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- EMDB-13015: Pol II-CSB-CRL4CSA-UVSSA-SPT6-PAF (Structure 4) -

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Basic information

Entry
Database: EMDB / ID: EMD-13015
TitlePol II-CSB-CRL4CSA-UVSSA-SPT6-PAF (Structure 4)
Map dataThe main map.
Sample
  • Complex: Transcribing Pol II bound to CSB, CRL4CSA, UVSSA, PAF and SPT6.
    • Complex: DNA-directed RNA polymerase with RNA_pol_L_2 and RNA polymerase
      • Protein or peptide: x 12 types
    • Complex: Supplementary proteins
      • Protein or peptide: x 12 types
    • Complex: NTS, RNA, TS
      • DNA: x 2 types
      • RNA: x 1 types
    • Complex: E3 ubiquitin-protein ligase RBX1
      • Protein or peptide: x 1 types
  • Ligand: x 2 types
Function / homology
Function and homology information


Prolactin receptor signaling / negative regulation of double-strand break repair via nonhomologous end joining / regulation of transcription-coupled nucleotide-excision repair / Regulation of BACH1 activity / Recognition of DNA damage by PCNA-containing replication complex / blastocyst growth / inner cell mass cell differentiation / Ski complex / DNA Damage Recognition in GG-NER / Formation of TC-NER Pre-Incision Complex ...Prolactin receptor signaling / negative regulation of double-strand break repair via nonhomologous end joining / regulation of transcription-coupled nucleotide-excision repair / Regulation of BACH1 activity / Recognition of DNA damage by PCNA-containing replication complex / blastocyst growth / inner cell mass cell differentiation / Ski complex / DNA Damage Recognition in GG-NER / Formation of TC-NER Pre-Incision Complex / RNA polymerase II C-terminal domain phosphoserine binding / Dual Incision in GG-NER / Dual incision in TC-NER / positive regulation of mRNA 3'-end processing / Formation of Incision Complex in GG-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / nucleotide-excision repair complex / mRNA decay by 3' to 5' exoribonuclease / Regulation of RAS by GAPs / Regulation of RUNX2 expression and activity / Degradation of GLI1 by the proteasome / GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2 / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / Degradation of DVL / Orc1 removal from chromatin / nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay / Cdc73/Paf1 complex / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / Hedgehog 'on' state / regulation of isotype switching / Degradation of beta-catenin by the destruction complex / regulation of mRNA export from nucleus / regulation of muscle cell differentiation / endodermal cell fate commitment / eukaryotic initiation factor 4E binding / negative regulation of myeloid cell differentiation / negative regulation of granulocyte differentiation / blastocyst hatching / Interleukin-1 signaling / positive regulation of cell cycle G1/S phase transition / regulation of transcription elongation by RNA polymerase II / KEAP1-NFE2L2 pathway / anaphase-promoting complex / nucleosome organization / GLI3 is processed to GLI3R by the proteasome / B-WICH complex / single strand break repair / trophectodermal cell differentiation / regulation of mRNA processing / cullin-RING-type E3 NEDD8 transferase / Neddylation / Antigen processing: Ubiquitination & Proteasome degradation / cullin-RING ubiquitin ligase complex / positive regulation by virus of viral protein levels in host cell / DNA protection / regulation of DNA damage checkpoint / regulation of nucleotide-excision repair / mRNA 3'-end processing / Cul7-RING ubiquitin ligase complex / ubiquitin-dependent protein catabolic process via the C-end degron rule pathway / epigenetic programming in the zygotic pronuclei / B-WICH complex positively regulates rRNA expression / RNA Polymerase I Transcription Initiation / RNA Polymerase I Promoter Escape / RNA Polymerase I Transcription Termination / RNA Polymerase III Transcription Initiation From Type 1 Promoter / RNA Polymerase III Transcription Initiation From Type 2 Promoter / RNA Polymerase III Transcription Initiation From Type 3 Promoter / Formation of RNA Pol II elongation complex / Formation of the Early Elongation Complex / Transcriptional regulation by small RNAs / RNA Polymerase II Pre-transcription Events / TP53 Regulates Transcription of DNA Repair Genes / FGFR2 alternative splicing / RNA polymerase II transcribes snRNA genes / mRNA Capping / mRNA Splicing - Major Pathway / mRNA Splicing - Minor Pathway / Processing of Capped Intron-Containing Pre-mRNA / RNA Polymerase II Promoter Escape / RNA Polymerase II Transcription Pre-Initiation And Promoter Opening / RNA Polymerase II Transcription Initiation / RNA Polymerase II Transcription Elongation / RNA Polymerase II Transcription Initiation And Promoter Clearance / RNA Pol II CTD phosphorylation and interaction with CE / Estrogen-dependent gene expression / spindle assembly involved in female meiosis / double-strand break repair via classical nonhomologous end joining / Formation of TC-NER Pre-Incision Complex / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / response to superoxide / blastocyst formation / Cul4-RING E3 ubiquitin ligase complex / VCB complex / photoreceptor cell maintenance / UV-damage excision repair / positive regulation of protein autoubiquitination / : / :
Similarity search - Function
UV-stimulated scaffold protein A / : / : / Uncharacterized conserved protein (DUF2043) / UVSSA N-terminal domain / Paf1 complex subunit Cdc73, N-terminal domain / Paf1 complex subunit CDC73 N-terminal / DNA excision repair protein Rad28/ERCC8/Ckn1/ATCSA-1 / HHH domain 9 / HHH domain ...UV-stimulated scaffold protein A / : / : / Uncharacterized conserved protein (DUF2043) / UVSSA N-terminal domain / Paf1 complex subunit Cdc73, N-terminal domain / Paf1 complex subunit CDC73 N-terminal / DNA excision repair protein Rad28/ERCC8/Ckn1/ATCSA-1 / HHH domain 9 / HHH domain / Leo1-like protein / Leo1-like protein / Cdc73/Parafibromin / RNA polymerase-associated protein Ctr9 / Cell division control protein 73, C-terminal / Cell division control protein 73, C-terminal domain superfamily / RNA pol II accessory factor, Cdc73 family, C-terminal / RNA polymerase II associated factor Paf1 / Paf1 / YqgF/RNase H-like domain / Likely ribonuclease with RNase H fold. / Spt6 acidic, N-terminal domain / Helix-turn-helix DNA-binding domain of Spt6 / Transcription elongation factor Spt6, YqgF domain / Transcription elongation factor Spt6, helix-hairpin-helix motif / Spt6, SH2 domain, C terminus / Acidic N-terminal SPT6 / Helix-hairpin-helix motif / Holliday-junction resolvase-like of SPT6 / Helix-turn-helix DNA-binding domain of SPT6 / Tex-like protein, HTH domain superfamily / Tex-like domain superfamily / Spt6, Death-like domain / Transcription elongation factor Spt6 / Spt6, SH2 domain, N terminus / Spt6, SH2 domain / SH2 domain / YqgF/RNase H-like domain superfamily / Tetratricopeptide repeat / ENTH/VHS / Zinc finger, RING-H2-type / RING-H2 zinc finger domain / Tetratricopeptide repeat / RNA-binding domain, S1 / Cullin protein neddylation domain / Cullin, conserved site / Cullin family signature. / Cullin / RuvA domain 2-like / Cullin repeat-like-containing domain superfamily / Cullin protein, neddylation domain / Cullin protein neddylation domain / Cullin / : / Cullin, N-terminal / Cullin homology domain / Cullin homology domain superfamily / Cullin family / Cullin family profile. / Cleavage/polyadenylation specificity factor, A subunit, N-terminal / Mono-functional DNA-alkylating methyl methanesulfonate N-term / Cleavage/polyadenylation specificity factor, A subunit, C-terminal / CPSF A subunit region / SNF2-like, N-terminal domain superfamily / SNF2, N-terminal / SNF2-related domain / Tetratricopeptide repeat / 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 / S1 domain profile. / RNA polymerase subunit Rpb4/RPC9 / RNA polymerase Rpb4 / Zinc finger TFIIS-type signature. / RNA polymerase subunit Rpb7-like / RNA polymerase Rpb7-like , N-terminal / RNA polymerase Rpb7-like, N-terminal domain superfamily / SHS2 domain found in N terminus of Rpb7p/Rpc25p/MJ0397 / HRDC-like superfamily / RNA polymerase Rpb2, domain 4 / RNA polymerase Rpb2, domain 4 / RNA polymerase Rpb2, domain 5 / RNA polymerase Rpb2, domain 5 / DNA-directed RNA polymerase, M/15kDa subunit / RNA polymerases M/15 Kd subunit / RNA polymerase subunit 9 / DNA-directed RNA polymerase subunit RPABC5/Rpb10 / RNA polymerases, subunit N, zinc binding site / RNA polymerase subunit RPB10
Similarity search - Domain/homology
RNA polymerase II subunit D / DNA-directed RNA polymerase II subunit RPB11-a / DNA-directed RNA polymerases I, II, and III subunit RPABC3 / DNA-directed RNA polymerases I, II, and III subunit RPABC5 / DNA-directed RNA polymerases I, II, and III subunit RPABC2 / DNA-directed RNA polymerase II subunit RPB3 / DNA-directed RNA polymerase subunit beta / DNA-directed RNA polymerase II subunit RPB7 / RNA polymerase II, I and III subunit K / DNA-directed RNA polymerase II subunit E ...RNA polymerase II subunit D / DNA-directed RNA polymerase II subunit RPB11-a / DNA-directed RNA polymerases I, II, and III subunit RPABC3 / DNA-directed RNA polymerases I, II, and III subunit RPABC5 / DNA-directed RNA polymerases I, II, and III subunit RPABC2 / DNA-directed RNA polymerase II subunit RPB3 / DNA-directed RNA polymerase subunit beta / DNA-directed RNA polymerase II subunit RPB7 / RNA polymerase II, I and III subunit K / DNA-directed RNA polymerase II subunit E / DNA-directed RNA polymerase II subunit RPB1 / DNA-directed RNA polymerase II subunit RPB9 / E3 ubiquitin-protein ligase RBX1 / DNA excision repair protein ERCC-6 / DNA excision repair protein ERCC-8 / Cullin-4A / DNA damage-binding protein 1 / UV-stimulated scaffold protein A / Parafibromin / RNA polymerase-associated protein CTR9 homolog / Transcription elongation factor SPT6 / RNA polymerase II-associated factor 1 homolog / RNA polymerase-associated protein LEO1 / Superkiller complex protein 8
Similarity search - Component
Biological speciesSus scrofa (pig) / Homo sapiens (human) / Mus musculus (house mouse) / Pig (pig)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.0 Å
AuthorsKokic G / Cramer P
Funding support Germany, 2 items
OrganizationGrant numberCountry
German Research Foundation (DFG)EXC 2067/1 39072994, SFB860, SPP2191 Germany
European Research Council (ERC)882357 Germany
CitationJournal: Nature / Year: 2021
Title: Structural basis of human transcription-DNA repair coupling.
Authors: Goran Kokic / Felix R Wagner / Aleksandar Chernev / Henning Urlaub / Patrick Cramer /
Abstract: Transcription-coupled DNA repair removes bulky DNA lesions from the genome and protects cells against ultraviolet (UV) irradiation. Transcription-coupled DNA repair begins when RNA polymerase II ...Transcription-coupled DNA repair removes bulky DNA lesions from the genome and protects cells against ultraviolet (UV) irradiation. Transcription-coupled DNA repair begins when RNA polymerase II (Pol II) stalls at a DNA lesion and recruits the Cockayne syndrome protein CSB, the E3 ubiquitin ligase, CRL4 and UV-stimulated scaffold protein A (UVSSA). Here we provide five high-resolution structures of Pol II transcription complexes containing human transcription-coupled DNA repair factors and the elongation factors PAF1 complex (PAF) and SPT6. Together with biochemical and published data, the structures provide a model for transcription-repair coupling. Stalling of Pol II at a DNA lesion triggers replacement of the elongation factor DSIF by CSB, which binds to PAF and moves upstream DNA to SPT6. The resulting elongation complex, EC, uses the CSA-stimulated translocase activity of CSB to pull on upstream DNA and push Pol II forward. If the lesion cannot be bypassed, CRL4 spans over the Pol II clamp and ubiquitylates the RPB1 residue K1268, enabling recruitment of TFIIH to UVSSA and DNA repair. Conformational changes in CRL4 lead to ubiquitylation of CSB and to release of transcription-coupled DNA repair factors before transcription may continue over repaired DNA.
History
DepositionMay 31, 2021-
Header (metadata) releaseOct 13, 2021-
Map releaseOct 13, 2021-
UpdateOct 27, 2021-
Current statusOct 27, 2021Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.01
  • Imaged by UCSF Chimera
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  • Surface view colored by radius
  • Surface level: 0.01
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  • Surface view with fitted model
  • Atomic models: PDB-7opc
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_13015.png

Downloads & links

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Map

FileDownload / File: emd_13015.map.gz / Format: CCP4 / Size: 282.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationThe main map.
Voxel sizeX=Y=Z: 1.05 Å
Density
Contour LevelBy AUTHOR: 0.01 / Movie #1: 0.01
Minimum - Maximum-0.11203127 - 0.17304169
Average (Standard dev.)9.106722e-05 (±0.0027596594)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions420420420
Spacing420420420
CellA=B=C: 440.99997 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.051.051.05
M x/y/z420420420
origin x/y/z0.0000.0000.000
length x/y/z441.000441.000441.000
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ243257325
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS420420420
D min/max/mean-0.1120.1730.000

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Supplemental data

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Mask #1

Fileemd_13015_msk_1.map
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Mask #2

Fileemd_13015_msk_2.map
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Mask #3

Fileemd_13015_msk_3.map
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Mask #4

Fileemd_13015_msk_4.map
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Mask #5

Fileemd_13015_msk_5.map
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Additional map: Half map corresponding to the main map.

Fileemd_13015_additional_1.map
AnnotationHalf map corresponding to the main map.
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Additional map: Half map corresponding to the map focused refined on CSB-CSA-DDB1.

Fileemd_13015_additional_10.map
AnnotationHalf map corresponding to the map focused refined on CSB-CSA-DDB1.
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Additional map: Half map corresponding to the map focused refined on Pol II.

Fileemd_13015_additional_11.map
AnnotationHalf map corresponding to the map focused refined on Pol II.
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Additional map: Half map corresponding to the map focused refined on PAF.

Fileemd_13015_additional_12.map
AnnotationHalf map corresponding to the map focused refined on PAF.
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Additional map: Half map corresponding to the map focused refined on PAF.

Fileemd_13015_additional_13.map
AnnotationHalf map corresponding to the map focused refined on PAF.
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Additional map: Half map corresponding to the map focused refined on Pol II.

Fileemd_13015_additional_14.map
AnnotationHalf map corresponding to the map focused refined on Pol II.
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Additional map: Mask for PAF.

Fileemd_13015_additional_15.map
AnnotationMask for PAF.
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Additional map: Half map corresponding to the main map.

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Additional map: Half map corresponding to the map focused refined...

Fileemd_13015_additional_3.map
AnnotationHalf map corresponding to the map focused refined on CRL4CSA-UVSSA. The map was resampled while making the main map.
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Additional map: Half map corresponding to the map focused refined...

Fileemd_13015_additional_4.map
AnnotationHalf map corresponding to the map focused refined on CRL4CSA-UVSSA. This map was not used to make the main map.
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Additional map: Half map corresponding to the map focused refined...

Fileemd_13015_additional_5.map
AnnotationHalf map corresponding to the map focused refined on CRL4CSA-UVSSA. This map was not used to make the main map.
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Additional map: Half map corresponding to the map focused refined...

Fileemd_13015_additional_6.map
AnnotationHalf map corresponding to the map focused refined on CRL4CSA-UVSSA. The map was resampled while making the main map.
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Additional map: Half map corresponding to the map focused refined on SPT6.

Fileemd_13015_additional_7.map
AnnotationHalf map corresponding to the map focused refined on SPT6.
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Additional map: Half map corresponding to the map focused refined on CSB-CSA-DDB1.

Fileemd_13015_additional_8.map
AnnotationHalf map corresponding to the map focused refined on CSB-CSA-DDB1.
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Additional map: Half map corresponding to the map focused refined on SPT6.

Fileemd_13015_additional_9.map
AnnotationHalf map corresponding to the map focused refined on SPT6.
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Sample components

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Entire : Transcribing Pol II bound to CSB, CRL4CSA, UVSSA, PAF and SPT6.

EntireName: Transcribing Pol II bound to CSB, CRL4CSA, UVSSA, PAF and SPT6.
Components
  • Complex: Transcribing Pol II bound to CSB, CRL4CSA, UVSSA, PAF and SPT6.
    • Complex: DNA-directed RNA polymerase with RNA_pol_L_2 and RNA polymerase
      • Protein or peptide: DNA-directed RNA polymerase II subunit RPB1Polymerase
      • Protein or peptide: DNA-directed RNA polymerase subunit betaPolymerase
      • Protein or peptide: DNA-directed RNA polymerase II subunit RPB3Polymerase
      • Protein or peptide: RPOL4c domain-containing protein
      • Protein or peptide: DNA-directed RNA polymerase II subunit EPolymerase
      • Protein or peptide: DNA-directed RNA polymerase II subunit FPolymerase
      • Protein or peptide: DNA-directed RNA polymerase II subunit RPB7Polymerase
      • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC3RNA polymerase
      • Protein or peptide: DNA-directed RNA polymerase II subunit RPB9Polymerase
      • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC5RNA polymerase
      • Protein or peptide: RNA_pol_L_2 domain-containing protein
      • Protein or peptide: RNA polymerase II subunit K
    • Complex: Supplementary proteins
      • Protein or peptide: Transcription elongation factor SPT6
      • Protein or peptide: LEO1 helix
      • Protein or peptide: RNA polymerase-associated protein CTR9 homolog
      • Protein or peptide: RNA polymerase-associated protein LEO1
      • Protein or peptide: RNA polymerase II-associated factor 1 homolog
      • Protein or peptide: WD repeat-containing protein 61
      • Protein or peptide: Parafibromin
      • Protein or peptide: DNA excision repair protein ERCC-8
      • Protein or peptide: DNA excision repair protein ERCC-6
      • Protein or peptide: UV-stimulated scaffold protein A
      • Protein or peptide: DNA damage-binding protein 1
      • Protein or peptide: Cullin-4A
    • Complex: NTS, RNA, TS
      • DNA: NTS
      • RNA: RNA
      • DNA: TS
    • Complex: E3 ubiquitin-protein ligase RBX1
      • Protein or peptide: E3 ubiquitin-protein ligase RBX1
  • Ligand: ZINC ION
  • Ligand: MAGNESIUM ION

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Supramolecule #1: Transcribing Pol II bound to CSB, CRL4CSA, UVSSA, PAF and SPT6.

SupramoleculeName: Transcribing Pol II bound to CSB, CRL4CSA, UVSSA, PAF and SPT6.
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#28

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Supramolecule #2: DNA-directed RNA polymerase with RNA_pol_L_2 and RNA polymerase

SupramoleculeName: DNA-directed RNA polymerase with RNA_pol_L_2 and RNA polymerase
type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#12
Source (natural)Organism: Sus scrofa (pig)

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Supramolecule #3: Supplementary proteins

SupramoleculeName: Supplementary proteins / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #13, #16-#17, #19-#27
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)

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Supramolecule #4: NTS, RNA, TS

SupramoleculeName: NTS, RNA, TS / type: complex / ID: 4 / Parent: 1 / Macromolecule list: #14-#15, #18
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: synthetic construc (others)

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Supramolecule #5: E3 ubiquitin-protein ligase RBX1

SupramoleculeName: E3 ubiquitin-protein ligase RBX1 / type: complex / ID: 5 / Parent: 1 / Macromolecule list: #28
Source (natural)Organism: Mus musculus (house mouse)
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)

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Macromolecule #1: DNA-directed RNA polymerase II subunit RPB1

MacromoleculeName: DNA-directed RNA polymerase II subunit RPB1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 217.450078 KDa
SequenceString: MHGGGPPSGD SACPLRTIKR VQFGVLSPDE LKRMSVTEGG IKYPETTEGG RPKLGGLMDP RQGVIERTGR CQTCAGNMTE CPGHFGHIE LAKPVFHVGF LVKTMKVLRC VCFFCSKLLV DSNNPKIKDI LAKSKGQPKK RLTHVYDLCK GKNICEGGEE M DNKFGVEQ ...String:
MHGGGPPSGD SACPLRTIKR VQFGVLSPDE LKRMSVTEGG IKYPETTEGG RPKLGGLMDP RQGVIERTGR CQTCAGNMTE CPGHFGHIE LAKPVFHVGF LVKTMKVLRC VCFFCSKLLV DSNNPKIKDI LAKSKGQPKK RLTHVYDLCK GKNICEGGEE M DNKFGVEQ PEGDEDLTKE KGHGGCGRYQ PRIRRSGLEL YAEWKHVNED SQEKKILLSP ERVHEIFKRI SDEECFVLGM EP RYARPEW MIVTVLPVPP LSVRPAVVMQ GSARNQDDLT HKLADIVKIN NQLRRNEQNG AAAHVIAEDV KLLQFHVATM VDN ELPGLP RAMQKSGRPL KSLKQRLKGK EGRVRGNLMG KRVDFSARTV ITPDPNLSID QVGVPRSIAA NMTFAEIVTP FNID RLQEL VRRGNSQYPG AKYIIRDNGD RIDLRFHPKP SDLHLQTGYK VERHMCDGDI VIFNRQPTLH KMSMMGHRVR ILPWS TFRL NLSVTTPYNA DFDGDEMNLH LPQSLETRAE IQELAMVPRM IVTPQSNRPV MGIVQDTLTA VRKFTKRDVF LERGEV MNL LMFLSTWDGK VPQPAILKPR PLWTGKQIFS LIIPGHINCI RTHSTHPDDE DSGPYKHISP GDTKVVVENG ELIMGIL CK KSLGTSAGSL VHISYLEMGH DITRLFYSNI QTVINNWLLI EGHTIGIGDS IADSKTYQDI QNTIKKAKQD VIEVIEKA H NNELEPTPGN TLRQTFENQV NRILNDARDK TGSSAQKSLS EYNNFKSMVV SGAKGSKINI SQVIAVVGQQ NVEGKRIPF GFKHRTLPHF IKDDYGPESR GFVENSYLAG LTPTEFFFHA MGGREGLIDT AVKTAETGYI QRRLIKSMES VMVKYDATVR NSINQVVQL RYGEDGLAGE SVEFQNLATL KPSNKAFEKK FRFDYTNERA LRRTLQEDLV KDVLSNAHIQ NELEREFERM R EDREVLRV IFPTGDSKVV LPCNLLRMIW NAQKIFHINP RLPSDLHPIK VVEGVKELSK KLVIVNGDDP LSRQAQENAT LL FNIHLRS TLCSRRMAEE FRLSGEAFDW LLGEIESKFN QAIAHPGEMV GALAAQSLGE PATQMTLNTF HYAGVSAKNV TLG VPRLKE LINISKKPKT PSLTVFLLGQ SARDAERAKD ILCRLEHTTL RKVTANTAIY YDPNPQSTVV AEDQEWVNVY YEMP DFDVA RISPWLLRVE LDRKHMTDRK LTMEQIAEKI NAGFGDDLNC IFNDDNAEKL VLRIRIMNSD ENKMQEEEEV VDKMD DDVF LRCIESNMLT DMTLQGIEQI SKVYMHLPQT DNKKKIIITE DGEFKALQEW ILETDGVSLM RVLSEKDVDP VRTTSN DIV EIFTVLGIEA VRKALERELY HVISFDGSYV NYRHLALLCD TMTCRGHLMA ITRHGVNRQD TGPLMKCSFE ETVDVLM EA AAHGESDPMK GVSENIMLGQ LAPAGTGCFD LLLDAEKCKY GMEIPTNIPG LGAAGPTGMF FGSAPSPMGG ISPAMTPW N QGATPAYGAW SPSVGSGMTP GAAGFSPSAA SDASGFSPGY SPAWSPTPGS PGSPGPSSPY IPSPGGAMSP SYSPTSPAY EPRSPGGYTP QSPSYSPTSP SYSPTSPSYS PTSPNYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP TSPSYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP TSPSYSPTSP SYSPTSPNYS PTSPNYTPTS P SYSPTSPS YSPTSPNYTP TSPNYSPTSP SYSPTSPSYS PTSPSYSPSS PRYTPQSPTY TPSSPSYSPS SPSYSPTSPK YT PTSPSYS PSSPEYTPTS PKYSPTSPKY SPTSPKYSPT SPTYSPTTPK YSPTSPTYSP TSPVYTPTSP KYSPTSPTYS PTS PKYSPT SPTYSPTSPK GSTYSPTSPG YSPTSPTYSL TSPAISPDDS DEEN

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Macromolecule #2: DNA-directed RNA polymerase subunit beta

MacromoleculeName: DNA-directed RNA polymerase subunit beta / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA-directed RNA polymerase
Source (natural)Organism: Pig (pig)
Molecular weightTheoretical: 134.041422 KDa
SequenceString: MYDADEDMQY DEDDDEITPD LWQEACWIVI SSYFDEKGLV RQQLDSFDEF IQMSVQRIVE DAPPIDLQAE AQHASGEVEE PPRYLLKFE QIYLSKPTHW ERDGAPSPMM PNEARLRNLT YSAPLYVDIT KTVIKEGEEQ LQTQHQKTFI GKIPIMLRST Y CLLNGLTD ...String:
MYDADEDMQY DEDDDEITPD LWQEACWIVI SSYFDEKGLV RQQLDSFDEF IQMSVQRIVE DAPPIDLQAE AQHASGEVEE PPRYLLKFE QIYLSKPTHW ERDGAPSPMM PNEARLRNLT YSAPLYVDIT KTVIKEGEEQ LQTQHQKTFI GKIPIMLRST Y CLLNGLTD RDLCELNECP LDPGGYFIIN GSEKVLIAQE KMATNTVYVF AKKDSKYAYT GECRSCLENS SRPTSTIWVS ML ARGGQGA KKSAIGQRIV ATLPYIKQEV PIIIVFRALG FVSDRDILEH IIYDFEDPEM MEMVKPSLDE AFVIQEQNVA LNF IGSRGA KPGVTKEKRI KYAKEVLQKE MLPHVGVSDF CETKKAYFLG YMVHRLLLAA LGRRELDDRD HYGNKRLDLA GPLL AFLFR GMFKNLLKEV RIYAQKFIDR GKDFNLELAI KTRIISDGLK YSLATGNWGD QKKAHQARAG VSQVLNRLTF ASTLS HLRR LNSPIGRDGK LAKPRQLHNT LWGMVCPAET PEGHAVGLVK NLALMAYISV GSQPSPILEF LEEWSMENLE EISPAA IAD ATKIFVNGCW VGIHKDPEQL MNTLRKLRRQ MDIIVSEVSM IRDIREREIR IYTDAGRICR PLLIVEKQKL LLKKRHI DQ LKEREYNNYS WQDLVASGVV EYIDTLEEET VMLAMTPDDL QEKEVAYCST YTHCEIHPSM ILGVCASIIP FPDHNQSP R NTYQSAMGKQ AMGVYITNFH VRMDTLAHVL YYPQKPLVTT RSMEYLRFRE LPAGINSIVA IASYTGYNQE DSVIMNRSA VDRGFFRSVF YRSYKEQESK KGFDQEEVFE KPTRETCQGM RHAIYDKLDD DGLIAPGVRV SGDDVIIGKT VTLPENEDEL EGTNRRYTK RDCSTFLRTS ETGIVDQVMV TLNQEGYKFC KIRVRSVRIP QIGDKFASRH GQKGTCGIQY RQEDMPFTCE G ITPDIIIN PHAIPSRMTI GHLIECLQGK VSANKGEIGD ATPFNDAVNV QKISNLLSDY GYHLRGNEVL YNGFTGRKIT SQ IFIGPTY YQRLKHMVDD KIHSRARGPI QILNRQPMEG RSRDGGLRFG EMERDCQIAH GAAQFLRERL FEASDPYQVH VCN LCGIMA IANTRTHTYE CRGCRNKTQI SLVRMPYACK LLFQELMSMS IAPRMMSV

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Macromolecule #3: DNA-directed RNA polymerase II subunit RPB3

MacromoleculeName: DNA-directed RNA polymerase II subunit RPB3 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Pig (pig)
Molecular weightTheoretical: 31.439074 KDa
SequenceString: MPYANQPTVR ITELTDENVK FIIENTDLAV ANSIRRVFIA EVPIIAIDWV QIDANSSVLH DEFIAHRLGL IPLTSDDIVD KLQYSRDCT CEEFCPECSV EFTLDVRCNE DQTRHVTSRD LISNSPRVIP VTSRNRDNDP SDYVEQDDIL IVKLRKGQEL R LRAYAKKG ...String:
MPYANQPTVR ITELTDENVK FIIENTDLAV ANSIRRVFIA EVPIIAIDWV QIDANSSVLH DEFIAHRLGL IPLTSDDIVD KLQYSRDCT CEEFCPECSV EFTLDVRCNE DQTRHVTSRD LISNSPRVIP VTSRNRDNDP SDYVEQDDIL IVKLRKGQEL R LRAYAKKG FGKEHAKWNP TAGVAFEYDP DNALRHTVYP KPEEWPKSEY SELDEDESQA PYDPNGKPER FYYNVESCGS LR PETIVLS ALSGLKKKLS DLQTQLSHEI QSDVLTIN

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Macromolecule #4: RPOL4c domain-containing protein

MacromoleculeName: RPOL4c domain-containing protein / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Pig (pig)
Molecular weightTheoretical: 16.331255 KDa
SequenceString:
MAAGGSDPRA GDVEEDASQL IFPKEFETAE TLLNSEVHML LEHRKQQNES AEDEQELSEV FMKTLNYTAR FSRFKNRETI ASVRSLLLQ KKLHKFELAC LANLCPETAE ESKALIPSLE GRFEDEELQQ ILDDIQTKRS FQY

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

MacromoleculeName: DNA-directed RNA polymerase II subunit E / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Pig (pig)
Molecular weightTheoretical: 24.644318 KDa
SequenceString: MDDEEETYRL WKIRKTIMQL CHDRGYLVTQ DELDQTLEEF KAQFGDKPSE GRPRRTDLTV LVAHNDDPTD QMFVFFPEEP KVGIKTIKV YCQRMQEENI TRALIVVQQG MTPSAKQSLV DMAPKYILEQ FLQQELLINI TEHELVPEHV VMTKEEVTEL L ARYKLREN ...String:
MDDEEETYRL WKIRKTIMQL CHDRGYLVTQ DELDQTLEEF KAQFGDKPSE GRPRRTDLTV LVAHNDDPTD QMFVFFPEEP KVGIKTIKV YCQRMQEENI TRALIVVQQG MTPSAKQSLV DMAPKYILEQ FLQQELLINI TEHELVPEHV VMTKEEVTEL L ARYKLREN QLPRIQAGDP VARYFGIKRG QVVKIIRPSE TAGRYITYRL VQ

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

MacromoleculeName: DNA-directed RNA polymerase II subunit F / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Pig (pig)
Molecular weightTheoretical: 14.477001 KDa
SequenceString:
MSDNEDNFDG DDFDDVEEDE GLDDLENAEE EGQENVEILP SGERPQANQK RITTPYMTKY ERARVLGTRA LQIAMCAPVM VELEGETDP LLIAMKELKA RKIPIIIRRY LPDGSYEDWG VDELIISD

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Macromolecule #7: DNA-directed RNA polymerase II subunit RPB7

MacromoleculeName: DNA-directed RNA polymerase II subunit RPB7 / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Pig (pig)
Molecular weightTheoretical: 19.314283 KDa
SequenceString:
MFYHISLEHE ILLHPRYFGP NLLNTVKQKL FTEVEGTCTG KYGFVIAVTT IDNIGAGVIQ PGRGFVLYPV KYKAIVFRPF KGEVVDAVV TQVNKVGLFT EIGPMSCFIS RHSIPSEMEF DPNSNPPCYK TMDEDIVIQQ DDEIRLKIVG TRVDKNDIFA I GSLMDDYL GLVS

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Macromolecule #8: 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: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Pig (pig)
Molecular weightTheoretical: 17.162273 KDa
SequenceString:
MAGILFEDIF DVKDIDPEGK KFDRVSRLHC ESESFKMDLI LDVNIQIYPV DLGDKFRLVI ASTLYEDGTL DDGEYNPTDD RPSRADQFE YVMYGKVYRI EGDETSTEAA TRLSAYVSYG GLLMRLQGDA NNLHGFEVDS RVYLLMKKLA F

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Macromolecule #9: DNA-directed RNA polymerase II subunit RPB9

MacromoleculeName: DNA-directed RNA polymerase II subunit RPB9 / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Pig (pig)
Molecular weightTheoretical: 14.541221 KDa
SequenceString:
MEPDGTYEPG FVGIRFCQEC NNMLYPKEDK ENRILLYACR NCDYQQEADN SCIYVNKITH EVDELTQIIA DVSQDPTLPR TEDHPCQKC GHKEAVFFQS HSARAEDAMR LYYVCTAPHC GHRWTE

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Macromolecule #10: 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: 10 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Pig (pig)
Molecular weightTheoretical: 7.655123 KDa
SequenceString:
MIIPVRCFTC GKIVGNKWEA YLGLLQAEYT EGDALDALGL KRYCCRRMLL AHVDLIEKLL NYAPLEK

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Macromolecule #11: RNA_pol_L_2 domain-containing protein

MacromoleculeName: RNA_pol_L_2 domain-containing protein / type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Pig (pig)
Molecular weightTheoretical: 13.310284 KDa
SequenceString:
MNAPPAFESF LLFEGEKKIT INKDTKVPNA CLFTINKEDH TLGNIIKSQL LKDPQVLFAG YKVPHPLEHK IIIRVQTTPD YSPQEAFTN AITDLISELS LLEERFRVAI KDKQEGIE

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Macromolecule #12: RNA polymerase II subunit K

MacromoleculeName: RNA polymerase II subunit K / type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Pig (pig)
Molecular weightTheoretical: 7.018244 KDa
SequenceString:
MDTQKDVQPP KQQPMIYICG ECHTENEIKS RDPIRCRECG YRIMYKKRTK RLVVFDAR

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Macromolecule #13: Transcription elongation factor SPT6

MacromoleculeName: Transcription elongation factor SPT6 / type: protein_or_peptide / ID: 13 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 199.602969 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: SNAMSDFVES EAEESEEEYN DEGEVVPRVT KKFVEEEDDD EEEEEENLDD QDEQGNLKGF INDDDDEDEG EEDEGSDSGD SEDDVGHKK RKRTSFDDRL EDDDFDLIEE NLGVKVKRGQ KYRRVKKMSD DEDDDEEEYG KEEHEKEAIA EEIFQDGEGE E GQEAMEAP ...String:
SNAMSDFVES EAEESEEEYN DEGEVVPRVT KKFVEEEDDD EEEEEENLDD QDEQGNLKGF INDDDDEDEG EEDEGSDSGD SEDDVGHKK RKRTSFDDRL EDDDFDLIEE NLGVKVKRGQ KYRRVKKMSD DEDDDEEEYG KEEHEKEAIA EEIFQDGEGE E GQEAMEAP MAPPEEEEED DEESDIDDFI VDDDGQPLKK PKWRKKLPGY TDAALQEAQE IFGVDFDYDE FEKYNEYDEE LE EEYEYED DEAEGEIRVR PKKTTKKRVS RRSIFEMYEP SELESSHLTD QDNEIRATDL PERFQLRSIP VKGAEDDELE EEA DWIYRN AFATPTISLQ ESCDYLDRGQ PASSFSRKGP STIQKIKEAL GFMRNQHFEV PFIAFYRKEY VEPELHINDL WRVW QWDEK WTQLRIRKEN LTRLFEKMQA YQYEQISADP DKPLADGIRA LDTTDMERLK DVQSMDELKD VYNHFLLYYG RDIPK MQNA AKASRKKLKR VREEGDEEGE GDEAEDEEQR GPELKQASRR DMYTICQSAG LDGLAKKFGL TPEQFGENLR DSYQRH ETE QFPAEPLELA KDYVCSQFPT PEAVLEGARY MVALQIAREP LVRQVLRQTF QERAKLNITP TKKGRKDVDE AHYAYSF KY LKNKPVKELR DDQFLKICLA EDEGLLTTDI SIDLKGVEGY GNDQTYFEEI KQFYYRDEFS HQVQEWNRQR TMAIERAL Q QFLYVQMAKE LKNKLLAEAK EYVIKACSRK LYNWLRVAPY RPDQQVEEDD DFMDENQGKG IRVLGIAFSS ARDHPVFCA LVNGEGEVTD FLRLPHFTKR RTAWREEERE KKAQDIETLK KFLLNKKPHV VTVAGENRDA QMLIEDVKRI VHELDQGQQL SSIGVELVD NELAILYMNS KKSEAEFRDY PPVLRQAVSL ARRIQDPLIE FAQVCSSDED ILCLKFHPLQ EHVVKEELLN A LYCEFINR VNEVGVDVNR AIAHPYSQAL IQYVCGLGPR KGTHLLKILK QNNTRLESRT QLVTMCHMGP KVFMNCAGFL KI DTASLGD STDSYIEVLD GSRVHPETYE WARKMAVDAL EYDESAEDAN PAGALEEILE NPERLKDLDL DAFAEELERQ GYG DKHITL YDIRAELSCR YKDLRTAYRS PNTEEIFNML TKETPETFYI GKLIICNVTG IAHRRPQGES YDQAIRNDET GLWQ CPFCQ QDNFPELSEV WNHFDSGSCP GQAIGVKTRL DNGVTGFIPT KFLSDKVVKR PEERVKVGMT VHCRIMKIDI EKFSA DLTC RTSDLMDRNN EWKLPKDTYY DFDAEAADHK QEEDMKRKQQ RTTYIKRVIA HPSFHNINFK QAEKMMETMD QGDVII RPS SKGENHLTVT WKVSDGIYQH VDVREEGKEN AFSLGATLWI NSEEFEDLDE IVARYVQPMA SFARDLLNHK YYQDCSG GD RKKLEELLIK TKKEKPTFIP YFICACKELP GKFLLGYQPR GKPRIEYVTV TPEGFRYRGQ IFPTVNGLFR WFKDHYQD P VPGITPSSSS RTRTPASINA TPANINLADL TRAVNALPQN MTSQMFSAIA AVTGQGQNPN ATPAQWASSQ YGYGGSGGG SSAYHVFPTP AQQPVATPLM TPSYSYTTPS QPITTPQYHQ LQASTTPQSA QAQPQPSSSS RQRQQQPKSN SHAAIDWGKM AEQWLQEKE AERRKQKQRL TPRPSPSPMI ESTPMSIAGD ATPLLDEMDR

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Macromolecule #16: LEO1 helix

MacromoleculeName: LEO1 helix / type: protein_or_peptide / ID: 16 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 3.422209 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString:
(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)

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Macromolecule #17: RNA polymerase-associated protein CTR9 homolog

MacromoleculeName: RNA polymerase-associated protein CTR9 homolog / type: protein_or_peptide / ID: 17 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 134.510203 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MSRGSIEIPL RDTDEVIELD FDQLPEGDEV ISILKQEHTQ LHIWIALALE YYKQGKTEEF VKLLEAARID GNLDYRDHEK DQMTCLDTL AAYYVQQARK EKNKDNKKDL ITQATLLYTM ADKIIMYDQN HLLGRACFCL LEGDKMDQAD AQFHFVLNQS P NNIPALLG ...String:
MSRGSIEIPL RDTDEVIELD FDQLPEGDEV ISILKQEHTQ LHIWIALALE YYKQGKTEEF VKLLEAARID GNLDYRDHEK DQMTCLDTL AAYYVQQARK EKNKDNKKDL ITQATLLYTM ADKIIMYDQN HLLGRACFCL LEGDKMDQAD AQFHFVLNQS P NNIPALLG KACISFNKKD YRGALAYYKK ALRTNPGCPA EVRLGMGHCF VKLNKLEKAR LAFSRALELN SKCVGALVGL AV LELNNKE ADSIKNGVQL LSRAYTIDPS NPMVLNHLAN HFFFKKDYSK VQHLALHAFH NTEVEAMQAE SCYQLARSFH VQE DYDQAF QYYYQATQFA SSSFVLPFFG LGQMYIYRGD KENASQCFEK VLKAYPNNYE TMKILGSLYA ASEDQEKRDI AKGH LKKVT EQYPDDVEAW IELAQILEQT DIQGALSAYG TATRILQEKV QADVPPEILN NVGALHFRLG NLGEAKKYFL ASLDR AKAE AEHDEHYYNA ISVTTSYNLA RLYEAMCEFH EAEKLYKNIL REHPNYVDCY LRLGAMARDK GNFYEASDWF KEALQI NQD HPDAWSLIGN LHLAKQEWGP GQKKFERILK QPSTQSDTYS MLALGNVWLQ TLHQPTRDRE KEKRHQDRAL AIYKQVL RN DAKNLYAANG IGAVLAHKGY FREARDVFAQ VREATADISD VWLNLAHIYV EQKQYISAVQ MYENCLRKFY KHQNTEVV L YLARALFKCG KLQECKQTLL KARHVAPSDT VLMFNVALVL QRLATSVLKD EKSNLKEVLN AVKELELAHR YFSYLSKVG DKMRFDLALA ATEARQCSDL LSQAQYHVAR ARKQDEEERE LRAKQEQEKE LLRQKLLKEQ EEKRLREKEE QKKLLEQRAQ YVEKTKNIL MFTGETEATK EKKRGGGGGR RSKKGGEFDE FVNDDTDDDL PISKKKKRRK GSGSEQEGED EEGGERKKKK R RRHPKGEE GSDDDETENG PKPKKRRPPK AEKKKAPKPE RLPPSMKGKI KSKAIISSSD DSSDEDKLKI ADEGHPRNSN SN SDSDEDE QRKKCASSES DSDENQNKSG SEAGSPRRPR RQRSDQDSDS DQPSRKRRPS GSEQSDNESV QSGRSHSGVS END SRPASP SAESDHESER GSDNEGSGQG SGNESEPEGS NNEASDRGSE HGSDDSDENL YFQ

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Macromolecule #19: RNA polymerase-associated protein LEO1

MacromoleculeName: RNA polymerase-associated protein LEO1 / type: protein_or_peptide / ID: 19 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 75.514172 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MADMEDLFGS DADSEAERKD SDSGSDSDSD QENAASGSNA SGSESDQDER GDSGQPSNKE LFGDDSEDEG ASHHSGSDNH SERSDNRSE ASERSDHEDN DPSDVDQHSG SEAPNDDEDE GHRSDGGSHH SEAEGSEKAH SDDEKWGRED KSDQSDDEKI Q NSDDEERA ...String:
MADMEDLFGS DADSEAERKD SDSGSDSDSD QENAASGSNA SGSESDQDER GDSGQPSNKE LFGDDSEDEG ASHHSGSDNH SERSDNRSE ASERSDHEDN DPSDVDQHSG SEAPNDDEDE GHRSDGGSHH SEAEGSEKAH SDDEKWGRED KSDQSDDEKI Q NSDDEERA QGSDEDKLQN SDDDEKMQNT DDEERPQLSD DERQQLSEEE KANSDDERPV ASDNDDEKQN SDDEEQPQLS DE EKMQNSD DERPQASDEE HRHSDDEEEQ DHKSESARGS DSEDEVLRMK RKNAIASDSE ADSDTEVPKD NSGTMDLFGG ADD ISSGSD GEDKPPTPGQ PVDENGLPQD QQEEEPIPET RIEVEIPKVN TDLGNDLYFV KLPNFLSVEP RPFDPQYYED EFED EEMLD EEGRTRLKLK VENTIRWRIR RDEEGNEIKE SNARIVKWSD GSMSLHLGNE VFDVYKAPLQ GDHNHLFIRQ GTGLQ GQAV FKTKLTFRPH STDSATHRKM TLSLADRCSK TQKIRILPMA GRDPECQRTE MIKKEEERLR ASIRRESQQR RMREKQ HQR GLSASYLEPD RYDEEEEGEE SISLAAIKNR YKGGIREERA RIYSSDSDEG SEEDKAQRLL KAKKLTSDEE GEPSGKR KA EDDDKANKKH KKYVISDEEE EDDD

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Macromolecule #20: RNA polymerase II-associated factor 1 homolog

MacromoleculeName: RNA polymerase II-associated factor 1 homolog / type: protein_or_peptide / ID: 20 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 60.052672 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MAPTIQTQAQ REDGHRPNSH RTLPERSGVV CRVKYCNSLP DIPFDPKFIT YPFDQNRFVQ YKATSLEKQH KHDLLTEPDL GVTIDLINP DTYRIDPNVL LDPADEKLLE EEIQAPTSSK RSQQHAKVVP WMRKTEYIST EFNRYGISNE KPEVKIGVSV K QQFTEEEI ...String:
MAPTIQTQAQ REDGHRPNSH RTLPERSGVV CRVKYCNSLP DIPFDPKFIT YPFDQNRFVQ YKATSLEKQH KHDLLTEPDL GVTIDLINP DTYRIDPNVL LDPADEKLLE EEIQAPTSSK RSQQHAKVVP WMRKTEYIST EFNRYGISNE KPEVKIGVSV K QQFTEEEI YKDRDSQITA IEKTFEDAQK SISQHYSKPR VTPVEVMPVF PDFKMWINPC AQVIFDSDPA PKDTSGAAAL EM MSQAMIR GMMDEEGNQF VAYFLPVEET LKKRKRDQEE EMDYAPDDVY DYKIAREYNW NVKNKASKGY EENYFFIFRE GDG VYYNEL ETRVRLSKRR AKAGVQSGTN ALLVVKHRDM NEKELEAQEA RKAQLENHEP EEEEEEEMET EEKEAGGSDE EQEK GSSSE KEGSEDEHSG SESEREEGDR DEASDKSGSG EDESSEDEAR AARDKEEIFG SDADSEDDAD SDDEDRGQAQ GGSDN DSDS GSNGGGQRSR SHSRSASPFP SGSEHSAQED GSEAAASDSS EADSDSD

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Macromolecule #21: WD repeat-containing protein 61

MacromoleculeName: WD repeat-containing protein 61 / type: protein_or_peptide / ID: 21 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 33.617465 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MTNQYGILFK QEQAHDDAIW SVAWGTNKKE NSETVVTGSL DDLVKVWKWR DERLDLQWSL EGHQLGVVSV DISHTLPIAA SSSLDAHIR LWDLENGKQI KSIDAGPVDA WTLAFSPDSQ YLATGTHVGK VNIFGVESGK KEYSLDTRGK FILSIAYSPD G KYLASGAI ...String:
MTNQYGILFK QEQAHDDAIW SVAWGTNKKE NSETVVTGSL DDLVKVWKWR DERLDLQWSL EGHQLGVVSV DISHTLPIAA SSSLDAHIR LWDLENGKQI KSIDAGPVDA WTLAFSPDSQ YLATGTHVGK VNIFGVESGK KEYSLDTRGK FILSIAYSPD G KYLASGAI DGIINIFDIA TGKLLHTLEG HAMPIRSLTF SPDSQLLVTA SDDGYIKIYD VQHANLAGTL SGHASWVLNV AF CPDDTHF VSSSSDKSVK VWDVGTRTCV HTFFDHQDQV WGVKYNGNGS KIVSVGDDQE IHIYDCPI

+
Macromolecule #22: Parafibromin

MacromoleculeName: Parafibromin / type: protein_or_peptide / ID: 22 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 60.673539 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MADVLSVLRQ YNIQKKEIVV KGDEVIFGEF SWPKNVKTNY VVWGTGKEGQ PREYYTLDSI LFLLNNVHLS HPVYVRRAAT ENIPVVRRP DRKDLLGYLN GEASTSASID RSAPLEIGLQ RSTQVKRAAD EVLAEAKKPR IEDEECVRLD KERLAARLEG H KEGIVQTE ...String:
MADVLSVLRQ YNIQKKEIVV KGDEVIFGEF SWPKNVKTNY VVWGTGKEGQ PREYYTLDSI LFLLNNVHLS HPVYVRRAAT ENIPVVRRP DRKDLLGYLN GEASTSASID RSAPLEIGLQ RSTQVKRAAD EVLAEAKKPR IEDEECVRLD KERLAARLEG H KEGIVQTE QIRSLSEAMS VEKIAAIKAK IMAKKRSTIK TDLDDDITAL KQRSFVDAEV DVTRDIVSRE RVWRTRTTIL QS TGKNFSK NIFAILQSVK AREEGRAPEQ RPAPNAAPVD PTLRTKQPIP AAYNRYDQER FKGKEETEGF KIDTMGTYHG MTL KSVTEG ASARKTQTPA AQPVPRPVSQ ARPPPNQKKG SRTPIIIIPA ATTSLITMLN AKDLLQDLKF VPSDEKKKQG CQRE NETLI QRRKDQMQPG GTAISVTVPY RVVDQPLKLM PQDWDRVVAV FVQGPAWQFK GWPWLLPDGS PVDIFAKIKA FHLKY DEVR LDPNVQKWDV TVLELSYHKR HLDRPVFLRF WETLDRYMVK HKSHLRF

+
Macromolecule #23: DNA excision repair protein ERCC-8

MacromoleculeName: DNA excision repair protein ERCC-8 / type: protein_or_peptide / ID: 23 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 44.10716 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MLGFLSARQT GLEDPLRLRR AESTRRVLGL ELNKDRDVER IHGGGINTLD IEPVEGRYML SGGSDGVIVL YDLENSSRQS YYTCKAVCS IGRDHPDVHR YSVETVQWYP HDTGMFTSSS FDKTLKVWDT NTLQTADVFN FEETVYSHHM SPVSTKHCLV A VGTRGPKV ...String:
MLGFLSARQT GLEDPLRLRR AESTRRVLGL ELNKDRDVER IHGGGINTLD IEPVEGRYML SGGSDGVIVL YDLENSSRQS YYTCKAVCS IGRDHPDVHR YSVETVQWYP HDTGMFTSSS FDKTLKVWDT NTLQTADVFN FEETVYSHHM SPVSTKHCLV A VGTRGPKV QLCDLKSGSC SHILQGHRQE ILAVSWSPRY DYILATASAD SRVKLWDVRR ASGCLITLDQ HNGKKSQAVE SA NTAHNGK VNGLCFTSDG LHLLTVGTDN RMRLWNSSNG ENTLVNYGKV CNNSKKGLKF TVSCGCSSEF VFVPYGSTIA VYT VYSGEQ ITMLKGHYKT VDCCVFQSNF QELYSGSRDC NILAWVPSLY EPVPDDDETT TKSQLNPAFE DAWSSSDEEG

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Macromolecule #24: DNA excision repair protein ERCC-6

MacromoleculeName: DNA excision repair protein ERCC-6 / type: protein_or_peptide / ID: 24 / 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: 168.973812 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: SNAMPNEGIP HSSQTQEQDC LQSQPVSNNE EMAIKQESGG DGEVEEYLSF RSVGDGLSTS AVGCASAAPR RGPALLHIDR HQIQAVEPS AQALELQGLG VDVYDQDVLE QGVLQQVDNA IHEASRASQL VDVEKEYRSV LDDLTSCTTS LRQINKIIEQ L SPQAATSR ...String:
SNAMPNEGIP HSSQTQEQDC LQSQPVSNNE EMAIKQESGG DGEVEEYLSF RSVGDGLSTS AVGCASAAPR RGPALLHIDR HQIQAVEPS AQALELQGLG VDVYDQDVLE QGVLQQVDNA IHEASRASQL VDVEKEYRSV LDDLTSCTTS LRQINKIIEQ L SPQAATSR DINRKLDSVK RQKYNKEQQL KKITAKQKHL QAILGGAEVK IELDHASLEE DAEPGPSSLG SMLMPVQETA WE ELIRTGQ MTPFGTQIPQ KQEKKPRKIM LNEASGFEKY LADQAKLSFE RKKQGCNKRA ARKAPAPVTP PAPVQNKNKP NKK ARVLSK KEERLKKHIK KLQKRALQFQ GKVGLPKARR PWESDMRPEA EGDSEGEESE YFPTEEEEEE EDDEVEGAEA DLSG DGTDY ELKPLPKGGK RQKKVPVQEI DDDFFPSSGE EAEAASVGEG GGGGRKVGRY RDDGDEDYYK QRLRRWNKLR LQDKE KRLK LEDDSEESDA EFDEGFKVPG FLFKKLFKYQ QTGVRWLWEL HCQQAGGILG DEMGLGRTIQ IIAFLAGLSY SKIRTR GSN YRFEGLGPTV IVCPTTVMHQ WVKEFHTWWP PFRVAILHET GSYTHKKEKL IRDVAHCHGI LITSYSYIRL MQDDISR YD WHYVILDEGH KIRNPNAAVT LACKQFRTPH RIILSGSPMQ NNLRELWSLF DFIFPGKLGT LPVFMEQFSV PITMGGYS N ASPVQVKTAY KCACVLRDTI NPYLLRRMKS DVKMSLSLPD KNEQVLFCRL TDEQHKVYQN FVDSKEVYRI LNGEMQIFS GLIALRKICN HPDLFSGGPK NLKGLPDDEL EEDQFGYWKR SGKMIVVESL LKIWHKQGQR VLLFSQSRQM LDILEVFLRA QKYTYLKMD GTTTIASRQP LITRYNEDTS IFVFLLTTRV GGLGVNLTGA NRVVIYDPDW NPSTDTQARE RAWRIGQKKQ V TVYRLLTA GTIEEKIYHR QIFKQFLTNR VLKDPKQRRF FKSNDLYELF TLTSPDASQS TETSAIFAGT GSDVQTPKCH LK RRIQPAF GADHDVPKRK KFPASNISVN DATSSEEKSE AKGAEVNAVT SNRSDPLKDD PHMSSNVTSN DRLGEETNAV SGP EELSVI SGNGECSNSS GTGKTSMPSG DESIDEKLGL SYKRERPSQA QTEAFWENKQ MENNFYKHKS KTKHHSVAEE ETLE KHLRP KQKPKNSKHC RDAKFEGTRI PHLVKKRRYQ KQDSENKSEA KEQSNDDYVL EKLFKKSVGV HSVMKHDAIM DGASP DYVL VEAEANRVAQ DALKALRLSR QRCLGAVSGV PTWTGHRGIS GAPAGKKSRF GKKRNSNFSV QHPSSTSPTE KCQDGI MKK EGKDNVPEHF SGRAEDADSS SGPLASSSLL AKMRARNHLI LPERLESESG HLQEASALLP TTEHDDLLVE MRNFIAF QA HTDGQASTRE ILQEFESKLS ASQSCVFREL LRNLCTFHRT SGGEGIWKLK PEYC

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Macromolecule #25: UV-stimulated scaffold protein A

MacromoleculeName: UV-stimulated scaffold protein A / type: protein_or_peptide / ID: 25 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 80.993945 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: SNAMDQKLSK LVEELTTSGE PRLNPEKMKE LKKICKSSEE QLSRAYRLLI AQLTQEHAEI RLSAFQIVEE LFVRSHQFRM LVVSNFQEF LELTLGTDPA QPLPPPREAA QRLRQATTRA VEGWNEKFGE AYKKLALGYH FLRHNKKVDF QDTNARSLAE R KREEEKQK ...String:
SNAMDQKLSK LVEELTTSGE PRLNPEKMKE LKKICKSSEE QLSRAYRLLI AQLTQEHAEI RLSAFQIVEE LFVRSHQFRM LVVSNFQEF LELTLGTDPA QPLPPPREAA QRLRQATTRA VEGWNEKFGE AYKKLALGYH FLRHNKKVDF QDTNARSLAE R KREEEKQK HLDKIYQERA SQAEREMQEM SGEIESCLTE VESCFRLLVP FDFDPNPETE SLGMASGMSD ALRSSCAGQV GP CRSGTPD PRDGEQPCCS RDLPASAGHP RAGGGAQPSQ TATGDPSDED EDSDLEEFVR SHGLGSHKYT LDVELCSEGL KVQ ENEDNL ALIHAARDTL KLIRNKFLPA VCSWIQRFTR VGTHGGCLKR AIDLKAELEL VLRKYKELDI EPEGGERRRT EALG DAEED EDDEDFVEVP EKEGYEPHIP DHLRPEYGLE AAPEKDTVVR CLRTRTRMDE EVSDPTSAAA QLRQLRDHLP PPSSA SPSR ALPEPQEAQK LAAERARAPV VPYGVDLHYW GQELPTAGKI VKSDSQHRFW KPSEVEEEVV NADISEMLRS RHITFA GKF EPVQHWCRAP RPDGRLCERQ DRLKCPFHGK IVPRDDEGRP LDPEDRAREQ RRQLQKQERP EWQDPELMRD VEAATGQ DL GSSRYSGKGR GKKRRYPSLT NLKAQADTAR ARIGRKVFAK AAVRRVVAAM NRMDQKKHEK FSNQFNYALN

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Macromolecule #26: DNA damage-binding protein 1

MacromoleculeName: DNA damage-binding protein 1 / type: protein_or_peptide / ID: 26 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 127.369719 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: SNAMSYNYVV TAQKPTAVNG CVTGHFTSAE DLNLLIAKNT RLEIYVVTAE GLRPVKEVGM YGKIAVMELF RPKGESKDLL FILTAKYNA CILEYKQSGE SIDIITRAHG NVQDRIGRPS ETGIIGIIDP ECRMIGLRLY DGLFKVIPLD RDNKELKAFN I RLEELHVI ...String:
SNAMSYNYVV TAQKPTAVNG CVTGHFTSAE DLNLLIAKNT RLEIYVVTAE GLRPVKEVGM YGKIAVMELF RPKGESKDLL FILTAKYNA CILEYKQSGE SIDIITRAHG NVQDRIGRPS ETGIIGIIDP ECRMIGLRLY DGLFKVIPLD RDNKELKAFN I RLEELHVI DVKFLYGCQA PTICFVYQDP QGRHVKTYEV SLREKEFNKG PWKQENVEAE ASMVIAVPEP FGGAIIIGQE SI TYHNGDK YLAIAPPIIK QSTIVCHNRV DPNGSRYLLG DMEGRLFMLL LEKEEQMDGT VTLKDLRVEL LGETSIAECL TYL DNGVVF VGSRLGDSQL VKLNVDSNEQ GSYVVAMETF TNLGPIVDMC VVDLERQGQG QLVTCSGAFK EGSLRIIRNG IGIH EHASI DLPGIKGLWP LRSDPNRETD DTLVLSFVGQ TRVLMLNGEE VEETELMGFV DDQQTFFCGN VAHQQLIQIT SASVR LVSQ EPKALVSEWK EPQAKNISVA SCNSSQVVVA VGRALYYLQI HPQELRQISH TEMEHEVACL DITPLGDSNG LSPLCA IGL WTDISARILK LPSFELLHKE MLGGEIIPRS ILMTTFESSH YLLCALGDGA LFYFGLNIET GLLSDRKKVT LGTQPTV LR TFRSLSTTNV FACSDRPTVI YSSNHKLVFS NVNLKEVNYM CPLNSDGYPD SLALANNSTL TIGTIDEIQK LHIRTVPL Y ESPRKICYQE VSQCFGVLSS RIEVQDTSGG TTALRPSAST QALSSSVSSS KLFSSSTAPH ETSFGEEVEV HNLLIIDQH TFEVLHAHQF LQNEYALSLV SCKLGKDPNT YFIVGTAMVY PEEAEPKQGR IVVFQYSDGK LQTVAEKEVK GAVYSMVEFN GKLLASINS TVRLYEWTTE KELRTECNHY NNIMALYLKT KGDFILVGDL MRSVLLLAYK PMEGNFEEIA RDFNPNWMSA V EILDDDNF LGAENAFNLF VCQKDSAATT DEERQHLQEV GLFHLGEFVN VFCHGSLVMQ NLGETSTPTQ GSVLFGTVNG MI GLVTSLS ESWYNLLLDM QNRLNKVIKS VGKIEHSFWR SFHTERKTEP ATGFIDGDLI ESFLDISRPK MQEVVANLQY DDG SGMKRE ATADDLIKVV EELTRIH

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Macromolecule #27: Cullin-4A

MacromoleculeName: Cullin-4A / type: protein_or_peptide / ID: 27 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 88.086562 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: SNAMADEAPR KGSFSALVGR TNGLTKPAAL AAAPAKPGGA GGSKKLVIKN FRDRPRLPDN YTQDTWRKLH EAVRAVQSST SIRYNLEEL YQAVENLCSH KVSPMLYKQL RQACEDHVQA QILPFREDSL DSVLFLKKIN TCWQDHCRQM IMIRSIFLFL D RTYVLQNS ...String:
SNAMADEAPR KGSFSALVGR TNGLTKPAAL AAAPAKPGGA GGSKKLVIKN FRDRPRLPDN YTQDTWRKLH EAVRAVQSST SIRYNLEEL YQAVENLCSH KVSPMLYKQL RQACEDHVQA QILPFREDSL DSVLFLKKIN TCWQDHCRQM IMIRSIFLFL D RTYVLQNS TLPSIWDMGL ELFRTHIISD KMVQSKTIDG ILLLIERERS GEAVDRSLLR SLLGMLSDLQ VYKDSFELKF LE ETNCLYA AEGQRLMQER EVPEYLNHVS KRLEEEGDRV ITYLDHSTQK PLIACVEKQL LGEHLTAILQ KGLDHLLDEN RVP DLAQMY QLFSRVRGGQ QALLQHWSEY IKTFGTAIVI NPEKDKDMVQ DLLDFKDKVD HVIEVCFQKN ERFVNLMKES FETF INKRP NKPAELIAKH VDSKLRAGNK EATDEELERT LDKIMILFRF IHGKDVFEAF YKKDLAKRLL VGKSASVDAE KSMLS KLKH ECGAAFTSKL EGMFKDMELS KDIMVHFKQH MQNQSDSGPI DLTVNILTMG YWPTYTPMEV HLTPEMIKLQ EVFKAF YLG KHSGRKLQWQ TTLGHAVLKA EFKEGKKEFQ VSLFQTLVLL MFNEGDGFSF EEIKMATGIE DSELRRTLQS LACGKAR VL IKSPKGKEVE DGDKFIFNGE FKHKLFRIKI NQIQMKETVE EQVSTTERVF QDRQYQIDAA IVRIMKMRKT LGHNLLVS E LYNQLKFPVK PGDLKKRIES LIDRDYMERD KDNPNQYHYV A

+
Macromolecule #28: E3 ubiquitin-protein ligase RBX1

MacromoleculeName: E3 ubiquitin-protein ligase RBX1 / type: protein_or_peptide / ID: 28 / Number of copies: 1 / Enantiomer: LEVO / EC number: RING-type E3 ubiquitin transferase
Source (natural)Organism: Mus musculus (house mouse)
Molecular weightTheoretical: 12.289977 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString:
MAAAMDVDTP SGTNSGAGKK RFEVKKWNAV ALWAWDIVVD NCAICRNHIM DLCIECQANQ ASATSEECTV AWGVCNHAFH FHCISRWLK TRQVCPLDNR EWEFQKYGH

+
Macromolecule #14: NTS

MacromoleculeName: NTS / type: dna / ID: 14 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 14.494314 KDa
SequenceString:
(DC)(DT)(DA)(DG)(DT)(DT)(DG)(DA)(DT)(DC) (DT)(DC)(DA)(DT)(DA)(DT)(DT)(DT)(DC)(DA) (DT)(DT)(DC)(DC)(DT)(DA)(DC)(DT)(DC) (DA)(DG)(DG)(DA)(DG)(DA)(DA)(DG)(DG)(DA) (DG) (DC)(DA)(DG)(DA)(DG)(DC)(DG)

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Macromolecule #18: TS

MacromoleculeName: TS / type: dna / ID: 18 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 14.269129 KDa
SequenceString:
(DC)(DG)(DC)(DT)(DC)(DT)(DG)(DC)(DT)(DC) (DC)(DT)(DT)(DC)(DT)(DC)(DC)(DC)(DA)(DT) (DC)(DC)(DT)(DC)(DT)(DC)(DG)(DA)(DT) (DG)(DG)(DC)(DT)(DA)(DT)(DG)(DA)(DG)(DA) (DT) (DC)(DA)(DA)(DC)(DT)(DA)(DG)

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Macromolecule #15: RNA

MacromoleculeName: RNA / type: rna / ID: 15 / Number of copies: 1
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 14.490756 KDa
SequenceString:
ACAUCAUAAC AUUUGAACAA GAAUAUAUAU ACAAAAUCGA GAGGA

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Macromolecule #29: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 29 / Number of copies: 8 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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Macromolecule #30: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 30 / Number of copies: 1 / Formula: MG
Molecular weightTheoretical: 24.305 Da

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

Concentration0.3 mg/mL
BufferpH: 7.5
GridModel: Quantifoil R2/1 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Nominal magnification: 81000
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 40.4 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

-
Image processing

CTF correctionSoftware - Name: Warp
Initial angle assignmentType: PROJECTION MATCHING
Final angle assignmentType: PROJECTION MATCHING
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.0 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION
Details: Different number of particles was used for different focused refined maps.
Number images used: 100000
FSC plot (resolution estimation)

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