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- EMDB-4180: RNA Polymerase III open complex -

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Basic information

Entry
Database: EMDB / ID: EMD-4180
TitleRNA Polymerase III open complex
Map dataOC map sharpened with relion_postprocess
Sample
  • Complex: RNA Polymerase III open complex
    • Complex: RNA Polymerase III
      • Protein or peptide: x 17 types
    • Complex: Transcription factor IIIB
      • Protein or peptide: x 3 types
    • Complex: Nucleic acidsNucleic acid
      • DNA: x 2 types
  • Ligand: x 1 types
Function / homology
Function and homology information


RNA polymerase III core binding / TFIIA-class transcription factor complex binding / transcription factor TFIIIB complex / RNA polymerase III preinitiation complex assembly / RNA polymerase III transcription regulatory region sequence-specific DNA binding / DNA-templated transcription open complex formation / TFIIIC-class transcription factor complex binding / RNA polymerase III type 3 promoter sequence-specific DNA binding / regulation of transcription by RNA polymerase III / RNA polymerase I general transcription initiation factor binding ...RNA polymerase III core binding / TFIIA-class transcription factor complex binding / transcription factor TFIIIB complex / RNA polymerase III preinitiation complex assembly / RNA polymerase III transcription regulatory region sequence-specific DNA binding / DNA-templated transcription open complex formation / TFIIIC-class transcription factor complex binding / RNA polymerase III type 3 promoter sequence-specific DNA binding / regulation of transcription by RNA polymerase III / RNA polymerase I general transcription initiation factor binding / RNA polymerase III general transcription initiation factor activity / RNA polymerase III activity / transcription factor TFIIA complex / RNA polymerase I preinitiation complex assembly / transcription preinitiation complex / DNA binding, bending / RNA Polymerase I Transcription Initiation / Processing of Capped Intron-Containing Pre-mRNA / : / RNA Polymerase III Transcription Initiation From Type 2 Promoter / RNA Pol II CTD phosphorylation and interaction with CE / Formation of the Early Elongation Complex / mRNA Capping / Formation of TC-NER Pre-Incision Complex / RNA polymerase II transcribes snRNA genes / RNA Polymerase I Promoter Escape / TP53 Regulates Transcription of DNA Repair Genes / Estrogen-dependent gene expression / RNA Polymerase II Promoter Escape / RNA Polymerase II Transcription Pre-Initiation And Promoter Opening / RNA Polymerase II Transcription Initiation / RNA Polymerase II Transcription Initiation And Promoter Clearance / RNA polymerase II general transcription initiation factor activity / transcription factor TFIID complex / RNA-templated transcription / termination of RNA polymerase III transcription / RNA Polymerase II Pre-transcription Events / Dual incision in TC-NER / RNA polymerase I activity / termination of RNA polymerase I transcription / transcription initiation at RNA polymerase III promoter / tRNA transcription by RNA polymerase III / nucleolar large rRNA transcription by RNA polymerase I / Gap-filling DNA repair synthesis and ligation in TC-NER / transcription initiation at RNA polymerase I promoter / transcription elongation by RNA polymerase I / RNA polymerase II core promoter sequence-specific DNA binding / RNA polymerase I complex / transcription by RNA polymerase I / RNA polymerase III complex / transcription by RNA polymerase III / RNA polymerase II, core complex / RNA polymerase II preinitiation complex assembly / TBP-class protein binding / nucleotidyltransferase activity / transcription elongation by RNA polymerase II / DNA-templated transcription initiation / transcription initiation at RNA polymerase II promoter / ribonucleoside binding / DNA-directed 5'-3' RNA polymerase activity / DNA-directed RNA polymerase / peroxisome / disordered domain specific binding / single-stranded DNA binding / ribosome biogenesis / DNA-binding transcription factor binding / transcription regulator complex / RNA polymerase II-specific DNA-binding transcription factor binding / transcription by RNA polymerase II / nucleic acid binding / protein dimerization activity / nucleotide binding / negative regulation of DNA-templated transcription / chromatin binding / nucleolus / regulation of DNA-templated transcription / positive regulation of transcription by RNA polymerase II / protein-containing complex / mitochondrion / DNA binding / zinc ion binding / nucleoplasm / metal ion binding / nucleus / cytosol / cytoplasm
Similarity search - Function
Transcription factor TFIIIB component B'', fungi / Brf1, TBP-binding domain / Brf1-like TBP-binding domain / Transcription factor TFIIIB component B'', Myb domain / Myb DNA-binding like / DNA-directed RNA polymerase III subunit RPC4 / RNA polymerase III RPC4 / DNA-directed RNA polymerase III, subunit Rpc31 / DNA-directed RNA polymerase III subunit Rpc31 / Pol III subunit C11, C-terminal zinc ribbon ...Transcription factor TFIIIB component B'', fungi / Brf1, TBP-binding domain / Brf1-like TBP-binding domain / Transcription factor TFIIIB component B'', Myb domain / Myb DNA-binding like / DNA-directed RNA polymerase III subunit RPC4 / RNA polymerase III RPC4 / DNA-directed RNA polymerase III, subunit Rpc31 / DNA-directed RNA polymerase III subunit Rpc31 / Pol III subunit C11, C-terminal zinc ribbon / DNA-directed RNA polymerase III subunit Rpc5 / DNA-directed RNA polymerase III subunit RPC1, N-terminal / DNA-directed RNA polymerase III subunit RPC1, C-terminal / RPC5 protein / RNA polymerase III, subunit Rpc25 / DNA-directed RNA polymerase III subunit RPC9 / RNA polymerase III subunit Rpc25 / RNA polymerase Rpc34 / RNA polymerase III Rpc82, C -terminal / RNA polymerase Rpc34-like / DNA-directed RNA polymerase III subunit RPC3 / RNA polymerase Rpc34 subunit / RNA polymerase III subunit RPC82 / DNA-directed RNA polymerase III subunit RPC3, helical hairpin domain / RNA polymerase III subunit RPC82-related, helix-turn-helix / RNA polymerase III subunit RPC82 helix-turn-helix domain / DNA-directed RNA polymerase, subunit E/RPC8 / DNA-directed RNA polymerases I and III subunit AC19 / DNA-directed RNA polymerases I and III subunit AC40 / Transcription factor TFIIB, cyclin-like domain / Transcription factor TFIIB, conserved site / Transcription factor TFIIB repeat / Transcription factor TFIIB repeat signature. / Transcription factor TFIIB / Zinc finger TFIIB-type profile. / Zinc finger, TFIIB-type / TFIIB zinc-binding / TATA-box binding protein, eukaryotic / TATA-box binding protein / TATA-box binding protein, conserved site / Transcription factor TFIID (or TATA-binding protein, TBP) / Transcription factor TFIID repeat signature. / TBP domain superfamily / SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains / Rpb4/RPC9 superfamily / SANT/Myb domain / RNA polymerase subunit Rpb4/RPC9 / RNA polymerase Rpb4 / Cyclin-like / domain present in cyclins, TFIIB and Retinoblastoma / Cyclin-like superfamily / HRDC-like superfamily / 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 / RNA polymerase Rpb2, domain 4 / RNA polymerase Rpb2, domain 4 / RNA polymerase Rpb2, domain 5 / RNA polymerase Rpb2, domain 5 / 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, 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 Rpo11 / DNA directed RNA polymerase, 7 kDa subunit / RNA polymerase archaeal subunit P/eukaryotic subunit RPABC4 / RNA polymerase, subunit H/Rpb5, conserved site / RNA polymerases H / 23 Kd subunits signature. / RNA polymerase subunit CX / DNA-directed RNA polymerase Rpb11, 13-16kDa subunit, conserved site / DNA-directed RNA polymerase subunit Rpo5/Rpb5 / RNA polymerases L / 13 to 16 Kd subunits signature. / DNA-directed RNA polymerase, 30-40kDa subunit, conserved site / DNA-directed RNA polymerase subunit Rpo3/Rpb3/RPAC1 / RNA polymerases D / 30 to 40 Kd subunits signature. / DNA-directed RNA polymerase, RBP11-like dimerisation domain / RNA polymerase Rpb3/Rpb11 dimerisation domain / RNA polymerase, subunit H/Rpb5 C-terminal / RNA polymerase subunit RPABC4/transcription elongation factor Spt4 / RPB5-like RNA polymerase subunit superfamily / RNA polymerase Rpb5, C-terminal domain / Zinc finger, TFIIS-type / Transcription factor S-II (TFIIS) / Zinc finger TFIIS-type profile.
Similarity search - Domain/homology
DNA-directed RNA polymerase III subunit RPC1 / DNA-directed RNA polymerases I and III subunit RPAC1 / TATA-box-binding protein / DNA-directed RNA polymerase III subunit RPC7 / DNA-directed RNA polymerases I, II, and III subunit RPABC1 / DNA-directed RNA polymerases I, II, and III subunit RPABC2 / DNA-directed RNA polymerases I, II, and III subunit RPABC3 / DNA-directed RNA polymerases I, II, and III subunit RPABC5 / DNA-directed RNA polymerase III subunit RPC2 / DNA-directed RNA polymerase III subunit RPC4 ...DNA-directed RNA polymerase III subunit RPC1 / DNA-directed RNA polymerases I and III subunit RPAC1 / TATA-box-binding protein / DNA-directed RNA polymerase III subunit RPC7 / DNA-directed RNA polymerases I, II, and III subunit RPABC1 / DNA-directed RNA polymerases I, II, and III subunit RPABC2 / DNA-directed RNA polymerases I, II, and III subunit RPABC3 / DNA-directed RNA polymerases I, II, and III subunit RPABC5 / DNA-directed RNA polymerase III subunit RPC2 / DNA-directed RNA polymerase III subunit RPC4 / DNA-directed RNA polymerases I and III subunit RPAC2 / Transcription factor IIIB 70 kDa subunit / DNA-directed RNA polymerase III subunit RPC3 / DNA-directed RNA polymerase III subunit RPC6 / DNA-directed RNA polymerase III subunit RPC8 / DNA-directed RNA polymerase III subunit RPC5 / DNA-directed RNA polymerases I, II, and III subunit RPABC4 / Transcription factor TFIIIB component B'' / DNA-directed RNA polymerase III subunit RPC9 / DNA-directed RNA polymerase III subunit RPC10
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast) / Baker's yeast (brewer's yeast) / Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.7 Å
AuthorsVorlaender MK / Khatter H / Wetzel R / Hagen WJH / Mueller CW
Funding support1 items
OrganizationGrant numberCountry
European Research CouncilERC-2013-AdG340964-POL1PIC
CitationJournal: Nature / Year: 2018
Title: Molecular mechanism of promoter opening by RNA polymerase III.
Authors: Matthias K Vorländer / Heena Khatter / Rene Wetzel / Wim J H Hagen / Christoph W Müller /
Abstract: RNA polymerase III (Pol III) and transcription factor IIIB (TFIIIB) assemble together on different promoter types to initiate the transcription of small, structured RNAs. Here we present structures ...RNA polymerase III (Pol III) and transcription factor IIIB (TFIIIB) assemble together on different promoter types to initiate the transcription of small, structured RNAs. Here we present structures of Pol III preinitiation complexes, comprising the 17-subunit Pol III and the heterotrimeric transcription factor TFIIIB, bound to a natural promoter in different functional states. Electron cryo-microscopy reconstructions, varying from 3.7 Å to 5.5 Å resolution, include two early intermediates in which the DNA duplex is closed, an open DNA complex, and an initially transcribing complex with RNA in the active site. Our structures reveal an extremely tight, multivalent interaction between TFIIIB and promoter DNA, and explain how TFIIIB recruits Pol III. Together, TFIIIB and Pol III subunit C37 activate the intrinsic transcription factor-like activity of the Pol III-specific heterotrimer to initiate the melting of double-stranded DNA, in a mechanism similar to that of the Pol II system.
History
DepositionNov 29, 2017-
Header (metadata) releaseJan 17, 2018-
Map releaseJan 17, 2018-
UpdateDec 11, 2019-
Current statusDec 11, 2019Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.05
  • Imaged by UCSF Chimera
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  • Surface view colored by radius
  • Surface level: 0.05
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6f40
  • Surface level: 0.05
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_4180.png

Downloads & links

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Map

FileDownload / File: emd_4180.map.gz / Format: CCP4 / Size: 52.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationOC map sharpened with relion_postprocess
Voxel sizeX=Y=Z: 1.35 Å
Density
Contour LevelBy AUTHOR: 0.05 / Movie #1: 0.05
Minimum - Maximum-0.17192116 - 0.31068677
Average (Standard dev.)0.0012636378 (±0.009942414)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderZXY
Origin000
Dimensions240240240
Spacing240240240
CellA=B=C: 324.0 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.351.351.35
M x/y/z240240240
origin x/y/z0.0000.0000.000
length x/y/z324.000324.000324.000
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ240240240
MAP C/R/S312
start NC/NR/NS000
NC/NR/NS240240240
D min/max/mean-0.1720.3110.001

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Supplemental data

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Mask #1

Fileemd_4180_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: OC map sharpened with LocScale

Fileemd_4180_additional.map
AnnotationOC map sharpened with LocScale
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : RNA Polymerase III open complex

EntireName: RNA Polymerase III open complex
Components
  • Complex: RNA Polymerase III open complex
    • Complex: RNA Polymerase III
      • Protein or peptide: DNA-directed RNA polymerase III subunit RPC1Polymerase
      • Protein or peptide: DNA-directed RNA polymerase III subunit RPC2Polymerase
      • Protein or peptide: DNA-directed RNA polymerases I and III subunit RPAC1
      • Protein or peptide: DNA-directed RNA polymerase III subunit RPC9Polymerase
      • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC1RNA polymerase
      • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC2RNA polymerase
      • Protein or peptide: DNA-directed RNA polymerase III subunit RPC8Polymerase
      • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC3RNA polymerase
      • Protein or peptide: DNA-directed RNA polymerase III subunit RPC10Polymerase
      • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC5RNA polymerase
      • Protein or peptide: DNA-directed RNA polymerases I and III subunit RPAC2
      • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC4RNA polymerase
      • Protein or peptide: DNA-directed RNA polymerase III subunit RPC5Polymerase
      • Protein or peptide: DNA-directed RNA polymerase III subunit RPC4Polymerase
      • Protein or peptide: DNA-directed RNA polymerase III subunit RPC3Polymerase
      • Protein or peptide: DNA-directed RNA polymerase III subunit RPC6Polymerase
      • Protein or peptide: DNA-directed RNA polymerase III subunit RPC7Polymerase
    • Complex: Transcription factor IIIB
      • Protein or peptide: TATA-box-binding protein
      • Protein or peptide: Transcription factor IIIB 70 kDa subunit
      • Protein or peptide: Transcription factor TFIIIB component B''
    • Complex: Nucleic acidsNucleic acid
      • DNA: Non-Template DNA
      • DNA: Template DNA
  • Ligand: ZINC ION

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Supramolecule #1: RNA Polymerase III open complex

SupramoleculeName: RNA Polymerase III open complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#22
Molecular weightTheoretical: 893 KDa

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Supramolecule #2: RNA Polymerase III

SupramoleculeName: RNA Polymerase III / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#17
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)

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Supramolecule #3: Transcription factor IIIB

SupramoleculeName: Transcription factor IIIB / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #18-#20
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Recombinant expressionOrganism: Escherichia coli (E. coli)

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Supramolecule #4: Nucleic acids

SupramoleculeName: Nucleic acids / type: complex / ID: 4 / Parent: 1 / Macromolecule list: #21-#22
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)

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Macromolecule #1: DNA-directed RNA polymerase III subunit RPC1

MacromoleculeName: DNA-directed RNA polymerase III subunit RPC1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA-directed RNA polymerase
Source (natural)Organism: Baker's yeast (brewer's yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 162.517812 KDa
SequenceString: MKEVVVSETP KRIKGLEFSA LSAADIVAQS EVEVSTRDLF DLEKDRAPKA NGALDPKMGV SSSSLECATC HGNLASCHGH FGHLKLALP VFHIGYFKAT IQILQGICKN CSAILLSETD KRQFLHELRR PGVDNLRRMG ILKKILDQCK KQRRCLHCGA L NGVVKKAA ...String:
MKEVVVSETP KRIKGLEFSA LSAADIVAQS EVEVSTRDLF DLEKDRAPKA NGALDPKMGV SSSSLECATC HGNLASCHGH FGHLKLALP VFHIGYFKAT IQILQGICKN CSAILLSETD KRQFLHELRR PGVDNLRRMG ILKKILDQCK KQRRCLHCGA L NGVVKKAA AGAGSAALKI IHDTFRWVGK KSAPEKDIWV GEWKEVLAHN PELERYVKRC MDDLNPLKTL NLFKQIKSAD CE LLGIDAT VPSGRPETYI WRYLPAPPVC IRPSVMMQDS PASNEDDLTV KLTEIVWTSS LIKAGLDKGI SINNMMEHWD YLQ LTVAMY INSDSVNPAM LPGSSNGGGK VKPIRGFCQR LKGKQGRFRG NLSGKRVDFS GRTVISPDPN LSIDEVAVPD RVAK VLTYP EKVTRYNRHK LQELIVNGPN VHPGANYLLK RNEDARRNLR YGDRMKLAKN LQIGDVVERH LEDGDVVLFN RQPSL HRLS ILSHYAKIRP WRTFRLNECV CTPYNADFDG DEMNLHVPQT EEARAEAINL MGVKNNLLTP KSGEPIIAAT QDFITG SYL ISHKDSFYDR ATLTQLLSMM SDGIEHFDIP PPAIMKPYYL WTGKQVFSLL IKPNHNSPVV INLDAKNKVF VPPKSKS LP NEMSQNDGFV IIRGSQILSG VMDKSVLGDG KKHSVFYTIL RDYGPQEAAN AMNRMAKLCA RFLGNRGFSI GINDVTPA D DLKQKKEELV EIAYHKCDEL ITLFNKGELE TQPGCNEEQT LEAKIGGLLS KVREEVGDVC INELDNWNAP LIMATCGSK GSTLNVSQMV AVVGQQIISG NRVPDGFQDR SLPHFPKNSK TPQSKGFVRN SFFSGLSPPE FLFHAISGRE GLVDTAVKTA ETGYMSRRL MKSLEDLSCQ YDNTVRTSAN GIVQFTYGGD GLDPLEMEGN AQPVNFNRSW DHAYNITFNN QDKGLLPYAI M ETANEILG PLEERLVRYD NSGCLVKRED LNKAEYVDQY DAERDFYHSL REYINGKATA LANLRKSRGM LGLLEPPAKE LQ GIDPDET VPDNVKTSVS QLYRISEKSV RKFLEIALFK YRKARLEPGT AIGAIGAQSI GEPGTQMTLK TFHFAGVASM NVT LGVPRI KEIINASKVI STPIINAVLV NDNDERAARV VKGRVEKTLL SDVAFYVQDV YKDNLSFIQV RIDLGTIDKL QLEL TIEDI AVAITRASKL KIQASDVNII GKDRIAINVF PEGYKAKSIS TSAKEPSEND VFYRMQQLRR ALPDVVVKGL PDISR AVIN IRDDGKRELL VEGYGLRDVM CTDGVIGSRT TTNHVLEVFS VLGIEAARYS IIREINYTMS NHGMSVDPRH IQLLGD VMT YKGEVLGITR FGLSKMRDSV LQLASFEKTT DHLFDAAFYM KKDAVEGVSE CIILGQTMSI GTGSFKVVKG TNISEKD LV PKRCLFESLS NEAALKAN

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Macromolecule #2: DNA-directed RNA polymerase III subunit RPC2

MacromoleculeName: DNA-directed RNA polymerase III subunit RPC2 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA-directed RNA polymerase
Source (natural)Organism: Baker's yeast (brewer's yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 129.629383 KDa
SequenceString: MVAATKRRKT HIHKHVKDEA FDDLLKPVYK GKKLTDEINT AQDKWHLLPA FLKVKGLVKQ HLDSFNYFVD TDLKKIIKAN QLILSDVDP EFYLKYVDIR VGKKSSSSTK DYLTPPHECR LRDMTYSAPI YVDIEYTRGR NIIMHKDVEI GRMPIMLRSN K CILYDADE ...String:
MVAATKRRKT HIHKHVKDEA FDDLLKPVYK GKKLTDEINT AQDKWHLLPA FLKVKGLVKQ HLDSFNYFVD TDLKKIIKAN QLILSDVDP EFYLKYVDIR VGKKSSSSTK DYLTPPHECR LRDMTYSAPI YVDIEYTRGR NIIMHKDVEI GRMPIMLRSN K CILYDADE SKMAKLNECP LDPGGYFIVN GTEKVILVQE QLSKNRIIVE ADEKKGIVQA SVTSSTHERK SKTYVITKNG KI YLKHNSI AEEIPIAIVL KACGILSDLE IMQLVCGNDS SYQDIFAVNL EESSKLDIYT QQQALEYIGA KVKTMRRQKL TIL QEGIEA IATTVIAHLT VEALDFREKA LYIAMMTRRV VMAMYNPKMI DDRDYVGNKR LELAGQLISL LFEDLFKKFN NDFK LSIDK VLKKPNRAME YDALLSINVH SNNITSGLNR AISTGNWSLK RFKMERAGVT HVLSRLSYIS ALGMMTRISS QFEKS RKVS GPRALQPSQF GMLCTADTPE GEACGLVKNL ALMTHITTDD EEEPIKKLCY VLGVEDITLI DSASLHLNYG VYLNGT LIG SIRFPTKFVT QFRHLRRTGK VSEFISIYSN SHQMAVHIAT DGGRICRPLI IVSDGQSRVK DIHLRKLLDG ELDFDDF LK LGLVEYLDVN EENDSYIALY EKDIVPSMTH LEIEPFTILG AVAGLIPYPH HNQSPRNTYQ CAMGKQAIGA IAYNQFKR I DTLLYLMTYP QQPMVKTKTI ELIDYDKLPA GQNATVAVMS YSGYDIEDAL VLNKSSIDRG FGRCETRRKT TTVLKRYAN HTQDIIGGMR VDENGDPIWQ HQSLGPDGLG EVGMKVQSGQ IYINKSVPTN SADAPNPNNV NVQTQYREAP VIYRGPEPSH IDQVMMSVS DNDQALIKVL LRQNRRPELG DKFSSRHGQK GVCGIIVKQE DMPFNDQGIV PDIIMNPHGF PSRMTVGKMI E LISGKAGV LNGTLEYGTC FGGSKLEDMS KILVDQGFNY SGKDMLYSGI TGECLQAYIF FGPIYYQKLK HMVLDKMHAR AR GPRAVLT RQPTEGRSRD GGLRLGEMER DCVIAYGASQ LLLERLMISS DAFEVDVCDK CGLMGYSGWC TTCKSAENII KMT IPYAAK LLFQELLSMN IAPRLRLEDI FQQ

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Macromolecule #3: DNA-directed RNA polymerases I and III subunit RPAC1

MacromoleculeName: DNA-directed RNA polymerases I and III subunit RPAC1 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Baker's yeast (brewer's yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 37.732613 KDa
SequenceString: MSNIVGIEYN RVTNTTSTDF PGFSKDAENE WNVEKFKKDF EVNISSLDAR EANFDLINID TSIANAFRRI MISEVPSVAA EYVYFFNNT SVIQDEVLAH RIGLVPLKVD PDMLTWVDSN LPDDEKFTDE NTIVLSLNVK CTRNPDAPKG STDPKELYNN A HVYARDLK ...String:
MSNIVGIEYN RVTNTTSTDF PGFSKDAENE WNVEKFKKDF EVNISSLDAR EANFDLINID TSIANAFRRI MISEVPSVAA EYVYFFNNT SVIQDEVLAH RIGLVPLKVD PDMLTWVDSN LPDDEKFTDE NTIVLSLNVK CTRNPDAPKG STDPKELYNN A HVYARDLK FEPQGRQSTT FADCPVVPAD PDILLAKLRP GQEISLKAHC ILGIGGDHAK FSPVSTASYR LLPQINILQP IK GESARRF QKCFPPGVIG IDEGSDEAYV KDARKDTVSR EVLRYEEFAD KVKLGRVRNH FIFNVESAGA MTPEEIFFKS VRI LKNKAE YLKNCPITQ

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Macromolecule #4: DNA-directed RNA polymerase III subunit RPC9

MacromoleculeName: DNA-directed RNA polymerase III subunit RPC9 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Baker's yeast (brewer's yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 18.623123 KDa
SequenceString:
MKVLEERNAF LSDYEVLKFL TDLEKKHLWD QKSLAALKKS RSKGKQNRPY NHPELQGITR NVVNYLSINK NFINQEDEGE ERESSGAKD AEKSGISKMS DESFAELMTK LNSFKLFKAE KLQIVNQLPA NMVHLYSIVE ECDARFDEKT IEEMLEIISG Y A

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Macromolecule #5: DNA-directed RNA polymerases I, II, and III subunit RPABC1

MacromoleculeName: DNA-directed RNA polymerases I, II, and III subunit RPABC1
type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Baker's yeast (brewer's yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 25.117094 KDa
SequenceString: MDQENERNIS RLWRAFRTVK EMVKDRGYFI TQEEVELPLE DFKAKYCDSM GRPQRKMMSF QANPTEESIS KFPDMGSLWV EFCDEPSVG VKTMKTFVIH IQEKNFQTGI FVYQNNITPS AMKLVPSIPP ATIETFNEAA LVVNITHHEL VPKHIRLSSD E KRELLKRY ...String:
MDQENERNIS RLWRAFRTVK EMVKDRGYFI TQEEVELPLE DFKAKYCDSM GRPQRKMMSF QANPTEESIS KFPDMGSLWV EFCDEPSVG VKTMKTFVIH IQEKNFQTGI FVYQNNITPS AMKLVPSIPP ATIETFNEAA LVVNITHHEL VPKHIRLSSD E KRELLKRY RLKESQLPRI QRADPVALYL GLKRGEVVKI IRKSETSGRY ASYRICM

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Macromolecule #6: 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: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Baker's yeast (brewer's yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 17.931834 KDa
SequenceString:
MSDYEEAFND GNENFEDFDV EHFSDEETYE EKPQFKDGET TDANGKTIVT GGNGPEDFQQ HEQIRRKTLK EKAIPKDQRA TTPYMTKYE RARILGTRAL QISMNAPVFV DLEGETDPLR IAMKELAEKK IPLVIRRYLP DGSFEDWSVE ELIVDL

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Macromolecule #7: DNA-directed RNA polymerase III subunit RPC8

MacromoleculeName: DNA-directed RNA polymerase III subunit RPC8 / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Baker's yeast (brewer's yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 24.34977 KDa
SequenceString: MFILSKIADL VRIPPDQFHR DTISAITHQL NNKFANKIIP NVGLCITIYD LLTVEEGQLK PGDGSSYINV TFRAVVFKPF LGEIVTGWI SKCTAEGIKV SLLGIFDDIF IPQNMLFEGC YYTPEESAWI WPMDEETKLY FDVNEKIRFR IEREVFVDVK P KSPKEREL ...String:
MFILSKIADL VRIPPDQFHR DTISAITHQL NNKFANKIIP NVGLCITIYD LLTVEEGQLK PGDGSSYINV TFRAVVFKPF LGEIVTGWI SKCTAEGIKV SLLGIFDDIF IPQNMLFEGC YYTPEESAWI WPMDEETKLY FDVNEKIRFR IEREVFVDVK P KSPKEREL EERAQLENEI EGKNEETPQN EKPPAYALLG SCQTDGMGLV SWWE

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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: Baker's yeast (brewer's yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 16.525363 KDa
SequenceString:
MSNTLFDDIF QVSEVDPGRY NKVCRIEAAS TTQDQCKLTL DINVELFPVA AQDSLTVTIA SSLNLEDTPA NDSSATRSWR PPQAGDRSL ADDYDYVMYG TAYKFEEVSK DLIAVYYSFG GLLMRLEGNY RNLNNLKQEN AYLLIRR

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Macromolecule #9: DNA-directed RNA polymerase III subunit RPC10

MacromoleculeName: DNA-directed RNA polymerase III subunit RPC10 / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Baker's yeast (brewer's yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 12.525109 KDa
SequenceString:
MLSFCPSCNN MLLITSGDSG VYTLACRSCP YEFPIEGIEI YDRKKLPRKE VDDVLGGGWD NVDQTKTQCP NYDTCGGESA YFFQLQIRS ADEPMTTFYK CVNCGHRWKE N

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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: Baker's yeast (brewer's yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 8.290732 KDa
SequenceString:
MIVPVRCFSC GKVVGDKWES YLNLLQEDEL DEGTALSRLG LKRYCCRRMI LTHVDLIEKF LRYNPLEKRD

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Macromolecule #11: DNA-directed RNA polymerases I and III subunit RPAC2

MacromoleculeName: DNA-directed RNA polymerases I and III subunit RPAC2 / type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Baker's yeast (brewer's yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 16.16786 KDa
SequenceString:
MTEDIEQKKT ATEVTPQEPK HIQEEEEQDV DMTGDEEQEE EPDREKIKLL TQATSEDGTS ASFQIVEEDH TLGNALRYVI MKNPDVEFC GYSIPHPSEN LLNIRIQTYG ETTAVDALQK GLKDLMDLCD VVESKFTEKI KSM

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Macromolecule #12: DNA-directed RNA polymerases I, II, and III subunit RPABC4

MacromoleculeName: DNA-directed RNA polymerases I, II, and III subunit RPABC4
type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Baker's yeast (brewer's yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 7.729969 KDa
SequenceString:
MSREGFQIPT NLDAAAAGTS QARTATLKYI CAECSSKLSL SRTDAVRCKD CGHRILLKAR TKRLVQFEAR

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Macromolecule #13: DNA-directed RNA polymerase III subunit RPC5

MacromoleculeName: DNA-directed RNA polymerase III subunit RPC5 / type: protein_or_peptide / ID: 13 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Baker's yeast (brewer's yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 32.178115 KDa
SequenceString: MSIDNKLFVT EEDEEDRTQD RADVEDESND IDMIADENGT NSAIANEQEE KSEEVKAEDD TGEEEEDDPV IEEFPLKISG EEESLHVFQ YANRPRLVGR KPAEHPFISA ARYKPKSHLW EIDIPLDEQA FYNKDKAESE WNGVNVQTLK GVGVENNGQY A AFVKDMQV ...String:
MSIDNKLFVT EEDEEDRTQD RADVEDESND IDMIADENGT NSAIANEQEE KSEEVKAEDD TGEEEEDDPV IEEFPLKISG EEESLHVFQ YANRPRLVGR KPAEHPFISA ARYKPKSHLW EIDIPLDEQA FYNKDKAESE WNGVNVQTLK GVGVENNGQY A AFVKDMQV YLVPIERVAQ LKPFFKYIDD ANVTRKQEDA RRNPNPSSQR AQVVTMSVKS VNDPSQNRLT GSLLAHKVAD EE ANIELTW AEGTFEQFKD TIVKEAEDKT LVALEKQEDY IDNLV

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Macromolecule #14: DNA-directed RNA polymerase III subunit RPC4

MacromoleculeName: DNA-directed RNA polymerase III subunit RPC4 / type: protein_or_peptide / ID: 14 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Baker's yeast (brewer's yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 46.751469 KDa
SequenceString: MSSNKGNGRL PSLKDSSSNG GGSAKPSLKF KPKAVARKSK EEREAAASKV KLEEESKRGN DKKHFNNKNK RVTGAGGQQR RMAKYLNNT HVISSGPLAA GNFVSEKGDL RRGFIKSEGS GSSLVQKGLE TIDNGAESSE NEAEDDDNEG VASKSKKKFN M GKEFEARN ...String:
MSSNKGNGRL PSLKDSSSNG GGSAKPSLKF KPKAVARKSK EEREAAASKV KLEEESKRGN DKKHFNNKNK RVTGAGGQQR RMAKYLNNT HVISSGPLAA GNFVSEKGDL RRGFIKSEGS GSSLVQKGLE TIDNGAESSE NEAEDDDNEG VASKSKKKFN M GKEFEARN LIEDEDDGES EKSSDVDMDD EEWRSKRIEQ LFPVRPVRVR HEDVETVKRE IQEALSEKPT REPTPSVKTE PV GTGLQSY LEERERQVNE KLADLGLEKE FQSVDGKEAA AELELLNADH QHILRKLKKM NNKPERFMVF QLPTRLPAFE RPA VKEEKE DMETQASDPS KKKKNIKKKD TKDALSTREL AGKVGSIRVH KSGKLSVKIG NVVMDIGKGA ETTFLQDVIA LSIA DDASS AELLGRVDGK IVVTPQI

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Macromolecule #15: DNA-directed RNA polymerase III subunit RPC3

MacromoleculeName: DNA-directed RNA polymerase III subunit RPC3 / type: protein_or_peptide / ID: 15 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Baker's yeast (brewer's yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 74.11282 KDa
SequenceString: MDELLGEALS AENQTGESTV ESEKLVTPED VMTISSLEQR TLNPDLFLYK ELVKAHLGER AASVIGMLVA LGRLSVRELV EKIDGMDVD SVKTTLVSLT QLRCVKYLQE TAISGKKTTY YYYNEEGIHI LLYSGLIIDE IITQMRVNDE EEHKQLVAEI V QNVISLGS ...String:
MDELLGEALS AENQTGESTV ESEKLVTPED VMTISSLEQR TLNPDLFLYK ELVKAHLGER AASVIGMLVA LGRLSVRELV EKIDGMDVD SVKTTLVSLT QLRCVKYLQE TAISGKKTTY YYYNEEGIHI LLYSGLIIDE IITQMRVNDE EEHKQLVAEI V QNVISLGS LTVEDYLSSV TSDSMKYTIS SLFVQLCEMG YLIQISKLHY TPIEDLWQFL YEKHYKNIPR NSPLSDLKKR SQ AKMNAKT DFAKIINKPN ELSQILTVDP KTSLRIVKPT VSLTINLDRF MKGRRSKQLI NLAKTRVGSV TAQVYKIALR LTE QKSPKI RDPLTQTGLL QDLEEAKSFQ DEAELVEEKT PGLTFNAIDL ARHLPAELDL RGSLLSRKPS DNKKRSGSNA AASL PSKKL KTEDGFVIPA LPAAVSKSLQ ESGDTQEEDE EEEDLDADTE DPHSASLINS HLKILASSNF PFLNETKPGV YYVPY SKLM PVLKSSVYEY VIASTLGPSA MRLSRCIRDN KLVSEKIINS TALMKEKDIR STLASLIRYN SVEIQEVPRT ADRSAS RAV FLFRCKETHS YNFMRQNLEW NMANLLFKKE KLKQENSTLL KKANRDDVKG RENELLLPSE LNQLKMVNER ELNVFAR LS RLLSLWEVFQ MA

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Macromolecule #16: DNA-directed RNA polymerase III subunit RPC6

MacromoleculeName: DNA-directed RNA polymerase III subunit RPC6 / type: protein_or_peptide / ID: 16 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Baker's yeast (brewer's yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 36.17416 KDa
SequenceString: MSGMIENGLQ LSDNAKTLHS QMMSKGIGAL FTQQELQKQM GIGSLTDLMS IVQELLDKNL IKLVKQNDEL KFQGVLESEA QKKATMSAE EALVYSYIEA SGREGIWSKT IKARTNLHQH VVLKCLKSLE SQRYVKSVKS VKFPTRKIYM LYSLQPSVDI T GGPWFTDG ...String:
MSGMIENGLQ LSDNAKTLHS QMMSKGIGAL FTQQELQKQM GIGSLTDLMS IVQELLDKNL IKLVKQNDEL KFQGVLESEA QKKATMSAE EALVYSYIEA SGREGIWSKT IKARTNLHQH VVLKCLKSLE SQRYVKSVKS VKFPTRKIYM LYSLQPSVDI T GGPWFTDG ELDIEFINSL LTIVWRFISE NTFPNGFKNF ENGPKKNVFY APNVKNYSTT QEILEFITAA QVANVELTPS NI RSLCEVL VYDDKLEKVT HDCYRVTLES ILQMNQGEGE PEAGNKALED EEEFSIFNYF KMFPASKHDK EVVYFDEWTI

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Macromolecule #17: DNA-directed RNA polymerase III subunit RPC7

MacromoleculeName: DNA-directed RNA polymerase III subunit RPC7 / type: protein_or_peptide / ID: 17 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Baker's yeast (brewer's yeast) / Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 27.752971 KDa
SequenceString: MSSYRGGSRG GGSNYMSNLP FGLGYGDVGK NHITEFPSIP LPINGPITNK ERSLAVKYIN FGKTVKDGPF YTGSMSLIID QQENSKSGK RKPNIILDED DTNDGIERYS DKYLKKRKIG ISIDDHPYNL NLFPNELYNV MGINKKKLLA ISKFNNADDV F TGTGLQDE ...String:
MSSYRGGSRG GGSNYMSNLP FGLGYGDVGK NHITEFPSIP LPINGPITNK ERSLAVKYIN FGKTVKDGPF YTGSMSLIID QQENSKSGK RKPNIILDED DTNDGIERYS DKYLKKRKIG ISIDDHPYNL NLFPNELYNV MGINKKKLLA ISKFNNADDV F TGTGLQDE NIGLSMLAKL KELAEDVDDA STGDGAAKGS KTGEGEDDDL ADDDFEEDED EEDDDDYNAE KYFNNGDDDD YG DEEDPNE EAAF

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Macromolecule #18: TATA-box-binding protein

MacromoleculeName: TATA-box-binding protein / type: protein_or_peptide / ID: 18 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 27.042275 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MADEERLKEF KEANKIVFDP NTRQVWENQN RDGTKPATTF QSEEDIKRAA PESEKDTSAT SGIVPTLQNI VATVTLGCRL DLKTVALHA RNAEYNPKRF AAVIMRIREP KTTALIFASG KMVVTGAKSE DDSKLASRKY ARIIQKIGFA AKFTDFKIQN I VGSCDVKF ...String:
MADEERLKEF KEANKIVFDP NTRQVWENQN RDGTKPATTF QSEEDIKRAA PESEKDTSAT SGIVPTLQNI VATVTLGCRL DLKTVALHA RNAEYNPKRF AAVIMRIREP KTTALIFASG KMVVTGAKSE DDSKLASRKY ARIIQKIGFA AKFTDFKIQN I VGSCDVKF PIRLEGLAFS HGTFSSYEPE LFPGLIYRMV KPKIVLLIFV SGKIVLTGAK QREEIYQAFE AIYPVLSEFR KM

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Macromolecule #19: Transcription factor IIIB 70 kDa subunit

MacromoleculeName: Transcription factor IIIB 70 kDa subunit / type: protein_or_peptide / ID: 19 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 67.011477 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MPVCKNCHGT EFERDLSNAN NDLVCKACGV VSEDNPIVSE VTFGETSAGA AVVQGSFIGA GQSHAAFGGS SALESREATL NNARRKLRA VSYALHIPEY ITDAAFQWYK LALANNFVQG RRSQNVIASC LYVACRKEKT HHMLIDFSSR LQVSVYSIGA T FLKMVKKL ...String:
MPVCKNCHGT EFERDLSNAN NDLVCKACGV VSEDNPIVSE VTFGETSAGA AVVQGSFIGA GQSHAAFGGS SALESREATL NNARRKLRA VSYALHIPEY ITDAAFQWYK LALANNFVQG RRSQNVIASC LYVACRKEKT HHMLIDFSSR LQVSVYSIGA T FLKMVKKL HITELPLADP SLFIQHFAEK LDLADKKIKV VKDAVKLAQR MSKDWMFEGR RPAGIAGACI LLACRMNNLR RT HTEIVAV SHVAEETLQQ RLNEFKNTKA AKLSVQKFRE NDVEDGEARP PSFVKNRKKE RKIKDSLDKE EMFQTSEEAL NKN PILTQV LGEQELSSKE VLFYLKQFSE RRARVVERIK ATNGIDGENI YHEGSENETR KRKLSEVSIQ NEHVEGEDKE TEGT EEKVK KVKTKTSEEK KENESGHFQD AIDGYSLETD PYCPRNLHLL PTTDTYLSKV SDDPDNLEDV DDEELNAHLL NEEAS KLKE RIWIGLNADF LLEQESKRLK QEADIATGNT SVKKKRTRRR NNTRSDEPTK TVDAAAAIGL MSDLQDKSGL HAALKA AEE SGDFTTADSV KNMLQKASFS KKINYDAIDG LFR

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Macromolecule #20: Transcription factor TFIIIB component B''

MacromoleculeName: Transcription factor TFIIIB component B'' / type: protein_or_peptide / ID: 20 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Strain: ATCC 204508 / S288c
Molecular weightTheoretical: 67.801906 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MSSIVNKSGT RFAPKVRQRR AATGGTPTPK PRTPQLFIPE SKEIEEDNSD NDKGVDENET AIVEKPSLVG ERSLEGFTLT GTNGHDNEI GDEGPIDAST QNPKADVIED NVTLKPAPLQ THRDQKVPRS SRLASLSKDN ESRPSFKPSF LDSSSNSNGT A RRLSTISN ...String:
MSSIVNKSGT RFAPKVRQRR AATGGTPTPK PRTPQLFIPE SKEIEEDNSD NDKGVDENET AIVEKPSLVG ERSLEGFTLT GTNGHDNEI GDEGPIDAST QNPKADVIED NVTLKPAPLQ THRDQKVPRS SRLASLSKDN ESRPSFKPSF LDSSSNSNGT A RRLSTISN KLPKKIRLGS ITENDMNLKT FKRHRVLGKP SSAKKPAGAH RISIVSKISP PTAMTDSLDR NEFSSETSTS RE ADENENY VISKVKDIPK KVRDGESAKY FIDEENFTMA ELCKPNFPIG QISENFEKSK MAKKAKLEKR RHLRELRMRA RQE FKPLHS LTKEEQEEEE EKRKEERDKL LNADIPESDR KAHTAIQLKL NPDGTMAIDE ETMVVDRHKN ASIENEYKEK VDEN PFANL YNYGSYGRGS YTDPWTVEEM IKFYKALSMW GTDFNLISQL YPYRSRKQVK AKFVNEEKKR PILIELALRS KLPPN FDEY CCEIKKNIGT VADFNEKLIE LQNEHKHHMK EIEEAKNTAK EEDQTAQRLN DANLNKKGSG GIMTNDLKVY RKTEVV LGT IDDLKRKKLK ERNNDDNEDN EGSEEEPEID Q

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Macromolecule #21: Non-Template DNA

MacromoleculeName: Non-Template DNA / type: dna / ID: 21 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 24.885926 KDa
SequenceString: (DC)(DG)(DT)(DC)(DC)(DA)(DC)(DT)(DA)(DT) (DT)(DT)(DT)(DC)(DG)(DG)(DC)(DT)(DA)(DC) (DT)(DA)(DT)(DA)(DA)(DA)(DT)(DA)(DA) (DA)(DT)(DG)(DT)(DT)(DT)(DT)(DT)(DT)(DT) (DC) (DG)(DC)(DA)(DA)(DC)(DT) ...String:
(DC)(DG)(DT)(DC)(DC)(DA)(DC)(DT)(DA)(DT) (DT)(DT)(DT)(DC)(DG)(DG)(DC)(DT)(DA)(DC) (DT)(DA)(DT)(DA)(DA)(DA)(DT)(DA)(DA) (DA)(DT)(DG)(DT)(DT)(DT)(DT)(DT)(DT)(DT) (DC) (DG)(DC)(DA)(DA)(DC)(DT)(DA)(DT) (DG)(DT)(DG)(DT)(DT)(DC)(DG)(DC)(DG)(DA) (DA)(DG) (DT)(DA)(DA)(DC)(DC)(DC)(DT) (DT)(DC)(DG)(DT)(DG)(DG)(DA)(DC)(DA)(DT) (DT)(DT)(DG) (DG)

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Macromolecule #22: Template DNA

MacromoleculeName: Template DNA / type: dna / ID: 22 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 25.065127 KDa
SequenceString: (DC)(DC)(DA)(DA)(DA)(DT)(DG)(DT)(DC)(DC) (DA)(DC)(DG)(DA)(DA)(DG)(DG)(DG)(DT)(DT) (DA)(DC)(DT)(DT)(DC)(DG)(DC)(DG)(DA) (DA)(DC)(DA)(DC)(DA)(DT)(DA)(DG)(DT)(DT) (DG) (DC)(DG)(DA)(DA)(DA)(DA) ...String:
(DC)(DC)(DA)(DA)(DA)(DT)(DG)(DT)(DC)(DC) (DA)(DC)(DG)(DA)(DA)(DG)(DG)(DG)(DT)(DT) (DA)(DC)(DT)(DT)(DC)(DG)(DC)(DG)(DA) (DA)(DC)(DA)(DC)(DA)(DT)(DA)(DG)(DT)(DT) (DG) (DC)(DG)(DA)(DA)(DA)(DA)(DA)(DA) (DA)(DC)(DA)(DT)(DT)(DT)(DA)(DT)(DT)(DT) (DA)(DT) (DA)(DG)(DT)(DA)(DG)(DC)(DC) (DG)(DA)(DA)(DA)(DA)(DT)(DA)(DG)(DT)(DG) (DG)(DA)(DC) (DG)

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Macromolecule #23: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 23 / Number of copies: 7 / Formula: ZN
Molecular weightTheoretical: 65.409 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

Concentration0.02 mg/mL
BufferpH: 7.5
GridModel: Quantifoil R2/1 / Material: COPPER / Pretreatment - Type: GLOW DISCHARGE
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV
DetailsCrosslinked with glutaraldehyde

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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
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Average electron dose: 60.9 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: PDB ENTRY
PDB model - PDB ID:

5fj8

Initial angle assignmentType: PROJECTION MATCHING
Final angle assignmentType: PROJECTION MATCHING
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 2.0) / Number images used: 62751
FSC plot (resolution estimation)

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Atomic model buiding 1

RefinementSpace: REAL / Protocol: AB INITIO MODEL / Overall B value: 130 / Target criteria: Cross-correlation coefficient
Output model

PDB-6f40:
RNA Polymerase III open complex

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