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- EMDB-11322: SARS-CoV-2-Nsp1-40S complex, focused on head -

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Basic information

Entry
Database: EMDB / ID: EMD-11322
TitleSARS-CoV-2-Nsp1-40S complex, focused on head
Map data
Sample
  • Complex: SARS-CoV-2-Nsp1-40S complex, focused on head
    • RNA: x 1 types
    • Protein or peptide: x 15 types
  • Ligand: x 2 types
Function / homology
Function and homology information


positive regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis / negative regulation of endoplasmic reticulum unfolded protein response / oxidized pyrimidine DNA binding / response to TNF agonist / positive regulation of base-excision repair / protein tyrosine kinase inhibitor activity / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage / positive regulation of respiratory burst involved in inflammatory response / positive regulation of gastrulation / IRE1-RACK1-PP2A complex ...positive regulation of cysteine-type endopeptidase activity involved in execution phase of apoptosis / negative regulation of endoplasmic reticulum unfolded protein response / oxidized pyrimidine DNA binding / response to TNF agonist / positive regulation of base-excision repair / protein tyrosine kinase inhibitor activity / positive regulation of intrinsic apoptotic signaling pathway in response to DNA damage / positive regulation of respiratory burst involved in inflammatory response / positive regulation of gastrulation / IRE1-RACK1-PP2A complex / nucleolus organization / response to extracellular stimulus / positive regulation of endodeoxyribonuclease activity / positive regulation of Golgi to plasma membrane protein transport / TNFR1-mediated ceramide production / negative regulation of DNA repair / oxidized purine DNA binding / negative regulation of intrinsic apoptotic signaling pathway in response to hydrogen peroxide / supercoiled DNA binding / NF-kappaB complex / negative regulation of phagocytosis / ubiquitin-like protein conjugating enzyme binding / regulation of establishment of cell polarity / Formation of the ternary complex, and subsequently, the 43S complex / erythrocyte homeostasis / cytoplasmic side of rough endoplasmic reticulum membrane / positive regulation of signal transduction by p53 class mediator / ubiquitin ligase inhibitor activity / pigmentation / protein kinase A binding / Ribosomal scanning and start codon recognition / ion channel inhibitor activity / Translation initiation complex formation / phagocytic cup / positive regulation of mitochondrial depolarization / negative regulation of Wnt signaling pathway / positive regulation of T cell receptor signaling pathway / positive regulation of activated T cell proliferation / fibroblast growth factor binding / regulation of cell division / SARS-CoV-1 modulates host translation machinery / iron-sulfur cluster binding / BH3 domain binding / Peptide chain elongation / Selenocysteine synthesis / monocyte chemotaxis / cysteine-type endopeptidase activator activity involved in apoptotic process / Formation of a pool of free 40S subunits / ribosomal small subunit export from nucleus / positive regulation of cyclic-nucleotide phosphodiesterase activity / Eukaryotic Translation Termination / Response of EIF2AK4 (GCN2) to amino acid deficiency / translation regulator activity / 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 / negative regulation of respiratory burst involved in inflammatory response / negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / L13a-mediated translational silencing of Ceruloplasmin expression / Major pathway of rRNA processing in the nucleolus and cytosol / gastrulation / spindle assembly / regulation of translational fidelity / MDM2/MDM4 family protein binding / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / negative regulation of smoothened signaling pathway / rescue of stalled ribosome / signaling adaptor activity / negative regulation of peptidyl-serine phosphorylation / maturation of SSU-rRNA / positive regulation of intrinsic apoptotic signaling pathway / maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / class I DNA-(apurinic or apyrimidinic site) endonuclease activity / positive regulation of apoptotic signaling pathway / Maturation of protein E / positive regulation of microtubule polymerization / Maturation of protein E / positive regulation of JUN kinase activity / ER Quality Control Compartment (ERQC) / negative regulation of protein ubiquitination / translational initiation / Myoclonic epilepsy of Lafora / FLT3 signaling by CBL mutants / DNA-(apurinic or apyrimidinic site) endonuclease activity / Prevention of phagosomal-lysosomal fusion / IRAK2 mediated activation of TAK1 complex / Alpha-protein kinase 1 signaling pathway / Glycogen synthesis / IRAK1 recruits IKK complex / IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation / Membrane binding and targetting of GAG proteins / Constitutive Signaling by NOTCH1 HD Domain Mutants / NOTCH2 Activation and Transmission of Signal to the Nucleus / Hsp70 protein binding / Endosomal Sorting Complex Required For Transport (ESCRT) / IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation / Regulation of FZD by ubiquitination / PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1 / Negative regulation of FLT3
Similarity search - Function
: / Ribosomal protein S12e / Small (40S) ribosomal subunit Asc1/RACK1 / Ribosomal protein S19e, conserved site / S27a-like superfamily / Ribosomal protein S10, eukaryotic/archaeal / Ribosomal protein S25 / Ribosomal protein S17e, conserved site / 40S ribosomal protein S29/30S ribosomal protein S14 type Z / Ribosomal protein S27a ...: / Ribosomal protein S12e / Small (40S) ribosomal subunit Asc1/RACK1 / Ribosomal protein S19e, conserved site / S27a-like superfamily / Ribosomal protein S10, eukaryotic/archaeal / Ribosomal protein S25 / Ribosomal protein S17e, conserved site / 40S ribosomal protein S29/30S ribosomal protein S14 type Z / Ribosomal protein S27a / Ribosomal protein S27a / Ribosomal protein S3, eukaryotic/archaeal / S25 ribosomal protein / Ribosomal protein S19A/S15e / Ribosomal protein S12e signature. / Ribosomal protein S17e / Ribosomal protein S17e-like superfamily / Ribosomal protein S27a / Ribosomal protein S19e / Ribosomal_S19e / Ribosomal S17 / Ribosomal protein S19e signature. / Ribosomal protein S19e / 40S Ribosomal protein S10 / Ribosomal protein S28e conserved site / Ribosomal protein S28e / Plectin/S10, N-terminal / Plectin/S10 domain / Ribosomal protein S5/S7, eukaryotic/archaeal / Ribosomal protein S17e signature. / Ribosomal protein S28e / Ribosomal protein S28e signature. / Ribosomal protein L7Ae/L30e/S12e/Gadd45 / Ribosomal protein S14/S29 / Ribosomal protein L7Ae/L30e/S12e/Gadd45 family / 50S ribosomal protein L30e-like / Ubiquitin conserved site / Ubiquitin domain / Ubiquitin domain signature. / Ribosomal protein S3, conserved site / Ribosomal protein S14, conserved site / Ribosomal protein S10, conserved site / K Homology domain, type 2 / Ribosomal protein S3, C-terminal / Ribosomal protein S3, C-terminal domain superfamily / Ribosomal protein S15/S19, conserved site / KH domain / Ribosomal protein S19/S15 / Ribosomal protein S19/S15, superfamily / Ribosomal protein S10 / Ribosomal protein S3, C-terminal domain / Ribosomal protein S3 signature. / Ribosomal protein S10 signature. / Ribosomal protein S14 signature. / Ribosomal protein S7, conserved site / K homology domain superfamily, prokaryotic type / Ribosomal protein S19 / Ubiquitin family / Ribosomal protein S13, conserved site / Ribosomal protein S13 / 30s ribosomal protein S13, C-terminal / Ribosomal protein S14 / Type-2 KH domain profile. / Ribosomal protein S13/S18 / Ubiquitin homologues / Ribosomal protein S19 signature. / K homology domain-like, alpha/beta / Ribosomal protein S14p/S29e / Ribosomal protein S7 signature. / Ribosomal protein S10p/S20e / Ribosomal protein S9, conserved site / Ribosomal protein S10 domain / Ribosomal protein S10 domain superfamily / Ribosomal protein S13-like, H2TH / Ubiquitin-like domain / Ribosomal protein S13 signature. / Ribosomal protein S5/S7 / Ribosomal protein S7 domain / Ribosomal protein S7 domain superfamily / Ribosomal protein S13 family profile. / Ribosomal protein S10p/S20e / Ribosomal protein S9 / Ribosomal protein S7p/S5e / Ribosomal protein S9/S16 / Ubiquitin domain profile. / Ribosomal protein S9 signature. / Zinc-binding ribosomal protein / Ribosomal protein S5 domain 2-type fold, subgroup / G-protein beta WD-40 repeat / Ubiquitin-like domain superfamily / Winged helix DNA-binding domain superfamily / WD40 repeat, conserved site / Ribosomal protein S5 domain 2-type fold / Trp-Asp (WD) repeats signature. / WD domain, G-beta repeat / WD40 repeats / WD40 repeat / Trp-Asp (WD) repeats profile. / Trp-Asp (WD) repeats circular profile. / WD40-repeat-containing domain superfamily
Similarity search - Domain/homology
Small ribosomal subunit protein eS17 / Small ribosomal subunit protein uS3 / Small ribosomal subunit protein eS12 / Small ribosomal subunit protein eS19 / Small ribosomal subunit protein uS7 / Small ribosomal subunit protein eS10 / Small ribosomal subunit protein uS10 / Small ribosomal subunit protein uS9 / Small ribosomal subunit protein uS13 / Small ribosomal subunit protein uS14 ...Small ribosomal subunit protein eS17 / Small ribosomal subunit protein uS3 / Small ribosomal subunit protein eS12 / Small ribosomal subunit protein eS19 / Small ribosomal subunit protein uS7 / Small ribosomal subunit protein eS10 / Small ribosomal subunit protein uS10 / Small ribosomal subunit protein uS9 / Small ribosomal subunit protein uS13 / Small ribosomal subunit protein uS14 / Small ribosomal subunit protein uS19 / Small ribosomal subunit protein eS25 / Small ribosomal subunit protein eS28 / Ubiquitin-ribosomal protein eS31 fusion protein / Small ribosomal subunit protein RACK1 / Ubiquitin-ribosomal protein eS31 fusion protein
Similarity search - Component
Biological speciesHomo sapiens (human) / Human (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.8 Å
AuthorsSchubert K / Karousis ED / Jomaa A / Scaiola A / Echeverria B / Gurzeler L-A / Leibundgut ML / Thiel V / Muehlemann O / Ban N
Funding support Switzerland, 3 items
OrganizationGrant numberCountry
Swiss National Science Foundation173085 Switzerland
Swiss National Science Foundation182831 Switzerland
Swiss National Science Foundation182341 Switzerland
CitationJournal: Nat Struct Mol Biol / Year: 2020
Title: SARS-CoV-2 Nsp1 binds the ribosomal mRNA channel to inhibit translation.
Authors: Katharina Schubert / Evangelos D Karousis / Ahmad Jomaa / Alain Scaiola / Blanca Echeverria / Lukas-Adrian Gurzeler / Marc Leibundgut / Volker Thiel / Oliver Mühlemann / Nenad Ban /
Abstract: The SARS-CoV-2 non-structural protein 1 (Nsp1), also referred to as the host shutoff factor, suppresses host innate immune functions. By combining cryo-electron microscopy and biochemistry, we show ...The SARS-CoV-2 non-structural protein 1 (Nsp1), also referred to as the host shutoff factor, suppresses host innate immune functions. By combining cryo-electron microscopy and biochemistry, we show that SARS-CoV-2 Nsp1 binds to the human 40S subunit in ribosomal complexes, including the 43S pre-initiation complex and the non-translating 80S ribosome. The protein inserts its C-terminal domain into the mRNA channel, where it interferes with mRNA binding. We observe translation inhibition in the presence of Nsp1 in an in vitro translation system and in human cells. Based on the high-resolution structure of the 40S-Nsp1 complex, we identify residues of Nsp1 crucial for mediating translation inhibition. We further show that the full-length 5' untranslated region of the genomic viral mRNA stimulates translation in vitro, suggesting that SARS-CoV-2 combines global inhibition of translation by Nsp1 with efficient translation of the viral mRNA to allow expression of viral genes.
History
DepositionJul 7, 2020-
Header (metadata) releaseJul 22, 2020-
Map releaseJul 22, 2020-
UpdateFeb 10, 2021-
Current statusFeb 10, 2021Processing site: PDBe / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.8
  • Imaged by UCSF Chimera
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  • Surface view colored by height
  • Surface level: 0.8
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6zol
  • Surface level: 0.8
  • Imaged by UCSF Chimera
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  • Simplified surface model + fitted atomic model
  • Atomic modelsPDB-6zol
  • Imaged by Jmol
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_11322.png

Downloads & links

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Map

FileDownload / File: emd_11322.map.gz / Format: CCP4 / Size: 669.9 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 1.08 Å
Density
Contour LevelBy AUTHOR: 0.8 / Movie #1: 0.8
Minimum - Maximum-3.122065 - 6.601135
Average (Standard dev.)-0.0015698844 (±0.124801345)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions560560560
Spacing560560560
CellA=B=C: 604.80005 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.081.081.08
M x/y/z560560560
origin x/y/z0.0000.0000.000
length x/y/z604.800604.800604.800
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ250250250
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS560560560
D min/max/mean-3.1226.601-0.002

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Supplemental data

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Mask #1

Fileemd_11322_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_11322_half_map_1.map
Projections & Slices
AxesZYX

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Slices (1/2)
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Histogram

Histogram (log scale)

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Half map: #2

Fileemd_11322_half_map_2.map
Projections & Slices
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Sample components

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Entire : SARS-CoV-2-Nsp1-40S complex, focused on head

EntireName: SARS-CoV-2-Nsp1-40S complex, focused on head
Components
  • Complex: SARS-CoV-2-Nsp1-40S complex, focused on head
    • RNA: 18S ribosomal RNA
    • Protein or peptide: 40S ribosomal protein S3
    • Protein or peptide: 40S ribosomal protein S5
    • Protein or peptide: 40S ribosomal protein S10
    • Protein or peptide: 40S ribosomal protein S12
    • 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 S25
    • Protein or peptide: 40S ribosomal protein S28
    • Protein or peptide: 40S ribosomal protein S29
    • Protein or peptide: Ribosomal protein S27aRibosome
    • Protein or peptide: Receptor of activated protein C kinase 1
  • Ligand: MAGNESIUM ION
  • Ligand: ZINC ION

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Supramolecule #1: SARS-CoV-2-Nsp1-40S complex, focused on head

SupramoleculeName: SARS-CoV-2-Nsp1-40S complex, focused on head / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#16
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: 18S ribosomal RNA

MacromoleculeName: 18S ribosomal RNA / type: rna / ID: 1 / Number of copies: 1
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 602.777875 KDa
SequenceString: UACCUGGUUG AUCCUGCCAG UAGCAUAUGC UUGUCUCAAA GAUUAAGCCA UGCAUGUCUA AGUACGCACG GCCGGUACAG UGAAACUGC GAAUGGCUCA UUAAAUCAGU UAUGGUUCCU UUGGUCGCUC GCUCCUCUCC UACUUGGAUA ACUGUGGUAA U UCUAGAGC ...String:
UACCUGGUUG AUCCUGCCAG UAGCAUAUGC UUGUCUCAAA GAUUAAGCCA UGCAUGUCUA AGUACGCACG GCCGGUACAG UGAAACUGC GAAUGGCUCA UUAAAUCAGU UAUGGUUCCU UUGGUCGCUC GCUCCUCUCC UACUUGGAUA ACUGUGGUAA U UCUAGAGC UAAUACAUGC CGACGGGCGC UGACCCCCUU CGCGGGGGGG AUGCGUGCAU UUAUCAGAUC AAAACCAACC CG GUCAGCC CCUCUCCGGC CCCGGCCGGG GGGCGGGCGC CGGCGGCUUU GGUGACUCUA GAUAACCUCG GGCCGAUCGC ACG CCCCCC GUGGCGGCGA CGACCCAUUC GAACGUCUGC CCUAUCAACU UUCGAUGGUA GUCGCCGUGC CUACCAUGGU GACC ACGGG UGACGGGGAA UCAGGGUUCG AUUCCGGAGA GGGAGCCUGA GAAACGGCUA CCACAUCCAA GGAAGGCAGC AGGCG CGCA AAUUACCCAC UCCCGACCCG GGGAGGUAGU GACGAAAAAU AACAAUACAG GACUCUUUCG AGGCCCUGUA AUUGGA AUG AGUCCACUUU AAAUCCUUUA ACGAGGAUCC AUUGGAGGGC AAGUCUGGUG CCAGCAGCCG CGGUAAUUCC AGCUCCA AU AGCGUAUAUU AAAGUUGCUG CAGUUAAAAA GCUCGUAGUU GGAUCUUGGG AGCGGGCGGG CGGUCCGCCG CGAGGCGA G CCACCGCCCG UCCCCGCCCC UUGCCUCUCG GCGCCCCCUC GAUGCUCUUA GCUGAGUGUC CCGCGGGGCC CGAAGCGUU UACUUUGAAA AAAUUAGAGU GUUCAAAGCA GGCCCGAGCC GCCUGGAUAC CGCAGCUAGG AAUAAUGGAA UAGGACCGCG GUUCUAUUU UGUUGGUUUU CGGAACUGAG GCCAUGAUUA AGAGGGACGG CCGGGGGCAU UCGUAUUGCG CCGCUAGAGG U GAAAUUCU UGGACCGGCG CAAGACGGAC CAGAGCGAAA GCAUUUGCCA AGAAUGUUUU CAUUAAUCAA GAACGAAAGU CG GAGGUUC GAAGACGAUC AGAUACCGUC GUAGUUCCGA CCAUAAACGA UGCCGACCGG CGAUGCGGCG GCGUUAUUCC CAU GACCCG CCGGGCAGCU UCCGGGAAAC CAAAGUCUUU GGGUUCCGGG GGGAGUAUGG UUGCAAAGCU GAAACUUAAA GGAA UUGAC GGAAGGGCAC CACCAGGAGU GGAGCCUGCG GCUUAAUUUG ACUCAACACG GGAAACCUCA CCCGGCCCGG ACACG GACA GGAUUGACAG AUUGAUAGCU CUUUCUCGAU UCCGUGGGUG GUGGUGCAUG GCCGUUCUUA GUUGGUGGAG CGAUUU GUC UGGUUAAUUC CGAUAACGAA CGAGACUCUG GCAUGCUAAC UAGUUACGCG ACCCCCGAGC GGUCGGCGUC CCCCAAC UU CUUAGAGGGA CAAGUGGCGU UCAGCCACCC GAGAUUGAGC AAUAACAGGU CUGUGAUGCC CUUAGAUGUC CGGGGCUG C ACGCGCGCUA CACUGACUGG CUCAGCGUGU GCCUACCCUA CGCCGGCAGG CGCGGGUAAC CCGUUGAACC CCAUUCGUG AUGGGGAUCG GGGAUUGCAA UUAUUCCCCA UGAACGAGGA AUUCCCAGUA AGUGCGGGUC AUAAGCUUGC GUUGAUUAAG UCCCUGCCC UUUGUACACA CCGCCCGUCG CUACUACCGA UUGGAUGGUU UAGUGAGGCC CUCGGAUCGG CCCCGCCGGG G UCGGCCCA CGGCCCUGGC GGAGCGCUGA GAAGACGGUC GAACUUGACU AUCUAGAGGA AGUAAAAGUC GUAACAAGGU UU CCGUAGG UGAACCUGCG GAAGGAUCAU UA

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Macromolecule #2: 40S ribosomal protein S3

MacromoleculeName: 40S ribosomal protein S3 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA-(apurinic or apyrimidinic site) lyase
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 26.729369 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 PTTPISEQKG GKPEPPAMPQ PV PTA

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Macromolecule #3: 40S ribosomal protein S5

MacromoleculeName: 40S ribosomal protein S5 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 22.913453 KDa
SequenceString: MTEWETAAPA VAETPDIKLF GKWSTDDVQI NDISLQDYIA VKEKYAKYLP HSAGRYAAKR FRKAQCPIVE RLTNSMMMHG RNNGKKLMT VRIVKHAFEI IHLLTGENPL QVLVNAIINS GPREDSTRIG RAGTVRRQAV DVSPLRRVNQ AIWLLCTGAR E AAFRNIKT ...String:
MTEWETAAPA VAETPDIKLF GKWSTDDVQI NDISLQDYIA VKEKYAKYLP HSAGRYAAKR FRKAQCPIVE RLTNSMMMHG RNNGKKLMT VRIVKHAFEI IHLLTGENPL QVLVNAIINS GPREDSTRIG RAGTVRRQAV DVSPLRRVNQ AIWLLCTGAR E AAFRNIKT IAECLADELI NAAKGSSNSY AIKKKDELER VAKSNR

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Macromolecule #4: 40S ribosomal protein S10

MacromoleculeName: 40S ribosomal protein S10 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 18.933846 KDa
SequenceString:
MLMPKKNRIA IYELLFKEGV MVAKKDVHMP KHPELADKNV PNLHVMKAMQ SLKSRGYVKE QFAWRHFYWY LTNEGIQYLR DYLHLPPEI VPATLRRSRP ETGRPRPKGL EGERPARLTR GEADRDTYRR SAVPPGADKK AEAGAGSATE FQFRGGFGRG R GQPPQ

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Macromolecule #5: 40S ribosomal protein S12

MacromoleculeName: 40S ribosomal protein S12 / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 14.538987 KDa
SequenceString:
MAEEGIAAGG VMDVNTALQE VLKTALIHDG LARGIREAAK ALDKRQAHLC VLASNCDEPM YVKLVEALCA EHQINLIKVD DNKKLGEWV GLCKIDREGK PRKVVGCSCV VVKDYGKESQ AKDVIEEYFK CKK

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Macromolecule #6: 40S ribosomal protein S15

MacromoleculeName: 40S ribosomal protein S15 / type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 17.076207 KDa
SequenceString:
MAEVEQKKKR TFRKFTYRGV DLDQLLDMSY EQLMQLYSAR QRRRLNRGLR RKQHSLLKRL RKAKKEAPPM EKPEVVKTHL RDMIILPEM VGSMVGVYNG KTFNQVEIKP EMIGHYLGEF SITYKPVKHG RPGIGATHSS RFIPLK

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Macromolecule #7: 40S ribosomal protein S16

MacromoleculeName: 40S ribosomal protein S16 / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 16.477377 KDa
SequenceString:
MPSKGPLQSV QVFGRKKTAT AVAHCKRGNG LIKVNGRPLE MIEPRTLQYK LLEPVLLLGK ERFAGVDIRV RVKGGGHVAQ IYAIRQSIS KALVAYYQKY VDEASKKEIK DILIQYDRTL LVADPRRCES KKFGGPGARA RYQKSYR

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Macromolecule #8: 40S ribosomal protein S17

MacromoleculeName: 40S ribosomal protein S17 / type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 15.578156 KDa
SequenceString:
MGRVRTKTVK KAARVIIEKY YTRLGNDFHT NKRVCEEIAI IPSKKLRNKI AGYVTHLMKR IQRGPVRGIS IKLQEEERER RDNYVPEVS ALDQEIIEVD PDTKEMLKLL DFGSLSNLQV TQPTVGMNFK TPRGPV

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Macromolecule #9: 40S ribosomal protein S18

MacromoleculeName: 40S ribosomal protein S18 / type: protein_or_peptide / ID: 9 / Details: P62269 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 17.759777 KDa
SequenceString:
MSLVIPEKFQ HILRVLNTNI DGRRKIAFAI TAIKGVGRRY AHVVLRKADI DLTKRAGELT EDEVERVITI MQNPRQYKIP DWFLNRQKD VKDGKYSQVL ANGLDNKLRE DLERLKKIRA HRGLRHFWGL RVRGQHTKTT GRRGRTVGVS KKK

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Macromolecule #10: 40S ribosomal protein S19

MacromoleculeName: 40S ribosomal protein S19 / type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 16.091562 KDa
SequenceString:
MPGVTVKDVN QQEFVRALAA FLKKSGKLKV PEWVDTVKLA KHKELAPYDE NWFYTRAAST ARHLYLRGGA GVGSMTKIYG GRQRNGVMP SHFSRGSKSV ARRVLQALEG LKMVEKDQDG GRKLTPQGQR DLDRIAGQVA AANKKH

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Macromolecule #11: 40S ribosomal protein S20

MacromoleculeName: 40S ribosomal protein S20 / type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 13.398763 KDa
SequenceString:
MAFKDTGKTP VEPEVAIHRI RITLTSRNVK SLEKVCADLI RGAKEKNLKV KGPVRMPTKT LRITTRKTPC GEGSKTWDRF QMRIHKRLI DLHSPSEIVK QITSISIEPG VEVEVTIADA

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Macromolecule #12: 40S ribosomal protein S25

MacromoleculeName: 40S ribosomal protein S25 / type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 13.776224 KDa
SequenceString:
MPPKDDKKKK DAGKSAKKDK DPVNKSGGKA KKKKWSKGKV RDKLNNLVLF DKATYDKLCK EVPNYKLITP AVVSERLKIR GSLARAALQ ELLSKGLIKL VSKHRAQVIY TRNTKGGDAP AAGEDA

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Macromolecule #13: 40S ribosomal protein S28

MacromoleculeName: 40S ribosomal protein S28 / type: protein_or_peptide / ID: 13 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 6.87894 KDa
SequenceString:
PIKLARVTKV LGRTGSQGQC TQVRVEFMDD TSRSIIRNVK GPVREGDVLT LLESEREARR L

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Macromolecule #14: 40S ribosomal protein S29

MacromoleculeName: 40S ribosomal protein S29 / type: protein_or_peptide / ID: 14 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 6.559625 KDa
SequenceString:
GHQQLYWSHP RKFGQGSRSC RVCSNRHGLI RKYGLNMCRQ CFRQYAKDIG FIKLD

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Macromolecule #15: Ribosomal protein S27a

MacromoleculeName: Ribosomal protein S27a / type: protein_or_peptide / ID: 15 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 8.45315 KDa
SequenceString:
KKRKKKSCTT PKKNKHKRKK VKLAVLKYYK VDENGKISRL RRECPSDECG AGVFMASHFD RHYCGKCCLT YC

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Macromolecule #16: Receptor of activated protein C kinase 1

MacromoleculeName: Receptor of activated protein C kinase 1 / type: protein_or_peptide / ID: 16 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Human (human)
Molecular weightTheoretical: 34.857355 KDa
SequenceString: MTEQMTLRGT LKGHNGWVTQ IATTPQFPDM ILSASRDKTI IMWKLTRDET NYGIPQRALR GHSHFVSDVV ISSDGQFALS GSWDGTLRL WDLTTGTTTR RFVGHTKDVL SVAFSSDNRQ IVSGSRDKTI KLWNTLGVCK YTVQDESHSE WVSCVRFSPN S SNPIIVSC ...String:
MTEQMTLRGT LKGHNGWVTQ IATTPQFPDM ILSASRDKTI IMWKLTRDET NYGIPQRALR GHSHFVSDVV ISSDGQFALS GSWDGTLRL WDLTTGTTTR RFVGHTKDVL SVAFSSDNRQ IVSGSRDKTI KLWNTLGVCK YTVQDESHSE WVSCVRFSPN S SNPIIVSC GWDKLVKVWN LANCKLKTNH IGHTGYLNTV TVSPDGSLCA SGGKDGQAML WDLNEGKHLY TLDGGDIINA LC FSPNRYW LCAATGPSIK IWDLEGKIIV DELKQEVIST SSKAEPPQCT SLAWSADGQT LFAGYTDNLV RVWQVTIG

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Macromolecule #17: MAGNESIUM ION

MacromoleculeName: MAGNESIUM ION / type: ligand / ID: 17 / Number of copies: 57 / Formula: MG
Molecular weightTheoretical: 24.305 Da

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Macromolecule #18: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 18 / Number of copies: 2 / 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: 7.6
VitrificationCryogen name: ETHANE-PROPANE / Chamber humidity: 100 % / Chamber temperature: 277.15 K

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy
Image recordingFilm or detector model: GATAN K3 (6k x 4k) / Average electron dose: 60.0 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

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

5oa3

Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.8 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 118765

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