[English] 日本語
Yorodumi
- EMDB-9302: Human TFIID Lobe A canonical -

+
Open data


ID or keywords:

Loading...

-
Basic information

Entry
Database: EMDB / ID: EMD-9302
TitleHuman TFIID Lobe A canonical
Map dataprimary map
Sample
  • Complex: General transcription factor IID
    • Protein or peptide: x 12 types
Function / homology
Function and homology information


SAGA complex assembly / lateral mesodermal cell differentiation / allantois development / pre-snoRNP complex / negative regulation of protein autoubiquitination / transcription factor TFTC complex / RNA polymerase transcription factor SL1 complex / regulation of cell cycle G1/S phase transition / RNA polymerase I general transcription initiation factor activity / SLIK (SAGA-like) complex ...SAGA complex assembly / lateral mesodermal cell differentiation / allantois development / pre-snoRNP complex / negative regulation of protein autoubiquitination / transcription factor TFTC complex / RNA polymerase transcription factor SL1 complex / regulation of cell cycle G1/S phase transition / RNA polymerase I general transcription initiation factor activity / SLIK (SAGA-like) complex / RNA polymerase III general transcription initiation factor activity / positive regulation of response to cytokine stimulus / hepatocyte differentiation / maintenance of protein location in nucleus / 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 / positive regulation of androgen receptor activity / RNA Polymerase III Abortive And Retractive Initiation / transcription factor TFIIA complex / female germ cell nucleus / C2H2 zinc finger domain binding / box C/D snoRNP assembly / male pronucleus / transcription regulator inhibitor activity / female pronucleus / positive regulation by host of viral transcription / SAGA complex / nuclear vitamin D receptor binding / RNA polymerase binding / RNA polymerase II general transcription initiation factor binding / limb development / nuclear thyroid hormone receptor binding / transcription preinitiation complex / cellular response to ATP / RNA Polymerase I Transcription Termination / response to L-glutamate / midbrain development / 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 / ubiquitin conjugating enzyme activity / MLL1 complex / transcription initiation at RNA polymerase I promoter / RNA Polymerase I Transcription Initiation / aryl hydrocarbon receptor binding / RNA polymerase II transcribes snRNA genes / TFIIB-class transcription factor binding / 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 / RNA polymerase II core promoter sequence-specific DNA binding / regulation of DNA repair / transcription by RNA polymerase III / somitogenesis / positive regulation of intrinsic apoptotic signaling pathway / core promoter sequence-specific DNA binding / histone acetyltransferase activity / ovarian follicle development / RNA polymerase II preinitiation complex assembly / negative regulation of ubiquitin-dependent protein catabolic process / histone acetyltransferase / RNA Polymerase II Pre-transcription Events / TBP-class protein binding / response to interleukin-1 / SIRT1 negatively regulates rRNA expression / regulation of signal transduction by p53 class mediator / male germ cell nucleus / nuclear estrogen receptor binding / promoter-specific chromatin binding / DNA-templated transcription initiation / transcription initiation at RNA polymerase II promoter / nuclear receptor binding / RNA Polymerase I Promoter Escape / peptidyl-threonine phosphorylation / G1/S transition of mitotic cell cycle / multicellular organism growth / lysine-acetylated histone binding / euchromatin / mRNA transcription by RNA polymerase II / NoRC negatively regulates rRNA expression / B-WICH complex positively regulates rRNA expression / negative regulation of DNA-binding transcription factor activity / protein polyubiquitination / cellular response to UV / actin cytoskeleton / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / p53 binding / positive regulation of protein binding / kinase activity / HATs acetylate histones
Similarity search - Function
TAFII28-like protein domain / Transcription initiation factor TFIID subunit 11-like / hTAFII28-like protein conserved region / Transcription initiation factor TFIID component TAF4 / Transcription initiation factor TFIID component TAF4 family / Transcription initiation factor TFIID component TAF4, C-terminal / Transcription initiation factor IID, subunit 13 / Transcription initiation factor IID, 18kD subunit / TAFH/NHR1 domain superfamily / NHR1 homology to TAF ...TAFII28-like protein domain / Transcription initiation factor TFIID subunit 11-like / hTAFII28-like protein conserved region / Transcription initiation factor TFIID component TAF4 / Transcription initiation factor TFIID component TAF4 family / Transcription initiation factor TFIID component TAF4, C-terminal / Transcription initiation factor IID, subunit 13 / Transcription initiation factor IID, 18kD subunit / 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 / TAFII-230 TBP-binding / Transcription initiation factor TFIID subunit 1, animal / TAFII-230 TBP-binding domain superfamily / TATA box-binding protein binding / Zinc knuckle / Zinc knuckle / Transcription initiation factor TFIID subunit 1, histone acetyltransferase domain / Transcription initiation factor TFIID subunit 1 / Protein of unknown function (DUF3591) / LIS1 homology (LisH) motif profile. / LIS1 homology motif / 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. / TBP domain superfamily / Zinc finger, PHD-type, conserved site / PHD-finger / Zinc finger PHD-type signature. / TATA box binding protein associated factor / TATA box binding protein associated factor (TAF), histone-like fold domain / Zinc finger PHD-type profile. / Zinc finger, PHD-finger / Zinc finger, PHD-type / PHD zinc finger / Zinc finger, FYVE/PHD-type / Histone-fold / Bromodomain, conserved site / Bromodomain signature. / Bromodomain / Bromodomain profile. / bromo domain / Bromodomain / Bromodomain-like superfamily / Armadillo-type fold / G-protein beta WD-40 repeat / Zinc finger, RING/FYVE/PHD-type / 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 / TATA-box-binding protein / Transcription initiation factor TFIID subunit 1 / Transcription initiation factor TFIID subunit 6 / Transcription initiation factor TFIID subunit 10 / Transcription initiation factor TFIID subunit 5 / Transcription initiation factor TFIID subunit 13 / Transcription initiation factor TFIID subunit 11 / Transcription initiation factor TFIID subunit 12 / Transcription initiation factor TFIID subunit 9 / Transcription initiation factor TFIID subunit 3
Similarity search - Component
Biological speciesHomo sapiens (human) / Human (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 9.8 Å
AuthorsPatel AB / Louder RK / Greber BJ / Grunberg S / Luo J / Fang J / Liu Y / Ranish J / Hahn S / Nogales E
Funding support United States, 2 items
OrganizationGrant numberCountry
Howard Hughes Medical Institute (HHMI) United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01-GM63072 United States
CitationJournal: Science / Year: 2018
Title: Structure of human TFIID and mechanism of TBP loading onto promoter DNA.
Authors: Avinash B Patel / Robert K Louder / Basil J Greber / Sebastian Grünberg / Jie Luo / Jie Fang / Yutong Liu / Jeff Ranish / Steve Hahn / Eva Nogales /
Abstract: The general transcription factor IID (TFIID) is a critical component of the eukaryotic transcription preinitiation complex (PIC) and is responsible for recognizing the core promoter DNA and ...The general transcription factor IID (TFIID) is a critical component of the eukaryotic transcription preinitiation complex (PIC) and is responsible for recognizing the core promoter DNA and initiating PIC assembly. We used cryo-electron microscopy, chemical cross-linking mass spectrometry, and biochemical reconstitution to determine the complete molecular architecture of TFIID and define the conformational landscape of TFIID in the process of TATA box-binding protein (TBP) loading onto promoter DNA. Our structural analysis revealed five structural states of TFIID in the presence of TFIIA and promoter DNA, showing that the initial binding of TFIID to the downstream promoter positions the upstream DNA and facilitates scanning of TBP for a TATA box and the subsequent engagement of the promoter. Our findings provide a mechanistic model for the specific loading of TBP by TFIID onto the promoter.
History
DepositionNov 5, 2018-
Header (metadata) releaseNov 28, 2018-
Map releaseNov 28, 2018-
UpdateNov 25, 2020-
Current statusNov 25, 2020Processing site: RCSB / Status: Released

-
Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.06
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by radius
  • Surface level: 0.06
  • Imaged by UCSF Chimera
  • Download
  • Surface view with fitted model
  • Atomic models: PDB-6mzd
  • Surface level: 0.06
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_9302.png

Downloads & links

-
Map

FileDownload / File: emd_9302.map.gz / Format: CCP4 / Size: 91.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationprimary map
Voxel sizeX=Y=Z: 1.32 Å
Density
Contour LevelBy AUTHOR: 0.06 / Movie #1: 0.06
Minimum - Maximum-0.12629227 - 0.3521133
Average (Standard dev.)-0.0003763245 (±0.009759218)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions288288288
Spacing288288288
CellA=B=C: 380.16 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.321.321.32
M x/y/z288288288
origin x/y/z0.0000.0000.000
length x/y/z380.160380.160380.160
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS288288288
D min/max/mean-0.1260.352-0.000

-
Supplemental data

-
Sample components

+
Entire : General transcription factor IID

EntireName: General transcription factor IID
Components
  • Complex: General transcription factor IID
    • Protein or peptide: Transcription initiation factor TFIID subunit 1
    • Protein or peptide: Transcription initiation factor TFIID subunit 3
    • 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 9
    • Protein or peptide: Transcription initiation factor TFIID subunit 10
    • Protein or peptide: Transcription initiation factor TFIID subunit 11
    • Protein or peptide: Transcription initiation factor TFIID subunit 12
    • Protein or peptide: Transcription initiation factor TFIID subunit 13
    • Protein or peptide: TATA-box-binding protein
    • Protein or peptide: poly(UNK)

+
Supramolecule #1: General transcription factor IID

SupramoleculeName: General transcription factor IID / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human) / Strain: HeLa

+
Macromolecule #1: Transcription initiation factor TFIID subunit 1

MacromoleculeName: Transcription initiation factor TFIID subunit 1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: histone acetyltransferase
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 213.050125 KDa
SequenceString: MSDTDSDEDS AGGGPFSLAG FLFGNINGAG QLEGESVLDD ECKKHLAGLG ALGLGSLITE LTANEELTGT DGALVNDEGW VRSTEDAVD YSDINEVAED ESRRYQQTMG SLQPLCHSDY DEDDYDADCE DIDCKLMPPP PPPPGPMKKD KDQDSITGVS E NGEGIILP ...String:
MSDTDSDEDS AGGGPFSLAG FLFGNINGAG QLEGESVLDD ECKKHLAGLG ALGLGSLITE LTANEELTGT DGALVNDEGW VRSTEDAVD YSDINEVAED ESRRYQQTMG SLQPLCHSDY DEDDYDADCE DIDCKLMPPP PPPPGPMKKD KDQDSITGVS E NGEGIILP SIIAPSSLAS EKVDFSSSSD SESEMGPQEA TQAESEDGKL TLPLAGIMQH DATKLLPSVT ELFPEFRPGK VL RFLRLFG PGKNVPSVWR SARRKRKKKH RELIQEEQIQ EVECSVESEV SQKSLWNYDY APPPPPEQCL SDDEITMMAP VES KFSQST GDIDKVTDTK PRVAEWRYGP ARLWYDMLGV PEDGSGFDYG FKLRKTEHEP VIKSRMIEEF RKLEENNGTD LLAD ENFLM VTQLHWEDDI IWDGEDVKHK GTKPQRASLA GWLPSSMTRN AMAYNVQQGF AATLDDDKPW YSIFPIDNED LVYGR WEDN IIWDAQAMPR LLEPPVLTLD PNDENLILEI PDEKEEATSN SPSKESKKES SLKKSRILLG KTGVIKEEPQ QNMSQP EVK DPWNLSNDEY YYPKQQGLRG TFGGNIIQHS IPAVELRQPF FPTHMGPIKL RQFHRPPLKK YSFGALSQPG PHSVQPL LK HIKKKAKMRE QERQASGGGE MFFMRTPQDL TGKDGDLILA EYSEENGPLM MQVGMATKIK NYYKRKPGKD PGAPDCKY G ETVYCHTSPF LGSLHPGQLL QAFENNLFRA PIYLHKMPET DFLIIRTRQG YYIRELVDIF VVGQQCPLFE VPGPNSKRA NTHIRDFLQV FIYRLFWKSK DRPRRIRMED IKKAFPSHSE SSIRKRLKLC ADFKRTGMDS NWWVLKSDFR LPTEEEIRAM VSPEQCCAY YSMIAAEQRL KDAGYGEKSF FAPEEENEED FQMKIDDEVR TAPWNTTRAF IAAMKGKCLL EVTGVADPTG C GEGFSYVK IPNKPTQQKD DKEPQPVKKT VTGTDADLRR LSLKNAKQLL RKFGVPEEEI KKLSRWEVID VVRTMSTEQA RS GEGPMSK FARGSRFSVA EHQERYKEEC QRIFDLQNKV LSSTEVLSTD TDSSSAEDSD FEEMGKNIEN MLQNKKTSSQ LSR EREEQE RKELQRMLLA AGSAASGNNH RDDDTASVTS LNSSATGRCL KIYRTFRDEE GKEYVRCETV RKPAVIDAYV RIRT TKDEE FIRKFALFDE QHREEMRKER RRIQEQLRRL KRNQEKEKLK GPPEKKPKKM KERPDLKLKC GACGAIGHMR TNKFC PLYY QTNAPPSNPV AMTEEQEEEL EKTVIHNDNE ELIKVEGTKI VLGKQLIESA DEVRRKSLVL KFPKQQLPPK KKRRVG TTV HCDYLNRPHK SIHRRRTDPM VTLSSILESI INDMRDLPNT YPFHTPVNAK VVKDYYKIIT RPMDLQTLRE NVRKRLY PS REEFREHLEL IVKNSATYNG PKHSLTQISQ SMLDLCDEKL KEKEDKLARL EKAINPLLDD DDQVAFSFIL DNIVTQKM M AVPDSWPFHH PVNKKFVPDY YKVIVNPMDL ETIRKNISKH KYQSRESFLD DVNLILANSV KYNGPESQYT KTAQEIVNV CYQTLTEYDE HLTQLEKDIC TAKEAALEEA ELESLDPMTP GPYTPQPPDL YDTNTSLSMS RDASVFQDES NMSVLDIPSA TPEKQVTQE GEDGDGDLAD EEEGTVQQPQ ASVLYEDLLM SEGEDDEEDA GSDEEGDNPF SAIQLSESGS DSDVGSGGIR P KQPRMLQE NTRMDMENEE SMMSYEGDGG EASHGLEDSN ISYGSYEEPD PKSNTQDTSF SSIGGYEVSE EEEDEEEEEQ RS GPSVLSQ VHLSEDEEDS EDFHSIAGDS DLDSDE

+
Macromolecule #2: Transcription initiation factor TFIID subunit 3

MacromoleculeName: Transcription initiation factor TFIID subunit 3 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 103.76932 KDa
SequenceString: MCESYSRSLL RVSVAQICQA LGWDSVQLSA CHLLTDVLQR YLQQLGRGCH RYSELYGRTD PILDDVGEAF QLMGVSLHEL EDYIHNIEP VTFPHQIPSF PVSKNNVLQF PQPGSKDAEE RKEYIPDYLP PIVSSQEEEE EEQVPTDGGT SAEAMQVPLE E DDELEEEE ...String:
MCESYSRSLL RVSVAQICQA LGWDSVQLSA CHLLTDVLQR YLQQLGRGCH RYSELYGRTD PILDDVGEAF QLMGVSLHEL EDYIHNIEP VTFPHQIPSF PVSKNNVLQF PQPGSKDAEE RKEYIPDYLP PIVSSQEEEE EEQVPTDGGT SAEAMQVPLE E DDELEEEE IINDENFLGK RPLDSPEAEE LPAMKRPRLL STKGDTLDVV LLEAREPLSS INTQKIPPML SPVHVQDSTD LA PPSPEPP MLAPVAKSQM PTAKPLETKS FTPKTKTKTS SPGQKTKSPK TAQSPAMVGS PIRSPKTVSK EKKSPGRSKS PKS PKSPKV TTHIPQTPVR PETPNRTPSA TLSEKISKET IQVKQIQTPP DAGKLNSENQ PKKAVVADKT IEASIDAVIA RACA EREPD PFEFSSGSES EGDIFTSPKR ISGPECTTPK ASTSANNFTK SGSTPLPLSG GTSSSDNSWT MDASIDEVVR KAKLG TPSN MPPNFPYISS PSVSPPTPEP LHKVYEEKTK LPSSVEVKKK LKKELKTKMK KKEKQRDRER EKDKNKDKSK EKDKVK EKE KDKETGRETK YPWKEFLKEE EADPYKFKIK EFEDVDPKVK LKDGLVRKEK EKHKDKKKDR EKGKKDKDKR EKEKVKD KG REDKMKAPAP PLVLPPKELA LPLFSPATAS RVPAMLPSLL PVLPEKLFEE KEKVKEKEKK KDKKEKKKKK EKEKEKKE K EREKEKRERE KREKEKEKHK HEKIKVEPVA LAPSPVIPRL TLRVGAGQDK IVISKVVPAP EAKPAPSQNR PKTPPPAPA PAPGPMLVSP APVPLPLLAQ AAAGPALLPS PGPAASGASA KAPVRSVVTE TVSTYVIRDE WGNQIWICPG CNKPDDGSPM IGCDDCDDW YHWPCVGIMT APPEEMQWFC PKCANKKKDK KHKKRKHRAH

+
Macromolecule #3: Transcription initiation factor TFIID subunit 4

MacromoleculeName: Transcription initiation factor TFIID subunit 4 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 110.221883 KDa
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

+
Macromolecule #4: Transcription initiation factor TFIID subunit 5

MacromoleculeName: Transcription initiation factor TFIID subunit 5 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 85.785164 KDa
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 RV(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)KILYGH SGPVYGASFS PDRN YLLSS SEDGTVRLWS LQTFTCLVGY KGHNYPVWDT QFSPYGYYFV SGGHDRVARL WATDHYQPLR IFAGHLADVN CTRFH PNSN YVATGSADRT VRLWDVLNGN CVRIFTGHKG PIHSLTFSPN GRFLATGATD GRVLLWDIGH GLMVGELKGH TDTVCS LRF SRDGEILASG SMDNTVRLWD AIKAFEDLET DDFTTATGHI NLPENSQELL LGTYMTKSTP VVHLHFTRRN LVLAAGA YS PQ

+
Macromolecule #5: Transcription initiation factor TFIID subunit 6

MacromoleculeName: Transcription initiation factor TFIID subunit 6 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 72.749297 KDa
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

+
Macromolecule #6: Transcription initiation factor TFIID subunit 9

MacromoleculeName: Transcription initiation factor TFIID subunit 9 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 28.830689 KDa
SequenceString: MESGKTASPK SMPKDAQMMA QILKDMGITE YEPRVINQML EFAFRYVTTI LDDAKIYSSH AKKATVDADD VRLAIQCRAD QSFTSPPPR DFLLDIARQR NQTPLPLIKP (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)PDR YCLTAPNYRL KSL QKKAST ...String:
MESGKTASPK SMPKDAQMMA QILKDMGITE YEPRVINQML EFAFRYVTTI LDDAKIYSSH AKKATVDADD VRLAIQCRAD QSFTSPPPR DFLLDIARQR NQTPLPLIKP (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)PDR YCLTAPNYRL KSL QKKAST SAGRITVPRL SVGSVTSRPS TPTLGTPTPQ TMSVSTKVGT PMSLTGQRFT VQMPTSQSPA VKASIPATSA VQNV LINPS LIGSKNILIT TNMMSSQNTA NESSNALKRK REDDDDDDDD DDDYDNL

+
Macromolecule #7: Transcription initiation factor TFIID subunit 10

MacromoleculeName: Transcription initiation factor TFIID subunit 10 / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 21.731248 KDa
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

+
Macromolecule #8: Transcription initiation factor TFIID subunit 11

MacromoleculeName: Transcription initiation factor TFIID subunit 11 / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 23.340094 KDa
SequenceString: MDDAHESPSD KGGETGESDE TAAVPGDPGA TDTDGIPEET DGDADVDLKE AAAEEGELES QDVSDLTTVE REDSSLLNPA AKKLKIDTK EKKEKKQKVD EDEIQKMQIL VSSFSEEQLN RYEMYRRSAF PKAAIKRLIQ SITGTSVSQN VVIAMSGISK V FVGEVVEE ...String:
MDDAHESPSD KGGETGESDE TAAVPGDPGA TDTDGIPEET DGDADVDLKE AAAEEGELES QDVSDLTTVE REDSSLLNPA AKKLKIDTK EKKEKKQKVD EDEIQKMQIL VSSFSEEQLN RYEMYRRSAF PKAAIKRLIQ SITGTSVSQN VVIAMSGISK V FVGEVVEE ALDVCEKWGE MPPLQPKHMR EAVRRLKSKG QIPNSKHKKI IFF

+
Macromolecule #9: Transcription initiation factor TFIID subunit 12

MacromoleculeName: Transcription initiation factor TFIID subunit 12 / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 17.948467 KDa
SequenceString:
MNQFGPSALI NLSNFSSIKP EPASTPPQGS MANSTAVVKI PGTPGAGGRL SPENNQVLTK KKLQDLVREV DPNEQLDEDV EEMLLQIAD DFIESVVTAA CQLARHRKSS TLEVKDVQLH LERQWNMWIP GFGSEEIRPY KKACTTEAHK QRMALIRKTT K K

+
Macromolecule #10: Transcription initiation factor TFIID subunit 13

MacromoleculeName: Transcription initiation factor TFIID subunit 13 / type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 14.307068 KDa
SequenceString:
MADEEEDPTF EEENEEIGGG AEGGQGKRKR LFSKELRCMM YGFGDDQNPY TESVDILEDL VIEFITEMTH KAMSIGRQGR VQVEDIVFL IRKDPRKFAR VKDLLTMNEE LKRARKAFDE ANYGS

+
Macromolecule #11: TATA-box-binding protein

MacromoleculeName: TATA-box-binding protein / type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 37.729938 KDa
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

+
Macromolecule #12: poly(UNK)

MacromoleculeName: poly(UNK) / type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 8.188084 KDa
SequenceString: (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) ...String:
(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK) (UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK)(UNK) (UNK)

-
Experimental details

-
Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

-
Sample preparation

Concentration.2 mg/mL
BufferpH: 7.9
Component:
ConcentrationFormula
20.0 mMHEPES
0.1 mMEDTAEthylenediaminetetraacetic acid
5.0 mMMgCl
2.0 %Glycerol
1.0 %Trehalose
100.0 mMKCl
0.01 %NP-40
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K / Instrument: FEI VITROBOT MARK IV / Details: BT 4s; BF 15N.

-
Electron microscopy

MicroscopeFEI TITAN
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 50.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm
Sample stageSpecimen holder model: GATAN 626 SINGLE TILT LIQUID NITROGEN CRYO TRANSFER HOLDER
Cooling holder cryogen: NITROGEN
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 40.0 e/Å2

-
Image processing

CTF correctionSoftware - Name: Gctf
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION
Final reconstructionResolution.type: BY AUTHOR / Resolution: 9.8 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 107900

+
About Yorodumi

-
News

-
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

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242)：Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi

Thousand views of thousand structures

  • 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

Read more