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- EMDB-21114: RSC-NCP locked -

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Basic information

Entry
Database: EMDB / ID: EMD-21114
TitleRSC-NCP locked
Map dataRSC bound to acetylated nucleosome
Sample
  • Complex: RSC-NCP complex
    • Protein or peptide: x 25 types
    • DNA: x 1 types
  • Ligand: x 1 types
KeywordsChromatin remodeler / RSC / GENE REGULATION / GENE REGULATION-DNA complex
Function / homology
Function and homology information


regulation of sporulation resulting in formation of a cellular spore / RHO GTPases activate IQGAPs / RHO GTPases Activate WASPs and WAVEs / Regulation of actin dynamics for phagocytic cup formation / chromatin remodeling at centromere / histone H4 reader activity / regulation of nuclear cell cycle DNA replication / plasmid maintenance / Platelet degranulation / DNA translocase activity ...regulation of sporulation resulting in formation of a cellular spore / RHO GTPases activate IQGAPs / RHO GTPases Activate WASPs and WAVEs / Regulation of actin dynamics for phagocytic cup formation / chromatin remodeling at centromere / histone H4 reader activity / regulation of nuclear cell cycle DNA replication / plasmid maintenance / Platelet degranulation / DNA translocase activity / nucleosome array spacer activity / ATP-dependent chromatin remodeler activity / RSC-type complex / UV-damage excision repair / nucleosome disassembly / SWI/SNF complex / sister chromatid cohesion / sporulation resulting in formation of a cellular spore / nuclear chromosome / NuA4 histone acetyltransferase complex / rRNA transcription / chromosome, centromeric region / negative regulation of megakaryocyte differentiation / protein localization to CENP-A containing chromatin / Chromatin modifying enzymes / Replacement of protamines by nucleosomes in the male pronucleus / CENP-A containing nucleosome / nucleosome binding / Packaging Of Telomere Ends / Recognition and association of DNA glycosylase with site containing an affected purine / Cleavage of the damaged purine / Recognition and association of DNA glycosylase with site containing an affected pyrimidine / Cleavage of the damaged pyrimidine / cytoskeleton organization / Deposition of new CENPA-containing nucleosomes at the centromere / telomere organization / Inhibition of DNA recombination at telomere / Meiotic synapsis / Interleukin-7 signaling / RNA Polymerase I Promoter Opening / Assembly of the ORC complex at the origin of replication / Regulation of endogenous retroelements by the Human Silencing Hub (HUSH) complex / SUMOylation of chromatin organization proteins / DNA methylation / Condensation of Prophase Chromosomes / Chromatin modifications during the maternal to zygotic transition (MZT) / HCMV Late Events / SIRT1 negatively regulates rRNA expression / epigenetic regulation of gene expression / ERCC6 (CSB) and EHMT2 (G9a) positively regulate rRNA expression / chloroplast / PRC2 methylates histones and DNA / Regulation of endogenous retroelements by KRAB-ZFP proteins / Defective pyroptosis / meiotic cell cycle / : / Regulation of endogenous retroelements by Piwi-interacting RNAs (piRNAs) / positive regulation of transcription elongation by RNA polymerase II / helicase activity / HDACs deacetylate histones / chromosome segregation / transcription coregulator activity / Nonhomologous End-Joining (NHEJ) / RNA Polymerase I Promoter Escape / transcription elongation by RNA polymerase II / Transcriptional regulation by small RNAs / Formation of the beta-catenin:TCF transactivating complex / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3 / double-strand break repair via homologous recombination / G2/M DNA damage checkpoint / HDMs demethylate histones / NoRC negatively regulates rRNA expression / base-excision repair / DNA Damage/Telomere Stress Induced Senescence / B-WICH complex positively regulates rRNA expression / PKMTs methylate histone lysines / Meiotic recombination / chromatin DNA binding / Pre-NOTCH Transcription and Translation / double-strand break repair via nonhomologous end joining / Metalloprotease DUBs / RMTs methylate histone arginines / Activation of anterior HOX genes in hindbrain development during early embryogenesis / Transcriptional regulation of granulopoiesis / HCMV Early Events / G2/M transition of mitotic cell cycle / structural constituent of chromatin / UCH proteinases / nucleosome / heterochromatin formation / double-strand break repair / nucleosome assembly / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / chromatin organization / HATs acetylate histones / RUNX1 regulates transcription of genes involved in differentiation of HSCs / Factors involved in megakaryocyte development and platelet production / MLL4 and MLL3 complexes regulate expression of PPARG target genes in adipogenesis and hepatic steatosis / Processing of DNA double-strand break ends
Similarity search - Function
Chromatin structure-remodeling complex protein Rsc14 / RSC complex, Rsc14/Ldb7 subunit / : / Rsc1/Rsc2, bromodomain / : / Rsc8/Ssr1/Ssr2, zinc finger, ZZ-type / : / RSC4 Ig-like domain / Chromatin-remodelling complex, RSC SWI/SNF subunit Rsc7/Swp82 / Chromatin remodelling complex Rsc7/Swp82 subunit ...Chromatin structure-remodeling complex protein Rsc14 / RSC complex, Rsc14/Ldb7 subunit / : / Rsc1/Rsc2, bromodomain / : / Rsc8/Ssr1/Ssr2, zinc finger, ZZ-type / : / RSC4 Ig-like domain / Chromatin-remodelling complex, RSC SWI/SNF subunit Rsc7/Swp82 / Chromatin remodelling complex Rsc7/Swp82 subunit / DNA-binding RFX-type winged-helix domain / Transcription regulator protein Rtt102 / Rtt102p-like transcription regulator protein / RFX-type winged-helix DNA-binding domain profile. / : / Chromatin-remodeling complex component Sfh1/SNF5 / SMARCC, C-terminal / SWIRM-associated region 1 / SNF5/SMARCB1/INI1 / SNF5 / SMARCB1 / INI1 / Remodelling complex subunit Rsc/polybromo / Zn(2)-C6 fungal-type DNA-binding domain signature. / Fungal Zn(2)-Cys(6) binuclear cluster domain / Zn(2)-C6 fungal-type DNA-binding domain superfamily / Zn(2)-C6 fungal-type DNA-binding domain profile. / GAL4-like Zn(II)2Cys6 (or C6 zinc) binuclear cluster DNA-binding domain / Zn(2)-C6 fungal-type DNA-binding domain / Snf2-ATP coupling, chromatin remodelling complex / Snf2, ATP coupling domain / Snf2-ATP coupling, chromatin remodelling complex / HSA domain / Helicase/SANT-associated domain / HSA domain profile. / SWIRM domain / SWIRM domain / SWIRM domain profile. / Bromo adjacent homology domain / BAH domain / Bromo adjacent homology (BAH) domain / Bromo adjacent homology (BAH) domain superfamily / BAH domain profile. / SWIB/MDM2 domain superfamily / SANT domain profile. / SANT domain / Zinc-binding domain, present in Dystrophin, CREB-binding protein. / Zinc finger, ZZ type / Zinc finger, ZZ-type / Zinc finger, ZZ-type superfamily / Zinc finger ZZ-type profile. / Myb-like DNA-binding domain / : / SNF2-like, N-terminal domain superfamily / SNF2, N-terminal / SNF2-related domain / SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains / SANT/Myb domain / Actin / Actin family / Actin / Histone H2A conserved site / Histone H2A signature. / Histone H2A, C-terminal domain / C-terminus of histone H2A / Histone H2A / Histone 2A / TATA box binding protein associated factor / TATA box binding protein associated factor (TAF), histone-like fold domain / Histone H4, conserved site / Histone H4 signature. / Histone H4 / Histone H4 / CENP-T/Histone H4, histone fold / Centromere kinetochore component CENP-T histone fold / Helicase conserved C-terminal domain / Histone H3 signature 1. / Homeobox-like domain superfamily / Ribosomal protein S6, plastid/chloroplast / Histone H3 signature 2. / Histone H3 / Histone H3/CENP-A / ATPase, nucleotide binding domain / Ribosomal protein S6 / Ribosomal protein S6 / Ribosomal protein S6 superfamily / Histone H2A/H2B/H3 / Core histone H2A/H2B/H3/H4 / Translation elongation factor EF1B/ribosomal protein S6 / Bromodomain, conserved site / Bromodomain signature. / Histone-fold / Bromodomain / Bromodomain profile. / bromo domain / Bromodomain / Bromodomain-like superfamily / helicase superfamily c-terminal domain / Superfamilies 1 and 2 helicase C-terminal domain profile. / Superfamilies 1 and 2 helicase ATP-binding type-1 domain profile. / DEAD-like helicases superfamily / Helicase, C-terminal
Similarity search - Domain/homology
Small ribosomal subunit protein bS6c alpha / Histone H2A type 1-B/E / Chromatin structure-remodeling complex protein RSC6 / Nuclear protein STH1/NPS1 / Chromatin structure-remodeling complex subunit RSC7 / Chromatin structure-remodeling complex protein RSC14 / Chromatin structure-remodeling complex protein RSC30 / Chromatin structure-remodeling complex protein RSC8 / Regulator of Ty1 transposition protein 102 / Histone H4 ...Small ribosomal subunit protein bS6c alpha / Histone H2A type 1-B/E / Chromatin structure-remodeling complex protein RSC6 / Nuclear protein STH1/NPS1 / Chromatin structure-remodeling complex subunit RSC7 / Chromatin structure-remodeling complex protein RSC14 / Chromatin structure-remodeling complex protein RSC30 / Chromatin structure-remodeling complex protein RSC8 / Regulator of Ty1 transposition protein 102 / Histone H4 / Histone H3.1 / Chromatin structure-remodeling complex subunit RSC4 / Chromatin structure-remodeling complex subunit RSC9 / Actin-like protein ARP9 / Chromatin structure-remodeling complex subunit SFH1 / Chromatin structure-remodeling complex subunit RSC2 / Chromatin structure-remodeling complex protein RSC3 / Chromatin structure-remodeling complex protein RSC58 / Actin-related protein 7 / High temperature lethal protein 1
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast) / Homo sapiens (human) / synthetic construct (others)
Methodsingle particle reconstruction / cryo EM / Resolution: 20.0 Å
AuthorsPatel AB / Moore CM / Greber BJ / Nogales E
Funding support United States, 2 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01-GM63072 United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R35-GM127018 United States
CitationJournal: Elife / Year: 2019
Title: Architecture of the chromatin remodeler RSC and insights into its nucleosome engagement.
Authors: Avinash B Patel / Camille M Moore / Basil J Greber / Jie Luo / Stefan A Zukin / Jeff Ranish / Eva Nogales /
Abstract: Eukaryotic DNA is packaged into nucleosome arrays, which are repositioned by chromatin remodeling complexes to control DNA accessibility. The RSC (emodeling the tructure of hromatin) complex, a ...Eukaryotic DNA is packaged into nucleosome arrays, which are repositioned by chromatin remodeling complexes to control DNA accessibility. The RSC (emodeling the tructure of hromatin) complex, a member of the SWI/SNF chromatin remodeler family, plays critical roles in genome maintenance, transcription, and DNA repair. Here, we report cryo-electron microscopy (cryo-EM) and crosslinking mass spectrometry (CLMS) studies of yeast RSC complex and show that RSC is composed of a rigid tripartite core and two flexible lobes. The core structure is scaffolded by an asymmetric Rsc8 dimer and built with the evolutionarily conserved subunits Sfh1, Rsc6, Rsc9 and Sth1. The flexible ATPase lobe, composed of helicase subunit Sth1, Arp7, Arp9 and Rtt102, is anchored to this core by the N-terminus of Sth1. Our cryo-EM analysis of RSC bound to a nucleosome core particle shows that in addition to the expected nucleosome-Sth1 interactions, RSC engages histones and nucleosomal DNA through one arm of the core structure, composed of the Rsc8 SWIRM domains, Sfh1 and Npl6. Our findings provide structural insights into the conserved assembly process for all members of the SWI/SNF family of remodelers, and illustrate how RSC selects, engages, and remodels nucleosomes.
History
DepositionDec 13, 2019-
Header (metadata) releaseJan 15, 2020-
Map releaseJan 15, 2020-
UpdateMar 6, 2024-
Current statusMar 6, 2024Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.03
  • Imaged by UCSF Chimera
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  • Surface view colored by radius
  • Surface level: 0.03
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6v92
  • Surface level: 0.03
  • Imaged by UCSF Chimera
  • Download
  • Simplified surface model + fitted atomic model
  • Atomic modelsPDB-6v92
  • Imaged by Jmol
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_21114.png

Downloads & links

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Map

FileDownload / File: emd_21114.map.gz / Format: CCP4 / Size: 8 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationRSC bound to acetylated nucleosome
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
3.42 Å/pix.
x 128 pix.
= 437.76 Å		3.42 Å/pix.
x 128 pix.
= 437.76 Å		3.42 Å/pix.
x 128 pix.
= 437.76 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 3.42 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.03 / Movie #1: 0.03
Minimum - Maximum-0.06397076 - 0.10974972
Average (Standard dev.)0.0010008872 (±0.008293402)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions128128128
Spacing128128128
CellA=B=C: 437.76 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z3.423.423.42
M x/y/z128128128
origin x/y/z0.0000.0000.000
length x/y/z437.760437.760437.760
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS128128128
D min/max/mean-0.0640.1100.001

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Supplemental data

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Sample components

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Entire : RSC-NCP complex

EntireName: RSC-NCP complex
Components
  • Complex: RSC-NCP complex
    • Protein or peptide: Actin-related protein 7
    • Protein or peptide: Nuclear protein STH1/NPS1
    • Protein or peptide: Actin-like protein ARP9
    • Protein or peptide: Regulator of Ty1 transposition protein 102
    • Protein or peptide: High temperature lethal protein 1
    • Protein or peptide: Chromatin structure-remodeling complex protein RSC14
    • Protein or peptide: Chromatin structure-remodeling complex subunit RSC7
    • Protein or peptide: Chromatin structure-remodeling complex subunit RSC2
    • Protein or peptide: Chromatin structure-remodeling complex protein RSC3
    • Protein or peptide: Chromatin structure-remodeling complex subunit RSC4
    • Protein or peptide: Chromatin structure-remodeling complex protein RSC8
    • Protein or peptide: Chromatin structure-remodeling complex protein RSC6
    • Protein or peptide: Chromatin structure-remodeling complex subunit RSC9
    • Protein or peptide: Chromatin structure-remodeling complex protein RSC58
    • Protein or peptide: Chromatin structure-remodeling complex subunit SFH1
    • Protein or peptide: Chromatin structure-remodeling complex protein RSC30
    • Protein or peptide: Unknown Protein
    • Protein or peptide: Unknown Protein
    • Protein or peptide: Unknown Protein
    • Protein or peptide: Uuknown Protein
    • Protein or peptide: Unknown Protein
    • DNA: DNA (146-MER)
    • Protein or peptide: Histone H3.1
    • Protein or peptide: Histone H4
    • Protein or peptide: Histone H2A type 1-B/E
    • Protein or peptide: Histone H2B type 1-K
  • Ligand: ZINC ION

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Supramolecule #1: RSC-NCP complex

SupramoleculeName: RSC-NCP complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#26
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c

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Macromolecule #1: Actin-related protein 7

MacromoleculeName: Actin-related protein 7 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 53.863016 KDa
SequenceString: MTLNRKCVVI HNGSHRTVAG FSNVELPQCI IPSSYIKRTD EGGEAEFIFG TYNMIDAAAE KRNGDEVYTL VDSQGLPYNW DALEMQWRY LYDTQLKVSP EELPLVITMP ATNGKPDMAI LERYYELAFD KLNVPVFQIV IEPLAIALSM GKSSAFVIDI G ASGCNVTP ...String:
MTLNRKCVVI HNGSHRTVAG FSNVELPQCI IPSSYIKRTD EGGEAEFIFG TYNMIDAAAE KRNGDEVYTL VDSQGLPYNW DALEMQWRY LYDTQLKVSP EELPLVITMP ATNGKPDMAI LERYYELAFD KLNVPVFQIV IEPLAIALSM GKSSAFVIDI G ASGCNVTP IIDGIVVKNA VVRSKFGGDF LDFQVHERLA PLIKEENDME NMADEQKRST DVWYEASTWI QQFKSTMLQV SE KDLFELE RYYKEQADIY AKQQEQLKQM DQQLQYTALT GSPNNPLVQK KNFLFKPLNK TLTLDLKECY QFAEYLFKPQ LIS DKFSPE DGLGPLMAKS VKKAGASINS MKANTSTNPN GLGTSHINTN VGDNNSTASS SNISPEQVYS LLLTNVIITG STSL IEGME QRIIKELSIR FPQYKLTTFA NQVMMDRKIQ GWLGALTMAN LPSWSLGKWY SKEDYETLKR DRKQSQATNA TN

UniProtKB: Actin-related protein 7

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Macromolecule #2: Nuclear protein STH1/NPS1

MacromoleculeName: Nuclear protein STH1/NPS1 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA helicase
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 156.982406 KDa
SequenceString: MLQEQSELMS TVMNNTPTTV AALAAVAAAS ETNGKLGSEE QPEITIPKPR SSAQLEQLLY RYRAIQNHPK ENKLEIKAIE DTFRNISRD QDIYETKLDT LRKSIDKGFQ YDEDLLNKHL VALQLLEKDT DVPDYFLDLP DTKNDNTTAI EVDYSEKKPI K ISADFNAK ...String:
MLQEQSELMS TVMNNTPTTV AALAAVAAAS ETNGKLGSEE QPEITIPKPR SSAQLEQLLY RYRAIQNHPK ENKLEIKAIE DTFRNISRD QDIYETKLDT LRKSIDKGFQ YDEDLLNKHL VALQLLEKDT DVPDYFLDLP DTKNDNTTAI EVDYSEKKPI K ISADFNAK AKSLGLESKF SNATKTALGD PDTEIRISAR ISNRINELER LPANLGTYSL DDCLEFITKD DLSSRMDTFK IK ALVELKS LKLLTKQKSI RQKLINNVAS QAHHNIPYLR DSPFTAAAQR SVQIRSKVIV PQTVRLAEEL ERQQLLEKRK KER NLHLQK INSIIDFIKE RQSEQWSRQE RCFQFGRLGA SLHNQMEKDE QKRIERTAKQ RLAALKSNDE EAYLKLLDQT KDTR ITQLL RQTNSFLDSL SEAVRAQQNE AKILHGEEVQ PITDEEREKT DYYEVAHRIK EKIDKQPSIL VGGTLKEYQL RGLEW MVSL YNNHLNGILA DEMGLGKTIQ SISLITYLYE VKKDIGPFLV IVPLSTITNW TLEFEKWAPS LNTIIYKGTP NQRHSL QHQ IRVGNFDVLL TTYEYIIKDK SLLSKHDWAH MIIDEGHRMK NAQSKLSFTI SHYYRTRNRL ILTGTPLQNN LPELWAL LN FVLPKIFNSA KTFEDWFNTP FANTGTQEKL ELTEEETLLI IRRLHKVLRP FLLRRLKKEV EKDLPDKVEK VIKCKLSG L QQQLYQQMLK HNALFVGAGT EGATKGGIKG LNNKIMQLRK ICNHPFVFDE VEGVVNPSRG NSDLLFRVAG KFELLDRVL PKFKASGHRV LMFFQMTQVM DIMEDFLRMK DLKYMRLDGS TKTEERTEML NAFNAPDSDY FCFLLSTRAG GLGLNLQTAD TVIIFDTDW NPHQDLQAQD RAHRIGQKNE VRILRLITTD SVEEVILERA MQKLDIDGKV IQAGKFDNKS TAEEQEAFLR R LIESETNR DDDDKAELDD DELNDTLARS ADEKILFDKI DKERMNQERA DAKAQGLRVP PPRLIQLDEL PKVFREDIEE HF KKEDSEP LGRIRQKKRV YYDDGLTEEQ FLEAVEDDNM SLEDAIKKRR EARERRRLRQ NGTKENEIET LENTPEASET SLI ENNSFT AAVDEETNAD KETTASRSKR RSSRKKRTIS IVTAEDKENT QEESTSQENG GAKVEEEVKS SSVEIINGSE SKKK KPKLT VKIKLNKTTV LENNDGKRAE EKPESKSPAK KTAAKKTKTK SKSLGIFPTV EKLVEEMREQ LDEVDSHPRT SIFEK LPSK RDYPDYFKVI EKPMAIDIIL KNCKNGTYKT LEEVRQALQT MFENARFYNE EGSWVYVDAD KLNEFTDEWF KEHSS

UniProtKB: Nuclear protein STH1/NPS1

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Macromolecule #3: Actin-like protein ARP9

MacromoleculeName: Actin-like protein ARP9 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 53.13193 KDa
SequenceString: MAPFRQDSIL IIYPRSQTTL VQFGLNEETF TVPELEIPTQ IYRTTRQDGS YTYHSTNKDN KAELIKPIQN GEIIDISAFT QFLRLIFVS ILSDRANKNQ DAFEAELSNI PLLLITHHSW SQSDLEIITQ YVFESLEINN LIQLPASLAA TYSMISLQNC C IIDVGTHH ...String:
MAPFRQDSIL IIYPRSQTTL VQFGLNEETF TVPELEIPTQ IYRTTRQDGS YTYHSTNKDN KAELIKPIQN GEIIDISAFT QFLRLIFVS ILSDRANKNQ DAFEAELSNI PLLLITHHSW SQSDLEIITQ YVFESLEINN LIQLPASLAA TYSMISLQNC C IIDVGTHH TDIIPIVDYA QLDHLVSSIP MGGQSINDSL KKLLPQWDDD QIESLKKSPI FEVLSDDAKK LSSFDFGNEN ED EDEGTLN VAEIITSGRD TREVLEERER GQKVKNVKNS DLEFNTFWDE KGNEIKVGKQ RFQGCNNLIK NISNRVGLTL DNI DDINKA KAVWENIIIV GGTTSISGFK EALLGQLLKD HLIIEPEEEK SKREEEAKSV LPAATKKKSK FMTNSTAFVP TIEY VQCPT VIKLAKYPDY FPEWKKSGYS EIIFLGAQIV SKQIFTHPKD TFYITREKYN MKGPAALWDV QF

UniProtKB: Actin-like protein ARP9

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Macromolecule #4: Regulator of Ty1 transposition protein 102

MacromoleculeName: Regulator of Ty1 transposition protein 102 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 17.817615 KDa
SequenceString:
MDPQTLITKA NKVSYYGNPT SKESWRYDWY QPSKVSSNVQ QPQQQLGDME NNLEKYPFRY KTWLRNQEDE KNLQRESCED ILDLKEFDR RILKKSLMTS HTKGDTSKAT GAPSANQGDE ALSVDDIRGA VGNSEAIPGL SAGVNNDNTK ESKDVKMN

UniProtKB: Regulator of Ty1 transposition protein 102

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Macromolecule #5: High temperature lethal protein 1

MacromoleculeName: High temperature lethal protein 1 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 9.192524 KDa
SequenceString:
MSQNNTISSM NPERAYNNVT LKNLTAFQLL SQRENICELL NLVESTERHN SIINPERQRM SLEEMKKMLD ALKNERKK

UniProtKB: High temperature lethal protein 1

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Macromolecule #6: Chromatin structure-remodeling complex protein RSC14

MacromoleculeName: Chromatin structure-remodeling complex protein RSC14 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 19.825398 KDa
SequenceString:
MSGSNMGYYD VLAGLSALEK SSQVVFSATE LQQLTQQSHA TDKGIEGSEN SKAKVSKPKR VAVHGYLGGK VSLADAAQVE YEVGHSLLG SYVPRQQLEA LSSVDFSHHF HRTLECKAAL ETHDVFLAGA GQLSLPFQSH IESPRNSEAK RKRKVIICKR C QSRFIGSH RRSQLREHAC VD

UniProtKB: Chromatin structure-remodeling complex protein RSC14

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Macromolecule #7: Chromatin structure-remodeling complex subunit RSC7

MacromoleculeName: Chromatin structure-remodeling complex subunit RSC7 / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 49.71652 KDa
SequenceString: MSDSEGGLAS EVEHEKRSRS TSNRPNYAID TEDLDIDEND ENEDDDYREE EANEGVNEEE ISDEEEQINK SGRNKRRHVD EEEDLSEDK GVTRSRNRSK FKKPVFPGID DAEENLNPLK VVNEEYVLPD DPEGETKITA DGDLLGGREF LVRTFTLTEK G NRKFMLAT ...String:
MSDSEGGLAS EVEHEKRSRS TSNRPNYAID TEDLDIDEND ENEDDDYREE EANEGVNEEE ISDEEEQINK SGRNKRRHVD EEEDLSEDK GVTRSRNRSK FKKPVFPGID DAEENLNPLK VVNEEYVLPD DPEGETKITA DGDLLGGREF LVRTFTLTEK G NRKFMLAT EPARIVGFRD SYLFFQTHPN LYKFILNQTQ KNDLIDRGVL PYSYRNRQIA LVTARGVFKE FGAKIIRGGK HI TDDYYAS ELRTKGNVIE GKLAGDPIDK SARALETMMY PASENGINPA KNQVEFFEHR PHGHMSNSNI IASGSKLSST NWL YQHSAA CSRFNSDLFY DRVKVLLVDQ QGLRDAYTNI LHIPESTQST TVLGWRRSKN DSPSDTSIVY ETVIHDNDLN KPKT GLSEI PKEIYEDVVD EDVLRAITEQ QNFEKCNEYI

UniProtKB: Chromatin structure-remodeling complex subunit RSC7

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Macromolecule #8: Chromatin structure-remodeling complex subunit RSC2

MacromoleculeName: Chromatin structure-remodeling complex subunit RSC2 / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 102.443664 KDa
SequenceString: MMPDDNSNSS TQNSSALYKD LRKEYESLFT LKEDSGLEIS PIFNVLPPKK DYPDYYAVIK NPVSFNTLKK RIPHYTDAQQ FMNDVVQIP WNAKTYNTRD SGIYKYALVL EKYLKDTIYP NLKEKYPQLV YPDLGPLPDE PGYEEFQQKL REKAEEVARA N AARAESSS ...String:
MMPDDNSNSS TQNSSALYKD LRKEYESLFT LKEDSGLEIS PIFNVLPPKK DYPDYYAVIK NPVSFNTLKK RIPHYTDAQQ FMNDVVQIP WNAKTYNTRD SGIYKYALVL EKYLKDTIYP NLKEKYPQLV YPDLGPLPDE PGYEEFQQKL REKAEEVARA N AARAESSS SMNSTEAARR LRKTRTSVKR ESEPGTDTNN DEDYEATDMD IDNPKDADFP DLIRKPLINI NPYTRKPLRD NR STTPSHS GTPQPLGPRH RQVSRTQVKR GRPPIIDLPY IQRMKNVMKV LKKEVLDSGI GLTDLFERLP DRHRDANYYI MIA NPISLQ DINKKVKTRR YKTFQEFQND FNLMLTNFRI SHRGDPESIK ISNILEKTFT SLARFELSKP DRSFIPEGEL RYPL DEVIV NNISYHVGDW ALLRNQNDPQ KPIVGQIFRL WKTPDGKQWL NACWYYRPEQ TVHRVDRLFY KNEVMKTGQY RDHLV SNLV GKCYVIHFTR YQRGNPDMKL EGPLFVCEFR YNESDKIFNK IRTWKACLPE EIRDLDEATI PVNGRKFFKY PSPIRH LLP ANATPHDRVP EPTMGSPDAP PLVGAVYMRP KMQRDDLGEY ATSDDCPRYI IRPNDSPEEG QVDIETGTIT TNTPTAN AL PKTGYSSSKL SSLRYNRSSM SLENQNAIGQ QQIPLSRVGS PGAGGPLTVQ GLKQHQLQRL QQQQHQYQQQ KRSQASRY N IPTIIDDLTS QASRGNLGNI MIDAASSFVL PISITKNVDV LQRTDLHSQT KRSGREEMFP WKKTKGEILW FRGPSVIVN ERIINSGDPH LSLPLNRWFT TNKKRKLEYE EVEETMEDVT GKDKDDDGLE PDVENEKESL PGPFVLGLRP SAKFTAHRLS MLRPPSSSS

UniProtKB: Chromatin structure-remodeling complex subunit RSC2

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Macromolecule #9: Chromatin structure-remodeling complex protein RSC3

MacromoleculeName: Chromatin structure-remodeling complex protein RSC3 / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 101.833961 KDa
SequenceString: MDIRGRKMKK PPACVQCRKR KIGCDRVKPI CGNCMKHNKM DCFYPDVPGQ YVPSSSSSSN TRQVANGPYL NSYYASRRVS KETAALLQK NPELASLEQI REYNTRLQLL NAQNQLNNRS SAANATLNQQ HTQYIPKSVP SLESKPVTSA NESSTPLNWV Q GPAIFHML ...String:
MDIRGRKMKK PPACVQCRKR KIGCDRVKPI CGNCMKHNKM DCFYPDVPGQ YVPSSSSSSN TRQVANGPYL NSYYASRRVS KETAALLQK NPELASLEQI REYNTRLQLL NAQNQLNNRS SAANATLNQQ HTQYIPKSVP SLESKPVTSA NESSTPLNWV Q GPAIFHML TSPYTQDEII NHEMNFLKGR LLELQEITGK KITGVNLDLK QDSSAQMQSS HSNRNQEEFL TIKKRKLSED GV TDGDGKP IPESERRPHL NEFKDLDPQF LDTNKVFNVF NSAISEEGRN RLWLLPKNIN KSSIFQIQYL IERDPFLFKF FND LNILIE TQFNGPLHDL VASRNSIERN SGISQILKFP SQSITQTLIN KYLSTITETN SILPILKPKR LLPIVEQLFP SNTI NKPNS KDFETIFQVF SVTNDQLLNL GFITLCLLIL FESLNSTVLI PLRDDEHLQL FNVLFNYLPL LKSNLTTLRF EIEKR SMCN IETLRFISLW KYYQFVMDTS SSSSFVIDYD EDMHMACLLS LNHETQNQSH ILTWNFIFKN YCWRHLFLGQ LPLLMS EPF TNSTPIIDPL LNNDFELIDF EVNLMKYLQS KDQQLSIDKI IQLIKLLKNK NIEVSQGCLT TPSIINNIMD SLIYRNS ML YLNFYLLLQF ETLKNYAKFN EILEDFLELS RETLFFVFSN LANIKFAGHE FTFINKSIVV LQTLVLMLLA LYQRSFDS S KRTNDANEIS EQTDIHSNND NSKRIKNKNV IHLIINKIAM LLSDYTKNCK KQNKLIENLI IKIKTISKYI KNLEENKVT TSADSNYSIN NGFSGISAEQ LIKLNHELSK ISESLIKTDF YEQRKNSTVS NGVLGAAAPV DSDANSDTFG LTKENFNEVF EAIRS

UniProtKB: Chromatin structure-remodeling complex protein RSC3

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Macromolecule #10: Chromatin structure-remodeling complex subunit RSC4

MacromoleculeName: Chromatin structure-remodeling complex subunit RSC4 / type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 72.372375 KDa
SequenceString: MVVKKRKLAT EAGGSDERPK YLPGKHPKNQ EKTPHVDYNA PLNPKSELFL DDWHIPKFNR FISFTLDVLI DKYKDIFKDF IKLPSRKFH PQYYYKIQQP MSINEIKSRD YEYEDGPSNF LLDVELLTKN CQAYNEYDSL IVKNSMQVVM LIEFEVLKAK N LKRNYLIN ...String:
MVVKKRKLAT EAGGSDERPK YLPGKHPKNQ EKTPHVDYNA PLNPKSELFL DDWHIPKFNR FISFTLDVLI DKYKDIFKDF IKLPSRKFH PQYYYKIQQP MSINEIKSRD YEYEDGPSNF LLDVELLTKN CQAYNEYDSL IVKNSMQVVM LIEFEVLKAK N LKRNYLIN SEVKAKLLHY LNKLVDATEK KINQALLGAS SPKNLDDKVK LSEPFMELVD KDELPEYYEI VHSPMALSIV KQ NLEIGQY SKIYDFIIDM LLVFQNAHIF NDPSALIYKD ATTLTNYFNY LIQKEFFPEL QDLNERGEIN LEFDKFEFEN YLA IGGGGP AAAGALAISA LDNDIEPESN REDLIDQADY DFNHFEGLGN GYNRSLLTED YLLNPNNFKK LIAKPETVQS EVKN ERSTT SDIEKTNSLE SEHLKIPKYN VIKSMQKEMQ SLSEQHTMEY KPYKLIQQIY IFSSKNLYSQ ATKPLLGSRP SCNQN WVEY IFNGNELSQN ENAFSFMLQP MQTFLTLQSH LTSSLKDTET LLTINKEPVK SRTSNVNSNL SQPQQQENDV IGNDTK QDI ENLTIGGGNN NDIVGNDNDK RNNITEIFDI RLSEGLNHLM FRCEDKISHE TEFMNFWINV LP

UniProtKB: Chromatin structure-remodeling complex subunit RSC4

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Macromolecule #11: Chromatin structure-remodeling complex protein RSC8

MacromoleculeName: Chromatin structure-remodeling complex protein RSC8 / type: protein_or_peptide / ID: 11 / Number of copies: 4 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 63.253965 KDa
SequenceString: MSDTEKDKDV PMVDSHEATE EPPTTSTNTP SFPHLAQEQA KEESATLGAE VAHKKINYEQ EAQKLEEKAL RFLAKQTHPV IIPSFASWF DISKIHEIEK RSNPDFFNDS SRFKTPKAYK DTRNFIINTY RLSPYEYLTI TAVRRNVAMD VASIVKIHAF L EKWGLINY ...String:
MSDTEKDKDV PMVDSHEATE EPPTTSTNTP SFPHLAQEQA KEESATLGAE VAHKKINYEQ EAQKLEEKAL RFLAKQTHPV IIPSFASWF DISKIHEIEK RSNPDFFNDS SRFKTPKAYK DTRNFIINTY RLSPYEYLTI TAVRRNVAMD VASIVKIHAF L EKWGLINY QIDPRTKPSL IGPSFTGHFQ VVLDTPQGLK PFLPENVIKQ EVEGGDGAEP QVKKEFPVNL TIKKNVYDSA QD FNALQDE SRNSRQIHKV YICHTCGNES INVRYHNLRA RDTNLCSRCF QEGHFGANFQ SSDFIRLENN GNSVKKNWSD QEM LLLLEG IEMYEDQWEK IADHVGGHKR VEDCIEKFLS LPIEDNYIRE VVGSTLNGKG GDSRDGSVSG SKLMECVNDA VQTL LQGDD KLGKVSDKSR EISEKYIEES QAIIQELVKL TMEKLESKFT KLCDLETQLE MEKLKYVKES EKMLNDRLSL SKQIL DLNK SLEELNVSKK LVLISEQVDS GIQLVEKDQE GDDEDGNTAT GHGVKRVGKE GEEVGEGDSI AKLQPQVYKP WSL

UniProtKB: Chromatin structure-remodeling complex protein RSC8

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Macromolecule #12: Chromatin structure-remodeling complex protein RSC6

MacromoleculeName: Chromatin structure-remodeling complex protein RSC6 / type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 54.222691 KDa
SequenceString: MVTQTNPVPV TYPTDAYIPT YLPDDKVSNL ADLKKLIEMD SRLDLYLTRR RLDTSINLPT NTKTKDHPPN KEMLRIYVYN TTESSPRSD SGTPADSGKT TWTLRIEGKL LHESANGKHP FSEFLEGVAV DFKRLKPLGM GKKRKRDSSL SLPLNLQQPE Y NDQDSTMG ...String:
MVTQTNPVPV TYPTDAYIPT YLPDDKVSNL ADLKKLIEMD SRLDLYLTRR RLDTSINLPT NTKTKDHPPN KEMLRIYVYN TTESSPRSD SGTPADSGKT TWTLRIEGKL LHESANGKHP FSEFLEGVAV DFKRLKPLGM GKKRKRDSSL SLPLNLQQPE Y NDQDSTMG DNDNGEDEDS AEAESREEIV DALEWNYDEN NVVEFDGIDI KRQGKDNLRC SITIQLRGVD GGKVQYSPNL AT LIGMQTG SVNDAVYSIY KYILINNLFV TEQTEAQDGS NDAEDSSNEN NNKNGAGDDD GVEGSTPKDK PELGEVKLDS LLQ KVLDTN AAHLPLMNVV QTVNKLVSPL PPIILDYTID LSKDTTYGAT TLDVDVSHIL HQPQPQPNLQ KEEETDAEDT AKLR EITKL ALQLNSSAQK YQFFHELSLH PRETLTHYLW SSKQNELVLQ GDQYFNEDAA RTSDIYSNNN NDRSLMGNIS LLYSQ GRL

UniProtKB: Chromatin structure-remodeling complex protein RSC6

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Macromolecule #13: Chromatin structure-remodeling complex subunit RSC9

MacromoleculeName: Chromatin structure-remodeling complex subunit RSC9 / type: protein_or_peptide / ID: 13 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 65.289309 KDa
SequenceString: MNSLASNTPL NGTPVSEAPA TSSEPVNMFE TMVANPIKVS RLQSNGVLTG PAANTKSIHY SLANFNVFQS LPKETARGVD DLTRMEMAL LSGIPEEIKW SLKKYLTYSN KAPYMISLRT LPDLLPLFKT FILPLERIVE GLNKSSICDS KAMDSLQMGL N ALLILRNL ...String:
MNSLASNTPL NGTPVSEAPA TSSEPVNMFE TMVANPIKVS RLQSNGVLTG PAANTKSIHY SLANFNVFQS LPKETARGVD DLTRMEMAL LSGIPEEIKW SLKKYLTYSN KAPYMISLRT LPDLLPLFKT FILPLERIVE GLNKSSICDS KAMDSLQMGL N ALLILRNL AQDTDSVQIL VKDREIKSFI LFILKKFQCV ATGDNKWQLY EGNATFFNEL THYTLDLMEA ISSYIAPAMK DD HYFQTLV SILNYTKDRY MVISILRSLS RLLVRSKANE ESAADNLDHK TLSLIVSFLL LECDSELIIA SLDFLYQYIL PGS QRITEL FKSKECSLIL EATLPNLLSY NIATPDYHLL QKHKIRLIKR LKPPAPKEPP NLSEDLFQQL FKLNEPLRST AWLR CCFEP VQEAEFTQIS LWRSYESKFG QPVRESGRKL LPAVEFIKNV SNAFNNAAAI VITDPVTGKK RFVIKGIQPR FKALG IADG ERESQVPISA LKSKFLNDSK EITPARQNSI PEVKFPQELS DVSKVACTFL CLLSNDTDDG AGSAFCQRIR PLVLHK LAD IPPLTLALSE YMENTSGL

UniProtKB: Chromatin structure-remodeling complex subunit RSC9

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Macromolecule #14: Chromatin structure-remodeling complex protein RSC58

MacromoleculeName: Chromatin structure-remodeling complex protein RSC58 / type: protein_or_peptide / ID: 14 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 57.871309 KDa
SequenceString: MTESVGGNKL VDFLVNVQSI LNAASVKCHV VDESFPAKFF EKNPDKIYES YCKFIKNRSN SEGLIRNEDK LVLTTINKRF ENGEYEPIQ GGFYKLYHDI KLVCTILIHF YPQGTRNYQL VDKFYKFSSE LLLRECCRIG IALTQTNNIK SRSGKLLSGN E MDEYDDDD ...String:
MTESVGGNKL VDFLVNVQSI LNAASVKCHV VDESFPAKFF EKNPDKIYES YCKFIKNRSN SEGLIRNEDK LVLTTINKRF ENGEYEPIQ GGFYKLYHDI KLVCTILIHF YPQGTRNYQL VDKFYKFSSE LLLRECCRIG IALTQTNNIK SRSGKLLSGN E MDEYDDDD ATELDKIISY DFIKISMNYT VPISQTYQIR TKDMDLFSSI ISKSNLDKRP HELPNTNFKI NNVLPQTDIE NE APRLGFV GANTSNIPDP TLPPTEMMTR FLHPNWYALP TTVWLKYGNY NSWAPSFNEN GTVVDSTTRG LIWLERIGYM DLY EKNEKK VKQEELLNTN EEGINRKQND ENNKNVDGKS NGVQDDGGDN DNDATIASAN SESTENKEQF IIKLQNLYNW TPSN YIGDD EIENFRNGTP DKLVSDSLLK LKRLRKERIL NKVLKPTTEE RELYFKVKRI LKEVILAKKV SKVPINNVRA FPVLQ TNYN GSIPVVRAQP GRKRKHKK

UniProtKB: Chromatin structure-remodeling complex protein RSC58

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Macromolecule #15: Chromatin structure-remodeling complex subunit SFH1

MacromoleculeName: Chromatin structure-remodeling complex subunit SFH1 / type: protein_or_peptide / ID: 15 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 48.83318 KDa
SequenceString: MSHQNQLIPQ AYISNFHNRL TNEDDGIPIF TMAQQTRQHK RAKVVNYAEY DNDLFDEFNM NGSNFNNADT HYKDNAVSHE NTPALTNGV TMDGSEYNVL ENMNGADSII SNNKYDAGSN MVVESLSGLN SNNNASNGPS NKAQAQDIGN AVLPDLQDQH H NPFNILRY ...String:
MSHQNQLIPQ AYISNFHNRL TNEDDGIPIF TMAQQTRQHK RAKVVNYAEY DNDLFDEFNM NGSNFNNADT HYKDNAVSHE NTPALTNGV TMDGSEYNVL ENMNGADSII SNNKYDAGSN MVVESLSGLN SNNNASNGPS NKAQAQDIGN AVLPDLQDQH H NPFNILRY PKIRDTFING KVVSPYRLNT DQETKANANS GEAIMIPITL DIEHMGHTIK DQFLWNYNDD SISPEEFASI YC KDLDMTS ATLQTQIANI IKEQLKDLEN IAATEIMSDL HVIINLTCNL QDRFFEDNFQ WNLNDKSLTP ERFATSIVQD LGL TREFIP LISQSLHETI LKIKKDWVDG HLIQDHVPND AAFGYLSGIR LDIDELGSNW CPRVEILTKE EIQKREIEKE RNLR RLKRE TDRLSRRGRR RLDDLETTMR M

UniProtKB: Chromatin structure-remodeling complex subunit SFH1

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Macromolecule #16: Chromatin structure-remodeling complex protein RSC30

MacromoleculeName: Chromatin structure-remodeling complex protein RSC30 / type: protein_or_peptide / ID: 16 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 101.448211 KDa
SequenceString: MMDMQVRKVR KPPACTQCRK RKIGCDRAKP ICGNCVKYNK PDCFYPDGPG KMVAVPSASG MSTHGNGQGS NHFSQGNGVN QKNVMIQTQ YPIMQTSIEA FNFSFNPSVD TAMQWTKAAS YQNNNTNNNT APRQNSSTVS SNVHGNTIVR SDSPDVPSMD Q IREYNTRL ...String:
MMDMQVRKVR KPPACTQCRK RKIGCDRAKP ICGNCVKYNK PDCFYPDGPG KMVAVPSASG MSTHGNGQGS NHFSQGNGVN QKNVMIQTQ YPIMQTSIEA FNFSFNPSVD TAMQWTKAAS YQNNNTNNNT APRQNSSTVS SNVHGNTIVR SDSPDVPSMD Q IREYNTRL QLVNAQSFDY TDNPYSFNVG INQDSAVFDL MTSPFTQEEV LIKEIDFLKN KLLDLQSLQL KSLKEKSNLN AD NTTANKI NKTGENSKKG KVDGKRAGFD HQTSRTSQSS QKYFTALTIT DVQSLVQVKP LKDTPNYLFT KNFIIFRDHY LFK FYNILH DICHINQFKV SPPNNKNHQQ YMEVCKVNFP PKAIIIETLN SESLNNLNIE EFLPIFDKTL LLEFVHNSFP NGDT CPSFS TVDLPLSQLT KLGELTVLLL LLNDSMTLFN KQAINNHVSA LMNNLRLIRS QITLINLEYY DQETIKFIAI TKFYE SLYM HDDHKSSLDE DLSCLLSFQI KDFKLFHFLK KMYYSRHSLL GQSSFMVPAA ENLSPIPASI DTNDIPLIAN DLKLLE TQA KLINILQGVP FYLPVNLTKI ESLLETLTMG VSNTVDLYFH DNEVRKEWKD TLNFINTIVY TNFFLFVQNE SSLSMAV QH SSNNNKTSNS ERCAKDLMKI ISNMHIFYSI TFNFIFPIKS IKSFSSGNNR FHSNGKEFLF ANHFIEILQN FIAITFAI F QRCEVILYDE FYKNLSNEEI NVQLLLIHDK ILEILKKIEI IVSFLRDEMN SNGSFKSIKG FNKVLNLIKY MLRFSKKKQ NFARNSDNNN VTDYSQSAKN KNVLLKFPVS ELNRIYLKFK EISDFLMERE VVQRSIIIDK DLESDNLGIT TANFNDFYDA FYN

UniProtKB: Chromatin structure-remodeling complex protein RSC30

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Macromolecule #17: Unknown Protein

MacromoleculeName: Unknown Protein / type: protein_or_peptide / ID: 17 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 2.400951 KDa
SequenceString:
(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)

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Macromolecule #18: Unknown Protein

MacromoleculeName: Unknown Protein / type: protein_or_peptide / ID: 18 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 1.635006 KDa
SequenceString:
(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)

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Macromolecule #19: Unknown Protein

MacromoleculeName: Unknown Protein / type: protein_or_peptide / ID: 19 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 1.209482 KDa
SequenceString:
(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)

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Macromolecule #20: Uuknown Protein

MacromoleculeName: Uuknown Protein / type: protein_or_peptide / ID: 20 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 1.294587 KDa
SequenceString:
(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)

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Macromolecule #21: Unknown Protein

MacromoleculeName: Unknown Protein / type: protein_or_peptide / ID: 21 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 4.188154 KDa
SequenceString: (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) ...String:
(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)

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Macromolecule #23: Histone H3.1

MacromoleculeName: Histone H3.1 / type: protein_or_peptide / ID: 23 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 15.437167 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSA VMALQEACEA YLVGLFEDTN LCAIHAKRVT IMPKDIQLAR RIRGERA

UniProtKB: Histone H3.1

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Macromolecule #24: Histone H4

MacromoleculeName: Histone H4 / type: protein_or_peptide / ID: 24 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 11.394426 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK VFLENVIRDA VTYTEHAKRK TVTAMDVVY ALKRQGRTLY GFGG

UniProtKB: Histone H4

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Macromolecule #25: Histone H2A type 1-B/E

MacromoleculeName: Histone H2A type 1-B/E / type: protein_or_peptide / ID: 25 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 14.165551 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MSGRGKQGGK ARAKAKTRSS RAGLQFPVGR VHRLLRKGNY SERVGAGAPV YLAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAIR NDEELNKLLG RVTIAQGGVL PNIQAVLLPK KTESHHKAKG K

UniProtKB: Histone H2A type 1-B/E

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Macromolecule #26: Histone H2B type 1-K

MacromoleculeName: Histone H2B type 1-K / type: protein_or_peptide / ID: 26 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 13.921213 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MPEPAKSAPA PKKGSKKAVT KAQKKDGKKR KRSRKESYSV YVYKVLKQVH PDTGISSKAM GIMNSFVNDI FERIAGEASR LAHYNKRST ITSREIQTAV RLLLPGELAK HAVSEGTKAV TKYTSAK

UniProtKB: Small ribosomal subunit protein bS6c alpha

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Macromolecule #22: DNA (146-MER)

MacromoleculeName: DNA (146-MER) / type: dna / ID: 22 / Number of copies: 2 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 45.053855 KDa
SequenceString: (DA)(DT)(DC)(DA)(DA)(DT)(DA)(DT)(DC)(DC) (DA)(DC)(DC)(DT)(DG)(DC)(DA)(DG)(DA)(DT) (DT)(DC)(DT)(DA)(DC)(DC)(DA)(DA)(DA) (DA)(DG)(DT)(DG)(DT)(DA)(DT)(DT)(DT)(DG) (DG) (DA)(DA)(DA)(DC)(DT)(DG) ...String:
(DA)(DT)(DC)(DA)(DA)(DT)(DA)(DT)(DC)(DC) (DA)(DC)(DC)(DT)(DG)(DC)(DA)(DG)(DA)(DT) (DT)(DC)(DT)(DA)(DC)(DC)(DA)(DA)(DA) (DA)(DG)(DT)(DG)(DT)(DA)(DT)(DT)(DT)(DG) (DG) (DA)(DA)(DA)(DC)(DT)(DG)(DC)(DT) (DC)(DC)(DA)(DT)(DC)(DA)(DA)(DA)(DA)(DG) (DG)(DC) (DA)(DT)(DG)(DT)(DT)(DC)(DA) (DG)(DC)(DT)(DG)(DA)(DA)(DT)(DT)(DC)(DA) (DG)(DC)(DT) (DG)(DA)(DA)(DC)(DA)(DT) (DG)(DC)(DC)(DT)(DT)(DT)(DT)(DG)(DA)(DT) (DG)(DG)(DA)(DG) (DC)(DA)(DG)(DT)(DT) (DT)(DC)(DC)(DA)(DA)(DA)(DT)(DA)(DC)(DA) (DC)(DT)(DT)(DT)(DT) (DG)(DG)(DT)(DA) (DG)(DA)(DA)(DT)(DC)(DT)(DG)(DC)(DA)(DG) (DG)(DT)(DG)(DG)(DA)(DT) (DA)(DT)(DT) (DG)(DA)(DT)

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Macromolecule #27: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 27 / Number of copies: 1 / Formula: ZN
Molecular weightTheoretical: 65.409 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
GridDetails: unspecifed
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TALOS ARCTICA
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Talos Arctica / Image courtesy: FEI Company

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Image processing

Startup modelType of model: OTHER
Final reconstructionResolution.type: BY AUTHOR / Resolution: 20.0 Å / Resolution method: FSC 0.5 CUT-OFF / Number images used: 13337
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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