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Yorodumi- PDB-2mpo: Structural basis of Toxoplasma gondii MIC2-Associated Protein int... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 2mpo | ||||||
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| Title | Structural basis of Toxoplasma gondii MIC2-Associated Protein interaction with MIC2 | ||||||
Components | MIC2-associated protein | ||||||
Keywords | CELL ADHESION / Toxoplasma gondii / Plasmodium / Microneme / Mic2 / M2AP | ||||||
| Function / homology | : / MIC2-associated protein, central beta-domain / MIC2-associated protein Function and homology information | ||||||
| Biological species | ![]() | ||||||
| Method | SOLUTION NMR / simulated annealing, distance geometry | ||||||
| Model details | lowest energy, model1 | ||||||
Authors | Liu, B. / Matthews, S. | ||||||
Citation | Journal: To Be PublishedTitle: Structural basis of Toxoplasma gondii MIC2-Associated Protein interaction with MIC2 Authors: Liu, B. / Huynh, M. / Henry, M. / Liew, L. / Matthews, S.J. / Carruthers, V.B. | ||||||
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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 | 2mpo.cif.gz | 63.6 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb2mpo.ent.gz | 46.4 KB | Display | PDB format |
| PDBx/mmJSON format | 2mpo.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 2mpo_validation.pdf.gz | 394.3 KB | Display | wwPDB validaton report |
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| Full document | 2mpo_full_validation.pdf.gz | 398.5 KB | Display | |
| Data in XML | 2mpo_validation.xml.gz | 7.5 KB | Display | |
| Data in CIF | 2mpo_validation.cif.gz | 9.6 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mp/2mpo ftp://data.pdbj.org/pub/pdb/validation_reports/mp/2mpo | HTTPS FTP |
-Related structure data
| Similar structure data | |
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| Other databases |
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Links
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Assembly
| Deposited unit | ![]()
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| NMR ensembles |
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Components
| #1: Protein | Mass: 19343.619 Da / Num. of mol.: 1 / Fragment: UNP RESIDUES 47-228 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||
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| NMR experiment |
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Sample preparation
| Details | Contents: 50 mM potassium phosphate-1, 100 mM sodium chloride-2, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | |||||||||
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| Sample conditions | Ionic strength: 0.1 / pH: 5.8 / Pressure: ambient / Temperature: 310 K |
-NMR measurement
| NMR spectrometer |
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Processing
| NMR software |
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| Refinement | Method: simulated annealing, distance geometry / Software ordinal: 1 | |||||||||
| NMR representative | Selection criteria: lowest energy | |||||||||
| NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 1 / Conformers submitted total number: 1 / Representative conformer: 1 |
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