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Yorodumi- PDB-6ch9: Crystal structure of a natively-glycosylated B41 SOSIP.664 HIV-1 ... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 6ch9 | ||||||||||||
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| Title | Crystal structure of a natively-glycosylated B41 SOSIP.664 HIV-1 Envelope Trimer in complex with the broadly-neutralizing antibodies BG18 and 35O22 | ||||||||||||
 Components | 
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 Keywords | IMMUNE SYSTEM / Env glycoprotein / broadly neutralizing antibodies | ||||||||||||
| Function / homology |  Function and homology informationpositive regulation of plasma membrane raft polarization / positive regulation of receptor clustering / host cell endosome membrane / clathrin-dependent endocytosis of virus by host cell / viral protein processing / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / host cell plasma membrane ...positive regulation of plasma membrane raft polarization / positive regulation of receptor clustering / host cell endosome membrane / clathrin-dependent endocytosis of virus by host cell / viral protein processing / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / host cell plasma membrane / virion membrane / structural molecule activity / membrane Similarity search - Function  | ||||||||||||
| Biological species | ![]()  Human immunodeficiency virus 1 Homo sapiens (human) | ||||||||||||
| Method |  X-RAY DIFFRACTION /  SYNCHROTRON /  MOLECULAR REPLACEMENT / Resolution: 4.85 Å  | ||||||||||||
 Authors | Barnes, C.O. / Bjorkman, P.J. | ||||||||||||
| Funding support |   United States, 3items 
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 Citation |  Journal: Nat Commun / Year: 2018Title: Structural characterization of a highly-potent V3-glycan broadly neutralizing antibody bound to natively-glycosylated HIV-1 envelope. Authors: Barnes, C.O. / Gristick, H.B. / Freund, N.T. / Escolano, A. / Lyubimov, A.Y. / Hartweger, H. / West, A.P. / Cohen, A.E. / Nussenzweig, M.C. / Bjorkman, P.J.  | ||||||||||||
| History | 
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Structure visualization
| Structure viewer | Molecule:  Molmil Jmol/JSmol | 
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Downloads & links
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Download
| PDBx/mmCIF format |  6ch9.cif.gz | 289.8 KB | Display |  PDBx/mmCIF format | 
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| PDB format |  pdb6ch9.ent.gz | 228.7 KB | Display |  PDB format | 
| PDBx/mmJSON format |  6ch9.json.gz | Tree view |  PDBx/mmJSON format | |
| Others |  Other downloads | 
-Validation report
| Summary document |  6ch9_validation.pdf.gz | 3.5 MB | Display |  wwPDB validaton report | 
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| Full document |  6ch9_full_validation.pdf.gz | 3.6 MB | Display | |
| Data in XML |  6ch9_validation.xml.gz | 61.7 KB | Display | |
| Data in CIF |  6ch9_validation.cif.gz | 81.9 KB | Display | |
| Arichive directory |  https://data.pdbj.org/pub/pdb/validation_reports/ch/6ch9 ftp://data.pdbj.org/pub/pdb/validation_reports/ch/6ch9 | HTTPS FTP  | 
-Related structure data
| Related structure data | ![]() 6ch7C ![]() 6ch8C ![]() 6chbC ![]() 4toyS ![]() 5t3zS ![]() 5ud9S S: Starting model for refinement C: citing same article (  | 
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| Similar structure data | 
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Links
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Assembly
| Deposited unit | ![]() 
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| 1 | ![]() 
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| Unit cell | 
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Components
-Envelope glycoprotein  ... , 2 types, 2 molecules BG 
| #1: Protein |   Mass: 17357.824 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]()  Human immunodeficiency virus 1 / Gene: env / Plasmid: pAM/C / Cell line (production host): K1 / Production host: ![]()  | 
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| #4: Protein |   Mass: 57929.727 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]()  Human immunodeficiency virus 1 / Gene: env / Plasmid: pAM/C / Cell line (production host): K1 / Production host: ![]()  | 
-Protein , 2 types, 2 molecules DQ 
| #2: Protein |   Mass: 26171.520 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.)  Homo sapiens (human) / Plasmid: pTT5 / Cell line (production host): HEK293-6E / Production host:  Homo sapiens (human) | 
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| #5: Protein |   Mass: 26020.229 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.)  Homo sapiens (human) / Production host:  Homo sapiens (human) | 
-Antibody , 2 types, 2 molecules ER 
| #3: Antibody |   Mass: 23318.824 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.)  Homo sapiens (human) / Plasmid: pTT5 / Cell line (production host): HEK293-6E / Production host:  Homo sapiens (human) | 
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| #6: Antibody |   Mass: 23021.447 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.)  Homo sapiens (human) / Production host:  Homo sapiens (human) | 
-Sugars , 8 types, 19 molecules 
| #7: Polysaccharide | beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source #8: Polysaccharide |  alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1- ...alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | Source method: isolated from a genetically manipulated source #9: Polysaccharide | Source method: isolated from a genetically manipulated source #10: Polysaccharide |  alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D- ...alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | Source method: isolated from a genetically manipulated source #11: Polysaccharide |  alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1- ...alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | Source method: isolated from a genetically manipulated source #12: Polysaccharide |  alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2- ...alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | Source method: isolated from a genetically manipulated source #13: Polysaccharide |  alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D- ...alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | Source method: isolated from a genetically manipulated source #14: Sugar | ChemComp-NAG /  | 
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-Details
| Has protein modification | Y | 
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-Experimental details
-Experiment
| Experiment | Method:  X-RAY DIFFRACTION / Number of used crystals: 1  | 
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Sample preparation
| Crystal | Density Matthews: 5.54 Å3/Da / Density % sol: 77.81 % / Mosaicity: 0.19 ° | 
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| Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 8 / Details: 5% Tacismate pH 8.0, 15% PEG 3350 | 
-Data collection
| Diffraction | Mean temperature: 100 K | 
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| Diffraction source | Source:  SYNCHROTRON / Site:  SSRL   / Beamline: BL12-2 / Wavelength: 1 Å | 
| Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Apr 26, 2017 | 
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | 
| Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 | 
| Reflection | Resolution: 4.85→39.9 Å / Num. obs: 18521 / % possible obs: 99.8 % / Redundancy: 9.9 % / Biso Wilson estimate: 283.59 Å2 / CC1/2: 0.996 / Rmerge(I) obs: 0.259 / Rpim(I) all: 0.086 / Rrim(I) all: 0.273 / Net I/σ(I): 5 / Num. measured all: 183962 / Scaling rejects: 310 | 
| Reflection shell | Resolution: 4.85→5.31 Å / Redundancy: 9.6 % / Rmerge(I) obs: 5.063 / Num. unique obs: 4397 / CC1/2: 0.347 / Rpim(I) all: 1.712 / Rrim(I) all: 5.351 / % possible all: 100 | 
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Processing
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| Refinement | Method to determine structure:  MOLECULAR REPLACEMENTStarting model: 5T3Z, 5UD9, 4TOY Resolution: 4.85→39.9 Å / Cor.coef. Fo:Fc: 0.884 / Cor.coef. Fo:Fc free: 0.875 / Cross valid method: THROUGHOUT / σ(F): 0 / SU Rfree Blow DPI: 1.146 
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| Displacement parameters | Biso  mean: 281.83 Å2
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| Refine analyze | Luzzati coordinate error obs: 1.06 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: 1  / Resolution: 4.85→39.9 Å
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| Refine LS restraints | 
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| LS refinement shell | Resolution: 4.85→5.14 Å / Total num. of bins used: 9 
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About Yorodumi




Human immunodeficiency virus 1
Homo sapiens (human)
X-RAY DIFFRACTION
United States, 3items 
Citation













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