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Yorodumi- PDB-2mv0: Solution NMR Structure of Maltose-binding protein from Escherichi... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2mv0 | ||||||
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Title | Solution NMR Structure of Maltose-binding protein from Escherichia coli, Northeast Structural Genomics Consortium (NESG) Target ER690 | ||||||
Components | Maltose-binding periplasmic protein | ||||||
Keywords | PERIPLASMIC BINDING PROTEIN / Structural Genomics / NORTHEAST STRUCTURAL GENOMICS CONSORTIUM / NESG / PSI-Biology / Protein Structure Initiative | ||||||
Function / homology | Function and homology information detection of maltose stimulus / maltose transport complex / carbohydrate transport / carbohydrate transmembrane transporter activity / maltose binding / maltose transport / maltodextrin transmembrane transport / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / ATP-binding cassette (ABC) transporter complex / cell chemotaxis ...detection of maltose stimulus / maltose transport complex / carbohydrate transport / carbohydrate transmembrane transporter activity / maltose binding / maltose transport / maltodextrin transmembrane transport / ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing / 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 K-12 (bacteria) | ||||||
Method | SOLUTION NMR / simulated annealing, molecular dynamics | ||||||
Model details | lowest energy, model1 | ||||||
Authors | Rossi, P. / Lange, O.F. / Sgourakis, N.G. / Song, Y. / Lee, H. / Aramini, J.M. / Ertekin, A. / Xiao, R. / Acton, T.B. / Baker, D. ...Rossi, P. / Lange, O.F. / Sgourakis, N.G. / Song, Y. / Lee, H. / Aramini, J.M. / Ertekin, A. / Xiao, R. / Acton, T.B. / Baker, D. / Montelione, G.T. / Northeast Structural Genomics Consortium (NESG) | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 2012 Title: Determination of solution structures of proteins up to 40 kDa using CS-Rosetta with sparse NMR data from deuterated samples. Authors: Lange, O.F. / Rossi, P. / Sgourakis, N.G. / Song, Y. / Lee, H.W. / Aramini, J.M. / Ertekin, A. / Xiao, R. / Acton, T.B. / Montelione, G.T. / Baker, D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2mv0.cif.gz | 1.1 MB | Display | PDBx/mmCIF format |
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PDB format | pdb2mv0.ent.gz | 965.2 KB | Display | PDB format |
PDBx/mmJSON format | 2mv0.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2mv0_validation.pdf.gz | 471.3 KB | Display | wwPDB validaton report |
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Full document | 2mv0_full_validation.pdf.gz | 2.6 MB | Display | |
Data in XML | 2mv0_validation.xml.gz | 431.7 KB | Display | |
Data in CIF | 2mv0_validation.cif.gz | 285.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mv/2mv0 ftp://data.pdbj.org/pub/pdb/validation_reports/mv/2mv0 | HTTPS FTP |
-Related structure data
Related structure data | 2kw5C 2kznC 2lmdC 2lnuC 2lokC 2loyC C: citing same article (ref.) |
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Similar structure data | |
Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 40753.152 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli K-12 (bacteria) / Strain: K12 / Gene: b4034, JW3994, malE / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)pMgK / 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: 1.05 mM ER690.005, 90% H2O/10% D2O / Solvent system: 90% H2O/10% D2O |
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Sample conditions | pH: 7.2 / Pressure: ambient / Temperature: 310 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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