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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | PRD-0038 Spike glycoprotein NTD | |||||||||
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![]() | Sarbecoviruses / Spike glycoprotein / fusion protein / neutralizing antibodies / Structural Genomics / Seattle Structural Genomics Center for Infectious Disease / SSGCID / inhibitor / viral protein | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 2.9 Å | |||||||||
![]() | Lee J / Park YJ / Veesler D | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Broad receptor tropism and immunogenicity of a clade 3 sarbecovirus. Authors: Lee J / Zepeda SK / Park YJ / Taylor AL / Quispe J / Stewart C / Leaf EM / Treichel C / Corti D / King NP / Starr TN / Veesler D | |||||||||
History |
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Structure visualization
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Downloads & links
-EMDB archive
Map data | ![]() | 483.9 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 16.1 KB 16.1 KB | Display Display | ![]() |
Images | ![]() | 64.3 KB | ||
Filedesc metadata | ![]() | 5.4 KB | ||
Others | ![]() ![]() ![]() | 257.5 MB 475 MB 475 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 876.8 KB | Display | ![]() |
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Full document | ![]() | 876.4 KB | Display | |
Data in XML | ![]() | 17.3 KB | Display | |
Data in CIF | ![]() | 20.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
EMDB pages | ![]() ![]() |
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Map
File | ![]() | ||||||||||||||||||||
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Voxel size | X=Y=Z: 1 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
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Sample components
-Entire : PRD-0038 Spike glycoprotein
Entire | Name: PRD-0038 Spike glycoprotein |
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Components |
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-Supramolecule #1: PRD-0038 Spike glycoprotein
Supramolecule | Name: PRD-0038 Spike glycoprotein / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: PRD-0038 Spike glycoprotein NTD
Macromolecule | Name: PRD-0038 Spike glycoprotein NTD / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Sequence | String: MGILPSPGMP ALLSLVSLLS VLLMGCVAET GTQEGCGILS NKSKPALTQY SSSRRGFYYF DDTFRSSVRV LTTGYFLPFN SNLTGYSSRN AVTGRLIQFD NPNIPFKDGL YFAATERSNV IRGWIFGSTL DNTTQSAVLF NNGTHIVINV CNFYFCQDPM LTVANGSHYK ...String: MGILPSPGMP ALLSLVSLLS VLLMGCVAET GTQEGCGILS NKSKPALTQY SSSRRGFYYF DDTFRSSVRV LTTGYFLPFN SNLTGYSSRN AVTGRLIQFD NPNIPFKDGL YFAATERSNV IRGWIFGSTL DNTTQSAVLF NNGTHIVINV CNFYFCQDPM LTVANGSHYK SWVFLNATNC TYNRVHAFEI DPSLNTGAFI HLREHVFRNV DGFLYVYHNY ERANVYDNFP SGFSVLKPIL KLPFGLNITQ FKVIMTLFSP TTSSFNADAS VYFVGHLKPL TMLAEFDENG TITDAVDCSQ DPLSELKCTT KSLTVEKGIY QTSNFRVSPS TEVVRFPNIT NLCPFGQVFN ASKFPSVYAW ERLRISDCVA DYSVLYNSSS SFSTFKCYGV SPTKLNDLCF SSVYADYFVV KGDDVRQIAP AQTGVIADYN YKLPDDFTGC VLAWNTNSVD SKQGNNFYYR LFRHGKIKPY ERDISNVLYN SAGGTCSSTS QLGCYEPLKS YGFTPTVGVG YQPYRVVVLS FELLNAPATV CGPKKSTELV KNKCVNFNFN GLTGTGVLTS STKKFQPFQQ FGRDVSDFTD SVRDPKTLEI LDISPCSYGG VSVITPGTNT SKAVAVLYQD VNCTDVPTML HVEQVSTDWR VYALSADGNM FQTQAGCLVG ATYENSTYEC DIPIGAGICA KFGSNKLRLE SIVAYTMSIG EDQSIAYSNN TIAIPTNFSI SVTTEVLPVS MTKTSVDCNM YICGDSTECS NLLLQYGSFC TQLNRALSGI AVEQDRNTRD VFAQTKAIYK TPNIKDFGGF NFSQILPDPK KPSYRSPIED LLYNKVTLSD PGFMKQYGDC LGGINARDLI CAQKFNGLTV LPPLLTDDMI AAYTAALISG TATAGYTFGA GAALQIPFPM QMAYRFNGIG VTQNVLYENQ KQIANQFNNA ISKIQDSLTT TPAALGKLQD VINQNAVALN TLVKQLSSNF GAISSVLNDI LSRLDPPEAE VQIDRLITGR LQSLQTYVTQ QLIRAAEIRA SANLAATKMS ECVLGQSKRV DFCGKGYHLM SFPQAAPHGV VFLHVTYVPS QQQNFTTAPA ICHNGKAYFP REGVFVMNGT HWFITQRNFY SPQVITTDNT FESGSCDVVI GIVNNTVYDP LQPELESFKQ ELDKYFKNHT SPDVDLGDIS GINASVVDIK KEIAHLNEIA KNLNESLIDL QELGKYEQYV KSGRENLYFQ GGGGSGYIPE APRDGQAYVR KDGEWVLLST FLGHHHHHHH HGGSSGLNDI FEAQKIEWHE |
-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: 60.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 0.0 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: NONE |
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Final reconstruction | Applied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 2.9 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 310041 |
Initial angle assignment | Type: PROJECTION MATCHING |
Final angle assignment | Type: PROJECTION MATCHING |