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- EMDB-46798: Human V-ATPase Vo subcomplex (containing subunit isoform a4) boun... -

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Basic information

Entry
Database: EMDB / ID: EMD-46798
TitleHuman V-ATPase Vo subcomplex (containing subunit isoform a4) bound to nanobody and inhibitor
Map dataHuman V-ATPase Vo subcomplex (containing subunit isoform a4) bound to nanobody and inhibitor
Sample
  • Complex: Vo subcomplex from human V-ATPase bound to Nanobody and inhibitor
    • Protein or peptide: x 9 types
  • Ligand: x 5 types
KeywordsV-ATPase / lipid nanodisc / Vo subcomplex / inhibitor / MEMBRANE PROTEIN
Function / homology
Function and homology information


proton-transporting two-sector ATPase complex / Ion channel transport / Regulation of MITF-M-dependent genes involved in lysosome biogenesis and autophagy / renal tubular secretion / intracellular pH reduction / plasma membrane proton-transporting V-type ATPase complex / eye pigmentation / central nervous system maturation / ATPase-coupled ion transmembrane transporter activity / rostrocaudal neural tube patterning ...proton-transporting two-sector ATPase complex / Ion channel transport / Regulation of MITF-M-dependent genes involved in lysosome biogenesis and autophagy / renal tubular secretion / intracellular pH reduction / plasma membrane proton-transporting V-type ATPase complex / eye pigmentation / central nervous system maturation / ATPase-coupled ion transmembrane transporter activity / rostrocaudal neural tube patterning / positive regulation of transforming growth factor beta1 production / Golgi lumen acidification / synaptic vesicle lumen acidification / proton-transporting V-type ATPase, V0 domain / Transferrin endocytosis and recycling / cellular response to increased oxygen levels / vacuolar transport / endosome to plasma membrane protein transport / vacuolar proton-transporting V-type ATPase, V0 domain / clathrin-coated vesicle membrane / lysosomal lumen acidification / endosomal lumen acidification / regulation of pH / XBP1(S) activates chaperone genes / proton-transporting V-type ATPase complex / Amino acids regulate mTORC1 / vacuolar proton-transporting V-type ATPase complex / head morphogenesis / osteoclast development / vacuolar acidification / ROS and RNS production in phagocytes / regulation of cellular pH / dendritic spine membrane / azurophil granule membrane / ATPase activator activity / regulation of MAPK cascade / autophagosome membrane / tertiary granule membrane / proton-transporting ATPase activity, rotational mechanism / ficolin-1-rich granule membrane / cilium assembly / RHOA GTPase cycle / positive regulation of Wnt signaling pathway / regulation of macroautophagy / transporter activator activity / Metabolism of Angiotensinogen to Angiotensins / angiotensin maturation / Insulin receptor recycling / proton-transporting ATP synthase activity, rotational mechanism / receptor-mediated endocytosis of virus by host cell / axon terminus / endoplasmic reticulum-Golgi intermediate compartment membrane / RNA endonuclease activity / proton transmembrane transport / ossification / receptor-mediated endocytosis / brush border membrane / sensory perception of sound / small GTPase binding / transmembrane transport / phagocytic vesicle membrane / apical part of cell / synaptic vesicle membrane / positive regulation of canonical Wnt signaling pathway / signaling receptor activity / ATPase binding / basolateral plasma membrane / Hydrolases; Acting on ester bonds / intracellular iron ion homeostasis / postsynaptic membrane / early endosome / lysosome / endosome / endosome membrane / apical plasma membrane / Golgi membrane / axon / lysosomal membrane / external side of plasma membrane / focal adhesion / ubiquitin protein ligase binding / Neutrophil degranulation / endoplasmic reticulum membrane / protein-containing complex binding / extracellular exosome / membrane / plasma membrane
Similarity search - Function
ATPase, V0 complex, subunit e1/e2, metazoa / V0 complex accessory subunit Ac45 / V-type proton ATPase subunit S1, luminal domain / V-type proton ATPase subunit S1, luminal domain / Renin receptor-like / : / Renin receptor-like transmembrane spanning segment / Renin receptor N-terminal domain / : / V-type proton ATPase subunit f-like ...ATPase, V0 complex, subunit e1/e2, metazoa / V0 complex accessory subunit Ac45 / V-type proton ATPase subunit S1, luminal domain / V-type proton ATPase subunit S1, luminal domain / Renin receptor-like / : / Renin receptor-like transmembrane spanning segment / Renin receptor N-terminal domain / : / V-type proton ATPase subunit f-like / Ribonuclease kappa / V-type proton ATPase subunit S1/VOA1, transmembrane domain / V0 complex accessory subunit Ac45/VOA1 transmembrane domain / ATPase, V0 complex, subunit e1/e2 / ATP synthase subunit H / ATPase, V0 complex, subunit d / V-ATPase proteolipid subunit C, eukaryotic / ATPase, V0 complex, subunit 116kDa, eukaryotic / ATPase, V0 complex, c/d subunit / V-type ATPase subunit C/d / V-type ATP synthase subunit c/d subunit superfamily / V-type ATP synthase c/d subunit, domain 3 superfamily / ATP synthase (C/AC39) subunit / V-ATPase proteolipid subunit / V-type ATPase, V0 complex, 116kDa subunit family / V-type ATPase 116kDa subunit family / V-ATPase proteolipid subunit C-like domain / F/V-ATP synthase subunit C superfamily / ATP synthase subunit C
Similarity search - Domain/homology
V-type proton ATPase subunit e 1 / Renin receptor / V-type proton ATPase 16 kDa proteolipid subunit c / V-type proton ATPase subunit d 1 / V-type proton ATPase subunit S1 / Ribonuclease kappa / V-type proton ATPase 21 kDa proteolipid subunit c'' / V-type proton ATPase 116 kDa subunit a 4
Similarity search - Component
Biological speciesHomo sapiens (human) / Lama glama (llama)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.0 Å
AuthorsOot RA / Park JB / Roh S-H / Wilkens S
Funding support United States, Korea, Republic Of, 5 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM141908 United States
National Institutes of Health/National Cancer Institute (NIH/NCI)CA228340 United States
Other private73258
National Research Foundation (NRF, Korea)2020R1A6C101A183 Korea, Republic Of
National Research Foundation (NRF, Korea)2021M3A9I4021220 Korea, Republic Of
CitationJournal: To Be Published
Title: Inhibitor bound Vo subcomplex from human V-ATPase
Authors: Oot RA / Park JB / Roh S-H / Wilkens S
History
DepositionAug 29, 2024-
Header (metadata) releaseSep 10, 2025-
Map releaseSep 10, 2025-
UpdateSep 10, 2025-
Current statusSep 10, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_46798.png

Downloads & links

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Map

FileDownload / File: emd_46798.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationHuman V-ATPase Vo subcomplex (containing subunit isoform a4) bound to nanobody and inhibitor
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesX (Sec.)Y (Row.)Z (Col.)
1.1 Å/pix.
x 300 pix.
= 330. Å		1.1 Å/pix.
x 300 pix.
= 330. Å		1.1 Å/pix.
x 300 pix.
= 330. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.1 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 5.0
Minimum - Maximum-18.650480000000002 - 30.665168999999999
Average (Standard dev.)0.0052858335 (±0.995727)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderZYX
Origin000
Dimensions300300300
Spacing300300300
CellA=B=C: 330.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Sample components

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Entire : Vo subcomplex from human V-ATPase bound to Nanobody and inhibitor

EntireName: Vo subcomplex from human V-ATPase bound to Nanobody and inhibitor
Components
  • Complex: Vo subcomplex from human V-ATPase bound to Nanobody and inhibitor
    • Protein or peptide: V-type proton ATPase subunit e 1
    • Protein or peptide: Ribonuclease kappa
    • Protein or peptide: V-type proton ATPase subunit S1
    • Protein or peptide: Renin receptor
    • Protein or peptide: V-type proton ATPase 21 kDa proteolipid subunit
    • Protein or peptide: V-type proton ATPase 16 kDa proteolipid subunit
    • Protein or peptide: V-type proton ATPase subunit d 1
    • Protein or peptide: V-type proton ATPase 116 kDa subunit a 4
    • Protein or peptide: Anti V-ATPase Nanobody 2CAS66
  • Ligand: 2-acetamido-2-deoxy-beta-D-glucopyranose
  • Ligand: CHOLESTEROL
  • Ligand: (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate
  • Ligand: Cladoniamide A
  • Ligand: methyl (3R,6Z,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl dihydrogen diphosphate

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Supramolecule #1: Vo subcomplex from human V-ATPase bound to Nanobody and inhibitor

SupramoleculeName: Vo subcomplex from human V-ATPase bound to Nanobody and inhibitor
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#9
Details: Subunit a, isoform 4 (a4) carrying a C-terminal 2x FLAG tag was stably expressed in HEK293F cells. All other subunits present in the complex are endogenously expressed and have formed a ...Details: Subunit a, isoform 4 (a4) carrying a C-terminal 2x FLAG tag was stably expressed in HEK293F cells. All other subunits present in the complex are endogenously expressed and have formed a complex with the FLAG tagged a4. The Nanobody was raised against a4 and used for concentrating the sample for EM. A small molecule inhibitor is also bound to the complex.
Source (natural)Organism: Homo sapiens (human) / Location in cell: Membranes

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Macromolecule #1: V-type proton ATPase subunit e 1

MacromoleculeName: V-type proton ATPase subunit e 1 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 9.380329 KDa
SequenceString:
MAYHGLTVPL IVMSVFWGFV GFLVPWFIPK GPNRGVIITM LVTCSVCCYL FWLIAILAQL NPLFGPQLKN ETIWYLKYHW P

UniProtKB: V-type proton ATPase subunit e 1

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Macromolecule #2: Ribonuclease kappa

MacromoleculeName: Ribonuclease kappa / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: Hydrolases; Acting on ester bonds
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 15.43522 KDa
SequenceString:
MGWLRPGPRP LCPPARASWA FSHRFPSPLA PRRSPTPFFM ASLLCCGPKL AACGIVLSAW GVIMLIMLGI FFNVHSAVLI EDVPFTEKD FENGPQNIYN LYEQVSYNCF IAAGLYLLLG GFSFCQVRLN KRKEYMVR

UniProtKB: Ribonuclease kappa

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Macromolecule #3: V-type proton ATPase subunit S1

MacromoleculeName: V-type proton ATPase subunit S1 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 52.06748 KDa
SequenceString: MMAAMATARV RMGPRCAQAL WRMPWLPVFL SLAAAAAAAA AEQQVPLVLW SSDRDLWAPA ADTHEGHITS DLQLSTYLDP ALELGPRNV LLFLQDKLSI EDFTAYGGVF GNKQDSAFSN LENALDLAPS SLVLPAVDWY AVSTLTTYLQ EKLGASPLHV D LATLRELK ...String:
MMAAMATARV RMGPRCAQAL WRMPWLPVFL SLAAAAAAAA AEQQVPLVLW SSDRDLWAPA ADTHEGHITS DLQLSTYLDP ALELGPRNV LLFLQDKLSI EDFTAYGGVF GNKQDSAFSN LENALDLAPS SLVLPAVDWY AVSTLTTYLQ EKLGASPLHV D LATLRELK LNASLPALLL IRLPYTASSG LMAPREVLTG NDEVIGQVLS TLKSEDVPYT AALTAVRPSR VARDVAVVAG GL GRQLLQK QPVSPVIHPP VSYNDTAPRI LFWAQNFSVA YKDQWEDLTP LTFGVQELNL TGSFWNDSFA RLSLTYERLF GTT VTFKFI LANRLYPVSA RHWFTMERLE VHSNGSVAYF NASQVTGPSI YSFHCEYVSS LSKKGSLLVA RTQPSPWQMM LQDF QIQAF NVMGEQFSYA SDCASFFSPG IWMGLLTSLF MLFIFTYGLH MILSLKTMDR FDDHKGPTIS LTQIV

UniProtKB: V-type proton ATPase subunit S1

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Macromolecule #4: Renin receptor

MacromoleculeName: Renin receptor / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 39.045855 KDa
SequenceString: MAVFVVLLAL VAGVLGNEFS ILKSPGSVVF RNGNWPIPGE RIPDVAALSM GFSVKEDLSW PGLAVGNLFH RPRATVMVMV KGVNKLALP PGSVISYPLE NAVPFSLDSV ANSIHSLFSE ETPVVLQLAP SEERVYMVGK ANSVFEDLSV TLRQLRNRLF Q ENSVLSSL ...String:
MAVFVVLLAL VAGVLGNEFS ILKSPGSVVF RNGNWPIPGE RIPDVAALSM GFSVKEDLSW PGLAVGNLFH RPRATVMVMV KGVNKLALP PGSVISYPLE NAVPFSLDSV ANSIHSLFSE ETPVVLQLAP SEERVYMVGK ANSVFEDLSV TLRQLRNRLF Q ENSVLSSL PLNSLSRNNE VDLLFLSELQ VLHDISSLLS RHKHLAKDHS PDLYSLELAG LDEIGKRYGE DSEQFRDASK IL VDALQKF ADDMYSLYGG NAVVELVTVK SFDTSLIRKT RTILEAKQAK NPASPYNLAY KYNFEYSVVF NMVLWIMIAL ALA VIITSY NIWNMDPGYD SIIYRMTNQK IRMD

UniProtKB: Renin receptor

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Macromolecule #5: V-type proton ATPase 21 kDa proteolipid subunit

MacromoleculeName: V-type proton ATPase 21 kDa proteolipid subunit / type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 21.418213 KDa
SequenceString: MTGLALLYSG VFVAFWACAL AVGVCYTIFD LGFRFDVAWF LTETSPFMWS NLGIGLAISL SVVGAAWGIY ITGSSIIGGG VKAPRIKTK NLVSIIFCEA VAIYGIIMAI VISNMAEPFS ATDPKAIGHR NYHAGYSMFG AGLTVGLSNL FCGVCVGIVG S GAALADAQ ...String:
MTGLALLYSG VFVAFWACAL AVGVCYTIFD LGFRFDVAWF LTETSPFMWS NLGIGLAISL SVVGAAWGIY ITGSSIIGGG VKAPRIKTK NLVSIIFCEA VAIYGIIMAI VISNMAEPFS ATDPKAIGHR NYHAGYSMFG AGLTVGLSNL FCGVCVGIVG S GAALADAQ NPSLFVKILI VEIFGSAIGL FGVIVAILQT SRVKMGD

UniProtKB: V-type proton ATPase 21 kDa proteolipid subunit c''

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Macromolecule #6: V-type proton ATPase 16 kDa proteolipid subunit

MacromoleculeName: V-type proton ATPase 16 kDa proteolipid subunit / type: protein_or_peptide / ID: 6 / Number of copies: 9 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 15.743655 KDa
SequenceString:
MSESKSGPEY ASFFAVMGAS AAMVFSALGA AYGTAKSGTG IAAMSVMRPE QIMKSIIPVV MAGIIAIYGL VVAVLIANSL NDDISLYKS FLQLGAGLSV GLSGLAAGFA IGIVGDAGVR GTAQQPRLFV GMILILIFAE VLGLYGLIVA LILSTK

UniProtKB: V-type proton ATPase 16 kDa proteolipid subunit c

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Macromolecule #7: V-type proton ATPase subunit d 1

MacromoleculeName: V-type proton ATPase subunit d 1 / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 40.369949 KDa
SequenceString: MSFFPELYFN VDNGYLEGLV RGLKAGVLSQ ADYLNLVQCE TLEDLKLHLQ STDYGNFLAN EASPLTVSVI DDRLKEKMVV EFRHMRNHA YEPLASFLDF ITYSYMIDNV ILLITGTLHQ RSIAELVPKC HPLGSFEQME AVNIAQTPAE LYNAILVDTP L AAFFQDCI ...String:
MSFFPELYFN VDNGYLEGLV RGLKAGVLSQ ADYLNLVQCE TLEDLKLHLQ STDYGNFLAN EASPLTVSVI DDRLKEKMVV EFRHMRNHA YEPLASFLDF ITYSYMIDNV ILLITGTLHQ RSIAELVPKC HPLGSFEQME AVNIAQTPAE LYNAILVDTP L AAFFQDCI SEQDLDEMNI EIIRNTLYKA YLESFYKFCT LLGGTTADAM CPILEFEADR RAFIITINSF GTELSKEDRA KL FPHCGRL YPEGLAQLAR ADDYEQVKNV ADYYPEYKLL FEGAGSNPGD KTLEDRFFEH EVKLNKLAFL NQFHFGVFYA FVK LKEQEC RNIVWIAECI AQRHRAKIDN YIPIF

UniProtKB: V-type proton ATPase subunit d 1

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Macromolecule #8: V-type proton ATPase 116 kDa subunit a 4

MacromoleculeName: V-type proton ATPase 116 kDa subunit a 4 / type: protein_or_peptide / ID: 8 / Details: C-terminal 2 x FLAG tag / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 99.168164 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MVSVFRSEEM CLSQLFLQVE AAYCCVAELG ELGLVQFKDL NMNVNSFQRK FVNEVRRCES LERILRFLED EMQNEIVVQL LEKSPLTPL PREMITLETV LEKLEGELQE ANQNQQALKQ SFLELTELKY LLKKTQDFFE TETNLADDFF TEDTSGLLEL K AVPAYMTG ...String:
MVSVFRSEEM CLSQLFLQVE AAYCCVAELG ELGLVQFKDL NMNVNSFQRK FVNEVRRCES LERILRFLED EMQNEIVVQL LEKSPLTPL PREMITLETV LEKLEGELQE ANQNQQALKQ SFLELTELKY LLKKTQDFFE TETNLADDFF TEDTSGLLEL K AVPAYMTG KLGFIAGVIN RERMASFERL LWRICRGNVY LKFSEMDAPL EDPVTKEEIQ KNIFIIFYQG EQLRQKIKKI CD GFRATVY PCPEPAVERR EMLESVNVRL EDLITVITQT ESHRQRLLQE AAANWHSWLI KVQKMKAVYH ILNMCNIDVT QQC VIAEIW FPVADATRIK RALEQGMELS GSSMAPIMTT VQSKTAPPTF NRTNKFTAGF QNIVDAYGVG SYREINPAPY TIIT FPFLF AVMFGDCGHG TVMLLAALWM ILNERRLLSQ KTDNEIWNTF FHGRYLILLM GIFSIYTGLI YNDCFSKSLN IFGSS WSVQ PMFRNGTWNT HVMEESLYLQ LDPAIPGVYF GNPYPFGIDP IWNLASNKLT FLNSYKMKMS VILGIVQMVF GVILSL FNH IYFRRTLNII LQFIPEMIFI LCLFGYLVFM IIFKWCCFDV HVSQHAPSIL IHFINMFLFN YSDSSNAPLY KHQQEVQ SF FVVMALISVP WMLLIKPFIL RASHRKSQLQ ASRIQEDATE NIEGDSSSPS SRSGQRTSAD THGALDDHGE EFNFGDVF V HQAIHTIEYC LGCISNTASY LRLWALSLAH AQLSEVLWTM VMNSGLQTRG WGGIVGVFII FAVFAVLTVA ILLIMEGLS AFLHALRLHW VEFQNKFYVG DGYKFSPFSF KHILDGTAEE GDLDYKDDDD KLDYKDDDDK ADL

UniProtKB: V-type proton ATPase 116 kDa subunit a 4

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Macromolecule #9: Anti V-ATPase Nanobody 2CAS66

MacromoleculeName: Anti V-ATPase Nanobody 2CAS66 / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Lama glama (llama)
Molecular weightTheoretical: 15.14292 KDa
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString:
MGQVQLQESG GGLVQAGGSL RLSCAGSGRT FTYHTMGWFR QAPGKEREFV ASINWSDTRL YYTDSVKGRF TISRDNAKST VYLQMNSLK PEDTAVYYCV ATAMTTGATM TVDNVDYWGQ GTQVTVSSAA ALEVLFQGPK

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Macromolecule #10: 2-acetamido-2-deoxy-beta-D-glucopyranose

MacromoleculeName: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 10 / Number of copies: 8 / Formula: NAG
Molecular weightTheoretical: 221.208 Da
Chemical component information

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

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Macromolecule #11: CHOLESTEROL

MacromoleculeName: CHOLESTEROL / type: ligand / ID: 11 / Number of copies: 1 / Formula: CLR
Molecular weightTheoretical: 386.654 Da
Chemical component information

ChemComp-CLR:
CHOLESTEROL

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Macromolecule #12: (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(tri...

MacromoleculeName: (2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate
type: ligand / ID: 12 / Number of copies: 3 / Formula: POV
Molecular weightTheoretical: 760.076 Da
Chemical component information

ChemComp-POV:
(2S)-3-(hexadecanoyloxy)-2-[(9Z)-octadec-9-enoyloxy]propyl 2-(trimethylammonio)ethyl phosphate / phospholipid*YM

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Macromolecule #13: Cladoniamide A

MacromoleculeName: Cladoniamide A / type: ligand / ID: 13 / Number of copies: 9 / Formula: A1A4Q
Molecular weightTheoretical: 437.833 Da

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Macromolecule #14: methyl (3R,6Z,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-t...

MacromoleculeName: methyl (3R,6Z,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl dihydrogen diphosphate
type: ligand / ID: 14 / Number of copies: 1 / Formula: WJP
Molecular weightTheoretical: 534.603 Da
Chemical component information

ChemComp-WJP:
methyl (3R,6Z,10E,14E)-3,7,11,15,19-pentamethylicosa-6,10,14,18-tetraen-1-yl dihydrogen diphosphate

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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

Concentration2 mg/mL
BufferpH: 7.2
Component:
ConcentrationFormulaName
150.0 mMNaClSodium Chloride
20.0 mMC4H11NO3Tris
0.5 mMC10H14N2Na2O8Ethylenediaminetetraacetic acid
2.0 mMC4H10O2S2Dithiothreitol

Details: 20 mM Tris, 150 mM NaCl, 0.5 mM EDTA, 2 mM DTT, pH 7.2
GridMaterial: GOLD
VitrificationCryogen name: ETHANE / Instrument: HOMEMADE PLUNGER

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Electron microscopy

MicroscopeTFS GLACIOS
Image recordingFilm or detector model: TFS FALCON 4i (4k x 4k) / Average electron dose: 39.96 e/Å2
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.3 µm

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: NONE
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.0 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 144439
Initial angle assignmentType: NOT APPLICABLE
Final angle assignmentType: MAXIMUM LIKELIHOOD

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