+Open data
-Basic information
Entry | Database: PDB / ID: 5m3v | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | BEAT Fc | |||||||||
Components |
| |||||||||
Keywords | IMMUNE SYSTEM / Antibody TCR Bispecific Interface | |||||||||
Function / homology | Function and homology information complement-dependent cytotoxicity / antibody-dependent cellular cytotoxicity / Fc-gamma receptor I complex binding / Classical antibody-mediated complement activation / IgG immunoglobulin complex / Initial triggering of complement / FCGR activation / Role of phospholipids in phagocytosis / immunoglobulin complex, circulating / immunoglobulin receptor binding ...complement-dependent cytotoxicity / antibody-dependent cellular cytotoxicity / Fc-gamma receptor I complex binding / Classical antibody-mediated complement activation / IgG immunoglobulin complex / Initial triggering of complement / FCGR activation / Role of phospholipids in phagocytosis / immunoglobulin complex, circulating / immunoglobulin receptor binding / complement activation, classical pathway / FCGR3A-mediated IL10 synthesis / antigen binding / Regulation of Complement cascade / FCGR3A-mediated phagocytosis / B cell receptor signaling pathway / Regulation of actin dynamics for phagocytic cup formation / antibacterial humoral response / Interleukin-4 and Interleukin-13 signaling / adaptive immune response / blood microparticle / extracellular space / extracellular exosome / extracellular region / plasma membrane Similarity search - Function | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.97 Å | |||||||||
Authors | Skegro, D. / Stutz, C. / Bourquin, F. / Blein, S. | |||||||||
Citation | Journal: J. Biol. Chem. / Year: 2017 Title: Immunoglobulin domain interface exchange as a platform technology for the generation of Fc heterodimers and bispecific antibodies. Authors: Skegro, D. / Stutz, C. / Ollier, R. / Svensson, E. / Wassmann, P. / Bourquin, F. / Monney, T. / Gn, S. / Blein, S. | |||||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 5m3v.cif.gz | 199.6 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb5m3v.ent.gz | 157.8 KB | Display | PDB format |
PDBx/mmJSON format | 5m3v.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/m3/5m3v ftp://data.pdbj.org/pub/pdb/validation_reports/m3/5m3v | HTTPS FTP |
---|
-Related structure data
Related structure data | 1h3tS S: Starting model for refinement |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-Components
#1: Protein | Mass: 26496.016 Da / Num. of mol.: 1 Mutation: S364K T366V K370T K392Y F405S Y407V K409W T411N,S364K T366V K370T K392Y F405S Y407V K409W T411N,S364K T366V K370T K392Y F405S Y407V K409W T411N,S364K T366V K370T K392Y F405S Y407V K409W T411N Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: IGHG1, IGHG3 / Production host: Homo sapiens (human) / References: UniProt: P01857, UniProt: P01860 | ||
---|---|---|---|
#2: Protein | Mass: 25508.832 Da / Num. of mol.: 1 Mutation: Q347E Y349A L351F S364T T366V K370T T394D V397L D399E F405A Y407S K409R T411R Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: IGHG1 / Production host: Homo sapiens (human) / References: UniProt: P01857 | ||
#3: Polysaccharide | Source method: isolated from a genetically manipulated source #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 2.49 Å3/Da / Density % sol: 50.69 % |
---|---|
Crystal grow | Temperature: 293.15 K / Method: vapor diffusion, hanging drop Details: CRYSTALS GROWN BY VAPOR DIFFUSION BY MIXING 10.2 MG/ML PROTEIN IN 10 MM TRIS-HCL PH8.0, 100 MM NACL, 1 MM EDTA, EQUALLY WITH 27.00 %(W/V) PEG 1500 |
-Data collection
Diffraction | Mean temperature: 93.15 K |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I04 / Wavelength: 0.9795 Å |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: May 17, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9795 Å / Relative weight: 1 |
Reflection | Resolution: 1.97→30 Å / Num. obs: 35360 / % possible obs: 99.2 % / Redundancy: 3.6 % / Rmerge(I) obs: 0.119 / Net I/σ(I): 5.2 |
Reflection shell | Resolution: 1.97→2.02 Å / Redundancy: 3.5 % / Rmerge(I) obs: 0.765 / Mean I/σ(I) obs: 1.3 / % possible all: 98.6 |
-Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1H3T Resolution: 1.97→30 Å / Cor.coef. Fo:Fc: 0.958 / Cor.coef. Fo:Fc free: 0.919 / SU B: 13.227 / SU ML: 0.188 / Cross valid method: THROUGHOUT / ESU R: 0.186 / ESU R Free: 0.186 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: BABINET MODEL WITH MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 56.556 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: 1 / Resolution: 1.97→30 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
|