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Yorodumi- PDB-1him: STRUCTURAL EVIDENCE FOR INDUCED FIT AS A MECHANISM FOR ANTIBODY-A... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1him | ||||||
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Title | STRUCTURAL EVIDENCE FOR INDUCED FIT AS A MECHANISM FOR ANTIBODY-ANTIGEN RECOGNITION | ||||||
Components |
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Keywords | IMMUNOGLOBULIN | ||||||
Function / homology | Function and homology information viral budding from plasma membrane / clathrin-dependent endocytosis of virus by host cell / membrane => GO:0016020 / host cell surface receptor binding / apical plasma membrane / fusion of virus membrane with host plasma membrane / fusion of virus membrane with host endosome membrane / viral envelope / virion attachment to host cell / host cell plasma membrane / virion membrane Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.9 Å | ||||||
Authors | Schulze-Gahmen, U. / Wilson, I.A. | ||||||
Citation | Journal: Science / Year: 1992 Title: Structural evidence for induced fit as a mechanism for antibody-antigen recognition. Authors: Rini, J.M. / Schulze-Gahmen, U. / Wilson, I.A. #1: Journal: J.Biol.Chem. / Year: 1988 Title: Preliminary Crystallographic Data, Primary Sequence, and Binding Data for an Anti-Peptide Fab and its Complex with a Synthetic Peptide from Influenza Virus Hemagglutinin Authors: Schulze-Gahmen, U. / Rini, J.M. / Arevalo, J. / Stura, E.A. / Kenten, J.H. / Wilson, I.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1him.cif.gz | 170.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1him.ent.gz | 141.1 KB | Display | PDB format |
PDBx/mmJSON format | 1him.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hi/1him ftp://data.pdbj.org/pub/pdb/validation_reports/hi/1him | HTTPS FTP |
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-Related 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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Atom site foot note | 1: RESIDUES PRO 8, PRO 95, AND PRO 141 OF LIGHT CHAINS AND RESIDUES PRO 149, PRO 151 AND PRO 200 OF HEAVY CHAINS ARE CIS PROLINES. |
-Components
#1: Antibody | Mass: 23911.369 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) #2: Antibody | Mass: 23677.441 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) #3: Protein/peptide | | Mass: 926.947 Da / Num. of mol.: 1 / Source method: obtained synthetically / References: UniProt: I6SHA6*PLUS #4: Protein/peptide | | Mass: 1040.105 Da / Num. of mol.: 1 / Source method: obtained synthetically / References: UniProt: I6SHA6*PLUS |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.95 Å3/Da / Density % sol: 58.34 % | ||||||||||||||||||||||||
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Crystal grow | *PLUS Method: vapor diffusion, hanging drop / Details: using macroseeding | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.9 Å / % possible obs: 87 % / Rmerge(I) obs: 0.12 |
-Processing
Software |
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Refinement | Resolution: 2.9→8 Å / Rfactor Rwork: 0.2 / Rfactor obs: 0.2 / σ(F): 2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.9→8 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.9 Å / Lowest resolution: 8 Å / σ(F): 2 / Rfactor obs: 0.2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 3.7 |