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Open data
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Basic information
Entry | Database: PDB / ID: 1oaz | ||||||
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Title | IgE Fv SPE7 complexed with a recombinant thioredoxin | ||||||
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![]() | IMMUNE SYSTEM / ANTIBODY-COMPLEX / ANTIBODY / ALLERGY / IGE / CONFORMATIONAL DIVERSITY / MULTISPECFICITY / REDOX-ACTIVE CENTER / ELECTRON TRANSPORT | ||||||
Function / homology | ![]() positive regulation of DNA-directed DNA polymerase activity / immunoglobulin complex / DNA polymerase processivity factor activity / protein-disulfide reductase activity / cell redox homeostasis / adaptive immune response / oxidoreductase activity / immune response / extracellular space / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | James, L.C. / Roversi, P. / Tawfik, D. | ||||||
![]() | ![]() Title: Antibody Multispecificity Mediated by Conformational Diversity Authors: James, L.C. / Roversi, P. / Tawfik, D. | ||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 145.5 KB | Display | ![]() |
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PDB format | ![]() | 121.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1oaqC ![]() 1oarC ![]() 1oauC ![]() 1oaxC ![]() 1oayC ![]() 1ocwC ![]() 1anqS S: Starting model for refinement C: citing same article ( |
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Similar 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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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
NCS ensembles :
NCS oper:
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Components
#1: Protein | Mass: 13466.326 Da / Num. of mol.: 2 / Fragment: TRX-SHEAR3, RESIDUES 1-123 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Antibody | Mass: 13687.315 Da / Num. of mol.: 2 / Fragment: FV REGION, RESIDUES 1-122 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #3: Antibody | Mass: 11530.808 Da / Num. of mol.: 2 / Fragment: FV REGION, RESIDUES 1-110 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.5 Å3/Da / Density % sol: 70 % | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 5 Details: 21% PEG 8K, 0.1M NA CACODYLATE, 0.2M NA ACETATE PH5.5, pH 5.00 | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 6.5 / 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 | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Nov 15, 2000 / Details: MIRRORS |
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: 2.25→35.8 Å / Num. obs: 26942 / % possible obs: 99.6 % / Observed criterion σ(I): 2 / Redundancy: 13.7 % / Rmerge(I) obs: 0.067 |
Reflection shell | Rmerge(I) obs: 0.114 |
Reflection | *PLUS Highest resolution: 2.7 Å / Num. obs: 27717 / % possible obs: 99.2 % / Redundancy: 11 % / Rmerge(I) obs: 0.086 |
Reflection shell | *PLUS % possible obs: 95.3 % / Rmerge(I) obs: 0.375 / Mean I/σ(I) obs: 2.6 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1ANQ Resolution: 2.78→30.15 Å / Cor.coef. Fo:Fc: 0.931 / Cor.coef. Fo:Fc free: 0.879 / SU B: 12.85 / SU ML: 0.256 / Cross valid method: THROUGHOUT / ESU R Free: 0.363 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: BABINET MODEL PLUS MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 53.56 Å2
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Refinement step | Cycle: LAST / Resolution: 2.78→30.15 Å
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Refine LS restraints |
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