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- EMDB-50892: Influenza A/H7N9 polymerase pre-cleavage cap-snatching complex -

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Entry
Database: EMDB / ID: EMD-50892
TitleInfluenza A/H7N9 polymerase pre-cleavage cap-snatching complex
Map dataH7N9 cap-snatching pre-cleavage complex consensus
Sample
  • Complex: Influenza A/H7N9 polymerase pre-cleavage cap-snatching complex
    • Complex: Transcription elongation factors SPT4 and SPT5
      • Protein or peptide: x 3 types
    • Complex: RNA
      • RNA: x 3 types
    • Complex: Influenza virus RNA-dependent RNA polymerase
      • Protein or peptide: x 3 types
    • Complex: DNA
      • DNA: x 2 types
    • Complex: Human RNA polymerase II
      • Protein or peptide: x 12 types
  • Ligand: x 4 types
KeywordsInfluenza virus / influenza A / cap-snatching / transcription / VIRUS
Function / homology
Function and homology information


negative regulation of DNA-templated transcription, elongation / DSIF complex / regulation of transcription elongation by RNA polymerase II / 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 ...negative regulation of DNA-templated transcription, elongation / DSIF complex / regulation of transcription elongation by RNA polymerase II / 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 - 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 / Formation of TC-NER Pre-Incision Complex / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / mRNA Splicing - Major Pathway / positive regulation of DNA-templated transcription, elongation / Abortive elongation of HIV-1 transcript in the absence of Tat / transcription elongation-coupled chromatin remodeling / RNA Pol II CTD phosphorylation and interaction with CE during HIV infection / RNA Pol II CTD phosphorylation and interaction with CE / Formation of the Early Elongation Complex / Formation of the HIV-1 Early Elongation Complex / cap snatching / mRNA Capping / viral transcription / RNA polymerase II complex binding / symbiont-mediated suppression of host mRNA transcription via inhibition of RNA polymerase II activity / maintenance of transcriptional fidelity during transcription elongation by RNA polymerase II / negative regulation of transcription elongation by RNA polymerase II / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / RNA polymerase II transcribes snRNA genes / positive regulation of macroautophagy / host cell mitochondrion / 7-methylguanosine mRNA capping / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / Tat-mediated elongation of the HIV-1 transcript / RNA polymerase I complex / RNA polymerase III complex / Formation of HIV-1 elongation complex containing HIV-1 Tat / transcription elongation by RNA polymerase I / core promoter sequence-specific DNA binding / Formation of HIV elongation complex in the absence of HIV Tat / RNA polymerase II, core complex / tRNA transcription by RNA polymerase III / transcription by RNA polymerase I / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / transcription-coupled nucleotide-excision repair / translation initiation factor binding / RNA Polymerase II Pre-transcription Events / DNA-directed RNA polymerase complex / TP53 Regulates Transcription of DNA Repair Genes / transcription initiation at RNA polymerase II promoter / transcription elongation by RNA polymerase II / DNA-templated transcription initiation / positive regulation of transcription elongation by RNA polymerase II / euchromatin / mRNA transcription by RNA polymerase II / virion component / ribonucleoside binding / fibrillar center / DNA-directed RNA polymerase / DNA-directed RNA polymerase activity / endonuclease activity / transcription by RNA polymerase II / nucleic acid binding / Hydrolases; Acting on ester bonds / host cell cytoplasm / protein dimerization activity / nuclear speck / protein heterodimerization activity / symbiont-mediated suppression of host gene expression / viral translational frameshifting / RNA-directed RNA polymerase / hydrolase activity / viral RNA genome replication / nucleotide binding / RNA-directed RNA polymerase activity / mRNA binding / chromatin binding / DNA-templated transcription / regulation of DNA-templated transcription / nucleolus / host cell nucleus / enzyme binding / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / DNA binding / RNA binding
Similarity search - Function
Spt5, KOW domain repeat 6 / : / Transcription elongation factor SPT5, seventh KOW domain / Transcription elongation factor SPT5, sixth KOW domain / : / Transcription initiation Spt4 / Spt4 superfamily / Spt4/RpoE2 zinc finger / Spt4/RpoE2 zinc finger / Spt4/RpoE2 zinc finger ...Spt5, KOW domain repeat 6 / : / Transcription elongation factor SPT5, seventh KOW domain / Transcription elongation factor SPT5, sixth KOW domain / : / Transcription initiation Spt4 / Spt4 superfamily / Spt4/RpoE2 zinc finger / Spt4/RpoE2 zinc finger / Spt4/RpoE2 zinc finger / Transcription elongation factor SPT5, KOWx domain / Transcription elongation factor SPT5, second KOW domain / Transcription elongation factor SPT5, fifth KOW domain / Transcription elongation factor SPT5, KOW1 domain / Transcription elongation factor SPT5, fourth KOW domain / Transcription elongation factor Spt5, eukaryote / Spt5 transcription elongation factor, N-terminal / Spt5 C-terminal domain / Spt5, KOW domain repeat 2 / Spt5, KOW domain repeat 3 / Spt5, KOW domain repeat 5 / Spt5 transcription elongation factor, acidic N-terminal / Spt5 C-terminal nonapeptide repeat binding Spt4 / NGN domain, eukaryotic / Spt5, KOW domain repeat 1 / Spt5, KOW domain repeat 4 / NGN domain / Transcription elongation factor SPT5 / Early transcription elongation factor of RNA pol II, NGN section / Influenza RNA-dependent RNA polymerase subunit PB2 / PB2, C-terminal / Influenza RNA-dependent RNA polymerase subunit PB1 / Influenza RNA-dependent RNA polymerase subunit PB1 / : / : / Influenza RNA polymerase PB2 N-terminal region / Influenza RNA polymerase PB2 second domain / : / : / Influenza RNA polymerase PB2 middle domain / Influenza RNA polymerase PB2 C-terminal domain / : / Influenza RNA polymerase PB2 6th domain / : / Influenza RNA polymerase PB2 CAP binding domain / : / Influenza RNA polymerase PB2 helical domain / Polymerase acidic protein / NusG, N-terminal / In Spt5p, this domain may confer affinity for Spt4p. It possesses a RNP-like fold. / NusG, N-terminal domain superfamily / Influenza RNA-dependent RNA polymerase subunit PA / Influenza RNA-dependent RNA polymerase subunit PA, endonuclease domain / Influenza RNA-dependent RNA polymerase subunit PA / RNA-directed RNA polymerase, negative-strand RNA virus / RdRp of negative ssRNA viruses with segmented genomes catalytic domain profile. / DNA-directed RNA polymerase II subunit Rpb4-like / RNA polymerase Rpb1 C-terminal repeat / RNA polymerase II, heptapeptide repeat, eukaryotic / Eukaryotic RNA polymerase II heptapeptide repeat. / RNA polymerase Rpb1, domain 6 / RNA polymerase Rpb1, domain 6 / RNA polymerase Rpb4/RPC9, core / DNA-directed RNA-polymerase II subunit / RNA polymerase Rpb1, domain 7 / RNA polymerase Rpb1, domain 7 superfamily / RNA polymerase Rpb1, domain 7 / Pol II subunit B9, C-terminal zinc ribbon / RNA polymerase RBP11 / Rpb4/RPC9 superfamily / RNA polymerase subunit Rpb4/RPC9 / RNA polymerase Rpb4 / Zinc finger TFIIS-type signature. / 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 / HRDC-like superfamily / 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 RPB6 / DNA-directed RNA polymerase subunit RPABC5/Rpb10 / RNA polymerases, subunit N, zinc binding site / RNA polymerase subunit RPB10
Similarity search - Domain/homology
DNA-directed RNA polymerase subunit beta / DNA-directed RNA polymerase II subunit RPB4 / DNA-directed RNA polymerases I, II, and III subunit RPABC4 / DNA-directed RNA polymerases I, II, and III subunit RPABC2 / DNA-directed RNA polymerase subunit / DNA-directed RNA polymerases I, II, and III subunit RPABC5 / DNA-directed RNA polymerase II subunit RPB11-a / DNA-directed RNA polymerases I, II, and III subunit RPABC3 / DNA-directed RNA polymerase II subunit RPB3 / DNA-directed RNA polymerase subunit ...DNA-directed RNA polymerase subunit beta / DNA-directed RNA polymerase II subunit RPB4 / DNA-directed RNA polymerases I, II, and III subunit RPABC4 / DNA-directed RNA polymerases I, II, and III subunit RPABC2 / DNA-directed RNA polymerase subunit / DNA-directed RNA polymerases I, II, and III subunit RPABC5 / DNA-directed RNA polymerase II subunit RPB11-a / DNA-directed RNA polymerases I, II, and III subunit RPABC3 / DNA-directed RNA polymerase II subunit RPB3 / DNA-directed RNA polymerase subunit / DNA-directed RNA polymerases I, II, and III subunit RPABC1 / Polymerase acidic protein / RNA-directed RNA polymerase catalytic subunit / Transcription elongation factor SPT5 / DNA-directed RNA polymerase II subunit RPB9 / Transcription elongation factor SPT4 / Polymerase basic protein 2
Similarity search - Component
Biological speciesHomo sapiens (human) / Influenza B virus / Influenza A virus (A/Zhejiang/DTID-ZJU01/2013(H7N9)) / synthetic construct (others) / Sus scrofa domesticus (domestic pig)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.3 Å
AuthorsRotsch AH / Li D / Dienemann C / Cusack S / Cramer P
Funding support Germany, European Union, 2 items
OrganizationGrant numberCountry
German Research Foundation (DFG)SFB860 Germany
European Research Council (ERC)882357European Union
CitationJournal: Nature / Year: 2026
Title: Mechanism of co-transcriptional cap snatching by influenza polymerase.
Authors: Alexander Helmut Rotsch / Delong Li / Maud Dupont / Tim Krischuns / Ute Neef / Christiane Oberthür / Alice Stelfox / Maria Lukarska / Isaac Fianu / Michael Lidschreiber / Nadia Naffakh / ...Authors: Alexander Helmut Rotsch / Delong Li / Maud Dupont / Tim Krischuns / Ute Neef / Christiane Oberthür / Alice Stelfox / Maria Lukarska / Isaac Fianu / Michael Lidschreiber / Nadia Naffakh / Christian Dienemann / Stephen Cusack / Patrick Cramer /
Abstract: Influenza virus mRNAs are stable and competent for nuclear export and translation because they receive a 5' cap(1) structure in a process called cap snatching. During cap snatching, the viral RNA- ...Influenza virus mRNAs are stable and competent for nuclear export and translation because they receive a 5' cap(1) structure in a process called cap snatching. During cap snatching, the viral RNA-dependent RNA polymerase (FluPol) binds to host RNA polymerase II (Pol II) and the emerging transcript. The FluPol endonuclease then cleaves a capped RNA fragment that subsequently acts as a primer for the transcription of viral genes. Here we present the cryogenic electron microscopy structure of FluPol bound to a transcribing Pol II in complex with the elongation factor DSIF in the pre-cleavage state. The structure shows that FluPol directly interacts with both Pol II and DSIF, positioning the FluPol endonuclease domain near the RNA exit channel of Pol II. These interactions are important for the endonuclease activity of FluPol and FluPol activity in cells. A second structure, trapped after cap snatching, shows that the cleaved capped RNA rearranges within FluPol, directing the capped RNA 3' end toward the FluPol polymerase active site for viral transcription initiation. Together, our results provide the molecular mechanisms of co-transcriptional cap snatching by FluPol.
History
DepositionJul 4, 2024-
Header (metadata) releaseJul 16, 2025-
Map releaseJul 16, 2025-
UpdateMar 11, 2026-
Current statusMar 11, 2026Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_50892.png

Downloads & links

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Map

FileDownload / File: emd_50892.map.gz / Format: CCP4 / Size: 343 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationH7N9 cap-snatching pre-cleavage complex consensus
Projections & slices

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AxesZ (Sec.)Y (Row.)X (Col.)
1.05 Å/pix.
x 448 pix.
= 470.4 Å		1.05 Å/pix.
x 448 pix.
= 470.4 Å		1.05 Å/pix.
x 448 pix.
= 470.4 Å

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Voxel sizeX=Y=Z: 1.05 Å
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Contour LevelBy AUTHOR: 0.007
Minimum - Maximum-0.0067321057 - 0.028166644
Average (Standard dev.)0.000031959775 (±0.0010094168)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions448448448
Spacing448448448
CellA=B=C: 470.39996 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_50892_msk_1.map
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Mask #2

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Mask #3

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Additional map: H7N9 cap-snatching pre-cleavage complex Pol II focussed refinement

Fileemd_50892_additional_1.map
AnnotationH7N9 cap-snatching pre-cleavage complex Pol II focussed refinement
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Additional map: H7N9 cap-snatching pre-cleavage complex consensus, post processed

Fileemd_50892_additional_2.map
AnnotationH7N9 cap-snatching pre-cleavage complex consensus, post processed
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Additional map: H7N9 cap-snatching pre-cleavage complex Pol II focussed refinement,...

Fileemd_50892_additional_3.map
AnnotationH7N9 cap-snatching pre-cleavage complex Pol II focussed refinement, post processed
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Additional map: H7N9 cap-snatching pre-cleavage complex Pol II focussed refinement,...

Fileemd_50892_additional_4.map
AnnotationH7N9 cap-snatching pre-cleavage complex Pol II focussed refinement, Halfmap 1
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Additional map: H7N9 cap-snatching pre-cleavage complex Pol II focussed refinement,...

Fileemd_50892_additional_5.map
AnnotationH7N9 cap-snatching pre-cleavage complex Pol II focussed refinement, Halfmap 2
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Additional map: H7N9 cap-snatching pre-cleavage complex FluPol focussed refinement, post...

Fileemd_50892_additional_6.map
AnnotationH7N9 cap-snatching pre-cleavage complex FluPol focussed refinement, post processed
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Additional map: H7N9 cap-snatching pre-cleavage complex FluPol focussed refinement

Fileemd_50892_additional_7.map
AnnotationH7N9 cap-snatching pre-cleavage complex FluPol focussed refinement
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Additional map: H7N9 cap-snatching pre-cleavage complex FluPol focussed refinement, Halfmap...

Fileemd_50892_additional_8.map
AnnotationH7N9 cap-snatching pre-cleavage complex FluPol focussed refinement, Halfmap 1
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Additional map: H7N9 cap-snatching pre-cleavage complex FluPol focussed refinement, Halfmap...

Fileemd_50892_additional_9.map
AnnotationH7N9 cap-snatching pre-cleavage complex FluPol focussed refinement, Halfmap 2
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Half map: H7N9 cap-snatching pre-cleavage complex consensus, half map 1

Fileemd_50892_half_map_1.map
AnnotationH7N9 cap-snatching pre-cleavage complex consensus, half map 1
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Half map: H7N9 cap-snatching pre-cleavage complex consensus, half map 2

Fileemd_50892_half_map_2.map
AnnotationH7N9 cap-snatching pre-cleavage complex consensus, half map 2
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Sample components

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Entire : Influenza A/H7N9 polymerase pre-cleavage cap-snatching complex

EntireName: Influenza A/H7N9 polymerase pre-cleavage cap-snatching complex
Components
  • Complex: Influenza A/H7N9 polymerase pre-cleavage cap-snatching complex
    • Complex: Transcription elongation factors SPT4 and SPT5
      • Protein or peptide: Transcription elongation factor SPT4
      • Protein or peptide: Transcription elongation factor SPT5
      • Protein or peptide: Likely SPT5 KOWx4-KOW5 linker, register unclear
    • Complex: RNA
      • RNA: cap(1)-RNA (35-MER)
      • RNA: 3' vRNA
      • RNA: 5'-vRNA
    • Complex: Influenza virus RNA-dependent RNA polymerase
      • Protein or peptide: Polymerase acidic protein
      • Protein or peptide: RNA-directed RNA polymerase catalytic subunit
      • Protein or peptide: Polymerase basic protein 2
    • Complex: DNA
      • DNA: non-template DNA (43-mer)
      • DNA: Template DNA (43-MER)
    • Complex: Human RNA polymerase II
      • Protein or peptide: RNA polymerase II subunit D
      • Protein or peptide: DNA-directed RNA polymerase II subunit E
      • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC2
      • Protein or peptide: DNA-directed RNA polymerase subunit
      • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC3
      • Protein or peptide: DNA-directed RNA polymerase II subunit RPB9
      • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC5
      • Protein or peptide: DNA-directed RNA polymerase II subunit RPB11-a
      • Protein or peptide: RNA polymerase II, I and III subunit K
      • Protein or peptide: DNA-directed RNA polymerase subunit
      • Protein or peptide: DNA-directed RNA polymerase subunit beta
      • Protein or peptide: DNA-directed RNA polymerase II subunit RPB3
  • Ligand: ZINC ION
  • Ligand: 7-METHYL-GUANOSINE-5'-TRIPHOSPHATE-5'-(2'-O-METHYL)-GUANOSINE
  • Ligand: MAGNESIUM ION
  • Ligand: PHOSPHATE ION

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Supramolecule #1: Influenza A/H7N9 polymerase pre-cleavage cap-snatching complex

SupramoleculeName: Influenza A/H7N9 polymerase pre-cleavage cap-snatching complex
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#23

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Supramolecule #2: Transcription elongation factors SPT4 and SPT5

SupramoleculeName: Transcription elongation factors SPT4 and SPT5 / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #13-#14, #23
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #3: RNA

SupramoleculeName: RNA / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #11, #21-#22
Source (natural)Organism: Influenza B virus

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Supramolecule #4: Influenza virus RNA-dependent RNA polymerase

SupramoleculeName: Influenza virus RNA-dependent RNA polymerase / type: complex / ID: 4 / Parent: 1 / Macromolecule list: #18-#20
Source (natural)Organism: Influenza A virus (A/Zhejiang/DTID-ZJU01/2013(H7N9))

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Supramolecule #5: DNA

SupramoleculeName: DNA / type: complex / ID: 5 / Parent: 1 / Macromolecule list: #10, #12
Source (natural)Organism: synthetic construct (others)

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Supramolecule #6: Human RNA polymerase II

SupramoleculeName: Human RNA polymerase II / type: complex / ID: 6 / Parent: 1 / Macromolecule list: #1-#9, #15-#17
Source (natural)Organism: Sus scrofa domesticus (domestic pig)

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Macromolecule #1: RNA polymerase II subunit D

MacromoleculeName: RNA polymerase II subunit D / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa domesticus (domestic pig)
Molecular weightTheoretical: 20.962621 KDa
SequenceString:
MWGPAQPYSD SALSPKPRPF RAVFRGSALP FPAVRVEVRG RSMAAGGSDP RAGDVEEDAS QLIFPKEFET AETLLNSEVH MLLEHRKQQ NESAEDEQEL SEVFMKTLNY TARFSRFKNR ETIASVRSLL LQKKLHKFEL ACLANLCPET AEESKALIPS L EGRFEDEE LQQILDDIQT KRSFQY

UniProtKB: DNA-directed RNA polymerase II subunit RPB4

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Macromolecule #2: DNA-directed RNA polymerase II subunit E

MacromoleculeName: DNA-directed RNA polymerase II subunit E / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa domesticus (domestic 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

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

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Macromolecule #3: 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: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa domesticus (domestic pig)
Molecular weightTheoretical: 14.477001 KDa
SequenceString:
MSDNEDNFDG DDFDDVEEDE GLDDLENAEE EGQENVEILP SGERPQANQK RITTPYMTKY ERARVLGTRA LQIAMCAPVM VELEGETDP LLIAMKELKA RKIPIIIRRY LPDGSYEDWG VDELIISD

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

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Macromolecule #4: DNA-directed RNA polymerase subunit

MacromoleculeName: DNA-directed RNA polymerase subunit / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa domesticus (domestic pig)
Molecular weightTheoretical: 19.227205 KDa
SequenceString:
MFYHISLEHE ILLHPRYFGP NLLNTVKQKL FTEVEGTCTG KYGFVIAVTT IDNIGAGVIQ PGRGFVLYPV KYKAIVFRPF KGEVVDAVV TQVNKVGLFT EIGPMSCFIS RHSIPSEMEF DPNSNPPCYK TMDEDIVIQQ DDEIRLKIVG TRVDKNDIFA I GSLMDDYL GLV

UniProtKB: DNA-directed RNA polymerase subunit

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Macromolecule #5: 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: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa domesticus (domestic pig)
Molecular weightTheoretical: 17.162273 KDa
SequenceString:
MAGILFEDIF DVKDIDPEGK KFDRVSRLHC ESESFKMDLI LDVNIQIYPV DLGDKFRLVI ASTLYEDGTL DDGEYNPTDD RPSRADQFE YVMYGKVYRI EGDETSTEAA TRLSAYVSYG GLLMRLQGDA NNLHGFEVDS RVYLLMKKLA F

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

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Macromolecule #6: DNA-directed RNA polymerase II subunit RPB9

MacromoleculeName: DNA-directed RNA polymerase II subunit RPB9 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa domesticus (domestic pig)
Molecular weightTheoretical: 14.541221 KDa
SequenceString:
MEPDGTYEPG FVGIRFCQEC NNMLYPKEDK ENRILLYACR NCDYQQEADN SCIYVNKITH EVDELTQIIA DVSQDPTLPR TEDHPCQKC GHKEAVFFQS HSARAEDAMR LYYVCTAPHC GHRWTE

UniProtKB: DNA-directed RNA polymerase II subunit RPB9

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Macromolecule #7: 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: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa domesticus (domestic pig)
Molecular weightTheoretical: 7.655123 KDa
SequenceString:
MIIPVRCFTC GKIVGNKWEA YLGLLQAEYT EGDALDALGL KRYCCRRMLL AHVDLIEKLL NYAPLEK

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

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Macromolecule #8: DNA-directed RNA polymerase II subunit RPB11-a

MacromoleculeName: DNA-directed RNA polymerase II subunit RPB11-a / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa domesticus (domestic pig)
Molecular weightTheoretical: 13.310284 KDa
SequenceString:
MNAPPAFESF LLFEGEKKIT INKDTKVPNA CLFTINKEDH TLGNIIKSQL LKDPQVLFAG YKVPHPLEHK IIIRVQTTPD YSPQEAFTN AITDLISELS LLEERFRVAI KDKQEGIE

UniProtKB: DNA-directed RNA polymerase II subunit RPB11-a

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Macromolecule #9: RNA polymerase II, I and III subunit K

MacromoleculeName: RNA polymerase II, I and III subunit K / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa domesticus (domestic pig)
Molecular weightTheoretical: 7.018244 KDa
SequenceString:
MDTQKDVQPP KQQPMIYICG ECHTENEIKS RDPIRCRECG YRIMYKKRTK RLVVFDAR

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

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Macromolecule #13: Transcription elongation factor SPT4

MacromoleculeName: Transcription elongation factor SPT4 / type: protein_or_peptide / ID: 13 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 13.210201 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MALETVPKDL RHLRACLLCS LVKTIDQFEY DGCDNCDAYL QMKGNREMVY DCTSSSFDGI IAMMSPEDSW VSKWQRVSNF KPGVYAVSV TGRLPQGIVR ELKSRGVAYK SRDTAIKT

UniProtKB: Transcription elongation factor SPT4

+
Macromolecule #14: Transcription elongation factor SPT5

MacromoleculeName: Transcription elongation factor SPT5 / type: protein_or_peptide / ID: 14 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 121.145477 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MSDSEDSNFS EEEDSERSSD GEEAEVDEER RSAAGSEKEE EPEDEEEEEE EEEYDEEEEE EDDDRPPKKP RHGGFILDEA DVDDEYEDE DQWEDGAEDI LEKEEIEASN IDNVVLDEDR SGARRLQNLW RDQREEELGE YYMKKYAKSS VGETVYGGSD E LSDDITQQ ...String:
MSDSEDSNFS EEEDSERSSD GEEAEVDEER RSAAGSEKEE EPEDEEEEEE EEEYDEEEEE EDDDRPPKKP RHGGFILDEA DVDDEYEDE DQWEDGAEDI LEKEEIEASN IDNVVLDEDR SGARRLQNLW RDQREEELGE YYMKKYAKSS VGETVYGGSD E LSDDITQQ QLLPGVKDPN LWTVKCKIGE ERATAISLMR KFIAYQFTDT PLQIKSVVAP EHVKGYIYVE AYKQTHVKQA IE GVGNLRL GYWNQQMVPI KEMTDVLKVV KEVANLKPKS WVRLKRGIYK DDIAQVDYVE PSQNTISLKM IPRIDYDRIK ARM SLKDWF AKRKKFKRPP QRLFDAEKIR SLGGDVASDG DFLIFEGNRY SRKGFLFKSF AMSAVITEGV KPTLSELEKF EDQP EGIDL EVVTESTGKE REHNFQPGDN VEVCEGELIN LQGKILSVDG NKITIMPKHE DLKDMLEFPA QELRKYFKMG DHVKV IAGR FEGDTGLIVR VEENFVILFS DLTMHELKVL PRDLQLCSET ASGVDVGGQH EWGELVQLDP QTVGVIVRLE RETFQV LNM YGKVVTVRHQ AVTRKKDNRF AVALDSEQNN IHVKDIVKVI DGPHSGREGE IRHLFRSFAF LHCKKLVENG GMFVCKT RH LVLAGGSKPR DVTNFTVGGF APMSPRISSP MHPSAGGQRG GFGSPGGGSG GMSRGRGRRD NELIGQTVRI SQGPYKGY I GVVKDATEST ARVELHSTCQ TISVDRQRLT TVGSRRPGGM TSTYGRTPMY GSQTPMYGSG SRTPMYGSQT PLQDGSRTP HYGSQTPLHD GSRTPAQSGA WDPNNPNTPS RAEEEYEYAF DDEPTPSPQA YGGTPNPQTP GYPDPSSPQV NPQYNPQTPG TPAMYNTDQ FSPYAAPSPQ GSYQPSPSPQ SYHQVAPSPA GYQNTHSPAS YHPTPSPMAY QASPSPSPVG YSPMTPGAPS P GGYNPHTP GSGIEQNSSD WVTTDIQVKV RDTYLDTQVV GQTGVIRSVT GGMCSVYLKD SEKVVSISSE HLEPITPTKN NK VKVILGE DREATGVLLS IDGEDGIVRM DLDEQLKILN LRFLGKLLEA

UniProtKB: Transcription elongation factor SPT5

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Macromolecule #15: DNA-directed RNA polymerase subunit

MacromoleculeName: DNA-directed RNA polymerase subunit / type: protein_or_peptide / ID: 15 / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA-directed RNA polymerase
Source (natural)Organism: Sus scrofa domesticus (domestic pig)
Molecular weightTheoretical: 183.24425 KDa
SequenceString: SACPLRTIKR VQFGVLSPDE LKRMSVTEGG IKYPETTEGG RPKLGGLMDP RQGVIERTGR CQTCAGNMTE CPGHFGHIEL AKPVFHVGF LVKTMKVLRC VCFFCSKLLV DSNNPKIKDI LAKSKGQPKK RLTHVYDLCK GKNICEGGEE MDNKFGVEQP E GDEDLTKE ...String:
SACPLRTIKR VQFGVLSPDE LKRMSVTEGG IKYPETTEGG RPKLGGLMDP RQGVIERTGR CQTCAGNMTE CPGHFGHIEL AKPVFHVGF LVKTMKVLRC VCFFCSKLLV DSNNPKIKDI LAKSKGQPKK RLTHVYDLCK GKNICEGGEE MDNKFGVEQP E GDEDLTKE KGHGGCGRYQ PRIRRSGLEL YAEWKHVNED SQEKKILLSP ERVHEIFKRI SDEECFVLGM EPRYARPEWM IV TVLPVPP LSVRPAVVMQ GSARNQDDLT HKLADIVKIN NQLRRNEQNG AAAHVIAEDV KLLQFHVATM VDNELPGLPR AMQ KSGRPL KSLKQRLKGK EGRVRGNLMG KRVDFSARTV ITPDPNLSID QVGVPRSIAA NMTFAEIVTP FNIDRLQELV RRGN SQYPG AKYIIRDNGD RIDLRFHPKP SDLHLQTGYK VERHMCDGDI VIFNRQPTLH KMSMMGHRVR ILPWSTFRLN LSVTT PYNA DFDGDEMNLH LPQSLETRAE IQELAMVPRM IVTPQSNRPV MGIVQDTLTA VRKFTKRDVF LERGEVMNLL MFLSTW DGK VPQPAILKPR PLWTGKQIFS LIIPGHINCI RTHSTHPDDE DSGPYKHISP GDTKVVVENG ELIMGILCKK SLGTSAG SL VHISYLEMGH DITRLFYSNI QTVINNWLLI EGHTIGIGDS IADSKTYQDI QNTIKKAKQD VIEVIEKAHN NELEPTPG N TLRQTFENQV NRILNDARDK TGSSAQKSLS EYNNFKSMVV SGAKGSKINI SQVIAVVGQQ NVEGKRIPFG FKHRTLPHF IKDDYGPESR GFVENSYLAG LTPTEFFFHA MGGREGLIDT AVKTAETGYI QRRLIKSMES VMVKYDATVR NSINQVVQLR YGEDGLAGE SVEFQNLATL KPSNKAFEKK FRFDYTNERA LRRTLQEDLV KDVLSNAHIQ NELEREFERM REDREVLRVI F PTGDSKVV LPCNLLRMIW NAQKIFHINP RLPSDLHPIK VVEGVKELSK KLVIVNGDDP LSRQAQENAT LLFNIHLRST LC SRRMAEE FRLSGEAFDW LLGEIESKFN QAIAHPGEMV GALAAQSLGE PATQMTLNTF HYAGVSAKNV TLGVPRLKEL INI SKKPKT PSLTVFLLGQ SARDAERAKD ILCRLEHTTL RKVTANTAIY YDPNPQSTVV AEDQEWVNVY YEMPDFDVAR ISPW LLRVE LDRKHMTDRK LTMEQIAEKI NAGFGDDLNC IFNDDNAEKL VLRIRIMNSD ENKMQEEEEV VDKMDDDVFL RCIES NMLT DMTLQGIEQI SKVYMHLPQT DNKKKIIITE DGEFKALQEW ILETDGVSLM RVLSEKDVDP VRTTSNDIVE IFTVLG IEA VRKALERELY HVISFDGSYV NYRHLALLCD TMTCRGHLMA ITRHGVNRQD TGPLMKCSFE ETVDVLMEAA AHGESDP MK GVSENIMLGQ LAPAGTGCFD LLLDAEKCKY GMEIPTNIPG LGAAGPTGMF FGSAPSPMGG ISPAMTPWNQ GATPAYGA W SPSVGSGMTP GAAGFSPSAA SDASGFSPGY SPAWSPTPGS PGSPGPSSPY IPSPGGAMSP SYSPTSPAYE PRSPGGYTP QSPSYSPTSP SYSPT(SEP)PSYS PTSPNYSPTS PSYSPT(SEP)PSY S

UniProtKB: DNA-directed RNA polymerase subunit

+
Macromolecule #16: DNA-directed RNA polymerase subunit beta

MacromoleculeName: DNA-directed RNA polymerase subunit beta / type: protein_or_peptide / ID: 16 / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA-directed RNA polymerase
Source (natural)Organism: Sus scrofa domesticus (domestic pig)
Molecular weightTheoretical: 132.30475 KDa
SequenceString: DEITPDLWQE ACWIVISSYF DEKGLVRQQL DSFDEFIQMS VQRIVEDAPP IDLQAEAQHA SGEVEEPPRY LLKFEQIYLS KPTHWERDG APSPMMPNEA RLRNLTYSAP LYVDITKTVI KEGEEQLQTQ HQKTFIGKIP IMLRSTYCLL NGLTDRDLCE L NECPLDPG ...String:
DEITPDLWQE ACWIVISSYF DEKGLVRQQL DSFDEFIQMS VQRIVEDAPP IDLQAEAQHA SGEVEEPPRY LLKFEQIYLS KPTHWERDG APSPMMPNEA RLRNLTYSAP LYVDITKTVI KEGEEQLQTQ HQKTFIGKIP IMLRSTYCLL NGLTDRDLCE L NECPLDPG GYFIINGSEK VLIAQEKMAT NTVYVFAKKD SKYAYTGECR SCLENSSRPT STIWVSMLAR GGQGAKKSAI GQ RIVATLP YIKQEVPIII VFRALGFVSD RDILEHIIYD FEDPEMMEMV KPSLDEAFVI QEQNVALNFI GSRGAKPGVT KEK RIKYAK EVLQKEMLPH VGVSDFCETK KAYFLGYMVH RLLLAALGRR ELDDRDHYGN KRLDLAGPLL AFLFRGMFKN LLKE VRIYA QKFIDRGKDF NLELAIKTRI ISDGLKYSLA TGNWGDQKKA HQARAGVSQV LNRLTFASTL SHLRRLNSPI GRDGK LAKP RQLHNTLWGM VCPAETPEGH AVGLVKNLAL MAYISVGSQP SPILEFLEEW SMENLEEISP AAIADATKIF VNGCWV GIH KDPEQLMNTL RKLRRQMDII VSEVSMIRDI REREIRIYTD AGRICRPLLI VEKQKLLLKK RHIDQLKERE YNNYSWQ DL VASGVVEYID TLEEETVMLA MTPDDLQEKE VAYCSTYTHC EIHPSMILGV CASIIPFPDH NQSPRNTYQS AMGKQAMG V YITNFHVRMD TLAHVLYYPQ KPLVTTRSME YLRFRELPAG INSIVAIASY TGYNQEDSVI MNRSAVDRGF FRSVFYRSY KEQESKKGFD QEEVFEKPTR ETCQGMRHAI YDKLDDDGLI APGVRVSGDD VIIGKTVTLP ENEDELEGTN RRYTKRDCST FLRTSETGI VDQVMVTLNQ EGYKFCKIRV RSVRIPQIGD KFASRHGQKG TCGIQYRQED MPFTCEGITP DIIINPHAIP S RMTIGHLI ECLQGKVSAN KGEIGDATPF NDAVNVQKIS NLLSDYGYHL RGNEVLYNGF TGRKITSQIF IGPTYYQRLK HM VDDKIHS RARGPIQILN RQPMEGRSRD GGLRFGEMER DCQIAHGAAQ FLRERLFEAS DPYQVHVCNL CGIMAIANTR THT YECRGC RNKTQISLVR MPYACKLLFQ ELMSMSIAPR MMSV

UniProtKB: DNA-directed RNA polymerase subunit beta

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Macromolecule #17: DNA-directed RNA polymerase II subunit RPB3

MacromoleculeName: DNA-directed RNA polymerase II subunit RPB3 / type: protein_or_peptide / ID: 17 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa domesticus (domestic 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

UniProtKB: DNA-directed RNA polymerase II subunit RPB3

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Macromolecule #18: Polymerase acidic protein

MacromoleculeName: Polymerase acidic protein / type: protein_or_peptide / ID: 18 / Number of copies: 1 / Enantiomer: LEVO / EC number: Hydrolases; Acting on ester bonds
Source (natural)Organism: Influenza A virus (A/Zhejiang/DTID-ZJU01/2013(H7N9))
Molecular weightTheoretical: 82.91657 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: GMEDFVRQCF NPMIVELAEK AMKEYGEDPK IETNKFASIC THLEVCFMYS DFHFIDERGE STIIESGDPN VLLKHRFEII EGRDRTMAW TVVNSICNTT GVEKPKFLPD LYDYKENRFI DIGVTRREVH IYYLEKANKI KSEKTHIHIF SFTGEEMATK A DYTLDEES ...String:
GMEDFVRQCF NPMIVELAEK AMKEYGEDPK IETNKFASIC THLEVCFMYS DFHFIDERGE STIIESGDPN VLLKHRFEII EGRDRTMAW TVVNSICNTT GVEKPKFLPD LYDYKENRFI DIGVTRREVH IYYLEKANKI KSEKTHIHIF SFTGEEMATK A DYTLDEES RARIKTRLFT IRQEMASRGL WDSFRQSERG EETIEERFEI TGTMRRLADQ SLPPNFSSLE NFRAYVDGFE PN GCIEGKL SQMSKEVNAR IEPFLRTTPR PLRLPDGPPC SQRSKFLLMD ALKLSIEDPS HEGEGIPLYD AIKCMKTFFG WKE PNIIKP HEKGINPNYL LTWKQVLAEL QDIENEEKIP RTKNMKKTSQ LKWALGENMA PEKVDFEDCK DVNDLKQYDS DEPE PRSLA CWIQSEFNKA CELTDSSWVE LDEIGEDVAP IEHIASMRRN YFTAEVSHCR ATEYIMKGVY INTALLNASC AAMDD FQLI PMISKCRTKE GRRKTNLYGF IIKGRSHLRN DTDVVNFVSM EFSLTDPRLE PHKWEKYCVL EIGDMLLRTA VGQVSR PMF LYVRTNGTSK IKMKWGMEMR RCLLQSLQQI ESMIEAESSV KEKDLTKEFF ENKSETWPIG ESPKGVEEGS IGKVCRT LL AKSVFNSLYA SPQLEGFSAE SRKLLLIVQA LRDNLEPGTF DLEGLYEAIE ECLINDPWVL LNASWFNSFL THALR

UniProtKB: Polymerase acidic protein

+
Macromolecule #19: RNA-directed RNA polymerase catalytic subunit

MacromoleculeName: RNA-directed RNA polymerase catalytic subunit / type: protein_or_peptide / ID: 19 / Number of copies: 1 / Enantiomer: LEVO / EC number: RNA-directed RNA polymerase
Source (natural)Organism: Influenza A virus (A/Zhejiang/DTID-ZJU01/2013(H7N9))
Molecular weightTheoretical: 86.496156 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MDVNPTLLFL KVPVQNAIST TFPYTGDPPY SHGTGTGYTM DTVNRTHKYS EKGKWTTNTE TGAPQLNPID GPLPEDNEPS GYAQTDCVL EAMAFLEESH PGIFENSCLE TMEIVQQTRV DKLTQGRQTY DWTLNRNQPA ATALANTIEV FRSNGLTANE S GRLIDFLK ...String:
MDVNPTLLFL KVPVQNAIST TFPYTGDPPY SHGTGTGYTM DTVNRTHKYS EKGKWTTNTE TGAPQLNPID GPLPEDNEPS GYAQTDCVL EAMAFLEESH PGIFENSCLE TMEIVQQTRV DKLTQGRQTY DWTLNRNQPA ATALANTIEV FRSNGLTANE S GRLIDFLK DVMDSMDKEE MEITTHFQRK RRVRDNMTKK MVTQRTIGKK KQRLNKRSYL IRALTLNTMT KDAERGKLKR RA IATPGMQ IRGFVYFVEA LARSICEKLE QSGLPVGGNE KKAKLANVVR KMMTNSQDTE LSFTITGDNT KWNENQNPRM FLA MITYIT RNQPEWFRNV LSIAPIMFSN KMARLGKGYM FESKSMKLRT QVPAEMLANI DLKYFNKSTR EKIEKIRPLL IDGT ASLSP GMMMGMFNML STVLGVSILN LGQKKYTKTT YWWDGLQSSD DFALIVNAPN HEGIQAGVDR FYRTCKLVGI NMSKK KSYI NRTGTFEFTS FFYRYGFVAN FSMELPSFGV SGINESADMS VGVTVIKNNM INNDLGPATA QMALQLFIKD YRYTYR CHR GDTQIQTRRA FELKKLWEQT RSKAGLLVSD GGPNLYNIRN LHIPEVCLKW ELMDEDYQGR LCNPMNPFVS HKEIDSV NN AVVMPAHGPA KSMEYDAVAT THSWIPKRNR SILNTSQRGI LEDEQMYQKC CNLFEKFFPS SSYRRPVGIS SMVEAMVS R ARIDARIDFE SGRIKKEEFA EIMKICSTIE ELRRQK

UniProtKB: RNA-directed RNA polymerase catalytic subunit

+
Macromolecule #20: Polymerase basic protein 2

MacromoleculeName: Polymerase basic protein 2 / type: protein_or_peptide / ID: 20 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Influenza A virus (A/Zhejiang/DTID-ZJU01/2013(H7N9))
Molecular weightTheoretical: 86.00732 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MERIKELRDL MSQSRTREIL TKTTVDHMAI IKKYTSGRQE KNPALRMKWM MAMKYPITAD KRIMEMIPER NEQGQTLWSK TNDAGSDRV MVSPLAVTWW NRNGPTTSTV HYPKVYKTYF EKVERLKHGT FGPVHFRNQV KIRRRVDINP GHADLSAKEA Q DVIMEVVF ...String:
MERIKELRDL MSQSRTREIL TKTTVDHMAI IKKYTSGRQE KNPALRMKWM MAMKYPITAD KRIMEMIPER NEQGQTLWSK TNDAGSDRV MVSPLAVTWW NRNGPTTSTV HYPKVYKTYF EKVERLKHGT FGPVHFRNQV KIRRRVDINP GHADLSAKEA Q DVIMEVVF PNEVGARILT SESQLTITKE KKKELQDCKI APLMVAYMLE RELVRKTRFL PVAGGTSSVY IEVLHLTQGT CW EQMYTPG GEVRNDDVDQ SLIIAARNIV RRATVSADPL ASLLEMCHST QIGGVRMVDI LRQNPTEEQA VDICKAAMGL RIS SSFSFG GFTFKRTSGS SVKREEEVLT GNLQTLKIRV HEGYEEFTMV GRRATAILRK ATRRLIQLIV SGKDEQSIAE AIIV AMVFS QEDCMIKAVR GDLNFVNRAN QRLNPMHQLL RHFQKDAKVL FQNWGIEPID NVMGMIGILP DMTPSTEMSL RGVRV SKMG VDEYSSTERV VVSIDRFLRV RDQRGNVLLS PEEVSETQGT EKLTITYSSS MMWEINGPES VLVNTYQWII RNWENV KIQ WSQDPTMLYN KMEFEPFQSL VPKAARGQYS GFVRVLFQQM RDVLGTFDTV QIIKLLPFAA APPEQSRMQF SSLTVNV RG SGMRIVVRGN SPVFNYNKAT KRLTVLGKDA GALMEDPDEG TAGVESAVLR GFLILGKENK RYGPALSINE LSNLAKGE K ANVLIGQGDV VLVMKRKRDS SILTDSQTAT KRIRMAIN

UniProtKB: Polymerase basic protein 2

+
Macromolecule #23: Likely SPT5 KOWx4-KOW5 linker, register unclear

MacromoleculeName: Likely SPT5 KOWx4-KOW5 linker, register unclear / type: protein_or_peptide / ID: 23 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 1.288408 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
AAAAAFAAAG AAAAAAA

+
Macromolecule #10: non-template DNA (43-mer)

MacromoleculeName: non-template DNA (43-mer) / type: dna / ID: 10 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 13.303563 KDa
SequenceString:
(DG)(DG)(DC)(DA)(DG)(DT)(DA)(DC)(DT)(DA) (DG)(DT)(DA)(DT)(DT)(DC)(DT)(DA)(DG)(DT) (DA)(DT)(DT)(DG)(DA)(DA)(DA)(DG)(DT) (DA)(DC)(DT)(DT)(DG)(DA)(DG)(DC)(DT)(DT) (DG) (DA)(DT)(DC)

+
Macromolecule #12: Template DNA (43-MER)

MacromoleculeName: Template DNA (43-MER) / type: dna / ID: 12 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 13.178483 KDa
SequenceString:
(DG)(DA)(DT)(DC)(DA)(DA)(DG)(DC)(DT)(DC) (DA)(DA)(DG)(DT)(DA)(DC)(DT)(DT)(DA)(DA) (DG)(DC)(DC)(DT)(DG)(DG)(DT)(DC)(DT) (DA)(DT)(DA)(DC)(DT)(DA)(DG)(DT)(DA)(DC) (DT) (DG)(DC)(DC)

+
Macromolecule #11: cap(1)-RNA (35-MER)

MacromoleculeName: cap(1)-RNA (35-MER) / type: rna / ID: 11 / Number of copies: 1
Source (natural)Organism: Influenza B virus
Molecular weightTheoretical: 11.461053 KDa
SequenceString:
GAAGCGAGAA GAACACAGAC AGCAGAAGAC CAGGC

+
Macromolecule #21: 3' vRNA

MacromoleculeName: 3' vRNA / type: rna / ID: 21 / Number of copies: 1
Source (natural)Organism: Influenza B virus
Molecular weightTheoretical: 4.008358 KDa
SequenceString:
CUCUGCUUCU GCU

+
Macromolecule #22: 5'-vRNA

MacromoleculeName: 5'-vRNA / type: rna / ID: 22 / Number of copies: 1
Source (natural)Organism: Influenza B virus
Molecular weightTheoretical: 4.55782 KDa
SequenceString:
AGUAGUAACA AGAG

+
Macromolecule #24: ZINC ION

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

+
Macromolecule #25: 7-METHYL-GUANOSINE-5'-TRIPHOSPHATE-5'-(2'-O-METHYL)-GUANOSINE

MacromoleculeName: 7-METHYL-GUANOSINE-5'-TRIPHOSPHATE-5'-(2'-O-METHYL)-GUANOSINE
type: ligand / ID: 25 / Number of copies: 1 / Formula: G1G
Molecular weightTheoretical: 817.467 Da
Chemical component information

ChemComp-G1G:
7-METHYL-GUANOSINE-5'-TRIPHOSPHATE-5'-(2'-O-METHYL)-GUANOSINE

+
Macromolecule #26: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 26 / Number of copies: 2 / Formula: MG
Molecular weightTheoretical: 24.305 Da

+
Macromolecule #27: PHOSPHATE ION

MacromoleculeName: PHOSPHATE ION / type: ligand / ID: 27 / Number of copies: 2 / Formula: PO4
Molecular weightTheoretical: 94.971 Da
Chemical component information

ChemComp-PO4:
PHOSPHATE ION

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

BufferpH: 8
Details: 20 mM BICINE pH 8.0 150 mM NaCl 0.1 mM MgCl2 4% glycerol
VitrificationCryogen name: ETHANE / Chamber humidity: 95 % / Instrument: FEI VITROBOT MARK IV

-
Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average exposure time: 1.95 sec. / Average electron dose: 39.94 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: OTHER / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.2 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

+
Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: OTHER
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.1) / Number images used: 369858
Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: ANGULAR RECONSTITUTION

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