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- EMDB-10544: early intermediate RNA Polymerase I Pre-initiation complex - eiPIC -

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Basic information

Entry
Database: EMDB / ID: EMD-10544
Titleearly intermediate RNA Polymerase I Pre-initiation complex - eiPIC
Map dataeiPIC reconstruction postprocessed
Sample
  • Complex: early intermediate RNA-Polymerase I Pre-initiation Complex - eiPIC
    • Complex: RNA polymerase
      • Protein or peptide: x 14 types
    • Complex: transcription initiation factor
      • Protein or peptide: x 4 types
    • Complex: DNA
      • DNA: x 4 types
  • Ligand: x 2 types
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 promoter sequence-specific DNA binding / RNA polymerase I core binding / rDNA binding / RNA polymerase I general transcription initiation factor binding / RNA polymerase I general transcription initiation factor activity / RNA polymerase III activity / RNA polymerase I preinitiation complex assembly / RNA Polymerase I Transcription Initiation ...RNA polymerase I transcription regulatory region sequence-specific DNA binding / RNA polymerase I core factor complex / RNA polymerase I core promoter sequence-specific DNA binding / RNA polymerase I core binding / rDNA binding / RNA polymerase I general transcription initiation factor binding / RNA polymerase I general transcription initiation factor activity / RNA polymerase III activity / 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 / regulation of cell size / 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-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 / transcription by RNA polymerase I / RNA polymerase I complex / RNA polymerase III complex / transcription by RNA polymerase III / RNA polymerase II, core complex / TBP-class protein binding / transcription elongation by RNA polymerase II / promoter-specific chromatin binding / transcription initiation at RNA polymerase II promoter / ribonucleoside binding / DNA-directed RNA polymerase / peroxisome / ribosome biogenesis / RNA polymerase II-specific DNA-binding transcription factor binding / transcription by RNA polymerase II / nucleic acid binding / protein dimerization activity / nucleolus / negative regulation of transcription by RNA polymerase II / 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 Rrn11 ...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 / RNA polymerase I, subunit Rpa14, fungi / Yeast RNA polymerase I subunit RPA14 / DNA-directed RNA polymerase I, subunit RPA34.5 / DNA-directed RNA polymerase I subunit RPA34.5 / RNA polymerase I associated factor, A49-like / A49-like RNA polymerase I associated factor / Rpa43, N-terminal ribonucleoprotein (RNP) domain / 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 / Pol I subunit A12, C-terminal zinc ribbon / : / 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 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 / 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 / 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 / DNA-directed RNA polymerase subunit Rpo5/Rpb5 / 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 / 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. / Zinc finger, TFIIS-type / Transcription factor S-II (TFIIS) / Zinc finger TFIIS-type profile. / C2C2 Zinc finger / RNA polymerase Rpb6 / RNA polymerase, subunit omega/Rpo6/RPB6 / RNA polymerase Rpb6 / RNA polymerase Rpb1, domain 3 superfamily / RNA polymerase Rpb1, clamp domain superfamily / RPB6/omega subunit-like superfamily / DNA-directed RNA polymerase, subunit beta-prime / RNA polymerase Rpb1, domain 3 / RNA polymerase Rpb1, domain 3 / RNA polymerase Rpb2, domain 2 superfamily / RNA polymerase Rpb1, domain 1 / RNA polymerase Rpb1, domain 1 / RNA polymerase, alpha subunit / RNA polymerase Rpb1, domain 4 / RNA polymerase Rpb1, domain 2
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) / Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast) / Synthetic construct (others) / Baker's yeast (brewer's yeast)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.54 Å
AuthorsPilsl M / Engel C
Funding support Germany, 2 items
OrganizationGrant numberCountry
German Research Foundation (DFG)EN 1204/1-1 Germany
German Research Foundation (DFG)CRC 960 Germany
CitationJournal: Nat Commun / Year: 2020
Title: Structural basis of RNA polymerase I pre-initiation complex formation and promoter melting.
Authors: Michael Pilsl / Christoph Engel /
Abstract: Transcription of the ribosomal RNA precursor by RNA polymerase (Pol) I is a prerequisite for the biosynthesis of ribosomes in eukaryotes. Compared to Pols II and III, the mechanisms underlying ...Transcription of the ribosomal RNA precursor by RNA polymerase (Pol) I is a prerequisite for the biosynthesis of ribosomes in eukaryotes. Compared to Pols II and III, the mechanisms underlying promoter recognition, initiation complex formation and DNA melting by Pol I substantially diverge. Here, we report the high-resolution cryo-EM reconstruction of a Pol I early initiation intermediate assembled on a double-stranded promoter scaffold that prevents the establishment of downstream DNA contacts. Our analyses demonstrate how efficient promoter-backbone interaction is achieved by combined re-arrangements of flexible regions in the 'core factor' subunits Rrn7 and Rrn11. Furthermore, structure-function analysis illustrates how destabilization of the melted DNA region correlates with contraction of the polymerase cleft upon transcription activation, thereby combining promoter recruitment with DNA-melting. This suggests that molecular mechanisms and structural features of Pol I initiation have co-evolved to support the efficient melting, initial transcription and promoter clearance required for high-level rRNA synthesis.
History
DepositionDec 14, 2019-
Header (metadata) releaseMar 18, 2020-
Map releaseMar 18, 2020-
UpdateDec 2, 2020-
Current statusDec 2, 2020Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.015
  • Imaged by UCSF Chimera
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  • Surface view colored by radius
  • Surface level: 0.015
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6tps
  • Surface level: 0.015
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

Downloads & links

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Map

FileDownload / File: emd_10544.map.gz / Format: CCP4 / Size: 282.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationeiPIC reconstruction postprocessed
Voxel sizeX=Y=Z: 1.09 Å
Density
Contour LevelBy AUTHOR: 0.015 / Movie #1: 0.015
Minimum - Maximum-0.051139303 - 0.09600031
Average (Standard dev.)0.0000035937 (±0.002695401)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions420420420
Spacing420420420
CellA=B=C: 457.80002 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.091.091.09
M x/y/z420420420
origin x/y/z0.0000.0000.000
length x/y/z457.800457.800457.800
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS420420420
D min/max/mean-0.0510.0960.000

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Supplemental data

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Additional map: focused CF refinement postporocessed

Fileemd_10544_additional.map
Annotationfocused CF refinement postporocessed
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Sample components

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Entire : early intermediate RNA-Polymerase I Pre-initiation Complex - eiPIC

EntireName: early intermediate RNA-Polymerase I Pre-initiation Complex - eiPIC
Components
  • Complex: early intermediate RNA-Polymerase I Pre-initiation Complex - eiPIC
    • Complex: RNA polymerase
      • Protein or peptide: DNA-directed RNA polymerase I subunit RPA190Polymerase
      • Protein or peptide: DNA-directed RNA polymerase I subunit RPA135Polymerase
      • Protein or peptide: DNA-directed RNA polymerases I and III subunit RPAC1
      • Protein or peptide: DNA-directed RNA polymerase I subunit RPA14Polymerase
      • 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 I subunit RPA43Polymerase
      • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC3RNA polymerase
      • Protein or peptide: DNA-directed RNA polymerase I subunit RPA12Polymerase
      • 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 I subunit RPA49Polymerase
      • Protein or peptide: DNA-directed RNA polymerase I subunit RPA34Polymerase
    • Complex: transcription initiation factor
      • Protein or peptide: RNA polymerase I-specific transcription initiation factor RRN3
      • 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
    • Complex: DNA
      • DNA: NTS-DNA (27-MER)
      • DNA: TS-DNA (27-MER)
      • DNA: DNA foreign
      • DNA: DNA foreign
  • Ligand: ZINC ION
  • Ligand: MAGNESIUM ION

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Supramolecule #1: early intermediate RNA-Polymerase I Pre-initiation Complex - eiPIC

SupramoleculeName: early intermediate RNA-Polymerase I Pre-initiation Complex - eiPIC
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#22

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Supramolecule #2: RNA polymerase

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

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Supramolecule #3: transcription initiation factor

SupramoleculeName: transcription initiation factor / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #15-#18
Source (natural)Organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (yeast)
Recombinant expressionOrganism: Escherichia coli (E. coli)

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Supramolecule #4: DNA

SupramoleculeName: DNA / type: complex / ID: 4 / Parent: 1 / Macromolecule list: #19-#22
Source (natural)Organism: Synthetic construct (others)
Recombinant expressionOrganism: Synthetic construct (others)

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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 / Details: (.ZN)(.ZN)(.MG) / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA-directed RNA polymerase
Source (natural)Organism: Baker's yeast (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

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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: Baker's yeast (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

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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)
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 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: Baker's yeast (brewer's yeast)
Molecular weightTheoretical: 14.599128 KDa
SequenceString:
MMKGSRRTGN NTATTLNTPV VIHATQLPQH VSTDEVLQFL ESFIDEKENI IDSTTMNTIS GNAADADAAA VANTSLNIDT NLSSSISQL KRIQRDFKGL PPAQDFSAAP IQVSTTEKKE TSIGVSATGG KKTTFADE

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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)
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)
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 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: Baker's yeast (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

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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)
Molecular weightTheoretical: 16.525363 KDa
SequenceString:
MSNTLFDDIF QVSEVDPGRY NKVCRIEAAS TTQDQCKLTL DINVELFPVA AQDSLTVTIA SSLNLEDTPA NDSSATRSWR PPQAGDRSL ADDYDYVMYG TAYKFEEVSK DLIAVYYSFG GLLMRLEGNY RNLNNLKQEN AYLLIRR

+
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: Baker's yeast (brewer's yeast)
Molecular weightTheoretical: 13.676566 KDa
SequenceString:
MSVVGSLIFC LDCGDLLENP NAVLGSNVEC SQCKAIYPKS QFSNLKVVTT TADDAFPSSL RAKKSVVKTS LKKNELKDGA TIKEKCPQC GNEEMNYHTL QLRSADEGAT VFYTCTSCGY KFRTNN

+
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)
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)
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)
Molecular weightTheoretical: 7.729969 KDa
SequenceString:
MSREGFQIPT NLDAAAAGTS QARTATLKYI CAECSSKLSL SRTDAVRCKD CGHRILLKAR TKRLVQFEAR

+
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: Baker's yeast (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

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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: Baker's yeast (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

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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 (strain ATCC 204508 / S288c) (yeast)
Molecular weightTheoretical: 72.458258 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
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

+
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 (strain ATCC 204508 / S288c) (yeast)
Molecular weightTheoretical: 73.523516 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: RPVDDTLAED ALDLHIVVKS LLCDTQDAFF WDPTVANRLD SQYIQTASDL RNYRDGTEII AYASGKTGSV LNIAVLTRQN TLHLNRHNN VTSIELHSPI KSIKIPGASE SIGRRSNLVG IITENSFQIF RIESVHSRSC DVMVSSSEPL YFVEIDDLQV V DFAFNPWD ...String:
RPVDDTLAED ALDLHIVVKS LLCDTQDAFF WDPTVANRLD SQYIQTASDL RNYRDGTEII AYASGKTGSV LNIAVLTRQN TLHLNRHNN VTSIELHSPI KSIKIPGASE SIGRRSNLVG IITENSFQIF RIESVHSRSC DVMVSSSEPL YFVEIDDLQV V DFAFNPWD LQQFAIIDIK GNWSIGRIPK NFNNNNKRKL QLIDNLHGTI FDPEELSSWK RIEWFSHFQK ILVFDRSKMI EI DFMNNWQ TEVVQAKAWS NIRDYKRIDD KNGILLTSRE IIIVGASESN DPVRRISWKH DLDPDDTTLR ITVQKVKKPD HIL LVAFVY SMRHKRIYMH VFSHRKANLF QSLGCSTVLE IPGGTPTGIE TILTLDHIDD ESRREEDADE NFELVVDFLV KLRN SSEVY YYALSNTQNS EPNKQETPII VDHPEWASLF NNADEREKES IGALVSQIKL KERERISRVQ NLIEHENSHD EDKYL QDLG YRLSIATNEL LESWQKTKDE SILSGSLSHS KLKNLLENSD SFASIPEFSS LLDQFFQYYQ DQDVTFIGFE KLLHLF LHE DVPGLDIFYN KLLQCWVLVS PQAELLTKEI VKDIIWSLAR LEKPSLFEPI QNEISRSLSG PYQDIISSWD MDD

+
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 (strain ATCC 204508 / S288c) (yeast)
Molecular weightTheoretical: 60.435195 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
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

+
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 (strain ATCC 204508 / S288c) (yeast)
Molecular weightTheoretical: 59.334262 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
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

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Macromolecule #19: NTS-DNA (27-MER)

MacromoleculeName: NTS-DNA (27-MER) / type: dna / ID: 19 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: Synthetic construct (others)
Molecular weightTheoretical: 8.411627 KDa
SequenceString:
(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA) (DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA)(DA) (DA)(DA)(DA)(DA)(DA)(DA)(DA)

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Macromolecule #20: TS-DNA (27-MER)

MacromoleculeName: TS-DNA (27-MER) / type: dna / ID: 20 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: Synthetic construct (others)
Molecular weightTheoretical: 8.153236 KDa
SequenceString:
(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT) (DT)(DC)(DT)(DT)(DT)(DT)(DT)(DT)(DT)(DT) (DT)(DT)(DT)(DT)(DT)(DT)(DT)

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Macromolecule #21: DNA foreign

MacromoleculeName: DNA foreign / type: dna / ID: 21 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: Synthetic construct (others)
Molecular weightTheoretical: 3.905512 KDa
SequenceString:
(DG)(DG)(DG)(DG)(DG)(DG)(DG)(DG)(DG)(DG) (DG)(DG)

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Macromolecule #22: DNA foreign

MacromoleculeName: DNA foreign / type: dna / ID: 22 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: Synthetic construct (others)
Molecular weightTheoretical: 3.425224 KDa
SequenceString:
(DC)(DC)(DC)(DC)(DC)(DC)(DC)(DC)(DC)(DC) (DC)(DC)

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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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Macromolecule #24: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 24 / 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 / Component - Formula: KCl
GridModel: Quantifoil R2/1 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: CONTINUOUS / Support film - Film thickness: 0.2 nm / Pretreatment - Type: PLASMA CLEANING / Pretreatment - Atmosphere: OTHER
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 0.01 mm / Nominal defocus max: 3.5 µm / Nominal defocus min: 1.5 µm / Nominal magnification: 105000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Number grids imaged: 1 / Number real images: 4088 / Average electron dose: 1.4 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionSoftware - Name: RELION / Software - details: 3
Startup modelType of model: NONE / Details: Initial model generated from 2D classes
Initial angle assignmentType: ANGULAR RECONSTITUTION / Software - Name: RELION / Software - details: 3
Final angle assignmentType: ANGULAR RECONSTITUTION / Software - Name: RELION / Software - details: 3
Final reconstructionNumber classes used: 1 / Applied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.54 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 3.08) / Number images used: 122099

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