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Yorodumi- PDB-2mgr: Structure of Plasmodium Yoelii Merozoite Surface Protein 1 - C-te... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2mgr | ||||||
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Title | Structure of Plasmodium Yoelii Merozoite Surface Protein 1 - C-terminal Domain, E28K mutant | ||||||
Components | Merozoite surface protein 1Merozoite surface protein | ||||||
Keywords | MEMBRANE PROTEIN | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Plasmodium yoelii yoelii (eukaryote) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | lowest energy, model1 | ||||||
Authors | Curd, R.D. / Birdsall, B. / Kadekoppala, M. / Ogun, S. / Kelly, G. / Holder, A.A. | ||||||
Citation | Journal: OPEN BIOLOGY / Year: 2014 Title: The structure of Plasmodium yoelii merozoite surface protein 119, antibody specificity and implications for malaria vaccine design Authors: Curd, R.D. / Birdsall, B. / Kadekoppala, M. / Ogun, S.A. / Kelly, G. / Holder, A.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2mgr.cif.gz | 550.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2mgr.ent.gz | 464.4 KB | Display | PDB format |
PDBx/mmJSON format | 2mgr.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mg/2mgr ftp://data.pdbj.org/pub/pdb/validation_reports/mg/2mgr | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 10729.788 Da / Num. of mol.: 1 / Fragment: C-terminal Domain, UNP residues 1656-1754 / Mutation: N25D, E28K Source method: isolated from a genetically manipulated source Source: (gene. exp.) Plasmodium yoelii yoelii (eukaryote) / Gene: MSP-1 / Production host: Komagataella pastoris (fungus) / References: UniProt: P13828 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 1 mM [U-99% 13C; U-99% 15N] MSP1_19-1, 25 mM potassium phosphate-2, 50 mM potassium chloride-3, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 75 / pH: 6.5 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: Standard SA protocol using ARIA with final water refinement | ||||||||||||||||||||||||
NMR constraints | NOE constraints total: 2004 / NOE intraresidue total count: 845 / NOE long range total count: 667 / NOE medium range total count: 179 / NOE sequential total count: 457 / Hydrogen bond constraints total count: 12 / Protein phi angle constraints total count: 53 / Protein psi angle constraints total count: 53 | ||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 / Representative conformer: 1 |