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- EMDB-11456: EDF1-ribosome complex -

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Basic information

Entry
Database: EMDB / ID: EMD-11456
TitleEDF1-ribosome complex
Map dataMap of EDF1 bound to 80S ribosomes, (local resolution filtered).
Sample
  • Complex: EDF1-ribosome complex
    • RNA: x 2 types
    • Protein or peptide: x 35 types
  • Ligand: x 2 types
Keywordstranslation / frameshifting / collision / RIBOSOME
Function / homology
Function and homology information


endothelial cell differentiation / negative regulation of endoplasmic reticulum unfolded protein response / oxidized pyrimidine DNA binding / response to TNF agonist / positive regulation of base-excision repair / negative regulation of peptidyl-serine phosphorylation / positive regulation of respiratory burst involved in inflammatory response / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage / positive regulation of gastrulation / regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway ...endothelial cell differentiation / negative regulation of endoplasmic reticulum unfolded protein response / oxidized pyrimidine DNA binding / response to TNF agonist / positive regulation of base-excision repair / negative regulation of peptidyl-serine phosphorylation / positive regulation of respiratory burst involved in inflammatory response / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage / positive regulation of gastrulation / regulation of adenylate cyclase-activating G protein-coupled receptor signaling pathway / protein tyrosine kinase inhibitor activity / IRE1-RACK1-PP2A complex / positive regulation of endodeoxyribonuclease activity / nucleolus organization / positive regulation of Golgi to plasma membrane protein transport / translation at postsynapse / TNFR1-mediated ceramide production / negative regulation of DNA repair / negative regulation of RNA splicing / mammalian oogenesis stage / supercoiled DNA binding / activation-induced cell death of T cells / neural crest cell differentiation / NF-kappaB complex / oxidized purine DNA binding / cysteine-type endopeptidase activator activity involved in apoptotic process / negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide / ubiquitin-like protein conjugating enzyme binding / regulation of establishment of cell polarity / translation at presynapse / positive regulation of ubiquitin-protein transferase activity / Formation of the ternary complex, and subsequently, the 43S complex / negative regulation of phagocytosis / erythrocyte homeostasis / rRNA modification in the nucleus and cytosol / positive regulation of DNA binding / cytoplasmic side of rough endoplasmic reticulum membrane / laminin receptor activity / protein kinase A binding / negative regulation of ubiquitin protein ligase activity / pigmentation / Ribosomal scanning and start codon recognition / ion channel inhibitor activity / Translation initiation complex formation / positive regulation of mitochondrial depolarization / positive regulation of T cell receptor signaling pathway / positive regulation of transcription by RNA polymerase I / positive regulation of activated T cell proliferation / fibroblast growth factor binding / negative regulation of Wnt signaling pathway / monocyte chemotaxis / negative regulation of translational frameshifting / Protein hydroxylation / BH3 domain binding / TOR signaling / SARS-CoV-1 modulates host translation machinery / TFIID-class transcription factor complex binding / regulation of cell division / mTORC1-mediated signalling / T cell proliferation involved in immune response / Peptide chain elongation / iron-sulfur cluster binding / positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator / regulation of lipid metabolic process / Selenocysteine synthesis / positive regulation of signal transduction by p53 class mediator / Formation of a pool of free 40S subunits / endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / ubiquitin ligase inhibitor activity / Eukaryotic Translation Termination / Response of EIF2AK4 (GCN2) to amino acid deficiency / SRP-dependent cotranslational protein targeting to membrane / negative regulation of ubiquitin-dependent protein catabolic process / Viral mRNA Translation / photoreceptor outer segment / negative regulation of respiratory burst involved in inflammatory response / phagocytic cup / 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 / erythrocyte development / Major pathway of rRNA processing in the nucleolus and cytosol / regulation of translational fidelity / transcription regulator inhibitor activity / 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) / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / Protein methylation / spindle assembly / positive regulation of phagocytosis / Nuclear events stimulated by ALK signaling in cancer / ribosomal small subunit export from nucleus / positive regulation of intrinsic apoptotic signaling pathway / rough endoplasmic reticulum / laminin binding / translation regulator activity / Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal / positive regulation of cell cycle / translation initiation factor binding / signaling adaptor activity / gastrulation
Similarity search - Function
Zinc finger, C2H2, LYAR-type / Cell growth-regulating nucleolar protein / LYAR-type C2HC zinc finger / Zinc finger C2HC LYAR-type profile. / Acetyl-coA carboxylase zinc finger domain / Acetyl-CoA carboxylase zinc finger domain / Multiprotein bridging factor 1, N-terminal / Multiprotein bridging factor 1 / Helix-turn-helix / Helix-turn-helix XRE-family like proteins ...Zinc finger, C2H2, LYAR-type / Cell growth-regulating nucleolar protein / LYAR-type C2HC zinc finger / Zinc finger C2HC LYAR-type profile. / Acetyl-coA carboxylase zinc finger domain / Acetyl-CoA carboxylase zinc finger domain / Multiprotein bridging factor 1, N-terminal / Multiprotein bridging factor 1 / Helix-turn-helix / Helix-turn-helix XRE-family like proteins / Cro/C1-type HTH domain profile. / Cro/C1-type helix-turn-helix domain / 40S ribosomal protein SA / 40S ribosomal protein SA, C-terminal domain / 40S ribosomal protein SA C-terminus / Ubiquitin-like protein FUBI / Lambda repressor-like, DNA-binding domain superfamily / : / 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 S12e signature. / Ribosomal protein S12e / Ribosomal protein S19e, conserved site / Ribosomal protein S19e signature. / Small (40S) ribosomal subunit Asc1/RACK1 / Ribosomal protein S5, eukaryotic/archaeal / Ribosomal protein S21e / Ribosomal protein S21e superfamily / Ribosomal protein S21e / Ribosomal protein S2, eukaryotic / S27a-like superfamily / 40S Ribosomal protein S10 / : / Ribosomal protein S7e signature. / Plectin/S10, N-terminal / Plectin/S10 domain / Ribosomal protein S10, eukaryotic/archaeal / Ribosomal protein S8e subdomain, eukaryotes / Ribosomal protein S25 / S25 ribosomal protein / Ribosomal protein S27a / Ribosomal protein S17e, conserved site / Ribosomal protein S27a / Ribosomal protein S17e signature. / Ribosomal protein S27a / Ribosomal protein S3Ae, conserved site / Ribosomal protein S3Ae signature. / Ribosomal protein S30 / Ribosomal protein S30 / Ribosomal protein S2, eukaryotic/archaeal / 40S ribosomal protein S29/30S ribosomal protein S14 type Z / Ribosomal protein S27e signature. / 40S ribosomal protein S4, C-terminal domain / 40S ribosomal protein S4 C-terminus / Ribosomal protein S4e, N-terminal, conserved site / Ribosomal protein S4e signature. / Ribosomal protein S3, eukaryotic/archaeal / Ribosomal protein S19e / Ribosomal protein S8e, conserved site / Ribosomal protein S19e / Ribosomal protein S8e signature. / Ribosomal_S19e / Ribosomal protein S6, eukaryotic / Ribosomal protein S7e / Ribosomal protein S7e / 40S ribosomal protein S1/3, eukaryotes / Ribosomal protein S19A/S15e / Ribosomal protein S17e / Ribosomal protein S17e-like superfamily / Ribosomal S17 / 40S ribosomal protein S11, N-terminal / Ribosomal_S17 N-terminal / : / Ribosomal S24e conserved site / Ribosomal protein S24e signature. / Ribosomal protein S4e, N-terminal / RS4NT (NUC023) domain / Ribosomal protein S4, KOW domain / Ribosomal protein S4e / Ribosomal protein S4e, central region / Ribosomal protein S4e, central domain superfamily / Ribosomal family S4e / Ribosomal protein S23, eukaryotic/archaeal / Ribosomal protein S6/S6e/A/B/2, conserved site / Ribosomal protein S6e signature. / Ribosomal protein S24e / Ribosomal protein S24e / Ribosomal protein S27 / Ribosomal protein S27, zinc-binding domain superfamily / Ribosomal protein S27 / Ribosomal protein S17, archaeal/eukaryotic / Ribosomal protein S8e / Ribosomal protein S3Ae / Ribosomal S3Ae family / Ribosomal S3Ae family
Similarity search - Domain/homology
Endothelial differentiation-related factor 1 / Small ribosomal subunit protein eS17 / Small ribosomal subunit protein uS2 / Small ribosomal subunit protein uS5 / Small ribosomal subunit protein uS3 / Small ribosomal subunit protein eS12 / Small ribosomal subunit protein eS19 / Small ribosomal subunit protein eS27 / Small ribosomal subunit protein uS4 / Small ribosomal subunit protein uS7 ...Endothelial differentiation-related factor 1 / Small ribosomal subunit protein eS17 / Small ribosomal subunit protein uS2 / Small ribosomal subunit protein uS5 / Small ribosomal subunit protein uS3 / Small ribosomal subunit protein eS12 / Small ribosomal subunit protein eS19 / Small ribosomal subunit protein eS27 / Small ribosomal subunit protein uS4 / Small ribosomal subunit protein uS7 / Small ribosomal subunit protein eS10 / Small ribosomal subunit protein uS10 / Small ribosomal subunit protein eS1 / Small ribosomal subunit protein eS7 / Small ribosomal subunit protein eS8 / Small ribosomal subunit protein uS8 / Small ribosomal subunit protein uS9 / Small ribosomal subunit protein uS11 / Small ribosomal subunit protein uS12 / Small ribosomal subunit protein uS13 / Small ribosomal subunit protein uS14 / Small ribosomal subunit protein uS15 / Small ribosomal subunit protein uS17 / Small ribosomal subunit protein eS4, X isoform / Small ribosomal subunit protein eS6 / Small ribosomal subunit protein uS19 / Small ribosomal subunit protein eS24 / Small ribosomal subunit protein eS25 / Small ribosomal subunit protein eS26 / Small ribosomal subunit protein eS28 / Ubiquitin-like FUBI-ribosomal protein eS30 fusion protein / Ubiquitin-ribosomal protein eS31 fusion protein / Small ribosomal subunit protein eS21 / Small ribosomal subunit protein RACK1 / Cell growth-regulating nucleolar protein
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.9 Å
AuthorsBest KM / Denk T
Funding support Germany, United States, 3 items
OrganizationGrant numberCountry
German Research Foundation (DFG) Germany
Howard Hughes Medical Institute (HHMI) United States
National Institutes of Health/National Center for Research Resources (NIH/NCRR) United States
CitationJournal: Elife / Year: 2020
Title: EDF1 coordinates cellular responses to ribosome collisions.
Authors: Niladri K Sinha / Alban Ordureau / Katharina Best / James A Saba / Boris Zinshteyn / Elayanambi Sundaramoorthy / Amit Fulzele / Danielle M Garshott / Timo Denk / Matthias Thoms / Joao A ...Authors: Niladri K Sinha / Alban Ordureau / Katharina Best / James A Saba / Boris Zinshteyn / Elayanambi Sundaramoorthy / Amit Fulzele / Danielle M Garshott / Timo Denk / Matthias Thoms / Joao A Paulo / J Wade Harper / Eric J Bennett / Roland Beckmann / Rachel Green /
Abstract: Translation of aberrant mRNAs induces ribosomal collisions, thereby triggering pathways for mRNA and nascent peptide degradation and ribosomal rescue. Here we use sucrose gradient fractionation ...Translation of aberrant mRNAs induces ribosomal collisions, thereby triggering pathways for mRNA and nascent peptide degradation and ribosomal rescue. Here we use sucrose gradient fractionation combined with quantitative proteomics to systematically identify proteins associated with collided ribosomes. This approach identified Endothelial differentiation-related factor 1 (EDF1) as a novel protein recruited to collided ribosomes during translational distress. Cryo-electron microscopic analyses of EDF1 and its yeast homolog Mbf1 revealed a conserved 40S ribosomal subunit binding site at the mRNA entry channel near the collision interface. EDF1 recruits the translational repressors GIGYF2 and EIF4E2 to collided ribosomes to initiate a negative-feedback loop that prevents new ribosomes from translating defective mRNAs. Further, EDF1 regulates an immediate-early transcriptional response to ribosomal collisions. Our results uncover mechanisms through which EDF1 coordinates multiple responses of the ribosome-mediated quality control pathway and provide novel insights into the intersection of ribosome-mediated quality control with global transcriptional regulation.
History
DepositionJul 24, 2020-
Header (metadata) releaseAug 19, 2020-
Map releaseAug 19, 2020-
UpdateMay 1, 2024-
Current statusMay 1, 2024Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.06
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  • Surface view colored by height
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  • Surface view with fitted model
  • Atomic models: PDB-6zvh
  • Surface level: 0.06
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  • Simplified surface model + fitted atomic model
  • Atomic modelsPDB-6zvh
  • Imaged by Jmol
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Structure viewerEM map:
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Supplemental images

emd_11456.png

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Map

FileDownload / File: emd_11456.map.gz / Format: CCP4 / Size: 244.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationMap of EDF1 bound to 80S ribosomes, (local resolution filtered).
Projections & slices

Image control

Size
Brightness
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Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.06 Å/pix.
x 400 pix.
= 423.6 Å		1.06 Å/pix.
x 400 pix.
= 423.6 Å		1.06 Å/pix.
x 400 pix.
= 423.6 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.059 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.06 / Movie #1: 0.06
Minimum - Maximum-0.06447853 - 0.33240378
Average (Standard dev.)0.0030061456 (±0.016341811)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions400400400
Spacing400400400
CellA=B=C: 423.6 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.0591.0591.059
M x/y/z400400400
origin x/y/z0.0000.0000.000
length x/y/z423.600423.600423.600
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ280280280
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS400400400
D min/max/mean-0.0640.3320.003

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Supplemental data

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Mask #1

Fileemd_11456_msk_1.map
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Additional map: Post processed map, bFactor -30

Fileemd_11456_additional.map
AnnotationPost processed map, bFactor -30
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Half map: Half map 2 of the 3D refinement

Fileemd_11456_half_map_1.map
AnnotationHalf map 2 of the 3D refinement
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Half map: Half map 1 of the 3D refinement

Fileemd_11456_half_map_2.map
AnnotationHalf map 1 of the 3D refinement
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Sample components

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Entire : EDF1-ribosome complex

EntireName: EDF1-ribosome complex
Components
  • Complex: EDF1-ribosome complex
    • RNA: 18S rRNA
    • Protein or peptide: 40S ribosomal protein SA
    • Protein or peptide: 40S ribosomal protein S3a
    • Protein or peptide: 40S ribosomal protein S3
    • Protein or peptide: 40S ribosomal protein S4, X isoform
    • Protein or peptide: 40S ribosomal protein S5
    • Protein or peptide: 40S ribosomal protein S7
    • Protein or peptide: 40S ribosomal protein S8
    • Protein or peptide: 40S ribosomal protein S10
    • Protein or peptide: 40S ribosomal protein S11
    • Protein or peptide: 40S ribosomal protein S15
    • Protein or peptide: 40S ribosomal protein S16
    • Protein or peptide: 40S ribosomal protein S17
    • Protein or peptide: 40S ribosomal protein S18
    • Protein or peptide: 40S ribosomal protein S19
    • Protein or peptide: 40S ribosomal protein S20
    • Protein or peptide: 40S ribosomal protein S21
    • Protein or peptide: 40S ribosomal protein S23
    • Protein or peptide: 40S ribosomal protein S26
    • Protein or peptide: 40S ribosomal protein S28
    • Protein or peptide: 40S ribosomal protein S29
    • Protein or peptide: Receptor of activated protein C kinase 1
    • Protein or peptide: 40S ribosomal protein S2
    • Protein or peptide: 40S ribosomal protein S6
    • Protein or peptide: 40S ribosomal protein S9
    • Protein or peptide: 40S ribosomal protein S12
    • Protein or peptide: 40S ribosomal protein S13
    • Protein or peptide: 40S ribosomal protein S14
    • Protein or peptide: 40S ribosomal protein S15a
    • Protein or peptide: 40S ribosomal protein S24
    • Protein or peptide: 40S ribosomal protein S25
    • Protein or peptide: 40S ribosomal protein S27
    • Protein or peptide: 40S ribosomal protein S30
    • Protein or peptide: Ubiquitin-40S ribosomal protein S27a
    • RNA: E-site tRNA
    • Protein or peptide: Cell growth-regulating nucleolar protein
    • Protein or peptide: Endothelial differentiation-related factor 1
  • Ligand: MAGNESIUM ION
  • Ligand: ZINC ION

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Supramolecule #1: EDF1-ribosome complex

SupramoleculeName: EDF1-ribosome complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#37
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: 18S rRNA

MacromoleculeName: 18S rRNA / type: rna / ID: 1 / Number of copies: 1
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 561.308438 KDa
SequenceString: UACCUGGUUG AUCCUGCCAG UAGCAUAUGC UUGUCUCAAA GAUUAAGCCA UGCAUGUCUA AGUACGCACG GCCGGUACAG UGAAACUGC GAAUGGCUCA UUAAAUCAGU UAUGGUUCCU UUGGUCGCUC GCUCCUCUCC CACUUGGAUA ACUGUGGUAA U UCUAGAGC ...String:
UACCUGGUUG AUCCUGCCAG UAGCAUAUGC UUGUCUCAAA GAUUAAGCCA UGCAUGUCUA AGUACGCACG GCCGGUACAG UGAAACUGC GAAUGGCUCA UUAAAUCAGU UAUGGUUCCU UUGGUCGCUC GCUCCUCUCC CACUUGGAUA ACUGUGGUAA U UCUAGAGC UAAUACAUGC CGACGGGCGC UGACCCCCUU CGCGGGGGGG AUGCGUGCAU UUAUCAGUGG UGACUCUAGA UA ACCUCGG GCCGAUCGCA CGCCCCCCGU GGCGGCGACG ACCCAUUCGA ACGUCUGCCC UAUCAACUUU CGAUGGUAGU CGC CGUGCC UACCAUGGUG ACCACGGGUG ACGGGGAAUC AGGGUUCGAU UCCGGAGAGG GAGCCUGAGA AACGGCUACC ACAU CCAAG GAAGGCAGCA GGCGCGCAAA UUACCCACUC CCGACCCGGG GAGGUAGUGA CGAAAAAUAA CAAUACAGGA CUCUU UCGA GGCCCUGUAA UUGGAAUGAG UCCACUUUAA AUCCUUCCGC GAGGAUCCAU UGGAGGGCAA GUCUGGUGCC AGCAGC CGC GGUAAUUCCA GCUCCAAUAG CGUAUAUUAA AGUUGCUGCA GUUAAAAAGC UCGUAGUUGG AUCUUGGGAG CGGGCGU CC CCGCCCUCUC GGCCGGGGCC CGAAGCAUUU ACUUUGAAAA AAUUAGAGUG UUCAAAGCAG GCCCGAGCCG CCUGGAUA C CGCAGCUAGG AAUAAUGGAA UAGGACCGCG GUUCUAUUUU GUUGGUUUUC GGAACUGAGG CCAUGAUUAA GAGGGACGG CCGGGGGCAU UCGUAUUGCG CCGCUAGAGG UGAAAUUCUU GGACCGGCGC AAGACGGACC AGAGCGAAAG CAUUUGCCAA GAAUGUUUU CAUUAAUCAA GAACGAAAGU CGGAGGUUCG AAGACGAUCA GAUACCGUCG UAGUUCCGAC CAUAAACGAU G CCGACUGG CGAUGCGGCG GCGUUAUUCC CAUGACCCGC CGGGCAGCUU CCGGGAAACC AAAGUCUUUG GGUUCCGGGG GG AGUAUGG UUGCAAAGCU GAAACUUAAA GGAAUUGACG GAAGGGCACC ACCAGGAGUG GAGCCUGCGG CUUAAUUUGA CUC AACACG GGAAACCUCA CCCGGCCCGG ACACGGACAG GAUUGACAGA UUGAUAGCUC UUUCUCGAUU CCGUGGGUGG UGGU GCAUG GCCGUUCUUA GUUGGUGGAG CGAUUUGUCU GGUUAAUUCC GAUAACGAAC GAGACUCUGG CAUGCUAACU AGUUA CGCG ACCCCCGAGC GGUCGGCGUC CCCCAACUUC UUAGAGGGAC AAGUGGCGUU CAGCCACCCG AGAUUGAGCA AUAACA GGU CUGUGAUGCC CUUAGAUGUC CGGGGCUGCA CGCGCGCUAC ACUGACUGGC UCAGCGUGUG CCUACCCUAC GCCGGCA GG CGCGGGUAAC CCGUUGAACC CCAUUCGUGA UGGGGAUCGG GGAUUGCAAU UAUUCCCCAU GAACGAGGAA UUCCCAGU A AGUGCGGGUC AUAAGCUUGC GUUGAUUAAG UCCCUGCCCU UUGUACACAC CGCCCGUCGC UACUACCGAU UGGAUGGUU UAGUGAGGCC CUCGGAUCGG CCCCGCCGGG GUCGGCCCAC GGCCCUGGCG GAGCGCUGAG AAGACGGUCG AACUUGACUA UCUAGAGGA AGUAAAAGUC GUAACAAGGU UUCCGUAGGU GAACCUGCGG AAGGAUCAUU A

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Macromolecule #35: E-site tRNA

MacromoleculeName: E-site tRNA / type: rna / ID: 35 / Number of copies: 1
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 24.004262 KDa
SequenceString:
UCCGAUAUAG CGUAACGGCU AUCACAUCAC GCUUUCACCG UGGAGACCGG GGUUCGACUC CCCGUAUCGG AGCCA

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Macromolecule #2: 40S ribosomal protein SA

MacromoleculeName: 40S ribosomal protein SA / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 24.774365 KDa
SequenceString: GALDVLQMKE EDVLKFLAAG THLGGTNLDF QMEQYIYKRK SDGIYIINLK RTWEKLLLAA RAIVAIENPA DVSVISSRNT GQRAVLKFA AATGATPIAG RFTPGTFTNQ IQAAFREPRL LVVTDPRADH QPLTEASYVN LPTIALCNTD SPLRYVDIAI P CNNKGAHS ...String:
GALDVLQMKE EDVLKFLAAG THLGGTNLDF QMEQYIYKRK SDGIYIINLK RTWEKLLLAA RAIVAIENPA DVSVISSRNT GQRAVLKFA AATGATPIAG RFTPGTFTNQ IQAAFREPRL LVVTDPRADH QPLTEASYVN LPTIALCNTD SPLRYVDIAI P CNNKGAHS VGLMWWMLAR EVLRMRGTIS REHPWEVMPD LYFYRDPEEI EKEEQAAAEK AVT

UniProtKB: Small ribosomal subunit protein uS2

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Macromolecule #3: 40S ribosomal protein S3a

MacromoleculeName: 40S ribosomal protein S3a / type: protein_or_peptide / ID: 3 / 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 #4: 40S ribosomal protein S3

MacromoleculeName: 40S ribosomal protein S3 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA-(apurinic or apyrimidinic site) lyase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 25.172561 KDa
SequenceString: MAVQISKKRK FVADGIFKAE LNEFLTRELA EDGYSGVEVR VTPTRTEIII LATRTQNVLG EKGRRIRELT AVVQKRFGFP EGSVELYAE KVATRGLCAI AQAESLRYKL LGGLAVRRAC YGVLRFIMES GAKGCEVVVS GKLRGQRAKS MKFVDGLMIH S GDPVNYYV ...String:
MAVQISKKRK FVADGIFKAE LNEFLTRELA EDGYSGVEVR VTPTRTEIII LATRTQNVLG EKGRRIRELT AVVQKRFGFP EGSVELYAE KVATRGLCAI AQAESLRYKL LGGLAVRRAC YGVLRFIMES GAKGCEVVVS GKLRGQRAKS MKFVDGLMIH S GDPVNYYV DTAVRHVLLR QGVLGIKVKI MLPWDPTGKI GPKKPLPDHV SIVEPKDEIL PTTPISEQK

UniProtKB: Small ribosomal subunit protein uS3

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

MacromoleculeName: 40S ribosomal protein S4, X isoform / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 29.523674 KDa
SequenceString: ARGPKKHLKR VAAPKHWMLD KLTGVFAPRP STGPHKLREC LPLIIFLRNR LKYALTGDEV KKICMQRFIK IDGKVRTDIT YPAGFMDVI SIDKTGENFR LIYDTKGRFA VHRITPEEAK YKLCKVRKIF VGTKGIPHLV THDARTIRYP DPLIKVNDTI Q IDLETGKI ...String:
ARGPKKHLKR VAAPKHWMLD KLTGVFAPRP STGPHKLREC LPLIIFLRNR LKYALTGDEV KKICMQRFIK IDGKVRTDIT YPAGFMDVI SIDKTGENFR LIYDTKGRFA VHRITPEEAK YKLCKVRKIF VGTKGIPHLV THDARTIRYP DPLIKVNDTI Q IDLETGKI TDFIKFDTGN LCMVTGGANL GRIGVITNRE RHPGSFDVVH VKDANGNSFA TRLSNIFVIG KGNKPWISLP RG KGIRLTI AEERDKRLAA KQSSG

UniProtKB: Small ribosomal subunit protein eS4, X isoform

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Macromolecule #6: 40S ribosomal protein S5

MacromoleculeName: 40S ribosomal protein S5 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 21.327723 KDa
SequenceString:
DIKLFGKWST DDVQINDISL QDYIAVKEKY AKYLPHSAGR YAAKRFRKAQ CPIVERLTNS MMMHGRNNGK KLMTVRIVKH AFEIIHLLT GENPLQVLVN AIINSGPRED STRIGRAGTV RRQAVDVSPL RRVNQAIWLL CTGAREAAFR NIKTIAECLA D ELINAAKG SSNSYAIKKK DELERVAKSN R

UniProtKB: Small ribosomal subunit protein uS7

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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: 21.603229 KDa
SequenceString:
SAKIVKPNGE KPDEFESGIS QALLELEMNS DLKAQLRELN ITAAKEIEVG GGRKAIIIFV PVPQLKSFQK IQVRLVRELE KKFSGKHVV FIAQRRILPK PTRKSRTKNK QKRPRSRTLT AVHDAILEDL VFPSEIVGKR IRVKLDGSRL IKVHLDKAQQ N NVEHKVET FSGVYKKLTG KDVNFEFPEF Q

UniProtKB: Small ribosomal subunit protein eS7

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Macromolecule #8: 40S ribosomal protein S8

MacromoleculeName: 40S ribosomal protein S8 / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 24.003012 KDa
SequenceString: GISRDNWHKR RKTGGKRKPY HKKRKYELGR PAANTKIGPR RIHTVRVRGG NKKYRALRLD VGNFSWGSEC CTRKTRIIDV VYNASNNEL VRTKTLVKNC IVLIDSTPYR QWYESHYALP LGRKKGAKLT PEEEEILNKK RSKKIQKKYD ERKKNAKISS L LEEQFQQG ...String:
GISRDNWHKR RKTGGKRKPY HKKRKYELGR PAANTKIGPR RIHTVRVRGG NKKYRALRLD VGNFSWGSEC CTRKTRIIDV VYNASNNEL VRTKTLVKNC IVLIDSTPYR QWYESHYALP LGRKKGAKLT PEEEEILNKK RSKKIQKKYD ERKKNAKISS L LEEQFQQG KLLACIASRP GQCGRADGYV LEGKELEFYL RKIKARKG

UniProtKB: Small ribosomal subunit protein eS8

+
Macromolecule #9: 40S ribosomal protein S10

MacromoleculeName: 40S ribosomal protein S10 / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 11.773953 KDa
SequenceString:
MLMPKKNRIA IYELLFKEGV MVAKKDVHMP KHPELADKNV PNLHVMKAMQ SLKSRGYVKE QFAWRHFYWY LTNEGIQYLR DYLHLPPEI VPATLRRSR

UniProtKB: Small ribosomal subunit protein eS10

+
Macromolecule #10: 40S ribosomal protein S11

MacromoleculeName: 40S ribosomal protein S11 / type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 17.785971 KDa
SequenceString:
ADIQTERAYQ KQPTIFQNKK RVLLGETGKE KLPRYYKNIG LGFKTPKEAI EGTYIDKKCP FTGNVSIRGR ILSGVVTKMK MQRTIVIRR DYLHYIRKYN RFEKRHKNMS VHLSPCFRDV QIGDIVTVGE CRPLSKTVRF NVLKVTKAAG TKKQ

UniProtKB: Small ribosomal subunit protein uS17

+
Macromolecule #11: 40S ribosomal protein S15

MacromoleculeName: 40S ribosomal protein S15 / type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 15.156846 KDa
SequenceString:
RTFRKFTYRG VDLDQLLDMS YEQLMQLYSA RQRRRLNRGL RRKQHSLLKR LRKAKKEAPP MEKPEVVKTH LRDMIILPEM VGSMVGVYN GKTFNQVEIK PEMIGHYLGE FSITYKPVKH GRPGIGATHS

UniProtKB: Small ribosomal subunit protein uS19

+
Macromolecule #12: 40S ribosomal protein S16

MacromoleculeName: 40S ribosomal protein S16 / type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 16.249062 KDa
SequenceString:
SKGPLQSVQV FGRKKTATAV AHCKRGNGLI KVNGRPLEMI EPRTLQYKLL EPVLLLGKER FAGVDIRVRV KGGGHVAQIY AIRQSISKA LVAYYQKYVD EASKKEIKDI LIQYDRTLLV ADPRRCESKK FGGPGARARY QKSYR

UniProtKB: Small ribosomal subunit protein uS9

+
Macromolecule #13: 40S ribosomal protein S17

MacromoleculeName: 40S ribosomal protein S17 / type: protein_or_peptide / ID: 13 / 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 #14: 40S ribosomal protein S18

MacromoleculeName: 40S ribosomal protein S18 / type: protein_or_peptide / ID: 14 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 17.029844 KDa
SequenceString:
MSLVIPEKFQ HILRVLNTNI DGRRKIAFAI TAIKGVGRRY AHVVLRKADI DLTKRAGELT EDEVERVITI MQNPRQYKIP DWFLNRQKD VKDGKYSQVL ANGLDNKLRE DLERLKKIRA HRGLRHFWGL RVRGQHTKTT GRRGRT

UniProtKB: Small ribosomal subunit protein uS13

+
Macromolecule #15: 40S ribosomal protein S19

MacromoleculeName: 40S ribosomal protein S19 / type: protein_or_peptide / ID: 15 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 15.822219 KDa
SequenceString:
PGVTVKDVNQ QEFVRALAAF LKKSGKLKVP EWVDTVKLAK HKELAPYDEN WFYTRAASTA RHLYLRGGAG VGSMTKIYGG RQRNGVMPS HFSRGSKSVA RRVLQALEGL KMVEKDQDGG RKLTPQGQRD LDRIAGQVAA ANKK

UniProtKB: Small ribosomal subunit protein eS19

+
Macromolecule #16: 40S ribosomal protein S20

MacromoleculeName: 40S ribosomal protein S20 / type: protein_or_peptide / ID: 16 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 11.76589 KDa
SequenceString:
AIHRIRITLT SRNVKSLEKV CADLIRGAKE KNLKVKGPVR MPTKTLRITT RKTPCGEGSK TWDRFQMRIH KRLIDLHSPS EIVKQITSI SIEPGVEVEV TIADA

UniProtKB: Small ribosomal subunit protein uS10

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Macromolecule #17: 40S ribosomal protein S21

MacromoleculeName: 40S ribosomal protein S21 / type: protein_or_peptide / ID: 17 / 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

+
Macromolecule #18: 40S ribosomal protein S23

MacromoleculeName: 40S ribosomal protein S23 / type: protein_or_peptide / ID: 18 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 15.626392 KDa
SequenceString:
GKCRGLRTAR KLRSHRRDQK WHDKQYKKAH LGTALKANPF GGASHAKGIV LEKVGVEAKQ PNSAIRKCVR VQLIKNGKKI TAFVPNDGC LNFIEENDEV LVAGFGRKGH AVGDIPGVRF KVVKVANVSL LALYKGKKER PR

UniProtKB: Small ribosomal subunit protein uS12

+
Macromolecule #19: 40S ribosomal protein S26

MacromoleculeName: 40S ribosomal protein S26 / type: protein_or_peptide / ID: 19 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 11.742908 KDa
SequenceString:
TKKRRNNGRA KKGRGHVQPI RCTNCARCVP KDKAIKKFVI RNIVEAAAVR DISEASVFDA YVLPKLYVKL HYCVSCAIHS KVVRNRSRE ARKDRTPPPR FRP

UniProtKB: Small ribosomal subunit protein eS26

+
Macromolecule #20: 40S ribosomal protein S28

MacromoleculeName: 40S ribosomal protein S28 / type: protein_or_peptide / ID: 20 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 7.263394 KDa
SequenceString:
RVQPIKLARV TKVLGRTGSQ GQCTQVRVEF MDDTSRSIIR NVKGPVREGD VLTLLESERE ARRL

UniProtKB: Small ribosomal subunit protein eS28

+
Macromolecule #21: 40S ribosomal protein S29

MacromoleculeName: 40S ribosomal protein S29 / type: protein_or_peptide / ID: 21 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 6.559625 KDa
SequenceString:
GHQQLYWSHP RKFGQGSRSC RVCSNRHGLI RKYGLNMCRQ CFRQYAKDIG FIKLD

UniProtKB: Small ribosomal subunit protein uS14

+
Macromolecule #22: Receptor of activated protein C kinase 1

MacromoleculeName: Receptor of activated protein C kinase 1 / type: protein_or_peptide / ID: 22 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 34.669113 KDa
SequenceString: TEQMTLRGTL KGHNGWVTQI ATTPQFPDMI LSASRDKTII MWKLTRDETN YGIPQRALRG HSHFVSDVVI SSDGQFALSG SWDGTLRLW DLTTGTTTRR FVGHTKDVLS VAFSSDNRQI VSGSRDKTIK LWNTLGVCKY TVQDESHSEW VSCVRFSPNS S NPIIVSCG ...String:
TEQMTLRGTL KGHNGWVTQI ATTPQFPDMI LSASRDKTII MWKLTRDETN YGIPQRALRG HSHFVSDVVI SSDGQFALSG SWDGTLRLW DLTTGTTTRR FVGHTKDVLS VAFSSDNRQI VSGSRDKTIK LWNTLGVCKY TVQDESHSEW VSCVRFSPNS S NPIIVSCG WDKLVKVWNL ANCKLKTNHI GHTGYLNTVT VSPDGSLCAS GGKDGQAMLW DLNEGKHLYT LDGGDIINAL CF SPNRYWL CAATGPSIKI WDLEGKIIVD ELKQEVISTS SKAEPPQCTS LAWSADGQTL FAGYTDNLVR VWQVTI

UniProtKB: Small ribosomal subunit protein RACK1

+
Macromolecule #23: 40S ribosomal protein S2

MacromoleculeName: 40S ribosomal protein S2 / type: protein_or_peptide / ID: 23 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 24.587029 KDa
SequenceString: EWMPVTKLGR LVKDMKIKSL EEIYLFSLPI KESEIIDFFL GASLKDEVLK IMPVQKQTRA GQRTRFKAFV AIGDYNGHVG LGVKCSKEV ATAIRGAIIL AKLSIVPVRR GYWGNKIGKP HTVPCKVTGR CGSVLVRLIP APRGTGIVSA PVPKKLLMMA G IDDCYTSA ...String:
EWMPVTKLGR LVKDMKIKSL EEIYLFSLPI KESEIIDFFL GASLKDEVLK IMPVQKQTRA GQRTRFKAFV AIGDYNGHVG LGVKCSKEV ATAIRGAIIL AKLSIVPVRR GYWGNKIGKP HTVPCKVTGR CGSVLVRLIP APRGTGIVSA PVPKKLLMMA G IDDCYTSA RGCTATLGNF AKATFDAISK TYSYLTPDLW KETVFTKSPY QEFTDHLVKT HTRV

UniProtKB: Small ribosomal subunit protein uS5

+
Macromolecule #24: 40S ribosomal protein S6

MacromoleculeName: 40S ribosomal protein S6 / type: protein_or_peptide / ID: 24 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 27.471535 KDa
SequenceString: MKLNISFPAT GCQKLIEVDD ERKLRTFYEK RMATEVAADA LGEEWKGYVV RISGGNDKQG FPMKQGVLTH GRVRLLLSKG HSCYRPRRT GERKRKSVRG CIVDANLSVL NLVIVKKGEK DIPGLTDTTV PRRLGPKRAS RIRKLFNLSK EDDVRQYVVR K PLNKEGKK ...String:
MKLNISFPAT GCQKLIEVDD ERKLRTFYEK RMATEVAADA LGEEWKGYVV RISGGNDKQG FPMKQGVLTH GRVRLLLSKG HSCYRPRRT GERKRKSVRG CIVDANLSVL NLVIVKKGEK DIPGLTDTTV PRRLGPKRAS RIRKLFNLSK EDDVRQYVVR K PLNKEGKK PRTKAPKIQR LVTPRVLQHK RRRIALKKQR TKKNKEEAAE YAKLLAKRMK EAKEKRQEQI AKRRRLSSL

UniProtKB: Small ribosomal subunit protein eS6

+
Macromolecule #25: 40S ribosomal protein S9

MacromoleculeName: 40S ribosomal protein S9 / type: protein_or_peptide / ID: 25 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 21.649633 KDa
SequenceString:
PVARSWVCRK TYVTPRRPFE KSRLDQELKL IGEYGLRNKR EVWRVKFTLA KIRKAARELL TLDEKDPRRL FEGNALLRRL VRIGVLDEG KMKLDYILGL KIEDFLERRL QTQVFKLGLA KSIHHARVLI RQRHIRVRKQ VVNIPSFIVR LDSQKHIDFS L RSPYGGGR PGRVKRKNAK KGQGGAG

UniProtKB: Small ribosomal subunit protein uS4

+
Macromolecule #26: 40S ribosomal protein S12

MacromoleculeName: 40S ribosomal protein S12 / type: protein_or_peptide / ID: 26 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 13.661928 KDa
SequenceString:
VMDVNTALQE VLKTALIHDG LARGIREAAK ALDKRQAHLC VQASNCDEPM YVKLVEALLA EHQINLIKVD DNKKLGEWVG LCKIDREGN PRKVVGCSCV VVKDYGKESQ AKDVIEEYFK CKK

UniProtKB: Small ribosomal subunit protein eS12

+
Macromolecule #27: 40S ribosomal protein S13

MacromoleculeName: 40S ribosomal protein S13 / type: protein_or_peptide / ID: 27 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 17.128191 KDa
SequenceString:
GRMHAPGKGL SQSALPYRRS VPTWLKLTSD DVKEQIYKLA KKGLTPSQIG VILRDSHGVA QVRFVTGNKI LRILKSKGLA PDLPEDLYH LIKKAVAVRK HLERNRKDKD AKFRLILIES RIHRLARYYK TKRVLPPNWK YESSTASALV A

UniProtKB: Small ribosomal subunit protein uS15

+
Macromolecule #28: 40S ribosomal protein S14

MacromoleculeName: 40S ribosomal protein S14 / type: protein_or_peptide / ID: 28 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 15.014187 KDa
SequenceString:
EQVISLGPQV AEGENVFGVC HIFASFNDTF VHVTDLSGKE TICRVTGGMK VKADRDESSP YAAMLAAQDV AQRCKELGIT ALHIKLRAT GGNRTKTPGP GAQSALRALA RSGMKIGRIE DVTPIPSDST RRKGGRRGRR L

UniProtKB: Small ribosomal subunit protein uS11

+
Macromolecule #29: 40S ribosomal protein S15a

MacromoleculeName: 40S ribosomal protein S15a / type: protein_or_peptide / ID: 29 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 14.734357 KDa
SequenceString:
VRMNVLADAL KSINNAEKRG KRQVLIRPCS KVIVRFLTVM MKHGYIGEFE IIDDHRAGKI VVNLTGRLNK CGVISPRFDV QLKDLEKWQ NNLLPSRQFG FIVLTTSAGI MDHEEARRKH TGGKILGFFF

UniProtKB: Small ribosomal subunit protein uS8

+
Macromolecule #30: 40S ribosomal protein S24

MacromoleculeName: 40S ribosomal protein S24 / type: protein_or_peptide / ID: 30 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 15.203022 KDa
SequenceString:
NDTVTIRTRK FMTNRLLQRK QMVIDVLHPG KATVPKTEIR EKLAKMYKTT PDVIFVFGFR THFGGGKTTG FGMIYDSLDY AKKNEPKHR LARHGLYEKK KTSRKQRKER KNRMKKVRGT AKANVGAGKK PK

UniProtKB: Small ribosomal subunit protein eS24

+
Macromolecule #31: 40S ribosomal protein S25

MacromoleculeName: 40S ribosomal protein S25 / type: protein_or_peptide / ID: 31 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 8.526119 KDa
SequenceString:
RDKLNNLVLF DKATYDKLCK EVPNYKLITP AVVSERLKIR GSLARAALQE LLSKGLIKLV SKHRAQVIYT RNTKG

UniProtKB: Small ribosomal subunit protein eS25

+
Macromolecule #32: 40S ribosomal protein S27

MacromoleculeName: 40S ribosomal protein S27 / type: protein_or_peptide / ID: 32 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 9.34899 KDa
SequenceString:
PLAKDLLHPS PEEEKRKHKK KRLVQSPNSY FMDVKCPGCY KITTVFSHAQ TVVLCVGCST VLCQPTGGKA RLTEGCSFRR KQH

UniProtKB: Small ribosomal subunit protein eS27

+
Macromolecule #33: 40S ribosomal protein S30

MacromoleculeName: 40S ribosomal protein S30 / type: protein_or_peptide / ID: 33 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 4.896883 KDa
SequenceString:
VHGSLARAGK VRGQTPKVAK QEKKKKKTGR AKRRMQYNRR FV

UniProtKB: Ubiquitin-like FUBI-ribosomal protein eS30 fusion protein

+
Macromolecule #34: Ubiquitin-40S ribosomal protein S27a

MacromoleculeName: Ubiquitin-40S ribosomal protein S27a / type: protein_or_peptide / ID: 34 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 7.884286 KDa
SequenceString:
YTTPKKNKHK RKKVKLAVLK YYKVDENGKI SRLRRECPSD ECGAGVFMAS HFDRHYCGKC CLTYCFN

UniProtKB: Ubiquitin-ribosomal protein eS31 fusion protein

+
Macromolecule #36: Cell growth-regulating nucleolar protein

MacromoleculeName: Cell growth-regulating nucleolar protein / type: protein_or_peptide / ID: 36 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 8.557207 KDa
SequenceString:
KFNWKGTIKA ILKQAPDNEI TIKKLRKKVL AQYYTVTDEH HRSEEELLVI FNKKISKNPT FKLLKDKVKL VK

UniProtKB: Cell growth-regulating nucleolar protein

+
Macromolecule #37: Endothelial differentiation-related factor 1

MacromoleculeName: Endothelial differentiation-related factor 1 / type: protein_or_peptide / ID: 37 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 12.330996 KDa
SequenceString:
SKQAILAAQR RGEDVETSKK WAAGQNKQHS ITKNTAKLDR ETEELHHDRV TLEVGKVIQQ GRQSKGLTQK DLATKINEKP QVIADYESG RAIPNNQVLG KIERAIGLKL R

UniProtKB: Endothelial differentiation-related factor 1

+
Macromolecule #38: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 38 / Number of copies: 30 / Formula: MG
Molecular weightTheoretical: 24.305 Da

+
Macromolecule #39: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 39 / Number of copies: 3 / 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
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 28.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: OTHER / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

+
Image processing

Startup modelType of model: PDB ENTRY
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 81976
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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