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- EMDB-19128: Structure of human eIF3 core from closed 48S translation initiati... -

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Basic information

Entry
Database: EMDB / ID: EMD-19128
TitleStructure of human eIF3 core from closed 48S translation initiation complex
Map data
Sample
  • Complex: Human 48S initiation complex 40S-eIF1-eIF1A-eIF2-eIF3-tRNA-Met-mRNA
    • Complex: Human 48S initiation complex 40S-eIF1-eIF1A-eIF2-eIF3-tRNA-Met
      • Protein or peptide: x 17 types
      • RNA: x 1 types
    • Complex: mRNA
      • RNA: x 1 types
  • Ligand: x 2 types
KeywordsRIBOSOME / TRANSLATION / initiation / 48S / eIF / human / eukaryotic / factor / codon / scanning / open / reading
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 / eukaryotic translation initiation factor 3 complex / formation of cytoplasmic translation initiation 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 / eukaryotic translation initiation factor 3 complex / formation of cytoplasmic translation initiation complex / cytoplasmic translational initiation / multi-eIF complex / eukaryotic 43S preinitiation complex / mRNA cap binding / eukaryotic 48S preinitiation complex / translation at postsynapse / negative regulation of RNA splicing / metal-dependent deubiquitinase activity / regulation of translational initiation / nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / translation at presynapse / Formation of the ternary complex, and subsequently, the 43S complex / erythrocyte homeostasis / rRNA modification in the nucleus and cytosol / cytoplasmic side of rough endoplasmic reticulum membrane / laminin receptor activity / Ribosomal scanning and start codon recognition / Translation initiation complex formation / SARS-CoV-1 modulates host translation machinery / Peptide chain elongation / Selenocysteine synthesis / Formation of a pool of free 40S subunits / Eukaryotic Translation Termination / Response of EIF2AK4 (GCN2) to amino acid deficiency / SRP-dependent cotranslational protein targeting to membrane / 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) / laminin binding / translation regulator activity / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / translation initiation factor binding / negative regulation of translational initiation / negative regulation of proteasomal ubiquitin-dependent protein catabolic process / cytosolic ribosome / Mitotic Prometaphase / antiviral innate immune response / EML4 and NUDC in mitotic spindle formation / translation initiation factor activity / Resolution of Sister Chromatid Cohesion / erythrocyte differentiation / positive regulation of translation / maturation of SSU-rRNA / translational initiation / small-subunit processome / RHO GTPases Activate Formins / PML body / mRNA 5'-UTR binding / Regulation of expression of SLITs and ROBOs / fibrillar center / metallopeptidase activity / rRNA processing / Separation of Sister Chromatids / ribosome biogenesis / presynapse / ribosome binding / virus receptor activity / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / cytosolic small ribosomal subunit / small ribosomal subunit rRNA binding / SARS-CoV-2 modulates host translation machinery / ubiquitinyl hydrolase 1 / cysteine-type deubiquitinase activity / cytoplasmic translation / cell differentiation / postsynaptic density / ribosome / structural constituent of ribosome / cadherin binding / translation / ribonucleoprotein complex / focal adhesion / mRNA binding / synapse / negative regulation of apoptotic process / chromatin / nucleolus / structural molecule activity / negative regulation of transcription by RNA polymerase II / endoplasmic reticulum / proteolysis / DNA binding / RNA binding / extracellular exosome / zinc ion binding / nucleoplasm
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 / Eukaryotic translation initiation factor 3 subunit M eIF3m/COP9 signalosome complex subunit 7 COPS7 / : / 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 / 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 S26e / Ribosomal protein S26e superfamily / Ribosomal protein S26e / Ribosomal protein S2, eukaryotic / Ribosomal protein S17e, conserved site / Ribosomal protein S17e signature. / Ribosomal protein S3Ae, conserved site / Ribosomal protein S3Ae signature. / Ribosomal protein S2, eukaryotic/archaeal / Ribosomal protein S27e signature. / JAB/MPN domain / JAB1/MPN/MOV34 metalloenzyme domain / 40S ribosomal protein S1/3, eukaryotes / Ribosomal protein S17e / Ribosomal protein S17e-like superfamily / Ribosomal S17 / MPN domain / MPN domain profile. / Ribosomal protein S27 / Ribosomal protein S27, zinc-binding domain superfamily / Ribosomal protein S27 / Ribosomal protein S3Ae / Ribosomal S3Ae family / Ribosomal S3Ae family / Ribosomal protein S28e conserved site / Ribosomal protein S28e signature. / Ribosomal protein S28e / Ribosomal protein S28e / 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 S2, conserved site / Ribosomal protein S2 / Ribosomal protein S2, flavodoxin-like domain superfamily / Ribosomal protein S2 / 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 / Ribosomal protein S15 / Ribosomal protein S11 superfamily / S15/NS1, RNA-binding / Zinc-binding ribosomal protein / Armadillo-type fold / Winged helix DNA-binding domain superfamily / Winged helix-like DNA-binding domain superfamily / Nucleic acid-binding, OB-fold
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 eS27 / Eukaryotic translation initiation factor 3 subunit E / Small ribosomal subunit protein eS1 / Small ribosomal subunit protein uS11 / Small ribosomal subunit protein uS15 ...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 eS27 / Eukaryotic translation initiation factor 3 subunit E / Small ribosomal subunit protein eS1 / Small ribosomal subunit protein uS11 / Small ribosomal subunit protein uS15 / Small ribosomal subunit protein eS26 / Small ribosomal subunit protein eS28 / 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: 3.4 Å
AuthorsPetrychenko V / Yi S-H / Liedtke D / Peng BZ / Rodnina MV / Fischer N
Funding support Germany, 2 items
OrganizationGrant numberCountry
Max Planck Society Germany
German Research Foundation (DFG)Leibniz-Preis Germany
CitationJournal: Nat Struct Mol Biol / Year: 2025
Title: Structural basis for translational control by the human 48S initiation complex.
Authors: Valentyn Petrychenko / Sung-Hui Yi / David Liedtke / Bee-Zen Peng / Marina V Rodnina / Niels Fischer /
Abstract: The selection of an open reading frame (ORF) for translation of eukaryotic mRNA relies on remodeling of the scanning 48S initiation complex into an elongation-ready 80S ribosome. Using cryo-electron ...The selection of an open reading frame (ORF) for translation of eukaryotic mRNA relies on remodeling of the scanning 48S initiation complex into an elongation-ready 80S ribosome. Using cryo-electron microscopy, we visualize the key commitment steps orchestrating 48S remodeling in humans. The mRNA Kozak sequence facilitates mRNA scanning in the 48S open state and stabilizes the 48S closed state by organizing the contacts of eukaryotic initiation factors (eIFs) and ribosomal proteins and by reconfiguring mRNA structure. GTPase-triggered large-scale fluctuations of 48S-bound eIF2 facilitate eIF5B recruitment, transfer of initiator tRNA from eIF2 to eIF5B and the release of eIF5 and eIF2. The 48S-bound multisubunit eIF3 complex controls ribosomal subunit joining by coupling eIF exchange to gradual displacement of the eIF3c N-terminal domain from the intersubunit interface. These findings reveal the structural mechanism of ORF selection in human cells and explain how eIF3 could function in the context of the 80S ribosome.
History
DepositionDec 13, 2023-
Header (metadata) releaseAug 14, 2024-
Map releaseAug 14, 2024-
UpdateJan 29, 2025-
Current statusJan 29, 2025Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_19128.png

Downloads & links

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Map

FileDownload / File: emd_19128.map.gz / Format: CCP4 / Size: 52.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

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Size
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AxesZ (Sec.)Y (Row.)X (Col.)
1.16 Å/pix.
x 240 pix.
= 278.4 Å		1.16 Å/pix.
x 240 pix.
= 278.4 Å		1.16 Å/pix.
x 240 pix.
= 278.4 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.16 Å
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Contour LevelBy AUTHOR: 4.0
Minimum - Maximum-15.71841 - 34.833424000000001
Average (Standard dev.)-0.000000000012867 (±1.0)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions240240240
Spacing240240240
CellA=B=C: 278.4 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_19128_msk_1.map
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Additional map: Map from focused flexible refinement with improved density...

Fileemd_19128_additional_1.map
AnnotationMap from focused flexible refinement with improved density for eIF3k/l
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Additional map: Unsharpened main map from 3D refinement step

Fileemd_19128_additional_2.map
AnnotationUnsharpened main map from 3D refinement step
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Half map: #2

Fileemd_19128_half_map_1.map
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Half map: #1

Fileemd_19128_half_map_2.map
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Sample components

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Entire : Human 48S initiation complex 40S-eIF1-eIF1A-eIF2-eIF3-tRNA-Met-mRNA

EntireName: Human 48S initiation complex 40S-eIF1-eIF1A-eIF2-eIF3-tRNA-Met-mRNA
Components
  • Complex: Human 48S initiation complex 40S-eIF1-eIF1A-eIF2-eIF3-tRNA-Met-mRNA
    • Complex: Human 48S initiation complex 40S-eIF1-eIF1A-eIF2-eIF3-tRNA-Met
      • Protein or peptide: Eukaryotic translation initiation factor 3 subunit K
      • Protein or peptide: Eukaryotic translation initiation factor 3 subunit F
      • Protein or peptide: Eukaryotic translation initiation factor 3 subunit L
      • Protein or peptide: Eukaryotic translation initiation factor 3 subunit M
      • Protein or peptide: Eukaryotic translation initiation factor 3 subunit H
      • RNA: 18S rRNA
      • Protein or peptide: 40S ribosomal protein S27
      • Protein or peptide: 40S ribosomal protein S13
      • Protein or peptide: 40S ribosomal protein S17
      • Protein or peptide: 40S ribosomal protein SA
      • Protein or peptide: 40S ribosomal protein S3a
      • Protein or peptide: 40S ribosomal protein S14
      • Protein or peptide: 40S ribosomal protein S26
      • Protein or peptide: 40S ribosomal protein S28
      • 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 D
      • Protein or peptide: Eukaryotic translation initiation factor 3 subunit C
    • Complex: mRNA
      • RNA: mRNA
  • Ligand: MAGNESIUM ION
  • Ligand: ZINC ION

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Supramolecule #1: Human 48S initiation complex 40S-eIF1-eIF1A-eIF2-eIF3-tRNA-Met-mRNA

SupramoleculeName: Human 48S initiation complex 40S-eIF1-eIF1A-eIF2-eIF3-tRNA-Met-mRNA
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#19

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Supramolecule #2: Human 48S initiation complex 40S-eIF1-eIF1A-eIF2-eIF3-tRNA-Met

SupramoleculeName: Human 48S initiation complex 40S-eIF1-eIF1A-eIF2-eIF3-tRNA-Met
type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#4, #6-#19
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #3: mRNA

SupramoleculeName: mRNA / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #5
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Eukaryotic translation initiation factor 3 subunit K

MacromoleculeName: Eukaryotic translation initiation factor 3 subunit K / type: protein_or_peptide / ID: 1 / 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

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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 L

MacromoleculeName: Eukaryotic translation initiation factor 3 subunit L / type: protein_or_peptide / ID: 3 / 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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Macromolecule #4: Eukaryotic translation initiation factor 3 subunit M

MacromoleculeName: Eukaryotic translation initiation factor 3 subunit M / type: protein_or_peptide / ID: 4 / 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 #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 #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

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Macromolecule #9: 40S ribosomal protein S13

MacromoleculeName: 40S ribosomal protein S13 / type: protein_or_peptide / ID: 9 / 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

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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

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Macromolecule #11: 40S ribosomal protein SA

MacromoleculeName: 40S ribosomal protein SA / type: protein_or_peptide / ID: 11 / 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

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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

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Macromolecule #13: 40S ribosomal protein S14

MacromoleculeName: 40S ribosomal protein S14 / type: protein_or_peptide / ID: 13 / 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

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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

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Macromolecule #15: 40S ribosomal protein S28

MacromoleculeName: 40S ribosomal protein S28 / type: protein_or_peptide / ID: 15 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 7.855052 KDa
SequenceString:
MDTSRVQPIK LARVTKVLGR TGSQGQCTQV RVEFMDDTSR SIIRNVKGPV REGDVLTLLE SEREARRLR

UniProtKB: Small ribosomal subunit protein eS28

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Macromolecule #16: Eukaryotic translation initiation factor 3 subunit A

MacromoleculeName: Eukaryotic translation initiation factor 3 subunit A / type: protein_or_peptide / ID: 16 / 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 #17: Eukaryotic translation initiation factor 3 subunit E

MacromoleculeName: Eukaryotic translation initiation factor 3 subunit E / type: protein_or_peptide / ID: 17 / 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 #18: Eukaryotic translation initiation factor 3 subunit D

MacromoleculeName: Eukaryotic translation initiation factor 3 subunit D / type: protein_or_peptide / ID: 18 / 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

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Macromolecule #19: Eukaryotic translation initiation factor 3 subunit C

MacromoleculeName: Eukaryotic translation initiation factor 3 subunit C / type: protein_or_peptide / ID: 19 / 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 #5: mRNA

MacromoleculeName: mRNA / type: rna / ID: 5 / Number of copies: 1
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 82.412445 KDa
SequenceString: GGGCAACAAC AACAAGCUAG CCACAACAAC AACAACAACA ACAACAAGUC GACCAACAAC AACAACAACA ACAACAACAA CUCGAGCAA CAACAACAAC AACAACAACA ACAAGGAUCC AAAACAGACC ACCAUGGUAC GUUUCAAGGC UUGAGCCCUC G UCACUGCC ...String:
GGGCAACAAC AACAAGCUAG CCACAACAAC AACAACAACA ACAACAAGUC GACCAACAAC AACAACAACA ACAACAACAA CUCGAGCAA CAACAACAAC AACAACAACA ACAAGGAUCC AAAACAGACC ACCAUGGUAC GUUUCAAGGC UUGAGCCCUC G UCACUGCC CUGUGGGGCA AGGUGACUCU GGAAGAAGUU GGUGGUGAGG CCCUGGGCAG GCUGCAGAGU GUGAGGGAAG GU CUGGUUG UCUACCAA

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Macromolecule #7: 18S rRNA

MacromoleculeName: 18S rRNA / type: rna / ID: 7
Details: Only small part of the 18S rRNA is provided with sequence truncated to visualized only parts.
Number of copies: 1
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 603.2455 KDa
SequenceString: UACCUGGUUG AUCCUGCCAG UAGCAU(A2M)UGC UUGUCUCAAA GAUUAAGCCA UGCAUGUCUG AGUACGCACG GCCGGU ACA GUGAAACUGC GAAUGGCUCA UUAAAUCAGU UAUGGU(OMU)CC(PSU) U(OMU)GGUCGCUC GCUCCUCUCC UACUU GGAU AACUGUGGUA ...String:
UACCUGGUUG AUCCUGCCAG UAGCAU(A2M)UGC UUGUCUCAAA GAUUAAGCCA UGCAUGUCUG AGUACGCACG GCCGGU ACA GUGAAACUGC GAAUGGCUCA UUAAAUCAGU UAUGGU(OMU)CC(PSU) U(OMU)GGUCGCUC GCUCCUCUCC UACUU GGAU AACUGUGGUA (A2M)UUCUAG(A2M)GC UAAUA(OMC)AUGC CGACGGGCGC UGACCCCCUU CGCGGGGGGG AUGC GUGCA UUUAUCAGAU CAAAACCAAC CCGGUCAGCC CCUCUCCGGC CCCGGCCGGG GGGCGGGCGC CGGCGGCUUU GGUGA CUCU AGAUAACCUC GGGCCGAUCG CACGCCCCCC GUGGCGGCGA CGACCCAUUC GAACGUCUGC CCUAUCAACU UUCGAU GGU AGUCGCCGUG CCUACCAUGG UGACCACGGG UGACGGGGAA UCAGGGUUCG AUUCCGGAGA GGGAGCCUGA GAAACGG CU ACCACAUCCA AGGAAGGCAG CAGGCGCGC(A2M) AAUUACCCAC UCCCGACCCG GGGA(OMG)GUAGU GA(OMC)GAA AAA UAACAAUACA GGACUCUUUC GAGGCCCUGU AAUUGGAAUG AGUCCACUUU AAAUCCUUUA ACGAGGAUCC AUUGGAG GG CAAGUCUGG(PSU) GCCAGCAGCC GCGGUAAUUC CAGCUCCAAU A(OMG)CGUAUAUU AAAGUUGCUG CAGUU(A2M) AAA AGCUCGUAGU U(OMG)GAUCUUGG GAGCGGGCGG GCGGUCCGCC GCGAGGCGAG CCACCGCCCG UCCCCGCCCC UUG CCUCUC GGCGCCCCCU CGAUGCUCUU AGCUGAGUGU CCCGCGGGGC CCGAAGCGUU UACUUUGAAA AAA(5MU)UAGAGU G(PSU)(PSU)CAAAGC AGGCCCGAGC CGCCUGGAUA CCGCAGCUAG GAAUAAUGGA AUAGGACCGC GGUUCUAUUU UGU UGGUUU UCGGAACUGA GGCCAUGAUU AAGAGGGACG GCCGGGGGCA UUCGUAUUGC GCCGCUAGAG GUGAAAUUCU UGGA CCGGC GCAAGACGGA CCAGAGCGAA AGCAUUUGCC AAGAAUGUUU UCAUUAAUCA AGA(A2M)CGAAAG UCGGAGGUUC G AAGACGAU CAGAUACCGU CGUAGUUCCG ACCA(PSU)AAACG AUGCCGACCG GCGAUGCGGC GGCGUUAUUC CCAUGACC C GCCGGGCAGC UUCCGGGAAA CCAAAGUCUU UGGGUUCCGG GGGGAGUAUG GUUGCAAAGC UGAAACUUAA AGGAAUUGA CGGAAGGGCA CCAC(JMH)AGGAG UGGAGCCUGC GGCUUAAU(PSU)U GAC(B8N)CAACAC GGGAAACCUC ACCCGGCC C GGACACGGAC AGGAUUGACA GAUUGAUAGC UCUUUCUCGA UUCCGUGGGU GGUGGUGCAU GGCCGUUCUU AGUUGGUGG AGCGAUUUGU CUGGUUAAUU C(5MC)GAUAACGA ACGAGACUCU GGCAUGCUAA CUAGUUACGC GACCCCCGAG CGGUCG GCG UCCCCCAACU UCUUAGAGGG ACAAGUGGCG UUCAGCCACC CGAGAUUGAG CAAUAACAGG UCUGUGAUGC CCUUAGA UG UCCGGGGCUG CACGCGCGCU ACACUGACUG GCUCAGCGUG UGCCUACCCU ACGCCGGCAG GCGCGGGUAA CCCGUUGA A CCCCAUUCGU GAUGGGGAUC GGGGAUUGCA AUUAUUCCCC AUGAACGAGG AAUUCCCAGU AAGUGCGGGU CAUAAGCUU GCGUUGAUU(A2M) AGUCCCUGCC CUUUGUACAC ACCG(OMC)CCGUC GCUACUACCG AUUGGAUGGU UUAGUGAGGC CC UCGGAUC GGCCCCGCCG GGGUCGGCCC ACGGCCCUGG CGGAGCGCUG AGAAGACGGU CGAACUUGAC UAUCUAGAGG AAG UAAAAG UCG(UR3)A(6MZ)CAAG GUUUCCGUAG GUG(MA6)(MA6)CCUGC GGAAGGAUCA UUA

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Macromolecule #20: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 20 / Number of copies: 1 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #21: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 21 / Number of copies: 1 / Formula: ZN
Molecular weightTheoretical: 65.409 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
Component:
ConcentrationNameFormula
20.0 mMHEPES
95.0 mMPotassium acetateKOAc
3.75 mMMagnesium acetateMg(OAc)2
1.0 mMAdenosine triphosphateATP
0.5 mMGuanosine triphosphateGTP
2.0 mMDithiothreitolDTT
0.25 mMSpermidine
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: HOMEMADE PLUNGER / Details: Manual blotting & plunge-freezing.

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Specialist opticsSpherical aberration corrector: Electron-optical aberrations were corrected using a CETCOR Cs-corrector (CEOS, Heidelberg) aligned with the CETCORPLUS 4.6.9 software package (CEOS, Heidelberg).
Image recordingFilm or detector model: FEI FALCON III (4k x 4k) / Detector mode: INTEGRATING / Average exposure time: 1.5 sec. / Average electron dose: 45.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: SPOT SCAN / Imaging mode: BRIGHT FIELD / Cs: 0.01 mm / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.2 µm / Nominal magnification: 59000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Startup modelType of model: OTHER
Details: Low resolution cryo-EM map of vacant human 40S subunit.
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 356632
Initial angle assignmentType: PROJECTION MATCHING
Final angle assignmentType: PROJECTION MATCHING
FSC plot (resolution estimation)

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Atomic model buiding 1

RefinementSpace: REAL
Output model

PDB-8rg0:
Structure of human eIF3 core from closed 48S translation initiation complex

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