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Open data
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Basic information
| Entry | Database: PDB / ID: 1r24 | ||||||
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| Title | FAB FROM MURINE IGG3 KAPPA | ||||||
Components |
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Keywords | IMMUNE SYSTEM / PRELIMINARY | ||||||
| Function / homology | Immunoglobulins / Immunoglobulin-like / Sandwich / Mainly Beta Function and homology information | ||||||
| Biological species | ![]() | ||||||
| Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 3.1 Å | ||||||
Authors | Evans, S.V. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 1999Title: The role of homophilic binding in anti-tumor antibody R24 recognition of molecular surfaces. Demonstration of an intermolecular beta-sheet interaction between vh domains. Authors: Kaminski, M.J. / MacKenzie, C.R. / Mooibroek, M.J. / Dahms, T.E. / Hirama, T. / Houghton, A.N. / Chapman, P.B. / Evans, S.V. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 1r24.cif.gz | 157.1 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1r24.ent.gz | 116.2 KB | Display | PDB format |
| PDBx/mmJSON format | 1r24.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 1r24_validation.pdf.gz | 450.8 KB | Display | wwPDB validaton report |
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| Full document | 1r24_full_validation.pdf.gz | 654 KB | Display | |
| Data in XML | 1r24_validation.xml.gz | 56 KB | Display | |
| Data in CIF | 1r24_validation.cif.gz | 72.8 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/r2/1r24 ftp://data.pdbj.org/pub/pdb/validation_reports/r2/1r24 | HTTPS FTP |
-Related structure data
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Links
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Assembly
| Deposited unit | ![]()
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| 1 |
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| 2 | ![]()
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| 3 | ![]()
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| Unit cell |
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Components
| #1: Antibody | Mass: 22827.256 Da / Num. of mol.: 2 / Fragment: FAB / Source method: isolated from a natural source / Details: FROM ASCITES / Source: (natural) ![]() #2: Antibody | Mass: 23068.889 Da / Num. of mol.: 2 / Fragment: FAB / Source method: isolated from a natural source / Details: FROM ASCITES / Source: (natural) ![]() Has protein modification | Y | |
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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: 4.57 Å3/Da / Density % sol: 73.06 % | ||||||||||||||||||||
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| Crystal grow | pH: 7 / Details: pH 7.0 | ||||||||||||||||||||
| Crystal grow | *PLUS Method: vapor diffusion, hanging drop | ||||||||||||||||||||
| Components of the solutions | *PLUS
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-Data collection
| Diffraction | Mean temperature: 270 K |
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| Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU300 / Wavelength: 1.5418 |
| Detector | Type: MAR scanner 300 mm plate / Detector: IMAGE PLATE |
| Radiation | Monochromator: NI FILTER / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
| Reflection | Resolution: 3.1→6 Å / Num. obs: 26595 / % possible obs: 92 % / Observed criterion σ(I): 0 / Redundancy: 2.2 % / Biso Wilson estimate: 35.3 Å2 / Rsym value: 0.075 |
| Reflection | *PLUS Num. measured all: 58762 / Rmerge(I) obs: 0.075 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: FAB FROM YST9.1 Resolution: 3.1→6 Å / σ(F): 0
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| Displacement parameters | Biso mean: 28.4 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 3.1→6 Å
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| Refine LS restraints |
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| Xplor file | Serial no: 1 / Param file: PARAM19X.PRO / Topol file: TOPH19X.PRO | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement | *PLUS Highest resolution: 3.1 Å / Lowest resolution: 6 Å / σ(F): 0 / Rfactor Rfree: 0.334 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | *PLUS Biso mean: 28.4 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refine LS restraints | *PLUS Type: x_angle_deg / Dev ideal: 3.8 |
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