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- EMDB-15006: Structure of SNAPc containing Pol II pre-initiation complex bound... -

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Basic information

Entry
Database: EMDB / ID: EMD-15006
TitleStructure of SNAPc containing Pol II pre-initiation complex bound to U1 snRNA promoter (CC)
Map data
Sample
  • Complex: Pre-initiation complex of RNA polymerase II with general transcription factors and SNAPc bound to U1 promoter
    • Complex: SNAPc
      • Protein or peptide: x 5 types
    • Complex: TATA-box-binding protein and transcription factors
      • Protein or peptide: x 5 types
    • Complex: Promoter
      • DNA: x 2 types
    • Complex: RNA polymerase II
      • Protein or peptide: x 12 types
  • Ligand: x 2 types
KeywordsRNA polymerase II / Pol II / PIC / SNAPc / snRNA / U1 promoter / TRANSCRIPTION
Function / homology
Function and homology information


snRNA-activating protein complex / snRNA transcription / snRNA transcription by RNA polymerase III / bent DNA binding / : / RNA polymerase III type 3 promoter sequence-specific DNA binding / positive regulation of core promoter binding / RNA polymerase II core complex assembly / meiotic sister chromatid cohesion / RNA polymerase transcription factor SL1 complex ...snRNA-activating protein complex / snRNA transcription / snRNA transcription by RNA polymerase III / bent DNA binding / : / RNA polymerase III type 3 promoter sequence-specific DNA binding / positive regulation of core promoter binding / RNA polymerase II core complex assembly / meiotic sister chromatid cohesion / RNA polymerase transcription factor SL1 complex / snRNA transcription by RNA polymerase II / phosphatase activator activity / RNA polymerase III general transcription initiation factor activity / RNA polymerase I core promoter sequence-specific DNA binding / TFIIF-class transcription factor complex binding / B-WICH complex positively regulates rRNA expression / RNA Polymerase I Transcription Initiation / RNA Polymerase I Promoter Escape / RNA Polymerase I Transcription Termination / RNA Polymerase III Transcription Initiation From Type 1 Promoter / RNA Polymerase III Transcription Initiation From Type 2 Promoter / RNA Polymerase III Transcription Initiation From Type 3 Promoter / RNA Polymerase III Transcription Initiation From Type 1 Promoter / RNA Polymerase III Transcription Initiation From Type 2 Promoter / transcriptional start site selection at RNA polymerase II promoter / RNA Polymerase III Transcription Initiation From Type 3 Promoter / 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 / transcription factor TFIIF complex / RNA Polymerase III Abortive And Retractive Initiation / transcription factor TFIIA complex / female germ cell nucleus / male pronucleus / female pronucleus / Abortive elongation of HIV-1 transcript in the absence of Tat / RNA polymerase II general transcription initiation factor binding / germinal vesicle / RNA Polymerase I Transcription Termination / transcription preinitiation complex / FGFR2 alternative splicing / nuclear thyroid hormone receptor binding / Viral Messenger RNA Synthesis / Signaling by FGFR2 IIIa TM / RNA Pol II CTD phosphorylation and interaction with CE during HIV infection / RNA Pol II CTD phosphorylation and interaction with CE / transcription factor TFIID complex / Formation of the Early Elongation Complex / Formation of the HIV-1 Early Elongation Complex / RNA polymerase II general transcription initiation factor activity / cell division site / mRNA Capping / protein acetylation / HIV Transcription Initiation / RNA Polymerase II HIV Promoter Escape / Transcription of the HIV genome / 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 / organelle membrane / transcription initiation at RNA polymerase III promoter / maintenance of transcriptional fidelity during transcription elongation by RNA polymerase II / RNA polymerase III activity / mRNA Splicing - Minor Pathway / acetyltransferase activity / RNA polymerase II complex binding / RNA Polymerase I Transcription Initiation / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / aryl hydrocarbon receptor binding / viral transcription / positive regulation of nuclear-transcribed mRNA poly(A) tail shortening / Processing of Capped Intron-Containing Pre-mRNA / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / TFIIB-class transcription factor binding / transcription by RNA polymerase III / RNA polymerase II transcribes snRNA genes / RNA polymerase II activity / Tat-mediated elongation of the HIV-1 transcript / positive regulation of transcription initiation by RNA polymerase II
Similarity search - Function
snRNA-activating protein complex subunit 5 / snRNA-activating protein complex subunit 19, SNAPc subunit 19 / snRNA-activating protein complex subunit 1 / snRNA-activating protein complex, subunit 3 / : / Small nuclear RNA activating complex (SNAPc), subunit 1 / snRNA-activating protein complex (SNAPc), subunit 3 / Myb-like domain profile. / Myb-like DNA-binding domain / RNA-binding domain, S1 ...snRNA-activating protein complex subunit 5 / snRNA-activating protein complex subunit 19, SNAPc subunit 19 / snRNA-activating protein complex subunit 1 / snRNA-activating protein complex, subunit 3 / : / Small nuclear RNA activating complex (SNAPc), subunit 1 / snRNA-activating protein complex (SNAPc), subunit 3 / Myb-like domain profile. / Myb-like DNA-binding domain / RNA-binding domain, S1 / Transcription factor IIA, alpha/beta subunit / Transcription factor IIA, alpha/beta subunit / Transcription factor IIA, alpha/beta subunit / Transcription initiation factor IIA, gamma subunit / Transcription factor IIA, alpha-helical domain / Transcription factor IIA, beta-barrel / Transcription initiation factor IIA, gamma subunit, C-terminal / Transcription initiation factor IIA, gamma subunit, N-terminal / Transcription initiation factor IIA, gamma subunit, helical domain / Transcription initiation factor IIA, gamma subunit / Transcription initiation factor IIF, beta subunit / TFIIF beta subunit, HTH domain / TFIIF, beta subunit, N-terminal / TFIIF, beta subunit HTH domain / TFIIF, beta subunit N-terminus / Transcription initiation factor IIF, alpha subunit / Transcription initiation factor IIF, alpha subunit (TFIIF-alpha) / Transcription Factor IIF, Rap30/Rap74, interaction / Transcription factor TFIIB, cyclin-like domain / Transcription factor TFIIB, conserved site / Transcription factor TFIIB repeat / Transcription factor TFIIB repeat signature. / Transcription factor TFIIB / Zinc finger TFIIB-type profile. / Zinc finger, TFIIB-type / TFIIB zinc-binding / Myb-type HTH DNA-binding domain profile. / SANT domain / TATA-box binding protein, eukaryotic / TATA-box binding protein / TATA-box binding protein, conserved site / Transcription factor TFIID (or TATA-binding protein, TBP) / Transcription factor TFIID repeat signature. / Myb domain / TBP domain superfamily / DNA-directed RNA polymerase II subunit Rpb4-like / RNA polymerase Rpb4/RPC9, core / DNA-directed RNA-polymerase II subunit / RNA polymerase II, heptapeptide repeat, eukaryotic / RNA polymerase Rpb1, domain 6 / RNA polymerase Rpb1, domain 6 / RNA polymerase Rpb1 C-terminal repeat / Eukaryotic RNA polymerase II heptapeptide repeat. / RNA polymerase Rpb1, domain 7 / RNA polymerase Rpb1, domain 7 superfamily / RNA polymerase Rpb1, domain 7 / Rpb4/RPC9 superfamily / Pol II subunit B9, C-terminal zinc ribbon / RNA polymerase RBP11 / SANT SWI3, ADA2, N-CoR and TFIIIB'' DNA-binding domains / RNA polymerase subunit Rpb4/RPC9 / RNA polymerase Rpb4 / Cyclin-like / domain present in cyclins, TFIIB and Retinoblastoma / SANT/Myb domain / Cyclin-like superfamily / 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 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, subunit RPB6 / 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 II subunit RPB11-a / DNA-directed RNA polymerases I, II, and III subunit RPABC3 / DNA-directed RNA polymerases I, II, and III subunit RPABC5 / DNA-directed RNA polymerase subunit / DNA-directed RNA polymerases I, II, and III subunit RPABC2 / DNA-directed RNA polymerase II subunit RPB3 / DNA-directed RNA polymerase subunit beta / DNA-directed RNA polymerase II subunit RPB7 / RNA polymerase II, I and III subunit K ...RNA polymerase II subunit D / DNA-directed RNA polymerase II subunit RPB11-a / DNA-directed RNA polymerases I, II, and III subunit RPABC3 / DNA-directed RNA polymerases I, II, and III subunit RPABC5 / DNA-directed RNA polymerase subunit / DNA-directed RNA polymerases I, II, and III subunit RPABC2 / DNA-directed RNA polymerase II subunit RPB3 / DNA-directed RNA polymerase subunit beta / DNA-directed RNA polymerase II subunit RPB7 / RNA polymerase II, I and III subunit K / DNA-directed RNA polymerase II subunit E / snRNA-activating protein complex subunit 5 / General transcription factor IIF subunit 2 / TATA-box-binding protein / General transcription factor IIF subunit 1 / Transcription initiation factor IIA subunit 1 / Transcription initiation factor IIA subunit 2 / DNA-directed RNA polymerase II subunit RPB9 / Transcription initiation factor IIB / snRNA-activating protein complex subunit 1 / snRNA-activating protein complex subunit 4 / snRNA-activating protein complex subunit 3
Similarity search - Component
Biological speciesHomo sapiens (human) / Sus scrofa (pig)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.4 Å
AuthorsRengachari S / Schilbach S / Kaliyappan T / Gouge J / Zumer K / Schwarz J / Urlaub H / Dienemann C / Vannini A / Cramer P
Funding support Germany, United Kingdom, 4 items
OrganizationGrant numberCountry
German Research Foundation (DFG)SFB860 Germany
German Research Foundation (DFG)EXC 2067/1 39072994 Germany
Cancer Research UKCR-UK C47547/A21536 United Kingdom
Wellcome Trust200818/Z/16/Z United Kingdom
Citation
Journal: Nat Struct Mol Biol / Year: 2022
Title: Structural basis of SNAPc-dependent snRNA transcription initiation by RNA polymerase II.
Authors: Srinivasan Rengachari / Sandra Schilbach / Thangavelu Kaliyappan / Jerome Gouge / Kristina Zumer / Juliane Schwarz / Henning Urlaub / Christian Dienemann / Alessandro Vannini / Patrick Cramer /
Abstract: RNA polymerase II (Pol II) carries out transcription of both protein-coding and non-coding genes. Whereas Pol II initiation at protein-coding genes has been studied in detail, Pol II initiation at ...RNA polymerase II (Pol II) carries out transcription of both protein-coding and non-coding genes. Whereas Pol II initiation at protein-coding genes has been studied in detail, Pol II initiation at non-coding genes, such as small nuclear RNA (snRNA) genes, is less well understood at the structural level. Here, we study Pol II initiation at snRNA gene promoters and show that the snRNA-activating protein complex (SNAPc) enables DNA opening and transcription initiation independent of TFIIE and TFIIH in vitro. We then resolve cryo-EM structures of the SNAPc-containing Pol IIpre-initiation complex (PIC) assembled on U1 and U5 snRNA promoters. The core of SNAPc binds two turns of DNA and recognizes the snRNA promoter-specific proximal sequence element (PSE), located upstream of the TATA box-binding protein TBP. Two extensions of SNAPc, called wing-1 and wing-2, bind TFIIA and TFIIB, respectively, explaining how SNAPc directs Pol II to snRNA promoters. Comparison of structures of closed and open promoter complexes elucidates TFIIH-independent DNA opening. These results provide the structural basis of Pol II initiation at non-coding RNA gene promoters.
#1: Journal: Biorxiv / Year: 2022
Title: Structural basis of SNAPc-dependent snRNA transcription initiation by RNA polymerase II
Authors: Rengachari S / Schilbach S / Kaliyappan T / Gouge J / Zumer K / Schwarz J / Urlaub H / Dienemann C / Vannini A / Cramer P
History
DepositionMay 20, 2022-
Header (metadata) releaseNov 30, 2022-
Map releaseNov 30, 2022-
UpdateJul 24, 2024-
Current statusJul 24, 2024Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_15006.png

Downloads & links

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Map

FileDownload / File: emd_15006.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
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AxesZ (Sec.)Y (Row.)X (Col.)
1.05 Å/pix.
x 400 pix.
= 420. Å		1.05 Å/pix.
x 400 pix.
= 420. Å		1.05 Å/pix.
x 400 pix.
= 420. 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: 0.0183
Minimum - Maximum-0.055162825 - 0.19323853
Average (Standard dev.)-0.00015393148 (±0.006349875)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions400400400
Spacing400400400
CellA=B=C: 419.99997 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_15006_msk_1.map
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Half map: #2

Fileemd_15006_half_map_1.map
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Half map: #1

Fileemd_15006_half_map_2.map
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Sample components

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Entire : Pre-initiation complex of RNA polymerase II with general transcri...

EntireName: Pre-initiation complex of RNA polymerase II with general transcription factors and SNAPc bound to U1 promoter
Components
  • Complex: Pre-initiation complex of RNA polymerase II with general transcription factors and SNAPc bound to U1 promoter
    • Complex: SNAPc
      • Protein or peptide: TATA-box-binding protein
      • Protein or peptide: snRNA-activating protein complex subunit 1
      • Protein or peptide: snRNA-activating protein complex subunit 3
      • Protein or peptide: snRNA-activating protein complex subunit 4
      • Protein or peptide: snRNA-activating protein complex subunit 5
    • Complex: TATA-box-binding protein and transcription factors
      • Protein or peptide: Transcription initiation factor IIB
      • Protein or peptide: General transcription factor IIF subunit 1
      • Protein or peptide: General transcription factor IIF subunit 2
      • Protein or peptide: Transcription initiation factor IIA subunit 1
      • Protein or peptide: Transcription initiation factor IIA subunit 2
    • Complex: Promoter
      • DNA: Non-template strand
      • DNA: Template strand
    • Complex: RNA polymerase II
      • 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 polymerase II subunit F
      • 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: RNA polymerase II subunit J
      • Protein or peptide: RNA polymerase II subunit K
  • Ligand: ZINC ION
  • Ligand: MAGNESIUM ION

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Supramolecule #1: Pre-initiation complex of RNA polymerase II with general transcri...

SupramoleculeName: Pre-initiation complex of RNA polymerase II with general transcription factors and SNAPc bound to U1 promoter
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#24

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Supramolecule #2: SNAPc

SupramoleculeName: SNAPc / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #15, #21-#24
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #3: TATA-box-binding protein and transcription factors

SupramoleculeName: TATA-box-binding protein and transcription factors / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #13, #16-#17, #19-#20
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #4: Promoter

SupramoleculeName: Promoter / type: complex / ID: 4 / Parent: 1 / Macromolecule list: #14, #18
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #5: RNA polymerase II

SupramoleculeName: RNA polymerase II / type: complex / ID: 5 / Parent: 1 / Macromolecule list: #1-#12
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 / EC number: DNA-directed RNA polymerase
Source (natural)Organism: Sus scrofa (pig)
Molecular weightTheoretical: 217.450078 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 QGATPAYGAW SPSVGSGMTP GAAGFSPSAA SDASGFSPGY SPAWSPTPGS PGSPGPSSPY IPSPGGAMSP SYSPTSPAY EPRSPGGYTP QSPSYSPTSP SYSPTSPSYS PTSPNYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP TSPSYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP TSPSYSPTSP SYSPTSPNYS PTSPNYTPTS P SYSPTSPS YSPTSPNYTP TSPNYSPTSP SYSPTSPSYS PTSPSYSPSS PRYTPQSPTY TPSSPSYSPS SPSYSPTSPK YT PTSPSYS PSSPEYTPTS PKYSPTSPKY SPTSPKYSPT SPTYSPTTPK YSPTSPTYSP TSPVYTPTSP KYSPTSPTYS PTS PKYSPT SPTYSPTSPK GSTYSPTSPG YSPTSPTYSL TSPAISPDDS DEEN

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: 134.041422 KDa
SequenceString: MYDADEDMQY DEDDDEITPD LWQEACWIVI SSYFDEKGLV RQQLDSFDEF IQMSVQRIVE DAPPIDLQAE AQHASGEVEE PPRYLLKFE QIYLSKPTHW ERDGAPSPMM PNEARLRNLT YSAPLYVDIT KTVIKEGEEQ LQTQHQKTFI GKIPIMLRST Y CLLNGLTD ...String:
MYDADEDMQY DEDDDEITPD LWQEACWIVI SSYFDEKGLV RQQLDSFDEF IQMSVQRIVE DAPPIDLQAE AQHASGEVEE PPRYLLKFE QIYLSKPTHW ERDGAPSPMM PNEARLRNLT YSAPLYVDIT KTVIKEGEEQ LQTQHQKTFI GKIPIMLRST Y CLLNGLTD RDLCELNECP LDPGGYFIIN GSEKVLIAQE KMATNTVYVF AKKDSKYAYT GECRSCLENS SRPTSTIWVS ML ARGGQGA KKSAIGQRIV ATLPYIKQEV PIIIVFRALG FVSDRDILEH IIYDFEDPEM MEMVKPSLDE AFVIQEQNVA LNF IGSRGA KPGVTKEKRI KYAKEVLQKE MLPHVGVSDF CETKKAYFLG YMVHRLLLAA LGRRELDDRD HYGNKRLDLA GPLL AFLFR GMFKNLLKEV RIYAQKFIDR GKDFNLELAI KTRIISDGLK YSLATGNWGD QKKAHQARAG VSQVLNRLTF ASTLS HLRR LNSPIGRDGK LAKPRQLHNT LWGMVCPAET PEGHAVGLVK NLALMAYISV GSQPSPILEF LEEWSMENLE EISPAA IAD ATKIFVNGCW VGIHKDPEQL MNTLRKLRRQ MDIIVSEVSM IRDIREREIR IYTDAGRICR PLLIVEKQKL LLKKRHI DQ LKEREYNNYS WQDLVASGVV EYIDTLEEET VMLAMTPDDL QEKEVAYCST YTHCEIHPSM ILGVCASIIP FPDHNQSP R NTYQSAMGKQ AMGVYITNFH VRMDTLAHVL YYPQKPLVTT RSMEYLRFRE LPAGINSIVA IASYTGYNQE DSVIMNRSA VDRGFFRSVF YRSYKEQESK KGFDQEEVFE KPTRETCQGM RHAIYDKLDD DGLIAPGVRV SGDDVIIGKT VTLPENEDEL EGTNRRYTK RDCSTFLRTS ETGIVDQVMV TLNQEGYKFC KIRVRSVRIP QIGDKFASRH GQKGTCGIQY RQEDMPFTCE G ITPDIIIN PHAIPSRMTI GHLIECLQGK VSANKGEIGD ATPFNDAVNV QKISNLLSDY GYHLRGNEVL YNGFTGRKIT SQ IFIGPTY YQRLKHMVDD KIHSRARGPI QILNRQPMEG RSRDGGLRFG EMERDCQIAH GAAQFLRERL FEASDPYQVH VCN LCGIMA IANTRTHTYE CRGCRNKTQI SLVRMPYACK LLFQELMSMS IAPRMMSV

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: 31.439074 KDa
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 QSDVLTIN

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

+
Macromolecule #6: DNA-directed RNA polymerase II subunit F

MacromoleculeName: DNA-directed RNA polymerase II subunit F / 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

+
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 II subunit RPB7

+
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

+
Macromolecule #11: RNA polymerase II subunit J

MacromoleculeName: RNA polymerase II subunit J / 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, I and III subunit K

+
Macromolecule #13: Transcription initiation factor IIB

MacromoleculeName: Transcription initiation factor IIB / type: protein_or_peptide / ID: 13 / Number of copies: 1 / Enantiomer: LEVO / EC number: histone acetyltransferase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 34.877949 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MASTSRLDAL PRVTCPNHPD AILVEDYRAG DMICPECGLV VGDRVIDVGS EWRTFSNDKA TKDPSRVGDS QNPLLSDGDL STMIGKGTG AASFDEFGNS KYQNRRTMSS SDRAMMNAFK EITTMADRIN LPRNIVDRTN NLFKQVYEQK SLKGRANDAI A SACLYIAC ...String:
MASTSRLDAL PRVTCPNHPD AILVEDYRAG DMICPECGLV VGDRVIDVGS EWRTFSNDKA TKDPSRVGDS QNPLLSDGDL STMIGKGTG AASFDEFGNS KYQNRRTMSS SDRAMMNAFK EITTMADRIN LPRNIVDRTN NLFKQVYEQK SLKGRANDAI A SACLYIAC RQEGVPRTFK EICAVSRISK KEIGRCFKLI LKALETSVDL ITTGDFMSRF CSNLCLPKQV QMAATHIARK AV ELDLVPG RSPISVAAAA IYMASQASAE KRTQKEIGDI AGVADVTIRQ SYRLIYPRAP DLFPTDFKFD TPVDKLPQL

UniProtKB: Transcription initiation factor IIB

+
Macromolecule #15: TATA-box-binding protein

MacromoleculeName: TATA-box-binding protein / type: protein_or_peptide / ID: 15 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 37.729938 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MDQNNSLPPY AQGLASPQGA MTPGIPIFSP MMPYGTGLTP QPIQNTNSLS ILEEQQRQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQ QQQQQQAVAA AAVQQSTSQQ ATQGTSGQAP QLFHSQTLTT APLPGTTPLY PSPMTPMTPI TPATPASESS G IVPQLQNI ...String:
MDQNNSLPPY AQGLASPQGA MTPGIPIFSP MMPYGTGLTP QPIQNTNSLS ILEEQQRQQQ QQQQQQQQQQ QQQQQQQQQQ QQQQQQQQQ QQQQQQAVAA AAVQQSTSQQ ATQGTSGQAP QLFHSQTLTT APLPGTTPLY PSPMTPMTPI TPATPASESS G IVPQLQNI VSTVNLGCKL DLKTIALRAR NAEYNPKRFA AVIMRIREPR TTALIFSSGK MVCTGAKSEE QSRLAARKYA RV VQKLGFP AKFLDFKIQN MVGSCDVKFP IRLEGLVLTH QQFSSYEPEL FPGLIYRMIK PRIVLLIFVS GKVVLTGAKV RAE IYEAFE NIYPILKGFR KTT

UniProtKB: TATA-box-binding protein

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Macromolecule #16: General transcription factor IIF subunit 1

MacromoleculeName: General transcription factor IIF subunit 1 / type: protein_or_peptide / ID: 16 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 58.343578 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MAALGPSSQN VTEYVVRVPK NTTKKYNIMA FNAADKVNFA TWNQARLERD LSNKKIYQEE EMPESGAGSE FNRKLREEAR RKKYGIVLK EFRPEDQPWL LRVNGKSGRK FKGIKKGGVT ENTSYYIFTQ CPDGAFEAFP VHNWYNFTPL ARHRTLTAEE A EEEWERRN ...String:
MAALGPSSQN VTEYVVRVPK NTTKKYNIMA FNAADKVNFA TWNQARLERD LSNKKIYQEE EMPESGAGSE FNRKLREEAR RKKYGIVLK EFRPEDQPWL LRVNGKSGRK FKGIKKGGVT ENTSYYIFTQ CPDGAFEAFP VHNWYNFTPL ARHRTLTAEE A EEEWERRN KVLNHFSIMQ QRRLKDQDQD EDEEEKEKRG RRKASELRIH DLEDDLEMSS DASDASGEEG GRVPKAKKKA PL AKGGRKK KKKKGSDDEA FEDSDDGDFE GQEVDYMSDG SSSSQEEPES KAKAPQQEEG PKGVDEQSDS SEESEEEKPP EED KEEEEE KKAPTPQEKK RRKDSSEESD SSEESDIDSE ASSALFMAKK KTPPKRERKP SGGSSRGNSR PGTPSAEGGS TSST LRAAA SKLEQGKRVS EMPAAKRLRL DTGPQSLSGK STPQPPSGKT TPNSGDVQVT EDAVRRYLTR KPMTTKDLLK KFQTK KTGL SSEQTVNVLA QILKRLNPER KMINDKMHFS LKE

UniProtKB: General transcription factor IIF subunit 1

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Macromolecule #17: General transcription factor IIF subunit 2

MacromoleculeName: General transcription factor IIF subunit 2 / type: protein_or_peptide / ID: 17 / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA helicase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 28.427309 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MAERGELDLT GAKQNTGVWL VKVPKYLSQQ WAKASGRGEV GKLRIAKTQG RTEVSFTLNE DLANIHDIGG KPASVSAPRE HPFVLQSVG GQTLTVFTES SSDKLSLEGI VVQRAECRPA ASENYMRLKR LQIEESSKPV RLSQQLDKVV TTNYKPVANH Q YNIEYERK ...String:
MAERGELDLT GAKQNTGVWL VKVPKYLSQQ WAKASGRGEV GKLRIAKTQG RTEVSFTLNE DLANIHDIGG KPASVSAPRE HPFVLQSVG GQTLTVFTES SSDKLSLEGI VVQRAECRPA ASENYMRLKR LQIEESSKPV RLSQQLDKVV TTNYKPVANH Q YNIEYERK KKEDGKRARA DKQHVLDMLF SAFEKHQYYN LKDLVDITKQ PVVYLKEILK EIGVQNVKGI HKNTWELKPE YR HYQGEEK SD

UniProtKB: General transcription factor IIF subunit 2

+
Macromolecule #19: Transcription initiation factor IIA subunit 1

MacromoleculeName: Transcription initiation factor IIA subunit 1 / type: protein_or_peptide / ID: 19 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 41.544551 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MANSANTNTV PKLYRSVIED VINDVRDIFL DDGVDEQVLM ELKTLWENKL MQSRAVDGFH SEEQQLLLQV QQQHQPQQQQ HHHHHHHQQ AQPQQTVPQQ AQTQQVLIPA SQQATAPQVI VPDSKLIQHM NASNMSAAAT AATLALPAGV TPVQQILTNS G QLLQVVRA ...String:
MANSANTNTV PKLYRSVIED VINDVRDIFL DDGVDEQVLM ELKTLWENKL MQSRAVDGFH SEEQQLLLQV QQQHQPQQQQ HHHHHHHQQ AQPQQTVPQQ AQTQQVLIPA SQQATAPQVI VPDSKLIQHM NASNMSAAAT AATLALPAGV TPVQQILTNS G QLLQVVRA ANGAQYIFQP QQSVVLQQQV IPQMQPGGVQ APVIQQVLAP LPGGISPQTG VIIQPQQILF TGNKTQVIPT TV AAPTPAQ AQITATGQQQ PQAQPAQTQA PLVLQVDGTG DTSSEEDEDE EEDYDDDEEE DKEKDGAEDG QVEEEPLNSE DDV SDEEGQ ELFDTENVVV CQYDKIHRSK NKWKFHLKDG IMNLNGRDYI FSKAIGDAEW

UniProtKB: Transcription initiation factor IIA subunit 1

+
Macromolecule #20: Transcription initiation factor IIA subunit 2

MacromoleculeName: Transcription initiation factor IIA subunit 2 / type: protein_or_peptide / ID: 20 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 12.469091 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MAYQLYRNTT LGNSLQESLD ELIQSQQITP QLALQVLLQF DKAINAALAQ RVRNRVNFRG SLNTYRFCDN VWTFVLNDVE FREVTELIK VDKVKIVACD GKNTGSNTTE

UniProtKB: Transcription initiation factor IIA subunit 2

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Macromolecule #21: snRNA-activating protein complex subunit 1

MacromoleculeName: snRNA-activating protein complex subunit 1 / type: protein_or_peptide / ID: 21 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 43.074473 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MGTPPGLQTD CEALLSRFQE TDSVRFEDFT ELWRNMKFGT IFCGRMRNLE KNMFTKEALA LAWRYFLPPY TFQIRVGALY LLYGLYNTQ LCQPKQKIRV ALKDWDEVLK FQQDLVNAQH FDAAYIFRKL RLDRAFHFTA MPKLLSYRMK KKIHRAEVTE E FKDPSDRV ...String:
MGTPPGLQTD CEALLSRFQE TDSVRFEDFT ELWRNMKFGT IFCGRMRNLE KNMFTKEALA LAWRYFLPPY TFQIRVGALY LLYGLYNTQ LCQPKQKIRV ALKDWDEVLK FQQDLVNAQH FDAAYIFRKL RLDRAFHFTA MPKLLSYRMK KKIHRAEVTE E FKDPSDRV MKLITSDVLE EMLNVHDHYQ NMKHVISVDK SKPDKALSLI KDDFFDNIKN IVLEHQQWHK DRKNPSLKSK TN DGEEKME GNSQETERCE RAESLAKIKS KAFSVVIQAS KSRRHRQVKL DSSDSDSASG QGQVKATRKK EKKERLKPAG RKM SLRNKG NVQNIHKEDK PLSLSMPVIT EEEENESLSG TEFTASKKRR KH

UniProtKB: snRNA-activating protein complex subunit 1

+
Macromolecule #22: snRNA-activating protein complex subunit 3

MacromoleculeName: snRNA-activating protein complex subunit 3 / type: protein_or_peptide / ID: 22 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 46.812605 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MAEGSRGGPT CSGVGGRQDP VSGSGGCNFP EYELPELNTR AFHVGAFGEL WRGRLRGAGD LSLREPPASA LPGSQAADSD REDAAVARD LDCSLEAAAE LRAVCGLDKL KCLEDGEDPE VIPENTDLVT LGVRKRFLEH REETITIDRA CRQETFVYEM E SHAIGKKP ...String:
MAEGSRGGPT CSGVGGRQDP VSGSGGCNFP EYELPELNTR AFHVGAFGEL WRGRLRGAGD LSLREPPASA LPGSQAADSD REDAAVARD LDCSLEAAAE LRAVCGLDKL KCLEDGEDPE VIPENTDLVT LGVRKRFLEH REETITIDRA CRQETFVYEM E SHAIGKKP ENSADMIEEG ELILSVNILY PVIFHKHKEH KPYQTMLVLG SQKLTQLRDS IRCVSDLQIG GEFSNTPDQA PE HISKDLY KSAFFYFEGT FYNDKRYPEC RDLSRTIIEW SESHDRGYGK FQTARMEDFT FNDLCIKLGF PYLYCHQGDC EHV IVITDI RLVHHDDCLD RTLYPLLIKK HWLWTRKCFV CKMYTARWVT NNDSFAPEDP CFFCDVCFRM LHYDSEGNKL GEFL AYPYV DPGTFN

UniProtKB: snRNA-activating protein complex subunit 3

+
Macromolecule #23: snRNA-activating protein complex subunit 4

MacromoleculeName: snRNA-activating protein complex subunit 4 / type: protein_or_peptide / ID: 23 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 159.645172 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString: MDVDAEREKI TQEIKELERI LDPGSSGSHV EISESSLESD SEADSLPSED LDPADPPISE EERWGEASND EDDPKDKTLP EDPETCLQL NMVYQEVIQE KLAEANLLLA QNREQQEELM RDLAGSKGTK VKDGKSLPPS TYMGHFMKPY FKDKVTGVGP P ANEDTREK ...String:
MDVDAEREKI TQEIKELERI LDPGSSGSHV EISESSLESD SEADSLPSED LDPADPPISE EERWGEASND EDDPKDKTLP EDPETCLQL NMVYQEVIQE KLAEANLLLA QNREQQEELM RDLAGSKGTK VKDGKSLPPS TYMGHFMKPY FKDKVTGVGP P ANEDTREK AAQGIKAFEE LLVTKWKNWE KALLRKSVVS DRLQRLLQPK LLKLEYLHQK QSKVSSELER QALEKQGREA EK EIQDINQ LPEEALLGNR LDSHDWEKIS NINFEGSRSA EEIRKFWQNS EHPSINKQEW SREEEERLQA IAAAHGHLEW QKI AEELGT SRSAFQCLQK FQQHNKALKR KEWTEEEDRM LTQLVQEMRV GSHIPYRRIV YYMEGRDSMQ LIYRWTKSLD PGLK KGYWA PEEDAKLLQA VAKYGEQDWF KIREEVPGRS DAQCRDRYLR RLHFSLKKGR WNLKEEEQLI ELIEKYGVGH WAKIA SELP HRSGSQCLSK WKIMMGKKQG LRRRRRRARH SVRWSSTSSS GSSSGSSGGS SSSSSSSSEE DEPEQAQAGE GDRALL SPQ YMVPDMDLWV PARQSTSQPW RGGAGAWLGG PAASLSPPKG SSASQGGSKE ASTTAAAPGE ETSPVQVPAR AHGPVPR SA QASHSADTRP AGAEKQALEG GRRLLTVPVE TVLRVLRANT AARSCTQKEQ LRQPPLPTSS PGVSSGDSVA RSHVQWLR H RATQSGQRRW RHALHRRLLN RRLLLAVTPW VGDVVVPCTQ ASQRPAVVQT QADGLREQLQ QARLASTPVF TLFTQLFHI DTAGCLEVVR ERKALPPRLP QAGARDPPVH LLQASSSAQS TPGHLFPNVP AQEASKSASH KGSRRLASSR VERTLPQASL LASTGPRPK PKTVSELLQE KRLQEARARE ATRGPVVLPS QLLVSSSVIL QPPLPHTPHG RPAPGPTVLN VPLSGPGAPA A AKPGTSGS WQEAGTSAKD KRLSTMQALP LAPVFSEAEG TAPAASQAPA LGPGQISVSC PESGLGQSQA PAASRKQGLP EA PPFLPAA PSPTPLPVQP LSLTHIGGPH VATSVPLPVT WVLTAQGLLP VPVPAVVSLP RPAGTPGPAG LLATLLPPLT ETR AAQGPR APALSSSWQP PANMNREPEP SCRTDTPAPP THALSQSPAE ADGSVAFVPG EAQVAREIPE PRTSSHADPP EAEP PWSGR LPAFGGVIPA TEPRGTPGSP SGTQEPRGPL GLEKLPLRQP GPEKGALDLE KPPLPQPGPE KGALDLGLLS QEGEA ATQQ WLGGQRGVRV PLLGSRLPYQ PPALCSLRAL SGLLLHKKAL EHKATSLVVG GEAERPAGAL QASLGLVRGQ LQDNPA YLL LRARFLAAFT LPALLATLAP QGVRTTLSVP SRVGSESEDE DLLSELELAD RDGQPGCTTA TCPIQGAPDS GKCSASS CL DTSNDPDDLD VLRTRHARHT RKRRRLV

UniProtKB: snRNA-activating protein complex subunit 4

+
Macromolecule #24: snRNA-activating protein complex subunit 5

MacromoleculeName: snRNA-activating protein complex subunit 5 / type: protein_or_peptide / ID: 24 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 11.343449 KDa
Recombinant expressionOrganism: Trichoplusia ni (cabbage looper)
SequenceString:
MLSRLQELRK EEETLLRLKA ALHDQLNRLK VEELALQSMI SSRRGDEMLS SHTVPEQSHD MLVHVDNEAS INQTTLELST KSHVTEEEE EEEEEESDS

UniProtKB: snRNA-activating protein complex subunit 5

+
Macromolecule #14: Non-template strand

MacromoleculeName: Non-template strand / type: dna / ID: 14 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 29.969139 KDa
SequenceString: (DG)(DC)(DA)(DA)(DG)(DT)(DG)(DA)(DC)(DC) (DG)(DT)(DG)(DT)(DG)(DT)(DG)(DT)(DA)(DA) (DA)(DG)(DA)(DG)(DT)(DG)(DA)(DG)(DG) (DC)(DG)(DT)(DA)(DT)(DG)(DA)(DG)(DG)(DC) (DT) (DG)(DT)(DG)(DT)(DC)(DG) ...String:
(DG)(DC)(DA)(DA)(DG)(DT)(DG)(DA)(DC)(DC) (DG)(DT)(DG)(DT)(DG)(DT)(DG)(DT)(DA)(DA) (DA)(DG)(DA)(DG)(DT)(DG)(DA)(DG)(DG) (DC)(DG)(DT)(DA)(DT)(DG)(DA)(DG)(DG)(DC) (DT) (DG)(DT)(DG)(DT)(DC)(DG)(DG)(DG) (DG)(DC)(DA)(DG)(DA)(DG)(DG)(DC)(DA)(DC) (DA)(DA) (DC)(DG)(DT)(DT)(DT)(DC)(DA) (DT)(DA)(DC)(DT)(DT)(DA)(DC)(DC)(DT)(DG) (DG)(DC)(DA) (DG)(DG)(DG)(DG)(DA)(DG) (DA)(DT)(DA)(DC)(DC)(DA)(DT)(DG)(DA)(DT)

+
Macromolecule #18: Template strand

MacromoleculeName: Template strand / type: dna / ID: 18 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 29.261691 KDa
SequenceString: (DA)(DT)(DC)(DA)(DT)(DG)(DG)(DT)(DA)(DT) (DC)(DT)(DC)(DC)(DC)(DC)(DT)(DG)(DC)(DC) (DA)(DG)(DG)(DT)(DA)(DA)(DG)(DT)(DA) (DT)(DG)(DA)(DA)(DA)(DC)(DG)(DT)(DT)(DG) (DT) (DG)(DC)(DC)(DT)(DC)(DT) ...String:
(DA)(DT)(DC)(DA)(DT)(DG)(DG)(DT)(DA)(DT) (DC)(DT)(DC)(DC)(DC)(DC)(DT)(DG)(DC)(DC) (DA)(DG)(DG)(DT)(DA)(DA)(DG)(DT)(DA) (DT)(DG)(DA)(DA)(DA)(DC)(DG)(DT)(DT)(DG) (DT) (DG)(DC)(DC)(DT)(DC)(DT)(DG)(DC) (DC)(DC)(DC)(DG)(DA)(DC)(DA)(DC)(DA)(DG) (DC)(DC) (DT)(DC)(DA)(DT)(DA)(DC)(DG) (DC)(DC)(DT)(DC)(DA)(DC)(DT)(DC)(DT)(DT) (DT)(DA)(DC) (DA)(DC)(DA)(DC)(DA)(DC) (DG)(DG)(DT)(DC)(DA)(DC)(DT)(DT)(DG)(DC)

+
Macromolecule #25: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 25 / Number of copies: 11 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

+
Macromolecule #26: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 26 / Number of copies: 1 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.5
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeTFS KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 54.45 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.3 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

+
Image processing

Startup modelType of model: INSILICO MODEL
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 47293
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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  • Yorodumi is a browser for structure data from EMDB, PDB, SASBDB, etc.
  • This page is also the successor to EM Navigator detail page, and also detail information page/front-end page for Omokage search.
  • The word "yorodu" (or yorozu) is an old Japanese word meaning "ten thousand". "mi" (miru) is to see.

Related info.:EMDB / PDB / SASBDB / Comparison of 3 databanks / Yorodumi Search / Aug 31, 2016. New EM Navigator & Yorodumi / Yorodumi Papers / Jmol/JSmol / Function and homology information / Changes in new EM Navigator and Yorodumi

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