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- EMDB-38745: ASFV RNAP elongation complex -

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Basic information

Entry
Database: EMDB / ID: EMD-38745
TitleASFV RNAP elongation complex
Map data
Sample
  • Complex: ASFV RNAP elongation complex
    • Protein or peptide: x 8 types
    • RNA: x 1 types
    • DNA: x 2 types
  • Ligand: x 2 types
KeywordsASFV / RNAP / elongation complex / TRANSCRIPTION/RNA/DNA / TRANSCRIPTION-RNA-DNA complex
Function / homology
Function and homology information


viral transcription / transcription elongation by RNA polymerase I / tRNA transcription by RNA polymerase III / DNA-directed RNA polymerase activity / DNA-directed RNA polymerase complex / ribonucleoside binding / virion component / : / : / : ...viral transcription / transcription elongation by RNA polymerase I / tRNA transcription by RNA polymerase III / DNA-directed RNA polymerase activity / DNA-directed RNA polymerase complex / ribonucleoside binding / virion component / : / : / : / : / : / : / DNA-directed RNA polymerase / host cell cytoplasm / protein dimerization activity / DNA-templated transcription / DNA binding / zinc ion binding
Similarity search - Function
RNA polymerase Rpb1, domain 7 / RNA polymerase Rpb1, domain 7 superfamily / RNA polymerase Rpb1, domain 7 / RNA polymerase Rpb2, domain 4 / RNA polymerase Rpb2, domain 4 / DNA-directed RNA polymerase subunit RPABC5/Rpb10 / RNA polymerases, subunit N, zinc binding site / RNA polymerase subunit RPB10 / RNA polymerases N / 8 kDa subunit / RNA polymerases N / 8 Kd subunits signature. ...RNA polymerase Rpb1, domain 7 / RNA polymerase Rpb1, domain 7 superfamily / RNA polymerase Rpb1, domain 7 / RNA polymerase Rpb2, domain 4 / RNA polymerase Rpb2, domain 4 / DNA-directed RNA polymerase subunit RPABC5/Rpb10 / RNA polymerases, subunit N, zinc binding site / RNA polymerase subunit RPB10 / RNA polymerases N / 8 kDa subunit / RNA polymerases N / 8 Kd subunits signature. / DNA-directed RNA polymerase, RBP11-like dimerisation domain / RNA polymerase Rpb3/Rpb11 dimerisation domain / RNA polymerase, subunit H/Rpb5 C-terminal / DNA-directed RNA polymerase subunit Rpo5/Rpb5 / RPB5-like RNA polymerase subunit superfamily / RNA polymerase Rpb5, C-terminal domain / Archaeal Rpo6/eukaryotic RPB6 RNA polymerase subunit / DNA-directed RNA polymerase, 14-18kDa subunit, conserved site / RNA polymerases K / 14 to 18 Kd subunits signature. / DNA-directed RNA polymerase, subunit beta-prime / RNA polymerase Rpb6 / RNA polymerase, subunit omega/Rpo6/RPB6 / RNA polymerase Rpb6 / RNA polymerase Rpb2, domain 2 superfamily / RNA polymerase Rpb1, domain 3 superfamily / RPB6/omega subunit-like superfamily / RNA polymerase Rpb1, clamp domain superfamily / RNA polymerase Rpb1, domain 3 / RNA polymerase Rpb1, domain 3 / RNA polymerase Rpb1, domain 1 / RNA polymerase Rpb1, domain 1 / RNA polymerase, beta subunit, protrusion / RNA polymerase beta subunit / RNA polymerase, alpha subunit / RNA polymerase Rpb1, domain 5 / RNA polymerase Rpb1, domain 4 / RNA polymerase Rpb1, domain 2 / RNA polymerase Rpb1, domain 5 / RNA polymerase Rpb1, domain 4 / DNA-directed RNA polymerase, insert domain superfamily / RNA polymerase, N-terminal / RNA polymerase Rpb1, funnel domain superfamily / RNA polymerase I subunit A N-terminus / RNA polymerase Rpb2, domain 2 / RNA polymerase Rpb2, domain 2 / RNA polymerase, RBP11-like subunit / RNA polymerase, beta subunit, conserved site / RNA polymerase Rpb2, domain 7 / RNA polymerase Rpb2, domain 3 / RNA polymerase Rpb2, OB-fold / RNA polymerase Rpb2, domain 7 / RNA polymerase Rpb2, domain 3 / RNA polymerases beta chain signature. / DNA-directed RNA polymerase, subunit 2, hybrid-binding domain / DNA-directed RNA polymerase, subunit 2 / DNA-directed RNA polymerase, subunit 2, hybrid-binding domain superfamily / RNA polymerase Rpb2, domain 6
Similarity search - Domain/homology
C122R / DNA-directed RNA polymerase RPB5 homolog / RNA polymerase subunit 6 / DNA-directed RNA polymerase RPB10 homolog / DNA-directed RNA polymerase subunit beta / DNA-directed RNA polymerase RPB3-11 homolog / D339L / DNA-directed RNA polymerase subunit
Similarity search - Component
Biological speciesAfrican swine fever virus
Methodsingle particle reconstruction / cryo EM / Resolution: 2.6 Å
AuthorsZhu GL / Zhu Y / Zhu ZX / Sun F / Zheng HX
Funding support China, 2 items
OrganizationGrant numberCountry
Ministry of Science and Technology (MoST, China)2021YFD1800105 China
Ministry of Science and Technology (MoST, China)2021YFD1801300 China
CitationJournal: Nat Commun / Year: 2025
Title: Structural basis of RNA polymerase complexes in African swine fever virus.
Authors: Guoliang Zhu / Fei Xi / Wuxia Zeng / Yifei Zhao / Weijun Cao / Chen Liu / Fan Yang / Yi Ru / Shuqi Xiao / Shilei Zhang / Huanan Liu / Hong Tian / Fayu Yang / Biao Lu / Shukai Sun / Haiyang ...Authors: Guoliang Zhu / Fei Xi / Wuxia Zeng / Yifei Zhao / Weijun Cao / Chen Liu / Fan Yang / Yi Ru / Shuqi Xiao / Shilei Zhang / Huanan Liu / Hong Tian / Fayu Yang / Biao Lu / Shukai Sun / Haiyang Song / Bozhang Sun / Xiaoyi Zhao / Lijie Tang / Kangli Li / Jijun He / Jianhong Guo / Yun Zhu / Zixiang Zhu / Fei Sun / Haixue Zheng /
Abstract: African swine fever virus is highly contagious and causes a fatal infectious disease in pigs, resulting in a significant global impact on pork supply. The African swine fever virus RNA polymerase ...African swine fever virus is highly contagious and causes a fatal infectious disease in pigs, resulting in a significant global impact on pork supply. The African swine fever virus RNA polymerase serves as a crucial multifunctional protein complex responsible for genome transcription and regulation. Therefore, it is essential to investigate its structural and functional characteristics for the prevention and control of African swine fever. Here, we determine the structures of endogenous African swine fever virus RNA polymerase in both nucleic acid-free and elongation states. The African swine fever virus RNA polymerase shares similarities with the core of typical RNA polymerases, but possesses a distinct subunit M1249L. Notably, the dynamic binding mode of M1249L with RNA polymerase, along with the C-terminal tail insertion of M1249L in the active center of DNA-RNA scaffold binding, suggests the potential of M1249L to regulate RNA polymerase activity within cells. These results are important for understanding the transcription cycle of the African swine fever virus and for developing antiviral strategies.
History
DepositionJan 17, 2024-
Header (metadata) releaseJan 22, 2025-
Map releaseJan 22, 2025-
UpdateJan 22, 2025-
Current statusJan 22, 2025Processing site: PDBc / Status: Released

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Structure visualization

Supplemental images

emd_38745.png

Downloads & links

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Map

FileDownload / File: emd_38745.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
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AxesZ (Sec.)Y (Row.)X (Col.)
0.82 Å/pix.
x 400 pix.
= 328. Å		0.82 Å/pix.
x 400 pix.
= 328. Å		0.82 Å/pix.
x 400 pix.
= 328. Å

Surface

Projections

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Images are generated by Spider.

Voxel sizeX=Y=Z: 0.82 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.25
Minimum - Maximum-0.76730937 - 1.3348635
Average (Standard dev.)-0.0000123966265 (±0.045071583)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions400400400
Spacing400400400
CellA=B=C: 328.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_38745_msk_1.map
Projections & Slices
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Half map: #1

Fileemd_38745_half_map_1.map
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Half map: #2

Fileemd_38745_half_map_2.map
Projections & Slices
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Sample components

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Entire : ASFV RNAP elongation complex

EntireName: ASFV RNAP elongation complex
Components
  • Complex: ASFV RNAP elongation complex
    • Protein or peptide: DNA-directed RNA polymerase subunit
    • Protein or peptide: DNA-directed RNA polymerase subunit beta
    • Protein or peptide: DNA-directed RNA polymerase RPB3-11 homolog
    • Protein or peptide: DNA-directed RNA polymerase RPB5 homolog
    • Protein or peptide: D339L
    • Protein or peptide: C122R
    • Protein or peptide: DNA-directed RNA polymerase RPB10 homolog
    • RNA: RNA (5'-R(P*CP*UP*AP*CP*AP*CP*AP*AP*A)-3')
    • DNA: DNA (5'-D(P*TP*TP*CP*GP*CP*CP*GP*TP*TP*GP*CP*GP*TP*AP*TP*TP*TP*GP*TP*GP*TP*AP*G)-3')
    • Protein or peptide: RNA polymerase subunit 6
    • DNA: DNA (5'-D(P*CP*GP*CP*AP*AP*CP*GP*GP*CP*GP*A)-3')
  • Ligand: ZINC ION
  • Ligand: MAGNESIUM ION

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Supramolecule #1: ASFV RNAP elongation complex

SupramoleculeName: ASFV RNAP elongation complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#11
Source (natural)Organism: African swine fever virus

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Macromolecule #1: DNA-directed RNA polymerase subunit

MacromoleculeName: DNA-directed RNA polymerase subunit / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA-directed RNA polymerase
Source (natural)Organism: African swine fever virus
Molecular weightTheoretical: 162.959797 KDa
SequenceString: MEAGYAEIAA VQFNIAGDND HKRQGVMEVT ISNLFEGTLP AEGGIYDARM GTTDHHYKCI TCSHQRKQCM GHPGILQMHA PVLQPLFIA EIRRWLRVIC LNCGAPIVDL KRYEHLIRPK RLIEAASSQT EGKQCYVCKA VHPKIVKDSE DYFTFWADQQ G KIDKLYPQ ...String:
MEAGYAEIAA VQFNIAGDND HKRQGVMEVT ISNLFEGTLP AEGGIYDARM GTTDHHYKCI TCSHQRKQCM GHPGILQMHA PVLQPLFIA EIRRWLRVIC LNCGAPIVDL KRYEHLIRPK RLIEAASSQT EGKQCYVCKA VHPKIVKDSE DYFTFWADQQ G KIDKLYPQ IIREIFSRVT YDTVVKLGRS KNSHPEKLVL KAIQIPPISI RPGIRLGIGS GPQSFHDINN VIQYLVRKNL LI PKDLQIV RGQKIPLNID RNLQTIQQLY YNFLLDSVST TATQGGTGKR GIVMGARPAP SIMRRLPRKE GRIRKSLLGS QVW SISRST ICGNSDLHLD EVGYPISFAR TLQVAETVQH YNINRLMPYF LNGKRQYPGC SRVYKQITQS VHDIEGLKQD FRLE VGDIL YRDVVTGDVA FFNRQPSLER SSIGVHRIVV LENPKISTFQ MNVSACAWYN ADFDGDQMNL WVPWSVMSRV EAELL CSVR NWFISTKSSG PVNGQVQDST VGSFLLTRTN TPMGKNVMNK LHAMGLFQTT QTDPPCFANY SPTDLLDGKS VVSMLL RQT PINYQRAPTW YSEVYAPYMH YNKQDISTQI RNGELIEGVL DKKAVGAGSS GGIYHLISRR YGPQQALKMI FATQQLA LN YVRNAGFTVS TADMLLTPEA HQEVQEIINE LLLESEEINN RLLHGDIMPP IGLTTHDFYE KLQLNALKFP DRILKPIM N SINPETNGLF QMVATGAKGS NPNMIHIMAG IGQIEINTQR IQPQFSFGRT LVYYPRFALE AQAYGFICNS YIAGLTSPE FIFGEMNGRF DLINKALSTS STGYANRKAI FGLQSCIVDY YRRVSIDTRL VQQLYGEDGL DARQLETVRF ETIMLSDQEL EDKFKYTGI QSPLFEEEFS RLKKDRDKYR QIFLNVENFN FSQLLTDVRQ VPVNVASIVK NILLSSTSGV LPFDEKSILQ K YAMVKTFC KNLPYVFINN IQERLQTPIP VYLKRAASLM RMLIRIELAT VKTLNITCEQ MSAILDLIRL QYTQSLINYG EA VGILAAQ SVSEPLTQYM LDSHHRSVAG GTNKSGIVRP QEIFSAKPVE AEQSSEMLLR LKNPEVETNK TYAQEIANSI ELI TFERLI LQWHLLYETY SSTKKNVMYP DFASDVEWMT DFLENHPLLQ PPEDIANWCI RLELNKTTMI LKSISLESII NSLR AKHPN TYIMHSVENT ASGIPIIIRI YLRESAFRRS TNTRMATDEK IAVNVVDKLL NSTIRGIPGI KNANVVKLMR HRVDA QGKL VRLDNIYAIK TNGTNIFGAM LDDNIDPYTI VSSSIGDTME LYGIEAARQK IISEIRTVMG DKGPNHRHLL MYADLM TRT GQVTSLEKAG LNAREPSNVL LRMALSSPVQ VLTDAAVDSA VNPIYGIAAP TLMGSVPRIG TMYSDIIMDE KYITENY K

UniProtKB: DNA-directed RNA polymerase subunit

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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: African swine fever virus
Molecular weightTheoretical: 138.989188 KDa
SequenceString: YGPIETVDNE ELTEADMLSF ISAAVNSTGL IGYNIKSFDD LMDNGIPQIV KQMFNVDITY KDQRDHTEID KLRESVQIQF NFTDVNIER PQHRNYSQGN KINLLPNKAR LCGLSYSGPV NLAAEVILTA HYSNGRQEVK RASIPPFQVS TFPIMRGSNR C HTHHLSKT ...String:
YGPIETVDNE ELTEADMLSF ISAAVNSTGL IGYNIKSFDD LMDNGIPQIV KQMFNVDITY KDQRDHTEID KLRESVQIQF NFTDVNIER PQHRNYSQGN KINLLPNKAR LCGLSYSGPV NLAAEVILTA HYSNGRQEVK RASIPPFQVS TFPIMRGSNR C HTHHLSKT AKKEIGEDPN EPGGYFIARG GEWVVDLLEN IRFNTLHIHY HTMQQGNNEI IRGEFISQPG GAFENSSQII IR YMTTGAI TIEINSTKFS KLRIPWYLIF RMFGMTGDDS IIEQVVFDLE SNSLVNTFMI EILEKSIHVL DPIFQPVQHE LNR EKIIQF LSEKVSKFVS NPSAYKSDEN AVQYLNERQL TILDKILLPH MGQTADTRVR KLRFLGLLIH KILLVIMNVF PPTD RDSYR TKRVHGSGVS LAKAFKAIFN TSVIAPIING FKELLKQTAF EELTQRNIIE AFSAALSKNT ASDLNRSMEQ SIISG NKTI MVRQRPIVNR VSTQSLERKN LLNTISALRT VNTHNTTNAS KQTERADMMR RVHASYPGYI CVAQSADTGE KVGMSK QLA ITANVCTAGE VLSLKQRLLS DPAIQQLADV SNKDIVRKGL ARVFINGEWI GCCTNAFELA QRYRMLRREG KVVHPHT TI YWDSMVDEVE FWLDVGRLTR PLLIVDNNIE KYNQACYKAA EARKKGDKDW EKHKIPFIQN TRFTPQMAKD ILAGTLTL E DLVAQGICEF ITPEEAENCL VAFSIIELRK HKHDVTRRFT HVDVPQAILG LAALVSPYAN CTQPARVTYE TNQGRQTGG WYCFSWPYRV DMNRFFQFYN EMPLVKTIAH NYVIPNGLNT IVAYMIYGGY NQEDSVIVSQ SFIDRGGFAG TFYREEKVEL ESDIESFGK PDPLITKNLK PGANYEKLVD GFVPVGTVVK KGDIIIGKVA KIRGEKDELN KYIDRSVMYG FDEPAVVDAV M RPHGPNDE IFGLMRLRYE RNLNIGDKMS SRSGNKGIAA LALPTSDMPF TEDGLQPDLI VNPHSHPSRM TNGQMIETTV GL ANALQGV VTDGTAFLPI NVQLLSERLA QEGLRFNGCQ KMFNGQTGEY FDAAIFIGPT YHQRLQKFVL DDRYAVASYG PTD ALTGQP LDGKRSHGGL RLGEMEHWVL TAQGAMQTII EKSHDDSDGC ISYICRNCGE PAIYNASHPI YKCMNCDVQA DIGM VDSRR SSIVFQHEMR AANVNITSVL SPRVFQPA

UniProtKB: DNA-directed RNA polymerase subunit beta

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Macromolecule #3: DNA-directed RNA polymerase RPB3-11 homolog

MacromoleculeName: DNA-directed RNA polymerase RPB3-11 homolog / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: African swine fever virus
Molecular weightTheoretical: 41.286941 KDa
SequenceString: EKIFQNVEIK PFLIDFSNLF IKNAAKKLFQ LEEQLPLVPV NVVMDFKGIS RAAVHGLSRV LQDEIPNYML DIKPGGYKIE DSTDLFMTE QFIRNRINFI PIYAKNETLV FALRSLNNSC EVKTIYSRDL IQVAGPKLKY PIFNPTFEIG FLQPGKSLII E DIYIKKGI ...String:
EKIFQNVEIK PFLIDFSNLF IKNAAKKLFQ LEEQLPLVPV NVVMDFKGIS RAAVHGLSRV LQDEIPNYML DIKPGGYKIE DSTDLFMTE QFIRNRINFI PIYAKNETLV FALRSLNNSC EVKTIYSRDL IQVAGPKLKY PIFNPTFEIG FLQPGKSLII E DIYIKKGI GRKHAAFNLA VKTHFSHLDI EQYPTDKKEY MALSGYKQSS MTSDPRHHRL GLCFPAVPLP HINQAVRTYL KN ACRIIIG RIQSIQKIYE NFEEPQPELV LFSMDEEKTK AIITIKDETH TIGNLLKTYI YEMIPDISFV GYQCVPHKQE MVL TIIHKA SQEDLITLLE KSIQNIIQTF QILEKNVDEL IA

UniProtKB: DNA-directed RNA polymerase RPB3-11 homolog

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Macromolecule #4: DNA-directed RNA polymerase RPB5 homolog

MacromoleculeName: DNA-directed RNA polymerase RPB5 homolog / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: African swine fever virus
Molecular weightTheoretical: 23.693711 KDa
SequenceString: MAMQKLFTYI YEFIEYRKMV LLEEKVPYDK FVQMVLNTGF FRINAETLNH GIVSVFIFGA NGKYVHHGGD MRTLLTNTLN EKKHYEELI LIVDKPVLSK KNILDIIVEQ RAANPTIVIN IYPYHLFCIN IPKVSAIPKH KLITQEEAQE FLGREYLQPQ D LMQISASD ...String:
MAMQKLFTYI YEFIEYRKMV LLEEKVPYDK FVQMVLNTGF FRINAETLNH GIVSVFIFGA NGKYVHHGGD MRTLLTNTLN EKKHYEELI LIVDKPVLSK KNILDIIVEQ RAANPTIVIN IYPYHLFCIN IPKVSAIPKH KLITQEEAQE FLGREYLQPQ D LMQISASD PPVVWLGGRP GDFVQIERPS ETAMHAVVIR FITKSKI

UniProtKB: DNA-directed RNA polymerase RPB5 homolog

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Macromolecule #5: D339L

MacromoleculeName: D339L / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: African swine fever virus
Molecular weightTheoretical: 9.200585 KDa
SequenceString:
IDQKIFETTL NIDDPTNFCT NVEAHLLKEL ENIYVGKCFK NSFILNITGV IQRSPCFIMR TNNSGRGYMH VRFSAVVSYL

UniProtKB: D339L

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Macromolecule #6: C122R

MacromoleculeName: C122R / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: African swine fever virus
Molecular weightTheoretical: 11.617615 KDa
SequenceString:
MKICKACSSC MVRTYVDGNI IFRCSCGESV QGDSQNLLVS SKVYHTGEME DKYKIFIKNA PFDPTNCQIK KDCPNCHLDY LTQICIGSQ KIIILVCRCG YMSN

UniProtKB: C122R

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Macromolecule #7: DNA-directed RNA polymerase RPB10 homolog

MacromoleculeName: DNA-directed RNA polymerase RPB10 homolog / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: African swine fever virus
Molecular weightTheoretical: 9.098826 KDa
SequenceString:
MLIPVVCFTC GFPIGTYAAI FDKARTEYIK TKMDGTLPQN IPLDASLQIE LKDLITALGI PMRVCCRTHL ITTLDYRKYY

UniProtKB: DNA-directed RNA polymerase RPB10 homolog

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Macromolecule #10: RNA polymerase subunit 6

MacromoleculeName: RNA polymerase subunit 6 / type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: African swine fever virus
Molecular weightTheoretical: 12.207306 KDa
SequenceString:
IVESPSICEG FVQASSQTLV IIPDNERITS NVLTTFEATR LVAVRAQQLA INGSTMLKKK YSSPIDIAKQ ELFNRKIPLL VMRCIKVTP EGQKIVEIWN PREMGIPLLD

UniProtKB: RNA polymerase subunit 6

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Macromolecule #8: RNA (5'-R(P*CP*UP*AP*CP*AP*CP*AP*AP*A)-3')

MacromoleculeName: RNA (5'-R(P*CP*UP*AP*CP*AP*CP*AP*AP*A)-3') / type: rna / ID: 8 / Number of copies: 1
Source (natural)Organism: African swine fever virus
Molecular weightTheoretical: 2.822783 KDa
SequenceString:
CUACACAAA

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Macromolecule #9: DNA (5'-D(P*TP*TP*CP*GP*CP*CP*GP*TP*TP*GP*CP*GP*TP*AP*TP*TP*TP*GP...

MacromoleculeName: DNA (5'-D(P*TP*TP*CP*GP*CP*CP*GP*TP*TP*GP*CP*GP*TP*AP*TP*TP*TP*GP*TP*GP*TP*AP*G)-3')
type: dna / ID: 9 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: African swine fever virus
Molecular weightTheoretical: 7.084553 KDa
SequenceString:
(DT)(DT)(DC)(DG)(DC)(DC)(DG)(DT)(DT)(DG) (DC)(DG)(DT)(DA)(DT)(DT)(DT)(DG)(DT)(DG) (DT)(DA)(DG)

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Macromolecule #11: DNA (5'-D(P*CP*GP*CP*AP*AP*CP*GP*GP*CP*GP*A)-3')

MacromoleculeName: DNA (5'-D(P*CP*GP*CP*AP*AP*CP*GP*GP*CP*GP*A)-3') / type: dna / ID: 11 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: African swine fever virus
Molecular weightTheoretical: 3.368213 KDa
SequenceString:
(DC)(DG)(DC)(DA)(DA)(DC)(DG)(DG)(DC)(DG) (DA)

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Macromolecule #12: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 12 / Number of copies: 6 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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Macromolecule #13: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 13 / Number of copies: 1 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 60.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: INSILICO MODEL / In silico model: Ab initio model / Details: Ab initio model was generated in CryoSPARC.
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.6 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 73192
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Details: Non-uniform refinement in CryoSPARC was used.
Final angle assignmentType: MAXIMUM LIKELIHOOD / Details: Non-uniform refinement in CryoSPARC was used.
FSC plot (resolution estimation)

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