+Open data
-Basic information
Entry | Database: PDB / ID: 5dj0 | |||||||||
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Title | Fc Heterodimer Design 11.2 Y349S/K370Y + E357D/S364Q | |||||||||
Components |
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Keywords | IMMUNE SYSTEM / Heterodimer / Immunoglobulin / CH3 / Fc / Bispecific Antibody | |||||||||
Function / homology | Function and homology information complement-dependent cytotoxicity / antibody-dependent cellular cytotoxicity / Fc-gamma receptor I complex binding / Classical antibody-mediated complement activation / Initial triggering of complement / immunoglobulin complex, circulating / IgG immunoglobulin complex / immunoglobulin receptor binding / FCGR activation / Role of phospholipids in phagocytosis ...complement-dependent cytotoxicity / antibody-dependent cellular cytotoxicity / Fc-gamma receptor I complex binding / Classical antibody-mediated complement activation / Initial triggering of complement / immunoglobulin complex, circulating / IgG immunoglobulin complex / immunoglobulin receptor binding / FCGR activation / Role of phospholipids in phagocytosis / complement activation, classical pathway / antigen binding / FCGR3A-mediated IL10 synthesis / Regulation of Complement cascade / FCGR3A-mediated phagocytosis / B cell receptor signaling pathway / Regulation of actin dynamics for phagocytic cup formation / antibacterial humoral response / blood microparticle / Interleukin-4 and Interleukin-13 signaling / adaptive immune response / extracellular space / extracellular exosome / extracellular region / plasma membrane Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) synthetic construct (others) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.28 Å | |||||||||
Model details | Design XXX | |||||||||
Authors | Atwell, S. / Leaver-Fay, A. / Froning, K.J. / Aldaz, H. / Pustilnik, A. / Lu, F. / Huang, F. / Yuan, R. / Dhanani, S.H. / Chamberlain, A.K. ...Atwell, S. / Leaver-Fay, A. / Froning, K.J. / Aldaz, H. / Pustilnik, A. / Lu, F. / Huang, F. / Yuan, R. / Dhanani, S.H. / Chamberlain, A.K. / Fitchett, J.R. / Gutierrez, B. / Hendle, J. / Demarest, S.J. / Kuhlman, B. | |||||||||
Citation | Journal: Structure / Year: 2016 Title: Computationally Designed Bispecific Antibodies using Negative State Repertoires. Authors: Leaver-Fay, A. / Froning, K.J. / Atwell, S. / Aldaz, H. / Pustilnik, A. / Lu, F. / Huang, F. / Yuan, R. / Hassanali, S. / Chamberlain, A.K. / Fitchett, J.R. / Demarest, S.J. / Kuhlman, B. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5dj0.cif.gz | 106.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5dj0.ent.gz | 81.9 KB | Display | PDB format |
PDBx/mmJSON format | 5dj0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/dj/5dj0 ftp://data.pdbj.org/pub/pdb/validation_reports/dj/5dj0 | HTTPS FTP |
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-Related structure data
Related structure data | 5di8C 5dj2C 5dj6C 5dj8C 5djaC 5djcC 5djdC 5djxC 5djyC 5djzC 5dk0C 5dk2C 5dvkC 5dvlC 5dvmC 5dvnC 5dvoC C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 25570.916 Da / Num. of mol.: 1 / Fragment: UNP residues 104-330 / Mutation: Y349S, K370Y Source method: isolated from a genetically manipulated source Details: transient expression / Source: (gene. exp.) Homo sapiens (human) / Gene: IGHG1 / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: P01857 | ||
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#2: Protein | Mass: 27009.330 Da / Num. of mol.: 1 / Fragment: UNP residues 104-330 / Mutation: E357D, S364Q Source method: isolated from a genetically manipulated source Details: transient expression / Source: (gene. exp.) Homo sapiens (human) / Gene: IGHG1 / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: P01857 | ||
#3: Protein/peptide | Mass: 1533.749 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: CPC Scientific Inc., Sunnyvale CA / Source: (synth.) synthetic construct (others) | ||
#4: Polysaccharide | Source method: isolated from a genetically manipulated source #5: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.85 Å3/Da / Density % sol: 56.8 % |
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Crystal grow | Temperature: 294 K / Method: vapor diffusion / Details: 13% PEG 3350 + 200mM Magnesium Formate dihydrate |
-Data collection
Diffraction | Mean temperature: 193 K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: SYNCHROTRON / Site: CLSI / Beamline: 08B1-1 / Wavelength: 0.97949 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: MARMOSAIC 300 mm CCD / Detector: CCD / Date: Oct 18, 2013 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.97949 Å / Relative weight: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 2.28→30 Å / Num. obs: 27745 / % possible obs: 99.6 % / Redundancy: 3.7 % / Rpim(I) all: 0.05 / Rrim(I) all: 0.097 / Rsym value: 0.07 / Net I/av σ(I): 9.512 / Net I/σ(I): 11.1 / Num. measured all: 103367 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell | Diffraction-ID: 1 / Rejects: 0
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-Processing
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.28→30 Å / Cor.coef. Fo:Fc: 0.951 / Cor.coef. Fo:Fc free: 0.922 / SU B: 7.05 / SU ML: 0.167 / Cross valid method: THROUGHOUT / ESU R: 0.256 / ESU R Free: 0.219 / Stereochemistry target values: MAXIMUM LIKELIHOOD
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 35.83 Å2
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Refinement step | Cycle: LAST / Resolution: 2.28→30 Å
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Refine LS restraints |
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