[English] 日本語
Yorodumi
- EMDB-0777: The ClassA RSC-Nucleosome Complex -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-0777
TitleThe ClassA RSC-Nucleosome Complex
Map dataThe ClassA RSC-Nucleosome Complex
Sample
  • Complex: RSC
    • Protein or peptide: x 19 types
    • DNA: x 2 types
  • Ligand: x 1 types
Keywordschromatin remodeler / SWI/SNF family / DNA BINDING PROTEIN-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 / regulation of nuclear cell cycle DNA replication / plasmid maintenance / Platelet degranulation / DNA translocase activity / RSC-type complex ...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 / regulation of nuclear cell cycle DNA replication / plasmid maintenance / Platelet degranulation / DNA translocase activity / RSC-type complex / UV-damage excision repair / SWI/SNF complex / nucleosome disassembly / sister chromatid cohesion / ATP-dependent chromatin remodeler activity / nuclear chromosome / sporulation resulting in formation of a cellular spore / NuA4 histone acetyltransferase complex / rRNA transcription / nucleosome binding / chromosome, centromeric region / ATP-dependent activity, acting on DNA / cytoskeleton organization / histone reader activity / meiotic cell cycle / DNA-templated transcription initiation / chromosome segregation / helicase activity / positive regulation of transcription elongation by RNA polymerase II / transcription elongation by RNA polymerase II / transcription coregulator activity / lysine-acetylated histone binding / double-strand break repair via homologous recombination / base-excision repair / chromatin DNA binding / double-strand break repair via nonhomologous end joining / structural constituent of chromatin / G2/M transition of mitotic cell cycle / nucleosome / double-strand break repair / nucleosome assembly / chromatin organization / histone binding / DNA helicase / sequence-specific DNA binding / DNA-binding transcription factor activity, RNA polymerase II-specific / chromatin remodeling / protein heterodimerization activity / RNA polymerase II cis-regulatory region sequence-specific DNA binding / chromatin binding / regulation of DNA-templated transcription / chromatin / regulation of transcription by RNA polymerase II / positive regulation of DNA-templated transcription / structural molecule activity / positive regulation of transcription by RNA polymerase II / ATP hydrolysis activity / DNA binding / zinc ion binding / nucleoplasm / ATP binding / nucleus
Similarity search - Function
: / Rsc1/Rsc2, bromodomain / : / Rsc8/Ssr1/Ssr2, zinc finger, ZZ-type / : / 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 ...: / Rsc1/Rsc2, bromodomain / : / Rsc8/Ssr1/Ssr2, zinc finger, ZZ-type / : / 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. / : / SNF2-like, N-terminal domain superfamily / Myb-like DNA-binding domain / SNF2, N-terminal / SNF2-related domain / SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains / SANT/Myb domain / Actin / Actin family / Actin / Histone H2B signature. / Histone H2B / Histone H2B / Histone H2A conserved site / Histone H2A signature. / Histone H2A, C-terminal domain / C-terminus of histone H2A / Histone H4, conserved site / Histone H4 signature. / Histone H4 / Histone H4 / Histone H2A / Histone 2A / CENP-T/Histone H4, histone fold / Centromere kinetochore component CENP-T histone fold / TATA box binding protein associated factor / TATA box binding protein associated factor (TAF), histone-like fold domain / Histone H3 signature 1. / Helicase conserved C-terminal domain / Histone H3 signature 2. / Histone H3 / Histone H3/CENP-A / Homeobox-like domain superfamily / ATPase, nucleotide binding domain / Histone H2A/H2B/H3 / Core histone H2A/H2B/H3/H4 / Histone-fold / Bromodomain, conserved site / Bromodomain signature. / 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 / Helicase superfamily 1/2, ATP-binding domain / Winged helix-like DNA-binding domain superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Histone H4 / Histone H2B 1.1 / Histone H2A type 1 / Chromatin structure-remodeling complex protein RSC6 / Nuclear protein STH1/NPS1 / Chromatin structure-remodeling complex subunit RSC7 / Chromatin structure-remodeling complex protein RSC30 / Chromatin structure-remodeling complex protein RSC8 / Regulator of Ty1 transposition protein 102 / Histone H4 ...Histone H4 / Histone H2B 1.1 / Histone H2A type 1 / Chromatin structure-remodeling complex protein RSC6 / Nuclear protein STH1/NPS1 / Chromatin structure-remodeling complex subunit RSC7 / Chromatin structure-remodeling complex protein RSC30 / Chromatin structure-remodeling complex protein RSC8 / Regulator of Ty1 transposition protein 102 / Histone H4 / Histone H3.2 / 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 / Histone H2A / High temperature lethal protein 1
Similarity search - Component
Biological speciesSaccharomyces cerevisiae S288c (yeast) / Xenopus laevis (African clawed frog) / Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast) / Homo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 7.13 Å
AuthorsYe YP / Wu H
CitationJournal: Science / Year: 2019
Title: Structure of the RSC complex bound to the nucleosome.
Authors: Youpi Ye / Hao Wu / Kangjing Chen / Cedric R Clapier / Naveen Verma / Wenhao Zhang / Haiteng Deng / Bradley R Cairns / Ning Gao / Zhucheng Chen /
Abstract: The RSC complex remodels chromatin structure and regulates gene transcription. We used cryo-electron microscopy to determine the structure of yeast RSC bound to the nucleosome. RSC is delineated into ...The RSC complex remodels chromatin structure and regulates gene transcription. We used cryo-electron microscopy to determine the structure of yeast RSC bound to the nucleosome. RSC is delineated into the adenosine triphosphatase motor, the actin-related protein module, and the substrate recruitment module (SRM). RSC binds the nucleosome mainly through the motor, with the auxiliary subunit Sfh1 engaging the H2A-H2B acidic patch to enable nucleosome ejection. SRM is organized into three substrate-binding lobes poised to bind their respective nucleosomal epitopes. The relative orientations of the SRM and the motor on the nucleosome explain the directionality of DNA translocation and promoter nucleosome repositioning by RSC. Our findings shed light on RSC assembly and functionality, and they provide a framework to understand the mammalian homologs BAF/PBAF and the Sfh1 ortholog INI1/BAF47, which are frequently mutated in cancers.
History
DepositionSep 5, 2019-
Header (metadata) releaseNov 13, 2019-
Map releaseNov 13, 2019-
UpdateMar 27, 2024-
Current statusMar 27, 2024Processing site: PDBj / Status: Released

-
Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.025
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by radius
  • Surface level: 0.025
  • Imaged by UCSF Chimera
  • Download
  • Surface view with fitted model
  • Atomic models: PDB-6kw3
  • Surface level: 0.025
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_0777.png

Downloads & links

-
Map

FileDownload / File: emd_0777.map.gz / Format: CCP4 / Size: 22.2 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationThe ClassA RSC-Nucleosome Complex
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
2.14 Å/pix.
x 180 pix.
= 385.2 Å		2.14 Å/pix.
x 180 pix.
= 385.2 Å		2.14 Å/pix.
x 180 pix.
= 385.2 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 2.14 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.025 / Movie #1: 0.025
Minimum - Maximum-0.01342345 - 0.11891705
Average (Standard dev.)0.0012106178 (±0.005624704)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions180180180
Spacing180180180
CellA=B=C: 385.2 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z2.142.142.14
M x/y/z180180180
origin x/y/z0.0000.0000.000
length x/y/z385.200385.200385.200
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS180180180
D min/max/mean-0.0130.1190.001

-
Supplemental data

-
Sample components

+
Entire : RSC

EntireName: RSC
Components
  • Complex: RSC
    • Protein or peptide: Histone H4
    • Protein or peptide: Histone H3.2
    • Protein or peptide: Histone H2A
    • DNA: DNA 167
    • DNA: DNA 167
    • Protein or peptide: Nuclear protein STH1/NPS1
    • Protein or peptide: Actin-related protein 7
    • Protein or peptide: Regulator of Ty1 transposition protein 102
    • Protein or peptide: Chromatin structure-remodeling complex subunit RSC7
    • Protein or peptide: Chromatin structure-remodeling complex protein RSC8
    • Protein or peptide: Chromatin structure-remodeling complex subunit RSC9
    • Protein or peptide: Chromatin structure-remodeling complex protein RSC6
    • Protein or peptide: Chromatin structure-remodeling complex subunit SFH1
    • Protein or peptide: Chromatin structure-remodeling complex protein RSC58
    • Protein or peptide: High temperature lethal protein 1
    • Protein or peptide: Chromatin structure-remodeling complex protein RSC30
    • 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 subunit RSC2
    • Protein or peptide: Histone H4
    • Protein or peptide: Actin-like protein ARP9
  • Ligand: ZINC ION

+
Supramolecule #1: RSC

SupramoleculeName: RSC / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#21
Source (natural)Organism: Saccharomyces cerevisiae S288c (yeast)

+
Macromolecule #1: Histone H4

MacromoleculeName: Histone H4 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Xenopus laevis (African clawed frog)
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

+
Macromolecule #2: Histone H3.2

MacromoleculeName: Histone H3.2 / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Xenopus laevis (African clawed frog)
Molecular weightTheoretical: 15.421101 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSA VMALQEASEA YLVGLFEDTN LCAIHAKRVT IMPKDIQLAR RIRGERA

UniProtKB: Histone H3.2

+
Macromolecule #3: Histone H2A

MacromoleculeName: Histone H2A / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Xenopus laevis (African clawed frog)
Molecular weightTheoretical: 14.109436 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MSGRGKQGGK TRAKAKTRSS RAGLQFPVGR VHRLLRKGNY AERVGAGAPV YLAAVLEYLT AEILELAGNA ARDNKKTRII PRHLQLAVR NDEELNKLLG RVTIAQGGVL PNIQSVLLPK KTESSKSAKS K

UniProtKB: Histone H2A

+
Macromolecule #6: Nuclear protein STH1/NPS1

MacromoleculeName: Nuclear protein STH1/NPS1 / type: protein_or_peptide / ID: 6 / Number of copies: 3 / 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

+
Macromolecule #7: Actin-related protein 7

MacromoleculeName: Actin-related protein 7 / 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: 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

+
Macromolecule #8: Regulator of Ty1 transposition protein 102

MacromoleculeName: Regulator of Ty1 transposition protein 102 / 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: 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

+
Macromolecule #9: Chromatin structure-remodeling complex subunit RSC7

MacromoleculeName: Chromatin structure-remodeling complex subunit RSC7 / 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: 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

+
Macromolecule #10: Chromatin structure-remodeling complex protein RSC8

MacromoleculeName: Chromatin structure-remodeling complex protein RSC8 / type: protein_or_peptide / ID: 10 / Number of copies: 2 / 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

+
Macromolecule #11: Chromatin structure-remodeling complex subunit RSC9

MacromoleculeName: Chromatin structure-remodeling complex subunit RSC9 / type: protein_or_peptide / ID: 11 / 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

+
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

+
Macromolecule #13: Chromatin structure-remodeling complex subunit SFH1

MacromoleculeName: Chromatin structure-remodeling complex subunit SFH1 / 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: 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

+
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

+
Macromolecule #15: High temperature lethal protein 1

MacromoleculeName: High temperature lethal protein 1 / 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: 9.192524 KDa
SequenceString:
MSQNNTISSM NPERAYNNVT LKNLTAFQLL SQRENICELL NLVESTERHN SIINPERQRM SLEEMKKMLD ALKNERKK

UniProtKB: High temperature lethal protein 1

+
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

+
Macromolecule #17: Chromatin structure-remodeling complex protein RSC3

MacromoleculeName: Chromatin structure-remodeling complex protein RSC3 / 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: 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

+
Macromolecule #18: Chromatin structure-remodeling complex subunit RSC4

MacromoleculeName: Chromatin structure-remodeling complex subunit RSC4 / type: protein_or_peptide / ID: 18 / 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

+
Macromolecule #19: Chromatin structure-remodeling complex subunit RSC2

MacromoleculeName: Chromatin structure-remodeling complex subunit RSC2 / 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: 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

+
Macromolecule #20: Histone H4

MacromoleculeName: Histone H4 / type: protein_or_peptide / ID: 20 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Xenopus laevis (African clawed frog)
Molecular weightTheoretical: 13.925202 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MPDPAKSAPA AKKGSKKAVT KTQKKDGKKR RKSRKESYAI YVYKVLKQVH PDTGISSKAM SIMNSFVNDV FERIAGEASR LAHYNKRST ITSREIQTAV RLLLPGELAK HAVSEGTKAV TKYTSAK

UniProtKB: Histone H4

+
Macromolecule #21: Actin-like protein ARP9

MacromoleculeName: Actin-like protein ARP9 / 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: 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

+
Macromolecule #4: DNA 167

MacromoleculeName: DNA 167 / type: dna / ID: 4 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 51.421781 KDa
SequenceString: (DG)(DA)(DT)(DG)(DA)(DG)(DA)(DA)(DT)(DC) (DC)(DC)(DG)(DG)(DT)(DG)(DC)(DC)(DG)(DA) (DG)(DG)(DC)(DC)(DG)(DC)(DT)(DC)(DA) (DA)(DT)(DT)(DG)(DG)(DT)(DC)(DG)(DT)(DA) (DG) (DA)(DC)(DA)(DG)(DC)(DT) ...String:
(DG)(DA)(DT)(DG)(DA)(DG)(DA)(DA)(DT)(DC) (DC)(DC)(DG)(DG)(DT)(DG)(DC)(DC)(DG)(DA) (DG)(DG)(DC)(DC)(DG)(DC)(DT)(DC)(DA) (DA)(DT)(DT)(DG)(DG)(DT)(DC)(DG)(DT)(DA) (DG) (DA)(DC)(DA)(DG)(DC)(DT)(DC)(DT) (DA)(DG)(DC)(DA)(DC)(DC)(DG)(DC)(DT)(DT) (DA)(DA) (DA)(DC)(DG)(DC)(DA)(DC)(DG) (DT)(DA)(DC)(DG)(DC)(DG)(DC)(DT)(DG)(DT) (DC)(DC)(DC) (DC)(DC)(DG)(DC)(DG)(DT) (DT)(DT)(DT)(DA)(DA)(DC)(DC)(DG)(DC)(DC) (DA)(DA)(DG)(DG) (DG)(DG)(DA)(DT)(DT) (DA)(DC)(DT)(DC)(DC)(DC)(DT)(DA)(DG)(DT) (DC)(DT)(DC)(DC)(DA) (DG)(DG)(DC)(DA) (DC)(DG)(DT)(DG)(DT)(DC)(DA)(DG)(DA)(DT) (DA)(DT)(DA)(DT)(DA)(DC) (DA)(DT)(DC) (DC)(DT)(DG)(DA)(DA)(DG)(DC)(DT)(DT)(DG) (DT)(DC)(DG)(DA)(DG)(DA)(DA) (DG)(DT) (DA)(DC)(DT)(DA)(DG)

+
Macromolecule #5: DNA 167

MacromoleculeName: DNA 167 / type: dna / ID: 5 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 51.683922 KDa
SequenceString: (DC)(DT)(DA)(DG)(DT)(DA)(DC)(DT)(DT)(DC) (DT)(DC)(DG)(DA)(DC)(DA)(DA)(DG)(DC)(DT) (DT)(DC)(DA)(DG)(DG)(DA)(DT)(DG)(DT) (DA)(DT)(DA)(DT)(DA)(DT)(DC)(DT)(DG)(DA) (DC) (DA)(DC)(DG)(DT)(DG)(DC) ...String:
(DC)(DT)(DA)(DG)(DT)(DA)(DC)(DT)(DT)(DC) (DT)(DC)(DG)(DA)(DC)(DA)(DA)(DG)(DC)(DT) (DT)(DC)(DA)(DG)(DG)(DA)(DT)(DG)(DT) (DA)(DT)(DA)(DT)(DA)(DT)(DC)(DT)(DG)(DA) (DC) (DA)(DC)(DG)(DT)(DG)(DC)(DC)(DT) (DG)(DG)(DA)(DG)(DA)(DC)(DT)(DA)(DG)(DG) (DG)(DA) (DG)(DT)(DA)(DA)(DT)(DC)(DC) (DC)(DC)(DT)(DT)(DG)(DG)(DC)(DG)(DG)(DT) (DT)(DA)(DA) (DA)(DA)(DC)(DG)(DC)(DG) (DG)(DG)(DG)(DG)(DA)(DC)(DA)(DG)(DC)(DG) (DC)(DG)(DT)(DA) (DC)(DG)(DT)(DG)(DC) (DG)(DT)(DT)(DT)(DA)(DA)(DG)(DC)(DG)(DG) (DT)(DG)(DC)(DT)(DA) (DG)(DA)(DG)(DC) (DT)(DG)(DT)(DC)(DT)(DA)(DC)(DG)(DA)(DC) (DC)(DA)(DA)(DT)(DT)(DG) (DA)(DG)(DC) (DG)(DG)(DC)(DC)(DT)(DC)(DG)(DG)(DC)(DA) (DC)(DC)(DG)(DG)(DG)(DA)(DT) (DT)(DC) (DT)(DC)(DA)(DT)(DC)

+
Macromolecule #22: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 22 / Number of copies: 1 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation statecell

-
Sample preparation

BufferpH: 7.5
VitrificationCryogen name: ETHANE

-
Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K2 QUANTUM (4k x 4k) / Average electron dose: 2.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: SPOT SCAN / Imaging mode: DARK FIELD
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

-
Image processing

Startup modelType of model: EMDB MAP
Final reconstructionResolution.type: BY AUTHOR / Resolution: 7.13 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 45077
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

+
About Yorodumi

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242)：Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

Read more