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- PDB-2cwg: CRYSTALLOGRAPHIC REFINEMENT AND STRUCTURE ANALYSIS OF THE COMPLEX... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2cwg | |||||||||||||||
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Title | CRYSTALLOGRAPHIC REFINEMENT AND STRUCTURE ANALYSIS OF THE COMPLEX OF WHEAT GERM AGGLUTININ WITH A BIVALENT SIALOGLYCOPEPTIDE FROM GLYCOPHORIN A | |||||||||||||||
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![]() | LECTIN(AGGLUTININ) | |||||||||||||||
Function / homology | ![]() | |||||||||||||||
Biological species | ![]() ![]() | |||||||||||||||
Method | ![]() | |||||||||||||||
![]() | Wright, C.S. | |||||||||||||||
![]() | ![]() Title: Crystallographic refinement and structure analysis of the complex of wheat germ agglutinin with a bivalent sialoglycopeptide from glycophorin A. Authors: Wright, C.S. / Jaeger, J. #1: ![]() Title: Crystal Structure of a Wheat Germ Agglutinin/Glycophorin-Sialoglycopeptide Receptor Complex: Structural Basis for Cooperative Lectin-Cell Binding Authors: Wright, C.S. #2: ![]() Title: 2.2 Angstroms Resolution Structure Analysis of Two Refined N-Acetylneuraminyl-Lactose-Wheat Germ Agglutinin Isolectin Complexes Authors: Wright, C.S. #3: ![]() Title: Preliminary X-Ray Diffraction Results on Co-Crystals of Wheat Germ Agglutinin with a Sialoglycopeptide from the Red Cell Receptor Glycophorin A Authors: Wright, C.S. / Kahane, I. | |||||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 83 KB | Display | ![]() |
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PDB format | ![]() | 65.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1018.2 KB | Display | ![]() |
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Full document | ![]() | 1 MB | Display | |
Data in XML | ![]() | 23.6 KB | Display | |
Data in CIF | ![]() | 33.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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: Protein | Mass: 17124.080 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #2: Protein/peptide | Mass: 894.949 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source #3: Polysaccharide | Source method: isolated from a genetically manipulated source #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.46 Å3/Da / Density % sol: 49.99 % | ||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Method: vapor diffusion / PH range low: 5.5 / PH range high: 4.5 | ||||||||||||||||||||||||||||||||||||||||||
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 Å |
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Processing
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Refinement | Resolution: 2→10 Å / σ(F): 1 /
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Refinement step | Cycle: LAST / Resolution: 2→10 Å
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Refine LS restraints |
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Refinement | *PLUS Highest resolution: 2 Å / Lowest resolution: 10 Å / Num. reflection obs: 22330 / σ(F): 1 / Rfactor obs: 0.171 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 31.99 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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