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Yorodumi- EMDB-19070: STRUCTURE OF THE MOUSE FCGBP DIMER PROTEIN IN ITS COMPACT CONFORMATION -
+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-19070 | |||||||||
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Title | STRUCTURE OF THE MOUSE FCGBP DIMER PROTEIN IN ITS COMPACT CONFORMATION | |||||||||
Map data | ||||||||||
Sample |
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Keywords | MUCUS / EPITHELIA / STRUCTURAL PROTEIN | |||||||||
Function / homology | Function and homology information | |||||||||
Biological species | Mus musculus (house mouse) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.7 Å | |||||||||
Authors | Gallego P / Hansson GC / Johansson MEV | |||||||||
Funding support | 1 items
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Citation | Journal: Febs J. / Year: 2025 Title: The structure of FCGBP is formed as a disulfide-mediated homodimer between its C-terminal domains Authors: Gallego P / Hansson GC | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_19070.map.gz | 82.5 MB | EMDB map data format | |
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Header (meta data) | emd-19070-v30.xml emd-19070.xml | 15.9 KB 15.9 KB | Display Display | EMDB header |
Images | emd_19070.png | 50 KB | ||
Filedesc metadata | emd-19070.cif.gz | 6.9 KB | ||
Others | emd_19070_half_map_1.map.gz emd_19070_half_map_2.map.gz | 154.1 MB 154.1 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-19070 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-19070 | HTTPS FTP |
-Validation report
Summary document | emd_19070_validation.pdf.gz | 1.2 MB | Display | EMDB validaton report |
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Full document | emd_19070_full_validation.pdf.gz | 1.2 MB | Display | |
Data in XML | emd_19070_validation.xml.gz | 14.7 KB | Display | |
Data in CIF | emd_19070_validation.cif.gz | 17.4 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-19070 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-19070 | HTTPS FTP |
-Related structure data
Related structure data | 8rdeMC 8r0tC 13900 M: atomic model generated by this map C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
EMDB pages | EMDB (EBI/PDBe) / EMDataResource |
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-Map
File | Download / File: emd_19070.map.gz / Format: CCP4 / Size: 166.4 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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Projections & slices | Image control
Images are generated by Spider. | ||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.86 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #1
File | emd_19070_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_19070_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : DISULFIDE-COVALENT HOMODIMER STRUCTURE OF THE MOUSE FCGBP PROTEIN
Entire | Name: DISULFIDE-COVALENT HOMODIMER STRUCTURE OF THE MOUSE FCGBP PROTEIN |
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Components |
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-Supramolecule #1: DISULFIDE-COVALENT HOMODIMER STRUCTURE OF THE MOUSE FCGBP PROTEIN
Supramolecule | Name: DISULFIDE-COVALENT HOMODIMER STRUCTURE OF THE MOUSE FCGBP PROTEIN type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1 |
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Source (natural) | Organism: Mus musculus (house mouse) |
-Macromolecule #1: Fc fragment of IgG binding protein
Macromolecule | Name: Fc fragment of IgG binding protein / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: Mus musculus (house mouse) |
Molecular weight | Theoretical: 275.970312 KDa |
Recombinant expression | Organism: Cricetulus griseus (Chinese hamster) |
Sequence | String: MGSPWKWWAL WAGATLLWAL LTPAEASCQG IQCASGQRCQ MVSGKARCVA ESTAVCRAQG DPHYTTFDGR RYDMMGTCSY TMAELCGSD ETLPAFSVEA KNEHRGSRQV SYVGLVTVYA YSHSVSLVRG EIGFVRIDNQ RSRLPASLSE GRLRVHKSGT R GVIEMDFG ...String: MGSPWKWWAL WAGATLLWAL LTPAEASCQG IQCASGQRCQ MVSGKARCVA ESTAVCRAQG DPHYTTFDGR RYDMMGTCSY TMAELCGSD ETLPAFSVEA KNEHRGSRQV SYVGLVTVYA YSHSVSLVRG EIGFVRIDNQ RSRLPASLSE GRLRVHKSGT R GVIEMDFG LVVTYDWDGQ LTLSLPKRFQ DQVCGLCGNY NGDPADDFLT PDLDQAPDAL EFANSWKLDD GDYLCDDGCH NS CPSCTPG QTQHYKGDRL CGMLTLSTGP FSACHEFLDP KPFLDDCVFD LCVTGGERLS LCRSLSAYAQ ACVELGVTLE NWR LPASCP MSCPANSCYD PCSPACPPSC NSEAVPTNCS SRPCVEGCVC LPGFVASGGD CVPVSSCGCI YQGRLLAPGQ EVFD DDRCR RRCTCDGATQ KVTCRDTTGC PSGERCNVQN GLLGCYPDNF ASCQASGDPH YVSFDGKRFD FMGTCTYLLV GSCGQ NAAL PAFKVLVENE HRGSQTVSYT RAVRVVAHGV EVAVRRENPG RVLVNGVLQY LPFQAAGGKI QVYRQGNDAI VSIDFG LTV TYNWDAHVTA KVPSSYAKDV CGLCGNFNGN PDDDLALKGG GQASNVLDFG NSWQEEIIPG CGATEPGDCP QLDSLVT QQ IQDKKECGIL ADPEGPFREC HKLLNPQGAI RDCVYDLCLL PGQSGPLCDA LAAYAAACQA AGGTVHPWRS EELCPLTC P PNSHYEQCSY GCPLSCGDLP VQGGCGSECR EGCVCNEGFA LSGESCVPLA SCGCVHEGAY HAPGETFYPG PGCDSLCHC EEGGLVSCEP SSCGPQEACQ PSNGVLGCVA VGTTTCQASG DPHYVTFDGR RFDFMGTCVY VLAQTCGNRP GLHQFTVLQE NEAWGNGKV SVTKVITVLV ANYTLRLEQS QWKVKVNGVD TKLPVMLDGG KIRVSQHGSD VVIETDFGLR VAYDLVYYVR V TIPGNYYK QMCGLCGDYN GDPKDDFQKP DGSQTTDPSD FGNSWEEAVP DSPCAPVPPC TGDDCDTECS PELQDKYHGE QF CGLLTSP TGPLAACHKL LDPQGPLQDC VFDLCLGGGN QSILCNIIHA YVSACQAAGG QVEPWRTETF CPMECPPHSH YEV CADTCS LGCWALNTPQ QCPEGCAEGC ECDSGFLYNG KACVPIEQCG CYHNGVYYEP EESVLIENCQ QHCVCQPGKG MMCQ DHSCK PGQVCEPSGG VLTCVTKDPC HGITCRPQET CKVQGGEGVC VPNYNSTCWL WGDPHYNSFD GWSFDFQGTC NYLLA GTLC PGVNAEGLTP FTVTTKNENR GSPAVSYVRQ VTVTTLNTNI SIHKNEIGKV RVNGVLMALP VYLAGGRISV INGGSK AVL ETDFGLQVTY DWNWRVDVTL PSSYHGAVCG LCGNMDKNHQ NDQVFPNGTM APSIPTWGGS WQVPGWDPLC WHECQGS CP TCPEDRVEEY EGPGFCGPLA PGTGSPFTSC HAHVPPESFF KGCVLDVCLG GGSKDILCQA LAAYAAACQA AGIKIEDW R TQAGCEITCP DNSHYELCGP PCPASCPPPA RHTAPTVCDG PCVEGCQCDE GFVLSADQCV PLDGGCGCWV NGTYYEAGT EFWADTTCSK RCHCGPGGDS LVCKPASCGL GEECALLPSG EIGCQPTSIT ECQAWGDPHY TTLDGHRFDF QGTCEYLLSA PCHEPPTGT EYFNVTVANE HRGSQAVSYT RSVTLQIYGL SLTLSAQWPR KLQVNGEFVA LPFHLDQKLS VYISGADVVV N TASGVSLA FDGDSFVRLR VPAAYAGTLC GLCGNYNKNP NDDLTAVGGK PEGWKVGGAP GCDQCEPEPC PKPCTPEEQE PF RGPDACG IITAPEGPLA PCHSLVPPTQ YFEACLLDAC QVQGHPGGLC PAIATYVAAC QAAGAQLGEW RKPDFCPLQC PAH SHYQLC GDSCPVSCPS LSAPVGCETI CREGCVCDAG FVLSGDTCVP VGQCGCLYQG RYYVLGATFY PGPECERLCE CGPD GQVTC QEGADCEPYE ECRIENGVQA CHPTGCGHCL ANGGLHYVTL DGRVYDLHGS CSYVLASVCH PKPGDEEFSI VLEKN SAGD PQRVVVTVAG QVVGLARGPQ VTVDGEVVTL PVATGHVSVT AEGRNIVLQT NKGMKVLFDG DAHILMSIPS SFRGRL CGL CGNFNGNWSD DFVLPSGAVA PNVEAFGTAW RAPGSSLGCG EGCGPQGCPV CLAEETQAYE KNDACGKIRD PHGPFAA CH KVLSPLEYFR QCVYDMCAHK GDKAYLCRSL AAYTAACQAA GAAVKPWRTD SVCPLQCPAH SHYSICTRSC QGSCAALS G LTGCTTRCFE GCECDDHFLL SHGVCIPAQD CGCVHNGQYM PVNSSLMSSD CSERCFCSPN NGLTCHEAGC PSGHVCEIQ AGVRECQAAR GLCSISVGAN LTTFDGAHNA ISSPGVYELS SRCPGLQKNV PWYRVLADVQ PCHNNDKIVS KVHIFFQDGL VTVIPSKGA WVNGLRVDLP ATVLTSVSVR RMPDGSMLVH QKAGVTVWLG KDGLLDVMVG DDLAAMLCGA CGNFDGDQTN D AYGSQGKT PIEKWRAQDF SPCSNTRTR UniProtKB: Fc fragment of IgG binding protein |
-Macromolecule #2: 2-acetamido-2-deoxy-beta-D-glucopyranose
Macromolecule | Name: 2-acetamido-2-deoxy-beta-D-glucopyranose / type: ligand / ID: 2 / Number of copies: 12 / Formula: NAG |
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Molecular weight | Theoretical: 221.208 Da |
Chemical component information | ChemComp-NAG: |
-Macromolecule #3: CALCIUM ION
Macromolecule | Name: CALCIUM ION / type: ligand / ID: 3 / Number of copies: 8 / Formula: CA |
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Molecular weight | Theoretical: 40.078 Da |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.4 |
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Grid | Details: 15MM |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 40.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 1.0 µm |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Startup model | Type of model: INSILICO MODEL |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 184178 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |