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Yorodumi- PDB-6nm6: Crystal Structure of HIV-1 BG505 SOSIP.664 Prefusion Env Trimer B... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 6nm6 | |||||||||
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| Title | Crystal Structure of HIV-1 BG505 SOSIP.664 Prefusion Env Trimer Bound to N6 FR3-03 scFv in Complex with Crystallization Chaperones 3H109L Fab and 35O22 scFv at 3.2 Angstrom | |||||||||
Components |
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Keywords | IMMUNE SYSTEM / HIV-1 Envelope Prefusion Trimer / CD4-binding site antibodies / chimeric 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 / identical protein binding / membrane Similarity search - Function | |||||||||
| Biological species | ![]() Human immunodeficiency virus 1 Homo sapiens (human) | |||||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.739 Å | |||||||||
Authors | Lai, Y.-T. / Kwong, P.D. | |||||||||
Citation | Journal: Nat Commun / Year: 2019Title: Improvement of antibody functionality by structure-guided paratope engraftment. Authors: Liu, Q. / Lai, Y.T. / Zhang, P. / Louder, M.K. / Pegu, A. / Rawi, R. / Asokan, M. / Chen, X. / Shen, C.H. / Chuang, G.Y. / Yang, E.S. / Miao, H. / Wang, Y. / Fauci, A.S. / Kwong, P.D. / Mascola, J.R. / Lusso, P. | |||||||||
| 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 | 6nm6.cif.gz | 322.7 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb6nm6.ent.gz | 253 KB | Display | PDB format |
| PDBx/mmJSON format | 6nm6.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 6nm6_validation.pdf.gz | 1.3 MB | Display | wwPDB validaton report |
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| Full document | 6nm6_full_validation.pdf.gz | 1.4 MB | Display | |
| Data in XML | 6nm6_validation.xml.gz | 61.1 KB | Display | |
| Data in CIF | 6nm6_validation.cif.gz | 78.2 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/nm/6nm6 ftp://data.pdbj.org/pub/pdb/validation_reports/nm/6nm6 | HTTPS FTP |
-Related 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: 54021.250 Da / Num. of mol.: 1 / Mutation: N137A, T332N, 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 , 6 types, 6 molecules DEHLUV
| #2: Antibody | Mass: 15837.336 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: 14188.641 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) |
| #7: Antibody | Mass: 16140.978 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Homo sapiens (human) |
| #8: Antibody | Mass: 12578.760 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 , 6 types, 18 molecules 
| #9: 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 | ||||||||
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| #10: 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 #11: 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 #12: 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 #13: 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 #14: Sugar | ChemComp-NAG / |
-Non-polymers , 1 types, 1 molecules 
| #15: Water | ChemComp-HOH / |
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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: 4.17 Å3/Da / Density % sol: 70.53 % |
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| Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop Details: 60 mM acetate pH 4.5, 420 mM sodium formate, 5% PEG 3,350 and 60 mM CaCl2 |
-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: Oct 20, 2017 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Reflection | Resolution: 2.7→50 Å / Num. obs: 43397 / % possible obs: 54.2 % / Redundancy: 2.9 % / Biso Wilson estimate: 33.77 Å2 / Rmerge(I) obs: 0.061 / Rpim(I) all: 0.042 / Rrim(I) all: 0.074 / Χ2: 0.721 / Net I/σ(I): 8.7 / Num. measured all: 123992 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Reflection shell | Diffraction-ID: 1
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Processing
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| Refinement | Resolution: 2.739→37.02 Å / SU ML: 0.43 / Cross valid method: THROUGHOUT / σ(F): 1.98 / Phase error: 29.44 Details: After data was collected and processed, UCLA anisotropy server was used to perform elliptical truncation to determine the diffraction limits along three principle directions. To account for ...Details: After data was collected and processed, UCLA anisotropy server was used to perform elliptical truncation to determine the diffraction limits along three principle directions. To account for the low completeness due to the high anisotropy, authors calculated an "effective resolution" by the following formula: Effective resolution = highest resolution / (overall completeness)^(1/3) Note: highest resolution was determined by UCLA anisotropy server.
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| Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso max: 165.27 Å2 / Biso mean: 57.1458 Å2 / Biso min: 4.98 Å2 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: final / Resolution: 2.739→37.02 Å
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| LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 12
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Human immunodeficiency virus 1
Homo sapiens (human)
X-RAY DIFFRACTION
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