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Yorodumi- PDB-6w03: Crystal Structure of HIV-1 BG505 DS-SOSIP.3mut Prefusion Env Trim... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 6w03 | |||||||||
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| Title | Crystal Structure of HIV-1 BG505 DS-SOSIP.3mut Prefusion Env Trimer in Complex with Human Antibodies 3H109L and 35O22 at 3.3 Angstrom | |||||||||
Components |
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Keywords | VIRAL PROTEIN/IMMUNE SYSTEM / HIV-1 Envelope Prefusion Trimer / VIRAL PROTEIN / VIRAL PROTEIN-IMMUNE SYSTEM complex | |||||||||
| 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 / identical protein binding / membrane Similarity search - Function | |||||||||
| Biological species | ![]() Human immunodeficiency virus 1 Homo sapiens (human) | |||||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 Å | |||||||||
Authors | Lai, Y.-T. / Kwong, P.D. | |||||||||
Citation | Journal: J.Virol. / Year: 2020Title: Development of a 3Mut-Apex-Stabilized Envelope Trimer That Expands HIV-1 Neutralization Breadth When Used To Boost Fusion Peptide-Directed Vaccine-Elicited Responses. Authors: Chuang, G.Y. / Lai, Y.T. / Boyington, J.C. / Cheng, C. / Geng, H. / Narpala, S. / Rawi, R. / Schmidt, S.D. / Tsybovsky, Y. / Verardi, R. / Xu, K. / Yang, Y. / Zhang, B. / Chambers, M. / ...Authors: Chuang, G.Y. / Lai, Y.T. / Boyington, J.C. / Cheng, C. / Geng, H. / Narpala, S. / Rawi, R. / Schmidt, S.D. / Tsybovsky, Y. / Verardi, R. / Xu, K. / Yang, Y. / Zhang, B. / Chambers, M. / Changela, A. / Corrigan, A.R. / Kong, R. / Olia, A.S. / Ou, L. / Sarfo, E.K. / Wang, S. / Wu, W. / Doria-Rose, N.A. / McDermott, A.B. / Mascola, J.R. / Kwong, P.D. | |||||||||
| 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 | 6w03.cif.gz | 273.1 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb6w03.ent.gz | 215.8 KB | Display | PDB format |
| PDBx/mmJSON format | 6w03.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 6w03_validation.pdf.gz | 856.4 KB | Display | wwPDB validaton report |
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| Full document | 6w03_full_validation.pdf.gz | 863.7 KB | Display | |
| Data in XML | 6w03_validation.xml.gz | 3.6 KB | Display | |
| Data in CIF | 6w03_validation.cif.gz | 16 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/w0/6w03 ftp://data.pdbj.org/pub/pdb/validation_reports/w0/6w03 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 6vziC ![]() 6mtjS 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: 17146.482 Da / Num. of mol.: 1 / Fragment: ectodomain / Mutation: I559P, T605C Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Human immunodeficiency virus 1 / Gene: env / Production host: Homo sapiens (human) / References: UniProt: Q2N0S6 |
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| #4: Protein | Mass: 54098.480 Da / Num. of mol.: 1 Mutation: N137A, I201C, N302M, T320L, A329P, T332N, A433C, A501C Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Human immunodeficiency virus 1 / Gene: env / Production host: Homo sapiens (human) / References: UniProt: Q2N0S6 |
-Antibody , 4 types, 4 molecules DEHL
| #2: Antibody | Mass: 14663.281 Da / Num. of mol.: 1 / Mutation: E10T, L11T, K12T, A16S, I68N, K83T, F84S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Homo sapiens (human) |
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| #3: Antibody | Mass: 12358.635 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Homo sapiens (human) |
| #5: Antibody | Mass: 26255.498 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Homo sapiens (human) |
| #6: Antibody | Mass: 23416.145 Da / Num. of mol.: 1 / Mutation: E184M, S188M Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Homo sapiens (human) |
-Sugars , 7 types, 16 molecules 
| #7: 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 | ||||||||||
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| #8: Polysaccharide | 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 | 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 #10: 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 #11: Polysaccharide | alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)-[alpha-D-mannopyranose-(1-3)]beta-D- ...alpha-D-mannopyranose-(1-3)-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 #12: Polysaccharide | alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D- ...alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-2)-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 #13: Sugar | ChemComp-NAG / |
-Details
| Has ligand of interest | N |
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| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 5.31 Å3/Da / Density % sol: 76.84 % |
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| Crystal grow | Temperature: 298 K / Method: evaporation Details: 75 mM imidazole pH6.5, 150 mM LiSO4, 3.8% PEG MPD and 6.2% PEG 3,350 |
-Data collection
| Diffraction | Mean temperature: 100 K / Serial crystal experiment: N | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 1 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Detector | Type: RAYONIX MX300-HS / Detector: CCD / Date: Aug 4, 2017 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Reflection | Resolution: 2.37→50 Å / Num. obs: 50660 / % possible obs: 42.3 % / Redundancy: 3.3 % / Rmerge(I) obs: 0.149 / Rpim(I) all: 0.087 / Rrim(I) all: 0.174 / Χ2: 2.51 / Net I/σ(I): 5.8 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Reflection shell | Diffraction-ID: 1
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: 6MTJ Resolution: 2.4→39.8 Å / SU ML: 0.33 / Cross valid method: THROUGHOUT / σ(F): 1.99 / Phase error: 28.08
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| Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso max: 168.67 Å2 / Biso mean: 47.7622 Å2 / Biso min: 4.09 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: final / Resolution: 2.4→39.8 Å
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| LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 13
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Human immunodeficiency virus 1
Homo sapiens (human)
X-RAY DIFFRACTION
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