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- PDB-5n0a: Crystal structure of A259C covalently linked dengue 2 virus envel... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5n0a | |||||||||
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Title | Crystal structure of A259C covalently linked dengue 2 virus envelope glycoprotein dimer in complex with the Fab fragment of the broadly neutralizing human antibody EDE2 A11 | |||||||||
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![]() | Immune System/Viral protein / IMMUNE SYSTEM-VIRAL PROTEIN COMPLEX / DENGUE VIRUS / ENVELOPE FUSION PROTEIN / BROADLY NEUTRALIZING ANTIBODY | |||||||||
Function / homology | ![]() symbiont-mediated suppression of host JAK-STAT cascade via inhibition of host TYK2 activity / host cell mitochondrion / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity / ribonucleoside triphosphate phosphatase activity / double-stranded RNA binding / viral capsid / protein complex oligomerization / monoatomic ion channel activity / clathrin-dependent endocytosis of virus by host cell ...symbiont-mediated suppression of host JAK-STAT cascade via inhibition of host TYK2 activity / host cell mitochondrion / symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT2 activity / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity / ribonucleoside triphosphate phosphatase activity / double-stranded RNA binding / viral capsid / protein complex oligomerization / monoatomic ion channel activity / clathrin-dependent endocytosis of virus by host cell / mRNA (nucleoside-2'-O-)-methyltransferase activity / mRNA 5'-cap (guanine-N7-)-methyltransferase activity / RNA helicase activity / host cell endoplasmic reticulum membrane / protein dimerization activity / symbiont-mediated suppression of host type I interferon-mediated signaling pathway / induction by virus of host autophagy / viral RNA genome replication / serine-type endopeptidase activity / RNA-dependent RNA polymerase activity / virus-mediated perturbation of host defense response / fusion of virus membrane with host endosome membrane / viral envelope / host cell nucleus / virion attachment to host cell / structural molecule activity / virion membrane / proteolysis / extracellular region / ATP binding / membrane / metal ion binding Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Vaney, M.C. / Rouvinski, A. / Guardado-Calvo, P. / Sharma, A. / Rey, F.A. | |||||||||
![]() | ![]() Title: Covalently linked dengue virus envelope glycoprotein dimers reduce exposure of the immunodominant fusion loop epitope. Authors: Rouvinski, A. / Dejnirattisai, W. / Guardado-Calvo, P. / Vaney, M.C. / Sharma, A. / Duquerroy, S. / Supasa, P. / Wongwiwat, W. / Haouz, A. / Barba-Spaeth, G. / Mongkolsapaya, J. / Rey, F.A. / Screaton, G.R. #1: ![]() Title: Recognition determinants of broadly neutralizing human antibodies against dengue viruses. Authors: Rouvinski, A. / Guardado-Calvo, P. / Barba-Spaeth, G. / Duquerroy, S. / Vaney, M.C. / Kikuti, C.M. / Navarro Sanchez, M.E. / Dejnirattisai, W. / Wongwiwat, W. / Haouz, A. / Girard-Blanc, C. ...Authors: Rouvinski, A. / Guardado-Calvo, P. / Barba-Spaeth, G. / Duquerroy, S. / Vaney, M.C. / Kikuti, C.M. / Navarro Sanchez, M.E. / Dejnirattisai, W. / Wongwiwat, W. / Haouz, A. / Girard-Blanc, C. / Petres, S. / Shepard, W.E. / Despres, P. / Arenzana-Seisdedos, F. / Dussart, P. / Mongkolsapaya, J. / Screaton, G.R. / Rey, F.A. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 515.9 KB | Display | ![]() |
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PDB format | ![]() | 424.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 45.9 KB | Display | |
Data in CIF | ![]() | 62.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5n09C ![]() 4ut7S ![]() 4utaS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 47477.172 Da / Num. of mol.: 2 / Mutation: A259C Source method: isolated from a genetically manipulated source Details: The SOLUBLE ECTODOMAIN of envelope glycoprotein E is mutated at position 259: Ala is replaced by Cys. Source: (gene. exp.) ![]() ![]() ![]() #2: Antibody | Mass: 30355.521 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: FAB FRAGMENT HEAVY CHAIN, RESIDUES 1-263. The residues numbering is the KABAT scheme numbering. Source: (gene. exp.) ![]() ![]() ![]() #3: Antibody | Mass: 23107.664 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: FAB FRAGMENT LIGHT CHAIN, RESIDUES 1-213. The residues numbering is the KABAT scheme numbering. Source: (gene. exp.) ![]() ![]() ![]() #4: Polysaccharide | Source method: isolated from a genetically manipulated source |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.77 Å3/Da / Density % sol: 55.59 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 100mM Hepes pH 7.5, 19% PEG 6K, 1.5% (v/v) 2-methyl-2,4-pentanediol |
-Data collection
Diffraction | Mean temperature: 173 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS EIGER X 9M / Detector: PIXEL / Date: Mar 12, 2015 |
Radiation | Monochromator: cryogenically cooled channel-cut Si[111] monochromator Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.984 Å / Relative weight: 1 |
Reflection | Resolution: 3.9→50 Å / Num. obs: 19112 / % possible obs: 96.9 % / Redundancy: 3.8 % / Biso Wilson estimate: 44.52 Å2 / Rmerge(I) obs: 0.316 / Rpim(I) all: 0.257 / Rrim(I) all: 0.41 / Rsym value: 0.316 / Net I/σ(I): 3.1 |
Reflection shell | Resolution: 3.9→4.1 Å / Redundancy: 3.8 % / Rmerge(I) obs: 0.8 / Mean I/σ(I) obs: 1.4 / Num. unique obs: 4789 / CC1/2: 0.68 / Rpim(I) all: 0.67 / % possible all: 97.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 4UTA;4UT7 Resolution: 3.9→20 Å / Cor.coef. Fo:Fc: 0.7623 / Cor.coef. Fo:Fc free: 0.7118 / Cross valid method: THROUGHOUT / σ(F): 0 / SU Rfree Blow DPI: 0.85 Details: BUSTER/TNT refinement was used with TLS and NCS resraints
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Displacement parameters | Biso mean: 145.06 Å2
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Refine analyze | Luzzati coordinate error obs: 0.858 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: 1 / Resolution: 3.9→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 3.9→4.11 Å / Total num. of bins used: 10
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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