IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ Structural basis for recognition of SMRT/N-CoR by the MYND domain and its contribution to AML1/ETO's activity. Structural basis for recognition of SMRT/N-CoR by the MYND domain and its contribution to AML1/ETO's activity. Cancer Cell (1535-6108) 2007 imex curation Liu Y., Chen W., Gaudet J., Cheney MD., Roudaia L., Cierpicki T., Klet RC., Hartman K., Laue TM., Speck NA., Bushweller JH. Cancer - Interactions investigated in the context of cancer The interaction detailed in S4 B was not curated as it is not clear how trimeric species arises and lack of inter-molecular NOEs suggests it is a very low affinity interaction. 15N-1H HSQC titration was performed at pH 6.0 and 37 C at 500 MHz. nancy.speck@dartmouth.edu,jhb4v@virginia.edu 07-Aug-2007: Contacted by JYOTI. Only protein-protein interactions 5 in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined Liu Y., Chen W., Gaudet J., Cheney MD., Roudaia L., Cierpicki T., Klet RC., Hartman K., Laue TM., Speck NA., Bushweller JH. Cancer - Interactions investigated in the context of cancer The interaction detailed in S4 B was not curated as it is not clear how trimeric species arises and lack of inter-molecular NOEs suggests it is a very low affinity interaction. 15N-1H HSQC titration was performed at pH 6.0 and 37 C at 500 MHz. nancy.speck@dartmouth.edu,jhb4v@virginia.edu Accepted 2007-JUL-27 by JYOTI. Cancer Cell (1535-6108) 2007 Only protein-protein interactions 5 imex curation Structural basis for recognition of SMRT/N-CoR by the MYND domain and its contribution to AML1/ETO's activity. Structural basis for recognition of SMRT/N-CoR by the MYND domain and its contribution to AML1/ETO's activity. Cancer Cell (1535-6108) 2007 imex curation Liu Y., Chen W., Gaudet J., Cheney MD., Roudaia L., Cierpicki T., Klet RC., Hartman K., Laue TM., Speck NA., Bushweller JH. Cancer - Interactions investigated in the context of cancer The interaction detailed in S4 B was not curated as it is not clear how trimeric species arises and lack of inter-molecular NOEs suggests it is a very low affinity interaction. 15N-1H HSQC titration was performed at pH 6.0 and 37 C at 500 MHz. nancy.speck@dartmouth.edu,jhb4v@virginia.edu 07-Aug-2007: Contacted by JYOTI. Only protein-protein interactions 5 in vitro In vitro fluorescence fluorescence technology fluorescence predetermined predetermined participant predetermined Liu Y., Chen W., Gaudet J., Cheney MD., Roudaia L., Cierpicki T., Klet RC., Hartman K., Laue TM., Speck NA., Bushweller JH. Cancer - Interactions investigated in the context of cancer The interaction detailed in S4 B was not curated as it is not clear how trimeric species arises and lack of inter-molecular NOEs suggests it is a very low affinity interaction. Fluoresence anisotropy measurements on 70 fluorescein-labeled peptides spanning residues 1031-1273 of SMRT were made in the presence and absence of the MYND domain of AML1-MTG8 and in the presence of MYND mutants. 15N-1H HSQC titration was performed at pH 6.0 and 37 C at 500 MHz. nancy.speck@dartmouth.edu,jhb4v@virginia.edu Accepted 2007-JUL-27 by JYOTI. 07-Aug-2007: Contacted by JYOTI. Cancer Cell (1535-6108) 2007 Only protein-protein interactions 5 imex curation Structural basis for recognition of SMRT/N-CoR by the MYND domain and its contribution to AML1/ETO's activity. Structural basis for recognition of SMRT/N-CoR by the MYND domain and its contribution to AML1/ETO's activity. Cancer Cell (1535-6108) 2007 imex curation Liu Y., Chen W., Gaudet J., Cheney MD., Roudaia L., Cierpicki T., Klet RC., Hartman K., Laue TM., Speck NA., Bushweller JH. Cancer - Interactions investigated in the context of cancer The interaction detailed in S4 B was not curated as it is not clear how trimeric species arises and lack of inter-molecular NOEs suggests it is a very low affinity interaction. 15N-1H HSQC titration was performed at pH 6.0 and 37 C at 500 MHz. nancy.speck@dartmouth.edu,jhb4v@virginia.edu 07-Aug-2007: Contacted by JYOTI. Only protein-protein interactions 5 in vitro In vitro itc isothermal titration calorimetry ITC ITC itc predetermined predetermined participant predetermined Liu Y., Chen W., Gaudet J., Cheney MD., Roudaia L., Cierpicki T., Klet RC., Hartman K., Laue TM., Speck NA., Bushweller JH. Cancer - Interactions investigated in the context of cancer The interaction detailed in S4 B was not curated as it is not clear how trimeric species arises and lack of inter-molecular NOEs suggests it is a very low affinity interaction. Isothermal titration calometry (ITC) was used to determine stoichiometry and Kd between the MYND domain and SMRT and N-CoR peptides. nancy.speck@dartmouth.edu,jhb4v@virginia.edu Accepted 2007-JUL-27 by JYOTI. 07-Aug-2007: Contacted by JYOTI. Cancer Cell (1535-6108) 2007 Only protein-protein interactions 5 imex curation Structural basis for recognition of SMRT/N-CoR by the MYND domain and its contribution to AML1/ETO's activity. Structural basis for recognition of SMRT/N-CoR by the MYND domain and its contribution to AML1/ETO's activity. Cancer Cell (1535-6108) 2007 imex curation Liu Y., Chen W., Gaudet J., Cheney MD., Roudaia L., Cierpicki T., Klet RC., Hartman K., Laue TM., Speck NA., Bushweller JH. Cancer - Interactions investigated in the context of cancer The interaction detailed in S4 B was not curated as it is not clear how trimeric species arises and lack of inter-molecular NOEs suggests it is a very low affinity interaction. 15N-1H HSQC titration was performed at pH 6.0 and 37 C at 500 MHz. nancy.speck@dartmouth.edu,jhb4v@virginia.edu 07-Aug-2007: Contacted by JYOTI. Only protein-protein interactions 5 in vitro In vitro solution sedimentati cosedimentation in solution solution sedimentati predetermined predetermined participant predetermined Liu Y., Chen W., Gaudet J., Cheney MD., Roudaia L., Cierpicki T., Klet RC., Hartman K., Laue TM., Speck NA., Bushweller JH. Cancer - Interactions investigated in the context of cancer The interaction detailed in S4 B was not curated as it is not clear how trimeric species arises and lack of inter-molecular NOEs suggests it is a very low affinity interaction. nancy.speck@dartmouth.edu,jhb4v@virginia.edu Accepted 2007-JUL-27 by JYOTI. 07-Aug-2007: Contacted by JYOTI. Cancer Cell (1535-6108) 2007 Only protein-protein interactions 5 imex curation aml1_mtg8_human_protein AML1-MTG8 (AML1-ETO) fusion protein protein protein human Homo sapiens Human MRIPVDASTSRRFTPPSTALSPGKMSEALPLGAPDAGAALAGKLRSGDRSMVEVLADHPGELVRTDSPNFLCSVLPTHWRCNKTLPIAFKVVALGDVPDGTLVTVMAGNDENYSAELRNATAAMKNQVARFNDLRFVGRSGRGKSFTLTITVFTNPPQVATYHRAIKITVDGPREPRNRTEKHSTMPDSPVDVKTQSRLTPPTMPPPPTTQGAPRTSSFTPTTLTNGTSHSPTALNGAPSPPNGFSNGPSSSSSSSLANQQLPPACGARQLSKLKRFLTTLQQFGNDISPEIGERVRTLVLGLVNSTLTIEEFHSKLQEATNFPLRPFVIPFLKANLPLLQRELLHCARLAKQNPAQYLAQHEQLLLDASTTSPVDSSELLLDVNENGKRRTPDRTKENGFDREPLHSEHPSKRPCTISPGQRYSPNNGLSYQPNGLPHPTPPPPQHYRLDDMAIAHHYRDSYRHPSHRDLRDRNRPMGLHGTRQEEMIDHRLTDREWAEEWKHLDHLLNCIMDMVEKTRRSLTVLRRCQEADREELNYWIRRYSDAEDLKKGGGSSSSHSRQQSPVNPDPVALDAHREFLHRPASGYVPEEIWKKAEEAVNEVKRQAMTELQKAVSEAERKAHDMITTERAKMERTVAEAKRQAAEDALAVINQQEDSSESCWNCGRKASETCSGCNTARYCGSFCQHKDWEKHHHICGQTLQAQQQGDTPAVSSSVTPNSGAGSPMDTPPAATPRSTTPGTPSTIETTPR An amino acid sequence which is not represented in UniProt The t(8;21) translocation juxtaposes the AMLI gene with the MTG8 on chromosome 8, resulting in the synthesis of an AMLI-MTG8 fusion transcript, which contributes to myeloid leukemogenesis. C4C5CA30972B046E ncor2_human Nuclear receptor corepressor 2 NCOR2 CTG26 Silencing mediator of retinoic acid and thyroid hormone receptor Thyroid-, retinoic-acid-receptor-associated corepressor T3 receptor-associating factor CTG repeat protein 26 SMAP270 protein protein human Homo sapiens Human MSGSTQPVAQTWRATEPRYPPHSLSYPVQIARTHTDVGLLEYQHHSRDYASHLSPGSIIQPQRRRPSLLSEFQPGNERSQELHLRPESHSYLPELGKSEMEFIESKRPRLELLPDPLLRPSPLLATGQPAGSEDLTKDRSLTGKLEPVSPPSPPHTDPELELVPPRLSKEELIQNMDRVDREITMVEQQISKLKKKQQQLEEEAAKPPEPEKPVSPPPIESKHRSLVQIIYDENRKKAEAAHRILEGLGPQVELPLYNQPSDTRQYHENIKINQAMRKKLILYFKRRNHARKQWEQKFCQRYDQLMEAWEKKVERIENNPRRRAKESKVREYYEKQFPEIRKQRELQERMQSRVGQRGSGLSMSAARSEHEVSEIIDGLSEQENLEKQMRQLAVIPPMLYDADQQRIKFINMNGLMADPMKVYKDRQVMNMWSEQEKETFREKFMQHPKNFGLIASFLERKTVAECVLYYYLTKKNENYKSLVRRSYRRRGKSQQQQQQQQQQQQQQQQQPMPRSSQEEKDEKEKEKEAEKEEEKPEVENDKEDLLKEKTDDTSGEDNDEKEAVASKGRKTANSQGRRKGRITRSMANEANSEEAITPQQSAELASMELNESSRWTEEEMETAKKGLLEHGRNWSAIARMVGSKTVSQCKNFYFNYKKRQNLDEILQQHKLKMEKERNARRKKKKAPAAASEEAAFPPVVEDEEMEASGVSGNEEEMVEEAEALHASGNEVPRGECSGPATVNNSSDTESIPSPHTEAAKDTGQNGPKPPATLGADGPPPGPPTPPPEDIPAPTEPTPASEATGAPTPPPAPPSPSAPPPVVPKEEKEEETAAAPPVEEGEEQKPPAAEELAVDTGKAEEPVKSECTEEAEEGPAKGKDAEAAEATAEGALKAEKKEGGSGRATTAKSSGAPQDSDSSATCSADEVDEAEGGDKNRLLSPRPSLLTPTGDPRANASPQKPLDLKQLKQRAAAIPPIQVTKVHEPPREDAAPTKPAPPAPPPPQNLQPESDAPQQPGSSPRGKSRSPAPPADKEAFAAEAQKLPGDPPCWTSGLPFPVPPREVIKASPHAPDPSAFSYAPPGHPLPLGLHDTARPVLPRPPTISNPPPLISSAKHPSVLERQIGAISQGMSVQLHVPYSEHAKAPVGPVTMGLPLPMDPKKLAPFSGVKQEQLSPRGQAGPPESLGVPTAQEASVLRGTALGSVPGGSITKGIPSTRVPSDSAITYRGSITHGTPADVLYKGTITRIIGEDSPSRLDRGREDSLPKGHVIYEGKKGHVLSYEGGMSVTQCSKEDGRSSSGPPHETAAPKRTYDMMEGRVGRAISSASIEGLMGRAIPPERHSPHHLKEQHHIRGSITQGIPRSYVEAQEDYLRREAKLLKREGTPPPPPPSRDLTEAYKTQALGPLKLKPAHEGLVATVKEAGRSIHEIPREELRHTPELPLAPRPLKEGSITQGTPLKYDTGASTTGSKKHDVRSLIGSPGRTFPPVHPLDVMADARALERACYEESLKSRPGTASSSGGSIARGAPVIVPELGKPRQSPLTYEDHGAPFAGHLPRGSPVTTREPTPRLQEGSLSSSKASQDRKLTSTPREIAKSPHSTVPEHHPHPISPYEHLLRGVSGVDLYRSHIPLAFDPTSIPRGIPLDAAAAYYLPRHLAPNPTYPHLYPPYLIRGYPDTAALENRQTIINDYITSQQMHHNAATAMAQRADMLRGLSPRESSLALNYAAGPRGIIDLSQVPHLPVLVPPTPGTPATAMDRLAYLPTAPQPFSSRHSSSPLSPGGPTHLTKPTTTSSSERERDRDRERDRDREREKSILTSTTTVEHAPIWRPGTEQSSGSSGGGGGSSSRPASHSHAHQHSPISPRTQDALQQRPSVLHNTGMKGIITAVEPSTPTVLRSTSTSSPVRPAATFPPATHCPLGGTLDGVYPTLMEPVLLPKEAPRVARPERPRADTGHAFLAKPPARSGLEPASSPSKGSEPRPLVPPVSGHATIARTPAKNLAPHHASPDPPAPPASASDPHREKTQSKPFSIQELELRSLGYHGSSYSPEGVEPVSPVSSPSLTHDKGLPKHLEELDKSHLEGELRPKQPGPVKLGGEAAHLPHLRPLPESQPSSSPLLQTAPGVKGHQRVVTLAQHISEVITQDYTRHHPQQLSAPLPAPLYSFPGASCPVLDLRRPPSDLYLPPPDHGAPARGSPHSEGGKRSPEPNKTSVLGGGEDGIEPVSPPEGMTEPGHSRSAVYPLLYRDGEQTEPSRMGSKSPGNTSQPPAFFSKLTESNSAMVKSKKQEINKKLNTHNRNEPEYNISQPGTEIFNMPAITGTGLMTYRSQAVQEHASTNMGLEAIIRKALMGKYDQWEESPPLSANAFNPLNASASLPAAMPITAADGRSDHTLTSPGGGGKAKVSGRPSSRKAKSPAPGLASGDRPPSVSSVHSEGDCNRRTPLTNRVWEDRPSSAGSTPFPYNPLIMRLQAGVMASPPPPGLPAGSGPLAGPHHAWDEEPKPLLCSQYETLSDSE DIP protein Q9Y618 original sequence version: 166 DIP protein Q9Y618-1 original sequence version: 119 DIP protein Q9Y618-1 original sequence version: 155 DIP protein Q9Y618 original sequence version: 134 DIP protein Q9Y618 original sequence version: 138 70A89C9A19612AAD ncor1_human Nuclear receptor corepressor 1 NCOR1 KIAA1047 protein protein human Homo sapiens Human MSSSGYPPNQGAFSTEQSRYPPHSVQYTFPNTRHQQEFAVPDYRSSHLEVSQASQLLQQQQQQQLRRRPSLLSEFHPGSDRPQERRTSYEPFHPGPSPVDHDSLESKRPRLEQVSDSHFQRVSAAVLPLVHPLPEGLRASADAKKDPAFGGKHEAPSSPISGQPCGDDQNASPSKLSKEELIQSMDRVDREIAKVEQQILKLKKKQQQLEEEAAKPPEPEKPVSPPPVEQKHRSIVQIIYDENRKKAEEAHKIFEGLGPKVELPLYNQPSDTKVYHENIKTNQVMRKKLILFFKRRNHARKQREQKICQRYDQLMEAWEKKVDRIENNPRRKAKESKTREYYEKQFPEIRKQREQQERFQRVGQRGAGLSATIARSEHEISEIIDGLSEQENNEKQMRQLSVIPPMMFDAEQRRVKFINMNGLMEDPMKVYKDRQFMNVWTDHEKEIFKDKFIQHPKNFGLIASYLERKSVPDCVLYYYLTKKNENYKALVRRNYGKRRGRNQQIARPSQEEKVEEKEEDKAEKTEKKEEEKKDEEEKDEKEDSKENTKEKDKIDGTAEETEEREQATPRGRKTANSQGRRKGRITRSMTNEAAAASAAAAAATEEPPPPLPPPPEPISTEPVETSRWTEEEMEVAKKGLVEHGRNWAAIAKMVGTKSEAQCKNFYFNYKRRHNLDNLLQQHKQKTSRKPREERDVSQCESVASTVSAQEDEDIEASNEEENPEDSEVEAVKPSEDSPENATSRGNTEPAVELEPTTETAPSTSPSLAVPSTKPAEDESVETQVNDSISAETAEQMDVDQQEHSAEEGSVCDPPPATKADSVDVEVRVPENHASKVEGDNTKERDLDRASEKVEPRDEDLVVAQQINAQRPEPQSDNDSSATCSADEDVDGEPERQRMFPMDSKPSLLNPTGSILVSSPLKPNPLDLPQLQHRAAVIPPMVSCTPCNIPIGTPVSGYALYQRHIKAMHESALLEEQRQRQEQIDLECRSSTSPCGTSKSPNREWEVLQPAPHQVITNLPEGVRLPTTRPTRPPPPLIPSSKTTVASEKPSFIMGGSISQGTPGTYLTSHNQASYTQETPKPSVGSISLGLPRQQESAKSATLPYIKQEEFSPRSQNSQPEGLLVRAQHEGVVRGTAGAIQEGSITRGTPTSKISVESIPSLRGSITQGTPALPQTGIPTEALVKGSISRMPIEDSSPEKGREEAASKGHVIYEGKSGHILSYDNIKNAREGTRSPRTAHEISLKRSYESVEGNIKQGMSMRESPVSAPLEGLICRALPRGSPHSDLKERTVLSGSIMQGTPRATTESFEDGLKYPKQIKRESPPIRAFEGAITKGKPYDGITTIKEMGRSIHEIPRQDILTQESRKTPEVVQSTRPIIEGSISQGTPIKFDNNSGQSAIKHNVKSLITGPSKLSRGMPPLEIVPENIKVVERGKYEDVKAGETVRSRHTSVVSSGPSVLRSTLHEAPKAQLSPGIYDDTSARRTPVSYQNTMSRGSPMMNRTSDVTISSNKSTNHERKSTLTPTQRESIPAKSPVPGVDPVVSHSPFDPHHRGSTAGEVYRSHLPTHLDPAMPFHRALDPAAAAYLFQRQLSPTPGYPSQYQLYAMENTRQTILNDYITSQQMQVNLRPDVARGLSPREQPLGLPYPATRGIIDLTNMPPTILVPHPGGTSTPPMDRITYIPGTQITFPPRPYNSASMSPGHPTHLAAAASAEREREREREKERERERIAAASSDLYLRPGSEQPGRPGSHGYVRSPSPSVRTQETMLQQRPSVFQGTNGTSVITPLDPTAQLRIMPLPAGGPSISQGLPASRYNTAADALAALVDAAASAPQMDVSKTKESKHEAARLEENLRSRSAAVSEQQQLEQKTLEVEKRSVQCLYTSSAFPSGKPQPHSSVVYSEAGKDKGPPPKSRYEEELRTRGKTTITAANFIDVIITRQIASDKDARERGSQSSDSSSSLSSHRYETPSDAIEVISPASSPAPPQEKLQTYQPEVVKANQAENDPTRQYEGPLHHYRPQQESPSPQQQLPPSSQAEGMGQVPRTHRLITLADHICQIITQDFARNQVSSQTPQQPPTSTFQNSPSALVSTPVRTKTSNRYSPESQAQSVHHQRPGSRVSPENLVDKSRGSRPGKSPERSHVSSEPYEPISPPQVPVVHEKQDSLLLLSQRGAEPAEQRNDARSPGSISYLPSFFTKLENTSPMVKSKKQEIFRKLNSSGGGDSDMAAAQPGTEIFNLPAVTTSGSVSSRGHSFADPASNLGLEDIIRKALMGSFDDKVEDHGVVMSQPMGVVPGTANTSVVTSGETRREEGDPSPHSGGVCKPKLISKSNSRKSKSPIPGQGYLGTERPSSVSSVHSEGDYHRQTPGWAWEDRPSSTGSTQFPYNPLTMRMLSSTPPTPIACAPSAVNQAAPHQQNRIWEREPAPLLSAQYETLSDSDD DIP protein O75376 original sequence version: 186 DIP protein O75376 original sequence version: 75 DIP protein O75376 original sequence version: 153 DIP protein O75376 original sequence version: 147 DIP protein O75376 original sequence version: 112 DIP protein O75376-1 original sequence version: 111 DIP protein O75376 original sequence version: 146 1647FE060373A125 aml1_mtg8-ncor2-2 1 5 unspecified role unspecified role neutral component neutral component region MYND domain sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecobb Escherichia coli (strain B / BL21) 6 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecobb Escherichia coli (strain B / BL21) direct interaction direct interaction 1 A We confirmed that an aa 1031-1273 SMRT polypeptide bound the MYND domain by HSQC titration aml1_mtg8-ncor2 2 5 unspecified role unspecified role neutral component neutral component region MYND domain sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain gln688ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain Q A trp692ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain W A his695ala mutation disrupting mutation disrupting interaction mutation disrupting alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain H A ser675ala mutation decreasing mutation decreasing interaction hotspot hotspot mutation decreasing alanine scanning alanine scanning certain certain sequence position certain certain certain sequence position certain S A ecobb Escherichia coli (strain B / BL21) 6 unspecified role unspecified role neutral component neutral component region NPPPLI required to bind necessary binding region required to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain region fluorescein-labeled fitc labelled fluorescein isothiocyanate label fluorescein isothiocyanate labbeled FITC labelled FITC labelled fluorescein isothiocyanate labbeled fitc labelled undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecobb Escherichia coli (strain B / BL21) direct interaction direct interaction 1 D, 3 A We identified three consecutive peptides that displayed significantly elevated anisotropy in the presence of the MYND domain (Figure 1D) and share the common sequence motif NPPPLI, corresponding to SMRT residues 1104�1109. H695A prevents SMRT peptide binding. W692A increased Kd more than 12-fold. Q688A and S675A impaired SMRT peptide binding 12-fold and 2.5-fold, respectively. aml1_mtg8-ncor2-1 3 5 unspecified role unspecified role neutral component neutral component region MYND domain sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecobb Escherichia coli (strain B / BL21) 6 unspecified role unspecified role neutral component neutral component region required to bind necessary binding region required to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain n-terminal YG tag tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecobb Escherichia coli (strain B / BL21) direct interaction direct interaction 1 E As N = 0.931, the stoichiometry is entered as 1 for each interactor. The NCOR2 peptide was tagged with YG at the N-terminus. Isothermal titration calorimetry (ITC) was employed to determine the stoichiometry and binding affinity between the MYND domain and the SMRT and N-CoR peptides aml1_mtg8-ncor1 3 7 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain n-terminal YG tag tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range ecobb Escherichia coli (strain B / BL21) 5 unspecified role unspecified role neutral component neutral component region MYND domain sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecobb Escherichia coli (strain B / BL21) direct interaction direct interaction 1 E Isothermal titration calorimetry (ITC) was employed to determine the stoichiometry and binding affinity between the MYND domain and the SMRT and N-CoR peptides The authors state that the NCOR1 sequence corresponds to aa 1000-1011 but the sequence corresponds to aa 1030-1041 of O75376. As N = 1.001, the stoichiometry is entered as 1 for each interactor. The NCOR1 peptide was tagged with YG at the N-terminus. aml1_mtg-aml1_mtg 4 5 unspecified role unspecified role neutral component neutral component region MYND domain sufficient to bind sufficient binding region sufficient to bind deletion analysis deletion analysis certain certain sequence position certain certain certain sequence position certain ecobb Escherichia coli (strain B / BL21) direct interaction direct interaction S4 A Analytical ultracentrifugation analysis of the isolated MYND domain showed a mixture of monomer and additional species of higher order oligomerization