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- EMDB-31116: TFIID lobe B subcomplex -

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Basic information

Entry
Database: EMDB / ID: EMD-31116
TitleTFIID lobe B subcomplex
Map dataTFIID lobe B subcomplex
Sample
  • Complex: TFIID lobe B subcomplex
    • Protein or peptide: Transcription initiation factor TFIID subunit 4
    • Protein or peptide: Transcription initiation factor TFIID subunit 5
    • Protein or peptide: Transcription initiation factor TFIID subunit 6
    • Protein or peptide: Transcription initiation factor TFIID subunit 8
    • Protein or peptide: Transcription initiation factor TFIID subunit 9
    • Protein or peptide: Transcription initiation factor TFIID subunit 10
    • Protein or peptide: Transcription initiation factor TFIID subunit 12
Function / homology
Function and homology information


SAGA complex assembly / lateral mesodermal cell differentiation / DNA-templated transcription open complex formation / allantois development / pre-snoRNP complex / transcription factor TFTC complex / SLIK (SAGA-like) complex / positive regulation of response to cytokine stimulus / hepatocyte differentiation / maintenance of protein location in nucleus ...SAGA complex assembly / lateral mesodermal cell differentiation / DNA-templated transcription open complex formation / allantois development / pre-snoRNP complex / transcription factor TFTC complex / SLIK (SAGA-like) complex / positive regulation of response to cytokine stimulus / hepatocyte differentiation / maintenance of protein location in nucleus / C2H2 zinc finger domain binding / box C/D snoRNP assembly / SAGA complex / RNA polymerase binding / limb development / transcription preinitiation complex / regulation of fat cell differentiation / response to L-glutamate / inner cell mass cell proliferation / negative regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator / RNA polymerase II general transcription initiation factor activity / transcription factor TFIID complex / regulation of RNA splicing / 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 / MLL1 complex / aryl hydrocarbon receptor binding / RNA polymerase II transcribes snRNA genes / negative regulation of proteasomal ubiquitin-dependent protein catabolic process / negative regulation of cell cycle / positive regulation of transcription initiation by RNA polymerase II / embryonic placenta development / regulation of DNA repair / somitogenesis / positive regulation of intrinsic apoptotic signaling pathway / ovarian follicle development / RNA polymerase II preinitiation complex assembly / RNA Polymerase II Pre-transcription Events / TBP-class protein binding / response to interleukin-1 / male germ cell nucleus / promoter-specific chromatin binding / nuclear estrogen receptor binding / DNA-templated transcription initiation / transcription initiation at RNA polymerase II promoter / G1/S transition of mitotic cell cycle / multicellular organism growth / mRNA transcription by RNA polymerase II / actin cytoskeleton / p53 binding / HATs acetylate histones / ATPase binding / DNA-binding transcription factor binding / Regulation of TP53 Activity through Phosphorylation / transcription by RNA polymerase II / cell differentiation / transcription coactivator activity / protein stabilization / transcription cis-regulatory region binding / Ub-specific processing proteases / chromatin remodeling / positive regulation of apoptotic process / protein heterodimerization activity / negative regulation of cell population proliferation / apoptotic process / DNA damage response / chromatin / regulation of DNA-templated transcription / regulation of transcription by RNA polymerase II / negative regulation of apoptotic process / perinuclear region of cytoplasm / positive regulation of DNA-templated transcription / enzyme binding / positive regulation of transcription by RNA polymerase II / protein-containing complex / DNA binding / nucleoplasm / identical protein binding / nucleus / cytosol / cytoplasm
Similarity search - Function
Transcription initiation factor TFIID subunit 8 / Transcription initiation factor TFIID component TAF4 / Transcription factor TFIID complex subunit 8 C-term / Transcription factor TFIID, subunit 8, C-terminal / Transcription initiation factor TFIID component TAF4 family / Transcription initiation factor TFIID component TAF4, C-terminal / TAFH/NHR1 domain superfamily / NHR1 homology to TAF / TAFH/NHR1 domain profile. / TAF homology ...Transcription initiation factor TFIID subunit 8 / Transcription initiation factor TFIID component TAF4 / Transcription factor TFIID complex subunit 8 C-term / Transcription factor TFIID, subunit 8, C-terminal / Transcription initiation factor TFIID component TAF4 family / Transcription initiation factor TFIID component TAF4, C-terminal / TAFH/NHR1 domain superfamily / NHR1 homology to TAF / TAFH/NHR1 domain profile. / TAF homology / TAFH/NHR1 / Bromodomain associated / Bromodomain transcription factors and PHD domain containing proteins / Bromodomain associated domain / Transcription initiation factor IID, 31kD subunit / Transcription initiation factor TFIID subunit 12 / Transcription initiation factor TFIID subunit A / TFIID subunit TAF5, NTD2 domain superfamily / WD40 associated region in TFIID subunit, NTD2 domain / Transcription initiation factor TAFII31 / TAF6, C-terminal HEAT repeat domain superfamily / TATA box binding protein associated factor (TAF) / Transcription initiation factor TFIID subunit 12 domain / TFIID subunit TAF5, NTD2 domain / Transcription initiation factor TFIID subunit 6 / TAF6 C-terminal HEAT repeat domain / TAF6, C-terminal HEAT repeat domain / Transcription initiation factor TFIID 23-30kDa subunit / Transcription initiation factor TFIID, 23-30kDa subunit / LIS1 homology (LisH) motif profile. / LIS1 homology motif / TATA box binding protein associated factor / TATA box binding protein associated factor (TAF), histone-like fold domain / Histone-fold / Armadillo-type fold / G-protein beta WD-40 repeat / WD40 repeat, conserved site / Trp-Asp (WD) repeats signature. / WD domain, G-beta repeat / WD40 repeats / WD40 repeat / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD40-repeat-containing domain superfamily / WD40/YVTN repeat-like-containing domain superfamily
Similarity search - Domain/homology
Transcription initiation factor TFIID subunit 4 / Transcription initiation factor TFIID subunit 6 / Transcription initiation factor TFIID subunit 10 / Transcription initiation factor TFIID subunit 5 / Transcription initiation factor TFIID subunit 12 / Transcription initiation factor TFIID subunit 9 / Transcription initiation factor TFIID subunit 8
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.77 Å
AuthorsChen X / Wu Z / Li J / Zhao D / Xu Y
CitationJournal: Science / Year: 2021
Title: Structural insights into preinitiation complex assembly on core promoters.
Authors: Xizi Chen / Yilun Qi / Zihan Wu / Xinxin Wang / Jiabei Li / Dan Zhao / Haifeng Hou / Yan Li / Zishuo Yu / Weida Liu / Mo Wang / Yulei Ren / Ze Li / Huirong Yang / Yanhui Xu /
Abstract: Transcription factor IID (TFIID) recognizes core promoters and supports preinitiation complex (PIC) assembly for RNA polymerase II (Pol II)-mediated eukaryotic transcription. We determined the ...Transcription factor IID (TFIID) recognizes core promoters and supports preinitiation complex (PIC) assembly for RNA polymerase II (Pol II)-mediated eukaryotic transcription. We determined the structures of human TFIID-based PIC in three stepwise assembly states and revealed two-track PIC assembly: stepwise promoter deposition to Pol II and extensive modular reorganization on track I (on TATA-TFIID-binding element promoters) versus direct promoter deposition on track II (on TATA-only and TATA-less promoters). The two tracks converge at an ~50-subunit holo PIC in identical conformation, whereby TFIID stabilizes PIC organization and supports loading of cyclin-dependent kinase (CDK)-activating kinase (CAK) onto Pol II and CAK-mediated phosphorylation of the Pol II carboxyl-terminal domain. Unexpectedly, TBP of TFIID similarly bends TATA box and TATA-less promoters in PIC. Our study provides structural visualization of stepwise PIC assembly on highly diversified promoters.
History
DepositionMar 24, 2021-
Header (metadata) releaseMay 5, 2021-
Map releaseMay 5, 2021-
UpdateMay 19, 2021-
Current statusMay 19, 2021Processing site: PDBj / Status: Released

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Structure visualization

Movie
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  • Atomic models: PDB-7egg
  • Surface level: 0.5
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_31116.png

Downloads & links

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Map

FileDownload / File: emd_31116.map.gz / Format: CCP4 / Size: 125 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationTFIID lobe B subcomplex
Voxel sizeX=Y=Z: 0.82 Å
Density
Contour LevelBy AUTHOR: 0.37 / Movie #1: 0.5
Minimum - Maximum-1.9962667 - 3.5641859
Average (Standard dev.)-8.295925e-05 (±0.09974613)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions320320320
Spacing320320320
CellA=B=C: 262.4 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z0.820.820.82
M x/y/z320320320
origin x/y/z0.0000.0000.000
length x/y/z262.400262.400262.400
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS320320320
D min/max/mean-1.9963.564-0.000

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Supplemental data

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Sample components

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Entire : TFIID lobe B subcomplex

EntireName: TFIID lobe B subcomplex
Components
  • Complex: TFIID lobe B subcomplex
    • Protein or peptide: Transcription initiation factor TFIID subunit 4
    • Protein or peptide: Transcription initiation factor TFIID subunit 5
    • Protein or peptide: Transcription initiation factor TFIID subunit 6
    • Protein or peptide: Transcription initiation factor TFIID subunit 8
    • Protein or peptide: Transcription initiation factor TFIID subunit 9
    • Protein or peptide: Transcription initiation factor TFIID subunit 10
    • Protein or peptide: Transcription initiation factor TFIID subunit 12

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Supramolecule #1: TFIID lobe B subcomplex

SupramoleculeName: TFIID lobe B subcomplex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Homo sapiens (human)

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Macromolecule #1: Transcription initiation factor TFIID subunit 4

MacromoleculeName: Transcription initiation factor TFIID subunit 4 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 110.221883 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MAAGSDLLDE VFFNSEVDEK VVSDLVGSLE SQLAASAAHH HHLAPRTPEV RAAAAGALGN HVVSGSPAGA AGAGPAAPAE GAPGAAPEP PPAGRARPGG GGPQRPGPPS PRRPLVPAGP APPAAKLRPP PEGSAGSCAP VPAAAAVAAG PEPAPAGPAK P AGPAALAA ...String:
MAAGSDLLDE VFFNSEVDEK VVSDLVGSLE SQLAASAAHH HHLAPRTPEV RAAAAGALGN HVVSGSPAGA AGAGPAAPAE GAPGAAPEP PPAGRARPGG GGPQRPGPPS PRRPLVPAGP APPAAKLRPP PEGSAGSCAP VPAAAAVAAG PEPAPAGPAK P AGPAALAA RAGPGPGPGP GPGPGPGPGK PAGPGAAQTL NGSAALLNSH HAAAPAVSLV NNGPAALLPL PKPAAPGTVI QT PPFVGAA APPAPAAPSP PAAPAPAAPA AAPPPPPPAP ATLARPPGHP AGPPTAAPAV PPPAAAQNGG SAGAAPAPAP AAG GPAGVS GQPGPGAAAA APAPGVKAES PKRVVQAAPP AAQTLAASGP ASTAASMVIG PTMQGALPSP AAVPPPAPGT PTGL PKGAA GAVTQSLSRT PTATTSGIRA TLTPTVLAPR LPQPPQNPTN IQNFQLPPGM VLVRSENGQL LMIPQQALAQ MQAQA HAQP QTTMAPRPAT PTSAPPVQIS TVQAPGTPII ARQVTPTTII KQVSQAQTTV QPSATLQRSP GVQPQLVLGG AAQTAS LGT ATAVQTGTPQ RTVPGATTTS SAATETMENV KKCKNFLSTL IKLASSGKQS TETAANVKEL VQNLLDGKIE AEDFTSR LY RELNSSPQPY LVPFLKRSLP ALRQLTPDSA AFIQQSQQQP PPPTSQATTA LTAVVLSSSV QRTAGKTAAT VTSALQPP V LSLTQPTQVG VGKQGQPTPL VIQQPPKPGA LIRPPQVTLT QTPMVALRQP HNRIMLTTPQ QIQLNPLQPV PVVKPAVLP GTKALSAVSA QAAAAQKNKL KEPGGGSFRD DDDINDVASM AGVNLSEESA RILATNSELV GTLTRSCKDE TFLLQAPLQR RILEIGKKH GITELHPDVV SYVSHATQQR LQNLVEKISE TAQQKNFSYK DDDRYEQASD VRAQLKFFEQ LDQIEKQRKD E QEREILMR AAKSRSRQED PEQLRLKQKA KEMQQQELAQ MRQRDANLTA LAAIGPRKKR KVDCPGPGSG AEGSGPGSVV PG SSGVGTP RQFTRQRITR VNLRDLIFCL ENERETSHSL LLYKAFLK

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Macromolecule #2: Transcription initiation factor TFIID subunit 5

MacromoleculeName: Transcription initiation factor TFIID subunit 5 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 86.932109 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MAALAEEQTE VAVKLEPEGP PTLLPPQAGD GAGEGSGGTT NNGPNGGGGN VAASSSTGGD GGTPKPTVAV SAAAPAGAAP VPAAAPDAG APHDRQTLLA VLQFLRQSKL REAEEALRRE AGLLEEAVAG SGAPGEVDSA GAEVTSALLS RVTASAPGPA A PDPPGTGA ...String:
MAALAEEQTE VAVKLEPEGP PTLLPPQAGD GAGEGSGGTT NNGPNGGGGN VAASSSTGGD GGTPKPTVAV SAAAPAGAAP VPAAAPDAG APHDRQTLLA VLQFLRQSKL REAEEALRRE AGLLEEAVAG SGAPGEVDSA GAEVTSALLS RVTASAPGPA A PDPPGTGA SGATVVSGSA SGPAAPGKVG SVAVEDQPDV SAVLSAYNQQ GDPTMYEEYY SGLKHFIECS LDCHRAELSQ LF YPLFVHM YLELVYNQHE NEAKSFFEKF HGDQECYYQD DLRVLSSLTK KEHMKGNETM LDFRTSKFVL RISRDSYQLL KRH LQEKQN NQIWNIVQEH LYIDIFDGMP RSKQQIDAMV GSLAGEAKRE ANKSKVFFGL LKEPEIEVPL DDEDEEGENE EGKP KKKKP KKDSIGSKSK KQDPNAPPQN RIPLPELKDS DKLDKIMNMK ETTKRVRLGP DCLPSICFYT FLNAYQGLTA VDVTD DSSL IAGGFADSTV RVWSVTPKKL RSVKQASDLS LIDKESDDVL ERIMDEKTAS ELKILYGHSG PVYGASFSPD RNYLLS SSE DGTVRLWSLQ TFTCLVGYKG HNYPVWDTQF SPYGYYFVSG GHDRVARLWA TDHYQPLRIF AGHLADVNCT RFHPNSN YV ATGSADRTVR LWDVLNGNCV RIFTGHKGPI HSLTFSPNGR FLATGATDGR VLLWDIGHGL MVGELKGHTD TVCSLRFS R DGEILASGSM DNTVRLWDAI KAFEDLETDD FTTATGHINL PENSQELLLG TYMTKSTPVV HLHFTRRNLV LAAGAYSPQ

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Macromolecule #3: Transcription initiation factor TFIID subunit 6

MacromoleculeName: Transcription initiation factor TFIID subunit 6 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 72.749297 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MAEEKKLKLS NTVLPSESMK VVAESMGIAQ IQEETCQLLT DEVSYRIKEI AQDALKFMHM GKRQKLTTSD IDYALKLKNV EPLYGFHAQ EFIPFRFASG GGRELYFYEE KEVDLSDIIN TPLPRVPLDV CLKAHWLSIE GCQPAIPENP PPAPKEQQKA E ATEPLKSA ...String:
MAEEKKLKLS NTVLPSESMK VVAESMGIAQ IQEETCQLLT DEVSYRIKEI AQDALKFMHM GKRQKLTTSD IDYALKLKNV EPLYGFHAQ EFIPFRFASG GGRELYFYEE KEVDLSDIIN TPLPRVPLDV CLKAHWLSIE GCQPAIPENP PPAPKEQQKA E ATEPLKSA KPGQEEDGPL KGKGQGATTA DGKGKEKKAP PLLEGAPLRL KPRSIHELSV EQQLYYKEIT EACVGSCEAK RA EALQSIA TDPGLYQMLP RFSTFISEGV RVNVVQNNLA LLIYLMRMVK ALMDNPTLYL EKYVHELIPA VMTCIVSRQL CLR PDVDNH WALRDFAARL VAQICKHFST TTNNIQSRIT KTFTKSWVDE KTPWTTRYGS IAGLAELGHD VIKTLILPRL QQEG ERIRS VLDGPVLSNI DRIGADHVQS LLLKHCAPVL AKLRPPPDNQ DAYRAEFGSL GPLLCSQVVK ARAQAALQAQ QVNRT TLTI TQPRPTLTLS QAPQPGPRTP GLLKVPGSIA LPVQTLVSAR AAAPPQPSPP PTKFIVMSSS SSAPSTQQVL SLSTSA PGS GSTTTSPVTT TVPSVQPIVK LVSTATTAPP STAPSGPGSV QKYIVVSLPP TGEGKGGPTS HPSPVPPPAS SPSPLSG SA LCGGKQEAGD SPPPAPGTPK ANGSQPNSGS PQPAP

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Macromolecule #4: Transcription initiation factor TFIID subunit 8

MacromoleculeName: Transcription initiation factor TFIID subunit 8 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 34.304359 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MADAAATAGA GGSGTRSGSK QSTNPADNYH LARRRTLQVV VSSLLTEAGF ESAEKASVET LTEMLQSYIS EIGRSAKSYC EHTARTQPT LSDIVVTLVE MGFNVDTLPA YAKRSQRMVI TAPPVTNQPV TPKALTAGQN RPHPPHIPSH FPEFPDPHTY I KTPTYREP ...String:
MADAAATAGA GGSGTRSGSK QSTNPADNYH LARRRTLQVV VSSLLTEAGF ESAEKASVET LTEMLQSYIS EIGRSAKSYC EHTARTQPT LSDIVVTLVE MGFNVDTLPA YAKRSQRMVI TAPPVTNQPV TPKALTAGQN RPHPPHIPSH FPEFPDPHTY I KTPTYREP VSDYQVLREK AASQRRDVER ALTRFMAKTG ETQSLFKDDV STFPLIAARP FTIPYLTALL PSELEMQQME ET DSSEQDE QTDTENLALH ISMEDSGAEK ENTSVLQQNP SLSGSRNGEE NIIDNPYLRP VKKPKIRRKK SLS

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Macromolecule #5: Transcription initiation factor TFIID subunit 9

MacromoleculeName: Transcription initiation factor TFIID subunit 9 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 29.006838 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MESGKTASPK SMPKDAQMMA QILKDMGITE YEPRVINQML EFAFRYVTTI LDDAKIYSSH AKKATVDADD VRLAIQCRAD QSFTSPPPR DFLLDIARQR NQTPLPLIKP YSGPRLPPDR YCLTAPNYRL KSLQKKASTS AGRITVPRLS VGSVTSRPST P TLGTPTPQ ...String:
MESGKTASPK SMPKDAQMMA QILKDMGITE YEPRVINQML EFAFRYVTTI LDDAKIYSSH AKKATVDADD VRLAIQCRAD QSFTSPPPR DFLLDIARQR NQTPLPLIKP YSGPRLPPDR YCLTAPNYRL KSLQKKASTS AGRITVPRLS VGSVTSRPST P TLGTPTPQ TMSVSTKVGT PMSLTGQRFT VQMPTSQSPA VKASIPATSA VQNVLINPSL IGSKNILITT NMMSSQNTAN ES SNALKRK REDDDDDDDD DDDYDNL

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Macromolecule #6: Transcription initiation factor TFIID subunit 10

MacromoleculeName: Transcription initiation factor TFIID subunit 10 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 21.731248 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MSCSGSGADP EAAPASAASA PGPAPPVSAP AALPSSTAAE NKASPAGTAG GPGAGAAAGG TGPLAARAGE PAERRGAAPV SAGGAAPPE GAISNGVYVL PSAANGDVKP VVSSTPLVDF LMQLEDYTPT IPDAVTGYYL NRAGFEASDP RIIRLISLAA Q KFISDIAN ...String:
MSCSGSGADP EAAPASAASA PGPAPPVSAP AALPSSTAAE NKASPAGTAG GPGAGAAAGG TGPLAARAGE PAERRGAAPV SAGGAAPPE GAISNGVYVL PSAANGDVKP VVSSTPLVDF LMQLEDYTPT IPDAVTGYYL NRAGFEASDP RIIRLISLAA Q KFISDIAN DALQHCKMKG TASGSSRSKS KDRKYTLTME DLTPALSEYG INVKKPHYFT

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Macromolecule #7: Transcription initiation factor TFIID subunit 12

MacromoleculeName: Transcription initiation factor TFIID subunit 12 / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 17.948467 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
MNQFGPSALI NLSNFSSIKP EPASTPPQGS MANSTAVVKI PGTPGAGGRL SPENNQVLTK KKLQDLVREV DPNEQLDEDV EEMLLQIAD DFIESVVTAA CQLARHRKSS TLEVKDVQLH LERQWNMWIP GFGSEEIRPY KKACTTEAHK QRMALIRKTT K K

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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: 7.9
GridMaterial: GOLD / Pretreatment - Type: PLASMA CLEANING
VitrificationCryogen name: ETHANE

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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: 2.7 mm
Specialist opticsEnergy filter - Slit width: 20 eV
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 / Average electron dose: 63.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Initial angle assignmentType: OTHER
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.77 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 84427

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Atomic model buiding 1

RefinementSpace: REAL / Protocol: AB INITIO MODEL
Output model

PDB-7egg:
TFIID lobe B subcomplex

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