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- EMDB-3590: Structure -

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Basic information

Entry
Database: EMDB / ID: EMD-3590
TitleStructure
Map dataNone
Sample
  • Complex: RNA polymerase I in complex with Rrn3 and Core Factor
    • Complex: RNA polymerase I
      • Protein or peptide: x 14 types
    • Complex: Initiation factor Rrn3
      • Protein or peptide: x 1 types
    • Complex: Core Factor
      • Protein or peptide: x 3 types
  • Ligand: x 3 types
KeywordsTranscription / RNA polymerase I initiation
Function / homology
Function and homology information


RNA polymerase I transcription regulatory region sequence-specific DNA binding / RNA polymerase I core factor complex / RNA polymerase I core binding / RNA polymerase I general transcription initiation factor activity / RNA polymerase I general transcription initiation factor binding / rDNA binding / RNA polymerase I core promoter sequence-specific DNA binding / RNA polymerase I preinitiation complex assembly / RNA Polymerase I Transcription Initiation / Processing of Capped Intron-Containing Pre-mRNA ...RNA polymerase I transcription regulatory region sequence-specific DNA binding / RNA polymerase I core factor complex / RNA polymerase I core binding / RNA polymerase I general transcription initiation factor activity / RNA polymerase I general transcription initiation factor binding / rDNA binding / RNA polymerase I core promoter sequence-specific DNA binding / RNA polymerase I preinitiation complex assembly / 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 / RNA polymerase II transcribes snRNA genes / TP53 Regulates Transcription of DNA Repair Genes / 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 / termination of RNA polymerase III transcription / RNA Polymerase II Pre-transcription Events / RNA-templated transcription / Formation of TC-NER Pre-Incision Complex / regulation of cell size / transcription initiation at RNA polymerase III promoter / RNA Polymerase I Promoter Escape / termination of RNA polymerase I transcription / Gap-filling DNA repair synthesis and ligation in TC-NER / transcription initiation at RNA polymerase I promoter / nucleolar large rRNA transcription by RNA polymerase I / Estrogen-dependent gene expression / transcription by RNA polymerase III / Dual incision in TC-NER / RNA polymerase I complex / transcription elongation by RNA polymerase I / RNA polymerase III complex / RNA polymerase II, core complex / tRNA transcription by RNA polymerase III / transcription by RNA polymerase I / TBP-class protein binding / transcription initiation at RNA polymerase II promoter / transcription elongation by RNA polymerase II / promoter-specific chromatin binding / ribonucleoside binding / DNA-directed RNA polymerase / DNA-directed RNA polymerase activity / peroxisome / ribosome biogenesis / nucleic acid binding / RNA polymerase II-specific DNA-binding transcription factor binding / transcription by RNA polymerase II / protein dimerization activity / nucleolus / negative regulation of transcription by RNA polymerase II / mitochondrion / DNA binding / zinc ion binding / nucleoplasm / metal ion binding / nucleus / cytoplasm
Similarity search - Function
RNA polymerase I specific transcription initiation factor RRN3 / RNA polymerase I specific transcription initiation factor RRN3 / Transcription initiation factor Rrn11 / RNA polymerase I-specific transcription initiation factor Rrn6 / Transcription initiation factor Rrn11, budding yeast / RNA polymerase I-specific transcription initiation factor RRN6-like / : / : / : / : ...RNA polymerase I specific transcription initiation factor RRN3 / RNA polymerase I specific transcription initiation factor RRN3 / Transcription initiation factor Rrn11 / RNA polymerase I-specific transcription initiation factor Rrn6 / Transcription initiation factor Rrn11, budding yeast / RNA polymerase I-specific transcription initiation factor RRN6-like / : / : / : / : / RNA polymerase I-specific transcription initiation factor Rrn11 / Rrn6, beta-propeller / RRN6, K-rich C-terminal domain / Rrn6, helical bundle domain / Transcription initiation factor Rrn7, Zinc-finger / RNA polymerase I transcription initiation factor TAF1B/Rrn7 / : / : / Zinc-finger of RNA-polymerase I-specific TFIIB, Rrn7 / Rrn7/TAF1B, N-terminal cyclin domain / Rrn7/TAF1B, C-terminal cyclin domain / : / DNA-directed RNA polymerase I, subunit RPA34.5 / DNA-directed RNA polymerase I subunit RPA34.5 / RNA polymerase I, subunit Rpa14, fungi / Yeast RNA polymerase I subunit RPA14 / RNA polymerase I associated factor, A49-like / A49-like RNA polymerase I associated factor / Rpa43, N-terminal ribonucleoprotein (RNP) domain / Pol I subunit A12, C-terminal zinc ribbon / RPA43, OB domain / RPA43 OB domain in RNA Pol I / DNA-directed RNA polymerase I subunit RPA2, domain 4 / DNA-directed RNA pol I, largest subunit / : / RNA polymerase I, Rpa2 specific domain / DNA-directed RNA polymerases I and III subunit AC19 / DNA-directed RNA polymerases I and III subunit AC40 / 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 / 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 / RNA polymerases N / 8 kDa subunit / RNA polymerases N / 8 Kd subunits signature. / DNA directed RNA polymerase, 7 kDa subunit / RNA polymerase archaeal subunit P/eukaryotic subunit RPABC4 / RNA polymerase, subunit H/Rpb5, conserved site / RNA polymerases H / 23 Kd subunits signature. / RNA polymerase subunit CX / DNA-directed RNA polymerase, 30-40kDa subunit, conserved site / DNA-directed RNA polymerase subunit Rpo3/Rpb3/RPAC1 / RNA polymerases D / 30 to 40 Kd subunits signature. / DNA-directed RNA polymerase Rpb11, 13-16kDa subunit, conserved site / DNA-directed RNA polymerase subunit Rpo11 / RNA polymerases L / 13 to 16 Kd subunits signature. / RNA polymerase subunit RPABC4/transcription elongation factor Spt4 / Zinc finger, TFIIS-type / Transcription factor S-II (TFIIS) / Zinc finger TFIIS-type profile. / C2C2 Zinc finger / 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 / DNA-directed RNA polymerase, insert domain / DNA-directed RNA polymerase, RpoA/D/Rpb3-type / RNA polymerase Rpb3/RpoA insert domain / RNA polymerase Rpb3/Rpb11 dimerisation domain / RNA polymerases D
Similarity search - Domain/homology
DNA-directed RNA polymerases I and III subunit RPAC1 / DNA-directed RNA polymerase I subunit RPA190 / 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 polymerase I subunit RPA135 / DNA-directed RNA polymerases I, II, and III subunit RPABC5 / DNA-directed RNA polymerases I and III subunit RPAC2 / DNA-directed RNA polymerase I subunit RPA12 / RNA polymerase I-specific transcription initiation factor RRN6 ...DNA-directed RNA polymerases I and III subunit RPAC1 / DNA-directed RNA polymerase I subunit RPA190 / 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 polymerase I subunit RPA135 / DNA-directed RNA polymerases I, II, and III subunit RPABC5 / DNA-directed RNA polymerases I and III subunit RPAC2 / DNA-directed RNA polymerase I subunit RPA12 / RNA polymerase I-specific transcription initiation factor RRN6 / RNA polymerase I-specific transcription initiation factor RRN3 / DNA-directed RNA polymerases I, II, and III subunit RPABC4 / RNA polymerase I-specific transcription initiation factor RRN7 / DNA-directed RNA polymerase I subunit RPA43 / DNA-directed RNA polymerase I subunit RPA34 / DNA-directed RNA polymerase I subunit RPA14 / DNA-directed RNA polymerase I subunit RPA49 / RNA polymerase I-specific transcription initiation factor RRN11
Similarity search - Component
Biological speciesSaccharomyces cerevisiae (brewer's yeast)
Methodsingle particle reconstruction / cryo EM / Resolution: 7.7 Å
AuthorsEngel C / Gubbey T / Neyer S / Sainsbury S / Oberthuer C / Baejen C / Bernecky C / Cramer P
Funding support Germany, 3 items
OrganizationGrant numberCountry
German Research FoundationSFB860, SPP1935 Germany
The Advanced Grant TRANSREGULON from the European Research Council693023 Germany
Volkswagen Foundation Germany
CitationJournal: Cell / Year: 2017
Title: Structural Basis of RNA Polymerase I Transcription Initiation.
Authors: Christoph Engel / Tobias Gubbey / Simon Neyer / Sarah Sainsbury / Christiane Oberthuer / Carlo Baejen / Carrie Bernecky / Patrick Cramer /
Abstract: Transcription initiation at the ribosomal RNA promoter requires RNA polymerase (Pol) I and the initiation factors Rrn3 and core factor (CF). Here, we combine X-ray crystallography and cryo-electron ...Transcription initiation at the ribosomal RNA promoter requires RNA polymerase (Pol) I and the initiation factors Rrn3 and core factor (CF). Here, we combine X-ray crystallography and cryo-electron microscopy (cryo-EM) to obtain a molecular model for basal Pol I initiation. The three-subunit CF binds upstream promoter DNA, docks to the Pol I-Rrn3 complex, and loads DNA into the expanded active center cleft of the polymerase. DNA unwinding between the Pol I protrusion and clamp domains enables cleft contraction, resulting in an active Pol I conformation and RNA synthesis. Comparison with the Pol II system suggests that promoter specificity relies on a distinct "bendability" and "meltability" of the promoter sequence that enables contacts between initiation factors, DNA, and polymerase.
History
DepositionFeb 14, 2017-
Header (metadata) releaseMar 22, 2017-
Map releaseApr 5, 2017-
UpdateOct 1, 2025-
Current statusOct 1, 2025Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.0205
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by radius
  • Surface level: 0.0205
  • Imaged by UCSF Chimera
  • Download
  • Surface view with fitted model
  • Atomic models: PDB-5n5y
  • Surface level: 0.0205
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_3590.png

Downloads & links

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Map

FileDownload / File: emd_3590.map.gz / Format: CCP4 / Size: 52.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationNone
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.35 Å/pix.
x 240 pix.
= 324. Å		1.35 Å/pix.
x 240 pix.
= 324. Å		1.35 Å/pix.
x 240 pix.
= 324. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.35 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.0205 / Movie #1: 0.0205
Minimum - Maximum-0.029996127 - 0.06755038
Average (Standard dev.)-0.000064416134 (±0.004714947)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
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
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS240240240
D min/max/mean-0.0300.068-0.000

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Supplemental data

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Sample components

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Entire : RNA polymerase I in complex with Rrn3 and Core Factor

EntireName: RNA polymerase I in complex with Rrn3 and Core Factor
Components
  • Complex: RNA polymerase I in complex with Rrn3 and Core Factor
    • Complex: RNA polymerase I
      • Protein or peptide: DNA-directed RNA polymerase I subunit RPA190
      • Protein or peptide: DNA-directed RNA polymerase I subunit RPA135
      • Protein or peptide: DNA-directed RNA polymerases I and III subunit RPAC1
      • Protein or peptide: DNA-directed RNA polymerase I subunit RPA14
      • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC1
      • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC2
      • Protein or peptide: DNA-directed RNA polymerase I subunit RPA43
      • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC3
      • Protein or peptide: DNA-directed RNA polymerase I subunit RPA12
      • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC5
      • Protein or peptide: DNA-directed RNA polymerases I and III subunit RPAC2
      • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC4
      • Protein or peptide: DNA-directed RNA polymerase I subunit RPA49
      • Protein or peptide: DNA-directed RNA polymerase I subunit RPA34
    • Complex: Initiation factor Rrn3
      • Protein or peptide: RNA polymerase I-specific transcription initiation factor RRN3
    • Complex: Core Factor
      • Protein or peptide: RNA polymerase I-specific transcription initiation factor RRN6
      • Protein or peptide: RNA polymerase I-specific transcription initiation factor RRN7
      • Protein or peptide: RNA polymerase I-specific transcription initiation factor RRN11
  • Ligand: ZINC ION
  • Ligand: SULFATE ION
  • Ligand: MAGNESIUM ION

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Supramolecule #1: RNA polymerase I in complex with Rrn3 and Core Factor

SupramoleculeName: RNA polymerase I in complex with Rrn3 and Core Factor / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#18

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Supramolecule #2: RNA polymerase I

SupramoleculeName: RNA polymerase I / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#14
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 590 KDa

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Supramolecule #3: Initiation factor Rrn3

SupramoleculeName: Initiation factor Rrn3 / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #15
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 70 KDa

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Supramolecule #4: Core Factor

SupramoleculeName: Core Factor / type: complex / ID: 4 / Parent: 1 / Macromolecule list: #16-#18
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 220 KDa

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Macromolecule #1: DNA-directed RNA polymerase I subunit RPA190

MacromoleculeName: DNA-directed RNA polymerase I subunit RPA190 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA-directed RNA polymerase
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 186.676969 KDa
SequenceString: MDISKPVGSE ITSVDFGILT AKEIRNLSAK QITNPTVLDN LGHPVSGGLY DLALGAFLRN LCSTCGLDEK FCPGHQGHIE LPVPCYNPL FFNQLYIYLR ASCLFCHHFR LKSVEVHRYA CKLRLLQYGL IDESYKLDEI TLGSLNSSMY TDDEAIEDNE D EMDGEGSK ...String:
MDISKPVGSE ITSVDFGILT AKEIRNLSAK QITNPTVLDN LGHPVSGGLY DLALGAFLRN LCSTCGLDEK FCPGHQGHIE LPVPCYNPL FFNQLYIYLR ASCLFCHHFR LKSVEVHRYA CKLRLLQYGL IDESYKLDEI TLGSLNSSMY TDDEAIEDNE D EMDGEGSK QSKDISSTLL NELKSKRSEY VDMAIAKALS DGRTTERGSF TATVNDERKK LVHEFHKKLL SRGKCDNCGM FS PKFRKDG FTKIFETALN EKQITNNRVK GFIRQDMIKK QKQAKKLDGS NEASANDEES FDVGRNPTTR PKTGSTYILS TEV KNILDT VFRKEQCVLQ YVFHSRPNLS RKLVKADSFF MDVLVVPPTR FRLPSKLGEE VHENSQNQLL SKVLTTSLLI RDLN DDLSK LQKDKVSLED RRVIFSRLMN AFVTIQNDVN AFIDSTKAQG RTSGKVPIPG VKQALEKKEG LFRKHMMGKR VNYAA RSVI SPDPNIETNE IGVPPVFAVK LTYPEPVTAY NIAELRQAVI NGPDKWPGAT QIQNEDGSLV SLIGMSVEQR KALANQ LLT PSSNVSTHTL NKKVYRHIKN RDVVLMNRQP TLHKASMMGH KVRVLPNEKT LRLHYANTGA YNADFDGDEM NMHFPQN EN ARAEALNLAN TDSQYLTPTS GSPVRGLIQD HISAGVWLTS KDSFFTREQY QQYIYGCIRP EDGHTTRSKI VTLPPTIF K PYPLWTGKQI ITTVLLNVTP PDMPGINLIS KNKIKNEYWG KGSLENEVLF KDGALLCGIL DKSQYGASKY GIVHSLHEV YGPEVAAKVL SVLGRLFTNY ITATAFTCGM DDLRLTAEGN KWRTDILKTS VDTGREAAAE VTNLDKDTPA DDPELLKRLQ EILRDNNKS GILDAVTSSK VNAITSQVVS KCVPDGTMKK FPCNSMQAMA LSGAKGSNVN VSQIMCLLGQ QALEGRRVPV M VSGKTLPS FKPYETDAMA GGYVKGRFYS GIKPQEYYFH CMAGREGLID TAVKTSRSGY LQRCLTKQLE GVHVSYDNSI RD ADGTLVQ FMYGGDAIDI TKESHMTQFE FCLDNYYALL KKYNPSALIE HLDVESALKY SKKTLKYRKK HSKEPHYKQS VKY DPVLAK YNPAKYLGSV SENFQDKLES FLDKNSKLFK SSDGVNEKKF RALMQLKYMR SLINPGEAVG IIASQSVGEP STQM TLNTF HFAGHGAANV TLGIPRLREI VMTASAAIKT PQMTLPIWND VSDEQADTFC KSISKVLLSE VIDKVIVTET TGTSN TAGG NAARSYVIHM RFFDNNEYSE EYDVSKEELQ NVISNQFIHL LEAAIVKEIK KQKRTTGPDI GVAVPRLQTD VANSSS NSK RLEEDNDEEQ SHKKTKQAVS YDEPDEDEIE TMREAEKSSD EEGIDSDKES DSDSEDEDVD MNEQINKSIV EANNNMN KV QRDRQSAIIS HHRFITKYNF DDESGKWCEF KLELAADTEK LLMVNIVEEI CRKSIIRQIP HIDRCVHPEP ENGKRVLV T EGVNFQAMWD QEAFIDVDGI TSNDVAAVLK TYGVEAARNT IVNEINNVFS RYAISVSFRH LDLIADMMTR QGTYLAFNR QGMETSTSSF MKMSYETTCQ FLTKAVLDNE REQLDSPSAR IVVGKLNNVG TGSFDVLAKV PNAA

UniProtKB: DNA-directed RNA polymerase I subunit RPA190

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Macromolecule #2: DNA-directed RNA polymerase I subunit RPA135

MacromoleculeName: DNA-directed RNA polymerase I subunit RPA135 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA-directed RNA polymerase
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 135.910328 KDa
SequenceString: MSKVIKPPGQ ARTADFRTLE RESRFINPPK DKSAFPLLQE AVQPHIGSFN ALTEGPDGGL LNLGVKDIGE KVIFDGKPLN SEDEISNSG YLGNKLSVSV EQVSIAKPMS NDGVSSAVER KVYPSESRQR LTSYRGKLLL KLKWSVNNGE ENLFEVRDCG G LPVMLQSN ...String:
MSKVIKPPGQ ARTADFRTLE RESRFINPPK DKSAFPLLQE AVQPHIGSFN ALTEGPDGGL LNLGVKDIGE KVIFDGKPLN SEDEISNSG YLGNKLSVSV EQVSIAKPMS NDGVSSAVER KVYPSESRQR LTSYRGKLLL KLKWSVNNGE ENLFEVRDCG G LPVMLQSN RCHLNKMSPY ELVQHKEESD EIGGYFIVNG IEKLIRMLIV QRRNHPMAII RPSFANRGAS YSHYGIQIRS VR PDQTSQT NVLHYLNDGQ VTFRFSWRKN EYLVPVVMIL KALCHTSDRE IFDGIIGNDV KDSFLTDRLE LLLRGFKKRY PHL QNRTQV LQYLGDKFRV VFQASPDQSD LEVGQEVLDR IVLVHLGKDG SQDKFRMLLF MIRKLYSLVA GECSPDNPDA TQHQ EVLLG GFLYGMILKE KIDEYLQNII AQVRMDINRG MAINFKDKRY MSRVLMRVNE NIGSKMQYFL STGNLVSQSG LDLQQ VSGY TVVAEKINFY RFISHFRMVH RGSFFAQLKT TTVRKLLPES WGFLCPVHTP DGSPCGLLNH FAHKCRISTQ QSDVSR IPS ILYSLGVAPA SHTFAAGPSL CCVQIDGKII GWVSHEQGKI IADTLRYWKV EGKTPGLPID LEIGYVPPST RGQYPGL YL FGGHSRMLRP VRYLPLDKED IVGPFEQVYM NIAVTPQEIQ NNVHTHVEFT PTNILSILAN LTPFSDFNQS PRNMYQCQ M GKQTMGTPGV ALCHRSDNKL YRLQTGQTPI VKANLYDDYG MDNFPNGFNA VVAVISYTGY DMDDAMIINK SADERGFGY GTMYKTEKVD LALNRNRGDP ITQHFGFGND EWPKEWLEKL DEDGLPYIGT YVEEGDPICA YFDDTLNKTK IKTYHSSEPA YIEEVNLIG DESNKFQELQ TVSIKYRIRR TPQIGDKFSS RHGQKGVCSR KWPTIDMPFS ETGIQPDIII NPHAFPSRMT I GMFVESLA GKAGALHGIA QDSTPWIFNE DDTPADYFGE QLAKAGYNYH GNEPMYSGAT GEELRADIYV GVVYYQRLRH MV NDKFQVR STGPVNSLTM QPVKGRKRHG GIRVGEMERD ALIGHGTSFL LQDRLLNSSD YTQASVCREC GSILTTQQSV PRI GSISTV CCRRCSMRFE DAKKLLTKSE DGEKIFIDDS QIWEDGQGNK FVGGNETTTV AIPFVLKYLD SELSAMGIRL RYNV EPK

UniProtKB: DNA-directed RNA polymerase I subunit RPA135

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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: Saccharomyces cerevisiae (brewer's yeast)
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

UniProtKB: DNA-directed RNA polymerases I and III subunit RPAC1

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Macromolecule #4: DNA-directed RNA polymerase I subunit RPA14

MacromoleculeName: DNA-directed RNA polymerase I subunit RPA14 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 14.599128 KDa
SequenceString:
MMKGSRRTGN NTATTLNTPV VIHATQLPQH VSTDEVLQFL ESFIDEKENI IDSTTMNTIS GNAADADAAA VANTSLNIDT NLSSSISQL KRIQRDFKGL PPAQDFSAAP IQVSTTEKKE TSIGVSATGG KKTTFADE

UniProtKB: DNA-directed RNA polymerase I subunit RPA14

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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: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 25.117094 KDa
SequenceString: MDQENERNIS RLWRAFRTVK EMVKDRGYFI TQEEVELPLE DFKAKYCDSM GRPQRKMMSF QANPTEESIS KFPDMGSLWV EFCDEPSVG VKTMKTFVIH IQEKNFQTGI FVYQNNITPS AMKLVPSIPP ATIETFNEAA LVVNITHHEL VPKHIRLSSD E KRELLKRY ...String:
MDQENERNIS RLWRAFRTVK EMVKDRGYFI TQEEVELPLE DFKAKYCDSM GRPQRKMMSF QANPTEESIS KFPDMGSLWV EFCDEPSVG VKTMKTFVIH IQEKNFQTGI FVYQNNITPS AMKLVPSIPP ATIETFNEAA LVVNITHHEL VPKHIRLSSD E KRELLKRY RLKESQLPRI QRADPVALYL GLKRGEVVKI IRKSETSGRY ASYRICM

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

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Macromolecule #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: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 17.931834 KDa
SequenceString:
MSDYEEAFND GNENFEDFDV EHFSDEETYE EKPQFKDGET TDANGKTIVT GGNGPEDFQQ HEQIRRKTLK EKAIPKDQRA TTPYMTKYE RARILGTRAL QISMNAPVFV DLEGETDPLR IAMKELAEKK IPLVIRRYLP DGSFEDWSVE ELIVDL

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

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Macromolecule #7: DNA-directed RNA polymerase I subunit RPA43

MacromoleculeName: DNA-directed RNA polymerase I subunit RPA43 / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 36.264852 KDa
SequenceString: MSQVKRANEN RETARFIKKH KKQVTNPIDE KNGTSNCIVR VPIALYVSLA PMYLENPLQG VMKQHLNPLV MKYNNKVGGV VLGYEGLKI LDADPLSKED TSEKLIKITP DTPFGFTWCH VNLYVWQPQV GDVLEGYIFI QSASHIGLLI HDAFNASIKK N NIPVDWTF ...String:
MSQVKRANEN RETARFIKKH KKQVTNPIDE KNGTSNCIVR VPIALYVSLA PMYLENPLQG VMKQHLNPLV MKYNNKVGGV VLGYEGLKI LDADPLSKED TSEKLIKITP DTPFGFTWCH VNLYVWQPQV GDVLEGYIFI QSASHIGLLI HDAFNASIKK N NIPVDWTF VHNDVEEDAD VINTDENNGN NNNEDNKDSN GGSNSLGKFS FGNRSLGHWV DSNGEPIDGK LRFTVRNVHT TG RVVSVDG TLISDADEEG NGYNSSRSQA ESLPIVSNKK IVFDDEVSIE NKESHKELDL PEVKEDNGSE IVYEENTSES NDG ESSDSD

UniProtKB: DNA-directed RNA polymerase I subunit RPA43

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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: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 16.525363 KDa
SequenceString:
MSNTLFDDIF QVSEVDPGRY NKVCRIEAAS TTQDQCKLTL DINVELFPVA AQDSLTVTIA SSLNLEDTPA NDSSATRSWR PPQAGDRSL ADDYDYVMYG TAYKFEEVSK DLIAVYYSFG GLLMRLEGNY RNLNNLKQEN AYLLIRR

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

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Macromolecule #9: DNA-directed RNA polymerase I subunit RPA12

MacromoleculeName: DNA-directed RNA polymerase I subunit RPA12 / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 13.676566 KDa
SequenceString:
MSVVGSLIFC LDCGDLLENP NAVLGSNVEC SQCKAIYPKS QFSNLKVVTT TADDAFPSSL RAKKSVVKTS LKKNELKDGA TIKEKCPQC GNEEMNYHTL QLRSADEGAT VFYTCTSCGY KFRTNN

UniProtKB: DNA-directed RNA polymerase I subunit RPA12

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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: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 8.290732 KDa
SequenceString:
MIVPVRCFSC GKVVGDKWES YLNLLQEDEL DEGTALSRLG LKRYCCRRMI LTHVDLIEKF LRYNPLEKRD

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

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Macromolecule #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: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 16.16786 KDa
SequenceString:
MTEDIEQKKT ATEVTPQEPK HIQEEEEQDV DMTGDEEQEE EPDREKIKLL TQATSEDGTS ASFQIVEEDH TLGNALRYVI MKNPDVEFC GYSIPHPSEN LLNIRIQTYG ETTAVDALQK GLKDLMDLCD VVESKFTEKI KSM

UniProtKB: DNA-directed RNA polymerases I and III subunit RPAC2

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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: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 7.729969 KDa
SequenceString:
MSREGFQIPT NLDAAAAGTS QARTATLKYI CAECSSKLSL SRTDAVRCKD CGHRILLKAR TKRLVQFEAR

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

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Macromolecule #13: DNA-directed RNA polymerase I subunit RPA49

MacromoleculeName: DNA-directed RNA polymerase I subunit RPA49 / type: protein_or_peptide / ID: 13 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 46.721707 KDa
SequenceString: MSVKRSVSEI EIESVQDQPS VAVGSFFKGF RAPSDTTFDL YKKKKSEKDE FVLHGENERL EYEGYTDSSS QASNQYVVGL FNPEKKSIQ LYKAPVLVSK VVSKSSKNLR GPKIKSKSDT RPSALRNALG EAFGTKKAKK AIADLERNRI DSDKLTDSAI D IVDSVRTA ...String:
MSVKRSVSEI EIESVQDQPS VAVGSFFKGF RAPSDTTFDL YKKKKSEKDE FVLHGENERL EYEGYTDSSS QASNQYVVGL FNPEKKSIQ LYKAPVLVSK VVSKSSKNLR GPKIKSKSDT RPSALRNALG EAFGTKKAKK AIADLERNRI DSDKLTDSAI D IVDSVRTA SKDLPTRAQL DEITSNDRPT PLANIDATDV EQIYPIESII PKKELQFIRV SSILKEADKE KKLELFPYQN NS KYVAKKL DSLTQPSQMT KLQLLYYLSL LLGVYENRRV NNKTKLLERL NSPPEILVDG ILSRFTVIKP GQFGRSKDRS YFI DPQNED KILCYILAII MHLDNFIVEI TPLAHELNLK PSKVVSLFRV LGAIVKGATV AQAEAFGIPK STAASYKIAT MKVP FKLPE MTRRGRGPRR

UniProtKB: DNA-directed RNA polymerase I subunit RPA49

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Macromolecule #14: DNA-directed RNA polymerase I subunit RPA34

MacromoleculeName: DNA-directed RNA polymerase I subunit RPA34 / type: protein_or_peptide / ID: 14 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 26.933518 KDa
SequenceString: MSKLSKDYVS DSDSDDEVIS NEFSIPDGFK KCKHLKNFPL NGDNKKKAKQ QQVWLIKFPS NVDISKLKSL PVDFESSTTM TIDKHDYKI MDDTDIESSL TQDNLSNMTL LVPSESKESL KIASTAKDNA PLQFDKVFSV SETAKIPAID YSKVRVPRKD V PKVEGLKL ...String:
MSKLSKDYVS DSDSDDEVIS NEFSIPDGFK KCKHLKNFPL NGDNKKKAKQ QQVWLIKFPS NVDISKLKSL PVDFESSTTM TIDKHDYKI MDDTDIESSL TQDNLSNMTL LVPSESKESL KIASTAKDNA PLQFDKVFSV SETAKIPAID YSKVRVPRKD V PKVEGLKL EHFATGYDAE DFHVAEEVKE NKKEPKKRSH HDDEEESSEK KKKKKEKREK REKKDKKDKK KKHRD

UniProtKB: DNA-directed RNA polymerase I subunit RPA34

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Macromolecule #15: RNA polymerase I-specific transcription initiation factor RRN3

MacromoleculeName: RNA polymerase I-specific transcription initiation factor RRN3
type: protein_or_peptide / ID: 15 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 72.458258 KDa
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: MMAFENTSKR PPQDFVAPID QKKRKVQFSD STGLVTLQPE EIKDEVFSAA MYSRFVKSAL DDLDKNDSTQ IGIIANQVAL PSKNPERIN DKNLNILLDI LSSNINRIES SRGTFLIQSI INFEKWWELP PHTLSKYIYF IKILCSSIPK WWQDVSMILV S CFILPIKQ ...String:
MMAFENTSKR PPQDFVAPID QKKRKVQFSD STGLVTLQPE EIKDEVFSAA MYSRFVKSAL DDLDKNDSTQ IGIIANQVAL PSKNPERIN DKNLNILLDI LSSNINRIES SRGTFLIQSI INFEKWWELP PHTLSKYIYF IKILCSSIPK WWQDVSMILV S CFILPIKQ TVCHHDMLKY FLRMIPSSMG FIDTYLAKFF PNKNDTRRKL VNYTSNLLKL RGYCSELGFQ IWSLLIEKII SI DVELQNE LDELDDDVDD DDLEEVDLED DDDLDDDSGD DDDENCGNSN EELRSGAADG SQSDSEDMDI IEGMDGTEEY NVE LTQGIK ELSTKLDSIL TLVSTHVEEQ VTPESLESGE GVGVFNTLTT LFKTHVLPTY YTRSIQYIMF HVSQQQLELM DSFL VTLID ISFAVNEAAE KKIKSLQYLG SYIARAKKLS RTQIIFVASY LTSWLNRYVI EREEEVDQRG GMERFKHFYA AFQAL CYIF CFRHNIFRDT DGNWECELDK FFQRMVISKF NPLKFCNENV MLMFARIAQQ ESVAYCFSII ENNNNERLRG IIGKAD SDK KENSAQANTT SSSWSLATRQ QFIDLQSYFP YDPLFLKNYK ILMKEYYIEW SEASGEYESD GSDD

UniProtKB: RNA polymerase I-specific transcription initiation factor RRN3

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Macromolecule #16: RNA polymerase I-specific transcription initiation factor RRN6

MacromoleculeName: RNA polymerase I-specific transcription initiation factor RRN6
type: protein_or_peptide / ID: 16 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 102.163227 KDa
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: MSEGQIPSSD VLGSQLGVGV QGASLYCPQE NYTTKKQEKP QWLRPVDDTL AEDALDLHIV VKSLLCDTAI RYISDDKVLQ ESDADDDLI TSDIDEDTDN QGDTSIVVNP VIPVVPKDVH FFKKVDVGND SMFGVNCDTP VSFQDYIPSD LLRNLDDTLQ E STNSSRPM ...String:
MSEGQIPSSD VLGSQLGVGV QGASLYCPQE NYTTKKQEKP QWLRPVDDTL AEDALDLHIV VKSLLCDTAI RYISDDKVLQ ESDADDDLI TSDIDEDTDN QGDTSIVVNP VIPVVPKDVH FFKKVDVGND SMFGVNCDTP VSFQDYIPSD LLRNLDDTLQ E STNSSRPM QDAFFWDPTV ANRLDSQYIQ TASDLRNYRD GTEIIAYASG KTGSVLNIAV LTRQNTLHLN RHNNVTSIEL HS PIKSIKI PGASESIGRR SNLVGIITEN SFQIFRIESV HSRSCDVMVS SSEPLYFVEI DDLQVVDFAF NPWDLQQFAI IDI KGNWSI GRIPKNFNNN NKRKLQLIDN LHGTIFDPEE LSSWKRIEWF SHFQKILVFD RSKMIEIDFM NNWQTEVVQA KAWS NIRDY KRIDDKNGIL LTSREIIIVG ASESNDPVRR ISWKHDLDPD DTTLRITVQK VKKPDHILLV AFVYSMRHKR IYMHV FSHR KANLFQSLGC STVLEIPGGT PTGIETILTL DHIDDESRRE EDADENFELV VDFLVKLRNS SEVYYYALSN TQNSEP NKQ ETPIIVDHPE WASLFNNADE REKESIGALV SQIKLKERER ISRVQNLIEH ENSHDEDKYL QDLGYRLSIA TNELLES WQ KTKDESILSG SLSHSKLKNL LENSDSFASI PEFSSLLDQF FQYYQDQDVT FIGFEKLLHL FLHEDVPGLD IFYNKLLQ C WVLVSPQAEL LTKEIVKDII WSLARLEKPS LFEPIQNEIS RSLSGPYQDI ISSWDMDDIN EEDESNEFNF DSQFSAPFN GRPPFNLNSQ SQIPTIKSSQ SSGLARRKRI LKTQSQKATP LSQSTQNLSV LPDSMTPAFT LMQPPSSQIS FVNDSQPRNS QKAKKKKKR IRGFG

UniProtKB: RNA polymerase I-specific transcription initiation factor RRN6

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Macromolecule #17: RNA polymerase I-specific transcription initiation factor RRN7

MacromoleculeName: RNA polymerase I-specific transcription initiation factor RRN7
type: protein_or_peptide / ID: 17 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 60.435195 KDa
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: MSTFIRGPIC GTDNCPSRLW RIIDGRRTCQ YGHVMEGDVE FNDDEDDLNG LGAGVITRRL NLTTNATGSF QSSQLTNSQL LQQQQRQSH KKFKKLIGHE AKLLFLKSFQ FILKRQIRWL ITEMRFPKEF EHVAKIIWLK ILKTINDQPQ EELKLQLHMT S TISILYLA ...String:
MSTFIRGPIC GTDNCPSRLW RIIDGRRTCQ YGHVMEGDVE FNDDEDDLNG LGAGVITRRL NLTTNATGSF QSSQLTNSQL LQQQQRQSH KKFKKLIGHE AKLLFLKSFQ FILKRQIRWL ITEMRFPKEF EHVAKIIWLK ILKTINDQPQ EELKLQLHMT S TISILYLA STHLSLPVYT CDYIKWICTA KMPYFQASEI LPKSWRIQLP NYYVSILEGS ISPFNGQLYN KIALTCGMIH FK EFFNSEI SCQGLLLKLV MQCALPPEFY FYTKQVIEFE ETDIRNLTLW ERTDERHTGR VSNHAELRVL SYFMLTINWM LSF DRDRQY PLKWILSLTE SLTQRTTTSE SIGRNIVKVV YPDKPTSSDY FQWSEEETLE FLKWMEKQFL PTQTKSLHNE NGSM EMTID QKIARRKLYK IFPLDREANH DGEFNDSTHQ LTFIEDLQER YAKQTPFFES NKIRDSLNYQ EANPPARKEA IGRLL THIA SQLLVDFAIS KEQLKDCISR IKNACLHRMN

UniProtKB: RNA polymerase I-specific transcription initiation factor RRN7

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Macromolecule #18: RNA polymerase I-specific transcription initiation factor RRN11

MacromoleculeName: RNA polymerase I-specific transcription initiation factor RRN11
type: protein_or_peptide / ID: 18 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Saccharomyces cerevisiae (brewer's yeast)
Molecular weightTheoretical: 59.334262 KDa
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: MFEVPITLTN RKFAQRRKLK YQYINYISRR FDRISKKSTT TDSLPTPENS AAENNDEEEG QNSEAGTYRR SVLQQKKRRR ERHWRSVVG EIYSTTESET DSQEEETEEG GEHDTGIDKE DSDEERKFWK KYEKPEKSFE IWRTVSSQNK QPINKQKMTY H NFKKIEKI ...String:
MFEVPITLTN RKFAQRRKLK YQYINYISRR FDRISKKSTT TDSLPTPENS AAENNDEEEG QNSEAGTYRR SVLQQKKRRR ERHWRSVVG EIYSTTESET DSQEEETEEG GEHDTGIDKE DSDEERKFWK KYEKPEKSFE IWRTVSSQNK QPINKQKMTY H NFKKIEKI PLRKMEIPLL HCTKENKLYF QSISRGLEPL KTSTSEVRNY RTRHIVTLTD LLHLNVSRHN WSLAYKIFAT LI RIPGVQI KSLWGIGVEI LDNLSNSSSG LDFLQWMCQI YSSKSRFVQN INYRSIVPPF QTGSRTHTAK FAITYLWSSL INC QKSMEP SSNIIDKPFD TENDLLQELI DKISEWVLTP PFMEDAEVWF IYASCHLLKA DTLSRQFVND NKNNDLIGLD RDIK INQVI KHIHYVRTFL KICLDKGGFA VPSRLIENQL KSFESRLYGE AQDIQERDVA NVYDSIDNSS VENSFGDVYE TNAEF LDTQ LMDLSPEDNG LDEMHYSDED SSE

UniProtKB: RNA polymerase I-specific transcription initiation factor RRN11

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Macromolecule #19: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 19 / Number of copies: 8 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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Macromolecule #20: SULFATE ION

MacromoleculeName: SULFATE ION / type: ligand / ID: 20 / Number of copies: 5 / Formula: SO4
Molecular weightTheoretical: 96.063 Da
Chemical component information

ChemComp-SO4:
SULFATE ION

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Macromolecule #21: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 21 / 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

Concentration0.1 mg/mL
BufferpH: 7.8
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 298 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 40.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: PDB ENTRY
Final reconstructionResolution.type: BY AUTHOR / Resolution: 7.7 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 8317
Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: ANGULAR RECONSTITUTION

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Atomic model buiding 1

RefinementProtocol: RIGID BODY FIT
Output model

PDB-5n5y:
Cryo-EM structure of RNA polymerase I in complex with Rrn3 and Core Factor (Orientation III)

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