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- EMDB-12450: RNA Polymerase II-Spt4/5-nucleosome-FACT structure -

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Basic information

Entry
Database: EMDB / ID: EMD-12450
TitleRNA Polymerase II-Spt4/5-nucleosome-FACT structure
Map dataMap D
Sample
  • Complex: Complex of RNA polymerase II-Spt4/5-FACT-nucleosome
    • Complex: RNA (5'-R(P*UP*CP*UP*UP*UP*UP*AP*UP*UP*UP*UP*UP*UP*CP*UP*G)-3')
      • RNA: x 1 types
    • Complex: DNA (138-MER)
      • DNA: x 1 types
    • Complex: DNA (148-MER)
      • DNA: x 1 types
    • Complex: DNA-directed RNA polymerase II subunit RPB1
      • Protein or peptide: x 1 types
    • Complex: DNA-directed RNA polymerase II subunit RPB2
      • Protein or peptide: x 1 types
    • Complex: DNA-directed RNA polymerase II subunit RPB3
      • Protein or peptide: x 1 types
    • Complex: DNA-directed RNA polymerases I, II, and III subunit RPABC1
      • Protein or peptide: x 1 types
    • Complex: DNA-directed RNA polymerases I, II, and III subunit RPABC2
      • Protein or peptide: x 1 types
    • Complex: DNA-directed RNA polymerases I, II, and III subunit RPABC3
      • Protein or peptide: x 1 types
    • Complex: DNA-directed RNA polymerase II subunit RPB9
      • Protein or peptide: x 1 types
    • Complex: DNA-directed RNA polymerases I, II, and III subunit RPABC5
      • Protein or peptide: x 1 types
    • Complex: DNA-directed RNA polymerase II subunit RPB11
      • Protein or peptide: x 1 types
    • Complex: DNA-directed RNA polymerases I, II, and III subunit RPABC4
      • Protein or peptide: x 1 types
    • Complex: Chromatin elongation factor SPT4
      • Protein or peptide: x 1 types
    • Complex: Transcription elongation factor SPT5
      • Protein or peptide: x 1 types
    • Complex: DNA-directed RNA polymerase II subunit RPB4
      • Protein or peptide: x 1 types
    • Complex: DNA-directed RNA polymerase II subunit RPB7
      • Protein or peptide: x 1 types
    • Complex: FACT complex subunit POB3
      • Protein or peptide: x 1 types
    • Complex: FACT complex subunit SPT16
      • Protein or peptide: x 1 types
    • Complex: Histone H3.2
      • Protein or peptide: x 1 types
    • Complex: Histone H4
      • Protein or peptide: x 1 types
    • Complex: Histone H2A type 1
      • Protein or peptide: x 1 types
    • Complex: Histone H2B 1.1
      • Protein or peptide: x 1 types
  • Ligand: x 2 types
KeywordsChromatin / nucleosome / elongation / histone chaperone / TRANSCRIPTION
Function / homology
Function and homology information


Regulation of TP53 Activity through Phosphorylation / regulation of sister chromatid cohesion / FACT complex / regulation of chromatin organization / DSIF complex / regulation of transcription elongation by RNA polymerase II / nucleosome organization / RPB4-RPB7 complex / replication fork protection complex / RNA Polymerase I Transcription Initiation ...Regulation of TP53 Activity through Phosphorylation / regulation of sister chromatid cohesion / FACT complex / regulation of chromatin organization / DSIF complex / regulation of transcription elongation by RNA polymerase II / nucleosome organization / RPB4-RPB7 complex / replication fork protection complex / RNA Polymerase I Transcription Initiation / Processing of Capped Intron-Containing Pre-mRNA / nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / RNA Polymerase III Transcription Initiation From Type 2 Promoter / transcription elongation-coupled chromatin remodeling / RNA Pol II CTD phosphorylation and interaction with CE / Formation of the Early Elongation Complex / mRNA Capping / RNA polymerase II transcribes snRNA genes / TP53 Regulates Transcription of DNA Repair Genes / termination of RNA polymerase II transcription / RNA Polymerase II Promoter Escape / RNA Polymerase II Transcription Pre-Initiation And Promoter Opening / RNA Polymerase II Transcription Initiation / RNA Polymerase II Transcription Initiation And Promoter Clearance / RNA Polymerase II Pre-transcription Events / RNA-templated transcription / termination of RNA polymerase III transcription / Formation of TC-NER Pre-Incision Complex / transcription initiation at RNA polymerase III promoter / maintenance of transcriptional fidelity during transcription elongation by RNA polymerase II / termination of RNA polymerase I transcription / RNA Polymerase I Promoter Escape / RNA polymerase II complex binding / nucleolar large rRNA transcription by RNA polymerase I / Gap-filling DNA repair synthesis and ligation in TC-NER / transcription by RNA polymerase I / transcription initiation at RNA polymerase I promoter / nuclear-transcribed mRNA catabolic process / Estrogen-dependent gene expression / positive regulation of nuclear-transcribed mRNA poly(A) tail shortening / transcription by RNA polymerase III / RNA polymerase II activity / chromosome, centromeric region / Dual incision in TC-NER / positive regulation of RNA polymerase II transcription preinitiation complex assembly / positive regulation of transcription initiation by RNA polymerase II / transcription elongation by RNA polymerase I / transcription-coupled nucleotide-excision repair / tRNA transcription by RNA polymerase III / RNA polymerase I complex / RNA polymerase I activity / RNA polymerase III complex / translesion synthesis / positive regulation of translational initiation / RNA polymerase II, core complex / translation initiation factor binding / regulation of DNA-templated transcription elongation / DNA-templated transcription initiation / transcription initiation at RNA polymerase II promoter / transcription elongation by RNA polymerase II / P-body / ribonucleoside binding / DNA-templated DNA replication / DNA-directed 5'-3' RNA polymerase activity / DNA-directed RNA polymerase / mRNA processing / cytoplasmic stress granule / structural constituent of chromatin / nucleosome / peroxisome / nucleosome assembly / ribosome biogenesis / chromatin organization / single-stranded DNA binding / chromosome / transcription by RNA polymerase II / DNA replication / nucleic acid binding / single-stranded RNA binding / protein dimerization activity / protein heterodimerization activity / DNA repair / mRNA binding / nucleotide binding / chromatin / regulation of transcription by RNA polymerase II / nucleolus / mitochondrion / DNA binding / zinc ion binding / nucleoplasm / nucleus / metal ion binding / cytoplasm
Similarity search - Function
FACT complex subunit Spt16, peptidase M24-like domain / : / FACT complex subunit SPT16, C-terminal domain / FACT complex subunit SSRP1/POB3 / SSRP1, dimerization domain / FACT complex subunit SSRP1/POB3, N-terminal PH domain / SSRP1 domain superfamily / Structure-specific recognition protein (SSRP1) / POB3-like N-terminal PH domain / FACT complex subunit Spt16 domain ...FACT complex subunit Spt16, peptidase M24-like domain / : / FACT complex subunit SPT16, C-terminal domain / FACT complex subunit SSRP1/POB3 / SSRP1, dimerization domain / FACT complex subunit SSRP1/POB3, N-terminal PH domain / SSRP1 domain superfamily / Structure-specific recognition protein (SSRP1) / POB3-like N-terminal PH domain / FACT complex subunit Spt16 domain / FACT complex subunit (SPT16/CDC68) / FACT complex subunit (SPT16/CDC68) / FACT complex subunit Spt16, N-terminal lobe domain / FACT complex subunit Spt16 / FACT complex subunit SPT16 N-terminal lobe domain / FACT complex subunit SPT16 N-terminal lobe domain / Histone chaperone RTT106/FACT complex subunit SPT16-like, middle domain / Histone chaperone Rttp106-like, middle domain / Histone chaperone Rttp106-like / Transcription initiation Spt4 / Spt4 superfamily / Spt4/RpoE2 zinc finger / Spt4/RpoE2 zinc finger / Spt4/RpoE2 zinc finger / Transcription elongation factor Spt5, eukaryote / Spt5 transcription elongation factor, N-terminal / Spt5, KOW domain repeat 2 / Spt5, KOW domain repeat 3 / Spt5, KOW domain repeat 5 / Spt5 transcription elongation factor, acidic N-terminal / NGN domain, eukaryotic / Spt5, KOW domain repeat 1 / Spt5, KOW domain repeat 4 / Spt5 C-terminal domain / Spt5 C-terminal nonapeptide repeat binding Spt4 / NGN domain / Transcription elongation factor SPT5 / Early transcription elongation factor of RNA pol II, NGN section / Creatinase/Aminopeptidase P/Spt16, N-terminal / NusG, N-terminal / In Spt5p, this domain may confer affinity for Spt4p. It possesses a RNP-like fold. / NusG, N-terminal domain superfamily / Peptidase M24 / Metallopeptidase family M24 / Creatinase/aminopeptidase-like / DNA-directed RNA polymerase II subunit Rpb4-like / RNA polymerase Rpb4/RPC9, core / DNA-directed RNA-polymerase II subunit / RNA polymerase II, heptapeptide repeat, eukaryotic / RNA polymerase Rpb1, domain 6 / RNA polymerase Rpb1, domain 6 / RNA polymerase Rpb1 C-terminal repeat / Eukaryotic RNA polymerase II heptapeptide repeat. / RNA polymerase Rpb1, domain 7 / RNA polymerase Rpb1, domain 7 superfamily / RNA polymerase Rpb1, domain 7 / Rpb4/RPC9 superfamily / Pol II subunit B9, C-terminal zinc ribbon / RNA polymerase RBP11 / RNA polymerase subunit Rpb4/RPC9 / RNA polymerase Rpb4 / Zinc finger TFIIS-type signature. / HRDC-like superfamily / RNA polymerase Rpb7-like , N-terminal / RNA polymerase Rpb7-like, N-terminal domain superfamily / RNA polymerase subunit Rpb7-like / SHS2 domain found in N terminus of Rpb7p/Rpc25p/MJ0397 / RNA polymerase Rpb2, domain 5 / RNA polymerase Rpb2, domain 5 / RNA polymerase Rpb2, domain 4 / RNA polymerase Rpb2, domain 4 / DNA-directed RNA polymerase, M/15kDa subunit / RNA polymerases M/15 Kd subunit / RNA polymerase subunit 9 / DNA-directed RNA polymerase M, 15kDa subunit, conserved site / RNA polymerases M / 15 Kd subunits signature. / DNA-directed RNA polymerase subunit/transcription factor S / : / RNA polymerase, Rpb8 / DNA-directed RNA polymerases I, II, and III subunit RPABC4 / RNA polymerase Rpb8 / RNA polymerase subunit 8 / RNA polymerase, Rpb5, N-terminal / RNA polymerase Rpb5, N-terminal domain superfamily / RNA polymerase Rpb5, N-terminal domain / DNA-directed RNA polymerase subunit RPABC5/Rpb10 / RNA polymerases, subunit N, zinc binding site / RNA polymerase subunit RPB10 / RNA polymerases N / 8 kDa subunit / RNA polymerases N / 8 Kd subunits signature. / DNA-directed RNA polymerase, subunit RPB6 / DNA directed RNA polymerase, 7 kDa subunit / RNA polymerase archaeal subunit P/eukaryotic subunit RPABC4 / RNA polymerase, subunit H/Rpb5, conserved site / RNA polymerases H / 23 Kd subunits signature. / RNA polymerase subunit CX / DNA-directed RNA polymerase, 30-40kDa subunit, conserved site / DNA-directed RNA polymerase subunit Rpo3/Rpb3/RPAC1 / RNA polymerases D / 30 to 40 Kd subunits signature. / DNA-directed RNA polymerase Rpb11, 13-16kDa subunit, conserved site
Similarity search - Domain/homology
FACT complex subunit POB3 / Transcription elongation factor SPT4 / Transcription elongation factor SPT5 / Histone H2B 1.1 / DNA-directed RNA polymerase II subunit RPB1 / Histone H2A type 1 / DNA-directed RNA polymerase II subunit RPB2 / DNA-directed RNA polymerase II subunit RPB3 / DNA-directed RNA polymerase II subunit RPB4 / DNA-directed RNA polymerases I, II, and III subunit RPABC1 ...FACT complex subunit POB3 / Transcription elongation factor SPT4 / Transcription elongation factor SPT5 / Histone H2B 1.1 / DNA-directed RNA polymerase II subunit RPB1 / Histone H2A type 1 / DNA-directed RNA polymerase II subunit RPB2 / DNA-directed RNA polymerase II subunit RPB3 / DNA-directed RNA polymerase II subunit RPB4 / DNA-directed RNA polymerases I, II, and III subunit RPABC1 / DNA-directed RNA polymerases I, II, and III subunit RPABC2 / DNA-directed RNA polymerases I, II, and III subunit RPABC3 / DNA-directed RNA polymerases I, II, and III subunit RPABC5 / DNA-directed RNA polymerase II subunit RPB9 / FACT complex subunit SPT16 / DNA-directed RNA polymerase II subunit RPB7 / DNA-directed RNA polymerase II subunit RPB11 / DNA-directed RNA polymerases I, II, and III subunit RPABC4 / Histone H4 / Histone H3.2
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast) / Xenopus laevis (African clawed frog) / synthetic RNA (others) / synthetic construct (others) / Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.2 Å
AuthorsFarnung L / Ochmann M
Funding supportEuropean Union, Germany, 4 items
OrganizationGrant numberCountry
European Research Council (ERC)693023European Union
German Research Foundation (DFG)EXC 2067/1- 390729940 Germany
German Research Foundation (DFG)SFB860 Germany
German Research Foundation (DFG)SPP2191 Germany
CitationJournal: Nat Struct Mol Biol / Year: 2021
Title: Structural basis of nucleosome transcription mediated by Chd1 and FACT.
Authors: Lucas Farnung / Moritz Ochmann / Maik Engeholm / Patrick Cramer /
Abstract: Efficient transcription of RNA polymerase II (Pol II) through nucleosomes requires the help of various factors. Here we show biochemically that Pol II transcription through a nucleosome is ...Efficient transcription of RNA polymerase II (Pol II) through nucleosomes requires the help of various factors. Here we show biochemically that Pol II transcription through a nucleosome is facilitated by the chromatin remodeler Chd1 and the histone chaperone FACT when the elongation factors Spt4/5 and TFIIS are present. We report cryo-EM structures of transcribing Saccharomyces cerevisiae Pol II-Spt4/5-nucleosome complexes with bound Chd1 or FACT. In the first structure, Pol II transcription exposes the proximal histone H2A-H2B dimer that is bound by Spt5. Pol II has also released the inhibitory DNA-binding region of Chd1 that is poised to pump DNA toward Pol II. In the second structure, Pol II has generated a partially unraveled nucleosome that binds FACT, which excludes Chd1 and Spt5. These results suggest that Pol II progression through a nucleosome activates Chd1, enables FACT binding and eventually triggers transfer of FACT together with histones to upstream DNA.
History
DepositionFeb 19, 2021-
Header (metadata) releaseJul 7, 2021-
Map releaseJul 7, 2021-
UpdateJul 10, 2024-
Current statusJul 10, 2024Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.003
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by cylindrical radius
  • Surface level: 0.003
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-7nky
  • Surface level: 0.003
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_12450.png

Downloads & links

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Map

FileDownload / File: emd_12450.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationMap D
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.05 Å/pix.
x 400 pix.
= 420. Å		1.05 Å/pix.
x 400 pix.
= 420. Å		1.05 Å/pix.
x 400 pix.
= 420. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.05 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.0023 / Movie #1: 0.003
Minimum - Maximum-0.013783644 - 0.04139818
Average (Standard dev.)-0.00009490438 (±0.0008007424)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions400400400
Spacing400400400
CellA=B=C: 419.99997 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.051.051.05
M x/y/z400400400
origin x/y/z0.0000.0000.000
length x/y/z420.000420.000420.000
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS400400400
D min/max/mean-0.0140.041-0.000

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Supplemental data

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Sample components

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Entire : Complex of RNA polymerase II-Spt4/5-FACT-nucleosome

EntireName: Complex of RNA polymerase II-Spt4/5-FACT-nucleosome
Components
  • Complex: Complex of RNA polymerase II-Spt4/5-FACT-nucleosome
    • Complex: RNA (5'-R(P*UP*CP*UP*UP*UP*UP*AP*UP*UP*UP*UP*UP*UP*CP*UP*G)-3')
      • RNA: RNA (5'-R(P*UP*CP*UP*UP*UP*UP*AP*UP*UP*UP*UP*UP*UP*CP*UP*G)-3')
    • Complex: DNA (138-MER)
      • DNA: DNA (138-MER)
    • Complex: DNA (148-MER)
      • DNA: DNA (148-MER)
    • Complex: DNA-directed RNA polymerase II subunit RPB1
      • Protein or peptide: DNA-directed RNA polymerase II subunit RPB1
    • Complex: DNA-directed RNA polymerase II subunit RPB2
      • Protein or peptide: DNA-directed RNA polymerase II subunit RPB2
    • Complex: DNA-directed RNA polymerase II subunit RPB3
      • Protein or peptide: DNA-directed RNA polymerase II subunit RPB3
    • Complex: DNA-directed RNA polymerases I, II, and III subunit RPABC1
      • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC1
    • Complex: DNA-directed RNA polymerases I, II, and III subunit RPABC2
      • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC2
    • Complex: DNA-directed RNA polymerases I, II, and III subunit RPABC3
      • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC3
    • Complex: DNA-directed RNA polymerase II subunit RPB9
      • Protein or peptide: DNA-directed RNA polymerase II subunit RPB9
    • Complex: DNA-directed RNA polymerases I, II, and III subunit RPABC5
      • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC5
    • Complex: DNA-directed RNA polymerase II subunit RPB11
      • Protein or peptide: DNA-directed RNA polymerase II subunit RPB11
    • Complex: DNA-directed RNA polymerases I, II, and III subunit RPABC4
      • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC4
    • Complex: Chromatin elongation factor SPT4
      • Protein or peptide: Chromatin elongation factor SPT4
    • Complex: Transcription elongation factor SPT5
      • Protein or peptide: Transcription elongation factor SPT5
    • Complex: DNA-directed RNA polymerase II subunit RPB4
      • Protein or peptide: DNA-directed RNA polymerase II subunit RPB4
    • Complex: DNA-directed RNA polymerase II subunit RPB7
      • Protein or peptide: DNA-directed RNA polymerase II subunit RPB7
    • Complex: FACT complex subunit POB3
      • Protein or peptide: FACT complex subunit POB3
    • Complex: FACT complex subunit SPT16
      • Protein or peptide: FACT complex subunit SPT16
    • Complex: Histone H3.2
      • Protein or peptide: Histone H3.2
    • Complex: Histone H4
      • Protein or peptide: Histone H4
    • Complex: Histone H2A type 1
      • Protein or peptide: Histone H2A type 1
    • Complex: Histone H2B 1.1
      • Protein or peptide: Histone H2B 1.1
  • Ligand: ZINC ION
  • Ligand: MAGNESIUM ION

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Supramolecule #1: Complex of RNA polymerase II-Spt4/5-FACT-nucleosome

SupramoleculeName: Complex of RNA polymerase II-Spt4/5-FACT-nucleosome / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#23

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Supramolecule #2: RNA (5'-R(P*UP*CP*UP*UP*UP*UP*AP*UP*UP*UP*UP*UP*UP*CP*UP*G)-3')

SupramoleculeName: RNA (5'-R(P*UP*CP*UP*UP*UP*UP*AP*UP*UP*UP*UP*UP*UP*CP*UP*G)-3')
type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1

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Supramolecule #3: DNA (138-MER)

SupramoleculeName: DNA (138-MER) / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #2

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Supramolecule #4: DNA (148-MER)

SupramoleculeName: DNA (148-MER) / type: complex / ID: 4 / Parent: 1 / Macromolecule list: #3

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Supramolecule #5: DNA-directed RNA polymerase II subunit RPB1

SupramoleculeName: DNA-directed RNA polymerase II subunit RPB1 / type: complex / ID: 5 / Parent: 1 / Macromolecule list: #4
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)

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Supramolecule #6: DNA-directed RNA polymerase II subunit RPB2

SupramoleculeName: DNA-directed RNA polymerase II subunit RPB2 / type: complex / ID: 6 / Parent: 1 / Macromolecule list: #5
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)

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Supramolecule #7: DNA-directed RNA polymerase II subunit RPB3

SupramoleculeName: DNA-directed RNA polymerase II subunit RPB3 / type: complex / ID: 7 / Parent: 1 / Macromolecule list: #6
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)

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Supramolecule #8: DNA-directed RNA polymerases I, II, and III subunit RPABC1

SupramoleculeName: DNA-directed RNA polymerases I, II, and III subunit RPABC1
type: complex / ID: 8 / Parent: 1 / Macromolecule list: #7
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)

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Supramolecule #9: DNA-directed RNA polymerases I, II, and III subunit RPABC2

SupramoleculeName: DNA-directed RNA polymerases I, II, and III subunit RPABC2
type: complex / ID: 9 / Parent: 1 / Macromolecule list: #8
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)

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Supramolecule #10: DNA-directed RNA polymerases I, II, and III subunit RPABC3

SupramoleculeName: DNA-directed RNA polymerases I, II, and III subunit RPABC3
type: complex / ID: 10 / Parent: 1 / Macromolecule list: #9
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)

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Supramolecule #11: DNA-directed RNA polymerase II subunit RPB9

SupramoleculeName: DNA-directed RNA polymerase II subunit RPB9 / type: complex / ID: 11 / Parent: 1 / Macromolecule list: #10
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)

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Supramolecule #12: DNA-directed RNA polymerases I, II, and III subunit RPABC5

SupramoleculeName: DNA-directed RNA polymerases I, II, and III subunit RPABC5
type: complex / ID: 12 / Parent: 1 / Macromolecule list: #11

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Supramolecule #13: DNA-directed RNA polymerase II subunit RPB11

SupramoleculeName: DNA-directed RNA polymerase II subunit RPB11 / type: complex / ID: 13 / Parent: 1 / Macromolecule list: #12
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)

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Supramolecule #14: DNA-directed RNA polymerases I, II, and III subunit RPABC4

SupramoleculeName: DNA-directed RNA polymerases I, II, and III subunit RPABC4
type: complex / ID: 14 / Parent: 1 / Macromolecule list: #13
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)

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Supramolecule #15: Chromatin elongation factor SPT4

SupramoleculeName: Chromatin elongation factor SPT4 / type: complex / ID: 15 / Parent: 1 / Macromolecule list: #14
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)

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Supramolecule #16: Transcription elongation factor SPT5

SupramoleculeName: Transcription elongation factor SPT5 / type: complex / ID: 16 / Parent: 1 / Macromolecule list: #15
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)

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Supramolecule #17: DNA-directed RNA polymerase II subunit RPB4

SupramoleculeName: DNA-directed RNA polymerase II subunit RPB4 / type: complex / ID: 17 / Parent: 1 / Macromolecule list: #16
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)

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Supramolecule #18: DNA-directed RNA polymerase II subunit RPB7

SupramoleculeName: DNA-directed RNA polymerase II subunit RPB7 / type: complex / ID: 18 / Parent: 1 / Macromolecule list: #17
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)

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Supramolecule #19: FACT complex subunit POB3

SupramoleculeName: FACT complex subunit POB3 / type: complex / ID: 19 / Parent: 1 / Macromolecule list: #18
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)

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Supramolecule #20: FACT complex subunit SPT16

SupramoleculeName: FACT complex subunit SPT16 / type: complex / ID: 20 / Parent: 1 / Macromolecule list: #19
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)

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Supramolecule #21: Histone H3.2

SupramoleculeName: Histone H3.2 / type: complex / ID: 21 / Parent: 1 / Macromolecule list: #20
Source (natural)Organism: Xenopus laevis (African clawed frog)

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Supramolecule #22: Histone H4

SupramoleculeName: Histone H4 / type: complex / ID: 22 / Parent: 1 / Macromolecule list: #21
Source (natural)Organism: Xenopus laevis (African clawed frog)

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Supramolecule #23: Histone H2A type 1

SupramoleculeName: Histone H2A type 1 / type: complex / ID: 23 / Parent: 1 / Macromolecule list: #22
Source (natural)Organism: Xenopus laevis (African clawed frog)

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Supramolecule #24: Histone H2B 1.1

SupramoleculeName: Histone H2B 1.1 / type: complex / ID: 24 / Parent: 1 / Macromolecule list: #23
Source (natural)Organism: Xenopus laevis (African clawed frog)

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Macromolecule #1: RNA (5'-R(P*UP*CP*UP*UP*UP*UP*AP*UP*UP*UP*UP*UP*UP*CP*UP*G)-3')

MacromoleculeName: RNA (5'-R(P*UP*CP*UP*UP*UP*UP*AP*UP*UP*UP*UP*UP*UP*CP*UP*G)-3')
type: rna / ID: 1 / Number of copies: 1
Source (natural)Organism: synthetic RNA (others)
Molecular weightTheoretical: 4.913807 KDa
SequenceString:
UCUUUUAUUU UUUCUG

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Macromolecule #2: DNA (138-MER)

MacromoleculeName: DNA (138-MER) / type: dna / ID: 2 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 42.792227 KDa
SequenceString: (DC)(DT)(DA)(DG)(DC)(DA)(DC)(DA)(DG)(DG) (DG)(DT)(DG)(DT)(DC)(DT)(DG)(DC)(DT)(DT) (DA)(DT)(DC)(DG)(DG)(DT)(DA)(DG)(DA) (DG)(DT)(DG)(DT)(DC)(DA)(DA)(DT)(DC)(DC) (DC) (DC)(DT)(DT)(DG)(DG)(DC) ...String:
(DC)(DT)(DA)(DG)(DC)(DA)(DC)(DA)(DG)(DG) (DG)(DT)(DG)(DT)(DC)(DT)(DG)(DC)(DT)(DT) (DA)(DT)(DC)(DG)(DG)(DT)(DA)(DG)(DA) (DG)(DT)(DG)(DT)(DC)(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)(DG)(DA)(DT)

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Macromolecule #3: DNA (148-MER)

MacromoleculeName: DNA (148-MER) / type: dna / ID: 3 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 45.537082 KDa
SequenceString: (DA)(DT)(DC)(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) ...String:
(DA)(DT)(DC)(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)(DG) (DA)(DC)(DA)(DC)(DT)(DC)(DT)(DA)(DC)(DC) (DG)(DA)(DT)(DA)(DA) (DG)(DC)(DA)(DG) (DA)(DC)(DG)(DA)(DC)(DA)(DG)(DA)(DA)(DA) (DA)(DA)(DA)(DC)(DC)(DC) (DT)(DG)(DT) (DG)(DC)(DT)(DA)(DG)

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Macromolecule #4: DNA-directed RNA polymerase II subunit RPB1

MacromoleculeName: DNA-directed RNA polymerase II subunit RPB1 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA-directed RNA polymerase
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast) / Strain: BJ5464
Molecular weightTheoretical: 191.821578 KDa
SequenceString: MVGQQYSSAP LRTVKEVQFG LFSPEEVRAI SVAKIRFPET MDETQTRAKI GGLNDPRLGS IDRNLKCQTC QEGMNECPGH FGHIDLAKP VFHVGFIAKI KKVCECVCMH CGKLLLDEHN ELMRQALAIK DSKKRFAAIW TLCKTKMVCE TDVPSEDDPT Q LVSRGGCG ...String:
MVGQQYSSAP LRTVKEVQFG LFSPEEVRAI SVAKIRFPET MDETQTRAKI GGLNDPRLGS IDRNLKCQTC QEGMNECPGH FGHIDLAKP VFHVGFIAKI KKVCECVCMH CGKLLLDEHN ELMRQALAIK DSKKRFAAIW TLCKTKMVCE TDVPSEDDPT Q LVSRGGCG NTQPTIRKDG LKLVGSWKKD RATGDADEPE LRVLSTEEIL NIFKHISVKD FTSLGFNEVF SRPEWMILTC LP VPPPPVR PSISFNESQR GEDDLTFKLA DILKANISLE TLEHNGAPHH AIEEAESLLQ FHVATYMDND IAGQPQALQK SGR PVKSIR ARLKGKEGRI RGNLMGKRVD FSARTVISGD PNLELDQVGV PKSIAKTLTY PEVVTPYNID RLTQLVRNGP NEHP GAKYV IRDSGDRIDL RYSKRAGDIQ LQYGWKVERH IMDNDPVLFN RQPSLHKMSM MAHRVKVIPY STFRLNLSVT SPYNA DFDG DEMNLHVPQS EETRAELSQL CAVPLQIVSP QSNKPCMGIV QDTLCGIRKL TLRDTFIELD QVLNMLYWVP DWDGVI PTP AIIKPKPLWS GKQILSVAIP NGIHLQRFDE GTTLLSPKDN GMLIIDGQII FGVVEKKTVG SSNGGLIHVV TREKGPQ VC AKLFGNIQKV VNFWLLHNGF STGIGDTIAD GPTMREITET IAEAKKKVLD VTKEAQANLL TAKHGMTLRE SFEDNVVR F LNEARDKAGR LAEVNLKDLN NVKQMVMAGS KGSFINIAQM SACVGQQSVE GKRIAFGFVD RTLPHFSKDD YSPESKGFV ENSYLRGLTP QEFFFHAMGG REGLIDTAVK TAETGYIQRR LVKALEDIMV HYDNTTRNSL GNVIQFIYGE DGMDAAHIEK QSLDTIGGS DAAFEKRYRV DLLNTDHTLD PSLLESGSEI LGDLKLQVLL DEEYKQLVKD RKFLREVFVD GEANWPLPVN I RRIIQNAQ QTFHIDHTKP SDLTIKDIVL GVKDLQENLL VLRGKNEIIQ NAQRDAVTLF CCLLRSRLAT RRVLQEYRLT KQ AFDWVLS NIEAQFLRSV VHPGEMVGVL AAQSIGEPAT QMTLNTFHFA GVASKKVTSG VPRLKEILNV AKNMKTPSLT VYL EPGHAA DQEQAKLIRS AIEHTTLKSV TIASEIYYDP DPRSTVIPED EEIIQLHFSL LDEEAEQSFD QQSPWLLRLE LDRA AMNDK DLTMGQVGER IKQTFKNDLF VIWSEDNDEK LIIRCRVVRP KSLDAETEAE EDHMLKKIEN TMLENITLRG VENIE RVVM MKYDRKVPSP TGEYVKEPEW VLETDGVNLS EVMTVPGIDP TRIYTNSFID IMEVLGIEAG RAALYKEVYN VIASDG SYV NYRHMALLVD VMTTQGGLTS VTRHGFNRSN TGALMRCSFE ETVEILFEAG ASAELDDCRG VSENVILGQM APIGTGA FD VMIDEESLVK YMPEQKITEI EDGQDGGVTP YSNESGLVNA DLDVKDELMF SPLVDSGSND AMAGGFTAYG GADYGEAT S PFGAYGEAPT SPGFGVSSPG FSPTSPTYSP TSPAYSPTSP SYSPTSPSYS PTSPSYSPTS PSYSPTSPSY SPTSPSYSP TSPSYSPTSP SYSPTSPSYS PTSPSYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPA YSPTSPSYSP TSPSYSPTSP SYSPTSPSY SPTSPNYSPT SPSYSPTSPG YSPGSPAYSP KQDEQKHNEN ENSR

UniProtKB: DNA-directed RNA polymerase II subunit RPB1

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Macromolecule #5: DNA-directed RNA polymerase II subunit RPB2

MacromoleculeName: DNA-directed RNA polymerase II subunit RPB2 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA-directed RNA polymerase
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast) / Strain: BJ5464
Molecular weightTheoretical: 138.937297 KDa
SequenceString: MSDLANSEKY YDEDPYGFED ESAPITAEDS WAVISAFFRE KGLVSQQLDS FNQFVDYTLQ DIICEDSTLI LEQLAQHTTE SDNISRKYE ISFGKIYVTK PMVNESDGVT HALYPQEARL RNLTYSSGLF VDVKKRTYEA IDVPGRELKY ELIAEESEDD S ESGKVFIG ...String:
MSDLANSEKY YDEDPYGFED ESAPITAEDS WAVISAFFRE KGLVSQQLDS FNQFVDYTLQ DIICEDSTLI LEQLAQHTTE SDNISRKYE ISFGKIYVTK PMVNESDGVT HALYPQEARL RNLTYSSGLF VDVKKRTYEA IDVPGRELKY ELIAEESEDD S ESGKVFIG RLPIMLRSKN CYLSEATESD LYKLKECPFD MGGYFIINGS EKVLIAQERS AGNIVQVFKK AAPSPISHVA EI RSALEKG SRFISTLQVK LYGREGSSAR TIKATLPYIK QDIPIVIIFR ALGIIPDGEI LEHICYDVND WQMLEMLKPC VED GFVIQD RETALDFIGR RGTALGIKKE KRIQYAKDIL QKEFLPHITQ LEGFESRKAF FLGYMINRLL LCALDRKDQD DRDH FGKKR LDLAGPLLAQ LFKTLFKKLT KDIFRYMQRT VEEAHDFNMK LAINAKTITS GLKYALATGN WGEQKKAMSS RAGVS QVLN RYTYSSTLSH LRRTNTPIGR DGKLAKPRQL HNTHWGLVCP AETPEGQACG LVKNLSLMSC ISVGTDPMPI ITFLSE WGM EPLEDYVPHQ SPDATRVFVN GVWHGVHRNP ARLMETLRTL RRKGDINPEV SMIRDIREKE LKIFTDAGRV YRPLFIV ED DESLGHKELK VRKGHIAKLM ATEYQDIEGG FEDVEEYTWS SLLNEGLVEY IDAEEEESIL IAMQPEDLEP AEANEEND L DVDPAKRIRV SHHATTFTHC EIHPSMILGV AASIIPFPDH NQSPRNTYQS AMGKQAMGVF LTNYNVRMDT MANILYYPQ KPLGTTRAME YLKFRELPAG QNAIVAIACY SGYNQEDSMI MNQSSIDRGL FRSLFFRSYM DQEKKYGMSI TETFEKPQRT NTLRMKHGT YDKLDDDGLI APGVRVSGED VIIGKTTPIS PDEEELGQRT AYHSKRDAST PLRSTENGIV DQVLVTTNQD G LKFVKVRV RTTKIPQIGD KFASRHGQKG TIGITYRRED MPFTAEGIVP DLIINPHAIP SRMTVAHLIE CLLSKVAALS GN EGDASPF TDITVEGISK LLREHGYQSR GFEVMYNGHT GKKLMAQIFF GPTYYQRLRH MVDDKIHARA RGPMQVLTRQ PVE GRSRDG GLRFGEMERD CMIAHGAASF LKERLMEASD AFRVHICGIC GLMTVIAKLN HNQFECKGCD NKIDIYQIHI PYAA KLLFQ ELMAMNITPR LYTDRSRDF

UniProtKB: DNA-directed RNA polymerase II subunit RPB2

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Macromolecule #6: DNA-directed RNA polymerase II subunit RPB3

MacromoleculeName: DNA-directed RNA polymerase II subunit RPB3 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast) / Strain: BJ5464
Molecular weightTheoretical: 35.330457 KDa
SequenceString: MSEEGPQVKI REASKDNVDF ILSNVDLAMA NSLRRVMIAE IPTLAIDSVE VETNTTVLAD EFIAHRLGLI PLQSMDIEQL EYSRDCFCE DHCDKCSVVL TLQAFGESES TTNVYSKDLV IVSNLMGRNI GHPIIQDKEG NGVLICKLRK GQELKLTCVA K KGIAKEHA ...String:
MSEEGPQVKI REASKDNVDF ILSNVDLAMA NSLRRVMIAE IPTLAIDSVE VETNTTVLAD EFIAHRLGLI PLQSMDIEQL EYSRDCFCE DHCDKCSVVL TLQAFGESES TTNVYSKDLV IVSNLMGRNI GHPIIQDKEG NGVLICKLRK GQELKLTCVA K KGIAKEHA KWGPAAAIEF EYDPWNKLKH TDYWYEQDSA KEWPQSKNCE YEDPPNEGDP FDYKAQADTF YMNVESVGSI PV DQVVVRG IDTLQKKVAS ILLALTQMDQ DKVNFASGDN NTASNMLGSN EDVMMTGAEQ DPYSNASQMG NTGSGGYDNA W

UniProtKB: DNA-directed RNA polymerase II subunit RPB3

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Macromolecule #7: DNA-directed RNA polymerases I, II, and III subunit RPABC1

MacromoleculeName: DNA-directed RNA polymerases I, II, and III subunit RPABC1
type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast) / Strain: BJ5464
Molecular weightTheoretical: 25.117094 KDa
SequenceString: MDQENERNIS RLWRAFRTVK EMVKDRGYFI TQEEVELPLE DFKAKYCDSM GRPQRKMMSF QANPTEESIS KFPDMGSLWV EFCDEPSVG VKTMKTFVIH IQEKNFQTGI FVYQNNITPS AMKLVPSIPP ATIETFNEAA LVVNITHHEL VPKHIRLSSD E KRELLKRY ...String:
MDQENERNIS RLWRAFRTVK EMVKDRGYFI TQEEVELPLE DFKAKYCDSM GRPQRKMMSF QANPTEESIS KFPDMGSLWV EFCDEPSVG VKTMKTFVIH IQEKNFQTGI FVYQNNITPS AMKLVPSIPP ATIETFNEAA LVVNITHHEL VPKHIRLSSD E KRELLKRY RLKESQLPRI QRADPVALYL GLKRGEVVKI IRKSETSGRY ASYRICM

UniProtKB: DNA-directed RNA polymerases I, II, and III subunit RPABC1

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Macromolecule #8: DNA-directed RNA polymerases I, II, and III subunit RPABC2

MacromoleculeName: DNA-directed RNA polymerases I, II, and III subunit RPABC2
type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast) / Strain: BJ5464
Molecular weightTheoretical: 17.931834 KDa
SequenceString:
MSDYEEAFND GNENFEDFDV EHFSDEETYE EKPQFKDGET TDANGKTIVT GGNGPEDFQQ HEQIRRKTLK EKAIPKDQRA TTPYMTKYE RARILGTRAL QISMNAPVFV DLEGETDPLR IAMKELAEKK IPLVIRRYLP DGSFEDWSVE ELIVDL

UniProtKB: DNA-directed RNA polymerases I, II, and III subunit RPABC2

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Macromolecule #9: DNA-directed RNA polymerases I, II, and III subunit RPABC3

MacromoleculeName: DNA-directed RNA polymerases I, II, and III subunit RPABC3
type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast) / Strain: BJ5464
Molecular weightTheoretical: 16.525363 KDa
SequenceString:
MSNTLFDDIF QVSEVDPGRY NKVCRIEAAS TTQDQCKLTL DINVELFPVA AQDSLTVTIA SSLNLEDTPA NDSSATRSWR PPQAGDRSL ADDYDYVMYG TAYKFEEVSK DLIAVYYSFG GLLMRLEGNY RNLNNLKQEN AYLLIRR

UniProtKB: DNA-directed RNA polymerases I, II, and III subunit RPABC3

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Macromolecule #10: DNA-directed RNA polymerase II subunit RPB9

MacromoleculeName: DNA-directed RNA polymerase II subunit RPB9 / type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast) / Strain: BJ5464
Molecular weightTheoretical: 14.308161 KDa
SequenceString:
MTTFRFCRDC NNMLYPREDK ENNRLLFECR TCSYVEEAGS PLVYRHELIT NIGETAGVVQ DIGSDPTLPR SDRECPKCHS RENVFFQSQ QRRKDTSMVL FFVCLSCSHI FTSDQKNKRT QFS

UniProtKB: DNA-directed RNA polymerase II subunit RPB9

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Macromolecule #11: DNA-directed RNA polymerases I, II, and III subunit RPABC5

MacromoleculeName: DNA-directed RNA polymerases I, II, and III subunit RPABC5
type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast) / Strain: BJ5464
Molecular weightTheoretical: 8.290732 KDa
SequenceString:
MIVPVRCFSC GKVVGDKWES YLNLLQEDEL DEGTALSRLG LKRYCCRRMI LTHVDLIEKF LRYNPLEKRD

UniProtKB: DNA-directed RNA polymerases I, II, and III subunit RPABC5

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Macromolecule #12: DNA-directed RNA polymerase II subunit RPB11

MacromoleculeName: DNA-directed RNA polymerase II subunit RPB11 / type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast) / Strain: BJ5464
Molecular weightTheoretical: 13.633493 KDa
SequenceString:
MNAPDRFELF LLGEGESKLK IDPDTKAPNA VVITFEKEDH TLGNLIRAEL LNDRKVLFAA YKVEHPFFAR FKLRIQTTEG YDPKDALKN ACNSIINKLG ALKTNFETEW NLQTLAADDA F

UniProtKB: DNA-directed RNA polymerase II subunit RPB11

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Macromolecule #13: DNA-directed RNA polymerases I, II, and III subunit RPABC4

MacromoleculeName: DNA-directed RNA polymerases I, II, and III subunit RPABC4
type: protein_or_peptide / ID: 13 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast) / Strain: BJ5464
Molecular weightTheoretical: 7.729969 KDa
SequenceString:
MSREGFQIPT NLDAAAAGTS QARTATLKYI CAECSSKLSL SRTDAVRCKD CGHRILLKAR TKRLVQFEAR

UniProtKB: DNA-directed RNA polymerases I, II, and III subunit RPABC4

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Macromolecule #14: Chromatin elongation factor SPT4

MacromoleculeName: Chromatin elongation factor SPT4 / type: protein_or_peptide / ID: 14 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast) / Strain: BJ5464
Molecular weightTheoretical: 11.168772 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString:
MSSERACMLC GIVQTTNEFN RDGCPNCQGI FEEAGVSTME CTSPSFEGLV GMCKPTKSWV AKWLSVDHSI AGMYAIKVDG RLPAEVVEL LPHYKPRDGS QVE

UniProtKB: Transcription elongation factor SPT4

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Macromolecule #15: Transcription elongation factor SPT5

MacromoleculeName: Transcription elongation factor SPT5 / type: protein_or_peptide / ID: 15 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 115.929109 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MSDNSDTNVS MQDHDQQFAD PVVVPQSTDT KDENTSDKDT VDSGNVTTTE STERAESTSN IPPLDGEEKE AKSEPQQPED NAETAATEQ VSSSNGPATD DAQATLNTDS SEANEIVKKE EGSDERKRPR EEDTKNSDGD TKDEGDNKDE DDDEDDDDDD D DEDDDDEA ...String:
MSDNSDTNVS MQDHDQQFAD PVVVPQSTDT KDENTSDKDT VDSGNVTTTE STERAESTSN IPPLDGEEKE AKSEPQQPED NAETAATEQ VSSSNGPATD DAQATLNTDS SEANEIVKKE EGSDERKRPR EEDTKNSDGD TKDEGDNKDE DDDEDDDDDD D DEDDDDEA PTKRRRQERN RFLDIEAEVS DDEDEDEDEE DSELVREGFI THGDDEDDEA SAPGARRDDR LHRQLDQDLN KT SEEDAQR LAKELRERYG RSSSKQYRAA AQDGYVPQRF LLPSVDTATI WGVRCRPGKE KELIRKLLKK KFNLDRAMGK KKL KILSIF QRDNYTGRIY IEAPKQSVIE KFCNGVPDIY ISQKLLIPVQ ELPLLLKPNL SDDVALEEGS YVRIKRGIYK GDLA MVDQI SENNLEVMLK IVPRLDYGKF DEIDPTTQQR KSRRPTFAHR APPQLFNPTM ALRLDQANLY KRDDRHFTYK NEDYI DGYL YKSFRIQHVE TKNIQPTVEE LARFGSKEGA VDLTSVSQSI KKAQAAKVTF QPGDRIEVLN GEQRGSKGIV TRTTKD IAT IKLNGFTTPL EFPISTLRKI FEPGDHVTVI NGEHQGDAGL VLMVEQGQVT FMSTQTSREV TITANNLSKS IDTTATS SE YALHDIVELS AKNVACIIQA GHDIFKVIDE TGKVSTITKG SILSKINTAR ARVSSVDANG NEIKIGDTIV EKVGSRRE G QVLYIQTQQI FVVSKKIVEN AGVFVVNPSN VEAVASKDNM LSNKMDLSKM NPEIISKMGP PSSKTFQQPI QSRGGREVA LGKTVRIRSA GYKGQLGIVK DVNGDKATVE LHSKNKHITI DKHKLTYYNR EGGEGITYDE LVNRRGRVPQ ARMGPSYVSA PRNMATGGI AAGAAATSSG LSGGMTPGWS SFDGGKTPAV NAHGGSGGGG VSSWGGASTW GGQGNGGASA WGGAGGGASA W GGQGTGAT STWGGASAWG NKSSWGGAST WASGGESNGA MSTWGGTGDR SAYGGASTWG GNNNNKSTRD GGASAWGNQD DG NRSAWNN QGNKSNYGGN STWGGHF

UniProtKB: Transcription elongation factor SPT5

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Macromolecule #16: DNA-directed RNA polymerase II subunit RPB4

MacromoleculeName: DNA-directed RNA polymerase II subunit RPB4 / type: protein_or_peptide / ID: 16 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast) / Strain: BJ5464
Molecular weightTheoretical: 25.451191 KDa
SequenceString: MNVSTSTFQT RRRRLKKVEE EENAATLQLG QEFQLKQINH QGEEEELIAL NLSEARLVIK EALVERRRAF KRSQKKHKKK HLKHENAND ETTAVEDEDD DLDEDDVNAD DDDFMHSETR EKELESIDVL LEQTTGGNNK DLKNTMQYLT NFSRFRDQET V GAVIQLLK ...String:
MNVSTSTFQT RRRRLKKVEE EENAATLQLG QEFQLKQINH QGEEEELIAL NLSEARLVIK EALVERRRAF KRSQKKHKKK HLKHENAND ETTAVEDEDD DLDEDDVNAD DDDFMHSETR EKELESIDVL LEQTTGGNNK DLKNTMQYLT NFSRFRDQET V GAVIQLLK STGLHPFEVA QLGSLACDTA DEAKTLIPSL NNKISDDELE RILKELSNLE TLY

UniProtKB: DNA-directed RNA polymerase II subunit RPB4

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Macromolecule #17: DNA-directed RNA polymerase II subunit RPB7

MacromoleculeName: DNA-directed RNA polymerase II subunit RPB7 / type: protein_or_peptide / ID: 17 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast) / Strain: BJ5464
Molecular weightTheoretical: 19.081053 KDa
SequenceString:
MFFIKDLSLN ITLHPSFFGP RMKQYLKTKL LEEVEGSCTG KFGYILCVLD YDNIDIQRGR ILPTDGSAEF NVKYRAVVFK PFKGEVVDG TVVSCSQHGF EVQVGPMKVF VTKHLMPQDL TFNAGSNPPS YQSSEDVITI KSRIRVKIEG CISQVSSIHA I GSIKEDYL GAI

UniProtKB: DNA-directed RNA polymerase II subunit RPB7

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Macromolecule #18: FACT complex subunit POB3

MacromoleculeName: FACT complex subunit POB3 / type: protein_or_peptide / ID: 18 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast) / Strain: BJ5464
Molecular weightTheoretical: 63.068594 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MSTDFDRIYL NQSKFSGRFR IADSGLGWKI STSGGSAANQ ARKPFLLPAT ELSTVQWSRG CRGYDLKINT KNQGVIQLDG FSQDDYNLI KNDFHRRFNI QVEQREHSLR GWNWGKTDLA RNEMVFALNG KPTFEIPYAR INNTNLTSKN EVGIEFNIQD E EYQPAGDE ...String:
MSTDFDRIYL NQSKFSGRFR IADSGLGWKI STSGGSAANQ ARKPFLLPAT ELSTVQWSRG CRGYDLKINT KNQGVIQLDG FSQDDYNLI KNDFHRRFNI QVEQREHSLR GWNWGKTDLA RNEMVFALNG KPTFEIPYAR INNTNLTSKN EVGIEFNIQD E EYQPAGDE LVEMRFYIPG VIQTNVDENM TKKEESSNEV VPKKEDGAEG EDVQMAVEEK SMAEAFYEEL KEKADIGEVA GD AIVSFQD VFFTTPRGRY DIDIYKNSIR LRGKTYEYKL QHRQIQRIVS LPKADDIHHL LVLAIEPPLR QGQTTYPFLV LQF QKDEET EVQLNLEDED YEENYKDKLK KQYDAKTHIV LSHVLKGLTD RRVIVPGEYK SKYDQCAVSC SFKANEGYLY PLDN AFFFL TKPTLYIPFS DVSMVNISRA GQTSTSSRTF DLEVVLRSNR GSTTFANISK EEQQLLEQFL KSKNLRVKNE DREVQ ERLQ TALGSDSDEE DINMGSAGED DESVDEDFQV SSDNDADEVA EEFDSDAALS DAEGGSDEER PSKKPKVE

UniProtKB: FACT complex subunit POB3

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Macromolecule #19: FACT complex subunit SPT16

MacromoleculeName: FACT complex subunit SPT16 / type: protein_or_peptide / ID: 19 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: BJ5464
Molecular weightTheoretical: 118.776984 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MEELNIDFDV FKKRIELLYS KYNEFEGSPN SLLFVLGSSN AENPYQKTTI LHNWLLSYEF PATLIALVPG KVIIITSSAK AKHLQKAID LFKDPESKIT LELWQRNNKE PELNKKLFDD VIALINSAGK TVGIPEKDSY QGKFMTEWNP VWEAAVKENE F NVIDISLG ...String:
MEELNIDFDV FKKRIELLYS KYNEFEGSPN SLLFVLGSSN AENPYQKTTI LHNWLLSYEF PATLIALVPG KVIIITSSAK AKHLQKAID LFKDPESKIT LELWQRNNKE PELNKKLFDD VIALINSAGK TVGIPEKDSY QGKFMTEWNP VWEAAVKENE F NVIDISLG LSKVWEVKDV NEQAFLSVSS KGSDKFMDLL SNEMVRAVDE ELKITNAKLS DKIENKIDDV KFLKQLSPDL SA LCPPNYK FNFDLLDWTY SPIIQSGKKF DLRVSARSTN DQLYGNGCIL ASCGIRYNNY CSNITRTFLI DPSEEMANNY DFL LTLQKE IVTNILKPGR TPKEVYESVI EYIEKTKPEL VPNFTKNIGS LIGLEFRDSN FILNVKNDYR KIQRGDCFNI SFGF NNLKD SQSANNYALQ LADTVQIPLD ETEPPRFLTN YTKAKSQISF YFNNEEEDNN KKKSSPATKV PSKPDRNSKI LRTKL RGEA RGGAEDAQKE QIRKENQKKL HEKLEKNGLL RFSAADANGP DSEPRQYFKK YESYVRDSQL PTNIRDLRIH VDWKSQ TII LPIYGRPVPF HINSYKNGSK NEEGEYTYLR LNFNSPGSSG GISKKVEELP YEESADNQFV RSITLRSKDG DRMSETF KQ IADLKKEATK REQERKALAD VVQQDKLIEN KTGRTKRLDQ IFVRPNPDTK RVPSTVFIHE NGIRFQSPLR TDSRIDIL F SNIKNLIFQS CKGELIVVIH IHLKNPILMG KKKIQDVQFY REASDMSVDE TGGGRRGQSR FRRYGDEDEL EQEQEERRK RAALDKEFKY FADAIAEASN GLLTVENTFR DLGFQGVPNR SAVFCMPTTD CLVQLIEPPF LVINLEEVEI CILERVQFGL KNFDMVFVY KDFNKPVTHI NTVPIESLDF LKQWLTDMDI PYTVSTINLN WATIMKSLQD DPYQFFLDGG WNFLATGSDD E ASDESEEE VSEYEASEDD VSDESAFSED EEGSEVDDDI SGDESEDYTG DESEEGEDWD ELEKKAARAD RGANFRD

UniProtKB: FACT complex subunit SPT16

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Macromolecule #20: Histone H3.2

MacromoleculeName: Histone H3.2 / type: protein_or_peptide / ID: 20 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Xenopus laevis (African clawed frog)
Molecular weightTheoretical: 15.435126 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSA VMALQEASEA YLVALFEDTN LCAIHAKRVT IMPKDIQLAR RIRGERA

UniProtKB: Histone H3.2

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Macromolecule #21: Histone H4

MacromoleculeName: Histone H4 / type: protein_or_peptide / ID: 21 / 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

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Macromolecule #22: Histone H2A type 1

MacromoleculeName: Histone H2A type 1 / type: protein_or_peptide / ID: 22 / 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 type 1

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Macromolecule #23: Histone H2B 1.1

MacromoleculeName: Histone H2B 1.1 / type: protein_or_peptide / ID: 23 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Xenopus laevis (African clawed frog)
Molecular weightTheoretical: 13.655948 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MAKSAPAPKK GSKKAVTKTQ KKDGKKRRKT RKESYAIYVY KVLKQVHPDT GISSKAMSIM NSFVNDVFER IAGEASRLAH YNKRSTITS REIQTAVRLL LPGELAKHAV SEGTKAVTKY TSAK

UniProtKB: Histone H2B 1.1

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Macromolecule #24: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 24 / Number of copies: 9 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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Macromolecule #25: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 25 / Number of copies: 1 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.4
GridModel: Quantifoil R2/2 / Material: GOLD / Mesh: 200
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 40.25 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: OTHER
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 47138
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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