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- EMDB-10775: Structure of a human 48S translational initiation complex - 40S body -

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Basic information

Entry
Database: EMDB / ID: EMD-10775
TitleStructure of a human 48S translational initiation complex - 40S body
Map data
SampleHuman 48S initiation complex
  • (40S ribosomal protein ...) x 19
  • (Eukaryotic translation initiation factor ...) x 4
  • 60S ribosomal protein L41
  • (nucleic-acidNucleic acid) x 2
  • (ligand) x 2
Function / homology
Function and homology information


positive regulation of mRNA binding / eukaryotic translation initiation factor 3 complex / eukaryotic 43S preinitiation complex / translation factor activity, RNA binding / dosage compensation by inactivation of X chromosome / negative regulation of RNA splicing / eukaryotic 48S preinitiation complex / ubiquitin ligase inhibitor activity / laminin receptor activity / formation of cytoplasmic translation initiation complex ...positive regulation of mRNA binding / eukaryotic translation initiation factor 3 complex / eukaryotic 43S preinitiation complex / translation factor activity, RNA binding / dosage compensation by inactivation of X chromosome / negative regulation of RNA splicing / eukaryotic 48S preinitiation complex / ubiquitin ligase inhibitor activity / laminin receptor activity / formation of cytoplasmic translation initiation complex / cytoplasmic side of rough endoplasmic reticulum membrane / negative regulation of ubiquitin protein ligase activity / regulation of translational initiation / erythrocyte homeostasis / endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / translation regulator activity / fibroblast growth factor binding / stress granule assembly / poly(U) RNA binding / positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator / 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) / positive regulation of ubiquitin-protein transferase activity / TOR signaling / ribosomal small subunit binding / SRP-dependent cotranslational protein targeting to membrane / maturation of SSU-rRNA / negative regulation of ubiquitin-dependent protein catabolic process / small-subunit processome / polysome / nuclear-transcribed mRNA catabolic process, nonsense-mediated decay / ribosomal small subunit biogenesis / viral transcription / translation initiation factor binding / erythrocyte differentiation / laminin binding / positive regulation of cell cycle / translation initiation factor activity / translational initiation / innate immune response in mucosa / polysomal ribosome / mRNA 3'-UTR binding / positive regulation of translational fidelity / rough endoplasmic reticulum / maintenance of translational fidelity / microtubule organizing center / small ribosomal subunit rRNA binding / ribosomal small subunit assembly / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / positive regulation of translation / response to virus / cytoplasmic ribonucleoprotein granule / neural tube closure / mRNA 5'-UTR binding / rRNA processing / cytoplasmic translation / virus receptor activity / cell body / cytosolic large ribosomal subunit / cytosolic small ribosomal subunit / ribosome binding / glucose homeostasis / small ribosomal subunit / ribonucleoprotein complex / protein N-terminus binding / antibacterial humoral response / protein stabilization / ribosome / rRNA binding / structural constituent of ribosome / antimicrobial humoral immune response mediated by antimicrobial peptide / cell differentiation / postsynaptic density / translation / cadherin binding / multicellular organism development / cell adhesion / defense response to Gram-positive bacterium / mRNA binding / synapse / positive regulation of apoptotic process / dendrite / focal adhesion / nucleolus / positive regulation of gene expression / positive regulation of cell population proliferation / protein kinase binding / negative regulation of apoptotic process / endoplasmic reticulum / negative regulation of transcription by RNA polymerase II / enzyme binding / protein-containing complex / RNA binding / DNA binding / extracellular space / extracellular exosome / zinc ion binding / membrane / nucleoplasm / plasma membrane / nucleus
Ribosomal protein S27e / Ribosomal protein S4e, central region / Ribosomal protein S30 / Ribosomal protein L41 / Eukaryotic translation initiation factor 3 subunit C, N-terminal domain / S15/NS1, RNA-binding / Zinc-binding ribosomal protein / Nucleic acid-binding, OB-fold / Ribosomal protein S13/S15, N-terminal / Ribosomal protein L23/L15e core domain superfamily ...Ribosomal protein S27e / Ribosomal protein S4e, central region / Ribosomal protein S30 / Ribosomal protein L41 / Eukaryotic translation initiation factor 3 subunit C, N-terminal domain / S15/NS1, RNA-binding / Zinc-binding ribosomal protein / Nucleic acid-binding, OB-fold / Ribosomal protein S13/S15, N-terminal / Ribosomal protein L23/L15e core domain superfamily / Ribosomal protein S5, N-terminal / Ribosomal protein S4e, N-terminal / Eukaryotic translation initiation factor 3 subunit J / Ribosomal protein S7e / Ribosomal protein S6, eukaryotic / Ribosomal protein S5 domain 2-type fold, subgroup / Ribosomal protein L2, domain 2 / Ribosomal protein S4, conserved site / Ribosomal protein S12/S23 / Ribosomal S11, conserved site / Translation initiation factor 1A (eIF-1A), conserved site / Ribosomal protein S2, conserved site / Ribosomal protein S5, N-terminal, conserved site / Ribosomal protein S4e, N-terminal, conserved site / Ribosomal protein S17/S11 / Ribosomal protein S15 / Ribosomal protein S21e, conserved site / Ribosomal protein S21e / KOW / Ribosomal protein S5, eukaryotic/archaeal / Ribosomal protein S4/S9, eukaryotic/archaeal / Ribosomal protein S2, eukaryotic/archaeal / Ribosomal protein S23, eukaryotic/archaeal / Ribosomal protein S5, C-terminal / RNA-binding S4 domain / Ribosomal protein S24e / Ribosomal protein S11 / SUI1 domain / Ribosomal protein S4/S9, N-terminal / RNA-binding domain, S1, IF1 type / Ribosomal protein S2 / Ribosomal protein S3Ae / Ribosomal protein S6e / Translation initiation factor 1A (eIF-1A) / Ribosomal protein S17e / Ribosomal protein S8e / Ribosomal protein S26e / Ribosomal protein S4e / Ribosomal protein S5 / Proteasome component (PCI) domain / Ribosomal protein S8 / Ribosomal protein S17e, conserved site / Ribosomal S24e conserved site / Ribosomal protein S3Ae, conserved site / Winged helix-like DNA-binding domain superfamily / Ribosomal protein S2, eukaryotic / 40S ribosomal protein S1/3, eukaryotes / Eukaryotic translation initiation factor 3 subunit C / Ribosomal protein S17, archaeal/eukaryotic / 40S ribosomal protein S4, C-terminal domain / 40S ribosomal protein SA, C-terminal domain / 40S ribosomal protein S11, N-terminal / Ribosomal protein S8 superfamily / Winged helix DNA-binding domain superfamily / Eukaryotic translation initiation factor 3-like domain superfamily / Ribosomal protein S17e-like superfamily / SUI1 domain superfamily / Ribosomal protein S11 superfamily / RNA-binding S4 domain superfamily / Ribosomal protein S4e, central domain superfamily / Ribosomal protein S26e superfamily / Ribosomal protein S21e superfamily / Ribosomal protein S4, KOW domain / Ribosomal protein S8e subdomain, eukaryotes / Ribosomal protein S2, flavodoxin-like domain superfamily / 40S ribosomal protein SA / Ribosomal protein S15P / Ribosomal protein S5 domain 2-type fold / Ribosomal protein S6e, conserved site / Ribosomal protein S8e, conserved site / Ribosomal protein S17, conserved site / Ribosomal protein S8e/ribosomal biogenesis NSA2 / Ribosomal protein S4/S9 / Eukaryotic translation initiation factor SUI1
40S ribosomal protein S21 / 60S ribosomal protein L41 / 40S ribosomal protein S30 / 40S ribosomal protein S26 / 40S ribosomal protein S24 / 40S ribosomal protein S14 / 40S ribosomal protein S6 / 40S ribosomal protein S4, X isoform / 40S ribosomal protein S11 / 40S ribosomal protein S13 ...40S ribosomal protein S21 / 60S ribosomal protein L41 / 40S ribosomal protein S30 / 40S ribosomal protein S26 / 40S ribosomal protein S24 / 40S ribosomal protein S14 / 40S ribosomal protein S6 / 40S ribosomal protein S4, X isoform / 40S ribosomal protein S11 / 40S ribosomal protein S13 / 40S ribosomal protein S23 / 40S ribosomal protein S27 / 40S ribosomal protein S15a / 40S ribosomal protein S8 / 40S ribosomal protein S7 / 40S ribosomal protein S3a / Eukaryotic translation initiation factor 1A, X-chromosomal / 40S ribosomal protein S9 / Eukaryotic translation initiation factor 1 / 40S ribosomal protein S2 / 40S ribosomal protein SA / 40S ribosomal protein S17 / Eukaryotic translation initiation factor 3 subunit J / Eukaryotic translation initiation factor 3 subunit C
Biological speciesHomo sapiens (human) / Human (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.1 Å
AuthorsBrito Querido J / Sokabe M / Kraatz S / Gordiyenko Y / Skehel M / Fraser C / Ramakrishnan V
Funding support United Kingdom, United States, 3 items
OrganizationGrant numberCountry
Wellcome TrustWTY096570 United Kingdom
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01GM092927 United States
Medical Research Council (MRC, United Kingdom)MC_U105184332 United Kingdom
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.
Validation ReportPDB-ID: 6ybw

SummaryFull reportAbout validation report
History
DepositionMar 18, 2020-
Header (metadata) releaseSep 16, 2020-
Map releaseSep 16, 2020-
UpdateSep 16, 2020-
Current statusSep 16, 2020Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.035
  • Imaged by UCSF Chimera
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  • Surface view colored by height
  • Surface level: 0.035
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6ybw
  • Surface level: 0.035
  • Imaged by UCSF Chimera
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  • Simplified surface model + fitted atomic model
  • Atomic modelsPDB-6ybw
  • Imaged by Jmol
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

Downloads & links

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Map

FileDownload / File: emd_10775.map.gz / Format: CCP4 / Size: 476.8 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 500 pix.
= 537. Å
1.07 Å/pix.
x 500 pix.
= 537. Å
1.07 Å/pix.
x 500 pix.
= 537. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.074 Å
Density
Contour LevelBy AUTHOR: 0.03 / Movie #1: 0.035
Minimum - Maximum-0.22808239 - 0.4096543
Average (Standard dev.)0.00031956309 (±0.006762035)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions500500500
Spacing500500500
CellA=B=C: 537.0 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.0741.0741.074
M x/y/z500500500
origin x/y/z0.0000.0000.000
length x/y/z537.000537.000537.000
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS500500500
D min/max/mean-0.2280.4100.000

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Supplemental data

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Additional map: #1

Fileemd_10775_additional_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

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Additional map: #2

Fileemd_10775_additional_2.map
Projections & Slices
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Half map: #1

Fileemd_10775_half_map_1.map
Projections & Slices
AxesZYX

Projections

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Half map: #2

Fileemd_10775_half_map_2.map
Projections & Slices
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Sample components

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Entire Human 48S initiation complex

EntireName: Human 48S initiation complex / Number of components: 32

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Component #1: protein, Human 48S initiation complex

ProteinName: Human 48S initiation complex / Recombinant expression: No

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Component #2: protein, Human 48S initiation complex

ProteinName: Human 48S initiation complex / Recombinant expression: No
SourceSpecies: Homo sapiens (human)

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Component #3: protein, Human 48S initiation complex

ProteinName: Human 48S initiation complex / Recombinant expression: No
SourceSpecies: Homo sapiens (human)
Source (engineered)Expression System: Escherichia coli (E. coli)

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Component #4: protein, Human 48S initiation complex

ProteinName: Human 48S initiation complex / Recombinant expression: No
SourceSpecies: Homo sapiens (human)
Source (engineered)Expression System: synthetic construct (others)

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Component #5: protein, 40S ribosomal protein S4, X isoform

ProteinName: 40S ribosomal protein S4, X isoformRibosome / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 29.654869 kDa
SourceSpecies: Human (human)

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Component #6: protein, 40S ribosomal protein S11

ProteinName: 40S ribosomal protein S11 / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 18.321652 kDa
SourceSpecies: Human (human)

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Component #7: protein, 40S ribosomal protein S23

ProteinName: 40S ribosomal protein S23 / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 15.844666 kDa
SourceSpecies: Human (human)

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Component #8: protein, 40S ribosomal protein S9

ProteinName: 40S ribosomal protein S9 / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 22.641564 kDa
SourceSpecies: Human (human)

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Component #9: protein, 40S ribosomal protein S7

ProteinName: 40S ribosomal protein S7 / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 22.168914 kDa
SourceSpecies: Human (human)

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Component #10: protein, 40S ribosomal protein S30

ProteinName: 40S ribosomal protein S30 / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 6.668938 kDa
SourceSpecies: Human (human)

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Component #11: protein, 40S ribosomal protein S27

ProteinName: 40S ribosomal protein S27 / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 9.480186 kDa
SourceSpecies: Human (human)

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Component #12: protein, 40S ribosomal protein S21

ProteinName: 40S ribosomal protein S21 / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 9.124389 kDa
SourceSpecies: Human (human)

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Component #13: protein, 40S ribosomal protein S15a

ProteinName: 40S ribosomal protein S15a / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 14.865555 kDa
SourceSpecies: Human (human)

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Component #14: protein, 40S ribosomal protein S17

ProteinName: 40S ribosomal protein S17 / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 15.578156 kDa
SourceSpecies: Human (human)

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Component #15: protein, 40S ribosomal protein S2

ProteinName: 40S ribosomal protein S2 / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 31.376516 kDa
SourceSpecies: Human (human)

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Component #16: protein, 40S ribosomal protein S3a

ProteinName: 40S ribosomal protein S3a / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 30.002061 kDa
SourceSpecies: Human (human)

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Component #17: protein, 40S ribosomal protein SA

ProteinName: 40S ribosomal protein SA / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 32.883938 kDa
SourceSpecies: Human (human)

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Component #18: protein, 40S ribosomal protein S26

ProteinName: 40S ribosomal protein S26 / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 13.047532 kDa
SourceSpecies: Human (human)

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Component #19: protein, 40S ribosomal protein S14

ProteinName: 40S ribosomal protein S14 / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 16.302772 kDa
SourceSpecies: Human (human)

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Component #20: protein, 40S ribosomal protein S6

ProteinName: 40S ribosomal protein S6 / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 28.751906 kDa
SourceSpecies: Human (human)

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Component #21: protein, 40S ribosomal protein S8

ProteinName: 40S ribosomal protein S8 / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 24.263387 kDa
SourceSpecies: Human (human)

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Component #22: protein, 40S ribosomal protein S24

ProteinName: 40S ribosomal protein S24 / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 15.463333 kDa
SourceSpecies: Human (human)

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Component #23: protein, Eukaryotic translation initiation factor 1A, X-chromosomal

ProteinName: Eukaryotic translation initiation factor 1A, X-chromosomal
Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 16.488449 kDa
SourceSpecies: Homo sapiens (human)
Source (engineered)Expression System: Escherichia coli (E. coli)

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Component #24: protein, Eukaryotic translation initiation factor 1

ProteinName: Eukaryotic translation initiation factor 1 / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 12.752498 kDa
SourceSpecies: Homo sapiens (human)
Source (engineered)Expression System: Escherichia coli (E. coli)

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Component #25: protein, 40S ribosomal protein S13

ProteinName: 40S ribosomal protein S13 / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 17.259389 kDa
SourceSpecies: Human (human)

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Component #26: protein, Eukaryotic translation initiation factor 3 subunit J

ProteinName: Eukaryotic translation initiation factor 3 subunit J / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 29.108453 kDa
SourceSpecies: Homo sapiens (human)
Source (engineered)Expression System: Escherichia coli (E. coli)

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Component #27: protein, Eukaryotic translation initiation factor 3 subunit C

ProteinName: Eukaryotic translation initiation factor 3 subunit C / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 105.503945 kDa
SourceSpecies: Human (human)

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Component #28: protein, 60S ribosomal protein L41

ProteinName: 60S ribosomal protein L41 / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 3.473451 kDa
SourceSpecies: Human (human)

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Component #29: nucleic-acid, 18S rRNA

nucleic acidName: 18S rRNA18S ribosomal RNA / Class: RNA / Structure: OTHER / Synthetic: No
Sequence: UACCUGGUUG AUCCUGCCAG UAGCAU(A2M)UGC UUGUCUCAAA GAUUAAGCCA UGCAUGUCUG AGUACGCACG GCCGGUACAG UGAAACUGCG AAUGGCUCAU UAAAUCAGUU AUGGU(OMU)CC(PSU)U (OMU)GGUCGCUCG CUCCUCUCCU ACUUGGAUAA ...Sequence:
UACCUGGUUG AUCCUGCCAG UAGCAU(A2M)UGC UUGUCUCAAA GAUUAAGCCA UGCAUGUCUG AGUACGCACG GCCGGUACAG UGAAACUGCG AAUGGCUCAU UAAAUCAGUU AUGGU(OMU)CC(PSU)U (OMU)GGUCGCUCG CUCCUCUCCU ACUUGGAUAA CUGUGGUA(A2M)U UCUAG(A2M)GCUA AUA(OMC)AUGCCG ACGGGCGCUG ACCCCCUUCG CGGGGGGGAU GCGUGCAUUU AUCAGAUCAA AACCAACCCG GUCAGCCCCU CUCCGGCCCC GGCCGGGGGG CGGGCGCCGG CGGCUUUGGU GACUCUAGAU AACCUCGGGC CGAUCGCACG CCCCCCGUGG CGGCGACGAC CCAUUCGAAC GUCUGCCCUA UCAACUUUCG AUGGUAGUCG CCGUGCCUAC CAUGGUGACC ACGGGUGACG GGGAAUCAGG GUUCGAUUCC GGAGAGGGAG CCUGAGAAAC GGCUACCACA UCCAAGGAAG GCAGCAGGCG CGC(A2M)AAUUAC CCACUCCCGA CCCGGGGA(OMG)G UAGUGA(OMC)GAA AAAUAACAAU ACAGGACUCU UUCGAGGCCC UGUAAUUGGA AUGAGUCCAC UUUAAAUCCU UUAACGAGGA UCCAUUGGAG GGCAAGUCUG G(PSU)GCCAGCAG CCGCGGUAAU UCCAGCUCCA AUA(OMG)CGUAUA UUAAAGUUGC UGCAGUU(A2M)AA AAGCUCGUAG UU(OMG)GAUCUUG GGAGCGGGCG GGCGGUCCGC CGCGAGGCGA GCCACCGCCC GUCCCCGCCC CUUGCCUCUC GGCGCCCCCU CGAUGCUCUU AGCUGAGUGU CCCGCGGGGC CCGAAGCGUU UACUUUGAAA AAA(5MU)UAGAGU G(PSU)(PSU)CAAAGCA GGCCCGAGCC GCCUGGAUAC CGCAGCUAGG AAUAAUGGAA UAGGACCGCG GUUCUAUUUU GUUGGUUUUC GGAACUGAGG CCAUGAUUAA GAGGGACGGC CGGGGGCAUU CGUAUUGCGC CGCUAGAGGU GAAAUUCUUG GACCGGCGCA AGACGGACCA GAGCGAAAGC AUUUGCCAAG AAUGUUUUCA UUAAUCAAGA (A2M)CGAAAGUCG GAGGUUCGAA GACGAUCAGA UACCGUCGUA GUUCCGACCA (PSU)AAACGAUGC CGACCGGCGA UGCGGCGGCG UUAUUCCCAU GACCCGCCGG GCAGCUUCCG GGAAACCAAA GUCUUUGGGU UCCGGGGGGA GUAUGGUUGC AAAGCUGAAA CUUAAAGGAA UUGACGGAAG GGCACCAC(JMH)A GGAGUGGAGC CUGCGGCUUA AU(PSU)UGACUCA ACACGGGAAA CCUCACCCGG CCCGGACACG GACAGGAUUG ACAGAUUGAU AGCUCUUUCU CGAUUCCGUG GGUGGUGGUG CAUGGCCGUU CUUAGUUGGU GGAGCGAUUU GUCUGGUUAA UUC(5MC)GAUAAC GAACGAGACU CUGGCAUGCU AACUAGUUAC GCGACCCCCG AGCGGUCGGC GUCCCCCAAC UUCUUAGAGG GACAAGUGGC GUUCAGCCAC CCGAGAUUGA GCAAUAACAG GUCUGUGAUG CCCUUAGAUG UCCGGGGCUG CACGCGCGCU ACACUGACUG GCUCAGCGUG UGCCUACCCU ACGCCGGCAG GCGCGGGUAA CCCGUUGAAC CCCAUUCGUG AUGGGGAUCG GGGAUUGCAA UUAUUCCCCA UGAACGAGGA AUUCCCAGUA AGUGCGGGUC AUAAGCUUGC GUUGAUU(A2M)AG UCCCUGCCCU UUGUACACAC CG(OMC)CCGUCGC UACUACCGAU UGGAUGGUUU AGUGAGGCCC UCGGAUCGGC CCCGCCGGGG UCGGCCCACG GCCCUGGCGG AGCGCUGAGA AGACGGUCGA ACUUGACUAU CUAGAGGAAG UAAAAGUCG(UR3) A(6MZ)CAAGGUUU CCGUAGGUG(MA6) (MA6)CCUGCGGAA GGAUCAUUA
MassTheoretical: 603.130375 kDa
SourceSpecies: Human (human)

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Component #30: nucleic-acid, mRNA

nucleic acidName: mRNAMessenger RNA / Class: RNA / Structure: OTHER / Synthetic: No
Sequence:
AAAAAAAAAA AAAAAAAAAA AAAAAAAA
MassTheoretical: 9.172806 kDa
SourceSpecies: Homo sapiens (human)

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Component #31: ligand, MAGNESIUM ION

LigandName: MAGNESIUM ION / Number of Copies: 60 / Recombinant expression: No
MassTheoretical: 2.430505 MDa

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Component #32: ligand, ZINC ION

LigandName: ZINC ION / Number of Copies: 1 / Recombinant expression: No
MassTheoretical: 6.540905 MDa

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Experimental details

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Sample preparation

SpecimenSpecimen state: Particle / Method: cryo EM
Sample solutionpH: 7.4
VitrificationCryogen name: ETHANE / Humidity: 100 %

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
ImagingMicroscope: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Electron dose: 107 e/Å2 / Illumination mode: FLOOD BEAM
LensImaging mode: BRIGHT FIELD
Specimen HolderModel: OTHER
CameraDetector: FEI FALCON III (4k x 4k)

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Image processing

ProcessingMethod: single particle reconstruction / Number of projections: 144882
3D reconstructionSoftware: RELION / Resolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF
FSC plot (resolution estimation)

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Atomic model buiding

Output model

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