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- PDB-1jfq: ANTIGEN-BINDING FRAGMENT OF THE MURINE ANTI-PHENYLARSONATE ANTIBO... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1jfq | ||||||
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Title | ANTIGEN-BINDING FRAGMENT OF THE MURINE ANTI-PHENYLARSONATE ANTIBODY 36-71, "FAB 36-71" | ||||||
![]() | (ANTIGEN-BINDING FRAGMENT OF ANTI-PHENYLARSONATE ANTIBODY) x 2 | ||||||
![]() | IMMUNE SYSTEM / immunoglobulin | ||||||
Function / homology | ![]() immunoglobulin production / positive regulation of B cell activation / phagocytosis, recognition / immunoglobulin complex / phagocytosis, engulfment / immunoglobulin complex, circulating / immunoglobulin receptor binding / complement activation, classical pathway / antigen binding / B cell receptor signaling pathway ...immunoglobulin production / positive regulation of B cell activation / phagocytosis, recognition / immunoglobulin complex / phagocytosis, engulfment / immunoglobulin complex, circulating / immunoglobulin receptor binding / complement activation, classical pathway / antigen binding / B cell receptor signaling pathway / adaptive immune response / defense response to bacterium / immune response / external side of plasma membrane / innate immune response / extracellular space Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Parhami-Seren, B. / Viswanathan, M. / Strong, R.K. / Margolies, M.N. | ||||||
![]() | ![]() Title: Structural analysis of mutants of high-affinity and low-affinity p-azophenylarsonate-specific antibodies generated by alanine scanning of heavy chain complementarity-determining region 2. Authors: Parhami-Seren, B. / Viswanathan, M. / Strong, R.K. / Margolies, M.N. | ||||||
History |
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Remark 999 | SEQUENCE The sequence database reference for the molecules in the this entry is not available |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 98.4 KB | Display | ![]() |
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PDB format | ![]() | 74.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 369.9 KB | Display | ![]() |
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Full document | ![]() | 378.2 KB | Display | |
Data in XML | ![]() | 10.3 KB | Display | |
Data in CIF | ![]() | 16 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6fabS S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Antibody | Mass: 23715.094 Da / Num. of mol.: 1 / Fragment: LIGHT CHAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Antibody | Mass: 23857.559 Da / Num. of mol.: 1 / Fragment: HEAVY CHAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.33 Å3/Da / Density % sol: 47.29 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: PEG 8000, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusionDetails: Rose, D.R., (1990) Proc.Natl.Acad.Sci.USA, 87, 338. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 298 K |
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Diffraction source | Source: ![]() |
Detector | Type: XUONG-HAMLIN MULTIWIRE / Detector: AREA DETECTOR |
Radiation | Monochromator: graphite / 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→50 Å / Num. obs: 28861 |
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Processing
Software |
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 6FAB Resolution: 1.9→6 Å / Isotropic thermal model: Isotropic / Cross valid method: not applied / σ(F): 2 / Stereochemistry target values: Engh & Huber /
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Refinement step | Cycle: LAST / Resolution: 1.9→6 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.9→1.98 Å /
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Software | *PLUS Name: ![]() | |||||||||||||||
Refinement | *PLUS Lowest resolution: 6 Å / σ(F): 2 | |||||||||||||||
Solvent computation | *PLUS | |||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rwork: 0.276 / Rfactor obs: 0.276 |