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- EMDB-15127: Structure of mammalian Pol II-DSIF-SPT6-PAF1-TFIIS-hexasome elong... -

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Basic information

Entry
Database: EMDB / ID: EMD-15127
TitleStructure of mammalian Pol II-DSIF-SPT6-PAF1-TFIIS-hexasome elongation complex
Map data
Sample
  • Complex: Mammalian Pol II-TFIIS elongation complex
    • Protein or peptide: x 23 types
    • DNA: x 1 types
    • RNA: x 1 types
  • Protein or peptide: x 1 types
  • DNA: x 1 types
  • Ligand: x 2 types
Keywordschromatin / rna polymerase II / nucleosome / TFIIS / transcription / elongation
Function / homology
Function and homology information


blastocyst growth / positive regulation of mRNA 3'-end processing / Ski complex / RNA polymerase II C-terminal domain phosphoserine binding / mRNA decay by 3' to 5' exoribonuclease / Cdc73/Paf1 complex / negative regulation of DNA-templated transcription, elongation / inner cell mass cell differentiation / nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay / endodermal cell fate commitment ...blastocyst growth / positive regulation of mRNA 3'-end processing / Ski complex / RNA polymerase II C-terminal domain phosphoserine binding / mRNA decay by 3' to 5' exoribonuclease / Cdc73/Paf1 complex / negative regulation of DNA-templated transcription, elongation / inner cell mass cell differentiation / nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay / endodermal cell fate commitment / negative regulation of myeloid cell differentiation / DSIF complex / positive regulation of cell cycle G1/S phase transition / trophectodermal cell differentiation / blastocyst hatching / regulation of transcription elongation by RNA polymerase II / Formation of RNA Pol II elongation complex / Formation of the Early Elongation Complex / Transcriptional regulation by small RNAs / RNA Polymerase II Pre-transcription Events / TP53 Regulates Transcription of DNA Repair Genes / FGFR2 alternative splicing / RNA polymerase II transcribes snRNA genes / mRNA Capping / mRNA Splicing - Minor Pathway / Processing of Capped Intron-Containing Pre-mRNA / RNA Polymerase II Promoter Escape / RNA Polymerase II Transcription Pre-Initiation And Promoter Opening / RNA Polymerase II Transcription Initiation / RNA Polymerase II Transcription Elongation / RNA Polymerase II Transcription Initiation And Promoter Clearance / RNA Pol II CTD phosphorylation and interaction with CE / Estrogen-dependent gene expression / Formation of TC-NER Pre-Incision Complex / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / mRNA Splicing - Major Pathway / nuclear lumen / mRNA 3'-end processing / positive regulation of DNA-templated transcription, elongation / Abortive elongation of HIV-1 transcript in the absence of Tat / transcription elongation-coupled chromatin remodeling / stem cell population maintenance / interleukin-6-mediated signaling pathway / negative regulation of G1/S transition of mitotic cell cycle / RNA Pol II CTD phosphorylation and interaction with CE during HIV infection / RNA Pol II CTD phosphorylation and interaction with CE / Formation of the Early Elongation Complex / Formation of the HIV-1 Early Elongation Complex / negative regulation of gene expression, epigenetic / mRNA Capping / RNA polymerase II complex binding / negative regulation of transcription elongation by RNA polymerase II / maintenance of transcriptional fidelity during transcription elongation by RNA polymerase II / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / positive regulation of macroautophagy / RNA polymerase II transcribes snRNA genes / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / positive regulation of Wnt signaling pathway / cell surface receptor signaling pathway via JAK-STAT / protein localization to nucleus / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat / transcription by RNA polymerase III / transcription by RNA polymerase I / RNA polymerase I complex / transcription elongation by RNA polymerase I / Formation of HIV elongation complex in the absence of HIV Tat / RNA polymerase III complex / transcription-coupled nucleotide-excision repair / RNA polymerase II, core complex / tRNA transcription by RNA polymerase III / RNA Polymerase II Transcription Elongation / : / negative regulation of fibroblast proliferation / Formation of RNA Pol II elongation complex / translation initiation factor binding / RNA Polymerase II Pre-transcription Events / rescue of stalled ribosome / DNA-directed RNA polymerase activity / DNA-directed RNA polymerase complex / SH2 domain binding / positive regulation of transcription elongation by RNA polymerase II / TP53 Regulates Transcription of DNA Repair Genes / transcription initiation at RNA polymerase II promoter / DNA-templated transcription initiation / regulation of cell growth / transcription elongation by RNA polymerase II / Formation of the beta-catenin:TCF transactivating complex / Hedgehog 'on' state / euchromatin / protein destabilization / ribonucleoside binding / Wnt signaling pathway / : / : / : / fibrillar center
Similarity search - Function
Paf1 complex subunit Cdc73, N-terminal domain / Paf1 complex subunit CDC73 N-terminal / Leo1-like protein / Leo1-like protein / Plus-3 domain / Plus3-like superfamily / Plus-3 domain / Plus3 domain profile. / Short conserved domain in transcriptional regulators. / RNA polymerase II associated factor Paf1 ...Paf1 complex subunit Cdc73, N-terminal domain / Paf1 complex subunit CDC73 N-terminal / Leo1-like protein / Leo1-like protein / Plus-3 domain / Plus3-like superfamily / Plus-3 domain / Plus3 domain profile. / Short conserved domain in transcriptional regulators. / RNA polymerase II associated factor Paf1 / Paf1 / Cdc73/Parafibromin / RNA polymerase-associated protein Ctr9 / Cell division control protein 73, C-terminal / Cell division control protein 73, C-terminal domain superfamily / RNA pol II accessory factor, Cdc73 family, C-terminal / : / Spt5, KOW domain repeat 6 / Transcription elongation factor SPT5, seventh KOW domain / Transcription elongation factor SPT5, sixth KOW domain / Tetratricopeptide repeat / Transcription initiation Spt4 / Spt4 superfamily / Spt4/RpoE2 zinc finger / Spt4/RpoE2 zinc finger / Spt4/RpoE2 zinc finger / Transcription elongation factor SPT5, KOWx domain / Transcription elongation factor SPT5, KOW1 domain / Transcription elongation factor SPT5, second KOW domain / Transcription elongation factor SPT5, fifth KOW domain / Transcription elongation factor SPT5, fourth KOW domain / Transcription elongation factor Spt5, eukaryote / Spt5 transcription elongation factor, N-terminal / Spt5, KOW domain repeat 2 / Spt5, KOW domain repeat 3 / Spt5, KOW domain repeat 5 / Spt5 transcription elongation factor, acidic N-terminal / NGN domain, eukaryotic / Spt5, KOW domain repeat 1 / Spt5, KOW domain repeat 4 / Spt5 C-terminal domain / Spt5 C-terminal nonapeptide repeat binding Spt4 / NGN domain / Transcription elongation factor SPT5 / Early transcription elongation factor of RNA pol II, NGN section / Tetratricopeptide repeat / NusG, N-terminal / In Spt5p, this domain may confer affinity for Spt4p. It possesses a RNP-like fold. / NusG, N-terminal domain superfamily / DNA-directed RNA polymerase II subunit Rpb4-like / Tetratricopeptide repeat / RNA polymerase Rpb1 C-terminal repeat / RNA polymerase II, heptapeptide repeat, eukaryotic / Eukaryotic RNA polymerase II heptapeptide repeat. / RNA polymerase Rpb1, domain 6 / RNA polymerase Rpb1, domain 6 / RNA polymerase Rpb4/RPC9, core / DNA-directed RNA-polymerase II subunit / RNA polymerase Rpb1, domain 7 / RNA polymerase Rpb1, domain 7 superfamily / RNA polymerase Rpb1, domain 7 / Pol II subunit B9, C-terminal zinc ribbon / RNA polymerase RBP11 / Rpb4/RPC9 superfamily / RNA polymerase subunit Rpb4/RPC9 / RNA polymerase Rpb4 / Zinc finger TFIIS-type signature. / HRDC-like superfamily / RNA polymerase Rpb7-like , N-terminal / RNA polymerase Rpb7-like, N-terminal domain superfamily / RNA polymerase subunit Rpb7-like / SHS2 domain found in N terminus of Rpb7p/Rpc25p/MJ0397 / RNA polymerase Rpb2, domain 5 / RNA polymerase Rpb2, domain 5 / RNA polymerase Rpb2, domain 4 / RNA polymerase Rpb2, domain 4 / DNA-directed RNA polymerase, M/15kDa subunit / RNA polymerases M/15 Kd subunit / RNA polymerase subunit 9 / DNA-directed RNA polymerase M, 15kDa subunit, conserved site / RNA polymerases M / 15 Kd subunits signature. / DNA-directed RNA polymerase subunit/transcription factor S / : / RNA polymerase, Rpb8 / DNA-directed RNA polymerases I, II, and III subunit RPABC4 / RNA polymerase Rpb8 / RNA polymerase subunit 8 / RNA polymerase, Rpb5, N-terminal / RNA polymerase Rpb5, N-terminal domain superfamily / RNA polymerase Rpb5, N-terminal domain / DNA-directed RNA polymerase, subunit RPB6 / DNA-directed RNA polymerase subunit RPABC5/Rpb10 / RNA polymerases, subunit N, zinc binding site / RNA polymerase subunit RPB10 / 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.
Similarity search - Domain/homology
RNA polymerase II subunit D / DNA-directed RNA polymerase subunit / DNA-directed RNA polymerases I, II, and III subunit RPABC5 / DNA-directed RNA polymerase subunit / RNA polymerase II subunit K / DNA-directed RNA polymerases I, II, and III subunit RPABC2 / Histone H2B / DNA-directed RNA polymerase II subunit RPB11-a / DNA-directed RNA polymerases I, II, and III subunit RPABC3 / DNA-directed RNA polymerase II subunit RPB3 ...RNA polymerase II subunit D / DNA-directed RNA polymerase subunit / DNA-directed RNA polymerases I, II, and III subunit RPABC5 / DNA-directed RNA polymerase subunit / RNA polymerase II subunit K / DNA-directed RNA polymerases I, II, and III subunit RPABC2 / Histone H2B / DNA-directed RNA polymerase II subunit RPB11-a / DNA-directed RNA polymerases I, II, and III subunit RPABC3 / DNA-directed RNA polymerase II subunit RPB3 / DNA-directed RNA polymerase subunit beta / DNA-directed RNA polymerase II subunit E / Transcription elongation factor SPT5 / DNA-directed RNA polymerase II subunit RPB9 / Histone H4 / Histone H3.2 / Transcription elongation factor SPT4 / Histone H2A / Parafibromin / RNA polymerase-associated protein CTR9 homolog / RNA polymerase II-associated factor 1 homolog / RNA polymerase-associated protein LEO1 / RNA polymerase-associated protein RTF1 homolog / Superkiller complex protein 8
Similarity search - Component
Biological speciesSus scrofa (pig) / Homo sapiens (human) / Xenopus laevis (African clawed frog) / synthetic construct (others)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.3 Å
AuthorsFarnung L / Ochmann M / Garg G / Vos SM / Cramer P
Funding supportEuropean Union, Germany, 3 items
OrganizationGrant numberCountry
European Research Council (ERC)693023European Union
German Research Foundation (DFG)SFB860 Germany
German Research Foundation (DFG)EXC 2067/1-390729940 Germany
CitationJournal: Mol Cell / Year: 2022
Title: Structure of a backtracked hexasomal intermediate of nucleosome transcription.
Authors: Lucas Farnung / Moritz Ochmann / Gaurika Garg / Seychelle M Vos / Patrick Cramer /
Abstract: During gene transcription, RNA polymerase II (RNA Pol II) passes nucleosomes with the help of various elongation factors. Here, we show that RNA Pol II achieves efficient nucleosome passage when the ...During gene transcription, RNA polymerase II (RNA Pol II) passes nucleosomes with the help of various elongation factors. Here, we show that RNA Pol II achieves efficient nucleosome passage when the human elongation factors DSIF, PAF1 complex (PAF), RTF1, SPT6, and TFIIS are present. The cryo-EM structure of an intermediate of the nucleosome passage shows a partially unraveled hexasome that lacks the proximal H2A-H2B dimer and interacts with the RNA Pol II jaw, DSIF, and the CTR9trestle helix. RNA Pol II adopts a backtracked state with the RNA 3' end dislodged from the active site and bound in the RNA Pol II pore. Additional structures and biochemical data show that human TFIIS enters the RNA Pol II pore and stimulates the cleavage of the backtracked RNA and nucleosome passage.
History
DepositionJun 9, 2022-
Header (metadata) releaseJul 31, 2024-
Map releaseJul 31, 2024-
UpdateNov 6, 2024-
Current statusNov 6, 2024Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_15127.png

Downloads & links

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Map

FileDownload / File: emd_15127.map.gz / Format: CCP4 / Size: 178 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

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AxesZ (Sec.)Y (Row.)X (Col.)
1.05 Å/pix.
x 360 pix.
= 378. Å		1.05 Å/pix.
x 360 pix.
= 378. Å		1.05 Å/pix.
x 360 pix.
= 378. Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.05 Å
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Histogram (log scale)
Contour LevelBy AUTHOR: 0.004
Minimum - Maximum-0.03599395 - 0.082023665
Average (Standard dev.)-0.00004320549 (±0.0021754515)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions360360360
Spacing360360360
CellA=B=C: 377.99997 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: Overall

Fileemd_15127_half_map_1.map
AnnotationOverall
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Half map: Overall

Fileemd_15127_half_map_2.map
AnnotationOverall
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Sample components

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Entire : Mammalian Pol II-TFIIS elongation complex

EntireName: Mammalian Pol II-TFIIS elongation complex
Components
  • Complex: Mammalian Pol II-TFIIS elongation complex
    • Protein or peptide: DNA-directed RNA polymerase subunit
    • Protein or peptide: DNA-directed RNA polymerase subunit beta
    • Protein or peptide: DNA-directed RNA polymerase II subunit RPB3
    • Protein or peptide: RNA polymerase II subunit D
    • Protein or peptide: DNA-directed RNA polymerase II subunit E
    • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC2
    • Protein or peptide: DNA-directed RNA polymerase II subunit RPB7
    • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC3
    • Protein or peptide: DNA-directed RNA polymerase II subunit RPB9
    • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC5
    • Protein or peptide: DNA-directed RNA polymerase II subunit RPB11-a
    • Protein or peptide: RNA polymerase II subunit K
    • Protein or peptide: SPT6
    • DNA: Non-template DNA
    • RNA: RNA, Template DNA
    • Protein or peptide: RNA polymerase-associated protein CTR9 homolog,RNA polymerase-associated protein LEO1
    • Protein or peptide: RNA polymerase-associated protein RTF1 homolog
    • Protein or peptide: WD repeat-containing protein 61
    • Protein or peptide: Parafibromin
    • Protein or peptide: Transcription elongation factor SPT4
    • Protein or peptide: Transcription elongation factor SPT5
    • Protein or peptide: Histone H3.2
    • Protein or peptide: Histone H4
    • Protein or peptide: Histone H2A
    • Protein or peptide: Histone H2B
  • Protein or peptide: RNA polymerase II-associated factor 1 homolog
  • DNA: RNA, Template DNA
  • Ligand: ZINC ION
  • Ligand: MAGNESIUM ION

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Supramolecule #1: Mammalian Pol II-TFIIS elongation complex

SupramoleculeName: Mammalian Pol II-TFIIS elongation complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#17, #20-#27
Source (natural)Organism: Sus scrofa (pig)

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Macromolecule #1: DNA-directed RNA polymerase subunit

MacromoleculeName: DNA-directed RNA polymerase subunit / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 219.0495 KDa
SequenceString: MHGGGPPSGD SACPLRTIKR VQFGVLSPDE LKRMSVTEGG IKYPETTEGG RPKLGGLMDP RQGVIERTGR CQTCAGNMTE CPGHFGHIE LAKPVFHVGF LVKTMKVLRC VCFFCSKLLV DSNNPKIKDI LAKSKGQPKK RLTHVYDLCK GKNICEGGEE M DNKFGVEQ ...String:
MHGGGPPSGD SACPLRTIKR VQFGVLSPDE LKRMSVTEGG IKYPETTEGG RPKLGGLMDP RQGVIERTGR CQTCAGNMTE CPGHFGHIE LAKPVFHVGF LVKTMKVLRC VCFFCSKLLV DSNNPKIKDI LAKSKGQPKK RLTHVYDLCK GKNICEGGEE M DNKFGVEQ PEGDEDLTKE KGHGGCGRYQ PRIRRSGLEL YAEWKHVNED SQEKKILLSP ERVHEIFKRI SDEECFVLGM EP RYARPEW MIVTVLPVPP LSVRPAVVMQ GSARNQDDLT HKLADIVKIN NQLRRNEQNG AAAHVIAEDV KLLQFHVATM VDN ELPGLP RAMQKSGRPL KSLKQRLKGK EGRVRGNLMG KRVDFSARTV ITPDPNLSID QVGVPRSIAA NMTFAEIVTP FNID RLQEL VRRGNSQYPG AKYIIRDNGD RIDLRFHPKP SDLHLQTGYK VERHMCDGDI VIFNRQPTLH KMSMMGHRVR ILPWS TFRL NLSVTTPYNA DFDGDEMNLH LPQSLETRAE IQELAMVPRM IVTPQSNRPV MGIVQDTLTA VRKFTKRDVF LERGEV MNL LMFLSTWDGK VPQPAILKPR PLWTGKQIFS LIIPGHINCI RTHSTHPDDE DSGPYKHISP GDTKVVVENG ELIMGIL CK KSLGTSAGSL VHISYLEMGH DITRLFYSNI QTVINNWLLI EGHTIGIGDS IADSKTYQDI QNTIKKAKQD VIEVIEKA H NNELEPTPGN TLRQTFENQV NRILNDARDK TGSSAQKSLS EYNNFKSMVV SGAKGSKINI SQVIAVVGQQ NVEGKRIPF GFKHRTLPHF IKDDYGPESR GFVENSYLAG LTPTEFFFHA MGGREGLIDT AVKTAETGYI QRRLIKSMES VMVKYDATVR NSINQVVQL RYGEDGLAGE SVEFQNLATL KPSNKAFEKK FRFDYTNERA LRRTLQEDLV KDVLSNAHIQ NELEREFERM R EDREVLRV IFPTGDSKVV LPCNLLRMIW NAQKIFHINP RLPSDLHPIK VVEGVKELSK KLVIVNGDDP LSRQAQENAT LL FNIHLRS TLCSRRMAEE FRLSGEAFDW LLGEIESKFN QAIAHPGEMV GALAAQSLGE PATQMTLNTF HYAGVSAKNV TLG VPRLKE LINISKKPKT PSLTVFLLGQ SARDAERAKD ILCRLEHTTL RKVTANTAIY YDPNPQSTVV AEDQEWVNVY YEMP DFDVA RISPWLLRVE LDRKHMTDRK LTMEQIAEKI NAGFGDDLNC IFNDDNAEKL VLRIRIMNSD ENKMQEEEEV VDKMD DDVF LRCIESNMLT DMTLQGIEQI SKVYMHLPQT DNKKKIIITE DGEFKALQEW ILETDGVSLM RVLSEKDVDP VRTTSN DIV EIFTVLGIEA VRKALERELY HVISFDGSYV NYRHLALLCD TMTCRGHLMA ITRHGVNRQD TGPLMKCSFE ETVDVLM EA AAHGESDPMK GVSENIMLGQ LAPAGTGCFD LLLDAEKCKY GMEIPTNIPG LGAAGPTGMF FGSAPSPMGG ISPAMTPW N QGA(TPO)PAYGAW SPSVGSGMTP GAAGF(SEP)PSAA SDASGFSPGY SPAWSPTPGS PGSPGPSSPY IPSPGGAMSP S YSPTSPAY EPRSPGGYTP QSPSYSPTSP SYSPTSPSYS PTSPNYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YS PTSPSYS PTSPSYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP TSPSYSPTSP SYSPTSPSYS PTS PSYSPT SPNYSPTSPN YTPTSPSYSP TSPSYSPTSP NYTPTSPNYS PTSPSYSPTS PSYSPTSPSY SPSSPRYTPQ SPTY TPSSP SYSPSSPSYS PTSPKYTPTS PSYSPSSPEY TPTSPKYSPT SPKYSPTSPK YSPTSPTYSP TTPKYSPTSP TYSPT SPVY TPTSPKYSPT SPTYSPTSPK YSPTSPTYSP TSPKGSTYSP TSPGYSPTSP TYSLTSPAIS PDDSDEEN

UniProtKB: DNA-directed RNA polymerase subunit

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Macromolecule #2: DNA-directed RNA polymerase subunit beta

MacromoleculeName: DNA-directed RNA polymerase subunit beta / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA-directed RNA polymerase
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 142.426125 KDa
SequenceString: MCSTNLSQAL AYFRAGANLT AASLWAGFRG SRRIFWERRK RKSLCLALRP GGACWRWLLA VSCVSLRGLG APGSCANMYD ADEDMQYDE DDDEITPDLW QEACWIVISS YFDEKGLVRQ QLDSFDEFIQ MSVQRIVEDA PPIDLQAEAQ HASGEVEEPP R YLLKFEQI ...String:
MCSTNLSQAL AYFRAGANLT AASLWAGFRG SRRIFWERRK RKSLCLALRP GGACWRWLLA VSCVSLRGLG APGSCANMYD ADEDMQYDE DDDEITPDLW QEACWIVISS YFDEKGLVRQ QLDSFDEFIQ MSVQRIVEDA PPIDLQAEAQ HASGEVEEPP R YLLKFEQI YLSKPTHWER DGAPSPMMPN EARLRNLTYS APLYVDITKT VIKEGEEQLQ TQHQKTFIGK IPIMLRSTYC LL NGLTDRD LCELNECPLD PGGYFIINGS EKVLIAQEKM ATNTVYVFAK KDSKYAYTGE CRSCLENSSR PTSTIWVSML ARG GQGAKK SAIGQRIVAT LPYIKQEVPI IIVFRALGFV SDRDILEHII YDFEDPEMME MVKPSLDEAF VIQEQNVALN FIGS RGAKP GVTKEKRIKY AKEVLQKEML PHVGVSDFCE TKKAYFLGYM VHRLLLAALG RRELDDRDHY GNKRLDLAGP LLAFL FRGM FKNLLKEVRI YAQKFIDRGK DFNLELAIKT RIISDGLKYS LATGNWGDQK KAHQARAGVS QVLNRLTFAS TLSHLR RLN SPIGRDGKLA KPRQLHNTLW GMVCPAETPE GHAVGLVKNL ALMAYISVGS QPSPILEFLE EWSMENLEEI SPAAIAD AT KIFVNGCWVG IHKDPEQLMN TLRKLRRQMD IIVSEVSMIR DIREREIRIY TDAGRICRPL LIVEKQKLLL KKRHIDQL K EREYNNYSWQ DLVASGVVEY IDTLEEETVM LAMTPDDLQE KEVAYCSTYT HCEIHPSMIL GVCASIIPFP DHNQSPRNT YQSAMGKQAM GVYITNFHVR MDTLAHVLYY PQKPLVTTRS MEYLRFRELP AGINSIVAIA SYTGYNQEDS VIMNRSAVDR GFFRSVFYR SYKEQESKKG FDQEEVFEKP TRETCQGMRH AIYDKLDDDG LIAPGVRVSG DDVIIGKTVT LPENEDELEG T NRRYTKRD CSTFLRTSET GIVDQVMVTL NQEGYKFCKI RVRSVRIPQI GDKFASRHGQ KGTCGIQYRQ EDMPFTCEGI TP DIIINPH AIPSRMTIGH LIECLQGKVS ANKGEIGDAT PFNDAVNVQK ISNLLSDYGY HLRGNEVLYN GFTGRKITSQ IFI GPTYYQ RLKHMVDDKI HSRARGPIQI LNRQPMEGRS RDGGLRFGEM ERDCQIAHGA AQFLRERLFE ASDPYQVHVC NLCG IMAIA NTRTHTYECR GCRNKTQISL VRMPYACKLL FQELMSMSIA PRMMSV

UniProtKB: DNA-directed RNA polymerase subunit beta

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Macromolecule #3: DNA-directed RNA polymerase II subunit RPB3

MacromoleculeName: DNA-directed RNA polymerase II subunit RPB3 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 30.898428 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MPYANQPTVR ITELTDENVK FIIENTDLAV ANSIRRVFIA EVPIIAIDWV QIDANSSVLH DEFIAHRLGL IPLTSDDIVD KLQYSRDCT CEEFCPECSV EFTLDVRCNE DQTRHVTSRD LISNSPRVIP VTSRNRDNDP SDYVEQDDIL IVKLRKGQEL R LRAYAKKG ...String:
MPYANQPTVR ITELTDENVK FIIENTDLAV ANSIRRVFIA EVPIIAIDWV QIDANSSVLH DEFIAHRLGL IPLTSDDIVD KLQYSRDCT CEEFCPECSV EFTLDVRCNE DQTRHVTSRD LISNSPRVIP VTSRNRDNDP SDYVEQDDIL IVKLRKGQEL R LRAYAKKG FGKEHAKWNP TAGVAFEYDP DNALRHTVYP KPEEWPKSEY SELDEDESQA PYDPNGKPER FYYNVESCGS LR PETIVLS ALSGLKKKLS DLQTQLSHEI QSD

UniProtKB: DNA-directed RNA polymerase II subunit RPB3

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Macromolecule #4: RNA polymerase II subunit D

MacromoleculeName: RNA polymerase II subunit D / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 16.331255 KDa
SequenceString:
MAAGGSDPRA GDVEEDASQL IFPKEFETAE TLLNSEVHML LEHRKQQNES AEDEQELSEV FMKTLNYTAR FSRFKNRETI ASVRSLLLQ KKLHKFELAC LANLCPETAE ESKALIPSLE GRFEDEELQQ ILDDIQTKRS FQY

UniProtKB: RNA polymerase II subunit D

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Macromolecule #5: DNA-directed RNA polymerase II subunit E

MacromoleculeName: DNA-directed RNA polymerase II subunit E / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 24.644318 KDa
SequenceString: MDDEEETYRL WKIRKTIMQL CHDRGYLVTQ DELDQTLEEF KAQFGDKPSE GRPRRTDLTV LVAHNDDPTD QMFVFFPEEP KVGIKTIKV YCQRMQEENI TRALIVVQQG MTPSAKQSLV DMAPKYILEQ FLQQELLINI TEHELVPEHV VMTKEEVTEL L ARYKLREN ...String:
MDDEEETYRL WKIRKTIMQL CHDRGYLVTQ DELDQTLEEF KAQFGDKPSE GRPRRTDLTV LVAHNDDPTD QMFVFFPEEP KVGIKTIKV YCQRMQEENI TRALIVVQQG MTPSAKQSLV DMAPKYILEQ FLQQELLINI TEHELVPEHV VMTKEEVTEL L ARYKLREN QLPRIQAGDP VARYFGIKRG QVVKIIRPSE TAGRYITYRL VQ

UniProtKB: DNA-directed RNA polymerase II subunit E

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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: Sus scrofa (pig)
Molecular weightTheoretical: 14.477001 KDa
SequenceString:
MSDNEDNFDG DDFDDVEEDE GLDDLENAEE EGQENVEILP SGERPQANQK RITTPYMTKY ERARVLGTRA LQIAMCAPVM VELEGETDP LLIAMKELKA RKIPIIIRRY LPDGSYEDWG VDELIISD

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

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Macromolecule #7: DNA-directed RNA polymerase II subunit RPB7

MacromoleculeName: DNA-directed RNA polymerase II subunit RPB7 / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 19.314283 KDa
SequenceString:
MFYHISLEHE ILLHPRYFGP NLLNTVKQKL FTEVEGTCTG KYGFVIAVTT IDNIGAGVIQ PGRGFVLYPV KYKAIVFRPF KGEVVDAVV TQVNKVGLFT EIGPMSCFIS RHSIPSEMEF DPNSNPPCYK TMDEDIVIQQ DDEIRLKIVG TRVDKNDIFA I GSLMDDYL GLVS

UniProtKB: DNA-directed RNA polymerase subunit

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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: Sus scrofa (pig)
Molecular weightTheoretical: 17.162273 KDa
SequenceString:
MAGILFEDIF DVKDIDPEGK KFDRVSRLHC ESESFKMDLI LDVNIQIYPV DLGDKFRLVI ASTLYEDGTL DDGEYNPTDD RPSRADQFE YVMYGKVYRI EGDETSTEAA TRLSAYVSYG GLLMRLQGDA NNLHGFEVDS RVYLLMKKLA F

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

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Macromolecule #9: DNA-directed RNA polymerase II subunit RPB9

MacromoleculeName: DNA-directed RNA polymerase II subunit RPB9 / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 14.541221 KDa
SequenceString:
MEPDGTYEPG FVGIRFCQEC NNMLYPKEDK ENRILLYACR NCDYQQEADN SCIYVNKITH EVDELTQIIA DVSQDPTLPR TEDHPCQKC GHKEAVFFQS HSARAEDAMR LYYVCTAPHC GHRWTE

UniProtKB: DNA-directed RNA polymerase II subunit RPB9

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Macromolecule #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: Sus scrofa (pig)
Molecular weightTheoretical: 7.655123 KDa
SequenceString:
MIIPVRCFTC GKIVGNKWEA YLGLLQAEYT EGDALDALGL KRYCCRRMLL AHVDLIEKLL NYAPLEK

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

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Macromolecule #11: DNA-directed RNA polymerase II subunit RPB11-a

MacromoleculeName: DNA-directed RNA polymerase II subunit RPB11-a / type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 13.310284 KDa
SequenceString:
MNAPPAFESF LLFEGEKKIT INKDTKVPNA CLFTINKEDH TLGNIIKSQL LKDPQVLFAG YKVPHPLEHK IIIRVQTTPD YSPQEAFTN AITDLISELS LLEERFRVAI KDKQEGIE

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

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Macromolecule #12: RNA polymerase II subunit K

MacromoleculeName: RNA polymerase II subunit K / type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 7.018244 KDa
SequenceString:
MDTQKDVQPP KQQPMIYICG ECHTENEIKS RDPIRCRECG YRIMYKKRTK RLVVFDAR

UniProtKB: RNA polymerase II subunit K

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Macromolecule #13: SPT6

MacromoleculeName: SPT6 / type: protein_or_peptide / ID: 13 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 117.027672 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: DQDNEIRATD LPERFQLRSI PVKGAEDDEL EEEADWIYRN AFATPTISLS RKGPSTIQKI KEALGFMRNQ HFEVPFIAFY RKEYVEPEL HINDLWRVWQ WDEKWTQLRI RKENLTRLFE KMQAYQYEQI SAIRALDTTD MERLKDVQSM DELKDVYNHF L LYYGRDIP ...String:
DQDNEIRATD LPERFQLRSI PVKGAEDDEL EEEADWIYRN AFATPTISLS RKGPSTIQKI KEALGFMRNQ HFEVPFIAFY RKEYVEPEL HINDLWRVWQ WDEKWTQLRI RKENLTRLFE KMQAYQYEQI SAIRALDTTD MERLKDVQSM DELKDVYNHF L LYYGRDIP KKFGLTPEQF GENLRDSYQR HETEQFPAEP LELAKDTPEA VLEGARYMVA LQIAREPLVR QVLRQTFQER AK LNITPTK KGRKDVDEAH YAYSFKYLKN KPVKELRDDQ FLKICLAEDE GLLTTDISID LKGTYFEEIK QFYYRDEFSH QVQ EWNRQR TMAIERALQQ FLYVQMAKEL KNKLLAEAKE YVIKACSRKL YNWLRVAPYR PDQQQGKGIR VLGIAFSSAR DHPV FCALV NGEGEVTDFL RLPHFTEERE KKAQDIETLK KFLLNKKPHV VTVAGENRDA QMLIEDVKRI VHELDQGQQL SSIGV ELVD NELAILYMNS KKSEAEFRDY PPVLRQAVSL ARRIQDPLIE FAQVCSEDIL CLKFHPLQEH VVKEELLNAL YCEFIN RVN EVGVDVNRAI AHPYSQALIQ YVCGLGPRKG THLLKILKQN NTRLESRTQL VTMCHMGPKV FMNCAGFLKI DTEVLDG SR VHPETYEWAR KMAVDALEYD ESAEDANPAG ALEEILENPE RLKDLDLDAF AEELERQGYG DKHITLYDIR AELSCRYK D LRTAYRSPNT EEIFNMLTKE TPETFYIGKL IICNVTGIAH IGVKTRLDNG VTGFIPTKFL SDKVVKRPEE RVKVGMTVH CRIMKIDIEK FSADLTCRTS DLMIAHPSFH NINFKQAEKM METMDQGDVI IRPSSKGENH LTVTWKVSDG IYQHVDVRAT LWINSEEFE DLDEIVARYV QPMASFARDL LNHKYYQDCS GGDRKKLEEL LIKTKKEKPT FIPYFICACK ELPGKFLLGY Q PRGKPRIE YVTVTPEGFR YRGQIFPTVN GLFRWFKDHY QDPV

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Macromolecule #16: RNA polymerase-associated protein CTR9 homolog,RNA polymerase-ass...

MacromoleculeName: RNA polymerase-associated protein CTR9 homolog,RNA polymerase-associated protein LEO1
type: protein_or_peptide / ID: 16 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 210.005672 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MSRGSIEIPL RDTDEVIELD FDQLPEGDEV ISILKQEHTQ LHIWIALALE YYKQGKTEEF VKLLEAARID GNLDYRDHEK DQMTCLDTL AAYYVQQARK EKNKDNKKDL ITQATLLYTM ADKIIMYDQN HLLGRACFCL LEGDKMDQAD AQFHFVLNQS P NNIPALLG ...String:
MSRGSIEIPL RDTDEVIELD FDQLPEGDEV ISILKQEHTQ LHIWIALALE YYKQGKTEEF VKLLEAARID GNLDYRDHEK DQMTCLDTL AAYYVQQARK EKNKDNKKDL ITQATLLYTM ADKIIMYDQN HLLGRACFCL LEGDKMDQAD AQFHFVLNQS P NNIPALLG KACISFNKKD YRGALAYYKK ALRTNPGCPA EVRLGMGHCF VKLNKLEKAR LAFSRALELN SKCVGALVGL AV LELNNKE ADSIKNGVQL LSRAYTIDPS NPMVLNHLAN HFFFKKDYSK VQHLALHAFH NTEVEAMQAE SCYQLARSFH VQE DYDQAF QYYYQATQFA SSSFVLPFFG LGQMYIYRGD KENASQCFEK VLKAYPNNYE TMKILGSLYA ASEDQEKRDI AKGH LKKVT EQYPDDVEAW IELAQILEQT DIQGALSAYG TATRILQEKV QADVPPEILN NVGALHFRLG NLGEAKKYFL ASLDR AKAE AEHDEHYYNA ISVTTSYNLA RLYEAMCEFH EAEKLYKNIL REHPNYVDCY LRLGAMARDK GNFYEASDWF KEALQI NQD HPDAWSLIGN LHLAKQEWGP GQKKFERILK QPSTQSDTYS MLALGNVWLQ TLHQPTRDRE KEKRHQDRAL AIYKQVL RN DAKNLYAANG IGAVLAHKGY FREARDVFAQ VREATADISD VWLNLAHIYV EQKQYISAVQ MYENCLRKFY KHQNTEVV L YLARALFKCG KLQECKQTLL KARHVAPSDT VLMFNVALVL QRLATSVLKD EKSNLKEVLN AVKELELAHR YFSYLSKVG DKMRFDLALA ATEARQCSDL LSQAQYHVAR ARKQDEEERE LRAKQEQEKE LLRQKLLKEQ EEKRLREKEE QKKLLEQRAQ YVEKTKNIL MFTGETEATK EKKRGGGGGR RSKKGGEFDE FVNDDTDDDL PISKKKKRRK GSGSEQEGED EEGGERKKKK R RRHPKGEE GSDDDETENG PKPKKRRPPK AEKKKAPKPE RLPPSMKGKI KSKAIISSSD DSSDEDKLKI ADEGHPRNSN SN SDSDEDE QRKKCASSES DSDENQNKSG SEAGSPRRPR RQRSDQDSDS DQPSRKRRPS GSEQSDNESV QSGRSHSGVS END SRPASP SAESDHESER GSDNEGSGQG SGNESEPEGS NNEASDRGSE HGSDDSDENL YFQMADMEDL FGSDADSEAE RKDS DSGSD SDSDQENAAS GSNASGSESD QDERGDSGQP SNKELFGDDS EDEGASHHSG SDNHSERSDN RSEASERSDH EDNDP SDVD QHSGSEAPND DEDEGHRSDG GSHHSEAEGS EKAHSDDEKW GREDKSDQSD DEKIQNSDDE ERAQGSDEDK LQNSDD DEK MQNTDDEERP QLSDDERQQL SEEEKANSDD ERPVASDNDD EKQNSDDEEQ PQLSDEEKMQ NSDDERPQAS DEEHRHS DD EEEQDHKSES ARGSDSEDEV LRMKRKNAIA SDSEADSDTE VPKDNSGTMD LFGGADDISS GSDGEDKPPT PGQPVDEN G LPQDQQEEEP IPETRIEVEI PKVNTDLGND LYFVKLPNFL SVEPRPFDPQ YYEDEFEDEE MLDEEGRTRL KLKVENTIR WRIRRDEEGN EIKESNARIV KWSDGSMSLH LGNEVFDVYK APLQGDHNHL FIRQGTGLQG QAVFKTKLTF RPHSTDSATH RKMTLSLAD RCSKTQKIRI LPMAGRDPEC QRTEMIKKEE ERLRASIRRE SQQRRMREKQ HQRGLSASYL EPDRYDEEEE G EESISLAA IKNRYKGGIR EERARIYSSD SDEGSEEDKA QRLLKAKKLT SDEEGEPSGK RKAEDDDKAN KKHKKYVISD EE EEDDD

UniProtKB: RNA polymerase-associated protein CTR9 homolog, RNA polymerase-associated protein LEO1

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Macromolecule #17: RNA polymerase-associated protein RTF1 homolog

MacromoleculeName: RNA polymerase-associated protein RTF1 homolog / type: protein_or_peptide / ID: 17 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 29.128234 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: VSLPEELNRV RLSRHKLERW CHMPFFAKTV TGCFVRIGIG NHNSKPVYRV AEITGVVETA KVYQLGGTRT NKGLQLRHGN DQRVFRLEF VSNQEFTESE FMKWKEAMFS AGMQLPTLDE INKKELSIKE ALNYKFNDQD IEEIVKEKER FRKAPPNYAM K KTQLLKEK ...String:
VSLPEELNRV RLSRHKLERW CHMPFFAKTV TGCFVRIGIG NHNSKPVYRV AEITGVVETA KVYQLGGTRT NKGLQLRHGN DQRVFRLEF VSNQEFTESE FMKWKEAMFS AGMQLPTLDE INKKELSIKE ALNYKFNDQD IEEIVKEKER FRKAPPNYAM K KTQLLKEK AMAEDLGDQD KAKQIQDQLN ELEERAEALD RQRTKNISAI SYINQRNREW NIVESEKALV AESHNMKNQQ MD PFTRRQC K

UniProtKB: RNA polymerase-associated protein RTF1 homolog

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Macromolecule #19: RNA polymerase II-associated factor 1 homolog

MacromoleculeName: RNA polymerase II-associated factor 1 homolog / type: protein_or_peptide / ID: 19 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 36.450977 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: ERSGVVCRVK YCNSLPDIPF DPKFITYPFD QNRFVQYKAT SLEKQHKHDL LTEPDLGVTI DLINPDTYRI DPNVLLDPAD EKLLEEEIQ APTSSKRSQQ HAKVVPWMRK TEYISTEFNR YGISNEKPEV KIGVSVKQQF TEEEIYKDRD SQITAIEKTF E DAQKSISQ ...String:
ERSGVVCRVK YCNSLPDIPF DPKFITYPFD QNRFVQYKAT SLEKQHKHDL LTEPDLGVTI DLINPDTYRI DPNVLLDPAD EKLLEEEIQ APTSSKRSQQ HAKVVPWMRK TEYISTEFNR YGISNEKPEV KIGVSVKQQF TEEEIYKDRD SQITAIEKTF E DAQKSISQ HYSKPRVTPV EVMPVFPDFK MWINPCAQVI FDSDPAPKDT SGAAALEMMS QAMIRGMMDE EGNQFVAYFL PV EETLKKR KRDQEEEMDY APDDVYDYKI AREYNWNVKN KASKGYEENY FFIFREGDGV YYNELETRVR LSKR

UniProtKB: RNA polymerase II-associated factor 1 homolog

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Macromolecule #20: WD repeat-containing protein 61

MacromoleculeName: WD repeat-containing protein 61 / type: protein_or_peptide / ID: 20 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 33.617465 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MTNQYGILFK QEQAHDDAIW SVAWGTNKKE NSETVVTGSL DDLVKVWKWR DERLDLQWSL EGHQLGVVSV DISHTLPIAA SSSLDAHIR LWDLENGKQI KSIDAGPVDA WTLAFSPDSQ YLATGTHVGK VNIFGVESGK KEYSLDTRGK FILSIAYSPD G KYLASGAI ...String:
MTNQYGILFK QEQAHDDAIW SVAWGTNKKE NSETVVTGSL DDLVKVWKWR DERLDLQWSL EGHQLGVVSV DISHTLPIAA SSSLDAHIR LWDLENGKQI KSIDAGPVDA WTLAFSPDSQ YLATGTHVGK VNIFGVESGK KEYSLDTRGK FILSIAYSPD G KYLASGAI DGIINIFDIA TGKLLHTLEG HAMPIRSLTF SPDSQLLVTA SDDGYIKIYD VQHANLAGTL SGHASWVLNV AF CPDDTHF VSSSSDKSVK VWDVGTRTCV HTFFDHQDQV WGVKYNGNGS KIVSVGDDQE IHIYDCPI

UniProtKB: Superkiller complex protein 8

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Macromolecule #21: Parafibromin

MacromoleculeName: Parafibromin / type: protein_or_peptide / ID: 21 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 60.673539 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MADVLSVLRQ YNIQKKEIVV KGDEVIFGEF SWPKNVKTNY VVWGTGKEGQ PREYYTLDSI LFLLNNVHLS HPVYVRRAAT ENIPVVRRP DRKDLLGYLN GEASTSASID RSAPLEIGLQ RSTQVKRAAD EVLAEAKKPR IEDEECVRLD KERLAARLEG H KEGIVQTE ...String:
MADVLSVLRQ YNIQKKEIVV KGDEVIFGEF SWPKNVKTNY VVWGTGKEGQ PREYYTLDSI LFLLNNVHLS HPVYVRRAAT ENIPVVRRP DRKDLLGYLN GEASTSASID RSAPLEIGLQ RSTQVKRAAD EVLAEAKKPR IEDEECVRLD KERLAARLEG H KEGIVQTE QIRSLSEAMS VEKIAAIKAK IMAKKRSTIK TDLDDDITAL KQRSFVDAEV DVTRDIVSRE RVWRTRTTIL QS TGKNFSK NIFAILQSVK AREEGRAPEQ RPAPNAAPVD PTLRTKQPIP AAYNRYDQER FKGKEETEGF KIDTMGTYHG MTL KSVTEG ASARKTQTPA AQPVPRPVSQ ARPPPNQKKG SRTPIIIIPA ATTSLITMLN AKDLLQDLKF VPSDEKKKQG CQRE NETLI QRRKDQMQPG GTAISVTVPY RVVDQPLKLM PQDWDRVVAV FVQGPAWQFK GWPWLLPDGS PVDIFAKIKA FHLKY DEVR LDPNVQKWDV TVLELSYHKR HLDRPVFLRF WETLDRYMVK HKSHLRF

UniProtKB: Parafibromin

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Macromolecule #22: Transcription elongation factor SPT4

MacromoleculeName: Transcription elongation factor SPT4 / type: protein_or_peptide / ID: 22 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 13.508496 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString:
GPGSMALETV PKDLRHLRAC LLCSLVKTID QFEYDGCDNC DAYLQMKGNR EMVYDCTSSS FDGIIAMMSP EDSWVSKWQR VSNFKPGVY AVSVTGRLPQ GIVRELKSRG VAYKSRDTAI KT

UniProtKB: Transcription elongation factor SPT4

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Macromolecule #23: Transcription elongation factor SPT5

MacromoleculeName: Transcription elongation factor SPT5 / type: protein_or_peptide / ID: 23 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 121.225477 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MSDSEDSNFS EEEDSERSSD GEEAEVDEER RSAAGSEKEE EPEDEEEEEE EEEYDEEEEE EDDDRPPKKP RHGGFILDEA DVDDEYEDE DQWEDGAEDI LEKEEIEASN IDNVVLDEDR SGARRLQNLW RDQREEELGE YYMKKYAKSS VGETVYGGSD E LSDDITQQ ...String:
MSDSEDSNFS EEEDSERSSD GEEAEVDEER RSAAGSEKEE EPEDEEEEEE EEEYDEEEEE EDDDRPPKKP RHGGFILDEA DVDDEYEDE DQWEDGAEDI LEKEEIEASN IDNVVLDEDR SGARRLQNLW RDQREEELGE YYMKKYAKSS VGETVYGGSD E LSDDITQQ QLLPGVKDPN LWTVKCKIGE ERATAISLMR KFIAYQFTDT PLQIKSVVAP EHVKGYIYVE AYKQTHVKQA IE GVGNLRL GYWNQQMVPI KEMTDVLKVV KEVANLKPKS WVRLKRGIYK DDIAQVDYVE PSQNTISLKM IPRIDYDRIK ARM SLKDWF AKRKKFKRPP QRLFDAEKIR SLGGDVASDG DFLIFEGNRY SRKGFLFKSF AMSAVITEGV KPTLSELEKF EDQP EGIDL EVVTESTGKE REHNFQPGDN VEVCEGELIN LQGKILSVDG NKITIMPKHE DLKDMLEFPA QELRKYFKMG DHVKV IAGR FEGDTGLIVR VEENFVILFS DLTMHELKVL PRDLQLCSET ASGVDVGGQH EWGELVQLDP QTVGVIVRLE RETFQV LNM YGKVVTVRHQ AVTRKKDNRF AVALDSEQNN IHVKDIVKVI DGPHSGREGE IRHLFRSFAF LHCKKLVENG GMFVCKT RH LVLAGGSKPR DVTNFTVGGF APMSPRISSP MHPSAGGQRG GFGSPGGGSG GMSRGRGRRD NELIGQTVRI SQGPYKGY I GVVKDATEST ARVELHSTCQ TISVDRQRLT TVGSRRPGGM TSTYGRTPMY GSQ(TPO)PMYGSG SRTPMYGSQT PLQDG SRTP HYGSQTPLHD GSRTPAQSGA WDPNNPNTPS RAEEEYEYAF DDEPTPSPQA YGGTPNPQTP GYPDPSSPQV NPQYNP QTP GTPAMYNTDQ FSPYAAPSPQ GSYQPSPSPQ SYHQVAPSPA GYQNTHSPAS YHPTPSPMAY QASPSPSPVG YSPMTPG AP SPGGYNPHTP GSGIEQNSSD WVTTDIQVKV RDTYLDTQVV GQTGVIRSVT GGMCSVYLKD SEKVVSISSE HLEPITPT K NNKVKVILGE DREATGVLLS IDGEDGIVRM DLDEQLKILN LRFLGKLLEA

UniProtKB: Transcription elongation factor SPT5

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Macromolecule #24: Histone H3.2

MacromoleculeName: Histone H3.2 / type: protein_or_peptide / ID: 24 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Xenopus laevis (African clawed frog)
Molecular weightTheoretical: 15.435126 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MARTKQTARK STGGKAPRKQ LATKAARKSA PATGGVKKPH RYRPGTVALR EIRRYQKSTE LLIRKLPFQR LVREIAQDFK TDLRFQSSA VMALQEASEA YLVALFEDTN LCAIHAKRVT IMPKDIQLAR RIRGERA

UniProtKB: Histone H3.2

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Macromolecule #25: Histone H4

MacromoleculeName: Histone H4 / type: protein_or_peptide / ID: 25 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Xenopus laevis (African clawed frog)
Molecular weightTheoretical: 11.394426 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MSGRGKGGKG LGKGGAKRHR KVLRDNIQGI TKPAIRRLAR RGGVKRISGL IYEETRGVLK VFLENVIRDA VTYTEHAKRK TVTAMDVVY ALKRQGRTLY GFGG

UniProtKB: Histone H4

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Macromolecule #26: Histone H2A

MacromoleculeName: Histone H2A / type: protein_or_peptide / ID: 26 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Xenopus laevis (African clawed frog)
Molecular weightTheoretical: 11.294136 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString:
TRSSRAGLQF PVGRVHRLLR KGNYAERVGA GAPVYLAAVL EYLTAEILEL AGNAARDNKK TRIIPRHLQL AVRNDEELNK LLGRVTIAQ GGVLPNIQSV LLPK

UniProtKB: Histone H2A

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Macromolecule #27: Histone H2B

MacromoleculeName: Histone H2B / type: protein_or_peptide / ID: 27 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Xenopus laevis (African clawed frog)
Molecular weightTheoretical: 10.607212 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
KTRKESYAIY VYKVLKQVHP DTGISSKAMS IMNSFVNDVF ERIAGEASRL AHYNKRSTIT SREIQTAVRL LLPGELAKHA VSEGTKAVT KYTSAK

UniProtKB: Histone H2B

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Macromolecule #14: Non-template DNA

MacromoleculeName: Non-template DNA / type: dna / ID: 14 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 39.557168 KDa
SequenceString: (DC)(DC)(DA)(DT)(DT)(DG)(DA)(DG)(DA)(DG) (DC)(DG)(DG)(DC)(DG)(DG)(DA)(DG)(DC)(DC) (DA)(DG)(DC)(DA)(DG)(DG)(DG)(DA)(DG) (DC)(DT)(DG)(DG)(DG)(DC)(DG)(DG)(DT)(DT) (DA) (DA)(DA)(DA)(DC)(DG)(DC) ...String:
(DC)(DC)(DA)(DT)(DT)(DG)(DA)(DG)(DA)(DG) (DC)(DG)(DG)(DC)(DG)(DG)(DA)(DG)(DC)(DC) (DA)(DG)(DC)(DA)(DG)(DG)(DG)(DA)(DG) (DC)(DT)(DG)(DG)(DG)(DC)(DG)(DG)(DT)(DT) (DA) (DA)(DA)(DA)(DC)(DG)(DC)(DG)(DG) (DG)(DG)(DG)(DA)(DC)(DA)(DG)(DC)(DG)(DC) (DG)(DT) (DA)(DC)(DG)(DT)(DG)(DC)(DG) (DT)(DT)(DT)(DA)(DA)(DG)(DC)(DG)(DG)(DT) (DG)(DC)(DT) (DA)(DG)(DA)(DG)(DC)(DT) (DG)(DT)(DC)(DT)(DA)(DC)(DG)(DA)(DC)(DC) (DA)(DA)(DT)(DT) (DG)(DA)(DG)(DC)(DG) (DG)(DC)(DC)(DT)(DC)(DG)(DG)(DC)(DA)(DC) (DC)(DG)(DG)(DG)(DA) (DT)(DT)(DC)(DT) (DG)(DA)(DT)

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Macromolecule #18: RNA, Template DNA

MacromoleculeName: RNA, Template DNA / type: dna / ID: 18 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 42.305887 KDa
SequenceString: (DA)(DT)(DC)(DA)(DG)(DA)(DA)(DT)(DC)(DC) (DC)(DG)(DG)(DT)(DG)(DC)(DC)(DG)(DA)(DG) (DG)(DC)(DC)(DG)(DC)(DT)(DC)(DA)(DA) (DT)(DT)(DG)(DG)(DT)(DC)(DG)(DT)(DA)(DG) (DA) (DC)(DA)(DG)(DC)(DT)(DC) ...String:
(DA)(DT)(DC)(DA)(DG)(DA)(DA)(DT)(DC)(DC) (DC)(DG)(DG)(DT)(DG)(DC)(DC)(DG)(DA)(DG) (DG)(DC)(DC)(DG)(DC)(DT)(DC)(DA)(DA) (DT)(DT)(DG)(DG)(DT)(DC)(DG)(DT)(DA)(DG) (DA) (DC)(DA)(DG)(DC)(DT)(DC)(DT)(DA) (DG)(DC)(DA)(DC)(DC)(DG)(DC)(DT)(DT)(DA) (DA)(DA) (DC)(DG)(DC)(DA)(DC)(DG)(DT) (DA)(DC)(DG)(DC)(DG)(DC)(DT)(DG)(DT)(DC) (DC)(DC)(DC) (DC)(DG)(DC)(DG)(DT)(DT) (DT)(DT)(DA)(DA)(DC)(DC)(DG)(DC)(DC)(DC) (DA)(DG)(DC)(DT) (DC)(DC)(DC)(DT)(DG) (DC)(DT)(DG)(DG)(DC)(DT)(DC)(DC)(DG)(DA) (DG)(DT)(DG)(DG)(DG) (DT)(DT)(DC)(DT) (DG)(DC)(DC)(DG)(DC)(DT)(DC)(DT)(DC)(DA) (DA)(DT)(DG)(DG)

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Macromolecule #15: RNA, Template DNA

MacromoleculeName: RNA, Template DNA / type: rna / ID: 15 / Number of copies: 1
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 9.054556 KDa
SequenceString:
UAACCGGAGA GGGAACCCAC UCAAAAAA

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Macromolecule #28: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 28 / Number of copies: 9 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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Macromolecule #29: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 29 / Number of copies: 1 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.4
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.2 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: OTHER
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 30000
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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About Yorodumi

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News

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Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

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