+Open data
-Basic information
Entry | Database: PDB / ID: 2q76 | ||||||
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Title | Mouse anti-hen egg white lysozyme antibody F10.6.6 Fab fragment | ||||||
Components |
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Keywords | IMMUNE SYSTEM / Antibody / Fab fragment / lysozyme / affinity maturation / VH-VL interface. | ||||||
Function / homology | Function and homology information IgG immunoglobulin complex / B cell differentiation / extracellular region / plasma membrane Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å | ||||||
Authors | Cauerhff, A. / Klinke, S. / Acierno, J.P. / Goldbaum, F.A. / Braden, B.C. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2007 Title: Affinity maturation increases the stability and plasticity of the Fv domain of anti-protein antibodies. Authors: Acierno, J.P. / Braden, B.C. / Klinke, S. / Goldbaum, F.A. / Cauerhff, A. #1: Journal: Proc.Natl.Acad.Sci.USA / Year: 2004 Title: Structural mechanism for affinity maturation of an anti-lysozyme antibody Authors: Cauerhff, A. / Goldbaum, F.A. / Braden, B.C. | ||||||
History |
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Remark 999 | sequence The sequences for Fab F10.6.6 fragment Light and heavy chains are not in the UNP database ...sequence The sequences for Fab F10.6.6 fragment Light and heavy chains are not in the UNP database at the time of processing. Author indicated the sequence references AF110316.3 GI:32456055 for VH, and AY277254.1 GI:33642144 for VL, respectively. Both sequences are identical to the sequences in the coordinates. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2q76.cif.gz | 181.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2q76.ent.gz | 144.9 KB | Display | PDB format |
PDBx/mmJSON format | 2q76.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/q7/2q76 ftp://data.pdbj.org/pub/pdb/validation_reports/q7/2q76 | HTTPS FTP |
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-Related structure data
Related structure data | 1p2cS S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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-Components
#1: Antibody | Mass: 23320.539 Da / Num. of mol.: 2 / Fragment: domain VL and CL / Source method: isolated from a natural source Details: The antibody was obtained from ascitic fluid generated by injecting monoclonal hybridoma cells. Source: (natural) Mus musculus (house mouse) / Strain: BALB/c / References: UniProt: P01837*PLUS #2: Antibody | Mass: 23198.896 Da / Num. of mol.: 2 / Fragment: domain VH and CH1 / Source method: isolated from a natural source Details: The antibody was obtained from ascitic fluid generated by injecting monoclonal hybridoma cells. Source: (natural) Mus musculus (house mouse) / Strain: BALB/c #3: 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: 2.14 Å3/Da / Density % sol: 42.63 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 4.7 Details: The F10.6.6 Fab fragment was crystallized in a mother liquor containing 24% (w/v) PEG 1000, 0.2 M CaCl2 and 0.1 M acetate buffer pH 4.7. Large prisms of about 0.30 mm x 0.05 mm x 0.05 mm ...Details: The F10.6.6 Fab fragment was crystallized in a mother liquor containing 24% (w/v) PEG 1000, 0.2 M CaCl2 and 0.1 M acetate buffer pH 4.7. Large prisms of about 0.30 mm x 0.05 mm x 0.05 mm were obtained after several weeks. VAPOR DIFFUSION, HANGING DROP, temperature 298K, pH 4.70 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: LNLS / Beamline: D03B-MX1 / Wavelength: 1.431 Å |
Detector | Type: MAR CCD 165 mm / Detector: CCD / Date: May 14, 2003 |
Radiation | Monochromator: SI SINGLE CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.431 Å / Relative weight: 1 |
Reflection | Resolution: 2→50 Å / Num. all: 50300 / Num. obs: 50300 / % possible obs: 96 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 8.1 % / Biso Wilson estimate: 19.3 Å2 / Rmerge(I) obs: 0.069 / Rsym value: 0.069 / Net I/σ(I): 9.8 |
Reflection shell | Resolution: 2→2.07 Å / Redundancy: 8.2 % / Rmerge(I) obs: 0.195 / Mean I/σ(I) obs: 3.3 / Num. unique all: 7122 / Rsym value: 0.195 / % possible all: 92 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: Fab fragment of PDB 1P2C Resolution: 2→50 Å / Cross valid method: THROUGHOUT / σ(F): 2 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 22 Å2 | |||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→50 Å
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Refine LS restraints |
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