+Open data
-Basic information
Entry | Database: PDB / ID: 4kq3 | |||||||||
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Title | Crystal structure of Anti-IL-17A antibody CNTO3186 | |||||||||
Components |
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Keywords | IMMUNE SYSTEM / immunoglobulin fold | |||||||||
Function / homology | Immunoglobulins / Immunoglobulin-like / Sandwich / Mainly Beta Function and homology information | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.92 Å | |||||||||
Authors | Teplyakov, A. / Obmolova, G. / Malia, T. / Gilliland, G.L. | |||||||||
Citation | Journal: Proteins / Year: 2014 Title: Structural evidence for a constrained conformation of short CDR-L3 in antibodies. Authors: Teplyakov, A. / Obmolova, G. / Malia, T.J. / Luo, J. / Gilliland, G.L. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4kq3.cif.gz | 99.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4kq3.ent.gz | 79.1 KB | Display | PDB format |
PDBx/mmJSON format | 4kq3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/kq/4kq3 ftp://data.pdbj.org/pub/pdb/validation_reports/kq/4kq3 | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
-Antibody , 2 types, 2 molecules LH
#1: Antibody | Mass: 23234.652 Da / Num. of mol.: 1 / Fragment: Fab Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Cell line (production host): HEK293E / Production host: Homo sapiens (human) |
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#2: Antibody | Mass: 24188.924 Da / Num. of mol.: 1 / Fragment: Fab Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Cell line (production host): HEK293E / Production host: Homo sapiens (human) |
-Non-polymers , 4 types, 344 molecules
#3: Chemical | #4: Chemical | ChemComp-MES / | #5: Chemical | ChemComp-EDO / | #6: 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: 2.12 Å3/Da / Density % sol: 42.03 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6.5 Details: 18% PEG3000, 0.2 M ammonium acetate, 0.1 M MES, pH 6.5, cryoprotectant: 20% PEG3000, 0.16 M ammonium acetate, 0.1 M MES, PH 6.5, 24% glycerol, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 95 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU MICROMAX-007 HF / Wavelength: 1.5418 / Wavelength: 1.5418 Å |
Detector | Type: RIGAKU SATURN 944 / Detector: CCD / Date: Nov 4, 2008 / Details: VARIMAX HF |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.92→30 Å / Num. all: 28013 / Num. obs: 28013 / % possible obs: 91.7 % / Observed criterion σ(F): 0 / Observed criterion σ(I): -3 / Redundancy: 4.9 % / Biso Wilson estimate: 27.2 Å2 / Rmerge(I) obs: 0.035 / Net I/σ(I): 32.8 |
Reflection shell | Resolution: 1.92→1.97 Å / Redundancy: 2.7 % / Rmerge(I) obs: 0.15 / Mean I/σ(I) obs: 6.6 / % possible all: 55 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.92→15 Å / Cor.coef. Fo:Fc: 0.96 / Cor.coef. Fo:Fc free: 0.938 / SU B: 3.472 / SU ML: 0.102 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.179 / ESU R Free: 0.16 / Stereochemistry target values: Engh & Huber
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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: BABINET MODEL WITH MASK | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 27 Å2
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Refinement step | Cycle: LAST / Resolution: 1.92→15 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.92→1.968 Å / Total num. of bins used: 20
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