+Open data
-Basic information
Entry | Database: PDB / ID: 3s7g | ||||||
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Title | Aglycosylated human igg1 fc fragment | ||||||
Components | Ig gamma-1 chain C region | ||||||
Keywords | IMMUNE SYSTEM / AGLYCOSYLATED / FC FRAGMENT / ANTIBODY / immunoglobulin | ||||||
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) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.13 Å | ||||||
Authors | Borrok, M.J. / Georgiou, G. | ||||||
Citation | Journal: To be Published Title: Structural Analysis of an Aglycosylated Fc Authors: Borrok, M.J. / Georgiou, G. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3s7g.cif.gz | 173.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3s7g.ent.gz | 138.8 KB | Display | PDB format |
PDBx/mmJSON format | 3s7g.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/s7/3s7g ftp://data.pdbj.org/pub/pdb/validation_reports/s7/3s7g | HTTPS FTP |
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-Related structure data
Related structure data | 3dnkS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
NCS ensembles :
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-Components
#1: Protein | Mass: 25580.955 Da / Num. of mol.: 4 / Fragment: CH2 and CH3 regions, UNP RESIDUES 104-330 Source method: isolated from a genetically manipulated source Details: FC PORTION OF IGG1 / Source: (gene. exp.) Homo sapiens (human) / Gene: IGHG1, IGHM / Plasmid: PTRC / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): DH10B / References: UniProt: P01857 #2: Water | ChemComp-HOH / | |
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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: 2.78 Å3/Da / Density % sol: 55.82 % |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, sitting drop / pH: 7 Details: 10% PEG 1000, 20% PEG 6000, 0.1M MAGNESIUM CHLORIDE, 0.2M TRIS, PH 7.0, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 295K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 5.0.2 / Wavelength: 1 |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Feb 25, 2010 |
Radiation | Monochromator: DOUBLE CRYSTAL SILICON 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 3.13→50 Å / Num. all: 19499 / Num. obs: 18883 / Observed criterion σ(I): 1 / Redundancy: 1.9 % / Biso Wilson estimate: 87.2 Å2 / Rmerge(I) obs: 0.061 / Net I/σ(I): 12.6 |
Reflection shell | Resolution: 3.13→3.26 Å / Redundancy: 1.9 % / Rmerge(I) obs: 0.347 / Mean I/σ(I) obs: 2.8 / % possible all: 97.1 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 3DNK (CH2 AND CH3 DOMAINS USED SEPARATELY) Resolution: 3.13→45 Å / Cor.coef. Fo:Fc: 0.911 / Cor.coef. Fo:Fc free: 0.879 / SU B: 35.961 / SU ML: 0.623 / Cross valid method: THROUGHOUT / ESU R Free: 0.632 / 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: 1.4 Å / Solvent model: MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 89.47 Å2
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Refinement step | Cycle: LAST / Resolution: 3.13→45 Å
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Refine LS restraints |
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Refine LS restraints NCS | Refine-ID: X-RAY DIFFRACTION
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