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- EMDB-40241: 1:1:1 agrin/LRP4/MuSK complex -

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Basic information

Entry
Database: EMDB / ID: EMD-40241
Title1:1:1 agrin/LRP4/MuSK complex
Map dataCryo-EM map of 1:1:1 agrin/LRP4/MuSK complex
Sample
  • Complex: 1:1:1 agrin/LRP4/MuSK complex
    • Protein or peptide: Agrin
    • Protein or peptide: Low-density lipoprotein receptor-related protein 4
    • Protein or peptide: Muscle, skeletal receptor tyrosine-protein kinaseSkeletal muscle
Keywordsagrin / LRP4 / MuSK / NMJ / RTK / SIGNALING PROTEIN
Function / homology
Function and homology information


positive regulation of presynaptic membrane organization / positive regulation of protein geranylgeranylation / Defective B3GALT6 causes EDSP2 and SEMDJL1 / Defective B4GALT7 causes EDS, progeroid type / Defective B3GAT3 causes JDSSDHD / regulation of synaptic assembly at neuromuscular junction / Defective EXT2 causes exostoses 2 / Defective EXT1 causes exostoses 1, TRPS2 and CHDS / : / clustering of voltage-gated sodium channels ...positive regulation of presynaptic membrane organization / positive regulation of protein geranylgeranylation / Defective B3GALT6 causes EDSP2 and SEMDJL1 / Defective B4GALT7 causes EDS, progeroid type / Defective B3GAT3 causes JDSSDHD / regulation of synaptic assembly at neuromuscular junction / Defective EXT2 causes exostoses 2 / Defective EXT1 causes exostoses 1, TRPS2 and CHDS / : / clustering of voltage-gated sodium channels / positive regulation of synaptic assembly at neuromuscular junction / postsynaptic membrane assembly / A tetrasaccharide linker sequence is required for GAG synthesis / skeletal muscle acetylcholine-gated channel clustering / chondroitin sulfate binding / presynaptic membrane assembly / HS-GAG biosynthesis / HS-GAG degradation / sialic acid binding / negative regulation of axonogenesis / proximal/distal pattern formation / positive regulation of skeletal muscle acetylcholine-gated channel clustering / dystroglycan binding / Wnt-protein binding / amyloid-beta clearance by cellular catabolic process / heparan sulfate proteoglycan binding / NCAM1 interactions / negative regulation of ossification / synaptic assembly at neuromuscular junction / dorsal/ventral pattern formation / positive regulation of kinase activity / dendrite morphogenesis / limb development / positive regulation of filopodium assembly / generation of neurons / embryonic digit morphogenesis / neuromuscular junction development / receptor clustering / odontogenesis of dentin-containing tooth / plasma membrane raft / apolipoprotein binding / Non-integrin membrane-ECM interactions / basement membrane / hair follicle development / ECM proteoglycans / laminin binding / Integrin cell surface interactions / Retinoid metabolism and transport / transmembrane receptor protein tyrosine kinase activity / lysosomal lumen / synaptic membrane / kidney development / synapse organization / negative regulation of canonical Wnt signaling pathway / neuromuscular junction / G protein-coupled acetylcholine receptor signaling pathway / structural constituent of cytoskeleton / positive regulation of neuron projection development / receptor tyrosine kinase binding / receptor protein-tyrosine kinase / memory / Wnt signaling pathway / positive regulation of GTPase activity / Golgi lumen / endocytosis / cell surface receptor protein tyrosine kinase signaling pathway / positive regulation of peptidyl-tyrosine phosphorylation / postsynaptic membrane / scaffold protein binding / collagen-containing extracellular matrix / protein tyrosine kinase activity / Attachment and Entry / postsynaptic density / protein autophosphorylation / cell differentiation / receptor complex / positive regulation of protein phosphorylation / dendrite / neuronal cell body / synapse / calcium ion binding / positive regulation of gene expression / cell surface / signal transduction / protein homodimerization activity / positive regulation of transcription by RNA polymerase II / extracellular exosome / extracellular region / ATP binding / metal ion binding / plasma membrane
Similarity search - Function
NtA (N-terminal agrin) domain / Agrin NtA domain / NtA (N-terminal agrin) domain profile. / Follistatin-like, N-terminal / Follistatin-N-terminal domain-like / Factor I / membrane attack complex / factor I membrane attack complex / Complement Clr-like EGF domain / Domain found in sea urchin sperm protein, enterokinase, agrin / Laminin-type EGF-like (LE) domain profile. ...NtA (N-terminal agrin) domain / Agrin NtA domain / NtA (N-terminal agrin) domain profile. / Follistatin-like, N-terminal / Follistatin-N-terminal domain-like / Factor I / membrane attack complex / factor I membrane attack complex / Complement Clr-like EGF domain / Domain found in sea urchin sperm protein, enterokinase, agrin / Laminin-type EGF-like (LE) domain profile. / Laminin G domain / Laminin-type EGF-like (LE) domain signature. / Laminin-type epidermal growth factor-like domai / Laminin EGF domain / Complement Clr-like EGF-like / Kazal-type serine protease inhibitor domain / SEA domain superfamily / Laminin-type EGF domain / SEA domain profile. / Kazal-type serine protease inhibitor domain / SEA domain / SEA domain / Frizzled domain / Frizzled cysteine-rich domain superfamily / Fz domain / Frizzled (fz) domain profile. / Low-density lipoprotein receptor repeat class B / LDL-receptor class B (LDLRB) repeat profile. / Laminin G domain profile. / LDLR class B repeat / Low-density lipoprotein-receptor YWTD domain / Kazal type serine protease inhibitors / Laminin G domain / Laminin G domain / Kazal domain superfamily / Kazal domain / Kazal domain profile. / Tissue inhibitor of metalloproteinases-like, OB-fold / Low-density lipoprotein receptor domain class A / Low-density lipoprotein (LDL) receptor class A, conserved site / LDL-receptor class A (LDLRA) domain signature. / LDL-receptor class A (LDLRA) domain profile. / Low-density lipoprotein receptor domain class A / Low-density lipoprotein (LDL) receptor class A repeat / LDL receptor-like superfamily / Six-bladed beta-propeller, TolB-like / Coagulation Factor Xa inhibitory site / EGF-like domain / EGF-like calcium-binding, conserved site / Calcium-binding EGF-like domain signature. / Immunoglobulin domain / Aspartic acid and asparagine hydroxylation site. / EGF-like calcium-binding domain / Calcium-binding EGF-like domain / Immunoglobulin I-set / Immunoglobulin I-set domain / Epidermal growth factor-like domain. / EGF-like domain profile. / Growth factor receptor cysteine-rich domain superfamily / EGF-like domain signature 2. / EGF-like domain signature 1. / EGF-like domain / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / Tyrosine-protein kinase, catalytic domain / Tyrosine kinase, catalytic domain / Concanavalin A-like lectin/glucanase domain superfamily / Tyrosine protein kinases specific active-site signature. / Immunoglobulin subtype / Immunoglobulin / Tyrosine-protein kinase, active site / Protein tyrosine and serine/threonine kinase / Serine-threonine/tyrosine-protein kinase, catalytic domain / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Immunoglobulin-like fold / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily
Similarity search - Domain/homology
Agrin / Muscle, skeletal receptor tyrosine-protein kinase / Low-density lipoprotein receptor-related protein 4
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.8 Å
AuthorsXie T / Xu GJ / Liu Y / Quade B / Lin WC / Bai XC
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01GM143158 United States
CitationJournal: Proc Natl Acad Sci U S A / Year: 2023
Title: Structural insights into the assembly of the agrin/LRP4/MuSK signaling complex.
Authors: Tian Xie / Guangjun Xu / Yun Liu / Bradley Quade / Weichun Lin / Xiao-Chen Bai /
Abstract: MuSK is a receptor tyrosine kinase (RTK) that plays essential roles in the formation and maintenance of the neuromuscular junction. Distinct from most members of RTK family, MuSK activation requires ...MuSK is a receptor tyrosine kinase (RTK) that plays essential roles in the formation and maintenance of the neuromuscular junction. Distinct from most members of RTK family, MuSK activation requires not only its cognate ligand agrin but also its coreceptors LRP4. However, how agrin and LRP4 coactivate MuSK remains unclear. Here, we report the cryo-EM structure of the extracellular ternary complex of agrin/LRP4/MuSK in a stoichiometry of 1:1:1. This structure reveals that arc-shaped LRP4 simultaneously recruits both agrin and MuSK to its central cavity, thereby promoting a direct interaction between agrin and MuSK. Our cryo-EM analyses therefore uncover the assembly mechanism of agrin/LRP4/MuSK signaling complex and reveal how MuSK receptor is activated by concurrent binding of agrin and LRP4.
History
DepositionMar 29, 2023-
Header (metadata) releaseMay 17, 2023-
Map releaseMay 17, 2023-
UpdateJun 14, 2023-
Current statusJun 14, 2023Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_40241.png

Downloads & links

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Map

FileDownload / File: emd_40241.map.gz / Format: CCP4 / Size: 52.7 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationCryo-EM map of 1:1:1 agrin/LRP4/MuSK complex
Voxel sizeX=Y=Z: 0.83 Å
Density
Contour LevelBy AUTHOR: 0.0085
Minimum - Maximum-0.03330369 - 0.05976056
Average (Standard dev.)0.00008625441 (±0.0018394103)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions240240240
Spacing240240240
CellA=B=C: 199.2 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: Cryo-EM map of 1:1:1 agrin/LRP4/MuSK complex, half 1

Fileemd_40241_half_map_1.map
AnnotationCryo-EM map of 1:1:1 agrin/LRP4/MuSK complex, half 1
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Cryo-EM map of 1:1:1 agrin/LRP4/MuSK complex, half 2

Fileemd_40241_half_map_2.map
AnnotationCryo-EM map of 1:1:1 agrin/LRP4/MuSK complex, half 2
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : 1:1:1 agrin/LRP4/MuSK complex

EntireName: 1:1:1 agrin/LRP4/MuSK complex
Components
  • Complex: 1:1:1 agrin/LRP4/MuSK complex
    • Protein or peptide: Agrin
    • Protein or peptide: Low-density lipoprotein receptor-related protein 4
    • Protein or peptide: Muscle, skeletal receptor tyrosine-protein kinaseSkeletal muscle

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Supramolecule #1: 1:1:1 agrin/LRP4/MuSK complex

SupramoleculeName: 1:1:1 agrin/LRP4/MuSK complex / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: Agrin

MacromoleculeName: Agrin / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 217.553922 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MAGRSHPGPL RPLLPLLVVA ACVLPGAGGT CPERALERRE EEANVVLTGT VEEILNVDPV QHTYSCKVRV WRYLKGKDLV ARESLLDGG NKVVISGFGD PLICDNQVST GDTRIFFVNP APPYLWPAHK NELMLNSSLM RITLRNLEEV EFCVEDKPGT H FTPVPPTP ...String:
MAGRSHPGPL RPLLPLLVVA ACVLPGAGGT CPERALERRE EEANVVLTGT VEEILNVDPV QHTYSCKVRV WRYLKGKDLV ARESLLDGG NKVVISGFGD PLICDNQVST GDTRIFFVNP APPYLWPAHK NELMLNSSLM RITLRNLEEV EFCVEDKPGT H FTPVPPTP PDACRGMLCG FGAVCEPNAE GPGRASCVCK KSPCPSVVAP VCGSDASTYS NECELQRAQC SQQRRIRLLS RG PCGSRDP CSNVTCSFGS TCARSADGLT ASCLCPATCR GAPEGTVCGS DGADYPGECQ LLRRACARQE NVFKKFDGPC DPC QGALPD PSRSCRVNPR TRRPEMLLRP ESCPARQAPV CGDDGVTYEN DCVMGRSGAA RGLLLQKVRS GQCQGRDQCP EPCR FNAVC LSRRGRPRCS CDRVTCDGAY RPVCAQDGRT YDSDCWRQQA ECRQQRAIPS KHQGPCDQAP SPCLGVQCAF GATCA VKNG QAACECLQAC SSLYDPVCGS DGVTYGSACE LEATACTLGR EIQVARKGPC DRCGQCRFGA LCEAETGRCV CPSECV ALA QPVCGSDGHT YPSECMLHVH ACTHQISLHV ASAGPCETCG DAVCAFGAVC SAGQCVCPRC EHPPPGPVCG SDGVTYG SA CELREAACLQ QTQIEEARAG PCEQAECGSG GSGSGEDGDC EQELCRQRGG IWDEDSEDGP CVCDFSCQSV PGSPVCGS D GVTYSTECEL KKARCESQRG LYVAAQGACR GPTFAPLPPV APLHCAQTPY GCCQDNITAA RGVGLAGCPS ACQCNPHGS YGGTCDPATG QCSCRPGVGG LRCDRCEPGF WNFRGIVTDG RSGCTPCSCD PQGAVRDDCE QMTGLCSCKP GVAGPKCGQC PDGRALGPA GCEADASAPA TCAEMRCEFG ARCVEESGSA HCVCPMLTCP EANATKVCGS DGVTYGNECQ LKTIACRQGL Q ISIQSLGP CQEAVAPSTH PTSASVTVTT PGLLLSQALP APPGALPLAP SSTAHSQTTP PPSSRPRTTA SVPRTTVWPV LT VPPTAPS PAPSLVASAF GESGSTDGSS DEELSGDQEA SGGGSGGLEP LEGSSVATPG PPVERASCYN SALGCCSDGK TPS LDAEGS NCPATKVFQG VLELEGVEGQ ELFYTPEMAD PKSELFGETA RSIESTLDDL FRNSDVKKDF RSVRLRDLGP GKSV RAIVD VHFDPTTAFR APDVARALLR QIQVSRRRSL GVRRPLQEHV RFMDFDWFPA FITGATSGAI AAGATARATT ASRLP SSAV TPRAPHPSHT SQPVAKTTAA PTTRRPPTTA PSRVPGRRPP APQQPPKPCD SQPCFHGGTC QDWALGGGFT CSCPAG RGG AVCEKVLGAP VPAFEGRSFL AFPTLRAYHT LRLALEFRAL EPQGLLLYNG NARGKDFLAL ALLDGRVQLR FDTGSGP AV LTSAVPVEPG QWHRLELSRH WRRGTLSVDG ETPVLGESPS GTDGLNLDTD LFVGGVPEDQ AAVALERTFV GAGLRGCI R LLDVNNQRLE LGIGPGAATR GSGVGECGDH PCLPNPCHGG APCQNLEAGR FHCQCPPGRV GPTCADEKSP CQPNPCHGA APCRVLPEGG AQCECPLGRE GTFCQTASGQ DGSGPFLADF NGFSHLELRG LHTFARDLGE KMALEVVFLA RGPSGLLLYN GQKTDGKGD FVSLALRDRR LEFRYDLGKG AAVIRSREPV TLGAWTRVSL ERNGRKGALR VGDGPRVLGE SPKSRKVPHT V LNLKEPLY VGGAPDFSKL ARAAAVSSGF DGAIQLVSLG GRQLLTPEHV LRQVDVTSFA GHPCTRASGH PCLNGASCVP RE AAYVCLC PGGFSGPHCE KGLVEKSAGD VDTLAFDGRT FVEYLNAVTE SELANEIPVP ETLDSGALHS EKALQSNHFE LSL RTEATQ GLVLWSGKAT ERADYVALAI VDGHLQLSYN LGSQPVVLRS TVPVNTNRWL RVVAHREQRE GSLQVGNEAP VTGS SPLGA TQLDTDGALW LGGLPELPVG PALPKAYGTG FVGCLRDVVV GRHPLHLLED AVTKPELRPC PTP

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Macromolecule #2: Low-density lipoprotein receptor-related protein 4

MacromoleculeName: Low-density lipoprotein receptor-related protein 4 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 212.287031 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MRRQWGALLL GALLCAHGLA SSPECACGRS HFTCAVSALG ECTCIPAQWQ CDGDNDCGDH SDEDGCILPT CSPLDFHCDN GKCIRRSWV CDGDNDCEDD SDEQDCPPRE CEEDEFPCQN GYCIRSLWHC DGDNDCGDNS DEQCDMRKCS DKEFRCSDGS C IAEHWYCD ...String:
MRRQWGALLL GALLCAHGLA SSPECACGRS HFTCAVSALG ECTCIPAQWQ CDGDNDCGDH SDEDGCILPT CSPLDFHCDN GKCIRRSWV CDGDNDCEDD SDEQDCPPRE CEEDEFPCQN GYCIRSLWHC DGDNDCGDNS DEQCDMRKCS DKEFRCSDGS C IAEHWYCD GDTDCKDGSD EENCPSAVPA PPCNLEEFQC AYGRCILDIY HCDGDDDCGD WSDESDCSSH QPCRSGEFMC DS GLCINAG WRCDGDADCD DQSDERNCTT SMCTAEQFRC HSGRCVRLSW RCDGEDDCAD NSDEENCENT GSPQCALDQF LCW NGRCIG QRKLCNGVND CGDNSDESPQ QNCRPRTGEE NCNVNNGGCA QKCQMVRGAV QCTCHTGYRL TEDGHTCQDV NECA EEGYC SQGCTNSEGA FQCWCETGYE LRPDRRSCKA LGPEPVLLFA NRIDIRQVLP HRSEYTLLLN NLENAIALDF HHRRE LVFW SDVTLDRILR ANLNGSNVEE VVSTGLESPG GLAVDWVHDK LYWTDSGTSR IEVANLDGAH RKVLLWQNLE KPRAIA LHP MEGTIYWTDW GNTPRIEASS MDGSGRRIIA DTHLFWPNGL TIDYAGRRMY WVDAKHHVIE RANLDGSHRK AVISQGL PH PFAITVFEDS LYWTDWHTKS INSANKFTGK NQEIIRNKLH FPMDIHTLHP QRQPAGKNRC GDNNGGCTHL CLPSGQNY T CACPTGFRKI SSHACAQSLD KFLLFARRMD IRRISFDTED LSDDVIPLAD VRSAVALDWD SRDDHVYWTD VSTDTISRA KWDGTGQEVV VDTSLESPAG LAIDWVTNKL YWTDAGTDRI EVANTDGSMR TVLIWENLDR PRDIVVEPMG GYMYWTDWGA SPKIERAGM DASGRQVIIS SNLTWPNGLA IDYGSQRLYW ADAGMKTIEF AGLDGSKRKV LIGSQLPHPF GLTLYGERIY W TDWQTKSI QSADRLTGLD RETLQENLEN LMDIHVFHRR RPPVSTPCAM ENGGCSHLCL RSPNPSGFSC TCPTGINLLS DG KTCSPGM NSFLIFARRI DIRMVSLDIP YFADVVVPIN ITMKNTIAIG VDPQEGKVYW SDSTLHRISR ANLDGSQHED IIT TGLQTT DGLAVDAIGR KVYWTDTGTN RIEVGNLDGS MRKVLVWQNL DSPRAIVLYH EMGFMYWTDW GENAKLERSG MDGS DRAVL INNNLGWPNG LTVDKASSQL LWADAHTERI EAADLNGANR HTLVSPVQHP YGLTLLDSYI YWTDWQTRSI HRADK GTGS NVILVRSNLP GLMDMQAVDR AQPLGFNKCG SRNGGCSHLC LPRPSGFSCA CPTGIQLKGD GKTCDPSPET YLLFSS RGS IRRISLDTSD HTDVHVPVPE LNNVISLDYD SVDGKVYYTD VFLDVIRRAD LNGSNMETVI GRGLKTTDGL AVDWVAR NL YWTDTGRNTI EASRLDGSCR KVLINNSLDE PRAIAVFPRK GYLFWTDWGH IAKIERANLD GSERKVLINT DLGWPNGL T LDYDTRRIYW VDAHLDRIES ADLNGKLRQV LVSHVSHPFA LTQQDRWIYW TDWQTKSIQR VDKYSGRNKE TVLANVEGL MDIIVVSPQR QTGTNACGVN NGGCTHLCFA RASDFVCACP DEPDSRPCSL VPGLVPPAPR ATGMSEKSPV LPNTPPTTLY SSTTRTRTS LEEVEGRCSE RDARLGLCAR SNDAVPAAPG EGLHISYAIG GLLSILLILV VIAALMLYRH KKSKFTDPGM G NLTYSNPS YRTSTQEVKI EAIPKPAMYN QLCYKKEGGP DHNYTKEKIK IVEGICLLSG DDAEWDDLKQ LRSSRGGLLR DH VCMKTDT VSIQASSGSL DDTETEQLLQ EEQSECSSVH TAATPERRGS LPDTGWKHER KLSSESQV

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Macromolecule #3: Muscle, skeletal receptor tyrosine-protein kinase

MacromoleculeName: Muscle, skeletal receptor tyrosine-protein kinase / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO / EC number: receptor protein-tyrosine kinase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 97.163227 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MRELVNIPLV HILTLVAFSG TEKLPKAPVI TTPLETVDAL VEEVATFMCA VESYPQPEIS WTRNKILIKL FDTRYSIREN GQLLTILSV EDSDDGIYCC TANNGVGGAV ESCGALQVKM KPKITRPPIN VKIIEGLKAV LPCTTMGNPK PSVSWIKGDS P LRENSRIA ...String:
MRELVNIPLV HILTLVAFSG TEKLPKAPVI TTPLETVDAL VEEVATFMCA VESYPQPEIS WTRNKILIKL FDTRYSIREN GQLLTILSV EDSDDGIYCC TANNGVGGAV ESCGALQVKM KPKITRPPIN VKIIEGLKAV LPCTTMGNPK PSVSWIKGDS P LRENSRIA VLESGSLRIH NVQKEDAGQY RCVAKNSLGT AYSKVVKLEV EVFARILRAP ESHNVTFGSF VTLHCTATGI PV PTITWIE NGNAVSSGSI QESVKDRVID SRLQLFITKP GLYTCIATNK HGEKFSTAKA AATISIAEWS KPQKDNKGYC AQY RGEVCN AVLAKDALVF LNTSYADPEE AQELLVHTAW NELKVVSPVC RPAAEALLCN HIFQECSPGV VPTPIPICRE YCLA VKELF CAKEWLVMEE KTHRGLYRSE MHLLSVPECS KLPSMHWDPT ACARLPHLDY NKENLKTFPP MTSSKPSVDI PNLPS SSSS SFSVSPTYSM TVIISIMSSF AIFVLLTITT LYCCRRRKQW KNKKRESAAV TLTTLPSELL LDRLHPNPMY QRMPLL LNP KLLSLEYPRN NIEYVRDIGE GAFGRVFQAR APGLLPYEPF TMVAVKMLKE EASADMQADF QREAALMAEF DNPNIVK LL GVCAVGKPMC LLFEYMAYGD LNEFLRSMSP HTVCSLSHSD LSMRAQVSSP GPPPLSCAEQ LCIARQVAAG MAYLSERK F VHRDLATRNC LVGENMVVKI ADFGLSRNIY SADYYKANEN DAIPIRWMPP ESIFYNRYTT ESDVWAYGVV LWEIFSYGL QPYYGMAHEE VIYYVRDGNI LSCPENCPVE LYNLMRLCWS KLPADRPSFT SIHRILERMC ERAEGTVSV

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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

Concentration0.56 mg/mL
BufferpH: 7.4 / Details: 25 mM HEPES pH 7.4, 150 mM NaCl, and 2 mM CaCl2
GridModel: Quantifoil / Material: GOLD / Mesh: 300 / Pretreatment - Type: GLOW DISCHARGE
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Instrument: FEI VITROBOT MARK IV

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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 / Nominal defocus max: 2.6 µm / Nominal defocus min: 1.6 µm
Specialist opticsEnergy filter - Name: GIF Bioquantum / Energy filter - Slit width: 20 eV
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (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

Particle selectionNumber selected: 2414116
Startup modelType of model: OTHER / Details: Built from RELION
Initial angle assignmentType: PROJECTION MATCHING / Software - Name: RELION
Final 3D classificationSoftware - Name: RELION
Final angle assignmentType: PROJECTION MATCHING / Software - Name: RELION
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.8 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION / Number images used: 82511

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