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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | Cryo-EM structure of the portal-tail complex of LME-1 phage | |||||||||
![]() | unsharpened map | |||||||||
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![]() | LME-1 / legionella pneumophila / phage / portal / tail / podovirus / podophage / VIRAL PROTEIN | |||||||||
Function / homology | Head-to-tail connector protein, podovirus-type / Bacteriophage head to tail connecting protein / symbiont entry into host cell / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein / Uncharacterized protein![]() | |||||||||
Biological species | ![]() ![]() ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 1.9 Å | |||||||||
![]() | Deme JC / Lea SM | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Phage resistance as an unexpected environmental determinant of the accidental virulence of Legionella pneumophila against the human host. Authors: Nicholson B / Sante JF / Chaney EH / Deme JC / Deecker SR / Sztanko K / Davidson AR / Lea SM / Ensminger AW | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 981.2 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 23.6 KB 23.6 KB | Display Display | ![]() |
FSC (resolution estimation) | ![]() | 26.2 KB | Display | ![]() |
Images | ![]() | 199.7 KB | ||
Masks | ![]() | 1.9 GB | ![]() | |
Filedesc metadata | ![]() | 7 KB | ||
Others | ![]() ![]() ![]() ![]() | 6.6 MB 1.8 GB 1.8 GB 1.8 GB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 1 MB | Display | ![]() |
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Full document | ![]() | 1 MB | Display | |
Data in XML | ![]() | 36.4 KB | Display | |
Data in CIF | ![]() | 48.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9efkMC ![]() 9eg4C 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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Map
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Annotation | unsharpened map | ||||||||||||||||||||||||||||||||||||
Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.878 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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Projections & Slices |
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Density Histograms |
-Additional map: mask used for FSC calculation
File | emd_47975_additional_1.map | ||||||||||||
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Annotation | mask used for FSC calculation | ||||||||||||
Projections & Slices |
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Density Histograms |
-Additional map: B-factor sharpened map
File | emd_47975_additional_2.map | ||||||||||||
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Annotation | B-factor sharpened map | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: half map 2
File | emd_47975_half_map_1.map | ||||||||||||
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Annotation | half map 2 | ||||||||||||
Projections & Slices |
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Density Histograms |
-Half map: half map 1
File | emd_47975_half_map_2.map | ||||||||||||
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Annotation | half map 1 | ||||||||||||
Projections & Slices |
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Density Histograms |
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Sample components
-Entire : LME-1
Entire | Name: ![]() ![]() |
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Components |
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-Supramolecule #1: LME-1
Supramolecule | Name: LME-1 / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 446 / Sci species name: LME-1 / Virus type: VIRION / Virus isolate: STRAIN / Virus enveloped: No / Virus empty: No |
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-Macromolecule #1: orf12
Macromolecule | Name: orf12 / type: protein_or_peptide / ID: 1 / Number of copies: 12 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 62.743062 KDa |
Sequence | String: MVDVKKLLGK RDNSKLYEEI RKETKPKLDV NRLCRMRNDA KSDLDMWRSI LQTAYHYAMP DYNPFENYGL AGFLTPGQQY NADIYDLTL PIAHKRLADK MLMNMVPQGQ QWVKFTPGDE FGEPGTPLYQ RALDATQRMT DHFFKIIDRS NFYLAVGESL Q DVLISTGI ...String: MVDVKKLLGK RDNSKLYEEI RKETKPKLDV NRLCRMRNDA KSDLDMWRSI LQTAYHYAMP DYNPFENYGL AGFLTPGQQY NADIYDLTL PIAHKRLADK MLMNMVPQGQ QWVKFTPGDE FGEPGTPLYQ RALDATQRMT DHFFKIIDRS NFYLAVGESL Q DVLISTGI IAINEGNRKR PVRYEAVPPA QVMFQGDAEG QVDAIFRDWY QVRIENIKSM WPKAEVAKLN KKPEDKVDIW EC AWIDYEA PEKERYQYVV MTSSKDVLLE QSNSSWPWVV YRMRRLTGEI RGRGPSLSAY PTAATINQAL EDELVAAAFQ ANP MYMAAS DSAFNQQTFT PRPGSIVPVQ MVQGEWPIKP FEQSGNIQFN ALLVNDFRQQ INELLYAFPL GAVNSPTRTA TEAE IRYTE NLESFSAMVP RLQNEFFIPV IQRTLWVINK VLPETFANIP DDIRNKMISV DGQILGLSFD TPLMTAKGQV KTAAL LGFY QAAASLLGPE AATASLDPVE VLTNLADNQG IDVRNIKTRE ELEQLLQAAG QIAQQEAAQQ GVIIGSEQPQ UniProtKB: Uncharacterized protein |
-Macromolecule #2: orf18
Macromolecule | Name: orf18 / type: protein_or_peptide / ID: 2 / Number of copies: 6 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 89.921969 KDa |
Sequence | String: MPIRSISNTF NRGELDPTLF ARDDLDIYDK GARKLRNMIA LWTGAARIAP GTIYIDMMVD RENGNAVIQD PLMVKGFDFT YDADAEITY TIIIRKSGTN IAFDIYYADT LQTTVTSTAY LATQIQDIHV AAAHDRVLIL HENVQIRQLK RGASHSSWSL T TFNPRVYP ...String: MPIRSISNTF NRGELDPTLF ARDDLDIYDK GARKLRNMIA LWTGAARIAP GTIYIDMMVD RENGNAVIQD PLMVKGFDFT YDADAEITY TIIIRKSGTN IAFDIYYADT LQTTVTSTAY LATQIQDIHV AAAHDRVLIL HENVQIRQLK RGASHSSWSL T TFNPRVYP TYDFSVIGEA INYQSFTFTL SATTGSITIT SSSAVFTHNH VGGLFRSLGG TARITAVAST TSASATVLDN FT GTSCAGN LSSLAEKLWN SDTTTAPVSA NRGWPARGVF YLNRLILGRS LAVKNLVNLS TAGVYDNFDD ADLDGLVAFS VTF NGKGEQ SVQSIVADDS ILFTTANKLF AQSPLVESPI TINNVYFAPQ SQSPATSIEA ASIDNQTLFV SSDRTKVMQA MYST ADGKY ITLPATMLSN SIVDYINSNG TWEPAGISTR LYLATQDNGT MLLYSTLQTQ NVAGWSLRTT TGKFRQVIGE GRQSH VIVE REINIGASFE QTLDYAYLSD PTFKARYDVT EFFASSPMTS AIGVLENQND YILIGNQAPF TALDIDFNLV ASSDCQ LQF EYLDGNGFWD VFTPTDNTSG FTVDGTITWT FDDVLNWAPY QVNAIENQYW IRIKRLAETV NTAPVIGQVL INTGNRI YL ERQSFDEYMD STQIVTSDSN GLVTGLTHLA GQQVYAITED GATIGSSFVD ASGETSVKNV NTTLTVGMQY KPELIPMP L YAPTQMGDSL YAEKYVQDLY VDYVDSLYLQ AGFRPQLTDI PNMHLGNYTL GQSVPPQTGI YRICPRGDWE PRQEFVITQ SQPGPMTIIG VGYNVEVA UniProtKB: Uncharacterized protein |
-Macromolecule #3: orf22
Macromolecule | Name: orf22 / type: protein_or_peptide / ID: 3 / Number of copies: 18 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 68.819797 KDa |
Sequence | String: MSNIKINDVF QRIQYAASAG QTQFTIPFPF FDNEYVLVWQ NGVQLVMGGA PGQYGISGAG SPSGGLITLV TPAALNDIIT IQGDMPIDR TSIYSATISN LTGSDLNGDF NREVVMMKQI QTTQALLQLQ YAPWLEVSQD PDVTKDRYLP LLGSGQVWRM N DSGTGIEA ...String: MSNIKINDVF QRIQYAASAG QTQFTIPFPF FDNEYVLVWQ NGVQLVMGGA PGQYGISGAG SPSGGLITLV TPAALNDIIT IQGDMPIDR TSIYSATISN LTGSDLNGDF NREVVMMKQI QTTQALLQLQ YAPWLEVSQD PDVTKDRYLP LLGSGQVWRM N DSGTGIEA YTIDETPAPS SSPFIIYQAD ATLSNAQNLG ALTSGILKQT VGGGSSTLSI AQNAVDYWAP GDELTRSQAP VS PDDVVNK AYADSIASGF TFINPVNAAS TANFNSTYNN GSSGVGATLT ATSNGAFSLD GQAGVLNKSY LMKDQTNTFE NGI YILTQV GDGSTPAILT RATYFDQPSE IQPGDLVPVL AGTVNNGTLW LQTDTVSAVG TDPITFIAFL PAFSNIVTIS GNQT ITGDK TFTGTTTLDN FIFVGSNIQH LGDTGNQIIF GTATQINTIN NNTISDLSSS GLRLGAANAR VSTILDEDDM ASDSA TALA TQQSIKAYVD NFRAAGAILQ TVSTNMTNTF SASLAAGSGF SDVTGFNVSI TPSATANKVF IKVDMLLASD TVDIVV VVR LKRNGTPIDI GNAAGSRIQI TTGSTNAKAL DGLQAVSFSF LDSPATTSAI TYQVDIGQRT SGSAVGIVVN RSGADVD SS SYTRGASTIT AQEIKG UniProtKB: Uncharacterized protein |
-Macromolecule #4: orf17
Macromolecule | Name: orf17 / type: protein_or_peptide / ID: 4 / Number of copies: 12 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() ![]() |
Molecular weight | Theoretical: 22.792135 KDa |
Sequence | String: MIELTSAPTT KIEIISAAIS MVGKQQTVNT IDGGGALAID AEKLYDTLVS AELGSNRWRF AQAFQQISII TTLNPTFDGW LYECQIPAD CIMVQYLYPN IQYIVFGDKI LTKSNQTFTL IYSRNVPVSK WPPPFSLYIV YHLASMLGIS VTNSDRMLAR I SQGMEMWE ...String: MIELTSAPTT KIEIISAAIS MVGKQQTVNT IDGGGALAID AEKLYDTLVS AELGSNRWRF AQAFQQISII TTLNPTFDGW LYECQIPAD CIMVQYLYPN IQYIVFGDKI LTKSNQTFTL IYSRNVPVSK WPPPFSLYIV YHLASMLGIS VTNSDRMLAR I SQGMEMWE SRALFADAQS SVTLPFRHNP YVDVRYRYKT RGY UniProtKB: Uncharacterized protein |
-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: 7.5 |
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Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | TFS KRIOS |
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Image recording | Film or detector model: TFS FALCON 4i (4k x 4k) / Average electron dose: 52.9 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.1 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |