+Open data
-Basic information
Entry | Database: EMDB / ID: EMD-43232 | |||||||||||||||
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Title | CH235.12 Fab bound to the HIV-1 CH505.M5 SOSIP | |||||||||||||||
Map data | ||||||||||||||||
Sample |
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Keywords | Immunogen / Vaccine / Antibody / VIRAL PROTEIN / VIRAL PROTEIN-IMMUNE SYSTEM complex | |||||||||||||||
Function / homology | Function and homology information positive regulation of plasma membrane raft polarization / positive regulation of receptor clustering / positive regulation of establishment of T cell polarity / host cell endosome membrane / clathrin-dependent endocytosis of virus by host cell / viral protein processing / fusion of virus membrane with host plasma membrane / virus-mediated perturbation of host defense response / fusion of virus membrane with host endosome membrane / viral envelope ...positive regulation of plasma membrane raft polarization / positive regulation of receptor clustering / positive regulation of establishment of T cell polarity / host cell endosome membrane / clathrin-dependent endocytosis of virus by host cell / viral protein processing / fusion of virus membrane with host plasma membrane / virus-mediated perturbation of host defense response / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / apoptotic process / host cell plasma membrane / structural molecule activity / virion membrane / plasma membrane Similarity search - Function | |||||||||||||||
Biological species | Human immunodeficiency virus 1 / Homo sapiens (human) | |||||||||||||||
Method | single particle reconstruction / cryo EM / Resolution: 4.31 Å | |||||||||||||||
Authors | Henderson R / Acharya P | |||||||||||||||
Funding support | United States, 4 items
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Citation | Journal: To Be Published Title: Engineering immunogens that select for specific mutations in HIV broadly neutralizing antibodies Authors: Henderson R / Haynes BF | |||||||||||||||
History |
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-Structure visualization
Supplemental images |
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-Downloads & links
-EMDB archive
Map data | emd_43232.map.gz | 53 MB | EMDB map data format | |
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Header (meta data) | emd-43232-v30.xml emd-43232.xml | 16.9 KB 16.9 KB | Display Display | EMDB header |
Images | emd_43232.png | 62.3 KB | ||
Filedesc metadata | emd-43232.cif.gz | 6 KB | ||
Others | emd_43232_half_map_1.map.gz emd_43232_half_map_2.map.gz | 95.4 MB 95.4 MB | ||
Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-43232 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-43232 | HTTPS FTP |
-Validation report
Summary document | emd_43232_validation.pdf.gz | 758.2 KB | Display | EMDB validaton report |
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Full document | emd_43232_full_validation.pdf.gz | 757.8 KB | Display | |
Data in XML | emd_43232_validation.xml.gz | 13.5 KB | Display | |
Data in CIF | emd_43232_validation.cif.gz | 16 KB | Display | |
Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-43232 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-43232 | HTTPS FTP |
-Related structure data
Related structure data | 8vh2MC 8vgvC 8vgwC 8vh1C 8vh3C 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_43232.map.gz / Format: CCP4 / Size: 103 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: 1.08 Å | ||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #1
File | emd_43232_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #2
File | emd_43232_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Sample components
-Entire : Antibody Fab bound HIV-1 ectodomain
Entire | Name: Antibody Fab bound HIV-1 ectodomain |
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Components |
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-Supramolecule #1: Antibody Fab bound HIV-1 ectodomain
Supramolecule | Name: Antibody Fab bound HIV-1 ectodomain / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all |
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Source (natural) | Organism: Human immunodeficiency virus 1 |
-Macromolecule #1: CH505.M5.G458Y SOSIP gp120
Macromolecule | Name: CH505.M5.G458Y SOSIP gp120 / type: protein_or_peptide / ID: 1 / Number of copies: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: Human immunodeficiency virus 1 |
Molecular weight | Theoretical: 52.246586 KDa |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: AENLWVTVYY GVPVWKEAKT TLFCASDAKA YEKKVHNVWA THACVPTDPN PQEMVLKNVT ENFNMWKNDM VDQMHEDVIS LWDQSLKPC VKLTPLCVTL NCTNATASNS SIIEGMKNCS FNITTELRDK REKKNALFYK LDIVQLDGNS SQYRLINCNT S VITQACPK ...String: AENLWVTVYY GVPVWKEAKT TLFCASDAKA YEKKVHNVWA THACVPTDPN PQEMVLKNVT ENFNMWKNDM VDQMHEDVIS LWDQSLKPC VKLTPLCVTL NCTNATASNS SIIEGMKNCS FNITTELRDK REKKNALFYK LDIVQLDGNS SQYRLINCNT S VITQACPK VSFDPIPIHY CAPAGYAILK CNNKTFTGTG PCNNVSTVQC THGIKPVVST QLLLNGSLAE GEIIIRSENI TK NVKTIIV HLNESVKIEC TRPNNKTRTS IRIGPGQWFY ATGQVIGDIR EAYCNINESK WNETLQRVSK KLKEYFPHKN ITF QPSSGG DLEITTHSFN CGGEFFYCNT SSLFNRTYMA NSTDMANSTE TNSTRTITIH CRIKQIINMW QEVGRAMYAP PIAG NITCI SNITGLLLTR DYGKNNTETF RPGGGNMKDN WRSELYKYKV VKIEPLGVAP TRCKRRVVG UniProtKB: Envelope glycoprotein gp160 |
-Macromolecule #2: Envelope glycoprotein gp160
Macromolecule | Name: Envelope glycoprotein gp160 / type: protein_or_peptide / ID: 2 / Number of copies: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: Human immunodeficiency virus 1 |
Molecular weight | Theoretical: 18.089646 KDa |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: RRRRRRAVGI GAVFLGFLGA AGSTMGAASM TLTVQARNLL SGIVQQQSNL LRAPEAQQHL LKLTVWGIKQ LQARVLAVER YLRDQQLLG IWGCSGKLIC CTNVPWNSSW SNRNLSEIWD NMTWLQWDKE ISNYTQIIYG LLEESQNQQE KNEQDLLALD UniProtKB: Envelope glycoprotein gp160 |
-Macromolecule #3: CH235.12 Fab Heavy Chain
Macromolecule | Name: CH235.12 Fab Heavy Chain / type: protein_or_peptide / ID: 3 / Number of copies: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 24.319373 KDa |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: QVRLAQYGGG VKRLGATMTL SCVASGYTFN DYYIHWVRQA PGQGFELLGY IDPANGRPDY AGALRERLSF YRDKSMETLY MDLRSLRYD DTAMYYCVRN VGTAGSLLHY DHWGSGSPVI VSSASTKGPS VFPLAPSSKS TSGGTAALGC LVKDYFPEPV T VSWNSGAL ...String: QVRLAQYGGG VKRLGATMTL SCVASGYTFN DYYIHWVRQA PGQGFELLGY IDPANGRPDY AGALRERLSF YRDKSMETLY MDLRSLRYD DTAMYYCVRN VGTAGSLLHY DHWGSGSPVI VSSASTKGPS VFPLAPSSKS TSGGTAALGC LVKDYFPEPV T VSWNSGAL TSGVHTFPAV LQSSGLYSLS SVVTVPSSSL GTQTYICNVN HKPSNTKVDK RVEPKSC |
-Macromolecule #4: CH235.12 Fab Light Chain
Macromolecule | Name: CH235.12 Fab Light Chain / type: protein_or_peptide / ID: 4 / Number of copies: 3 / Enantiomer: LEVO |
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Source (natural) | Organism: Homo sapiens (human) |
Molecular weight | Theoretical: 23.450996 KDa |
Recombinant expression | Organism: Homo sapiens (human) |
Sequence | String: EIVLTQSPAT LSASPGERVT LTCRASRSVR NNVAWYQHKG GQSPRLLIYD ASTRAAGVPA RFSGSASGTE FTLAISNLES EDFTVYFCL QYNNWWTFGQ GTRVDIKRTV AAPSVFIFPP SDEQLKSGTA SVVCLLNNFY PREAKVQWKV DNALQSGNSQ E SVTEQDSK ...String: EIVLTQSPAT LSASPGERVT LTCRASRSVR NNVAWYQHKG GQSPRLLIYD ASTRAAGVPA RFSGSASGTE FTLAISNLES EDFTVYFCL QYNNWWTFGQ GTRVDIKRTV AAPSVFIFPP SDEQLKSGTA SVVCLLNNFY PREAKVQWKV DNALQSGNSQ E SVTEQDSK DSTYSLSSTL TLSKADYEKH KVYACEVTHQ GLSSPVTKSF NRGEC |
-Experimental details
-Structure determination
Method | cryo EM |
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Processing | single particle reconstruction |
Aggregation state | particle |
-Sample preparation
Buffer | pH: 7.1 |
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Vitrification | Cryogen name: ETHANE |
-Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 59.7 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: 3.4 µm / Nominal defocus min: 0.1 µm |
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
-Image processing
Startup model | Type of model: OTHER |
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Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 4.31 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 148858 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |