+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-32763 | |||||||||
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Title | Structure of a membrane protein M | |||||||||
Map data | ||||||||||
Sample |
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Function / homology | Function and homology information hexameric IgM immunoglobulin complex / IgM B cell receptor complex / pentameric IgM immunoglobulin complex / pre-B cell allelic exclusion / B cell receptor complex / IgM immunoglobulin complex / CD22 mediated BCR regulation / B cell activation / B cell proliferation / immunoglobulin complex, circulating ...hexameric IgM immunoglobulin complex / IgM B cell receptor complex / pentameric IgM immunoglobulin complex / pre-B cell allelic exclusion / B cell receptor complex / IgM immunoglobulin complex / CD22 mediated BCR regulation / B cell activation / B cell proliferation / immunoglobulin complex, circulating / multivesicular body / B cell differentiation / complement activation, classical pathway / Antigen activates B Cell Receptor (BCR) leading to generation of second messengers / antigen binding / Cell surface interactions at the vascular wall / B cell receptor signaling pathway / transmembrane signaling receptor activity / antibacterial humoral response / defense response to Gram-negative bacterium / adaptive immune response / Potential therapeutics for SARS / blood microparticle / immune response / membrane raft / external side of plasma membrane / innate immune response / cell surface / signal transduction / extracellular space / extracellular exosome / identical protein binding / plasma membrane Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.09 Å | |||||||||
Authors | Ma X / Zhu Y / Chen Y / Huang Z | |||||||||
Funding support | China, 1 items
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Citation | Journal: To Be Published Title: Structure of a membrane protein M Authors: Ma X / Zhu Y / Chen Y / Huang Z | |||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_32763.map.gz | 59.6 MB | EMDB map data format | |
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Header (meta data) | emd-32763-v30.xml emd-32763.xml | 12 KB 12 KB | Display Display | EMDB header |
Images | emd_32763.png | 27.7 KB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-32763 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-32763 | HTTPS FTP |
-Related structure data
Related structure data | 7wspMC 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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Related items in Molecule of the Month |
-Map
File | Download / File: emd_32763.map.gz / Format: CCP4 / Size: 64 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||
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Voxel size | X=Y=Z: 1.1 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Sample components
-Entire : complex
Entire | Name: complex |
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Components |
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-Supramolecule #1: complex
Supramolecule | Name: complex / type: complex / ID: 1 / Chimera: Yes / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: Homo sapiens (human) |
-Macromolecule #1: B-cell antigen receptor complex-associated protein alpha chain
Macromolecule | Name: B-cell antigen receptor complex-associated protein alpha chain type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 15.504718 KDa |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: LWMHKVPASL MVSLGEDAHF QCPHNSSNNA NVTWWRVLHG NYTWPPEFLG PGEDPNGTLI IQNVNKSHGG IYVCRVQEGN ESYQQSCGT YLRVRQPPPR PFLDMGEGTK NRIITAEGII LLFCAVVPGT LLLFRKRW |
-Macromolecule #2: B-cell antigen receptor complex-associated protein beta chain
Macromolecule | Name: B-cell antigen receptor complex-associated protein beta chain type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 16.143744 KDa |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: SRIWQSPRFI ARKRGFTVKM HCYMNSASGN VSWLWKQEMD ENPQQLKLEK GRMEESQNES LATLTIQGIR FEDNGIYFCQ QKCNNTSEV YQGCGTELRV MGFSTLAQLK QRNTLKDGII MIQTLLIILF IIVPIFLLLD |
-Macromolecule #3: Isoform 2 of Immunoglobulin heavy constant mu
Macromolecule | Name: Isoform 2 of Immunoglobulin heavy constant mu / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 40.470355 KDa |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: IAELPPKVSV FVPPRDGFFG NPRKSKLICQ ATGFSPRQIQ VSWLREGKQV GSGVTTDQVQ AEAKESGPTT YKVTSTLTIK ESDWLGQSM FTCRVDHRGL TFQQNASSMC VPDQDTAIRV FAIPPSFASI FLTKSTKLTC LVTDLTTYDS VTISWTRQNG E AVKTHTNI ...String: IAELPPKVSV FVPPRDGFFG NPRKSKLICQ ATGFSPRQIQ VSWLREGKQV GSGVTTDQVQ AEAKESGPTT YKVTSTLTIK ESDWLGQSM FTCRVDHRGL TFQQNASSMC VPDQDTAIRV FAIPPSFASI FLTKSTKLTC LVTDLTTYDS VTISWTRQNG E AVKTHTNI SESHPNATFS AVGEASICED DWNSGERFTC TVTHTDLPSP LKQTISRPKG VALHRPDVYL LPPAREQLNL RE SATITCL VTGFSPADVF VQWMQRGQPL SPEKYVTSAP MPEPQAPGRY FAHSILTVSE EEWNTGETYT CVVAHEALPN RVT ERTVDK STEGEVSADE EGFENLWATA STFIVLFLLS LFYSTTVTLF |
-Macromolecule #4: Isoform 2 of Immunoglobulin heavy constant mu
Macromolecule | Name: Isoform 2 of Immunoglobulin heavy constant mu / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 40.599535 KDa |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: IAELPPKVSV FVPPRDGFFG NPRKSKLICQ ATGFSPRQIQ VSWLREGKQV GSGVTTDQVQ AEAKESGPTT YKVTSTLTIK ESDWLGQSM FTCRVDHRGL TFQQNASSMC VPDQDTAIRV FAIPPSFASI FLTKSTKLTC LVTDLTTYDS VTISWTRQNG E AVKTHTNI ...String: IAELPPKVSV FVPPRDGFFG NPRKSKLICQ ATGFSPRQIQ VSWLREGKQV GSGVTTDQVQ AEAKESGPTT YKVTSTLTIK ESDWLGQSM FTCRVDHRGL TFQQNASSMC VPDQDTAIRV FAIPPSFASI FLTKSTKLTC LVTDLTTYDS VTISWTRQNG E AVKTHTNI SESHPNATFS AVGEASICED DWNSGERFTC TVTHTDLPSP LKQTISRPKG VALHRPDVYL LPPAREQLNL RE SATITCL VTGFSPADVF VQWMQRGQPL SPEKYVTSAP MPEPQAPGRY FAHSILTVSE EEWNTGETYT CVVAHEALPN RVT ERTVDK STEGEVSADE EGFENLWATA STFIVLFLLS LFYSTTVTLF K |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7 |
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Vitrification | Cryogen name: NITROGEN |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K2 QUANTUM (4k x 4k) / Average electron dose: 1.5 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: 2.5 µm / Nominal defocus min: 1.2 µm |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Startup model | Type of model: PDB ENTRY PDB model - PDB ID: |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 4.09 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 47428 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |