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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | Postfusion Nipah virus fusion protein in complex with Fab 1H1 | |||||||||
![]() | Postfusion Nipah virus fusion protein in complex with Fab 1H1 | |||||||||
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![]() | Nipah / Nipah virus / NiV / fusion / F / antibody / neutralizing / conserved epitope / neutralizing antibody / VIRAL PROTEIN / VIRAL PROTEIN-Immune System complex | |||||||||
Function / homology | ![]() membrane fusion involved in viral entry into host cell / symbiont entry into host cell / fusion of virus membrane with host plasma membrane / viral envelope / host cell plasma membrane / virion membrane / membrane Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.2 Å | |||||||||
![]() | Byrne PO / Blade EG / McLellan JS | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Postfusion Nipah virus fusion protein in complex with Fab 1H1 Authors: Byrne PO / Blade EG / McLellan JS | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 285.7 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 19.6 KB 19.6 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 16.1 KB | Display | ![]() |
Images | ![]() | 87.9 KB | ||
Masks | ![]() | 343 MB | ![]() | |
Filedesc metadata | ![]() | 5.7 KB | ||
Others | ![]() ![]() ![]() ![]() | 171.4 MB 323.6 MB 318.7 MB 318.7 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 808.9 KB | Display | ![]() |
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Full document | ![]() | 808.5 KB | Display | |
Data in XML | ![]() | 23.9 KB | Display | |
Data in CIF | ![]() | 31.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8dmjMC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Annotation | Postfusion Nipah virus fusion protein in complex with Fab 1H1 | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.81 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Mask #1
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Density Histograms |
-Additional map: Additional Map 1
File | emd_27541_additional_1.map | ||||||||||||
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Annotation | Additional Map 1 | ||||||||||||
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Density Histograms |
-Additional map: Additional Map 2
File | emd_27541_additional_2.map | ||||||||||||
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Annotation | Additional Map 2 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half Map 1
File | emd_27541_half_map_1.map | ||||||||||||
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Annotation | Half Map 1 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: Half Map 2
File | emd_27541_half_map_2.map | ||||||||||||
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Annotation | Half Map 2 | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Postfusion Nipah virus fusion protein in complex with Fab 1H1
Entire | Name: Postfusion Nipah virus fusion protein in complex with Fab 1H1 |
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Components |
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-Supramolecule #1: Postfusion Nipah virus fusion protein in complex with Fab 1H1
Supramolecule | Name: Postfusion Nipah virus fusion protein in complex with Fab 1H1 type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Fusion glycoprotein F0,Fusion glycoprotein F1
Macromolecule | Name: Fusion glycoprotein F0,Fusion glycoprotein F1 / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 58.45198 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: MYSMQLASCV TLTLVLLVNS QGILHYEKLS KIGLVKGVTR KYKIKSNPLT KDIVIKMIPN VSNMSQCTGS VMENYKTRLN GILTPIKGA LEIYKNGGSG VAIGIATAAQ ITAGVALYEA MKNADNINKL KSSIESTNEA VVKLQETAEK TVYVLTALQD Y INTNLVPT ...String: MYSMQLASCV TLTLVLLVNS QGILHYEKLS KIGLVKGVTR KYKIKSNPLT KDIVIKMIPN VSNMSQCTGS VMENYKTRLN GILTPIKGA LEIYKNGGSG VAIGIATAAQ ITAGVALYEA MKNADNINKL KSSIESTNEA VVKLQETAEK TVYVLTALQD Y INTNLVPT IDKISCKQTE LSLDLALSKY LSDLLFVFGP NLQDPVSNSM TIQAISQAFG GNYETLLRTL GYATEDFDDL LE SDSITGQ IIYVDLSSYY IIVRVYFPIL TEIQQAYIQE LLPVSFNNDN SEWISIVPNF ILVRNTLISN IEIGFCLITK RSV ICNQDY ATPMTNNMRE CLTGSTEKCP RELVVSSHVP RFALSNGVLF ANCISVTCQC QTTGRAISQS GEQTLLMIDN TTCP TAVLG NVIISLGKYL GSVNYNSEGI AIGPPVFTDK VDISSQISSM NQSLQQSKDY IKEAQRLLDT VNPSLKLMKQ IEDKI EEIL SKIYHIENEI ARIKKLIGEA PGGLVPRGSH HHHHHSAWSH PQFEK UniProtKB: Fusion glycoprotein F0, Fusion glycoprotein F0 |
-Macromolecule #2: antibody 1H1 heavy chain
Macromolecule | Name: antibody 1H1 heavy chain / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 13.256589 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: AVQLQQSGAE LMRPGASMKI SCKATGYTFS SYWIDWVKQR PGHGLEWIGE ILPGSGDTNY NENFKGKAAF TADTSSNTAY MQLTSLTSE DSAVFYCARG GRYHGQGFFD YWGQGTTLTV SS |
-Macromolecule #3: antibody 1H1 light chain
Macromolecule | Name: antibody 1H1 light chain / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 11.752168 KDa |
Recombinant expression | Organism: ![]() |
Sequence | String: AIQMTQSPAS LSASVGETVT ITCRPSENVH IYLAWYQQKQ GKSPQLLVYN AKTLADGVPS RFSGSASGTQ FSLKINSLQP EDFGSYYCQ HFWSIPYTFG GGTKLEIK |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 8 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 70.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.5 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |