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- EMDB-54056: Structure of BAF in complex with OCT4-SOX2-bound nucleosome - SHL... -

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Basic information

Entry
Database: EMDB / ID: EMD-54056
TitleStructure of BAF in complex with OCT4-SOX2-bound nucleosome - SHL+6 class 1
Map dataAmplitude-scaled map (LocScale).
Sample
  • Complex: BAF in complex with a OCT4/SOX2-bound nucleosome
    • Complex: Nucleosome core particle
      • Protein or peptide: x 6 types
    • Complex: BAF complex
      • Protein or peptide: x 9 types
      • DNA: x 1 types
    • Complex: OCT4/SOX2 heterodimer
      • DNA: x 1 types
  • Ligand: x 1 types
KeywordsChromatin / remodeler / GENE REGULATION
Function / homology
Function and homology information


negative regulation of myeloid progenitor cell differentiation / glial cell fate commitment / single stranded viral RNA replication via double stranded DNA intermediate / Formation of the posterior neural plate / cell fate commitment involved in formation of primary germ layer / cardiac cell fate determination / POU5F1 (OCT4), SOX2, NANOG repress genes related to differentiation / Formation of the anterior neural plate / Positive Regulation of CDH1 Gene Transcription / endodermal-mesodermal cell signaling ...negative regulation of myeloid progenitor cell differentiation / glial cell fate commitment / single stranded viral RNA replication via double stranded DNA intermediate / Formation of the posterior neural plate / cell fate commitment involved in formation of primary germ layer / cardiac cell fate determination / POU5F1 (OCT4), SOX2, NANOG repress genes related to differentiation / Formation of the anterior neural plate / Positive Regulation of CDH1 Gene Transcription / endodermal-mesodermal cell signaling / regulation of asymmetric cell division / brahma complex / endodermal cell fate specification / positive regulation of glucose mediated signaling pathway / pituitary gland development / heart induction / blastocyst development / negative regulation of cell cycle G1/S phase transition / POU5F1 (OCT4), SOX2, NANOG activate genes related to proliferation / Specification of the neural plate border / Specification of primordial germ cells / neuronal stem cell population maintenance / nBAF complex / Regulation of MITF-M-dependent genes involved in extracellular matrix, focal adhesion and epithelial-to-mesenchymal transition / npBAF complex / positive regulation of norepinephrine uptake / positive regulation of telomere maintenance in response to DNA damage / Transcriptional regulation of pluripotent stem cells / regulation of DNA strand elongation / eye development / Transcriptional Regulation by MECP2 / negative regulation of androgen receptor signaling pathway / Germ layer formation at gastrulation / positive regulation of transcription of nucleolar large rRNA by RNA polymerase I / cellular response to cytochalasin B / neural retina development / N-acetyltransferase activity / Formation of the embryonic stem cell BAF (esBAF) complex / response to growth factor / EGR2 and SOX10-mediated initiation of Schwann cell myelination / regulation of transepithelial transport / Formation of the canonical BAF (cBAF) complex / morphogenesis of a polarized epithelium / Formation of annular gap junctions / Formation of the dystrophin-glycoprotein complex (DGC) / somatic stem cell population maintenance / Formation of the polybromo-BAF (pBAF) complex / structural constituent of postsynaptic actin cytoskeleton / Gap junction degradation / GBP-mediated host defense / Formation of neuronal progenitor and neuronal BAF (npBAF and nBAF) / protein localization to adherens junction / Formation of the non-canonical BAF (ncBAF) complex / Cell-extracellular matrix interactions / nucleosome array spacer activity / histone H3K14ac reader activity / regulation of G0 to G1 transition / dense body / RNA polymerase I preinitiation complex assembly / Tat protein binding / Folding of actin by CCT/TriC / Ino80 complex / cellular response to fatty acid / postsynaptic actin cytoskeleton / XY body / Regulation of CDH1 Function / host-mediated activation of viral transcription / forebrain development / apical protein localization / Adherens junctions interactions / Prefoldin mediated transfer of substrate to CCT/TriC / microtubule nucleation / SWI/SNF complex / RHOF GTPase cycle / adherens junction assembly / regulation of double-strand break repair / negative regulation of neuron differentiation / Sensory processing of sound by outer hair cells of the cochlea / ATP-dependent chromatin remodeler activity / miRNA binding / nucleosome disassembly / tight junction / Sensory processing of sound by inner hair cells of the cochlea / regulation of mitotic metaphase/anaphase transition / spinal cord development / nuclear androgen receptor binding / positive regulation of T cell differentiation / maintenance of blood-brain barrier / Interaction between L1 and Ankyrins / apical junction complex / inner ear development / regulation of nucleotide-excision repair / nuclear chromosome / positive regulation of stem cell population maintenance / regulation of chromosome organization / regulation of norepinephrine uptake / NuA4 histone acetyltransferase complex / transporter regulator activity / Recycling pathway of L1 / positive regulation of double-strand break repair
Similarity search - Function
SWI/SNF-like complex subunit BAF250a / SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1 / SWI/SNF-like complex subunit BAF250/Osa / SWI/SNF-like complex subunit BAF250, C-terminal / SWI/SNF-like complex subunit BAF250/Osa / DPF1-3, N-terminal domain / DPF1-3, N-terminal / Transcription factor SOX / SMARCC, SWIRM-associated domain / SMARCC, N-terminal ...SWI/SNF-like complex subunit BAF250a / SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1 / SWI/SNF-like complex subunit BAF250/Osa / SWI/SNF-like complex subunit BAF250, C-terminal / SWI/SNF-like complex subunit BAF250/Osa / DPF1-3, N-terminal domain / DPF1-3, N-terminal / Transcription factor SOX / SMARCC, SWIRM-associated domain / SMARCC, N-terminal / : / SOX transcription factor / SWIRM-associated domain at the N-terminal / SWIRM-associated domain at the C-terminal / MarR-like, BRCT and chromo domains module profile. / : / SWI/SNF Subunit INI1, DNA binding domain / SWIB domain / SWI complex, BAF60b domains / Chromatin-remodeling complex component Sfh1/SNF5 / SWI/SNF complex subunit BRG1 / : / POU-specific domain / POU domain / Pou domain - N-terminal to homeobox domain / POU-specific (POUs) domain signature 1. / POU-specific (POUs) domain signature 2. / POU-specific (POUs) domain profile. / Found in Pit-Oct-Unc transcription factors / : / SMARCC, C-terminal / SWIRM-associated region 1 / SNF5/SMARCB1/INI1 / SNF5 / SMARCB1 / INI1 / BRK domain / BRK domain / BRK domain superfamily / domain in transcription and CHROMO domain helicases / QLQ / Glutamine-Leucine-Glutamine, 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 / ARID DNA-binding domain / ARID DNA-binding domain superfamily / ARID/BRIGHT DNA binding domain / ARID domain profile. / BRIGHT, ARID (A/T-rich interaction domain) domain / ARID/BRIGHT DNA binding domain / SWIRM domain / SWIRM domain / SWIRM domain profile. / HSA domain / Homeobox, conserved site / SWIB/MDM2 domain / SWIB/MDM2 domain / SWIB/MDM2 domain profile. / Helicase/SANT-associated domain / 'Homeobox' domain signature. / HSA domain profile. / SWIB/MDM2 domain superfamily / Homeodomain / 'Homeobox' domain profile. / Homeodomain / Homeobox domain / HMG (high mobility group) box / SANT domain profile. / Chromo/chromo shadow domain / Chromatin organization modifier domain / SANT domain / HMG boxes A and B DNA-binding domains profile. / high mobility group / High mobility group box domain / High mobility group box domain superfamily / Myb-like DNA-binding domain / : / SNF2-like, N-terminal domain superfamily / Lambda repressor-like, DNA-binding domain superfamily / SNF2, N-terminal / SNF2-related domain / SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains / SANT/Myb domain / zinc finger / BRCT domain superfamily / PHD-finger / Zinc finger C2H2 type domain profile. / Actins signature 1. / Actin, conserved site / Actins signature 2. / Actin/actin-like conserved site / Actins and actin-related proteins signature. / Zinc finger PHD-type signature. / Green fluorescent protein, GFP / Zinc finger C2H2 superfamily / Zinc finger C2H2 type domain signature. / Actin / Actin family
Similarity search - Domain/homology
AT-rich interactive domain-containing protein 1A / Actin-like protein 6A / Histone H2A type 1-B/E / Histone H2B type 1-J / Green fluorescent protein / Transcription factor SOX-2 / SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4 / Actin, cytoplasmic 1 / Histone H4 / Histone H3.1 ...AT-rich interactive domain-containing protein 1A / Actin-like protein 6A / Histone H2A type 1-B/E / Histone H2B type 1-J / Green fluorescent protein / Transcription factor SOX-2 / SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4 / Actin, cytoplasmic 1 / Histone H4 / Histone H3.1 / POU domain, class 5, transcription factor 1 / SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1 / SWI/SNF complex subunit SMARCC2 / Zinc finger protein ubi-d4 / SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1 / SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1
Similarity search - Component
Biological speciesHomo spaiens (human) / Homo sapiens (human) / synthetic construct (others)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.2 Å
AuthorsVecchia L / Weiss J / Cavadini S / Kempf G / Kater L / Pathare G / Thoma NH
Funding supportEuropean Union, Switzerland, 5 items
OrganizationGrant numberCountry
European Research Council (ERC)European Union
Swiss National Science Foundation Switzerland
European Molecular Biology Organization (EMBO)European Union
Other private
Other private
CitationJournal: Mol Cell / Year: 2026
Title: The human BAF chromatin remodeler processes nucleosomes bound by pioneer transcription factors OCT4-SOX2.
Authors: Joscha Weiss / Luca Vecchia / David Domjan / Simone Cavadini / Anton Sabantsev / Georg Kempf / Ganesh R Pathare / Klaus Brackmann / Alicia K Michael / Lukas Kater / Eric Hietter-Pfeiffer / ...Authors: Joscha Weiss / Luca Vecchia / David Domjan / Simone Cavadini / Anton Sabantsev / Georg Kempf / Ganesh R Pathare / Klaus Brackmann / Alicia K Michael / Lukas Kater / Eric Hietter-Pfeiffer / Mina Haddawi / Urja P Kuber / Sandra Mühlhäusser / Ralph S Grand / Michael B Stadler / Sebastian Deindl / Nicolas H Thomä /
Abstract: Chromatin remodeling complexes mobilize nucleosomes and promote transcription factor (TF) binding. Using ensemble and single-molecule assays combined with cryo-electron microscopy (cryo-EM), we ...Chromatin remodeling complexes mobilize nucleosomes and promote transcription factor (TF) binding. Using ensemble and single-molecule assays combined with cryo-electron microscopy (cryo-EM), we studied the interaction between pioneer TFs OCT4-SOX2 and the human BRG1/BRM-associated factor (BAF) complex on nucleosomes. BAF engages TF-bound substrates in two orientations, placing OCT4-SOX2 at either the remodeler ENTRY or EXIT site. At the ENTRY site, OCT4-SOX2 initially coexists with BAF without structural interference. However, continued DNA translocation is expected to cause collisions with bound TFs, which can trigger remodeling direction reversals or may induce TF dissociation. To accommodate TFs at the EXIT site, BAF undergoes structural rearrangements, and ensemble assays reveal a nucleosome subpopulation translocating away from TF-binding sites. Moreover, single-molecule experiments show that nucleosome-bound BAF frequently changes remodeling direction, and we identify an ADP-bound remodeler conformation as a potential intermediate. Together, these findings reveal key aspects of the conformational dynamics and remodeling outcomes underlying BAF processing of TF-bound nucleosomes.
History
DepositionJun 18, 2025-
Header (metadata) releaseFeb 11, 2026-
Map releaseFeb 11, 2026-
UpdateSep 9, 2026-
Current statusSep 9, 2026Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_54056.png

Downloads & links

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Map

FileDownload / File: emd_54056.map.gz / Format: CCP4 / Size: 421.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationAmplitude-scaled map (LocScale).
Projections & slices

Image control

Size
Brightness
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AxesZ (Sec.)Y (Row.)X (Col.)
0.85 Å/pix.
x 480 pix.
= 405.6 Å		0.85 Å/pix.
x 480 pix.
= 405.6 Å		0.85 Å/pix.
x 480 pix.
= 405.6 Å

Surface

Projections

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Images are generated by Spider.

Voxel sizeX=Y=Z: 0.845 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.061
Minimum - Maximum-0.075168505 - 0.5536993
Average (Standard dev.)0.0015843614 (±0.013888151)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions480480480
Spacing480480480
CellA=B=C: 405.6 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: Full map.

Fileemd_54056_additional_1.map
AnnotationFull map.
Projections & Slices
AxesZYX

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Slices (1/2)
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Histogram (log scale)

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Sample components

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Entire : BAF in complex with a OCT4/SOX2-bound nucleosome

EntireName: BAF in complex with a OCT4/SOX2-bound nucleosome
Components
  • Complex: BAF in complex with a OCT4/SOX2-bound nucleosome
    • Complex: Nucleosome core particle
      • 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-J
      • Protein or peptide: Transcription activator BRG1
      • Protein or peptide: Actin-like protein 6A
    • Complex: BAF complex
      • Protein or peptide: Actin, cytoplasmic 1, N-terminally processed
      • Protein or peptide: AT-rich interactive domain-containing protein 1A
      • Protein or peptide: SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1
      • Protein or peptide: SWI/SNF complex subunit SMARCC2
      • Protein or peptide: SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1
      • Protein or peptide: SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1
      • Protein or peptide: Zinc finger protein ubi-d4
      • Protein or peptide: Green fluorescent protein,POU domain, class 5, transcription factor 1
      • Protein or peptide: Transcription factor SOX-2
      • DNA: DNA (148-MER)
    • Complex: OCT4/SOX2 heterodimer
      • DNA: DNA (148-MER)
  • Ligand: ZINC ION

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Supramolecule #1: BAF in complex with a OCT4/SOX2-bound nucleosome

SupramoleculeName: BAF in complex with a OCT4/SOX2-bound nucleosome / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#17

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Supramolecule #2: Nucleosome core particle

SupramoleculeName: Nucleosome core particle / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#6

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Supramolecule #3: BAF complex

SupramoleculeName: BAF complex / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #7-#16
Source (natural)Organism: Homo spaiens (human)

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Supramolecule #4: OCT4/SOX2 heterodimer

SupramoleculeName: OCT4/SOX2 heterodimer / type: complex / ID: 4 / Parent: 1 / Macromolecule list: #17

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Macromolecule #1: Histone H3.1

MacromoleculeName: Histone H3.1 / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 15.719445 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
GSHMARTKQT ARKSTGGKAP RKQLATKAAR KSAPATGGVK KPHRYRPGTV ALREIRRYQK STELLIRKLP FQRLVREIAQ DFKTDLRFQ SSAVMALQEA CEAYLVGLFE DTNLCAIHAK RVTIMPKDIQ LARRIRGERA

UniProtKB: Histone H3.1

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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: Homo sapiens (human)
Molecular weightTheoretical: 11.676703 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
GSHMSGRGKG GKGLGKGGAK RHRKVLRDNI QGITKPAIRR LARRGGVKRI SGLIYEETRG VLKVFLENVI RDAVTYTEHA KRKTVTAMD VVYALKRQGR TLYGFGG

UniProtKB: Histone H4

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Macromolecule #3: Histone H2A type 1-B/E

MacromoleculeName: Histone H2A type 1-B/E / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 14.447825 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
GSHMSGRGKQ GGKARAKAKT RSSRAGLQFP VGRVHRLLRK GNYSERVGAG APVYLAAVLE YLTAEILELA GNAARDNKKT RIIPRHLQL AIRNDEELNK LLGRVTIAQG GVLPNIQAVL LPKKTESHHK AKGK

UniProtKB: Histone H2A type 1-B/E

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Macromolecule #4: Histone H2B type 1-J

MacromoleculeName: Histone H2B type 1-J / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 14.088336 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
GSHMPEPAKS APAPKKGSKK AVTKAQKKDG KKRKRSRKES YSIYVYKVLK QVHPDTGISS KAMGIMNSFV NDIFERIAGE ASRLAHYNK RSTITSREIQ TAVRLLLPGE LAKHAVSEGT KAVTKYTSA

UniProtKB: Histone H2B type 1-J

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Macromolecule #5: Transcription activator BRG1

MacromoleculeName: Transcription activator BRG1 / type: protein_or_peptide / ID: 5 / 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: 184.923828 KDa
SequenceString: MSTPDPPLGG TPRPGPSPGP GPSPGAMLGP SPGPSPGSAH SMMGPSPGPP SAGHPIPTQG PGGYPQDNMH QMHKPMESMH EKGMSDDPR YNQMKGMGMR SGGHAGMGPP PSPMDQHSQG YPSPLGGSEH ASSPVPASGP SSGPQMSSGP GGAPLDGADP Q ALGQQNRG ...String:
MSTPDPPLGG TPRPGPSPGP GPSPGAMLGP SPGPSPGSAH SMMGPSPGPP SAGHPIPTQG PGGYPQDNMH QMHKPMESMH EKGMSDDPR YNQMKGMGMR SGGHAGMGPP PSPMDQHSQG YPSPLGGSEH ASSPVPASGP SSGPQMSSGP GGAPLDGADP Q ALGQQNRG PTPFNQNQLH QLRAQIMAYK MLARGQPLPD HLQMAVQGKR PMPGMQQQMP TLPPPSVSAT GPGPGPGPGP GP GPGPAPP NYSRPHGMGG PNMPPPGPSG VPPGMPGQPP GGPPKPWPEG PMANAAAPTS TPQKLIPPQP TGRPSPAPPA VPP AASPVM PPQTQSPGQP AQPAPMVPLH QKQSRITPIQ KPRGLDPVEI LQEREYRLQA RIAHRIQELE NLPGSLAGDL RTKA TIELK ALRLLNFQRQ LRQEVVVCMR RDTALETALN AKAYKRSKRQ SLREARITEK LEKQQKIEQE RKRRQKHQEY LNSIL QHAK DFKEYHRSVT GKIQKLTKAV ATYHANTERE QKKENERIEK ERMRRLMAED EEGYRKLIDQ KKDKRLAYLL QQTDEY VAN LTELVRQHKA AQVAKEKKKK KKKKKAENAE GQTPAIGPDG EPLDETSQMS DLPVKVIHVE SGKILTGTDA PKAGQLE AW LEMNPGYEVA PRSDSEESGS EEEEEEEEEE QPQAAQPPTL PVEEKKKIPD PDSDDVSEVD ARHIIENAKQ DVDDEYGV S QALARGLQSY YAVAHAVTER VDKQSALMVN GVLKQYQIKG LEWLVSLYNN NLNGILADEM GLGKTIQTIA LITYLMEHK RINGPFLIIV PLSTLSNWAY EFDKWAPSVV KVSYKGSPAA RRAFVPQLRS GKFNVLLTTY EYIIKDKHIL AKIRWKYMIV DEGHRMKNH HCKLTQVLNT HYVAPRRLLL TGTPLQNKLP ELWALLNFLL PTIFKSCSTF EQWFNAPFAM TGEKVDLNEE E TILIIRRL HKVLRPFLLR RLKKEVEAQL PEKVEYVIKC DMSALQRVLY RHMQAKGVLL TDGSEKDKKG KGGTKTLMNT IM QLRKICN HPYMFQHIEE SFSEHLGFTG GIVQGLDLYR ASGKFELLDR ILPKLRATNH KVLLFCQMTS LMTIMEDYFA YRG FKYLRL DGTTKAEDRG MLLKTFNEPG SEYFIFLLST RAGGLGLNLQ SADTVIIFDS DWNPHQDLQA QDRAHRIGQQ NEVR VLRLC TVNSVEEKIL AAAKYKLNVD QKVIQAGMFD QKSSSHERRA FLQAILEHEE QDESRHCSTG SGSASFAHTA PPPAG VNPD LEEPPLKEED EVPDDETVNQ MIARHEEEFD LFMRMDLDRR REEARNPKRK PRLMEEDELP SWIIKDDAEV ERLTCE EEE EKMFGRGSRH RKEVDYSDSL TEKQWLKAIE EGTLEEIEEE VRQKKSSRKR KRDSDAGSST PTTSTRSRDK DDESKKQ KK RGRPPAEKLS PNPPNLTKKM KKIVDAVIKY KDSSSGRQLS EVFIQLPSRK ELPEYYELIR KPVDFKKIKE RIRNHKYR S LNDLEKDVML LCQNAQTFNL EGSLIYEDSI VLQSVFTSVR QKIEKEDDSE GEESEEEEEG EEEGSESESR SVKVKIKLG RKEKAQDRLK GGRRRPSRGS RAKPVVSDDD SEEEQEEDRS GSGSEED

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

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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: 47.509812 KDa
SequenceString: MSGGVYGGDE VGALVFDIGS YTVRAGYAGE DCPKVDFPTA IGMVVERDDG STLMEIDGDK GKQGGPTYYI DTNALRVPRE NMEAISPLK NGMVEDWDSF QAILDHTYKM HVKSEASLHP VLMSEAPWNT RAKREKLTEL MFEHYNIPAF FLCKTAVLTA F ANGRSTGL ...String:
MSGGVYGGDE VGALVFDIGS YTVRAGYAGE DCPKVDFPTA IGMVVERDDG STLMEIDGDK GKQGGPTYYI DTNALRVPRE NMEAISPLK NGMVEDWDSF QAILDHTYKM HVKSEASLHP VLMSEAPWNT RAKREKLTEL MFEHYNIPAF FLCKTAVLTA F ANGRSTGL ILDSGATHTT AIPVHDGYVL QQGIVKSPLA GDFITMQCRE LFQEMNIELV PPYMIASKEA VREGSPANWK RK EKLPQVT RSWHNYMCNC VIQDFQASVL QVSDSTYDEQ VAAQMPTVHY EFPNGYNCDF GAERLKIPEG LFDPSNVKGL SGN TMLGVS HVVTTSVGMC DIDIRPGLYG SVIVAGGNTL IQSFTDRLNR ELSQKTPPSM RLKLIANNTT VERRFSSWIG GSIL ASLGT FQQMWISKQE YEEGGKQCVE RKCP

UniProtKB: Actin-like protein 6A

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Macromolecule #7: Actin, cytoplasmic 1, N-terminally processed

MacromoleculeName: Actin, cytoplasmic 1, N-terminally processed / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 41.78266 KDa
SequenceString: MDDDIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM TQIMFETFNT PAMYVAIQAV LSLYASGRTT GIVMDSGDGV T HTVPIYEG ...String:
MDDDIAALVV DNGSGMCKAG FAGDDAPRAV FPSIVGRPRH QGVMVGMGQK DSYVGDEAQS KRGILTLKYP IEHGIVTNWD DMEKIWHHT FYNELRVAPE EHPVLLTEAP LNPKANREKM TQIMFETFNT PAMYVAIQAV LSLYASGRTT GIVMDSGDGV T HTVPIYEG YALPHAILRL DLAGRDLTDY LMKILTERGY SFTTTAEREI VRDIKEKLCY VALDFEQEMA TAASSSSLEK SY ELPDGQV ITIGNERFRC PEALFQPSFL GMESCGIHET TFNSIMKCDV DIRKDLYANT VLSGGTTMYP GIADRMQKEI TAL APSTMK IKIIAPPERK YSVWIGGSIL ASLSTFQQMW ISKQEYDESG PSIVHRKCF

UniProtKB: Actin, cytoplasmic 1

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Macromolecule #8: AT-rich interactive domain-containing protein 1A

MacromoleculeName: AT-rich interactive domain-containing protein 1A / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 242.250312 KDa
SequenceString: MAAQVAPAAA SSLGNPPPPP PSELKKAEQQ QREEAGGEAA AAAAAERGEM KAAAGQESEG PAVGPPQPLG KELQDGAESN GGGGGGGAG SGGGPGAEPD LKNSNGNAGP RPALNNNLTE PPGGGGGGSS DGVGAPPHSA AAALPPPAYG FGQPYGRSPS A VAAAAAAV ...String:
MAAQVAPAAA SSLGNPPPPP PSELKKAEQQ QREEAGGEAA AAAAAERGEM KAAAGQESEG PAVGPPQPLG KELQDGAESN GGGGGGGAG SGGGPGAEPD LKNSNGNAGP RPALNNNLTE PPGGGGGGSS DGVGAPPHSA AAALPPPAYG FGQPYGRSPS A VAAAAAAV FHQQHGGQQS PGLAALQSGG GGGLEPYAGP QQNSHDHGFP NHQYNSYYPN RSAYPPPAPA YALSSPRGGT PG SGAAAAA GSKPPPSSSA SASSSSSSFA QQRFGAMGGG GPSAAGGGTP QPTATPTLNQ LLTSPSSARG YQGYPGGDYS GGP QDGGAG KGPADMASQC WGAAAAAAAA AAASGGAQQR SHHAPMSPGS SGGGGQPLAR TPQPSSPMDQ MGKMRPQPYG GTNP YSQQQ GPPSGPQQGH GYPGQPYGSQ TPQRYPMTMQ GRAQSAMGGL SYTQQIPPYG QQGPSGYGQQ GQTPYYNQQS PHPQQ QQPP YSQQPPSQTP HAQPSYQQQP QSQPPQLQSS QPPYSQQPSQ PPHQQSPAPY PSQQSTTQQH PQSQPPYSQP QAQSPY QQQ QPQQPAPSTL SQQAAYPQPQ SQQSQQTAYS QQRFPPPQEL SQDSFGSQAS SAPSMTSSKG GQEDMNLSLQ SRPSSLP DL SGSIDDLPMG TEGALSPGVS TSGISSSQGE QSNPAQSPFS PHTSPHLPGI RGPSPSPVGS PASVAQSRSG PLSPAAVP G NQMPPRPPSG QSDSIMHPSM NQSSIAQDRG YMQRNPQMPQ YSSPQPGSAL SPRQPSGGQI HTGMGSYQQN SMGSYGPQG GQYGPQGGYP RQPNYNALPN ANYPSAGMAG GINPMGAGGQ MHGQPGIPPY GTLPPGRMSH ASMGNRPYGP NMANMPPQVG SGMCPPPGG MNRKTQETAV AMHVAANSIQ NRPPGYPNMN QGGMMGTGPP YGQGINSMAG MINPQGPPYS MGGTMANNSA G MAASPEMM GLGDVKLTPA TKMNNKADGT PKTESKSKKS SSSTTTNEKI TKLYELGGEP ERKMWVDRYL AFTEEKAMGM TN LPAVGRK PLDLYRLYVS VKEIGGLTQV NKNKKWRELA TNLNVGTSSS AASSLKKQYI QCLYAFECKI ERGEDPPPDI FAA ADSKKS QPKIQPPSPA GSGSMQGPQT PQSTSSSMAE GGDLKPPTPA STPHSQIPPL PGMSRSNSVG IQDAFNDGSD STFQ KRNSM TPNPGYQPSM NTSDMMGRMS YEPNKDPYGS MRKAPGSDPF MSSGQGPNGG MGDPYSRAAG PGLGNVAMGP RQHYP YGGP YDRVRTEPGI GPEGNMSTGA PQPNLMPSNP DSGMYSPSRY PPQQQQQQQQ RHDSYGNQFS TQGTPSGSPF PSQQTT MYQ QQQQNYKRPM DGTYGPPAKR HEGEMYSVPY STGQGQPQQQ QLPPAQPQPA SQQQAAQPSP QQDVYNQYGN AYPATAT AA TERRPAGGPQ NQFPFQFGRD RVSAPPGTNA QQNMPPQMMG GPIQASAEVA QQGTMWQGRN DMTYNYANRQ STGSAPQG P AYHGVNRTDE MLHTDQRANH EGSWPSHGTR QPPYGPSAPV PPMTRPPPSN YQPPPSMQNH IPQVSSPAPL PRPMENRTS PSKSPFLHSG MKMQKAGPPV PASHIAPAPV QPPMIRRDIT FPPGSVEATQ PVLKQRRRLT MKDIGTPEAW RVMMSLKSGL LAESTWALD TINILLYDDN SIMTFNLSQL PGLLELLVEY FRRCLIEIFG ILKEYEVGDP GQRTLLDPGR FSKVSSPAPM E GGEEEEEL LGPKLEEEEE EEVVENDEEI AFSGKDKPAS ENSEEKLISK FDKLPVKIVQ KNDPFVVDCS DKLGRVQEFD SG LLHWRIG GGDTTEHIQT HFESKTELLP SRPHAPCPPA PRKHVTTAEG TPGTTDQEGP PPDGPPEKRI TATMDDMLST RSS TLTEDG AKSSEAIKES SKFPFGISPA QSHRNIKILE DEPHSKDETP LCTLLDWQDS LAKRCVCVSN TIRSLSFVPG NDFE MSKHP GLLLILGKLI LLHHKHPERK QAPLTYEKEE EQDQGVSCNK VEWWWDCLEM LRENTLVTLA NISGQLDLSP YPESI CLPV LDGLLHWAVC PSAEAQDPFS TLGPNAVLSP QRLVLETLSK LSIQDNNVDL ILATPPFSRL EKLYSTMVRF LSDRKN PVC REMAVVLLAN LAQGDSLAAR AIAVQKGSIG NLLGFLEDSL AATQFQQSQA SLLHMQNPPF EPTSVDMMRR AARALLA LA KVDENHSEFT LYESRLLDIS VSPLMNSLVS QVICDVLFLI GQS

UniProtKB: AT-rich interactive domain-containing protein 1A

+
Macromolecule #9: SWI/SNF-related matrix-associated actin-dependent regulator of ch...

MacromoleculeName: SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1
type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 44.199188 KDa
SequenceString: MMMMALSKTF GQKPVKFQLE DDGEFYMIGS EVGNYLRMFR GSLYKRYPSL WRRLATVEER KKIVASSHGK KTKPNTKDHG YTTLATSVT LLKASEVEEI LDGNDEKYKA VSISTEPPTY LREQKAKRNS QWVPTLPNSS HHLDAVPCST TINRNRMGRD K KRTFPLCF ...String:
MMMMALSKTF GQKPVKFQLE DDGEFYMIGS EVGNYLRMFR GSLYKRYPSL WRRLATVEER KKIVASSHGK KTKPNTKDHG YTTLATSVT LLKASEVEEI LDGNDEKYKA VSISTEPPTY LREQKAKRNS QWVPTLPNSS HHLDAVPCST TINRNRMGRD K KRTFPLCF DDHDPAVIHE NASQPEVLVP IRLDMEIDGQ KLRDAFTWNM NEKLMTPEMF SEILCDDLDL NPLTFVPAIA SA IRQQIES YPTDSILEDQ SDQRVIIKLN IHVGNISLVD QFEWDMSEKE NSPEKFALKL CSELGLGGEF VTTIAYSIRG QLS WHQKTY AFSENPLPTV EIAIRNTGDA DQWCPLLETL TDAEMEKKIR DQDRNTRRMR RLANTAPAW

UniProtKB: SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1

+
Macromolecule #10: SWI/SNF complex subunit SMARCC2

MacromoleculeName: SWI/SNF complex subunit SMARCC2 / type: protein_or_peptide / ID: 10 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 133.048109 KDa
SequenceString: MAVRKKDGGP NVKYYEAADT VTQFDNVRLW LGKNYKKYIQ AEPPTNKSLS SLVVQLLQFQ EEVFGKHVSN APLTKLPIKC FLDFKAGGS LCHILAAAYK FKSDQGWRRY DFQNPSRMDR NVEMFMTIEK SLVQNNCLSR PNIFLCPEIE PKLLGKLKDI I KRHQGTVT ...String:
MAVRKKDGGP NVKYYEAADT VTQFDNVRLW LGKNYKKYIQ AEPPTNKSLS SLVVQLLQFQ EEVFGKHVSN APLTKLPIKC FLDFKAGGS LCHILAAAYK FKSDQGWRRY DFQNPSRMDR NVEMFMTIEK SLVQNNCLSR PNIFLCPEIE PKLLGKLKDI I KRHQGTVT EDKNNASHVV YPVPGNLEEE EWVRPVMKRD KQVLLHWGYY PDSYDTWIPA SEIEASVEDA PTPEKPRKVH AK WILDTDT FNEWMNEEDY EVNDDKNPVS RRKKISAKTL TDEVNSPDSD RRDKKGGNYK KRKRSPSPSP TPEAKKKNAK KGP STPYTK SKRGHREEEQ EDLTKDMDEP SPVPNVEEVT LPKTVNTKKD SESAPVKGGT MTDLDEQEDE SMETTGKDED ENST GNKGE QTKNPDLHED NVTEQTHHII IPSYAAWFDY NSVHAIERRA LPEFFNGKNK SKTPEIYLAY RNFMIDTYRL NPQEY LTST ACRRNLAGDV CAIMRVHAFL EQWGLINYQV DAESRPTPMG PPPTSHFHVL ADTPSGLVPL QPKTPQQTSA SQQMLN FPD KGKEKPTDMQ NFGLRTDMYT KKNVPSKSKA AASATREWTE QETLLLLEAL EMYKDDWNKV SEHVGSRTQD ECILHFL RL PIEDPYLEDS EASLGPLAYQ PIPFSQSGNP VMSTVAFLAS VVDPRVASAA AKSALEEFSK MKEEVPTALV EAHVRKVE E AAKVTGKADP AFGLESSGIA GTTSDEPERI EESGNDEARV EGQATDEKKE PKEPREGGGA IEEEAKEKTS EAPKKDEEK GKEGDSEKES EKSDGDPIVD PEKEKEPKEG QEEVLKEVVE SEGERKTKVE RDIGEGNLST AAAAALAAAA VKAKHLAAVE ERKIKSLVA LLVETQMKKL EIKLRHFEEL ETIMDREREA LEYQRQQLLA DRQAFHMEQL KYAEMRARQQ HFQQMHQQQQ Q PPPALPPG SQPIPPTGAA GPPAVHGLAV APASVVPAPA GSGAPPGSLG PSEQIGQAGS TAGPQQQQPA GAPQPGAVPP GV PPPGPHG PSPFPNQQTP PSMMPGAVPG SGHPGVAGNA PLGLPFGMPP PPPPPAPSII PFGSLADSIS INLPAPPNLH GHH HHLPFA PGTLPPPNLP VSMANPLHPN LPATTTMPSS LPLGPGLGSA AAQSPAIVAA VQGNLLPSAS PLPDPGTPLP PDPT APSPG TVTPVPPPQ

UniProtKB: SWI/SNF complex subunit SMARCC2

+
Macromolecule #11: SWI/SNF-related matrix-associated actin-dependent regulator of ch...

MacromoleculeName: SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1
type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 58.311391 KDa
SequenceString: MAARAGFQSV APSGGAGASG GAGAAAALGP GGTPGPPVRM GPAPGQGLYR SPMPGAAYPR PGMLPGSRMT PQGPSMGPPG YGGNPSVRP GLAQSGMDQS RKRPAPQQIQ QVQQQAVQNR NHNAKKKKMA DKILPQRIRE LVPESQAYMD LLAFERKLDQ T IMRKRLDI ...String:
MAARAGFQSV APSGGAGASG GAGAAAALGP GGTPGPPVRM GPAPGQGLYR SPMPGAAYPR PGMLPGSRMT PQGPSMGPPG YGGNPSVRP GLAQSGMDQS RKRPAPQQIQ QVQQQAVQNR NHNAKKKKMA DKILPQRIRE LVPESQAYMD LLAFERKLDQ T IMRKRLDI QEALKRPIKQ KRKLRIFISN TFNPAKSDAE DGEGTVASWE LRVEGRLLED SALSKYDATK QKRKFSSFFK SL VIELDKD LYGPDNHLVE WHRTATTQET DGFQVKRPGD VNVRCTVLLM LDYQPPQFKL DPRLARLLGI HTQTRPVIIQ ALW QYIKTH KLQDPHEREF VICDKYLQQI FESQRMKFSE IPQRLHALLM PPEPIIINHV ISVDPNDQKK TACYDIDVEV DDTL KTQMN SFLLSTASQQ EIATLDNKIH ETIETINQLK TQREFMLSFA RDPQGFINDW LQSQCRDLKT MTDVVGNPEE ERRAE FYFQ PWAQEAVCRY FYSKVQQRRQ ELEQALGIRN T

UniProtKB: SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily D member 1

+
Macromolecule #12: SWI/SNF-related matrix-associated actin-dependent regulator of ch...

MacromoleculeName: SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1
type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 46.710371 KDa
SequenceString: MSKRPSYAPP PTPAPATQMP STPGFVGYNP YSHLAYNNYR LGGNPGTNSR VTASSGITIP KPPKPPDKPL MPYMRYSRKV WDQVKASNP DLKLWEIGKI IGGMWRDLTD EEKQEYLNEY EAEKIEYNES MKAYHNSPAY LAYINAKSRA EAALEEESRQ R QSRMEKGE ...String:
MSKRPSYAPP PTPAPATQMP STPGFVGYNP YSHLAYNNYR LGGNPGTNSR VTASSGITIP KPPKPPDKPL MPYMRYSRKV WDQVKASNP DLKLWEIGKI IGGMWRDLTD EEKQEYLNEY EAEKIEYNES MKAYHNSPAY LAYINAKSRA EAALEEESRQ R QSRMEKGE PYMSIQPAED PDDYDDGFSM KHTATARFQR NHRLISEILS ESVVPDVRSV VTTARMQVLK RQVQSLMVHQ RK LEAELLQ IEERHQEKKR KFLESTDSFN NELKRLCGLK VEVDMEKIAA EIAQAEEQAR KRQEEREKEA AEQAERSQSS IVP EEEQAA NKGEEKKDDE NIPMETEETH LEETTESQQN GEEGTSTPED KESGQEGVDS MAEEGTSDSN TGSESNSATV EEPP TDPIP EDEKKE

UniProtKB: SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1

+
Macromolecule #13: Zinc finger protein ubi-d4

MacromoleculeName: Zinc finger protein ubi-d4 / type: protein_or_peptide / ID: 13 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 48.554125 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MAAVVENVVK LLGEQYYKDA MEQCHNYNAR LCAERSVRLP FLDSQTGVAQ SNCYIWMEKR HRGPGLASGQ LYSYPARRWR KKRRAHPPE DPRLSFPSIK PDTDQTLKKE GLISQDGSSL EALLRTDPLE KRGAPDPRVD DDSLGEFPVT NSRARKRILE P DDFLDDLD ...String:
MAAVVENVVK LLGEQYYKDA MEQCHNYNAR LCAERSVRLP FLDSQTGVAQ SNCYIWMEKR HRGPGLASGQ LYSYPARRWR KKRRAHPPE DPRLSFPSIK PDTDQTLKKE GLISQDGSSL EALLRTDPLE KRGAPDPRVD DDSLGEFPVT NSRARKRILE P DDFLDDLD DEDYEEDTPK RRGKGKSKGK GVGSARKKLD ASILEDRDKP YACDICGKRY KNRPGLSYHY AHSHLAEEEG ED KEDSQPP TPVSQRSEEQ KSKKGPDGLA LPNNYCDFCL GDSKINKKTG QPEELVSCSD CGRSGHPSCL QFTPVMMAAV KTY RWQCIE CKCCNICGTS ENDDQLLFCD DCDRGYHMYC LTPSMSEPPE GSWSCHLCLD LLKEKASIYQ NQNSSGTLEV LFQG PGGSG SAWSHPQFEK GGGSGGGSGG SAWSHPQFEK

UniProtKB: Zinc finger protein ubi-d4

+
Macromolecule #14: Green fluorescent protein,POU domain, class 5, transcription factor 1

MacromoleculeName: Green fluorescent protein,POU domain, class 5, transcription factor 1
type: protein_or_peptide / ID: 14 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 70.735531 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString: MDWSHPQFEK SAVDENLYFQ GGGRMVSKGE ELFTGVVPIL VELDGDVNGH KFSVSGEGEG DATYGKLTLK FICTTGKLPV PWPTLVTTL TYGVQCFSRY PDHMKQHDFF KSAMPEGYVQ ERTIFFKDDG NYKTRAEVKF EGDTLVNRIE LKGIDFKEDG N ILGHKLEY ...String:
MDWSHPQFEK SAVDENLYFQ GGGRMVSKGE ELFTGVVPIL VELDGDVNGH KFSVSGEGEG DATYGKLTLK FICTTGKLPV PWPTLVTTL TYGVQCFSRY PDHMKQHDFF KSAMPEGYVQ ERTIFFKDDG NYKTRAEVKF EGDTLVNRIE LKGIDFKEDG N ILGHKLEY NYNSHNVYIM ADKQKNGIKV NFKIRHNIED GSVQLADHYQ QNTPIGDGPV LLPDNHYLST QSKLSKDPNE KR DHMVLLE FVTAAGITLG MDELYKEAAA KEAAAKMAGH LASDFAFSPP PGGGGDGPGG PEPGWVDPRT WLSFQGPPGG PGI GPGVGP GSEVWGIPPC PPPYEFCGGM AYCGPQVGVG LVPQGGLETS QPEGEAGVGV ESNSDGASPE PCTVTPGAVK LEKE KLEQN PEESQDIKAL QKELEQFAKL LKQKRITLGY TQADVGLTLG VLFGKVFSQT TICRFEALQL SFKNMCKLRP LLQKW VEEA DNNENLQEIC KAETLVQARK RKRTSIENRV RGNLENLFLQ CPKPTLQQIS HIAQQLGLEK DVVRVWFCNR RQKGKR SSS DYAQREDFEA AGSPFSGGPV SFPLAPGPHF GTPGYGSPHF TALYSSVPFP EGEAFPPVSV TTLGSPMHSN LPETGGH HH HHH

UniProtKB: Green fluorescent protein, POU domain, class 5, transcription factor 1

+
Macromolecule #15: Transcription factor SOX-2

MacromoleculeName: Transcription factor SOX-2 / type: protein_or_peptide / ID: 15 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 12.718679 KDa
Recombinant expressionOrganism: Spodoptera frugiperda (fall armyworm)
SequenceString:
MDWSHPQFEK SAVDENLYFQ GGMSPDRVKR PMNAFMVWSR GQRRKMAQEN PKMHNSEISK RLGAEWKLLS ETEKRPFIDE AKRLRALHM KEHPDYKYRP RRKTKT

UniProtKB: Transcription factor SOX-2

+
Macromolecule #16: DNA (148-MER)

MacromoleculeName: DNA (148-MER) / type: dna / ID: 16 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 69.794414 KDa
SequenceString: (DC)(DC)(DG)(DC)(DA)(DG)(DC)(DC)(DG)(DA) (DA)(DC)(DG)(DA)(DC)(DC)(DG)(DA)(DG)(DC) (DG)(DC)(DA)(DG)(DC)(DG)(DA)(DG)(DT) (DC)(DA)(DG)(DT)(DG)(DG)(DA)(DT)(DA)(DT) (DC) (DC)(DT)(DG)(DG)(DA)(DG) ...String:
(DC)(DC)(DG)(DC)(DA)(DG)(DC)(DC)(DG)(DA) (DA)(DC)(DG)(DA)(DC)(DC)(DG)(DA)(DG)(DC) (DG)(DC)(DA)(DG)(DC)(DG)(DA)(DG)(DT) (DC)(DA)(DG)(DT)(DG)(DG)(DA)(DT)(DA)(DT) (DC) (DC)(DT)(DG)(DG)(DA)(DG)(DA)(DA) (DT)(DC)(DC)(DC)(DG)(DG)(DT)(DC)(DT)(DG) (DC)(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)(DC)(DT)(DT)(DT)(DG)(DT)(DT)(DA)(DT) (DG)(DC)(DA)(DA)(DA)(DT)(DA)(DC) (DA) (DT)(DC)(DC)(DT)(DG)(DT)(DC)(DG)(DG)(DG) (DA)(DT)(DC)(DC)(DT)(DA)(DA)(DT)(DG) (DA)(DC)(DC)(DA)(DA)(DG)(DG)(DA)(DA)(DA) (DG)(DC)(DA)(DT)(DG)(DA)(DT)(DT)(DC)(DT) (DT)(DC)(DA)(DC)(DA)(DC)(DC)

+
Macromolecule #17: DNA (148-MER)

MacromoleculeName: DNA (148-MER) / type: dna / ID: 17 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 70.389781 KDa
SequenceString: (DG)(DG)(DT)(DG)(DT)(DG)(DA)(DA)(DG)(DA) (DA)(DT)(DC)(DA)(DT)(DG)(DC)(DT)(DT)(DT) (DC)(DC)(DT)(DT)(DG)(DG)(DT)(DC)(DA) (DT)(DT)(DA)(DG)(DG)(DA)(DT)(DC)(DC)(DC) (DG) (DA)(DC)(DA)(DG)(DG)(DA) ...String:
(DG)(DG)(DT)(DG)(DT)(DG)(DA)(DA)(DG)(DA) (DA)(DT)(DC)(DA)(DT)(DG)(DC)(DT)(DT)(DT) (DC)(DC)(DT)(DT)(DG)(DG)(DT)(DC)(DA) (DT)(DT)(DA)(DG)(DG)(DA)(DT)(DC)(DC)(DC) (DG) (DA)(DC)(DA)(DG)(DG)(DA)(DT)(DG) (DT)(DA)(DT)(DT)(DT)(DG)(DC)(DA)(DT)(DA) (DA)(DC) (DA)(DA)(DA)(DG)(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)(DG)(DC)(DA)(DG) (DA)(DC)(DC)(DG)(DG)(DG)(DA)(DT) (DT) (DC)(DT)(DC)(DC)(DA)(DG)(DG)(DA)(DT)(DA) (DT)(DC)(DC)(DA)(DC)(DT)(DG)(DA)(DC) (DT)(DC)(DG)(DC)(DT)(DG)(DC)(DG)(DC)(DT) (DC)(DG)(DG)(DT)(DC)(DG)(DT)(DT)(DC)(DG) (DG)(DC)(DT)(DG)(DC)(DG)(DG)

+
Macromolecule #18: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 18 / Number of copies: 1 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 8
VitrificationCryogen name: ETHANE

-
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: 2.5 µm / Nominal defocus min: 0.5 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

+
Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 4.2 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 30808
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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