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- EMDB-9100: The 20S supercomplex engaging the SNAP-25 N-terminus (class 1) -

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Basic information

Entry
Database: EMDB / ID: EMD-9100
TitleThe 20S supercomplex engaging the SNAP-25 N-terminus (class 1)
Map dataThe unsharpened map.
Sample
  • Complex: 20S supercomplex consisting of soluble neuronal SNARE complex, alpha-SNAP, and N-ethylmaleimide sensitive factor (NSF)
    • Complex: N-ethylmaleimide sensitive factor
      • Protein or peptide: Vesicle-fusing ATPase
    • Complex: Synaptosomal-associated protein 25
      • Protein or peptide: Synaptosomal-associated protein 25
    • Complex: Syntaxin-1A
      • Protein or peptide: Syntaxin-1A
    • Complex: Vesicle-associated membrane protein 2
      • Protein or peptide: Vesicle-associated membrane protein 2
    • Complex: Alpha-soluble NSF attachment protein
      • Protein or peptide: Alpha-soluble NSF attachment protein
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
KeywordsSNARE / NSF / SNAP / ATPase / AAA / disassembly / synapse / membrane fusion / exocytosis / HYDROLASE
Function / homology
Function and homology information


soluble NSF attachment protein activity / Intra-Golgi traffic / Retrograde transport at the Trans-Golgi-Network / COPI-dependent Golgi-to-ER retrograde traffic / COPI-mediated anterograde transport / trans-Golgi Network Vesicle Budding / BLOC-1 complex / SNARE complex disassembly / regulation of delayed rectifier potassium channel activity / exocytic insertion of neurotransmitter receptor to postsynaptic membrane ...soluble NSF attachment protein activity / Intra-Golgi traffic / Retrograde transport at the Trans-Golgi-Network / COPI-dependent Golgi-to-ER retrograde traffic / COPI-mediated anterograde transport / trans-Golgi Network Vesicle Budding / BLOC-1 complex / SNARE complex disassembly / regulation of delayed rectifier potassium channel activity / exocytic insertion of neurotransmitter receptor to postsynaptic membrane / myosin head/neck binding / Other interleukin signaling / synaptic vesicle fusion to presynaptic active zone membrane / synaptobrevin 2-SNAP-25-syntaxin-1a-complexin II complex / synaptobrevin 2-SNAP-25-syntaxin-1a complex / synaptobrevin 2-SNAP-25-syntaxin-1a-complexin I complex / calcium ion-regulated exocytosis of neurotransmitter / Glutamate Neurotransmitter Release Cycle / Norepinephrine Neurotransmitter Release Cycle / COPII-mediated vesicle transport / Acetylcholine Neurotransmitter Release Cycle / positive regulation of norepinephrine secretion / positive regulation of catecholamine secretion / Serotonin Neurotransmitter Release Cycle / GABA synthesis, release, reuptake and degradation / Lysosome Vesicle Biogenesis / presynaptic dense core vesicle exocytosis / Dopamine Neurotransmitter Release Cycle / regulated exocytosis / extrinsic component of presynaptic membrane / zymogen granule membrane / ribbon synapse / synaptic vesicle docking / regulation of synaptic vesicle priming / Golgi Associated Vesicle Biogenesis / storage vacuole / regulation of establishment of protein localization / Insertion of tail-anchored proteins into the endoplasmic reticulum membrane / response to gravity / positive regulation of calcium ion-dependent exocytosis / vesicle-mediated transport in synapse / protein-containing complex disassembly / vesicle docking / eosinophil degranulation / secretion by cell / SNAP receptor activity / chloride channel inhibitor activity / regulation of exocytosis / SNARE complex / vesicle fusion / neurotransmitter receptor internalization / regulation of vesicle-mediated transport / Cargo recognition for clathrin-mediated endocytosis / ATP-dependent protein disaggregase activity / calcium-ion regulated exocytosis / LGI-ADAM interactions / Clathrin-mediated endocytosis / intra-Golgi vesicle-mediated transport / hormone secretion / actomyosin / positive regulation of intracellular protein transport / Golgi to plasma membrane protein transport / Golgi stack / positive regulation of hormone secretion / neurotransmitter secretion / ATP-dependent protein binding / apical protein localization / neuron projection terminus / positive regulation of ATP-dependent activity / protein localization to membrane / syntaxin binding / vesicle-fusing ATPase / regulation of synaptic vesicle recycling / syntaxin-1 binding / clathrin-coated vesicle / insulin secretion / Neutrophil degranulation / SNARE complex assembly / endosomal transport / positive regulation of neurotransmitter secretion / neurotransmitter transport / synaptic vesicle priming / myosin binding / regulation of synapse assembly / positive regulation of receptor recycling / regulation of neuron projection development / exocytosis / modulation of excitatory postsynaptic potential / associative learning / synaptic vesicle exocytosis / positive regulation of exocytosis / postsynaptic cytosol / protein sumoylation / synaptic vesicle endocytosis / voltage-gated potassium channel activity / positive regulation of excitatory postsynaptic potential / long-term memory / calcium channel inhibitor activity / response to glucose / axonal growth cone
Similarity search - Function
NSF attachment protein / Soluble NSF attachment protein, SNAP / : / NSF, AAA+ ATPase lid domain / Vesicle-fusing ATPase / Synaptobrevin/Vesicle-associated membrane protein / Synaptosomal-associated protein 25 / SNAP-25 domain / SNAP-25 family / Synaptobrevin signature. ...NSF attachment protein / Soluble NSF attachment protein, SNAP / : / NSF, AAA+ ATPase lid domain / Vesicle-fusing ATPase / Synaptobrevin/Vesicle-associated membrane protein / Synaptosomal-associated protein 25 / SNAP-25 domain / SNAP-25 family / Synaptobrevin signature. / Syntaxin / Syntaxin N-terminal domain / Syntaxin, N-terminal domain / SNARE domain / Synaptobrevin-like / Syntaxin / Syntaxin/epimorphin, conserved site / Syntaxin / epimorphin family signature. / Synaptobrevin / v-SNARE, coiled-coil homology domain / v-SNARE coiled-coil homology domain profile. / SNARE / Helical region found in SNAREs / t-SNARE coiled-coil homology domain profile. / Target SNARE coiled-coil homology domain / Cell division protein 48 (CDC48), N-terminal domain / CDC48, N-terminal subdomain / Cell division protein 48 (CDC48) N-terminal domain / CDC48, domain 2 / Cell division protein 48 (CDC48), domain 2 / Cell division protein 48 (CDC48) domain 2 / CDC48 domain 2-like superfamily / Aspartate decarboxylase-like domain superfamily / AAA ATPase, AAA+ lid domain / AAA+ lid domain / ATPase, AAA-type, conserved site / AAA-protein family signature. / ATPase family associated with various cellular activities (AAA) / ATPase, AAA-type, core / Tetratricopeptide-like helical domain superfamily / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Vesicle-fusing ATPase / Syntaxin-1A / Alpha-soluble NSF attachment protein / Synaptosomal-associated protein 25 / Vesicle-associated membrane protein 2
Similarity search - Component
Biological speciesCricetulus griseus (Chinese hamster) / Rattus norvegicus (Norway rat)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.4 Å
AuthorsWhite KI / Zhao M
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Human Genome Research Institute (NIH/NHGRI)R37MH63105 United States
CitationJournal: Elife / Year: 2018
Title: Structural principles of SNARE complex recognition by the AAA+ protein NSF.
Authors: K Ian White / Minglei Zhao / Ucheor B Choi / Richard A Pfuetzner / Axel T Brunger /
Abstract: The recycling of SNARE proteins following complex formation and membrane fusion is an essential process in eukaryotic trafficking. A highly conserved AAA+ protein, NSF (-ethylmaleimide sensitive ...The recycling of SNARE proteins following complex formation and membrane fusion is an essential process in eukaryotic trafficking. A highly conserved AAA+ protein, NSF (-ethylmaleimide sensitive factor) and an adaptor protein, SNAP (soluble NSF attachment protein), disassemble the SNARE complex. We report electron-cryomicroscopy structures of the complex of NSF, αSNAP, and the full-length soluble neuronal SNARE complex (composed of syntaxin-1A, synaptobrevin-2, SNAP-25A) in the presence of ATP under non-hydrolyzing conditions at ~3.9 Å resolution. These structures reveal electrostatic interactions by which two αSNAP molecules interface with a specific surface of the SNARE complex. This interaction positions the SNAREs such that the 15 N-terminal residues of SNAP-25A are loaded into the D1 ring pore of NSF via a spiral pattern of interactions between a conserved tyrosine NSF residue and SNAP-25A backbone atoms. This loading process likely precedes ATP hydrolysis. Subsequent ATP hydrolysis then drives complete disassembly.
History
DepositionSep 4, 2018-
Header (metadata) releaseSep 19, 2018-
Map releaseSep 19, 2018-
UpdateMar 13, 2024-
Current statusMar 13, 2024Processing site: RCSB / Status: Released

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Structure visualization

Movie
  • Surface view with section colored by density value
  • Surface level: 0.0135
  • Imaged by UCSF Chimera
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  • Surface view colored by cylindrical radius
  • Surface level: 0.0135
  • Imaged by UCSF Chimera
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  • Surface view with fitted model
  • Atomic models: PDB-6mdm
  • Surface level: 0.0135
  • Imaged by UCSF Chimera
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Movie viewer
Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_9100.png

Downloads & links

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Map

FileDownload / File: emd_9100.map.gz / Format: CCP4 / Size: 46.4 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationThe unsharpened map.
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.31 Å/pix.
x 230 pix.
= 301.3 Å		1.31 Å/pix.
x 230 pix.
= 301.3 Å		1.31 Å/pix.
x 230 pix.
= 301.3 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.31 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.0135 / Movie #1: 0.0135
Minimum - Maximum-0.008086054 - 0.040476423
Average (Standard dev.)0.00031600829 (±0.002695571)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions230230230
Spacing230230230
CellA=B=C: 301.3 Å
α=β=γ: 90.0 °

CCP4 map header:

modeImage stored as Reals
Å/pix. X/Y/Z1.311.311.31
M x/y/z230230230
origin x/y/z0.0000.0000.000
length x/y/z301.300301.300301.300
α/β/γ90.00090.00090.000
MAP C/R/S123
start NC/NR/NS000
NC/NR/NS230230230
D min/max/mean-0.0080.0400.000

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Supplemental data

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Additional map: The sharpened map

Fileemd_9100_additional.map
AnnotationThe sharpened map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : 20S supercomplex consisting of soluble neuronal SNARE complex, al...

EntireName: 20S supercomplex consisting of soluble neuronal SNARE complex, alpha-SNAP, and N-ethylmaleimide sensitive factor (NSF)
Components
  • Complex: 20S supercomplex consisting of soluble neuronal SNARE complex, alpha-SNAP, and N-ethylmaleimide sensitive factor (NSF)
    • Complex: N-ethylmaleimide sensitive factor
      • Protein or peptide: Vesicle-fusing ATPase
    • Complex: Synaptosomal-associated protein 25
      • Protein or peptide: Synaptosomal-associated protein 25
    • Complex: Syntaxin-1A
      • Protein or peptide: Syntaxin-1A
    • Complex: Vesicle-associated membrane protein 2
      • Protein or peptide: Vesicle-associated membrane protein 2
    • Complex: Alpha-soluble NSF attachment protein
      • Protein or peptide: Alpha-soluble NSF attachment protein
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
  • Ligand: ADENOSINE-5'-DIPHOSPHATE

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Supramolecule #1: 20S supercomplex consisting of soluble neuronal SNARE complex, al...

SupramoleculeName: 20S supercomplex consisting of soluble neuronal SNARE complex, alpha-SNAP, and N-ethylmaleimide sensitive factor (NSF)
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#5
Molecular weightTheoretical: 33.25 KDa

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Supramolecule #2: N-ethylmaleimide sensitive factor

SupramoleculeName: N-ethylmaleimide sensitive factor / type: complex / ID: 2 / Parent: 1 / Macromolecule list: #1
Source (natural)Organism: Cricetulus griseus (Chinese hamster)

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Supramolecule #3: Synaptosomal-associated protein 25

SupramoleculeName: Synaptosomal-associated protein 25 / type: complex / ID: 3 / Parent: 1 / Macromolecule list: #2
Source (natural)Organism: Rattus norvegicus (Norway rat)

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Supramolecule #4: Syntaxin-1A

SupramoleculeName: Syntaxin-1A / type: complex / ID: 4 / Parent: 1 / Macromolecule list: #3
Source (natural)Organism: Rattus norvegicus (Norway rat)

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Supramolecule #5: Vesicle-associated membrane protein 2

SupramoleculeName: Vesicle-associated membrane protein 2 / type: complex / ID: 5 / Parent: 1 / Macromolecule list: #4
Source (natural)Organism: Rattus norvegicus (Norway rat)

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Supramolecule #6: Alpha-soluble NSF attachment protein

SupramoleculeName: Alpha-soluble NSF attachment protein / type: complex / ID: 6 / Parent: 1 / Macromolecule list: #5
Source (natural)Organism: Rattus norvegicus (Norway rat)

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Macromolecule #1: Vesicle-fusing ATPase

MacromoleculeName: Vesicle-fusing ATPase / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO / EC number: vesicle-fusing ATPase
Source (natural)Organism: Cricetulus griseus (Chinese hamster)
Molecular weightTheoretical: 85.509227 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MGHHHHHHDY DIPTTENLYF QGAHMAGRSM QAARCPTDEL SLSNCAVVSE KDYQSGQHVI VRTSPNHKYI FTLRTHPSVV PGSVAFSLP QRKWAGLSIG QEIEVALYSF DKAKQCIGTM TIEIDFLQKK NIDSNPYDTD KMAAEFIQQF NNQAFSVGQQ L VFSFNDKL ...String:
MGHHHHHHDY DIPTTENLYF QGAHMAGRSM QAARCPTDEL SLSNCAVVSE KDYQSGQHVI VRTSPNHKYI FTLRTHPSVV PGSVAFSLP QRKWAGLSIG QEIEVALYSF DKAKQCIGTM TIEIDFLQKK NIDSNPYDTD KMAAEFIQQF NNQAFSVGQQ L VFSFNDKL FGLLVKDIEA MDPSILKGEP ASGKRQKIEV GLVVGNSQVA FEKAENSSLN LIGKAKTKEN RQSIINPDWN FE KMGIGGL DKEFSDIFRR AFASRVFPPE IVEQMGCKHV KGILLYGPPG CGKTLLARQI GKMLNAREPK VVNGPEILNK YVG ESEANI RKLFADAEEE QRRLGANSGL HIIIFDEIDA ICKQRGSMAG STGVHDTVVN QLLSKIDGVE QLNNILVIGM TNRP DLIDE ALLRPGRLEV KMEIGLPDEK GRLQILHIHT ARMRGHQLLS ADVDIKELAV ETKNFSGAEL EGLVRAAQST AMNRH IIAS TKVEVDMEKA ESLQVTRGDF LASLENDIKP AFGTNQEDYA SYIMNGIIKW GDPVTRVLDD GELLVQQTKN SDRTPL VSV LLEGPPHSGK TALAAKIAEE SNFPFIKICS PDKMIGFSET AKCQAMKKIF DDAYKSQLSC VVVDDIERLL DYVPIGP RF SNLVLQALLV LLKKAPPQGR KLLIIGTTSR KDVLQEMEML NAFSTTIHVP NIATGEQLLE ALELLGNFKD KERTTIAQ Q VKGKKVWIGI KKLLMLIEMS LQMDPEYRVR KFLALLREEG ASPLDFD

UniProtKB: Vesicle-fusing ATPase

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Macromolecule #2: Synaptosomal-associated protein 25

MacromoleculeName: Synaptosomal-associated protein 25 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Rattus norvegicus (Norway rat)
Molecular weightTheoretical: 23.512387 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MASMAEDADM RNELEEMQRR ADQLADESLE STRRMLQLVE ESKDAGIRTL VMLDEQGEQL DRVEEGMNHI NQDMKEAEKN LKDLGKCCG LFICPCNKLK SSDAYKKAWG NNQDGVVASQ PARVVDEREQ MAISGGFIRR VTNDARENEM DENLEQVSGI I GNLRHMAL ...String:
MASMAEDADM RNELEEMQRR ADQLADESLE STRRMLQLVE ESKDAGIRTL VMLDEQGEQL DRVEEGMNHI NQDMKEAEKN LKDLGKCCG LFICPCNKLK SSDAYKKAWG NNQDGVVASQ PARVVDEREQ MAISGGFIRR VTNDARENEM DENLEQVSGI I GNLRHMAL DMGNEIDTQN RQIDRIMEKA DSNKTRIDEA NQRATKMLG

UniProtKB: Synaptosomal-associated protein 25

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Macromolecule #3: Syntaxin-1A

MacromoleculeName: Syntaxin-1A / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Rattus norvegicus (Norway rat)
Molecular weightTheoretical: 29.634129 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MKDRTQELRT AKDSDDDDDV TVTVDRDRFM DEFFEQVEEI RGFIDKIAEN VEEVKRKHSA ILASPNPDEK TKEELEELMS DIKKTANKV RSKLKSIEQS IEQEEGLNRS SADLRIRKTQ HSTLSRKFVE VMSEYNATQS DYRERSKGRI QRQLEITGRT T TSEELEDM ...String:
MKDRTQELRT AKDSDDDDDV TVTVDRDRFM DEFFEQVEEI RGFIDKIAEN VEEVKRKHSA ILASPNPDEK TKEELEELMS DIKKTANKV RSKLKSIEQS IEQEEGLNRS SADLRIRKTQ HSTLSRKFVE VMSEYNATQS DYRERSKGRI QRQLEITGRT T TSEELEDM LESGNPAIFA SGIIMDSSIS KQALSEIETR HSEIIKLENS IRELHDMFMD MAMLVESQGE MIDRIEYNVE HA VDYVERA VSDTKKAVK

UniProtKB: Syntaxin-1A

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Macromolecule #4: Vesicle-associated membrane protein 2

MacromoleculeName: Vesicle-associated membrane protein 2 / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Rattus norvegicus (Norway rat)
Molecular weightTheoretical: 12.981304 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
MASYYHHHHH HDYDIPTSEN LYFQGASHMS ATAATVPPAA PAGEGGPPAP PPNLTSNRRL QQTQAQVDEV VDIMRVNVDK VLERDQKLS ELDDRADALQ AGASQFETSA AKLKRKYW

UniProtKB: Vesicle-associated membrane protein 2

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Macromolecule #5: Alpha-soluble NSF attachment protein

MacromoleculeName: Alpha-soluble NSF attachment protein / type: protein_or_peptide / ID: 5 / Number of copies: 2 / Enantiomer: LEVO
Source (natural)Organism: Rattus norvegicus (Norway rat)
Molecular weightTheoretical: 35.598223 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MHHHHHHHHH HENLYFQGMD TSGKQAEAMA LLAEAERKVK NSQSFFSGLF GGSSKIEEAC EIYARAANMF KMAKNWSAAG NAFCQAAQL HLQLQSKHDA ATCFVDAGNA FKKADPQEAI NCLMRAIEIY TDMGRFTIAA KHHISIAEIY ETELVDVEKA I AHYEQSAD ...String:
MHHHHHHHHH HENLYFQGMD TSGKQAEAMA LLAEAERKVK NSQSFFSGLF GGSSKIEEAC EIYARAANMF KMAKNWSAAG NAFCQAAQL HLQLQSKHDA ATCFVDAGNA FKKADPQEAI NCLMRAIEIY TDMGRFTIAA KHHISIAEIY ETELVDVEKA I AHYEQSAD YYKGEESNSS ANKCLLKVAG YAAQLEQYQK AIDIYEQVGT SAMDSPLLKY SAKDYFFKAA LCHFCIDMLN AK LAVQKYE ELFPAFSDSR ECKLMKKLLE AHEEQNVDSY TESVKEYDSI SRLDQWLTTM LLRIKKTIQG DEEDLR

UniProtKB: Alpha-soluble NSF attachment protein

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Macromolecule #6: ADENOSINE-5'-TRIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 6 / Number of copies: 9 / Formula: ATP
Molecular weightTheoretical: 507.181 Da
Chemical component information

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

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Macromolecule #7: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 7 / Number of copies: 2 / Formula: ADP
Molecular weightTheoretical: 427.201 Da
Chemical component information

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

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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

Concentration15 mg/mL
BufferpH: 8
Component:
ConcentrationFormulaName
0.05 MC4H11NO3Tris HCl
0.15 MNaClSodium chloride
0.001 MC10H16N5O13P3Adenosine triphosphate
0.001 MC10H16N2O8Ethylenediaminetetraacetic acid
0.001 MC4H10O2S2Dithiothreitol
0.05 % v/vNonidet P-40
GridSupport film - Material: CARBON / Support film - topology: HOLEY ARRAY / Details: Not available
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 293 K / Instrument: FEI VITROBOT MARK I / Details: Blot for 3.5 seconds before plunging..

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Detector mode: SUPER-RESOLUTION / Digitization - Frames/image: 2-40 / Number grids imaged: 2 / Number real images: 5418 / Average exposure time: 10.0 sec. / Average electron dose: 58.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 70.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.5 µm
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 475680
Startup modelType of model: PDB ENTRY
PDB model - PDB ID:

3j96

Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 4.4 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: RELION (ver. 2.1) / Number images used: 55150
Initial angle assignmentType: PROJECTION MATCHING / Software - Name: RELION (ver. 2.1)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 2.1)
Final 3D classificationNumber classes: 4 / Software - Name: RELION (ver. 2.1)
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial modelPDB ID:

3j96


Chain - Source name: PDB / Chain - Initial model type: experimental model
RefinementSpace: REAL / Protocol: RIGID BODY FIT
Output model

PDB-6mdm:
The 20S supercomplex engaging the SNAP-25 N-terminus (class 1)

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