGGRRKKGMKDKMKEKLPGGHGTTTDQQQYGTAATHGQAQQHEKKGIMDKIKEKLPGGQH 1 155 155 Disordered Involved in mediating targeting and transport of secretory proteins; forms a complex with Snc2p and Sec9p 6319289 117 MSSSTPFDPYALSEHDEERPQNVQSKSRTAELQAEIDDTVGIMRDNINKVAERGERLTSIEDKADNLAVSAQGFKRGANRVRKAMWYKDLKMKMCLALVIIILLVVIIVPIAVHFSR 1 93 93 Disordered tubulin, beta, 5 [Homo sapiens] 5174739 444 MREIVHLQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLERINVYYNEATGGNYVPRAVLVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDAVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKMREEFPDRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPAFAPLTSRGSQQYRGLTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGRMSMKEVDEQMLSVQSKNSSYFVEWIPNNVKTAVCDIPPRGLKMAVTFIGNSTAIQELFKRISEQFTAMFRRKAFLHWYTGEGMDEMEFTEAESNMNDLVSEYQQYQDATAEQGEFEEEAEEEVA 394 444 51 Disordered tubulin, alpha, ubiquitous [Homo sapiens] 5174477 451 MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVIDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIIDLVLDRIRKLADQCTRLQGFLVFHSFGGGTGSGFTSLLMERLSVDYGKKSKLEFSIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLISQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLSVADITNACFEPANQMVKCDPGHGKYMACCLLYRGDVVPKDVNAAIATIKTKRTIQFVDWCPTGFKVGINYQPPTVVPGGDLAKVQRAVCMLSNTTAIAEAWARLDHKFDLMYAKRAFVHWYVGEGMEEGEFSEAREDMAALEKDYEEVGVDSVEGEGEEEGEEY 404 451 48 Disordered Osteocalcin Gamma-carboxyglutamic acid-containing protein Bone Gla-protein BGP 3914247 P81455 49 YLDSGLGAPVPYPDPLEPKREVCELNPNCDELADHIGFQEAYQRFYGPV 1 49 49 Disordered Protein transport protein SEC61 gamma subunit 585962 P38384 68 MDQVMQFVEPSRQFVKDSIRLVKRCTKPDRKEFQKIAMATAIGFAIMGFIGFFVKLIHIPINNIIVGG 1 42 42 Disordered chromogranin A [Bos taurus] 1890672 449 MRSAAVLALLLCAGQVIALPVNSPMNKGDTEVMKCIVEVISDTLSKPSPMPVSKECFETLRGDERILSILRHQNLLKELQDLALQGAKERTHQQKKHSSYEDELSEVLEKPNDQAEPKEVTEEVSSKDAAEKRDDFKEVEKSDEDSDGDRPQASPGLGPGPKVEEDNQAPGEEEEAPSNAHPLASLPSPKYPGPQAKEDSEGPSQGPASREKGLSAEQGRQTEREEEEEKWEEAEAREKAVPEEESPPTAAFKPPPSLGNKETQRAAPGWPEDGAGKMGAEEAKPPEGKGEWSHSRQEEEEMARAPQVLFRGGKSGEPEQEEQLSKEWEDAKRWSKMDQLAKELTAEKRLEGEEEEEEDPDRSMRLSFRARGYGFRGPGLQLRRGWRPNSREDSVEAGLPLQVRGYPEEKKEEEGSANRRPEDQELESLSAIEAELEKVAHQLEELRRG 1 449 449 Disordered salivary proline-rich glycoprotein precursor PRB4 (large allele) 2144912 310 MLLILLSVALLALSSAESSSEDVSQEESLFLISGKPQGRRPQGGNQPQRPPPPPGKPQGPPPQGGNQSQGPPPPPGKPEGRPPQGGNQSQGPPPHPGKPERPPPQGGNQSQGPPPHPGKPESRPPQGGHQSQGPPPTPGKPEGPPPQGGNQSQGTPPPPGKPEGRPPQGGNQSQGPPPHPGKPERPPPQGGNQSHRPPPPPGKPERPPPQGGNQSQGPPPHPGKPEGPPPQEGNKSRSARSPPGKPQGPPQQEGNKPQGPPPPGKPQGPPPPGGNPQQPQAPPAGKPQGPPPPPQGGRPPRPAQGQQPPQ 17 310 294 Disordered Caldesmon CDM 2506984 P12957 771 MDDFERRRELRRQKREEMRLEAERLSYQRNDDDEEEAARERRRRARQERLRQKEEGDVSGEVTEKSEVNAQNSVAEEETKRSTDDEAALLERLARREERRQKRLQEALERQKEFDPTITDGSLSVPSRREVNNVEENEITGKEEKVETRQGRCEIEETETVTKSYQRNNWRQDGEEEGKKEEKDSEEEKPKEVPTEENQVDVAVEKSTDKEEVVETKTLAVNAENDTNAMLEGEQSITDAADKEKEEAEKEREKLEAEEKERLKAEEEKKAAEEKQKAEEEKKAAEERERAKAEEEKRAAEERERAKAEEERKAAEERERAKAEEERKAAEERAKAEEERKAAEERAKAEEERKAAEERAKAEKERKAAEERERAKAEEEKRAAEEKARLEAEKLKEKKKMEEKKAQEEKAQANLLRKQEEDKEAKVEAKKESLPEKLQPTSKKDQVKDNKDKEKAPKEEMKSVWDRKRGVPEQKAQNGERELTTPKLKSTENAFGRSNLKGAANAEAGSEKLKEKQQEAAVELDELKKRREERRKILEEEEQKKKQEEAERKIREEEEKKRMKEEIERRRAEAAEKRQKVPEDGVSEEKKPFKCFSPKGSSLKIEERAEFLNKSAQKSGMKPAHTTAVVSKIDSRLEQYTSAVVGNKAAKPAKPAASDLPVPAEGVRNIKSMWEKGNVFSSPGGTGTPNKETAGLKVGVSSRINEWLTKTPEGNKSPAPKPSDLRPGDVSGKRNLWEKQSVEKPAASSSKVTATGKKSETNGLRQFEKEP 636 771 136 Disordered L protein 333590 2141 MLDPGEVYDDPIDPIELEAEPRGTPTVPNILRNSDYNLNSPLIEDPARLMLEWLKTGNRPYRMTLTDNCSRSFRVLKDYFKKVDLGSLKVGGMAAQSMISLWLYGAHSESNRSRRCITDLAHFYSKSSPIEKLLNLTLGNRGLRIPPEGVLSCLERVDYDNAFGRYLANTYSSYLFFHVITLYMNALDWDEEKTILALWKDLTSVDIGKDLVKFKDQIWGLLIVTKDFVYSQSSNCLFDRNYTLMLKDLFLSRFNSLMVLLSPPEPRYSDDLISQLCQLYIAGDQVLSMCGNSGYEVIKILEPYVVNSLVQRAEKFRPLIHSLGDFPVFIKDKVSQLEETFGSCARRFFRALDQFDNIHDLVFVYGCYRHWGHPYIDYRKGLSKLYDQVHIKKVIDKSYQECLASDLARRILRWGFDKYSKWYLDSRFLARDHPLTPYIKTQTWPPKHIVDLVGDTWHKLPITQIFEIPESMDPSEILDDKSHSFTRTRLASWLSENRGGPVPSEKVIITALSKPPVNPREFLKSIDLGGLPDEDLIIGLKPKERELKIEGRFFALMSWNLRLYFVITEKLLANYILPLFDALTMTDNLNKVFKKLIDRVTGQGLLDYSRVTYAFHLDYEKWNNHQRLESTEDVFSVLDQVFGLKRVFSRTHEFFQKSWIYYSDRSDLIGLREDQIYCLDASNGPTCWNGQDGGLEGLRQKGWSLVSLLMIDRESQIRNTRTKVLAQGDNQVLCPTYMLSPGLSQEGLLYELESISRNAFSIYRAVEEGASKLGLIIKKEETMCSYDFLIYGKTPLFRGNILVPESKRWARVSCVSNDQIVNLANIMSTVSTNALTVAQHSQSLIKPMRDFLLMSVQAVFHYLLFSPILKGRVYKILSAEGESFLLAMSRIIYLDPSLGGVSGMSLGRFHIRQFSDPVSEGLSFWREIWLSSHESWIHALCQEAGNPDLGERTLESFTRLLEDPTTLNIRGGASPTILLKDAIRKALYDEVDKVENSEFREAILLSKTHRDNFILFLTSVEPLFPRFLSELFSSSFLGIPESIIGLIQNSRTIRRQFRKSLSKTLEESFYNSEIHGISRMTQTPQRVGGVWPCSSERADLLREISWGRKVVGTTVPHPSEMLGLLPKSSISCTCGATGGGNPRVSVSVLPSFDQSFFCTGPLKGYLGSSTSMSTQLFHAWEKVTNVHVVKRALSLKESINWFITRDSNLAQTLIRNIVSLTGPDFPLEEAPVFKRTGSALHRFKSARYSEGGYSSVCPNLLSHISVSTDTMSDLTQDGKNYDFMFQPLMLYAQTWTSELVQRDTRLRDSTFHWHLQCNRCVRPIDDVTLETSQIFEFPDVSKRISRMVSGAVPHFQRLPDIRLRPGDFESLSGREKSHHIGSAQGLLYSILVAIHDSGYNDGTIFPVNIYGKVSPRDYLRGLARGVLIGSSICFLTRMTNININRPLELISGVISYILLRLDNHPSLYIMLREPSFREEIFSIPQKIPAAYPTTMKEGNRSILCYLQHVLRYEREVITASPENDWLWIFSDFRSAKMTYLTLITYQSHLLLQRVERNLSKSMRDNLRQLSSLMRQVLGGHGEDTLESDDNIQRLLKDSLRRTRWVDQEVRHAARTMTGDYSPNKKVSRKVGCSEWVCSAQQVAVSTSANPAPVSELDIRALSKRFQNPLISGLRVVQWATGAHYKLKPILDDLNVFPSLCLVVGDGSGGISRAVLNMFPDAKLVFNSLLEVNDLMASGTHPLPPSAIMRGGNDIVSRVIDFDSIWEKPSDLRNLATWKYFQSVQKQVNMSYDLIICDAEVTDIASINRITLLMSDFALSIDGPLYLVFKTYGTMLVNPNYKAIQHLSRAFPSVTGFITQVTSSFSSELYLRFSKRGKFFRDAEYLTSSTLREMSLVLFNCSSPKSEMQRARSLNYQDLVRGFPEEIISNPYNEMIITLIDSDVESFLVHKMVDDLELQRGTLSKVAIIIAIMIVFSNRVFNVSKPLTDPLFYPPSDPKILRHFNICCSTMMYLSTALGDVPSFARLHDLYNRPITYYFRQVILGNVYLSWSWSNDTSVFKRVACNSSLSLSSHWIRLIYKIVKTTRLVGSIKDLSGEVERHLHRYNRWITLENIRSRSSLLDYSCLCIGYSWKPAHAKTLV 1 42 42 Disordered microtubule-associated protein 2 [Homo sapiens] 4505097 1826 MADERKDEAKAPHWTSAPLTEASAHSHPPEIKDQGGRGEGLVRSANGFPYREDEEGAFGEHGSQGTYSNTKENGINGELTSADRETAEEVSARIVQVVTAEAVAVLKAEQEKEAQHKDQTAALPLAAEETANLPPSPPPSPASEQTVTVEEDLLTASKMEFHDQQELTPSTAEPSDQKEKESEKQSSPGEDLKHAALVSQPETTKTYPDKKDMQGTEEEKAPLALFGHTLVASLEDMKQKTEPSLVVPGIDLPKEPPTPKEQKDWFIEMPTEAKKDEWGLVAPISPGPLTPMREKDVFDDIPKWEGKQFDSPMPSPFQGGSFTLPLDVMKNEIVTETSPFAPAFLQPDDKKSLQQTSGPATAKDSFKIEEPHEAKPDKMAEAPPSEAMTLPKDAHIPVVEEHVMGKVLEEEKEAINQETVQQRDTFTPSGQEPILTEKETELKLEEKTTISDKEAVPKESKPPKPADEEIGIIQTSTEHTFSEQKDQEPTTDMLKQDSFPVSLEQAVTDSAMTSKTLEKAMTEPSALIEKSSIQELFEMRVDDKDKIEGVGAATSAELDMPFYEDKSGMSKYFETSALKEEATKSIEPGSDYYELSDTRESVHESIDTMSPMHKNGDKEFQTGKESQPSPPAQEAGYSTLAQSYPSDLPEEPSSPQERMFTIDPKVYGEKRDLHSKNKDDLTLSRSLGLGGRSAIEQRSMSINLPMSCLDSIALGFNFGRGHDLSPLASDILTNTSGSMDEGDDYLPATTPALEKAPCFPVESKEEEQIEKVKATGEESTQAEISCESPFLAKDFYKNGTVMAPDLPEMLDLAGTRSRLASVSADAEVARRKSVPSETVVEDSRTGLPPVTDENHVIVKTDSQLEDLGYCVFNKYTVPLPSPVQDSENLSGESGTFYEGTDDKVRRDLATDLSLIEVKLAAAGRVKDEFSVDKEASAHISGDKSGLSKEFDQEKKANDRLDTVLEKSEEHADSKEHAKKTEEAGDEIETFGLGVTYEQALAKDLSIPTDASSEKAEKGLSSVPEIAEVEPSKKVEQGLDFAVQGQLDVKISDFGQMASGLNIDDRRATELKLEATQDMTPSSKAPQEADAFMGVESGHMKEGTKVSETEVKQKVAKPDLVHQEAVDKEESYESSGEHESLTMESLKADEGKKETSPESSLIQDEIAVKLSVEIPCPPAVSEADLATDERADVQMEFIQGPKEESKETPDISITPSDVAEPLHETIVSEPAEIQSEEEEIEAQGEYDKLLFRSDTLQITDLGVSGAREEFVETCPSEHKGVIESVVTIEDDFITVVQTTTDEGESGSHSVRFAALEQPEVERRPSPHDEEEFEVEEAAEAQAEPKDGSPEAPASPEREEVALSEYKTETYDDYKDETTIDDSIMDADSLWVDTQDDDRSIMTEQLETIPKEEKAEKEARRSSLEKHRKEKPFKTGRGRISTPERKVAKKEPSTVSRDEVRRKKAVYKKAELAKKTEVQAHSPSRKFILKPAIKYTRPTHLSCVKRKTTAAGGESALAPSVFKQAKDKVSDGVTKSPEKRSSLPRPSSILPPRRGVSGDRDENSFSLNSSISSSARRTTRSEPIRRAGKSGTSTPTTPGSTAITPGTPPSYSSRTPGTPGTPSYPRTPHTPGTPKSAILVPSEKKVAIIRTPPKSPATPKQLRLINQPLPDLKNVKSKIGSTDNIKYQPKGGQVQIVTKKIDLSHVTSKCGSLKNIDRPGGGRVKIESVKLDFKEKVQAKVGSLDNAHHVPGGGNVKIDSQKLNFREHAKARVDHGAEIITQSPGRSSVASPRRLSNVSSSGSINLLESPQLATLAEDVTAALAKQGL 1 1826 1826 Disordered nerve growth factor receptor precursor [Homo sapiens] 4505393 427 MGAGATGRAMDGPRLLLLLLLGVSLGGAKEACPTGLYTHSGECCKACNLGEGVAQPCGANQTVCEPCLDSVTFSDVVSATEPCKPCTECVGLQSMSAPCVEADDAVCRCAYGYYQDETTGRCEACRVCEAGSGLVFSCQDKQNTVCEECPDGTYSDEANHVDPCLPCTVCEDTERQLRECTRWADAECEEIPGRWITRSTPPEGSDSTAPSTQEPEAPPEQDLIASTVAGVVTTVMGSSQPVVTRGTTDNLIPVYCSILAAVVVGLVAYIAFKRWNSCKQNKQGANSRPVNQTPPPEGEKLHSDSGISVDSQSLHDQQPHTQTASGQALKGDGGLYSSLPPAKREEVEKLLNGSAGDTWRHLAGELGYQPEHIDSFTHEACPVRALLASWATQDSATLDALLAALRRIQRADLVESLCSESTATSPV 1 222 222 Disordered chromogranin B [Bos taurus] 2052401 646 MQPAALLGLLGATVVAAVSSMPVDIRNHNEEVVTHCIIEVLSNALLKSSAPPITPECRQVLKKNGKELKDEEKSENENTRFEVRLLRDPADTSEAPGLSSREDSGEGDAQVPTVADTESGGHSRERAGEPPGSQVAKEAKTRYSKSEGQNREEEMVKYQKRERGEVGSEERLSEGPGKAQMAFLNQRNQTPAKKEELVSRYDTQSARGLEKSHSRERSSQESGEETKSQENWPQELQRHPEGQEAPGESEEDASPEVDKRRSRPRHHHGRSRPDRSSQEGNPPLEEESHVGTGNSDEEKARHPAHFRALEEGAEYGEEVRRHSAAQAPGDLQGARFGGRGRGEHQALRRPSEESLEQENKRHGLSPDLNMAQGYSEESEEERGPARGPSYRARGGEAAAYSTLGQTDEKRFLGETHHRVQESQRDKARRRLPGELRNYLDYGEEKGEEAARGKWQPQGDPRDADENREEARLRGKQYAPHHITEKRLGELLNPFYDPSQWKSSRFERKDPMDDSFLEGEEENGLTLNEKNFFPEYNYDWWEKKPFEEDVNWGYEKRNPVPKLDLKRQYDRVAELDQLLHYRKKSAEFPDFYDSEEQVSPQHTAENEEEKAGQGVLTEEEEKELENLAAMDLELQKIAEKFSGTRRG 1 646 646 Disordered SOMATOLIBERIN GROWTH HORMONE-RELEASING FACTOR GRF GROWTH HORMONE-RELEASING HORMONE GHRH 1173446 P42692 45 HADGMFNKAYRKALGQLSARKYLHTLMAKRVGGGSMIEDDNEPLS 1 45 45 Disordered MICROTUBULE-ASSOCIATED PROTEIN TAU 3915884 P10636 441 MAEPRQEFEVMEDHAGTYGLGDRKDQGGYTMHQDQEGDTDAGLKESPLQTPTEDGSEEPGSETSDAKSTPTAEDVTAPLVDEGAPGKQAAAQPHTEIPEGTTAEEAGIGDTPSLEDEAAGHVTQARMVSKSKDGTGSDDKKAKGADGKTKIATPRGAAPPGQKGQANATRIPAKTPPAPKTPPSSGEPPKSGDRSGYSSPGSPGTPGSRSRTPSLPTPPTREPKKVAVVRTPPKSPSSAKSRLQTAPVPMPDLKNVKSKIGSTENLKHQPGGGKVQIINKKLDLSNVQSKCGSKDNIKHVPGGGSVQIVYKPVDLSKVTSKCGSLGNIHHKPGGGQVEVKSEKLDFKDRVQSKIGSLDNITHVPGGGNKKIETHKLTFRENAKAKTDHGAEIVYKSPVVSGDTSPRHLSNVSSTGSIDMVDSPQLATLADEVSASLAKQGL 1 441 441 Disordered fibronecin binding protein [Streptococcus dysgalactiae] 288969 1091 MTNCKYKLRKLSIGLVSVGTMFMAAPVMGEDASQPTASVTTESPAIQTEEDQGSQAEALEEPTPAPQTSPSTVSAVPAEAAAMADEKGIAEAPAHEPAPKASVQAEAASPAGKAEATTNTGQPTNTEQARSRSKRAAEIAPQTIEVEKLEVDKENSSLTVKDGEKDKQLIKHRDGNQRDIFDISRDVKVNQDGTMDVTLTVKPKQIDEGAEVIVLLDTSQKMTETDFNTAKENIKKLVTTLTGTTDKEGKNVSHYNNRNSVRLIDFYRKVGESTDLSGWDAKKIDEKLNEVWKKAKDDYNGWGVDLQGAIHKAREIFNLDKEKRSGKRQHIVLFSQGESTFSYDIKDKSKMDKVAVEEPVTYSNPLFPWPFYFDTTTRTHNVVNDAKKLIDFLNKLGISQFNGAVDNVATVGNTLLGLGSFFGLKNPLDYISLADLETSKLNSEKFDYSRRVGEGYNFRSYFDREVDKVGFKKILVEKIKGNLKKFQPKQTDTWLSSLGLNSIKEKIQDWMIDKALDNLFYRRQYQFYNHNLSAQAEARMAREEGIKFYAVDVTEPERIAKEINSQKYSEAYTNHLKKKAEEARELAKKRNEKFDKYLKEMSESQKFFKDVEDPEKFKDILTELKVTETFEEKVSVNNSEQRKSNKEVEYKKASSNSSFLSFIFSSSTNESITWTLSKDKLQKALQSGETLTLEYKLKIHKDKFKLAPQTRSKRSLDTSENKKSVTEKVITSDVKYKINDKEVKGKELDDVSLTYSKETVRKPQVEPNVPDTPQEKPLTPLAPSEPSQPSIPETPLIPSEPSVPETSTPEGPTEGENNLGGQSEEITITEDSQSGMSGQNPGSGNETVVEDTQTSQEDIVLGGPGQVIDFTEDSQPGMSGNNSHTITEDSKPSQEDEVIIGGQGQVIDFTEDTQSGMSGDNSHTDGTVLEEDSKPSQEDEVIIGGQGQVIDFTEDTQTGMSGAGQVESPTITEETHKPEIIMGGQSDPIDMVEDTLPGMSGSNEATVVEEDTRPKLQFHFDNEEPVPATVPTVSQTPIAQVESKVPHAKAESALPQTGDTNKLETFFTITALTVIGAAGLLGKKRRNNQTD 810 969 160 Disordered Protein transport protein SEC9 730733 P40357 651 MGLKKFFKIKPPEEATPEQNKDTLMELGISVKNPSKKRKEKFAAYGKFANDKAEDKVYAPPGYEQYARPQDELEDLNASPLDANANEATAGSNRGSSGTQDLGNGAESNSMQDPYAIENDDYRYDDDPYARFQANKSNGRGSVNAAPYGDYGGGYNGTSLNSYNNDGPYSNQNTSNSWVNANGRNSLNHSNSTLNVGPSRQTRQPPVSTSTNSLSLDQRSPLANPMQEKRNPYADMNSYGGAYDSNTNRSSGTRQGSSKNANPYASMANDSYSNGNLNRSANPYSSRSVRQPQSQQAPMTYTPSFIASDEAARNSEVDLNEEPRTGEFDFEEVYADKSAENRAALDEPDLNAVMTNEDSIDLNASEVDHSSRQQQQQQWFMDEQQQQQQHFNATNNQYGDQRGYKTFEEIQKEEEARQQQEEDEAVDEIKQEIKFTKQSSVASTRNTLKMAQDAERAGMNTLGMLGHQSEQLNNVEGNLDLMKVQNKVADEKVAELKKLNRSILAVHVSNPFNSKRRRREREEQLKNRKIEEKLMREQTSQQLSQSTQRIEGAMNANNNISEVRERYQRKNVLEKAKRYQFENDEEDDEMELEIDRNLDQIQQVSNRLKKMALTTGKELDSQQKRLNNIEESTDDLDINLHMNTNRLAGIR 544 646 103 Disordered Nuclear factor NF-kappa-B p100 subunit H2TF1 Oncogene LYT-10 Lyt10 1708619 Q00653 898 MESCYNPGLDGIIEYDDFKLNSSIVEPKEPAPETADGPYLVIVEQPKQRGFRFRYGCEGPSHGGLPGASSEKGRKTYPTVKICNYEGPAKIEVDLVTHSDPPRAHAHSLVGKQCSELGICAVSVGPKDMTAQFNNLGVLHVTKKNMMGTMIQKLQRQRLRSRPQGLTEAEQRELEQEAKELKKVMDLSIVRLRFSAFLRASDGSFSLPLKPVTSQPIHDSKSPGASNLKISRMDKTAGSVRGGDEVYLLCDKVQKDDIEVRFYEDDENGWQAFGDFSPTDVHKQYAIVFRTPPYHKMKIERPVTVFLQLKRKRGGDVSDSKQFTYYPLVEDKEEVQRKRRKALPTFSQPFGGGSHMGGGSGGAAGGYGGAGGGGSLGFFPSSLAYSPYQSGAGPMRCYPGGGGGAQMAATVPSRDSGEEAAEPSAPSRTPQCEPQAPEMLQRAREYNARLFGLAHAAPSPTRLLRHRGRRALLAGQRHLLTAQDENGDTPLHLAIIHGQTSVIEQIVYVIHHAQDLGVVNLTNHLHQTPLHLAVITGQTSVVSFLLRVGADPALLDRHGDSAMHLALRAGAGAPELLRALLQSGAPAVPQLLHMPDFEGLYPVHLAVRARSPECLDLLVDSGAEVEATERQGGRTALHLATEMEELGLVTHLVTKLRANVNARTFAGNTPLHLAAGLGYPTLTRLLLKAGADIHAENEEPLCPLPSPPTSDSDSDSEGPEKDTRSSFRGHTPLDLTCSTLVKTLLLNAAQNTMEPPLTPPSPAGPGLSLGDTALQNLEQLLDGPEAQGSWAELAERLGLRSLVDTYRQTTSPSGSLLRSYELAGGDLAGLLEALSDMGLEEGVRLLRGPETRDKLPSTEVKEDSAYGSQSVEQEAEKLGPPPEPPGGLSHGHPQPQVH 864 898 35 Disordered small proline-rich protein 2 385227 72 MSYQQQQCKQPCQPPPVCPTPKCPEPCPPPKCPEPCPPPKCPQPCPPQQCQQKYPPVTPSPPCQPKYPPKSK 1 72 72 Disordered histidine-rich protein II [Plasmodium falciparum] 4877961 339 MVSFSKNKVLSAAVFASVLLLDNNNSAFNNNLCSKNAKGLNLNKRLLHETQAHVDDAHHAHHVADAHHAHHAADAHHAHHAADAHHAHHAADAHHAHHAADAHHAHHAAYAHHAHHAADAHRAHHASDAHHAADAHHAAYAHTAHHAADAHHAHHASDAHHAADAHHAAYAHHAHHAADAHHAHHASDAHHAGDAHHAAYAHHAHHAADAHHAADAHHATDAHHAHHAADAHHATDAHHAADAHHATDAHHAADAHHAADAHHATDAHHAADAHHATDVHHAADAHHAADAHHATDAHHAHHAADAHHAPAHHATDAHHATDAHHAAAHHEAATHCLRH 1 339 339 Disordered Calsequestrin, skeletal muscle isoform precursor Calsequestrin 1 Aspartactin Laminin-binding protein 115537 P07221 395 MNAADRMGARVALLLLLVLGSPQSGVHGEEGLDFPEYDGVDRVINVNAKNYKNVFKKYEVLALLYHEPPEDDKASQRQFEMEELILELAAQVLEDKGVGFGLVDSEKDAAVAKKLGLTEEDSIYVFKEDEVIEYDGEFSADTLVEFLLDVLEDPVELIEGERELQAFENIEDEIKLIGYFKNKDSEHYKAFKEAAEEFHPYIPFFATFDSKVAKKLTLKLNEIDFYEAFMEEPVTIPDKPNSEEEIVNFVEEHRRSTLRKLKPESMYETWEDDMDGIHIVAFAEEADPDGYEFLEILKSVAQDNTDNPDLSIIWIDPDDFPLLVPYWEKTFDIDLSAPQIGVVNVTDADSVWMEMDDEEDLPSAEELEDWLEDVLEGEINTEDDDDEDDDDDDDD 29 395 367 Disordered photosystem II manganese stabilizing protein [Cyanothece sp. ATCC 51142] 6478777 277 MIMRFRTLLIAFLALCLGLITACSEGPANAVNPQDLTYDEILNTGLANKCPQISEFTRGSIPIEPGQTYFVDDLCLEPQEYFVKEEPVNKRQEAEYVPGKLLTRYTTSLEQISGKITVDEDGVVTFYEEGGIDFQPVTVQLPGGEQVPFFFTIKNLVGKTEPGFSSINSSIDFEGDFRVPSYRGATFLDPKGRGLATGYDNAVALPATADKEDYANVKQTPIGKGSISLQVTKVDQATGEIAGVFDSEQPSDTDLGAKEPVEVKIRGIFYARVTPEA 1 244 244 Disordered integrase [Human immunodeficiency virus type 1] 6006964 95 IPAETGQETAYFLLKLAARWPVKIIHTDNGPNFTSATMKAACWWTNIQHEFGIPYNPQSQGVVEAMNKELKSIIQQVRDQTEHLRTAVQMAVFVH 1 55 55 Disordered protamine 2; Sperm protamine P2 [Homo sapiens] 4506111 102 MVRYRVRSLSERSHEVYRQQLHGQEQGHHGQEEQGLSRMHVEVYERTHGQSQYRRRHCSRRRLHRIHRRQHRSCRRRKRRSCRHRRRHRRGCRTRKRTCRRH 1 102 102 Disordered HISTONE H1.2 H1D 1170152 P15865 219 MSETAPAAPAAPAPAEKTPIKKKARKAAGGAKRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEAKPKAKKAGAAKAKKPAGAAKKPKKATGTATPKKSTKKTPKKAKKPAAAAGAKKAKSPKKAKATKAKKAPKSPAKARAVKPKAAKPKTSKPKAAKPKKTAAKKK 1 219 219 Disordered Hirudin variant-1 Lepirudin 124981 P01050 65 VVYTDCTESGQNLCLCEGSNVCGQGNKCILGSDGEKNQCVTGEGTPKPQSHNDGDFEEIPEEYLQ 1 65 65 Disordered Parathyroid hormone-related protein precursor PTH-rP PTHrP 131542 P12272 177 MQRRLVQQWSVAVFLLSYAVPSCGRSVEGLSRRLKRAVSEHQLLHDKGKSIQDLRRRFFLHHLIAEIHTAEIRATSEVSPNSKPSPNTKNHPVRFGSDDEGRYLTQETNKVETYKEQPLKTPGKKKKGKPGKRKEQEKKKRRTRSAWLDSGVTGSGLEGDHLSDTSTTSLELDSRRH 37 177 141 Disordered 50S ribosomal protein L2 132854 P02387 273 MAVVKCKPTSPGRRHVVKVVNPELHKGKPFAPLLEKNSKSGGRNNNGRITTRHIGGGHKQAYRIVDFKRNKDGIPAVVERLEYDPNRSANIALVLYKDGERRYILAPKGLKAGDQIQSGVDAAIKPGNTLPMRNIPVGSTVHNVEMKPGKGGQLARSAGTYVQIVARDGAYVTLRLRSGEMRKVEADCRATLGEVGNAEHMLRVLGKAGAARWRGVRPTVRGTAMNPVDHPHGGGEGRNFGKHPVTPWGVQTKGKKTRSNKRTDKFIVRRRSK 1 273 273 Disordered 50S ribosomal protein L27 132831 P02427 85 MAHKKAGGSTRNGRDSEAKRLGVKRFGGESVLAGSIIVRQRGTKFHAGANVGCGRDHTLFAKADGKVKFEVKGPKNRKFISIEAE 1 85 85 Disordered 50S ribosomal protein L31 417667 P02432 70 MKKDIHPKYEEITASCSCGNVMKIRSTVGHDLNLDVCSKCHPFFTGKQRDVATGGRVDRFNKRFNIPGSK 1 70 70 Disordered 50S ribosomal protein L32 132884 P02435 57 MAVQQNKPTRSKRGMRRSHDALTAVTSLSVDKTSGEKHLRHHITADGYYRGRKVIAK 1 57 57 Disordered 50S ribosomal protein L33 132895 P02436 55 MAKGIREKIKLVSSAGTGHFYTTTKNKRTKPEKLELKKFDPVVRQHVIYKEAKIK 1 55 55 Disordered 50S ribosomal protein L34 132905 P02437 46 MKRTFQPSVLKRNRSHGFRARMATKNGRQVLARRRAKGRARLTVSK 1 46 46 Disordered 30S ribosomal protein S12 133737 P02367 124 MATVNQLVRKPRARKVAKSNVPALEACPQKRGVCTRVYTTTPKKPNSALRKVCRVRLTNGFEVTSYIGGEGHNLQEHSVILIRGGRVKDLPGVRYHTVRGALDCSGVKDRKQARSKYGVKRPKA 1 124 124 Disordered 30S ribosomal protein S18 133836 P02374 75 MARYFRRRKFCRFTAEGVQEIDYKDIATLKNYITESGKIVPSRITGTRAKYQRQLARAIKRARYLSLLPYTDRHQ 1 75 75 Disordered 30S ribosomal protein S19 133848 P02375 92 MPRSLKKGPFIDLHLLKKVEKAVESGDKKPLRTWSRRSTIFPNMIGLTIAVHNGRQHVPVFVTDEMVGHKLGEFAPTRTYRGHAADKKAKKK 1 92 92 Disordered 30S ribosomal protein S21 133878 P02379 71 MPVIKVRENEPFDVALRRFKRSCEKAGVLAEVRRREFYEKPTTERKRAKASAVKRHAKKLARENARRTRLY 1 71 71 Disordered phospholamban - dog 89054 A29002 52 MDKVQYLTRSAIRRASTIEMPQQARQNLQNLFINFCLILICLLLICIIVMLL 1 31 31 Disordered Neurofilament triplet M protein 160 kDa neurofilament protein Neurofilament medium polypeptide NF-M P08553 848 SYTLDSLGNPSAYRRVPTETRSSFSRVSGSPSSGFRSQSWSRGSPSTVSSSYTRSAVAPRLAYSSAMLSSAESSLDFSQSSSLLNGGSGGDYKLSRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEESSMVKVELDKKVQSLQDEVAFLRRNHEEEVADLLAQIQASHITVERKDYLKTDISTALKEIRSQLECHSDQNMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEEIAEYRRQLQSKSIELESVRGTKESLERQLSDIEERHNHDLSSYQDTIQQLENELRGTKWEMARHLREYQDLLNVKMALDIEIAAYRKLLEGEETRFSTFSGSITGPLYTHRQPSVTISSKIQKTKVEAPKLKVQHKFVEEIIEETKVEDEKSEMEETLTAIAEELAASAKEEKEEAEEKEEEPEAEKSPVKSPEAKEEEEEGEKEEEEEGQEEEEEEDEGVKSDQAEEGGSEKEGSSEKDEGEQEEEEGETEAEGEGEEAEAKEEKKIEGKVEEVAVKEEIKVEKPEKAKSPMPKSPVEEVKPKPEAKAGKGEQKEEEKVEEEKKEVTKESPKEEKVEKKEEKPKDVADKKKAESPVKEKAVEEVITISKSVKVSLEKDTKEEKPQPQEKVKEKAEEEGGSEEEGSDRSPQESKKEDIAINGEVEGKEEEEQETQEKGSGREEEKGVVTNGLDVSPAEEKKGEDSSDDKVVVTKKVEKITSEGGDGATKYITKSVTVTQKVEEHEETFEEKLVSTKKVEKVTSHAIVKEVTQGD 411 848 438 Disordered Neurofilament triplet L protein 68 kDa neurofilament protein Neurofilament light polypeptide NF-L Micro glutamic acid-rich protein P02548 554 SSFSYEPYYSTSYKRRYVETPRVHISSVRSGYSTARSAYSSYSAPVSSSLSVRRSYSSSSGSLMPSLESLDLSQVAAISNDLKSIRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLRLAAEDATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEIAFLKKVHEEEIAELQAQIQYAQISVEMDVSSKPDLSAALKDIRAQYEKLAAKNMQNAEEWFKSRFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKTLEIEACRGMNEALEKQLQELEDKQNADISAMQDTINKLENELRTTKSEMARYLKEYQDLLNVKMALDIEIAAYRKLLEGEETRLSFTSVGSLTTGYTQSSQVFGRSAYGGLQTSSYLMSARSFPSYYTSHVQEEQIEVEETIEAAKAEEAKDEPPSEGEAEEEEKEKEEAEAEAEAEAEAEAEEEEGAQEEEAAKEDAEEAKEEEGGEGEEAEETKEAEEEEKKDEGAGEEQATKKKD 397 554 158 Disordered DNA repair protein XRCC4 5706611 334 MERKISRIHLVSEPSITHFLQVSWEKTLESGFVITLTDGHSAWTGTVSESEISQEADDMAMEKGKYVGELRKALLSGAGPADVYTFNFSKESCYFFFEKNLKDVSFRLGSFNLEKVENPAEVIRELICYCLDTIAENQAKNEHLQKENERLLRDWNDVQGRFEKCVSAKEALETDLYKRFILVLNEKKTKIRSLHNKLLNAAQEREKDIKQEGETAICSEMTADRDPVYDESTDEESENQTDLSGLASAAVSKDDSIISSLDVTDIAPSRKRRQRMQRNLGTEPKMAPQENQLQEKEKPDSSLPETSKKEHISAENMSLETLRNSSPEDLFDEI 179 265 87 Disordered 266 334 69 Undetermined PDB: 1fu1, chain A is part of the sequence