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- EMDB-10769: Structure of a human 48S translational initiation complex - eIF3 -

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Basic information

Entry
Database: EMDB / ID: EMD-10769
TitleStructure of a human 48S translational initiation complex - eIF3
Map data
Sample
  • Complex: 48S initiation complex
    • Protein or peptide: x 19 types
KeywordseIF3 / ribosome / translation / initiation complex
Function / homology
Function and homology information


positive regulation of mRNA binding / viral translational termination-reinitiation / eukaryotic translation initiation factor 3 complex, eIF3e / cap-dependent translational initiation / eukaryotic translation initiation factor 3 complex, eIF3m / IRES-dependent viral translational initiation / translation reinitiation / formation of cytoplasmic translation initiation complex / eukaryotic translation initiation factor 3 complex / cytoplasmic translational initiation ...positive regulation of mRNA binding / viral translational termination-reinitiation / eukaryotic translation initiation factor 3 complex, eIF3e / cap-dependent translational initiation / eukaryotic translation initiation factor 3 complex, eIF3m / IRES-dependent viral translational initiation / translation reinitiation / formation of cytoplasmic translation initiation complex / eukaryotic translation initiation factor 3 complex / cytoplasmic translational initiation / multi-eIF complex / eukaryotic 43S preinitiation complex / mRNA cap binding / eukaryotic 48S preinitiation complex / metal-dependent deubiquitinase activity / negative regulation of RNA splicing / nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / regulation of translational initiation / neural crest cell differentiation / positive regulation of ubiquitin-protein transferase activity / rRNA modification in the nucleus and cytosol / erythrocyte homeostasis / Formation of the ternary complex, and subsequently, the 43S complex / cytoplasmic side of rough endoplasmic reticulum membrane / negative regulation of ubiquitin protein ligase activity / laminin receptor activity / Ribosomal scanning and start codon recognition / Translation initiation complex formation / fibroblast growth factor binding / SARS-CoV-1 modulates host translation machinery / Peptide chain elongation / Selenocysteine synthesis / Formation of a pool of free 40S subunits / positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator / endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / Eukaryotic Translation Termination / negative regulation of ubiquitin-dependent protein catabolic process / SRP-dependent cotranslational protein targeting to membrane / Response of EIF2AK4 (GCN2) to amino acid deficiency / ubiquitin ligase inhibitor activity / Viral mRNA Translation / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / GTP hydrolysis and joining of the 60S ribosomal subunit / L13a-mediated translational silencing of Ceruloplasmin expression / Major pathway of rRNA processing in the nucleolus and cytosol / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / Protein methylation / endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / laminin binding / rough endoplasmic reticulum / translation regulator activity / translation initiation factor binding / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / negative regulation of translational initiation / translation initiation factor activity / negative regulation of proteasomal ubiquitin-dependent protein catabolic process / antiviral innate immune response / Mitotic Prometaphase / EML4 and NUDC in mitotic spindle formation / cytosolic ribosome / Resolution of Sister Chromatid Cohesion / positive regulation of translation / erythrocyte differentiation / mRNA 3'-UTR binding / maturation of SSU-rRNA / neural tube closure / translational initiation / small-subunit processome / RHO GTPases Activate Formins / PML body / receptor tyrosine kinase binding / negative regulation of ERK1 and ERK2 cascade / mRNA 5'-UTR binding / GABA-ergic synapse / Regulation of expression of SLITs and ROBOs / fibrillar center / RMTs methylate histone arginines / metallopeptidase activity / rRNA processing / Separation of Sister Chromatids / presynapse / ribosome binding / virus receptor activity / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / small ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / SARS-CoV-2 modulates host translation machinery / microtubule / ubiquitinyl hydrolase 1 / cytoplasmic translation / cell differentiation / cysteine-type deubiquitinase activity / postsynaptic density / protein stabilization / structural constituent of ribosome / cadherin binding / ribosome / translation
Similarity search - Function
Eukaryotic translation initiation factor 3 subunit D / Eukaryotic translation initiation factor 3 subunit 7 (eIF-3) / Eukaryotic translation initiation factor 3 subunit H / eIF3h, C-terminal / C-terminal region of eIF3h / Eukaryotic translation initiation factor 3 subunit F / Translation initiation factor 3 complex subunit L / RNA polymerase I-associated factor PAF67 / Eukaryotic translation initiation factor 3 subunit M / eIF3 subunit M, C-terminal helix domain ...Eukaryotic translation initiation factor 3 subunit D / Eukaryotic translation initiation factor 3 subunit 7 (eIF-3) / Eukaryotic translation initiation factor 3 subunit H / eIF3h, C-terminal / C-terminal region of eIF3h / Eukaryotic translation initiation factor 3 subunit F / Translation initiation factor 3 complex subunit L / RNA polymerase I-associated factor PAF67 / Eukaryotic translation initiation factor 3 subunit M / eIF3 subunit M, C-terminal helix domain / eIF3 subunit 6 N terminal domain / eIF3 subunit M, C-terminal helix / Eukaryotic translation initiation factor 3 subunit E, C-terminal / Eukaryotic translation initiation factor 3 subunit E / Eukaryotic translation initiation factor 3 subunit E, N-terminal / eIF3 subunit 6 N terminal domain / Eukaryotic translation initiation factor 3 subunit K / Translation initiation factor 3, subunit 12, N-terminal, eukaryotic / : / eIF3a, PCI domain, TPR-like region / Eukaryotic translation initiation factor 3 subunit A / Eukaryotic translation initiation factor 3 subunit C, N-terminal domain / Eukaryotic translation initiation factor 3 subunit C / Eukaryotic translation initiation factor 3 subunit 8 N-terminus / Eukaryotic translation initiation factor 3 subunit M eIF3m/COP9 signalosome complex subunit 7 COPS7 / CSN8/PSMD8/EIF3K / CSN8/PSMD8/EIF3K family / Rpn11/EIF3F, C-terminal / Maintenance of mitochondrial structure and function / : / motif in proteasome subunits, Int-6, Nip-1 and TRIP-15 / PCI domain / Proteasome component (PCI) domain / PCI domain profile. / 40S ribosomal protein SA / 40S ribosomal protein SA, C-terminal domain / 40S ribosomal protein SA C-terminus / JAB1/Mov34/MPN/PAD-1 ubiquitin protease / : / Ribosomal protein S26e signature. / Ribosomal protein S21e, conserved site / Ribosomal protein S21e signature. / Ribosomal protein S26e / Ribosomal protein S26e superfamily / Ribosomal protein S26e / Ribosomal protein S5, eukaryotic/archaeal / Ribosomal protein S21e / Ribosomal protein S21e superfamily / Ribosomal protein S21e / Ribosomal protein S2, eukaryotic / JAB/MPN domain / JAB1/MPN/MOV34 metalloenzyme domain / : / Ribosomal protein S7e signature. / Ribosomal protein S17e, conserved site / Ribosomal protein S17e signature. / Ribosomal protein S2, eukaryotic/archaeal / Ribosomal protein S3Ae, conserved site / Ribosomal protein S3Ae signature. / MPN domain / MPN domain profile. / Ribosomal protein S27e signature. / Ribosomal protein S17e / Ribosomal protein S17e-like superfamily / Ribosomal S17 / 40S ribosomal protein S1/3, eukaryotes / Ribosomal protein S7e / Ribosomal protein S7e / Ribosomal protein S27 / Ribosomal protein S27, zinc-binding domain superfamily / Ribosomal protein S27 / Ribosomal protein S3Ae / Ribosomal S3Ae family / Ribosomal S3Ae family / Ribosomal protein S13/S15, N-terminal / Ribosomal protein S15P / Ribosomal S13/S15 N-terminal domain / Ribosomal S13/S15 N-terminal domain / Ribosomal protein S2 signature 2. / Ribosomal protein S2 signature 1. / Ribosomal protein S5, N-terminal, conserved site / Ribosomal protein S5 signature. / Ribosomal protein S2, conserved site / Ribosomal protein S2 / Ribosomal protein S2, flavodoxin-like domain superfamily / Ribosomal protein S2 / Ribosomal protein S5 / S5 double stranded RNA-binding domain profile. / Ribosomal protein S5, N-terminal / Ribosomal protein S5, C-terminal / Ribosomal protein S5, N-terminal domain / Ribosomal protein S5, C-terminal domain / Ribosomal protein S15 signature. / Tetratricopeptide-like helical domain superfamily / Ribosomal S11, conserved site / Ribosomal protein S11 signature. / Ribosomal protein S11 / Ribosomal protein S11 / Ribosomal protein S15 / Ribosomal_S15
Similarity search - Domain/homology
Eukaryotic translation initiation factor 3 subunit F / Eukaryotic translation initiation factor 3 subunit D / Eukaryotic translation initiation factor 3 subunit H / Small ribosomal subunit protein eS17 / Small ribosomal subunit protein uS2 / Small ribosomal subunit protein uS5 / Small ribosomal subunit protein eS27 / Eukaryotic translation initiation factor 3 subunit E / Small ribosomal subunit protein eS1 / Small ribosomal subunit protein eS7 ...Eukaryotic translation initiation factor 3 subunit F / Eukaryotic translation initiation factor 3 subunit D / Eukaryotic translation initiation factor 3 subunit H / Small ribosomal subunit protein eS17 / Small ribosomal subunit protein uS2 / Small ribosomal subunit protein uS5 / Small ribosomal subunit protein eS27 / Eukaryotic translation initiation factor 3 subunit E / Small ribosomal subunit protein eS1 / Small ribosomal subunit protein eS7 / Small ribosomal subunit protein uS11 / Small ribosomal subunit protein uS15 / Small ribosomal subunit protein eS26 / Small ribosomal subunit protein eS21 / Eukaryotic translation initiation factor 3 subunit A / Eukaryotic translation initiation factor 3 subunit M / Eukaryotic translation initiation factor 3 subunit C / Eukaryotic translation initiation factor 3 subunit K / Eukaryotic translation initiation factor 3 subunit L
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.3 Å
AuthorsBrito Querido J / Sokabe M
Funding support United Kingdom, United States, 3 items
OrganizationGrant numberCountry
Wellcome TrustWTY096570 United Kingdom
Medical Research Council (MRC, United Kingdom)MC_U105184332 United Kingdom
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01GM092927 United States
CitationJournal: Science / Year: 2020
Title: Structure of a human 48 translational initiation complex.
Authors: Jailson Brito Querido / Masaaki Sokabe / Sebastian Kraatz / Yuliya Gordiyenko / J Mark Skehel / Christopher S Fraser / V Ramakrishnan /
Abstract: A key step in translational initiation is the recruitment of the 43 preinitiation complex by the cap-binding complex [eukaryotic initiation factor 4F (eIF4F)] at the 5' end of messenger RNA (mRNA) to ...A key step in translational initiation is the recruitment of the 43 preinitiation complex by the cap-binding complex [eukaryotic initiation factor 4F (eIF4F)] at the 5' end of messenger RNA (mRNA) to form the 48 initiation complex (i.e., the 48). The 48 then scans along the mRNA to locate a start codon. To understand the mechanisms involved, we used cryo-electron microscopy to determine the structure of a reconstituted human 48 The structure reveals insights into early events of translation initiation complex assembly, as well as how eIF4F interacts with subunits of eIF3 near the mRNA exit channel in the 43 The location of eIF4F is consistent with a slotting model of mRNA recruitment and suggests that downstream mRNA is unwound at least in part by being "pulled" through the 40 subunit during scanning.
History
DepositionMar 16, 2020-
Header (metadata) releaseSep 16, 2020-
Map releaseSep 16, 2020-
UpdateMay 22, 2024-
Current statusMay 22, 2024Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.04
  • Imaged by UCSF Chimera
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  • Surface view colored by radius
  • Surface level: 0.04
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6ybd
  • Surface level: 0.04
  • Imaged by UCSF Chimera
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  • Simplified surface model + fitted atomic model
  • Atomic modelsPDB-6ybd
  • Imaged by Jmol
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_10769.png

Downloads & links

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Map

FileDownload / File: emd_10769.map.gz / Format: CCP4 / Size: 83.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.07 Å/pix.
x 280 pix.
= 300.72 Å		1.07 Å/pix.
x 280 pix.
= 300.72 Å		1.07 Å/pix.
x 280 pix.
= 300.72 Å

Surface

Projections

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.074 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.015 / Movie #1: 0.04
Minimum - Maximum-0.18092114 - 0.29472923
Average (Standard dev.)0.0009115565 (±0.00900954)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions280280280
Spacing280280280
CellA=B=C: 300.72 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.0741.0741.074
M x/y/z280280280
origin x/y/z0.0000.0000.000
length x/y/z300.720300.720300.720
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS280280280
D min/max/mean-0.1810.2950.001

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Supplemental data

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Mask #1

Fileemd_10769_msk_1.map
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Additional map: #1

Fileemd_10769_additional.map
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Half map: #1

Fileemd_10769_half_map_1.map
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Half map: #2

Fileemd_10769_half_map_2.map
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Sample components

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Entire : 48S initiation complex

EntireName: 48S initiation complex
Components
  • Complex: 48S initiation complex
    • Protein or peptide: Eukaryotic translation initiation factor 3 subunit M
    • Protein or peptide: Eukaryotic translation initiation factor 3 subunit F
    • Protein or peptide: Eukaryotic translation initiation factor 3 subunit A
    • Protein or peptide: Eukaryotic translation initiation factor 3 subunit E
    • Protein or peptide: Eukaryotic translation initiation factor 3 subunit C
    • Protein or peptide: Eukaryotic translation initiation factor 3 subunit H
    • Protein or peptide: 40S ribosomal protein S7
    • Protein or peptide: 40S ribosomal protein S27
    • Protein or peptide: 40S ribosomal protein S21
    • Protein or peptide: 40S ribosomal protein S17
    • Protein or peptide: 40S ribosomal protein S2
    • Protein or peptide: 40S ribosomal protein S3a
    • Protein or peptide: 40S ribosomal protein SA
    • Protein or peptide: 40S ribosomal protein S26
    • Protein or peptide: 40S ribosomal protein S14
    • Protein or peptide: 40S ribosomal protein S13
    • Protein or peptide: Eukaryotic translation initiation factor 3 subunit D
    • Protein or peptide: Eukaryotic translation initiation factor 3 subunit K
    • Protein or peptide: Eukaryotic translation initiation factor 3 subunit L

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Supramolecule #1: 48S initiation complex

SupramoleculeName: 48S initiation complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Eukaryotic translation initiation factor 3 subunit M

MacromoleculeName: Eukaryotic translation initiation factor 3 subunit M / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 42.555832 KDa
SequenceString: MSVPAFIDIS EEDQAAELRA YLKSKGAEIS EENSEGGLHV DLAQIIEACD VCLKEDDKDV ESVMNSVVSL LLILEPDKQE ALIESLCEK LVKFREGERP SLRLQLLSNL FHGMDKNTPV RYTVYCSLIK VAASCGAIQY IPTELDQVRK WISDWNLTTE K KHTLLRLL ...String:
MSVPAFIDIS EEDQAAELRA YLKSKGAEIS EENSEGGLHV DLAQIIEACD VCLKEDDKDV ESVMNSVVSL LLILEPDKQE ALIESLCEK LVKFREGERP SLRLQLLSNL FHGMDKNTPV RYTVYCSLIK VAASCGAIQY IPTELDQVRK WISDWNLTTE K KHTLLRLL YEALVDCKKS DAASKVMVEL LGSYTEDNAS QARVDAHRCI VRALKDPNAF LFDHLLTLKP VKFLEGELIH DL LTIFVSA KLASYVKFYQ NNKDFIDSLG LLHEQNMAKM RLLTFMGMAV ENKEISFDTM QQELQIGADD VEAFVIDAVR TKM VYCKID QTQRKVVVSH STHRTFGKQQ WQQLYDTLNA WKQNLNKVKN SLLSLSDT

UniProtKB: Eukaryotic translation initiation factor 3 subunit M

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Macromolecule #2: Eukaryotic translation initiation factor 3 subunit F

MacromoleculeName: Eukaryotic translation initiation factor 3 subunit F / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: ubiquitinyl hydrolase 1
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 37.593645 KDa
SequenceString: MATPAVPVSA PPATPTPVPA AAPASVPAPT PAPAAAPVPA AAPASSSDPA AAAAATAAPG QTPASAQAPA QTPAPALPGP ALPGPFPGG RVVRLHPVIL ASIVDSYERR NEGAARVIGT LLGTVDKHSV EVTNCFSVPH NESEDEVAVD MEFAKNMYEL H KKVSPNEL ...String:
MATPAVPVSA PPATPTPVPA AAPASVPAPT PAPAAAPVPA AAPASSSDPA AAAAATAAPG QTPASAQAPA QTPAPALPGP ALPGPFPGG RVVRLHPVIL ASIVDSYERR NEGAARVIGT LLGTVDKHSV EVTNCFSVPH NESEDEVAVD MEFAKNMYEL H KKVSPNEL ILGWYATGHD ITEHSVLIHE YYSREAPNPI HLTVDTSLQN GRMSIKAYVS TLMGVPGRTM GVMFTPLTVK YA YYDTERI GVDLIMKTCF SPNRVIGLSS DLQQVGGASA RIQDALSTVL QYAEDVLSGK VSADNTVGRF LMSLVNQVPK IVP DDFETM LNSNINDLLM VTYLANLTQS QIALNEKLVN L

UniProtKB: Eukaryotic translation initiation factor 3 subunit F

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Macromolecule #3: Eukaryotic translation initiation factor 3 subunit A

MacromoleculeName: Eukaryotic translation initiation factor 3 subunit A / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 166.903781 KDa
SequenceString: MPAYFQRPEN ALKRANEFLE VGKKQPALDV LYDVMKSKKH RTWQKIHEPI MLKYLELCVD LRKSHLAKEG LYQYKNICQQ VNIKSLEDV VRAYLKMAEE KTEAAKEESQ QMVLDIEDLD NIQTPESVLL SAVSGEDTQD RTDRLLLTPW VKFLWESYRQ C LDLLRNNS ...String:
MPAYFQRPEN ALKRANEFLE VGKKQPALDV LYDVMKSKKH RTWQKIHEPI MLKYLELCVD LRKSHLAKEG LYQYKNICQQ VNIKSLEDV VRAYLKMAEE KTEAAKEESQ QMVLDIEDLD NIQTPESVLL SAVSGEDTQD RTDRLLLTPW VKFLWESYRQ C LDLLRNNS RVERLYHDIA QQAFKFCLQY TRKAEFRKLC DNLRMHLSQI QRHHNQSTAI NLNNPESQSM HLETRLVQLD SA ISMELWQ EAFKAVEDIH GLFSLSKKPP KPQLMANYYN KVSTVFWKSG NALFHASTLH RLYHLSREMR KNLTQDEMQR MST RVLLAT LSIPITPERT DIARLLDMDG IIVEKQRRLA TLLGLQAPPT RIGLINDMVR FNVLQYVVPE VKDLYNWLEV EFNP LKLCE RVTKVLNWVR EQPEKEPELQ QYVPQLQNNT ILRLLQQVSQ IYQSIEFSRL TSLVPFVDAF QLERAIVDAA RHCDL QVRI DHTSRTLSFG SDLNYATRED APIGPHLQSM PSEQIRNQLT AMSSVLAKAL EVIKPAHILQ EKEEQHQLAV TAYLKN SRK EHQRILARRQ TIEERKERLE SLNIQREKEE LEQREAELQK VRKAEEERLR QEAKEREKER ILQEHEQIKK KTVRERL EQ IKKTELGAKA FKDIDIEDLE ELDPDFIMAK QVEQLEKEKK ELQERLKNQE KKIDYFERAK RLEEIPLIKS AYEEQRIK D MDLWEQQEEE RITTMQLERE KALEHKNRMS RMLEDRDLFV MRLKAARQSV YEEKLKQFEE RLAEERHNRL EERKRQRKE ERRITYYREK EEEEQRRAEE QMLKEREERE RAERAKREEE LREYQERVKK LEEVERKKRQ RELEIEERER RREEERRLGD SSLSRKDSR WGDRDSEGTW RKGPEADSEW RRGPPEKEWR RGEGRDEDRS HRRDEERPRR LGDDEDREPS LRPDDDRVPR R GMDDDRGP RRGPEEDRFS RRGADDDRPS WRNTDDDRPP RRIADEDRGN WRHADDDRPP RRGLDEDRGS WRTADEDRGP RR GMDDDRG PRRGGADDER SSWRNADDDR GPRRGLDDDR GPRRGMDDDR GPRRGMDDDR GPRRGMDDDR GPRRGLDDDR GPW RNADDD RIPRRGAEDD RGPWRNMDDD RLSRRADDDR FPRRGDDSRP GPWRPLVKPG GWREKEKARE ESWGPPRESR PSEE REWDR EKERDRDNQD REENDKDPER ERDRERDVDR EDRFRRPRDE GGWRRGPAEE SSSWRDSSRR DDRDRDDRRR ERDDR RDLR ERRDLRDDRD RRGPPLRSER EEVSSWRRAD DRKDDRVEER DPPRRVPPPA LSRDRERDRD REREGEKEKA SWRAEK DRE SLRRTKNETD EDGWTTVRR

UniProtKB: Eukaryotic translation initiation factor 3 subunit A

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Macromolecule #4: Eukaryotic translation initiation factor 3 subunit E

MacromoleculeName: Eukaryotic translation initiation factor 3 subunit E / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 52.281633 KDa
SequenceString: MAEYDLTTRI AHFLDRHLVF PLLEFLSVKE IYNEKELLQG KLDLLSDTNM VDFAMDVYKN LYSDDIPHAL REKRTTVVAQ LKQLQAETE PIVKMFEDPE TTRQMQSTRD GRMLFDYLAD KHGFRQEYLD TLYRYAKFQY ECGNYSGAAE YLYFFRVLVP A TDRNALSS ...String:
MAEYDLTTRI AHFLDRHLVF PLLEFLSVKE IYNEKELLQG KLDLLSDTNM VDFAMDVYKN LYSDDIPHAL REKRTTVVAQ LKQLQAETE PIVKMFEDPE TTRQMQSTRD GRMLFDYLAD KHGFRQEYLD TLYRYAKFQY ECGNYSGAAE YLYFFRVLVP A TDRNALSS LWGKLASEIL MQNWDAAMED LTRLKETIDN NSVSSPLQSL QQRTWLIHWS LFVFFNHPKG RDNIIDLFLY QP QYLNAIQ TMCPHILRYL TTAVITNKDV RKRRQVLKDL VKVIQQESYT YKDPITEFVE CLYVNFDFDG AQKKLRECES VLV NDFFLV ACLEDFIENA RLFIFETFCR IHQCISINML ADKLNMTPEE AERWIVNLIR NARLDAKIDS KLGHVVMGNN AVSP YQQVI EKTKSLSFRS QMLAMNIEKK LNQNSRSEAP NWATQDSGFY

UniProtKB: Eukaryotic translation initiation factor 3 subunit E

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Macromolecule #5: Eukaryotic translation initiation factor 3 subunit C

MacromoleculeName: Eukaryotic translation initiation factor 3 subunit C / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 105.503945 KDa
SequenceString: MSRFFTTGSD SESESSLSGE ELVTKPVGGN YGKQPLLLSE DEEDTKRVVR SAKDKRFEEL TNLIRTIRNA MKIRDVTKCL EEFELLGKA YGKAKSIVDK EGVPRFYIRI LADLEDYLNE LWEDKEGKKK MNKNNAKALS TLRQKIRKYN RDFESHITSY K QNPEQSAD ...String:
MSRFFTTGSD SESESSLSGE ELVTKPVGGN YGKQPLLLSE DEEDTKRVVR SAKDKRFEEL TNLIRTIRNA MKIRDVTKCL EEFELLGKA YGKAKSIVDK EGVPRFYIRI LADLEDYLNE LWEDKEGKKK MNKNNAKALS TLRQKIRKYN RDFESHITSY K QNPEQSAD EDAEKNEEDS EGSSDEDEDE DGVSAATFLK KKSEAPSGES RKFLKKMDDE DEDSEDSEDD EDWDTGSTSS DS DSEEEEG KQTALASRFL KKAPTTDEDK KAAEKKREDK AKKKHDRKSK RLDEEEEDNE GGEWERVRGG VPLVKEKPKM FAK GTEITH AVVIKKLNEI LQARGKKGTD RAAQIELLQL LVQIAAENNL GEGVIVKIKF NIIASLYDYN PNLATYMKPE MWGK CLDCI NELMDILFAN PNIFVGENIL EESENLHNAD QPLRVRGCIL TLVERMDEEF TKIMQNTDPH SQEYVEHLKD EAQVC AIIE RVQRYLEEKG TTEEVCRIYL LRILHTYYKF DYKAHQRQLT PPEGSSKSEQ DQAENEGEDS AVLMERLCKY IYAKDR TDR IRTCAILCHI YHHALHSRWY QARDLMLMSH LQDNIQHADP PVQILYNRTM VQLGICAFRQ GLTKDAHNAL LDIQSSG RA KELLGQGLLL RSLQERNQEQ EKVERRRQVP FHLHINLELL ECVYLVSAML LEIPYMAAHE SDARRRMISK QFHHQLRV G ERQPLLGPPE SMREHVVAAS KAMKMGDWKT CHSFIINEKM NGKVWDLFPE ADKVRTMLVR KIQEESLRTY LFTYSSVYD SISMETLSDM FELDLPTVHS IISKMIINEE LMASLDQPTQ TVVMHRTEPT AQQNLALQLA EKLGSLVENN ERVFDHKQGT YGGYFRDQK DGYRKNEGYM RRGGYRQQQS QTAY

UniProtKB: Eukaryotic translation initiation factor 3 subunit C

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Macromolecule #6: Eukaryotic translation initiation factor 3 subunit H

MacromoleculeName: Eukaryotic translation initiation factor 3 subunit H / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 39.979277 KDa
SequenceString: MASRKEGTGS TATSSSSTAG AAGKGKGKGG SGDSAVKQVQ IDGLVVLKII KHYQEEGQGT EVVQGVLLGL VVEDRLEITN CFPFPQHTE DDADFDEVQY QMEMMRSLRH VNIDHLHVGW YQSTYYGSFV TRALLDSQFS YQHAIEESVV LIYDPIKTAQ G SLSLKAYR ...String:
MASRKEGTGS TATSSSSTAG AAGKGKGKGG SGDSAVKQVQ IDGLVVLKII KHYQEEGQGT EVVQGVLLGL VVEDRLEITN CFPFPQHTE DDADFDEVQY QMEMMRSLRH VNIDHLHVGW YQSTYYGSFV TRALLDSQFS YQHAIEESVV LIYDPIKTAQ G SLSLKAYR LTPKLMEVCK EKDFSPEALK KANITFEYMF EEVPIVIKNS HLINVLMWEL EKKSAVADKH ELLSLASSNH LG KNLQLLM DRVDEMSQDI VKYNTYMRNT SKQQQQKHQY QQRRQQENMQ RQSRGEPPLP EEDLSKLFKP PQPPARMDSL LIA GQINTY CQNIKEFTAQ NLGKLFMAQA LQEYNN

UniProtKB: Eukaryotic translation initiation factor 3 subunit H

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Macromolecule #7: 40S ribosomal protein S7

MacromoleculeName: 40S ribosomal protein S7 / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 22.168914 KDa
SequenceString: MFSSSAKIVK PNGEKPDEFE SGISQALLEL EMNSDLKAQL RELNITAAKE IEVGGGRKAI IIFVPVPQLK SFQKIQVRLV RELEKKFSG KHVVFIAQRR ILPKPTRKSR TKNKQKRPRS RTLTAVHDAI LEDLVFPSEI VGKRIRVKLD GSRLIKVHLD K AQQNNVEH ...String:
MFSSSAKIVK PNGEKPDEFE SGISQALLEL EMNSDLKAQL RELNITAAKE IEVGGGRKAI IIFVPVPQLK SFQKIQVRLV RELEKKFSG KHVVFIAQRR ILPKPTRKSR TKNKQKRPRS RTLTAVHDAI LEDLVFPSEI VGKRIRVKLD GSRLIKVHLD K AQQNNVEH KVETFSGVYK KLTGKDVNFE FPEFQL

UniProtKB: Small ribosomal subunit protein eS7

+
Macromolecule #8: 40S ribosomal protein S27

MacromoleculeName: 40S ribosomal protein S27 / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 9.480186 KDa
SequenceString:
MPLAKDLLHP SPEEEKRKHK KKRLVQSPNS YFMDVKCPGC YKITTVFSHA QTVVLCVGCS TVLCQPTGGK ARLTEGCSFR RKQH

UniProtKB: Small ribosomal subunit protein eS27

+
Macromolecule #9: 40S ribosomal protein S21

MacromoleculeName: 40S ribosomal protein S21 / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 9.124389 KDa
SequenceString:
MQNDAGEFVD LYVPRKCSAS NRIIGAKDHA SIQMNVAEVD KVTGRFNGQF KTYAICGAIR RMGESDDSIL RLAKADGIVS KNF

UniProtKB: Small ribosomal subunit protein eS21

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Macromolecule #10: 40S ribosomal protein S17

MacromoleculeName: 40S ribosomal protein S17 / type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 15.578156 KDa
SequenceString:
MGRVRTKTVK KAARVIIEKY YTRLGNDFHT NKRVCEEIAI IPSKKLRNKI AGYVTHLMKR IQRGPVRGIS IKLQEEERER RDNYVPEVS ALDQEIIEVD PDTKEMLKLL DFGSLSNLQV TQPTVGMNFK TPRGPV

UniProtKB: Small ribosomal subunit protein eS17

+
Macromolecule #11: 40S ribosomal protein S2

MacromoleculeName: 40S ribosomal protein S2 / type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 31.376516 KDa
SequenceString: MADDAGAAGG PGGPGGPGMG NRGGFRGGFG SGIRGRGRGR GRGRGRGRGA RGGKAEDKEW MPVTKLGRLV KDMKIKSLEE IYLFSLPIK ESEIIDFFLG ASLKDEVLKI MPVQKQTRAG QRTRFKAFVA IGDYNGHVGL GVKCSKEVAT AIRGAIILAK L SIVPVRRG ...String:
MADDAGAAGG PGGPGGPGMG NRGGFRGGFG SGIRGRGRGR GRGRGRGRGA RGGKAEDKEW MPVTKLGRLV KDMKIKSLEE IYLFSLPIK ESEIIDFFLG ASLKDEVLKI MPVQKQTRAG QRTRFKAFVA IGDYNGHVGL GVKCSKEVAT AIRGAIILAK L SIVPVRRG YWGNKIGKPH TVPCKVTGRC GSVLVRLIPA PRGTGIVSAP VPKKLLMMAG IDDCYTSARG CTATLGNFAK AT FDAISKT YSYLTPDLWK ETVFTKSPYQ EFTDHLVKTH TRVSVQRTQA PAVATT

UniProtKB: Small ribosomal subunit protein uS5

+
Macromolecule #12: 40S ribosomal protein S3a

MacromoleculeName: 40S ribosomal protein S3a / type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 30.002061 KDa
SequenceString: MAVGKNKRLT KGGKKGAKKK VVDPFSKKDW YDVKAPAMFN IRNIGKTLVT RTQGTKIASD GLKGRVFEVS LADLQNDEVA FRKFKLITE DVQGKNCLTN FHGMDLTRDK MCSMVKKWQT MIEAHVDVKT TDGYLLRLFC VGFTKKRNNQ IRKTSYAQHQ Q VRQIRKKM ...String:
MAVGKNKRLT KGGKKGAKKK VVDPFSKKDW YDVKAPAMFN IRNIGKTLVT RTQGTKIASD GLKGRVFEVS LADLQNDEVA FRKFKLITE DVQGKNCLTN FHGMDLTRDK MCSMVKKWQT MIEAHVDVKT TDGYLLRLFC VGFTKKRNNQ IRKTSYAQHQ Q VRQIRKKM MEIMTREVQT NDLKEVVNKL IPDSIGKDIE KACQSIYPLH DVFVRKVKML KKPKFELGKL MELHGEGSSS GK ATGDETG AKVERADGYE PPVQESV

UniProtKB: Small ribosomal subunit protein eS1

+
Macromolecule #13: 40S ribosomal protein SA

MacromoleculeName: 40S ribosomal protein SA / type: protein_or_peptide / ID: 13 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 32.883938 KDa
SequenceString: MSGALDVLQM KEEDVLKFLA AGTHLGGTNL DFQMEQYIYK RKSDGIYIIN LKRTWEKLLL AARAIVAIEN PADVSVISSR NTGQRAVLK FAAATGATPI AGRFTPGTFT NQIQAAFREP RLLVVTDPRA DHQPLTEASY VNLPTIALCN TDSPLRYVDI A IPCNNKGA ...String:
MSGALDVLQM KEEDVLKFLA AGTHLGGTNL DFQMEQYIYK RKSDGIYIIN LKRTWEKLLL AARAIVAIEN PADVSVISSR NTGQRAVLK FAAATGATPI AGRFTPGTFT NQIQAAFREP RLLVVTDPRA DHQPLTEASY VNLPTIALCN TDSPLRYVDI A IPCNNKGA HSVGLMWWML AREVLRMRGT ISREHPWEVM PDLYFYRDPE EIEKEEQAAA EKAVTKEEFQ GEWTAPAPEF TA TQPEVAD WSEGVQVPSV PIQQFPTEDW SAQPATEDWS AAPTAQATEW VGATTDWS

UniProtKB: Small ribosomal subunit protein uS2

+
Macromolecule #14: 40S ribosomal protein S26

MacromoleculeName: 40S ribosomal protein S26 / type: protein_or_peptide / ID: 14 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 13.047532 KDa
SequenceString:
MTKKRRNNGR AKKGRGHVQP IRCTNCARCV PKDKAIKKFV IRNIVEAAAV RDISEASVFD AYVLPKLYVK LHYCVSCAIH SKVVRNRSR EARKDRTPPP RFRPAGAAPR PPPKPM

UniProtKB: Small ribosomal subunit protein eS26

+
Macromolecule #15: 40S ribosomal protein S14

MacromoleculeName: 40S ribosomal protein S14 / type: protein_or_peptide / ID: 15 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 16.302772 KDa
SequenceString:
MAPRKGKEKK EEQVISLGPQ VAEGENVFGV CHIFASFNDT FVHVTDLSGK ETICRVTGGM KVKADRDESS PYAAMLAAQD VAQRCKELG ITALHIKLRA TGGNRTKTPG PGAQSALRAL ARSGMKIGRI EDVTPIPSDS TRRKGGRRGR RL

UniProtKB: Small ribosomal subunit protein uS11

+
Macromolecule #16: 40S ribosomal protein S13

MacromoleculeName: 40S ribosomal protein S13 / type: protein_or_peptide / ID: 16 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 17.259389 KDa
SequenceString:
MGRMHAPGKG LSQSALPYRR SVPTWLKLTS DDVKEQIYKL AKKGLTPSQI GVILRDSHGV AQVRFVTGNK ILRILKSKGL APDLPEDLY HLIKKAVAVR KHLERNRKDK DAKFRLILIE SRIHRLARYY KTKRVLPPNW KYESSTASAL VA

UniProtKB: Small ribosomal subunit protein uS15

+
Macromolecule #17: Eukaryotic translation initiation factor 3 subunit D

MacromoleculeName: Eukaryotic translation initiation factor 3 subunit D / type: protein_or_peptide / ID: 17 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 64.060758 KDa
SequenceString: MAKFMTPVIQ DNPSGWGPCA VPEQFRDMPY QPFSKGDRLG KVADWTGATY QDKRYTNKYS SQFGGGSQYA YFHEEDESSF QLVDTARTQ KTAYQRNRMR FAQRNLRRDK DRRNMLQFNL QILPKSAKQK ERERIRLQKK FQKQFGVRQK WDQKSQKPRD S SVEVRSDW ...String:
MAKFMTPVIQ DNPSGWGPCA VPEQFRDMPY QPFSKGDRLG KVADWTGATY QDKRYTNKYS SQFGGGSQYA YFHEEDESSF QLVDTARTQ KTAYQRNRMR FAQRNLRRDK DRRNMLQFNL QILPKSAKQK ERERIRLQKK FQKQFGVRQK WDQKSQKPRD S SVEVRSDW EVKEEMDFPQ LMKMRYLEVS EPQDIECCGA LEYYDKAFDR ITTRSEKPLR SIKRIFHTVT TTDDPVIRKL AK TQGNVFA TDAILATLMS CTRSVYSWDI VVQRVGSKLF FDKRDNSDFD LLTVSETANE PPQDEGNSFN SPRNLAMEAT YIN HNFSQQ CLRMGKERYN FPNPNPFVED DMDKNEIASV AYRYRRWKLG DDIDLIVRCE HDGVMTGANG EVSFINIKTL NEWD SRHCN GVDWRQKLDS QRGAVIATEL KNNSYKLARW TCCALLAGSE YLKLGYVSRY HVKDSSRHVI LGTQQFKPNE FASQI NLSV ENAWGILRCV IDICMKLEEG KYLILKDPNK QVIRVYSLPD GTFSSDEDEE EEEEEEEEEE EEET

UniProtKB: Eukaryotic translation initiation factor 3 subunit D

+
Macromolecule #18: Eukaryotic translation initiation factor 3 subunit K

MacromoleculeName: Eukaryotic translation initiation factor 3 subunit K / type: protein_or_peptide / ID: 18 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 25.083619 KDa
SequenceString: MAMFEQMRAN VGKLLKGIDR YNPENLATLE RYVETQAKEN AYDLEANLAV LKLYQFNPAF FQTTVTAQIL LKALTNLPHT DFTLCKCMI DQAHQEERPI RQILYLGDLL ETCHFQAFWQ ALDENMDLLE GITGFEDSVR KFICHVVGIT YQHIDRWLLA E MLGDLSDS ...String:
MAMFEQMRAN VGKLLKGIDR YNPENLATLE RYVETQAKEN AYDLEANLAV LKLYQFNPAF FQTTVTAQIL LKALTNLPHT DFTLCKCMI DQAHQEERPI RQILYLGDLL ETCHFQAFWQ ALDENMDLLE GITGFEDSVR KFICHVVGIT YQHIDRWLLA E MLGDLSDS QLKVWMSKYG WSADESGQIF ICSQEESIKP KNIVEKIDFD SVSSIMASSQ

UniProtKB: Eukaryotic translation initiation factor 3 subunit K

+
Macromolecule #19: Eukaryotic translation initiation factor 3 subunit L

MacromoleculeName: Eukaryotic translation initiation factor 3 subunit L / type: protein_or_peptide / ID: 19 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 66.803734 KDa
SequenceString: MSYPADDYES EAAYDPYAYP SDYDMHTGDP KQDLAYERQY EQQTYQVIPE VIKNFIQYFH KTVSDLIDQK VYELQASRVS SDVIDQKVY EIQDIYENSW TKLTERFFKN TPWPEAEAIA PQVGNDAVFL ILYKELYYRH IYAKVSGGPS LEQRFESYYN Y CNLFNYIL ...String:
MSYPADDYES EAAYDPYAYP SDYDMHTGDP KQDLAYERQY EQQTYQVIPE VIKNFIQYFH KTVSDLIDQK VYELQASRVS SDVIDQKVY EIQDIYENSW TKLTERFFKN TPWPEAEAIA PQVGNDAVFL ILYKELYYRH IYAKVSGGPS LEQRFESYYN Y CNLFNYIL NADGPAPLEL PNQWLWDIID EFIYQFQSFS QYRCKTAKKS EEEIDFLRSN PKIWNVHSVL NVLHSLVDKS NI NRQLEVY TSGGDPESVA GEYGRHSLYK MLGYFSLVGL LRLHSLLGDY YQAIKVLENI ELNKKSMYSR VPECQVTTYY YVG FAYLMM RRYQDAIRVF ANILLYIQRT KSMFQRTTYK YEMINKQNEQ MHALLAIALT MYPMRIDESI HLQLREKYGD KMLR MQKGD PQVYEELFSY SCPKFLSPVV PNYDNVHPNY HKEPFLQQLK VFSDEVQQQA QLSTIRSFLK LYTTMPVAKL AGFLD LTEQ EFRIQLLVFK HKMKNLVWTS GISALDGEFQ SASEVDFYID KDMIHIADTK VARRYGDFFI RQIHKFEELN RTLKKM GQR P

UniProtKB: Eukaryotic translation initiation factor 3 subunit L

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

BufferpH: 7.4
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: FEI FALCON III (4k x 4k) / Detector mode: INTEGRATING / Average exposure time: 1.0 sec. / Average electron dose: 107.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

+
Image processing

Startup modelType of model: PDB ENTRY
PDB model - PDB ID:

4kzy

Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.3 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 11882
Initial angle assignmentType: OTHER
Final angle assignmentType: OTHER
FSC plot (resolution estimation)

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