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- PDB-6uvo: Structure of antibody 3G12 bound to the central conserved domain ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6uvo | ||||||
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Title | Structure of antibody 3G12 bound to the central conserved domain of RSV G | ||||||
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![]() | VIRAL PROTEIN / IMMUNE SYSTEM / RSV / glycoprotein / G glycoprotein / viral attachment protein / antibody | ||||||
Function / homology | ![]() Translation of respiratory syncytial virus mRNAs / adhesion receptor-mediated virion attachment to host cell / RSV-host interactions / Assembly and release of respiratory syncytial virus (RSV) virions / Maturation of hRSV A proteins / Respiratory syncytial virus (RSV) attachment and entry / symbiont entry into host cell / virus-mediated perturbation of host defense response / host cell plasma membrane / virion membrane ...Translation of respiratory syncytial virus mRNAs / adhesion receptor-mediated virion attachment to host cell / RSV-host interactions / Assembly and release of respiratory syncytial virus (RSV) virions / Maturation of hRSV A proteins / Respiratory syncytial virus (RSV) attachment and entry / symbiont entry into host cell / virus-mediated perturbation of host defense response / host cell plasma membrane / virion membrane / extracellular region / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Fedechkin, S.O. / George, N.L. / Nunez Castrejon, A.M. / Dillen, J. / Kauvar, L.M. / DuBois, R.M. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Conformational Flexibility in Respiratory Syncytial Virus G Neutralizing Epitopes. Authors: Fedechkin, S.O. / George, N.L. / Nunez Castrejon, A.M. / Dillen, J.R. / Kauvar, L.M. / DuBois, R.M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 194.3 KB | Display | ![]() |
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PDB format | ![]() | 155.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 5k59S S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Antibody | Mass: 23218.771 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Antibody | Mass: 24838.816 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
#3: Protein/peptide | Mass: 5735.633 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Strain: A2 / Production host: ![]() ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 5.19 Å3/Da / Density % sol: 76.29 % |
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Crystal grow | Temperature: 277.15 K / Method: vapor diffusion / pH: 4.4 Details: 1.8M Ammonium Sulfate, 100mM sodium acetate trihydrate pH4.4 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N | |||||||||||||||||||||||||||
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Diffraction source | Source: ![]() ![]() ![]() | |||||||||||||||||||||||||||
Detector | Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Feb 24, 2018 / Details: Pilatus3 S, 25Hz, S/N 60-0134 | |||||||||||||||||||||||||||
Radiation | Monochromator: Si(111) Khozu / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 1.11503 Å / Relative weight: 1 | |||||||||||||||||||||||||||
Reflection | Resolution: 2.9→74.531 Å / Num. obs: 23682 / % possible obs: 99.5 % / Redundancy: 3.9 % / Biso Wilson estimate: 66.24 Å2 / CC1/2: 0.993 / Rmerge(I) obs: 0.109 / Rpim(I) all: 0.062 / Rrim(I) all: 0.126 / Net I/σ(I): 9.4 | |||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1 / Redundancy: 3.8 %
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 5K59 Resolution: 2.9→74.53 Å / SU ML: 0.32 / Cross valid method: THROUGHOUT / σ(F): 1.33 / Phase error: 20.56
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 190.21 Å2 / Biso mean: 63.3008 Å2 / Biso min: 27.71 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 2.9→74.53 Å
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Refine LS restraints |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0
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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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