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Yorodumi- PDB-2h25: Solution Structure of Maltose Binding Protein complexed with beta... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2h25 | ||||||
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Title | Solution Structure of Maltose Binding Protein complexed with beta-cyclodextrin | ||||||
Components | Maltose-binding periplasmic protein | ||||||
Keywords | SUGAR BINDING PROTEIN / alpha/beta protein | ||||||
Function / homology | Function and homology information detection of maltose stimulus / maltose binding / maltose transport complex / maltose transport / maltodextrin transmembrane transport / carbohydrate transmembrane transporter activity / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / carbohydrate transport / ATP-binding cassette (ABC) transporter complex / cell chemotaxis ...detection of maltose stimulus / maltose binding / maltose transport complex / maltose transport / maltodextrin transmembrane transport / carbohydrate transmembrane transporter activity / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / carbohydrate transport / ATP-binding cassette (ABC) transporter complex / cell chemotaxis / outer membrane-bounded periplasmic space / periplasmic space / DNA damage response / membrane Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Xu, Y. / Lin, Z. / Zheng, Y. / Yang, D. | ||||||
Citation | Journal: Nat.Methods / Year: 2006 Title: A new strategy for structure determination of large proteins in solution without deuteration Authors: Xu, Y. / Zheng, Y. / Fan, J.S. / Yang, D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2h25.cif.gz | 1.1 MB | Display | PDBx/mmCIF format |
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PDB format | pdb2h25.ent.gz | 959.2 KB | Display | PDB format |
PDBx/mmJSON format | 2h25.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/h2/2h25 ftp://data.pdbj.org/pub/pdb/validation_reports/h2/2h25 | 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: 40741.098 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Production host: Escherichia coli (E. coli) / References: UniProt: P0AEX9 |
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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: 1.2mM MBP, PH 7; 10% D2O / Solvent system: 10% D2O |
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Sample conditions | Ionic strength: 20mM sodium phosphates / pH: 7 / Pressure: ambient / Temperature: 303 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | |||||||||
NMR representative | Selection criteria: lowest energy | |||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 40 / Conformers submitted total number: 10 |