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- EMDB-64578: local ARP-NCP structure of the ncBAF-nucleosome complex in the ap... -

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Basic information

Entry
Database: EMDB / ID: EMD-64578
Titlelocal ARP-NCP structure of the ncBAF-nucleosome complex in the apo state
Map data
Sample
  • Complex: ncBAF-nucleosome complex
    • Protein or peptide: Histone H3
    • Protein or peptide: Histone H4
    • Protein or peptide: Histone H2A
    • Protein or peptide: Histone H2B
    • Protein or peptide: Actin, cytoplasmic 1, N-terminally processed
    • Protein or peptide: Actin-like protein 6A
    • Protein or peptide: SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
    • Protein or peptide: B-cell CLL/lymphoma 7 protein family member B
    • DNA: DNA (167-MER)
    • DNA: DNA (167-MER)
KeywordsChromatin remodeling / SWI/SNF / Epigenetics / GENE REGULATION/DNA / GENE REGULATION-DNA complex
Function / homology
Function and homology information


positive regulation of glucose mediated signaling pathway / regulation of DNA strand elongation / positive regulation of telomere maintenance in response to DNA damage / positive regulation of norepinephrine uptake / positive regulation of transcription of nucleolar large rRNA by RNA polymerase I / bBAF complex / Formation of the embryonic stem cell BAF (esBAF) complex / cellular response to cytochalasin B / neural retina development / npBAF complex ...positive regulation of glucose mediated signaling pathway / regulation of DNA strand elongation / positive regulation of telomere maintenance in response to DNA damage / positive regulation of norepinephrine uptake / positive regulation of transcription of nucleolar large rRNA by RNA polymerase I / bBAF complex / Formation of the embryonic stem cell BAF (esBAF) complex / cellular response to cytochalasin B / neural retina development / npBAF complex / brahma complex / nBAF complex / Formation of the canonical BAF (cBAF) complex / negative regulation of androgen receptor signaling pathway / regulation of transepithelial transport / EGR2 and SOX10-mediated initiation of Schwann cell myelination / Formation of neuronal progenitor and neuronal BAF (npBAF and nBAF) / morphogenesis of a polarized epithelium / Formation of the polybromo-BAF (pBAF) complex / structural constituent of postsynaptic actin cytoskeleton / Formation of annular gap junctions / Formation of the dystrophin-glycoprotein complex (DGC) / Gap junction degradation / Formation of the non-canonical BAF (ncBAF) complex / GBAF complex / protein localization to adherens junction / regulation of G0 to G1 transition / Cell-extracellular matrix interactions / dense body / Folding of actin by CCT/TriC / Tat protein binding / nucleosome array spacer activity / RNA polymerase I preinitiation complex assembly / postsynaptic actin cytoskeleton / Ino80 complex / RSC-type complex / blastocyst formation / Regulation of CDH1 Function / host-mediated activation of viral transcription / regulation of double-strand break repair / regulation of nucleotide-excision repair / Prefoldin mediated transfer of substrate to CCT/TriC / Adherens junctions interactions / RHOF GTPase cycle / adherens junction assembly / nucleosome disassembly / apical protein localization / Sensory processing of sound by outer hair cells of the cochlea / ATP-dependent chromatin remodeler activity / Interaction between L1 and Ankyrins / SWI/SNF complex / regulation of mitotic metaphase/anaphase transition / tight junction / Sensory processing of sound by inner hair cells of the cochlea / positive regulation of T cell differentiation / nuclear androgen receptor binding / apical junction complex / positive regulation of double-strand break repair / spinal cord development / regulation of chromosome organization / maintenance of blood-brain barrier / regulation of norepinephrine uptake / transporter regulator activity / positive regulation of stem cell population maintenance / NuA4 histone acetyltransferase complex / RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known / establishment or maintenance of cell polarity / Recycling pathway of L1 / cortical cytoskeleton / Regulation of MITF-M-dependent genes involved in pigmentation / regulation of DNA replication / nitric-oxide synthase binding / regulation of embryonic development / brush border / regulation of G1/S transition of mitotic cell cycle / EPH-ephrin mediated repulsion of cells / negative regulation of cell differentiation / RHO GTPases Activate WASPs and WAVEs / regulation of synaptic vesicle endocytosis / positive regulation of myoblast differentiation / positive regulation of signal transduction by p53 class mediator / kinesin binding / ATP-dependent activity, acting on DNA / regulation of DNA repair / positive regulation of Wnt signaling pathway / RHO GTPases activate IQGAPs / regulation of protein localization to plasma membrane / positive regulation of double-strand break repair via homologous recombination / Chromatin modifying enzymes / DNA polymerase binding / EPHB-mediated forward signaling / cytoskeleton organization / axonogenesis / substantia nigra development / Interleukin-7 signaling / telomere maintenance / calyx of Held / transcription initiation-coupled chromatin remodeling / nitric-oxide synthase regulator activity / positive regulation of DNA repair
Similarity search - Function
BCL7 / BCL7, N-terminal conserver region / SWI/SNF complex subunit BRG1 / BRK domain / BRK domain / BRK domain superfamily / domain in transcription and CHROMO domain helicases / Glutamine-Leucine-Glutamine, QLQ / QLQ / QLQ domain profile. ...BCL7 / BCL7, N-terminal conserver region / SWI/SNF complex subunit BRG1 / BRK domain / BRK domain / BRK domain superfamily / domain in transcription and CHROMO domain helicases / Glutamine-Leucine-Glutamine, QLQ / QLQ / QLQ domain profile. / QLQ / Snf2-ATP coupling, chromatin remodelling complex / Snf2, ATP coupling domain / Snf2-ATP coupling, chromatin remodelling complex / domain in helicases and associated with SANT domains / HSA domain / Helicase/SANT-associated domain / HSA domain profile. / : / SNF2-like, N-terminal domain superfamily / SNF2, N-terminal / SNF2-related 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 / : / Histone H2A conserved site / Histone H2A signature. / Histone H2B signature. / Histone H2B / Histone H2B / Histone H2A, C-terminal domain / C-terminus of histone H2A / Histone 2A / Histone H2A / 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. / Histone H3 signature 2. / ATPase, nucleotide binding domain / Histone H3 / Histone H3/CENP-A / Bromodomain, conserved site / Bromodomain signature. / Histone H2A/H2B/H3 / Core histone H2A/H2B/H3/H4 domain / Bromodomain / bromo domain / Bromodomain / Bromodomain (BrD) profile. / Bromodomain-like superfamily / Histone-fold / 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 / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Histone H3 / Histone H2B / Actin-like protein 6A / SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4 / Actin, cytoplasmic 1 / Histone H4 / Histone H2A / B-cell CLL/lymphoma 7 protein family member B
Similarity search - Component
Biological speciesHomo sapiens (human) / Xenopus laevis (African clawed frog) / artificial sequences (others)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.28 Å
AuthorsSun F / Zou B / Li H / Xu C / Luo Q / Wang C / Xu P / Pei D / Chen J / Qin D ...Sun F / Zou B / Li H / Xu C / Luo Q / Wang C / Xu P / Pei D / Chen J / Qin D / Zhang Y / He J
Funding support China, 6 items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)32361163669 China
Other government2023M743512 China
National Natural Science Foundation of China (NSFC)32170189 China
National Natural Science Foundation of China (NSFC)32241021 China
Other governmentGZC20232691 China
Other government2023A1515110923 China
CitationJournal: Nucleic Acids Res / Year: 2026
Title: Structural basis for BCL7B-mediated ncBAF-nucleosome engagement.
Authors: Fahui Sun / Binqian Zou / He Li / Chongshen Xu / Qiaohong Luo / Chi Wang / Pengqi Xu / Duanqing Pei / Jiekai Chen / Dajiang Qin / Ying Zhang / Jun He /
Abstract: The mammalian SWI/SNF family of chromatin remodelers comprises BRG1/BRM-associated factor (cBAF), polybromo-associated BAF (PBAF), and non-canonical BAF (ncBAF) complexes, which slide and disassemble ...The mammalian SWI/SNF family of chromatin remodelers comprises BRG1/BRM-associated factor (cBAF), polybromo-associated BAF (PBAF), and non-canonical BAF (ncBAF) complexes, which slide and disassemble nucleosomes to regulate gene expression and chromatin structure dependent on ATP hydrolysis energy. While the chromatin engagement mechanisms of cBAF and PBAF have been structurally resolved, the molecular architecture governing ncBAF interaction with chromatin remains elusive. In this study, by integrating cryo-electron microscopy, biochemical assays, and cross-linking mass spectrometry, we resolved the conformational transition of ncBAF-nucleosome complexes from nucleotide-free to nucleotide-bound states. Our analyses establish BCL7 proteins as dynamic molecular tethers connecting the ARP module to the nucleosomal acidic patch and demonstrate that BCL7B promotes ncBAF-mediated nucleosome remodeling, with BRG1-catalyzed ATP hydrolysis triggering conformational changes that modulate BCL7-mediated histone association. Structurally and biochemically, we further demonstrate that β-actin within the BCL7-containing ARP module retains ATP hydrolysis activity, rendering its exposed pointed end structurally compatible with incorporation into the barbed end of nuclear actin filaments, which provides a potential molecular basis for coordinating nuclear actin networks with chromatin remodeling. Collectively, our findings unravel a dynamic role of BCL7 in regulating ncBAF-mediated chromatin remodeling and establish a distinct chromatin engagement mode of ncBAF from that of cBAF/PBAF.
History
DepositionMay 13, 2025-
Header (metadata) releaseMay 6, 2026-
Map releaseMay 6, 2026-
UpdateMay 6, 2026-
Current statusMay 6, 2026Processing site: PDBc / Status: Released

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Structure visualization

Supplemental images

emd_64578.png

Downloads & links

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Map

FileDownload / File: emd_64578.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.93 Å/pix.
x 360 pix.
= 334.8 Å		0.93 Å/pix.
x 360 pix.
= 334.8 Å		0.93 Å/pix.
x 360 pix.
= 334.8 Å

Surface

Projections

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Images are generated by Spider.

Voxel sizeX=Y=Z: 0.93 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.136
Minimum - Maximum-0.13358864 - 0.89979625
Average (Standard dev.)0.006628568 (±0.020904621)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions360360360
Spacing360360360
CellA=B=C: 334.8 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_64578_msk_1.map
Projections & Slices
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Half map: #2

Fileemd_64578_half_map_1.map
Projections & Slices
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Half map: #1

Fileemd_64578_half_map_2.map
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Sample components

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Entire : ncBAF-nucleosome complex

EntireName: ncBAF-nucleosome complex
Components
  • Complex: ncBAF-nucleosome complex
    • Protein or peptide: Histone H3
    • Protein or peptide: Histone H4
    • Protein or peptide: Histone H2A
    • Protein or peptide: Histone H2B
    • Protein or peptide: Actin, cytoplasmic 1, N-terminally processed
    • Protein or peptide: Actin-like protein 6A
    • Protein or peptide: SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
    • Protein or peptide: B-cell CLL/lymphoma 7 protein family member B
    • DNA: DNA (167-MER)
    • DNA: DNA (167-MER)

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Supramolecule #1: ncBAF-nucleosome complex

SupramoleculeName: ncBAF-nucleosome complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 873 KDa

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Macromolecule #1: Histone H3

MacromoleculeName: Histone H3 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Xenopus laevis (African clawed frog)
Molecular weightTheoretical: 15.30393 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
ARTKQTARKS TGGKAPRKQL ATKAARKSAP ATGGVKKPHR YRPGTVALRE IRRYQKSTEL LIRKLPFQRL VREIAQDFKT DLRFQSSAV MALQEASEAY LVALFEDTNL CAIHAKRVTI MPKDIQLARR IRGERA

UniProtKB: Histone H3

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Macromolecule #2: Histone H4

MacromoleculeName: Histone H4 / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Xenopus laevis (African clawed frog)
Molecular weightTheoretical: 11.263231 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
SGRGKGGKGL GKGGAKRHRK VLRDNIQGIT KPAIRRLARR GGVKRISGLI YEETRGVLKV FLENVIRDAV TYTEHAKRKT VTAMDVVYA LKRQGRTLYG FGG

UniProtKB: Histone H4

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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: 14.163421 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
NASGRGKQGG KTRAKAKTRS SRAGLQFPVG RVHRLLRKGN YAERVGAGAP VYLAAVLEYL TAEILELAGN AARDNKKTRI IPRHLQLAV RNDEELNKLL GRVTIAQGGV LPNIQSVLLP KKTESSKSAK SK

UniProtKB: Histone H2A

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Macromolecule #4: Histone H2B

MacromoleculeName: Histone H2B / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Xenopus laevis (African clawed frog)
Molecular weightTheoretical: 13.524752 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
AKSAPAPKKG SKKAVTKTQK KDGKKRRKTR KESYAIYVYK VLKQVHPDTG ISSKAMSIMN SFVNDVFERI AGEASRLAHY NKRSTITSR EIQTAVRLLL PGELAKHAVS EGTKAVTKYT SAK

UniProtKB: Histone H2B

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Macromolecule #5: Actin, cytoplasmic 1, N-terminally processed

MacromoleculeName: Actin, cytoplasmic 1, N-terminally processed / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 41.853738 KDa
Recombinant expressionOrganism: Mammalia (mammals)
SequenceString: MADDDIAALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ SKRGILTLKY PIEHGIVTNW DDMEKIWHH TFYNELRVAP EEHPVLLTEA PLNPKANREK MTQIMFETFN TPAMYVAIQA VLSLYASGRT TGIVMDSGDG V THTVPIYE ...String:
MADDDIAALV VDNGSGMCKA GFAGDDAPRA VFPSIVGRPR HQGVMVGMGQ KDSYVGDEAQ SKRGILTLKY PIEHGIVTNW DDMEKIWHH TFYNELRVAP EEHPVLLTEA PLNPKANREK MTQIMFETFN TPAMYVAIQA VLSLYASGRT TGIVMDSGDG V THTVPIYE GYALPHAILR LDLAGRDLTD YLMKILTERG YSFTTTAERE IVRDIKEKLC YVALDFEQEM ATAASSSSLE KS YELPDGQ VITIGNERFR CPEALFQPSF LGMESCGIHE TTFNSIMKCD VDIRKDLYAN TVLSGGTTMY PGIADRMQKE ITA LAPSTM KIKIIAPPER KYSVWIGGSI LASLSTFQQM WISKQEYDES GPSIVHRKCF

UniProtKB: Actin, cytoplasmic 1

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Macromolecule #6: Actin-like protein 6A

MacromoleculeName: Actin-like protein 6A / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 46.663742 KDa
Recombinant expressionOrganism: Mammalia (mammals)
SequenceString: SGGVYGGDEV GALVFDIGSY TVRAGYAGED CPKVDFPTAI GMVVERDDGS TLMEIDGDKG KQGGPTYYID TNALRVPREN MEAISPLKN GMVEDWDSFQ AILDHTYKMH VKSEASLHPV LMSEAPWNTR AKREKLTELM FEHYNIPAFF LCKTAVLTAF A NGRSTGLI ...String:
SGGVYGGDEV GALVFDIGSY TVRAGYAGED CPKVDFPTAI GMVVERDDGS TLMEIDGDKG KQGGPTYYID TNALRVPREN MEAISPLKN GMVEDWDSFQ AILDHTYKMH VKSEASLHPV LMSEAPWNTR AKREKLTELM FEHYNIPAFF LCKTAVLTAF A NGRSTGLI LDSGATHTTA IPVHDGYVLQ QGIVKSPLAG DFITMQCREL FQEMNIELVP PYMIASKEAV REGSPANWKR KE KLPQVTR SWHNYMCNCV IQDFQASVLQ VSDSTYDEQV AAQMPTVHYE FPNGYNCDFG AERLKIPEGL FDPSNVKGLS GNT MLGVSH VVTTSVGMCD IDIRPGLYGS VIVAGGNTLI QSFTDRLNRE LSQKTPPSMR LKLIANNTTV ERRFSSWIGG SILA SLGTF QQMWISKQEY EEGGKQC

UniProtKB: Actin-like protein 6A

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Macromolecule #7: SWI/SNF-related matrix-associated actin-dependent regulator of ch...

MacromoleculeName: SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4
type: protein_or_peptide / ID: 7 / 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: Homo sapiens (human)
Molecular weightTheoretical: 184.934828 KDa
Recombinant expressionOrganism: Mammalia (mammals)
SequenceString: MASTPDPPLG GTPRPGPSPG PGPSPGAMLG PSPGPSPGSA HSMMGPSPGP PSAGHPIPTQ GPGGYPQDNM HQMHKPMESM HEKGMSDDP RYNQMKGMGM RSGGHAGMGP PPSPMDQHSQ GYPSPLGGSE HASSPVPASG PSSGPQMSSG PGGAPLDGAD P QALGQQNR ...String:
MASTPDPPLG GTPRPGPSPG PGPSPGAMLG PSPGPSPGSA HSMMGPSPGP PSAGHPIPTQ GPGGYPQDNM HQMHKPMESM HEKGMSDDP RYNQMKGMGM RSGGHAGMGP PPSPMDQHSQ GYPSPLGGSE HASSPVPASG PSSGPQMSSG PGGAPLDGAD P QALGQQNR GPTPFNQNQL HQLRAQIMAY KMLARGQPLP DHLQMAVQGK RPMPGMQQQM PTLPPPSVSA TGPGPGPGPG PG PGPGPAP PNYSRPHGMG GPNMPPPGPS GVPPGMPGQP PGGPPKPWPE GPMANAAAPT STPQKLIPPQ PTGRPSPAPP AVP PAASPV MPPQTQSPGQ PAQPAPMVPL HQKQSRITPI QKPRGLDPVE ILQEREYRLQ ARIAHRIQEL ENLPGSLAGD LRTK ATIEL KALRLLNFQR QLRQEVVVCM RRDTALETAL NAKAYKRSKR QSLREARITE KLEKQQKIEQ ERKRRQKHQE YLNSI LQHA KDFKEYHRSV TGKIQKLTKA VATYHANTER EQKKENERIE KERMRRLMAE DEEGYRKLID QKKDKRLAYL LQQTDE YVA NLTELVPQHK AAQVAKEKKK KKKKKKAENA EGQTPAIGPD GEPLDETSQM SDLPVKVIHV ESGKILTGTD APKAGQL EA WLEMNPGYEV APRSDSEESG SEEEEEEEEE EQPQAAQPPT LPVEEKKKIP DPDSDDVSEV DARHIIENAK QDVDDEYG V SQALARGLQS YYAVAHAVTE RVDKQSALMV NGVLKQYQIK GLEWLVSLYN NNLNGILADE MGLGKTIQTI ALITYLMEH KRINGPFLII VPLSTLSNWA YEFDKWAPSV VKVSYKGSPA ARRAFVPQLR SGKFNVLLTT YEYIIKDKHI LAKIRWKYMI VDEGHRMKN HHCKLTQVLN THYVAPRRLL LTGTPLQNKL PELWALLNFL LPTIFKSCST FEQWFNAPFA MTGEKVDLNE E ETILIIRR LHKVLRPFLL RRLKKEVEAQ LPEKVEYVIK CDMSALQRVL YRHMQAKGVL LTDGSEKDKK GKGGTKTLMN TI MQLRKIC NHPYMFQHIE ESFSEHLGFT GGIVQGLDLY RASGKFELLD RILPKLRATN HKVLLFCQMT SLMTIMEDYF AYR GFKYLR LDGTTKAEDR GMLLKTFNEP GSEYFIFLLS TRAGGLGLNL QSADTVIIFD SDWNPHQDLQ AQDRAHRIGQ QNEV RVLRL CTVNSVEEKI LAAAKYKLNV DQKVIQAGMF DQKSSSHERR AFLQAILEHE EQDESRHCST GSGSASFAHT APPPA GVNP DLEEPPLKEE DEVPDDETVN QMIARHEEEF DLFMRMDLDR RREEARNPKR KPRLMEEDEL PSWIIKDDAE VERLTC EEE EEKMFGRGSR HRKEVDYSDS LTEKQWLKAI EEGTLEEIEE EVRQKKSSRK RKRDSDAGSS TPTTSTRSRD KDDESKK QK KRGRPPAEKL SPNPPNLTKK MKKIVDAVIK YKDSSSGRQL SEVFIQLPSR KELPEYYELI RKPVDFKKIK ERIRNHKY R SLNDLEKDVM LLCQNAQTFN LEGSLIYEDS IVLQSVFTSV RQKIEKEDDS EGEESEEEEE GEEEGSESES RSVKVKIKL GRKEKAQDRL KGGRRRPSRG SRAKPVVSDD DSEEEQEEDR SGSGSEED

UniProtKB: SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4

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Macromolecule #8: B-cell CLL/lymphoma 7 protein family member B

MacromoleculeName: B-cell CLL/lymphoma 7 protein family member B / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 22.291344 KDa
Recombinant expressionOrganism: Mammalia (mammals)
SequenceString: MASGRSVRAE TRSRAKDDIK KVMAAIEKVR KWEKKWVTVG DTSLRIFKWV PVTDSKEKEK SKSNSSAARE PNGFPSDASA NSSLLLEFQ DENSNQSSVS DVYQLKVDSS TNSSPSPQQS ESLSPAHTSD FRTDDSQPPT LGQEILEEPS LPSSEVADEP P TLTKEEPV ...String:
MASGRSVRAE TRSRAKDDIK KVMAAIEKVR KWEKKWVTVG DTSLRIFKWV PVTDSKEKEK SKSNSSAARE PNGFPSDASA NSSLLLEFQ DENSNQSSVS DVYQLKVDSS TNSSPSPQQS ESLSPAHTSD FRTDDSQPPT LGQEILEEPS LPSSEVADEP P TLTKEEPV PLETQVVEEE EDSGAPPLKR FCVDQPTVPQ TASES

UniProtKB: B-cell CLL/lymphoma 7 protein family member B

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Macromolecule #9: DNA (167-MER)

MacromoleculeName: DNA (167-MER) / type: dna / ID: 9 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: artificial sequences (others)
Molecular weightTheoretical: 51.840988 KDa
SequenceString: (DG)(DC)(DG)(DG)(DT)(DG)(DG)(DC)(DG)(DG) (DC)(DC)(DG)(DC)(DT)(DC)(DT)(DA)(DG)(DA) (DA)(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:
(DG)(DC)(DG)(DG)(DT)(DG)(DG)(DC)(DG)(DG) (DC)(DC)(DG)(DC)(DT)(DC)(DT)(DA)(DG)(DA) (DA)(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)(DC)(DA)(DG)

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Macromolecule #10: DNA (167-MER)

MacromoleculeName: DNA (167-MER) / type: dna / ID: 10 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: artificial sequences (others)
Molecular weightTheoretical: 51.271625 KDa
SequenceString: (DC)(DT)(DG)(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:
(DC)(DT)(DG)(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)(DT)(DT)(DC)(DT)(DA)(DG)(DA) (DG)(DC)(DG)(DG)(DC)(DC)(DG) (DC)(DC) (DA)(DC)(DC)(DG)(DC)

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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: 7.5
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.4 µm / Nominal defocus min: 0.8 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.28 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 253908
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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