+Open data
-Basic information
Entry | Database: PDB / ID: 4qxg | ||||||
---|---|---|---|---|---|---|---|
Title | Antigen binding fragment of an anti IFNAR1 antibody | ||||||
Components |
| ||||||
Keywords | IMMUNE SYSTEM / IgV and IgC type folds / antigen binding / IFNAR1 / interferon alpha receptor 1 | ||||||
Function / homology | Immunoglobulins / Immunoglobulin-like / Sandwich / Mainly Beta / : / PHOSPHATE ION Function and homology information | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.3 Å | ||||||
Authors | Oganesyan, V.Y. / Dall'Acqua, W.F. | ||||||
Citation | Journal: MAbs / Year: 2015 Title: Molecular basis for antagonistic activity of anifrolumab, an anti-interferon-alpha receptor 1 antibody. Authors: Peng, L. / Oganesyan, V. / Wu, H. / Dall'Acqua, W.F. / Damschroder, M.M. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 4qxg.cif.gz | 94.1 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb4qxg.ent.gz | 75.2 KB | Display | PDB format |
PDBx/mmJSON format | 4qxg.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 4qxg_validation.pdf.gz | 457.7 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 4qxg_full_validation.pdf.gz | 462.9 KB | Display | |
Data in XML | 4qxg_validation.xml.gz | 18.8 KB | Display | |
Data in CIF | 4qxg_validation.cif.gz | 26.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/qx/4qxg ftp://data.pdbj.org/pub/pdb/validation_reports/qx/4qxg | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-Components
-Antibody , 2 types, 2 molecules HL
#1: Antibody | Mass: 23571.545 Da / Num. of mol.: 1 / Fragment: Fab, heavy chain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Homo sapiens (human) |
---|---|
#2: Antibody | Mass: 23445.965 Da / Num. of mol.: 1 / Fragment: Fab, light chain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Homo sapiens (human) |
-Non-polymers , 4 types, 192 molecules
#3: Chemical | ChemComp-K / |
---|---|
#4: Chemical | ChemComp-GOL / |
#5: Chemical | ChemComp-PO4 / |
#6: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 2.31 Å3/Da / Density % sol: 46.69 % |
---|---|
Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: 200 mM potassium di-hydrogen phosphate, 100 mM MES, pH 6.5 and 20% PEG 8000, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ROTATING ANODE / Type: RIGAKU MICROMAX-007 HF / Wavelength: 1.5418 Å |
Detector | Type: RIGAKU RAXIS IV++ / Detector: IMAGE PLATE / Date: Mar 10, 2007 |
Radiation | Monochromator: VariMax HF mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.17→48 Å / Num. all: 22461 / Num. obs: 21383 / % possible obs: 95.2 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Biso Wilson estimate: 27 Å2 |
-Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.3→48 Å / Cor.coef. Fo:Fc: 0.943 / Cor.coef. Fo:Fc free: 0.905 / SU B: 7.015 / SU ML: 0.171 / Cross valid method: THROUGHOUT / ESU R: 0.411 / ESU R Free: 0.257 / 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: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 24.44 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.3→48 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2.3→2.36 Å / Total num. of bins used: 20
|