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- EMDB-9842: eIF2 - eIF2B (2 molecule) -

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Basic information

Entry
Database: EMDB / ID: EMD-9842
TitleeIF2 - eIF2B (2 molecule)
Map data
Sample
  • Complex: eIF2 - eIF2B (2 molecule)
    • Complex: eIF2B
      • Protein or peptide: eIF2Ba
      • Protein or peptide: eIF2Bb
      • Protein or peptide: eIF2Bg
      • Protein or peptide: eIF2Bd
      • Protein or peptide: eIF2Be
    • Complex: eIF2
      • Protein or peptide: eIF2a
      • Protein or peptide: eIF2b
      • Protein or peptide: eIF2g
Function / homology
Function and homology information


male germ cell proliferation / regulation of translation in response to endoplasmic reticulum stress / translation initiation ternary complex / glial limiting end-foot / response to kainic acid / Cellular response to mitochondrial stress / response to manganese-induced endoplasmic reticulum stress / positive regulation of type B pancreatic cell apoptotic process / methionyl-initiator methionine tRNA binding / eukaryotic translation initiation factor 2B complex ...male germ cell proliferation / regulation of translation in response to endoplasmic reticulum stress / translation initiation ternary complex / glial limiting end-foot / response to kainic acid / Cellular response to mitochondrial stress / response to manganese-induced endoplasmic reticulum stress / positive regulation of type B pancreatic cell apoptotic process / methionyl-initiator methionine tRNA binding / eukaryotic translation initiation factor 2B complex / negative regulation of translational initiation in response to stress / Response of EIF2AK1 (HRI) to heme deficiency / Recycling of eIF2:GDP / PERK-mediated unfolded protein response / PERK regulates gene expression / eukaryotic translation initiation factor 2 complex / regulation of translational initiation in response to stress / selenocysteine metabolic process / selenocysteine incorporation / protein-synthesizing GTPase / cytoplasmic translational initiation / translation factor activity, RNA binding / formation of cytoplasmic translation initiation complex / oligodendrocyte development / selenocysteine insertion sequence binding / formation of translation preinitiation complex / guanyl-nucleotide exchange factor complex / astrocyte development / eukaryotic 48S preinitiation complex / astrocyte differentiation / regulation of translational initiation / Formation of the ternary complex, and subsequently, the 43S complex / Ribosomal scanning and start codon recognition / Translation initiation complex formation / Response of EIF2AK4 (GCN2) to amino acid deficiency / GTP hydrolysis and joining of the 60S ribosomal subunit / L13a-mediated translational silencing of Ceruloplasmin expression / positive regulation of translational initiation / response to glucose / stress granule assembly / ovarian follicle development / translation initiation factor binding / translational initiation / translation initiation factor activity / myelination / cellular response to amino acid starvation / response to endoplasmic reticulum stress / guanyl-nucleotide exchange factor activity / central nervous system development / hippocampus development / ABC-family proteins mediated transport / PKR-mediated signaling / response to peptide hormone / cytoplasmic stress granule / male gonad development / cellular response to UV / ribosome binding / regulation of translation / T cell receptor signaling pathway / cellular response to heat / cellular response to oxidative stress / response to heat / in utero embryonic development / cadherin binding / positive regulation of apoptotic process / GTPase activity / mRNA binding / synapse / GTP binding / RNA binding / extracellular exosome / ATP binding / identical protein binding / membrane / nucleus / metal ion binding / plasma membrane / cytoplasm / cytosol
Similarity search - Function
Translation initiation factor eIF-2B subunit alpha, N-terminal / Translation initiation factor eIF-2B subunit epsilon, N-terminal / Translation initiation factor eIF-2B subunit epsilon, W2 domain / Translation initiation factor IF2/IF5 / Translation initiation factor IF2/IF5 domain / Translation initiation factor IF2/IF5, N-terminal / Translation initiation factor IF2/IF5, zinc-binding / Domain found in IF2B/IF5 / domain present in translation initiation factor eIF2B and eIF5 / Initiation factor 2B-related ...Translation initiation factor eIF-2B subunit alpha, N-terminal / Translation initiation factor eIF-2B subunit epsilon, N-terminal / Translation initiation factor eIF-2B subunit epsilon, W2 domain / Translation initiation factor IF2/IF5 / Translation initiation factor IF2/IF5 domain / Translation initiation factor IF2/IF5, N-terminal / Translation initiation factor IF2/IF5, zinc-binding / Domain found in IF2B/IF5 / domain present in translation initiation factor eIF2B and eIF5 / Initiation factor 2B-related / Initiation factor 2B-like, C-terminal / Initiation factor 2 subunit family / eIF4-gamma/eIF5/eIF2-epsilon / Domain at the C-termini of GCD6, eIF-2B epsilon, eIF-4 gamma and eIF-5 / W2 domain / W2 domain profile. / IF2a, S1-like domain / Translation initiation factor 2, alpha subunit / Translation initiation factor 2, alpha subunit, middle domain superfamily / Translation initiation factor 2, alpha subunit, C-terminal / Eukaryotic translation initiation factor 2 alpha subunit / Initiation factor eIF2 gamma, domain 2 / Initiation factor eIF2 gamma, GTP-binding domain / Initiation factor eIF2 gamma, C-terminal / Initiation factor eIF2 gamma, C terminal / Nucleotidyl transferase domain / Nucleotidyl transferase / NagB/RpiA transferase-like / Translation elongation factor EF1A/initiation factor IF2gamma, C-terminal / Trimeric LpxA-like superfamily / S1 domain profile. / Translation elongation factor EFTu-like, domain 2 / Ribosomal protein S1-like RNA-binding domain / Elongation factor Tu domain 2 / S1 RNA binding domain / S1 domain / Translational (tr)-type GTP-binding domain / Elongation factor Tu GTP binding domain / Translational (tr)-type guanine nucleotide-binding (G) domain profile. / Nucleotide-diphospho-sugar transferases / Armadillo-type fold / Translation protein, beta-barrel domain superfamily / Nucleic acid-binding, OB-fold / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Eukaryotic translation initiation factor 2 subunit 1 / Eukaryotic translation initiation factor 2 subunit 2 / Eukaryotic translation initiation factor 2 subunit 3 / Translation initiation factor eIF2B subunit beta / Translation initiation factor eIF2B subunit epsilon / Translation initiation factor eIF2B subunit alpha / Translation initiation factor eIF2B subunit gamma / Translation initiation factor eIF2B subunit delta
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 6.8 Å
AuthorsKashiwagi K / Yokoyama T / Ito T
CitationJournal: Science / Year: 2019
Title: Structural basis for eIF2B inhibition in integrated stress response.
Authors: Kazuhiro Kashiwagi / Takeshi Yokoyama / Madoka Nishimoto / Mari Takahashi / Ayako Sakamoto / Mayumi Yonemochi / Mikako Shirouzu / Takuhiro Ito /
Abstract: A core event in the integrated stress response, an adaptive pathway common to all eukaryotic cells in response to various stress stimuli, is the phosphorylation of eukaryotic translation initiation ...A core event in the integrated stress response, an adaptive pathway common to all eukaryotic cells in response to various stress stimuli, is the phosphorylation of eukaryotic translation initiation factor 2 (eIF2). Normally, unphosphorylated eIF2 transfers the methionylated initiator tRNA to the ribosome in a guanosine 5'-triphosphate-dependent manner. By contrast, phosphorylated eIF2 inhibits its specific guanine nucleotide exchange factor, eIF2B. To elucidate how the eIF2 phosphorylation status regulates the eIF2B activity, we determined cryo-electron microscopic and crystallographic structures of eIF2B in complex with unphosphorylated or phosphorylated eIF2. The unphosphorylated and phosphorylated forms of eIF2 bind to eIF2B in completely different manners: the nucleotide exchange-active and -inactive modes, respectively. These structures explain how phosphorylated eIF2 dominantly inhibits the nucleotide exchange activity of eIF2B.
History
DepositionMar 7, 2019-
Header (metadata) releaseMay 1, 2019-
Map releaseMay 1, 2019-
UpdateJun 12, 2019-
Current statusJun 12, 2019Processing site: PDBj / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.0179
  • Imaged by UCSF Chimera
  • Download
  • Surface view colored by radius
  • Surface level: 0.0179
  • Imaged by UCSF Chimera
  • Download
Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_9842.png

Downloads & links

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Map

FileDownload / File: emd_9842.map.gz / Format: CCP4 / Size: 59.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Voxel sizeX=Y=Z: 1.47 Å
Density
Contour LevelBy AUTHOR: 0.0179 / Movie #1: 0.0179
Minimum - Maximum-0.025003737 - 0.07427283
Average (Standard dev.)0.00019365162 (±0.0034214372)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions250250250
Spacing250250250
CellA=B=C: 367.5 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.471.471.47
M x/y/z250250250
origin x/y/z0.0000.0000.000
length x/y/z367.500367.500367.500
α/β/γ90.00090.00090.000
start NX/NY/NZ000
NX/NY/NZ192192192
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS250250250
D min/max/mean-0.0250.0740.000

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Supplemental data

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Sample components

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Entire : eIF2 - eIF2B (2 molecule)

EntireName: eIF2 - eIF2B (2 molecule)
Components
  • Complex: eIF2 - eIF2B (2 molecule)
    • Complex: eIF2B
      • Protein or peptide: eIF2Ba
      • Protein or peptide: eIF2Bb
      • Protein or peptide: eIF2Bg
      • Protein or peptide: eIF2Bd
      • Protein or peptide: eIF2Be
    • Complex: eIF2
      • Protein or peptide: eIF2a
      • Protein or peptide: eIF2b
      • Protein or peptide: eIF2g

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Supramolecule #1: eIF2 - eIF2B (2 molecule)

SupramoleculeName: eIF2 - eIF2B (2 molecule) / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all

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Supramolecule #2: eIF2B

SupramoleculeName: eIF2B / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1-#5
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Escherichia coli (E. coli)

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Supramolecule #3: eIF2

SupramoleculeName: eIF2 / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #6-#8
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Homo sapiens (human)

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Macromolecule #1: eIF2Ba

MacromoleculeName: eIF2Ba / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MDDKELIEYF KSQMKEDPDM ASAVAAIRTL LEFLKRDKGE TIQGLRANLT SAIETLCGVD SSVAVSSGG ELFLRFISLA SLEYSDYSKC KKIMIERGEL FLRRISLSRN KIADLCHTFI K DGATILTH AYSRVVLRVL EAAVAAKKRF SVYVTESQPD LSGKKMAKAL ...String:
MDDKELIEYF KSQMKEDPDM ASAVAAIRTL LEFLKRDKGE TIQGLRANLT SAIETLCGVD SSVAVSSGG ELFLRFISLA SLEYSDYSKC KKIMIERGEL FLRRISLSRN KIADLCHTFI K DGATILTH AYSRVVLRVL EAAVAAKKRF SVYVTESQPD LSGKKMAKAL CHLNVPVTVV LD AAVGYIM EKADLVIVGA EGVVENGGII NKIGTNQMAV CAKAQNKPFY VVAESFKFVR LFP LNQQDV PDKFKYKADT LKVAQTGQDL KEEHPWVDYT APSLITLLFT DLGVLTPSAV SDEL IKLYL

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Macromolecule #2: eIF2Bb

MacromoleculeName: eIF2Bb / type: protein_or_peptide / ID: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MPGSAAKGSE LSERIESFVE TLKRGGGPRS SEEMARETLG LLRQIITDHR WSNAGELMEL IRREGRRMT AAQPSETTVG NMVRRVLKII REEYGRLHGR SDESDQQESL HKLLTSGGLN E DFSFHYAQ LQSNIIEAIN ELLVELEGTM ENIAAQALEH IHSNEVIMTI ...String:
MPGSAAKGSE LSERIESFVE TLKRGGGPRS SEEMARETLG LLRQIITDHR WSNAGELMEL IRREGRRMT AAQPSETTVG NMVRRVLKII REEYGRLHGR SDESDQQESL HKLLTSGGLN E DFSFHYAQ LQSNIIEAIN ELLVELEGTM ENIAAQALEH IHSNEVIMTI GFSRTVEAFL KE AARKRKF HVIVAECAPF CQGHEMAVNL SKAGIETTVM TDAAIFAVMS RVNKVIIGTK TIL ANGALR AVTGTHTLAL AAKHHSTPLI VCAPMFKLSP QFPNEEDSFH KFVAPEEVLP FTEG DILEK VSVHCPVFDY VPPELITLFI SNIGGNAPSY IYRLMSELYH PDDHVL

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Macromolecule #3: eIF2Bg

MacromoleculeName: eIF2Bg / type: protein_or_peptide / ID: 3 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MEFQAVVMAV GGGSRMTDLT SSIPKPLLPV GNKPLIWYPL NLLERVGFEE VIVVTTRDVQ KALCAEFKM KMKPDIVCIP DDADMGTADS LRYIYPKLKT DVLVLSCDLI TDVALHEVVD L FRAYDASL AMLMRKGQDS IEPVPGQKGK KKAVEQRDFI GVDSTGKRLL ...String:
MEFQAVVMAV GGGSRMTDLT SSIPKPLLPV GNKPLIWYPL NLLERVGFEE VIVVTTRDVQ KALCAEFKM KMKPDIVCIP DDADMGTADS LRYIYPKLKT DVLVLSCDLI TDVALHEVVD L FRAYDASL AMLMRKGQDS IEPVPGQKGK KKAVEQRDFI GVDSTGKRLL FMANEADLDE EL VIKGSIL QKHPRIRFHT GLVDAHLYCL KKYIVDFLME NGSITSIRSE LIPYLVRKQF SSA SSQQGQ EEKEEDLKKK ELKSLDIYSF IKEANTLNLA PYDACWNACR GDRWEDLSRS QVRC YVHIM KEGLCSRVST LGLYMEANRQ VPKLLSALCP EEPPVHSSAQ IVSKHLVGVD SLIGP ETQI GEKSSIKRSV IGSSCLIKDR VTITNCLLMN SVTVEEGSNI QGSVICNNAV IEKGAD IKD CLIGSGQRIE AKAKRVNEVI VGNDQLMEI

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Macromolecule #4: eIF2Bd

MacromoleculeName: eIF2Bd / type: protein_or_peptide / ID: 4 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MAAVAVAVRE DSGSGMKAEL PPGPGAVGRE MTKEEKLQLR KEKKQQKKKR KEEKGAEPET GSAVSAAQC QVGPTRELPE SGIQLGTPRE KVPAGRSKAE LRAERRAKQE AERALKQARK G EQGGPPPK ASPSTAGETP SGVKRLPEYP QVDDLLLRRL VKKPERQQVP ...String:
MAAVAVAVRE DSGSGMKAEL PPGPGAVGRE MTKEEKLQLR KEKKQQKKKR KEEKGAEPET GSAVSAAQC QVGPTRELPE SGIQLGTPRE KVPAGRSKAE LRAERRAKQE AERALKQARK G EQGGPPPK ASPSTAGETP SGVKRLPEYP QVDDLLLRRL VKKPERQQVP TRKDYGSKVS LF SHLPQYS RQNSLTQFMS IPSSVIHPAM VRLGLQYSQG LVSGSNARCI ALLRALQQVI QDY TTPPNE ELSRDLVNKL KPYMSFLTQC RPLSASMHNA IKFLNKEITS VGSSKREEEA KSEL RAAID RYVQEKIVLA AQAISRFAYQ KISNGDVILV YGCSSLVSRI LQEAWTEGRR FRVVV VDSR PWLEGRHTLR SLVHAGVPAS YLLIPAASYV LPEVSKVLLG AHALLANGSV MSRVGT AQL ALVARAHNVP VLVCCETYKF CERVQTDAFV SNELDDPDDL QCKRGEHVAL ANWQNHA SL RLLNLVYDVT PPELVDLVIT ELGMIPCSSV PVVLRVKSSD Q

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Macromolecule #5: eIF2Be

MacromoleculeName: eIF2Be / type: protein_or_peptide / ID: 5 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MAAPVVAPPG VVVSRANKRS GAGPGGSGGG GARGAEEEPP PPLQAVLVAD SFDRRFFPIS KDQPRVLLP LANVALIDYT LEFLTATGVQ ETFVFCCWKA AQIKEHLLKS KWCRPTSLNV V RIITSELY RSLGDVLRDV DAKALVRSDF LLVYGDVISN INITRALEEH ...String:
MAAPVVAPPG VVVSRANKRS GAGPGGSGGG GARGAEEEPP PPLQAVLVAD SFDRRFFPIS KDQPRVLLP LANVALIDYT LEFLTATGVQ ETFVFCCWKA AQIKEHLLKS KWCRPTSLNV V RIITSELY RSLGDVLRDV DAKALVRSDF LLVYGDVISN INITRALEEH RLRRKLEKNV SV MTMIFKE SSPSHPTRCH EDNVVVAVDS TTNRVLHFQK TQGLRRFAFP LSLFQGSSDG VEV RYDLLD CHISICSPQV AQLFTDNFDY QTRDDFVRGL LVNEEILGNQ IHMHVTAKEY GARV SNLHM YSAVCADVIR RWVYPLTPEA NFTDSTTQSC THSRHNIYRG PEVSLGHGSI LEENV LLGS GTVIGSNCFI TNSVIGPGCH IGDNVVLDQT YLWQGVRVAA GAQIHQSLLC DNAEVK ERV TLKPRSVLTS QVVVGPNITL PEGSVISLHP PDAEEDEDDG EFSDDSGADQ EKDKVKM KG YNPAEVGAAG KGYLWKAAGM NMEEEEELQQ NLWGLKINME EESESESEQS MDSEEPDS R GGSPQMDDIK VFQNEVLGTL QRGKEENISC DNLVLEINSL KYAYNISLKE VMQVLSHVV LEFPLQQMDS PLDSSRYCAL LLPLLKAWSP VFRNYIKRAA DHLEALAAIE DFFLEHEALG ISMAKVLMA FYQLEILAEE TILSWFSQRD TTDKGQQLRK NQQLQRFIQW LKEAEEESSE D D

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Macromolecule #6: eIF2a

MacromoleculeName: eIF2a / type: protein_or_peptide / ID: 6 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MPGLSCRFYQ HKFPEVEDVV MVNVRSIAEM GAYVSLLEYN NIEGMILLSE LSRRRIRSIN KLIRIGRNE CVVVIRVDKE KGYIDLSKRR VSPEEAIKCE DKFTKSKTVY SILRHVAEVL E YTKDEQLE SLFQRTAWVF DDKYKRPGYG AYDAFKHAVS DPSILDSLDL ...String:
MPGLSCRFYQ HKFPEVEDVV MVNVRSIAEM GAYVSLLEYN NIEGMILLSE LSRRRIRSIN KLIRIGRNE CVVVIRVDKE KGYIDLSKRR VSPEEAIKCE DKFTKSKTVY SILRHVAEVL E YTKDEQLE SLFQRTAWVF DDKYKRPGYG AYDAFKHAVS DPSILDSLDL NEDEREVLIN NI NRRLTPQ AVKIRADIEV ACYGYEGIDA VKEALRAGLN CSTENMPIKI NLIAPPRYVM TTT TLERTE GLSVLSQAMA VIKEKIEEKR GVFNVQMEPK VVTDTDETEL ARQMERLERE NAEV DGDDD AEEMEAKAED

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Macromolecule #7: eIF2b

MacromoleculeName: eIF2b / type: protein_or_peptide / ID: 7 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MSGDEMIFDP TMSKKKKKKK KPFMLDEEGD TQTEETQPSE TKEVEPEPTE DKDLEADEED TRKKDASDD LDDLNFFNQK KKKKKTKKIF DIDEAEEGVK DLKIESDVQE PTEPEDDLDI M LGNKKKKK KNVKFPDEDE ILEKDEALED EDNKKDDGIS FSNQTGPAWA ...String:
MSGDEMIFDP TMSKKKKKKK KPFMLDEEGD TQTEETQPSE TKEVEPEPTE DKDLEADEED TRKKDASDD LDDLNFFNQK KKKKKTKKIF DIDEAEEGVK DLKIESDVQE PTEPEDDLDI M LGNKKKKK KNVKFPDEDE ILEKDEALED EDNKKDDGIS FSNQTGPAWA GSERDYTYEE LL NRVFNIM REKNPDMVAG EKRKFVMKPP QVVRVGTKKT SFVNFTDICK LLHRQPKHLL AFL LAELGT SGSIDGNNQL VIKGRFQQKQ IENVLRRYIK EYVTCHTCRS PDTILQKDTR LYFL QCETC HSRCSVASIK TGFQAVTGKR AQLRAKAN

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Macromolecule #8: eIF2g

MacromoleculeName: eIF2g / type: protein_or_peptide / ID: 8 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MAGGEAGVTL GQPHLSRQDL TTLDVTKLTP LSHEVISRQA TINIGTIGHV AHGKSTVVKA ISGVHTVRF KNELERNITI KLGYANAKIY KLDDPSCPRP ECYRSCGSST PDEFPTDIPG T KGNFKLVR HVSFVDCPGH DILMATMLNG AAVMDAALLL IAGNESCPQP ...String:
MAGGEAGVTL GQPHLSRQDL TTLDVTKLTP LSHEVISRQA TINIGTIGHV AHGKSTVVKA ISGVHTVRF KNELERNITI KLGYANAKIY KLDDPSCPRP ECYRSCGSST PDEFPTDIPG T KGNFKLVR HVSFVDCPGH DILMATMLNG AAVMDAALLL IAGNESCPQP QTSEHLAAIE IM KLKHILI LQNKIDLVKE SQAKEQYEQI LAFVQGTVAE GAPIIPISAQ LKYNIEVVCE YIV KKIPVP PRDFTSEPRL IVIRSFDVNK PGCEVDDLKG GVAGGSILKG VLKVGQEIEV RPGI VSKDS EGKLMCKPIF SKIVSLFAEH NDLQYAAPGG LIGVGTKIDP TLCRADRMVG QVLGA VGAL PEIFTELEIS YFLLRRLLGV RTEGDKKAAK VQKLSKNEVL MVNIGSLSTG GRVSAV KAD LGKIVLTNPV CTEVGEKIAL SRRVEKHWRL IGWGQIRRGV TIKPTVDDD

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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 TECNAI ARCTICA
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 50.0 e/Å2
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Talos Arctica / Image courtesy: FEI Company

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Image processing

Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 6.8 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 35184
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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