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- EMDB-28575: Structure of the Yeast NuA4 Histone Acetyltransferase Complex -

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Basic information

Entry
Database: EMDB / ID: EMD-28575
TitleStructure of the Yeast NuA4 Histone Acetyltransferase Complex
Map data
Sample
  • Complex: NuA4
    • Protein or peptide: Transcription-associated protein 1
    • Protein or peptide: Actin-related protein 4
    • Protein or peptide: Actin
    • Protein or peptide: Enhancer of polycomb-like protein 1
    • Protein or peptide: Chromatin modification-related protein EAF1
    • Protein or peptide: SWR1-complex protein 4
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
  • Ligand: MAGNESIUM ION
Function / homology
Function and homology information


mitotic actomyosin contractile ring contraction / RHOA GTPase cycle / cellular bud neck contractile ring / piccolo histone acetyltransferase complex / RHO GTPases activate IQGAPs / RHO GTPases Activate WASPs and WAVEs / Regulation of actin dynamics for phagocytic cup formation / ascospore wall assembly / vacuole inheritance / actin cortical patch ...mitotic actomyosin contractile ring contraction / RHOA GTPase cycle / cellular bud neck contractile ring / piccolo histone acetyltransferase complex / RHO GTPases activate IQGAPs / RHO GTPases Activate WASPs and WAVEs / Regulation of actin dynamics for phagocytic cup formation / ascospore wall assembly / vacuole inheritance / actin cortical patch / Swr1 complex / Platelet degranulation / : / SLIK (SAGA-like) complex / Ino80 complex / kinetochore assembly / SWI/SNF complex / SAGA complex / NuA4 histone acetyltransferase complex / establishment of cell polarity / actin filament bundle / positive regulation of macroautophagy / protein secretion / chromosome organization / actin filament / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / structural constituent of cytoskeleton / endocytosis / transcription corepressor activity / nucleosome / chromatin organization / histone binding / protein-containing complex assembly / hydrolase activity / chromatin remodeling / cell cycle / DNA repair / DNA-templated transcription / chromatin binding / chromatin / regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / ATP binding / identical protein binding / nucleus
Similarity search - Function
SWR1-complex protein 4/DNA methyltransferase 1-associated protein 1 / DAMP1, SANT/Myb-like domain / SANT/Myb-like domain of DAMP1 / Enhancer of polycomb protein / Tra1, HEAT repeat ring region / Tra1, HEAT repeat central region / Tra1 HEAT repeat central region / Tra1 HEAT repeat ring region / Myb-like domain profile. / domain in helicases and associated with SANT domains ...SWR1-complex protein 4/DNA methyltransferase 1-associated protein 1 / DAMP1, SANT/Myb-like domain / SANT/Myb-like domain of DAMP1 / Enhancer of polycomb protein / Tra1, HEAT repeat ring region / Tra1, HEAT repeat central region / Tra1 HEAT repeat central region / Tra1 HEAT repeat ring region / Myb-like domain profile. / domain in helicases and associated with SANT domains / Myb-like DNA-binding domain / HSA domain / Helicase/SANT-associated domain / HSA domain profile. / PIK-related kinase, FAT / FAT domain / FATC domain / PIK-related kinase / FAT domain profile. / FATC domain profile. / Enhancer of polycomb-like, N-terminal / Enhancer of polycomb-like / SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains / SANT/Myb domain / Phosphatidylinositol 3-/4-kinase, catalytic domain superfamily / Phosphoinositide 3-kinase, catalytic domain / Phosphatidylinositol 3- and 4-kinase / Phosphatidylinositol 3- and 4-kinases catalytic domain profile. / Phosphatidylinositol 3-/4-kinase, catalytic domain / Actins signature 1. / Actin, conserved site / Actins signature 2. / Actin/actin-like conserved site / Actins and actin-related proteins signature. / Actin / Actin family / Actin / Homeobox-like domain superfamily / ATPase, nucleotide binding domain / Armadillo-type fold / Protein kinase-like domain superfamily
Similarity search - Domain/homology
Transcription-associated protein 1 / Enhancer of polycomb-like protein 1 / SWR1-complex protein 4 / Actin / Actin-related protein 4 / Chromatin modification-related protein EAF1
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.1 Å
AuthorsPatel AB / Zukin SA / Nogales E
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R35-GM127018 United States
CitationJournal: Elife / Year: 2022
Title: Structure and flexibility of the yeast NuA4 histone acetyltransferase complex.
Authors: Stefan A Zukin / Matthew R Marunde / Irina K Popova / Katarzyna M Soczek / Eva Nogales / Avinash B Patel /
Abstract: The NuA4 protein complex acetylates histones H4 and H2A to activate both transcription and DNA repair. We report the 3.1-Å resolution cryo-electron microscopy structure of the central hub of NuA4, ...The NuA4 protein complex acetylates histones H4 and H2A to activate both transcription and DNA repair. We report the 3.1-Å resolution cryo-electron microscopy structure of the central hub of NuA4, which flexibly tethers the histone acetyltransferase (HAT) and Trimer Independent of NuA4 involved in Transcription Interactions with Nucleosomes (TINTIN) modules. The hub contains the large Tra1 subunit and a core that includes Swc4, Arp4, Act1, Eaf1, and the C-terminal region of Epl1. Eaf1 stands out as the primary scaffolding factor that interacts with the Tra1, Swc4, and Epl1 subunits and contributes the conserved HSA helix to the Arp module. Using nucleosome-binding assays, we find that the HAT module, which is anchored to the core through Epl1, recognizes H3K4me3 nucleosomes with hyperacetylated H3 tails, while the TINTIN module, anchored to the core via Eaf1, recognizes nucleosomes that have hyperacetylated H2A and H4 tails. Together with the known interaction of Tra1 with site-specific transcription factors, our data suggest a model in which Tra1 recruits NuA4 to specific genomic sites then allowing the flexible HAT and TINTIN modules to select nearby nucleosomes for acetylation.
History
DepositionOct 13, 2022-
Header (metadata) releaseNov 16, 2022-
Map releaseNov 16, 2022-
UpdateNov 16, 2022-
Current statusNov 16, 2022Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_28575.png

Downloads & links

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Map

FileDownload / File: emd_28575.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 1.3404 Å
Density
Contour LevelBy AUTHOR: 0.02
Minimum - Maximum-0.12369774 - 0.27815
Average (Standard dev.)0.00027007714 (±0.004088094)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions320320320
Spacing320320320
CellA=B=C: 428.92798 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_28575_msk_1.map
Projections & Slices
AxesZYX

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Half map: #2

Fileemd_28575_half_map_1.map
Projections & Slices
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Half map: #1

Fileemd_28575_half_map_2.map
Projections & Slices
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Sample components

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Entire : NuA4

EntireName: NuA4
Components
  • Complex: NuA4
    • Protein or peptide: Transcription-associated protein 1
    • Protein or peptide: Actin-related protein 4
    • Protein or peptide: Actin
    • Protein or peptide: Enhancer of polycomb-like protein 1
    • Protein or peptide: Chromatin modification-related protein EAF1
    • Protein or peptide: SWR1-complex protein 4
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
  • Ligand: MAGNESIUM ION

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Supramolecule #1: NuA4

SupramoleculeName: NuA4 / type: complex / Chimera: Yes / ID: 1 / Parent: 0 / Macromolecule list: #1-#6
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 1.3 MDa

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Macromolecule #1: Transcription-associated protein 1

MacromoleculeName: Transcription-associated protein 1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 433.677281 KDa
SequenceString: MSLTEQIEQF ASRFRDDDAT LQSRYSTLSE LYDIMELLNS PEDYHFFLQA VIPLLLNQLK EVPISYDAHS PEQKLRNSML DIFNRCLMN QTFQPYAMEV LEFLLSVLPK ENEENGILCM KVLTTLFKSF KSILQDKLDS FIRIIIQIYK NTPNLINQTF Y EAGKAEQG ...String:
MSLTEQIEQF ASRFRDDDAT LQSRYSTLSE LYDIMELLNS PEDYHFFLQA VIPLLLNQLK EVPISYDAHS PEQKLRNSML DIFNRCLMN QTFQPYAMEV LEFLLSVLPK ENEENGILCM KVLTTLFKSF KSILQDKLDS FIRIIIQIYK NTPNLINQTF Y EAGKAEQG DLDSPKEPQA DELLDEFSKN DEEKDFPSKQ SSTEPRFENS TSSNGLRSSM FSFKILSECP ITMVTLYSSY KQ LTSTSLP EFTPLIMNLL NIQIKQQQEA REQAESRGEH FTSISTEIIN RPAYCDFILA QIKATSFLAY VFIRGYAPEF LQD YVNFVP DLIIRLLQDC PSELSSARKE LLHATRHILS TNYKKLFLPK LDYLFDERIL IGNGFTMHET LRPLAYSTVA DFIH NIRSE LQLSEIEKTI KIYTGYLLDE SLALTVQIMS AKLLLNLVER ILKLGKENPQ EAPRAKKLLM IIIDSYMNRF KTLNR QYDT IMKYYGRYET HKKEKAEKLK NSIQDNDKES EEFMRKVLEP SDDDHLMPQP KKEDINDSPD VEMTESDKVV KNDVEM FDI KNYAPILLLP TPTNDPIKDA FYLYRTLMSF LKTIIHDLKV FNPPPNEYTV ANPKLWASVS RVFSYEEVIV FKDLFHE CI IGLKFFKDHN EKLSPETTKK HFDISMPSLP VSATKDAREL MDYLAFMFMQ MDNATFNEII EQELPFVYER MLEDSGLL H VAQSFLTSEI TSPNFAGILL RFLKGKLKDL GNVDFNTSNV LIRLFKLSFM SVNLFPNINE VVLLPHLNDL ILNSLKYST TAEEPLVYFY LIRTLFRSIG GGRFENLYRS IKPILQVLLQ SLNQMILTAR LPHERELYVE LCITVPVRLS VLAPYLPFLM KPLVFALQQ YPDLVSQGLR TLELCIDNLT AEYFDPIIEP VIDDVSKALF NLLQPQPFNH AISHNVVRIL GKLGGRNRQF L KPPTDLTE KTELDIDAIA DFKINGMPED VPLSVTPGIQ SALNILQSYK SDIHYRKSAY KYLTCVLLLM TKSSAEFPTN YT ELLKTAV NSIKLERIGI EKNFDLEPTV NKRDYSNQEN LFLRLLESVF YATSIKELKD DAMDLLNNLL DHFCLLQVNT TLL NKRNYN GTFNIDLKNP NFMLDSSLIL DAIPFALSYY IPEVREVGVL AYKRIYEKSC LIYGEELALS HSFIPELAKQ FIHL CYDET YYNKRGGVLG IKVLIDNVKS SSVFLKKYQY NLANGLLFVL KDTQSEAPSA ITDSAEKLLI DLLSITFADV KEEDL GNKV LENTLTDIVC ELSNANPKVR NACQKSLHTI SNLTGIPIVK LMDHSKQFLL SPIFAKPLRA LPFTMQIGNV DAITFC LSL PNTFLTFNEE LFRLLQESIV LADAEDESLS TNIQKTTEYS TSEQLVQLRI ACIKLLAIAL KNEEFATAQQ GNIRIRI LA VFFKTMLKTS PEIINTTYEA LKGSLAENSK LPKELLQNGL KPLLMNLSDH QKLTVPGLDA LSKLLELLIA YFKVEIGR K LLDHLTAWCR VEVLDTLFGQ DLAEQMPTKI IVSIINIFHL LPPQADMFLN DLLLKVMLLE RKLRLQLDSP FRTPLARYL NRFHNPVTEY FKKNMTLRQL VLFMCNIVQR PEAKELAEDF EKELDNFYDF YISNIPKNQV RVVSFFTNMV DLFNTMVITN GDEWLKKKG NMILKLKDML NLTLKTIKEN SFYIDHLQLN QSIAKFQALY LRFTELSERD QNPLLLDFID FSFSNGIKAS Y SLKKFIFH NIIASSNKEK QNNFINDATL FVLSDKCLDA RIFVLKNVIN STLIYEVATS GSLKSYLVED KKPKWLELLH NK IWKNSNA ILAYDVLDHH DLFRFELLQL SAIFIKADPE IIAEIKKDII KFCWNFIKLE DTLIKQSAYL VTSYFISKFD FPI KVVTQV FVALLRSSHV EARYLVKQSL DVLTPVLHER MNAAGTPDTW INWVKRVMVE NSSSQNNILY QFLISHPDLF FNSR DLFIS NIIHHMNKIT FMSNSNSDSH TLAIDLASLI LYWENKTLEI TNVNNTKTDS DGDVVMSDSK SDINPVEADT TAIIV DANN NSPISLHLRE ACTAFLIRYV CASNHRAIET ELGLRAINIL SELISDKHWT NVNVKLVYFE KFLIFQDLDS ENILYY CMN ALDVLYVFFK NKTKEWIMEN LPTIQNLLEK CIKSDHHDVQ EALQKVLQVI MKAIKAQGVS VIIEEESPGK TFIQMLT SV ITQDLQETSS VTAGVTLAWV LFMNFPDNIV PLLTPLMKTF SKLCKDHLSI SQPKDAMALE EARITTKLLE KVLYILSL K VSLLGDSRRP FLSTVALLID HSMDQNFLRK IVNMSRSWIF NTEIFPTVKE KAAILTKMLA FEIRGEPSLS KLFYEIVLK LFDQEHFNNT EITVRMEQPF LVGTRVEDIG IRKRFMTILD NSLERDIKER LYYVIRDQNW EFIADYPWLN QALQLLYGSF NREKELSLK NIYCLSPPSI LQEYLPENAE MVTEVNDLEL SNFVKGHIAS MQGLCRIISS DFIDSLIEIF YQDPKAIHRA W VTLFPQVY KSIPKNEKYG FVRSIITLLS KPYHTRQISS RTNVINMLLD SISKIESLEL PPHLVKYLAI SYNAWYQSIN IL ESIQSNT SIDNTKIIEA NEDALLELYV NLQEEDMFYG LWRRRAKYTE TNIGLSYEQI GLWDKAQQLY EVAQVKARSG ALP YSQSEY ALWEDNWIQC AEKLQHWDVL TELAKHEGFT DLLLECGWRV ADWNSDRDAL EQSVKSVMDV PTPRRQMFKT FLAL QNFAE SRKGDQEVRK LCDEGIQLSL IKWVSLPIRY TPAHKWLLHG FQQYMEFLEA TQIYANLHTT TVQNLDSKAQ EIKRI LQAW RDRLPNTWDD VNMWNDLVTW RQHAFQVINN AYLPLIPALQ QSNSNSNINT HAYRGYHEIA WVINRFAHVA RKHNMP DVC ISQLARIYTL PNIEIQEAFL KLREQAKCHY QNMNELTTGL DVISNTNLVY FGTVQKAEFF TLKGMFLSKL RAYEEAN QA FATAVQIDLN LAKAWAQWGF FNDRRLSEEP NNISFASNAI SCYLQAAGLY KNSKIRELLC RILWLISIDD ASGMLTNA F DSFRGEIPVW YWITFIPQLL TSLSHKEANM VRHILIRIAK SYPQALHFQL RTTKEDFAVI QRQTMAVMGD KPDTNDRNG RRQPWEYLQE LNNILKTAYP LLALSLESLV AQINDRFKST TDEDLFRLIN VLLIDGTLNY NRLPFPRKNP KLPENTEKNL VKFSTTLLA PYIRPKFNAD FIDNKPDYET YIKRLRYWRR RLENKLDRAS KKENLEVLCP HLSNFHHQKF EDIEIPGQYL L NKDNNVHF IKIARFLPTV DFVRGTHSSY RRLMIRGHDG SVHSFAVQYP AVRHSRREER MFQLYRLFNK SLSKNVETRR RS IQFNLPI AIPLSPQVRI MNDSVSFTTL HEIHNEFCKK KGFDPDDIQD FMADKLNAAH DDALPAPDMT ILKVEIFNSI QTM FVPSNV LKDHFTSLFT QFEDFWLFRK QFASQYSSFV FMSYMMMINN RTPHKIHVDK TSGNVFTLEM LPSRFPYERV KPLL KNHDL SLPPDSPIFH NNEPVPFRLT PNIQSLIGDS ALEGIFAVNL FTISRALIEP DNELNTYLAL FIRDEIISWF SNLHR PIIE NPQLREMVQT NVDLIIRKVA QLGHLNSTPT VTTQFILDCI GSAVSPRNLA RTDVNFMPWF

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Macromolecule #2: Actin-related protein 4

MacromoleculeName: Actin-related protein 4 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 54.894684 KDa
SequenceString: MSNAALQVYG GDEVSAVVID PGSYTTNIGY SGSDFPQSIL PSVYGKYTAD EGNKKIFSEQ SIGIPRKDYE LKPIIENGLV IDWDTAQEQ WQWALQNELY LNSNSGIPAL LTEPVWNSTE NRKKSLEVLL EGMQFEACYL APTSTCVSFA AGRPNCLVVD I GHDTCSVS ...String:
MSNAALQVYG GDEVSAVVID PGSYTTNIGY SGSDFPQSIL PSVYGKYTAD EGNKKIFSEQ SIGIPRKDYE LKPIIENGLV IDWDTAQEQ WQWALQNELY LNSNSGIPAL LTEPVWNSTE NRKKSLEVLL EGMQFEACYL APTSTCVSFA AGRPNCLVVD I GHDTCSVS PIVDGMTLSK STRRNFIAGK FINHLIKKAL EPKEIIPLFA IKQRKPEFIK KTFDYEVDKS LYDYANNRGF FQ ECKETLC HICPTKTLEE TKTELSSTAK RSIESPWNEE IVFDNETRYG FAEELFLPKE DDIPANWPRS NSGVVKTWRN DYV PLKRTK PSGVNKSDKK VTPTEEKEQE AVSKSTSPAA NSADTPNETG KRPLEEEKPP KENNELIGLA DLVYSSIMSS DVDL RATLA HNVVLTGGTS SIPGLSDRLM TELNKILPSL KFRILTTGHT IERQYQSWLG GSILTSLGTF HQLWVGKKEY EEVGV ERLL NDRFR

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Macromolecule #3: Actin

MacromoleculeName: Actin / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
EC number: Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 41.735547 KDa
SequenceString: MDSEVAALVI DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGIMVGMGQK DSYVGDEAQS KRGILTLRYP IEHGIVTNWD DMEKIWHHT FYNELRVAPE EHPVLLTEAP MNPKSNREKM TQIMFETFNV PAFYVSIQAV LSLYSSGRTT GIVLDSGDGV T HVVPIYAG ...String:
MDSEVAALVI DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGIMVGMGQK DSYVGDEAQS KRGILTLRYP IEHGIVTNWD DMEKIWHHT FYNELRVAPE EHPVLLTEAP MNPKSNREKM TQIMFETFNV PAFYVSIQAV LSLYSSGRTT GIVLDSGDGV T HVVPIYAG FSLPHAILRI DLAGRDLTDY LMKILSERGY SFSTTAEREI VRDIKEKLCY VALDFEQEMQ TAAQSSSIEK SY ELPDGQV ITIGNERFRA PEALFHPSVL GLESAGIDQT TYNSIMKCDV DVRKELYGNI VMSGGTTMFP GIAERMQKEI TAL APSSMK VKIIAPPERK YSVWIGGSIL ASLTTFQQMW ISKQEYDESG PSIVHHKCF

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Macromolecule #4: Enhancer of polycomb-like protein 1

MacromoleculeName: Enhancer of polycomb-like protein 1 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 96.889867 KDa
SequenceString: MPTPSNAIEI NDGSHKSGRS TRRSGSRSAH DDGLDSFSKG DSGAGASAGS SNSRFRHRKI SVKQHLKIYL PNDLKHLDKD ELQQREVVE IETGVEKNEE KEVHLHRILQ MGSGHTKHKD YIPTPDASMT WNEYDKFYTG SFQETTSYIK FSATVEDCCG T NYNMDERD ...String:
MPTPSNAIEI NDGSHKSGRS TRRSGSRSAH DDGLDSFSKG DSGAGASAGS SNSRFRHRKI SVKQHLKIYL PNDLKHLDKD ELQQREVVE IETGVEKNEE KEVHLHRILQ MGSGHTKHKD YIPTPDASMT WNEYDKFYTG SFQETTSYIK FSATVEDCCG T NYNMDERD ETFLNEQVNK GSSDILTEDE FEILCSSFEH AIHERQPFLS MDPESILSFE ELKPTLIKSD MADFNLRNQL NH EINSHKT HFITQFDPVS QMNTRPLIQL IEKFGSKIYD YWRERKIEVN GYEIFPQLKF ERPGEKEEID PYVCFRRREV RHP RKTRRI DILNSQRLRA LHQELKNAKD LALLVAKREN VSLNWINDEL KIFDQRVKIK NLKRSLNISG EDDDLINHKR KRPT IVTVE QREAELRKAE LKRAAAAAAA AKAKNNKRNN QLEDKSSRLT KQQQQQLLQQ QQQQQQNALK TENGKQLANA SSSST SQPI TSHVYVKLPS SKIPDIVLED VDALLNSKEK NARKFVQEKM EKRKIEDADV FFNLTDDPFN PVFDMSLPKN FSTSNV PFA SIASSKFQID RSFYSSHLPE YLKGISDDIR IYDSNGRSRN KDNYNLDTKR IKKTELYDPF QENLEIHSRE YPIKFRK RV GRSNIKYVDR MPNFTTSSTK SACSLMDFVD FDSIEKEQYS REGSNDTDSI NVYDSKYDEF VRLYDKWKYD SPQNEYGI K FSDEPARLNQ ISNDTQVIRF GTMLGTKSYE QLREATIKYR RDYITRLKQK HIQHLQQQQQ QQQQQQQQAQ QQKQKSQNN NSNSSNSLKK LNDSLINSEA KQNSSITQKN SS

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Macromolecule #5: Chromatin modification-related protein EAF1

MacromoleculeName: Chromatin modification-related protein EAF1 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 112.667008 KDa
SequenceString: MSSRPSSAVP NSASLSEDQS SDRSKFPKAD DLIDERDRKL TELYCVSRLN QLLELTDENK LRKEIDAFLK KNDIRRGIRF DEASLPKLL HTAATPITKK KLKDVNLINV PNQRLSDSKM SRELPENSEN VSVKSESHFV PSHDNSIREN MMDSLRPAEK T GGMWNKRP ...String:
MSSRPSSAVP NSASLSEDQS SDRSKFPKAD DLIDERDRKL TELYCVSRLN QLLELTDENK LRKEIDAFLK KNDIRRGIRF DEASLPKLL HTAATPITKK KLKDVNLINV PNQRLSDSKM SRELPENSEN VSVKSESHFV PSHDNSIREN MMDSLRPAEK T GGMWNKRP LESTMGGEEE RHEKRQKMQS QSLESSNNSE MASLPISPRP PVPNALAHYT YYENIEYPPA DPTEVQPAVK FK DPLIKNI MAKEIDTSDH YNENNVDALE TVFLLMNDYI PSKIPQALPL AELKYMSQTL PLINLIPRAH KALTTNIINN ALN EARITV VGSRIEELRR LGLWSLRQPK RFIDPWKQHN THQNILLEEA KWMQADFKEG HKYKVAICTA MAQAIKDYWT YGEI CCVKR KTLLPGKENK LSDDGRISEK SGRPSDTSRN DSDISIAGKD DIGIIANVDD ITEKESAAAN DNDENGKNEA GAKSD FDFA DGLLSQEGAH DQIISSIDTK LLLKKPSSSS EVVLIQHEVA ASSALIETEE SKKELAPPFK LSIFVDELNT FEKTLI QDL PLYNGINEER PKKDDSLPFI PISKSVVSLD DNGFYKLLER QLIDEEPSIS QLSKRRGMFY GNRRNHYLRP PAVPSLR YL QNRTPTIWLS EDDQELVKNI NTYGYNWELI SAHMTHRLTY SYLSNIERRT PWQCFERFVQ LNERFNFSDL KGPRAHSA Q QWLIEAHKFQ QRQNRRISPL GVNTESIQRG HRRLRWASMF EAIRKCMKKR ENTPRPNPTQ PRKPLDCKNM KVPTPAEMS LLKAQRDEAL RRDIQLRRTV KNRLQQRQQQ SQQAHSSRAQ SPIPSNGKSS SNLARNGQAS APRPNQKQYT EQDIIESYSR KLLEQKPDI GPEMALKAAK NYYRTLREQQ QQLKQHQIQQ QRQQLQEESS HVQQLQQLQP GSQAPPPKSS PSQSSLSNIS N INSAPRIK SPTPQEILQR FQKQ

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Macromolecule #6: SWR1-complex protein 4

MacromoleculeName: SWR1-complex protein 4 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 55.297684 KDa
SequenceString: MSSSDIFDVL NIKQKSRSPT NGQVSVPSSS AANRPKPQVT GMQRELFNLL GENQPPVVIK SGNNFKEKML STSKPSPWSF VEFKANNSV TLRHWVKGSK ELIGDTPKES PYSKFNQHLS IPSFTKEEYE AFMNENEGTQ KSVESEKNHN ENFTNEKKDE S KNSWSFEE ...String:
MSSSDIFDVL NIKQKSRSPT NGQVSVPSSS AANRPKPQVT GMQRELFNLL GENQPPVVIK SGNNFKEKML STSKPSPWSF VEFKANNSV TLRHWVKGSK ELIGDTPKES PYSKFNQHLS IPSFTKEEYE AFMNENEGTQ KSVESEKNHN ENFTNEKKDE S KNSWSFEE IEYLFNLCKK YDLRWFLIFD RYSYNNSRTL EDLKEKFYYT CRNYFKASDP SNPLLSSLNF SAEKEIERKK YL QRLLSRS AAEIAEEEAL VVESKKFEMA AKRTLAERES LLRLLDSPHS DQTITQYLTS QGMSQLYNAL LADKTRKRKH DLN IPENPW MKQQQQFAQH RQLQQLNVKK SEVKENLSPK KTKRQRQEMQ TALKRKSESA YAEQLLKDFN SDERKALGVI THGE KLSPG VYLRSTKLST FKPALQNKIL AILQELSLPS RPVMPSFDVM ERQEELLKKI NTLIDLKKHV DKYEAGMSIT K

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Macromolecule #7: ADENOSINE-5'-TRIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 7 / Number of copies: 1 / Formula: ATP
Molecular weightTheoretical: 507.181 Da
Chemical component information

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

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Macromolecule #8: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 8 / Number of copies: 2 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.9
GridModel: Quantifoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Support film - Material: GRAPHENE OXIDE
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TECNAI ARCTICA
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal defocus max: 1.5 µm / Nominal defocus min: 0.5 µm
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 40.0 e/Å2
Experimental equipment
Model: Talos Arctica / Image courtesy: FEI Company

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Image processing

Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 635860
FSC plot (resolution estimation)

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