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Open data
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Basic information
Entry | Database: PDB / ID: 9mgb | ||||||
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Title | scFv antibody CL33 bound to R-phycoerythrin | ||||||
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![]() | IMMUNE SYSTEM / Phycoerythrin / antibody / scFv / immunity | ||||||
Function / homology | PHYCOERYTHROBILIN / PHYCOUROBILIN![]() | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.1 Å | ||||||
![]() | Rashleigh, L. / Gully, B.S. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Antibody-like recognition of a gamma delta T cell receptor toward a foreign antigen Authors: Rashleigh, L. / Venugopal, H. / Rice, M.T. / Gunasinghe, S.D. / Sok, C.L. / Gherardin, N.A. / Almeida, C.F. / Van Rhijn, I. / Moody, D.B. / Godfrey, D.I. / Rossjohn, J. / Gully, B.S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 639.2 KB | Display | ![]() |
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PDB format | ![]() | 538.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 3.4 MB | Display | ![]() |
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Full document | ![]() | 3.5 MB | Display | |
Data in XML | ![]() | 117.4 KB | Display | |
Data in CIF | ![]() | 163.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 48248MC ![]() 9mkoC ![]() 9o60C ![]() 9o61C ![]() 9o62C M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Components
#1: Protein | Mass: 17707.906 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() #2: Protein | Mass: 18398.875 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() #3: Antibody | Mass: 27609.285 Da / Num. of mol.: 6 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #4: Chemical | ChemComp-PEB / #5: Chemical | ChemComp-PUB / Has ligand of interest | Y | Has protein modification | Y | |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
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Sample preparation
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Molecular weight |
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Source (natural) |
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Source (recombinant) | Organism: ![]() ![]() | ||||||||||||||||||||||||
Buffer solution | pH: 8.5 | ||||||||||||||||||||||||
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||||||
Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
Experimental equipment | ![]() Model: Talos Arctica / Image courtesy: FEI Company |
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Microscopy | Model: FEI TALOS ARCTICA |
Electron gun | Electron source: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 800 nm |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: FEI FALCON III (4k x 4k) |
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Processing
EM software | Name: PHENIX / Version: 1.21.1_5286: / Category: model refinement | ||||||||||||||||||||||||
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CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
3D reconstruction | Resolution: 2.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 274000 / Symmetry type: POINT | ||||||||||||||||||||||||
Refine LS restraints |
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