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Yorodumi- PDB-1ce1: 1.9A STRUCTURE OF THE THERAPEUTIC ANTIBODY CAMPATH-1H FAB IN COMP... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1ce1 | ||||||
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Title | 1.9A STRUCTURE OF THE THERAPEUTIC ANTIBODY CAMPATH-1H FAB IN COMPLEX WITH A SYNTHETIC PEPTIDE ANTIGEN | ||||||
Components |
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Keywords | IMMUNE SYSTEM / THERAPEUTIC / ANTIBODY / CD52 | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.9 Å | ||||||
Authors | James, L.C. / Hale, G. / Waldmann, H. / Bloomer, A.C. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1999 Title: 1.9 A structure of the therapeutic antibody CAMPATH-1H fab in complex with a synthetic peptide antigen. Authors: James, L.C. / Hale, G. / Waldmann, H. / Bloomer, A.C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ce1.cif.gz | 103.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ce1.ent.gz | 79.2 KB | Display | PDB format |
PDBx/mmJSON format | 1ce1.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ce/1ce1 ftp://data.pdbj.org/pub/pdb/validation_reports/ce/1ce1 | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Antibody | Mass: 23306.965 Da / Num. of mol.: 1 / Fragment: FAB Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: GenBank: 243868 |
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#2: Antibody | Mass: 23547.422 Da / Num. of mol.: 1 / Fragment: FAB Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / References: GenBank: 243866, UniProt: Q6PYX1*PLUS |
#3: Protein/peptide | Mass: 720.685 Da / Num. of mol.: 1 / Source method: obtained synthetically / Details: SYNTHETIC PEPTIDE; |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.67 Å3/Da / Density % sol: 53.97 % | |||||||||||||||
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Crystal grow | pH: 8.5 / Details: pH 8.5 | |||||||||||||||
Crystal grow | *PLUS Temperature: 23 ℃ / Method: vapor diffusion, hanging drop | |||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Wavelength: 1.5418 |
Detector | Date: Feb 1, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→40 Å / Num. obs: 40254 / % possible obs: 98.8 % / Redundancy: 3 % / Rmerge(I) obs: 0.054 |
Reflection shell | Highest resolution: 1.9 Å / Redundancy: 2.9 % / Rmerge(I) obs: 0.0269 / % possible all: 95.1 |
Reflection | *PLUS Rmerge(I) obs: 0.062 |
Reflection shell | *PLUS Highest resolution: 1.9 Å / Lowest resolution: 2 Å / % possible obs: 95.1 % / Rmerge(I) obs: 0.269 / Mean I/σ(I) obs: 3.2 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.9→6 Å / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 1.9→6 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 8 Å / Rfactor obs: 0.208 / Rfactor Rfree: 0.265 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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