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- PDB-2n44: EC-NMR Structure of Escherichia coli Maltose-binding protein Dete... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2n44 | ||||||
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Title | EC-NMR Structure of Escherichia coli Maltose-binding protein Determined by Combining Evolutionary Couplings (EC) and Sparse NMR Data. Northeast Structural Genomics Consortium target ER690 | ||||||
![]() | Maltose-binding periplasmic protein | ||||||
![]() | PERIPLASMIC BINDING PROTEIN / EC-NMR / Structural Genomics / NORTHEAST STRUCTURAL GENOMICS CONSORTIUM / NESG / PSI-Biology / PROTEIN STRUCTURE INITIATIVE | ||||||
Function / homology | ![]() 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 | ![]() ![]() | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
![]() | Tang, Y. / Huang, Y.J. / Hopf, T.A. / Sander, C. / Marks, D. / Montelione, G.T. / Northeast Structural Genomics Consortium (NESG) | ||||||
![]() | ![]() 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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Remark 0 | THIS ENTRY 2N44 REFLECTS AN ALTERNATIVE MODELING OF THE ORIGINAL STRUCTURAL DATA IN PDB ENTRIES ...THIS ENTRY 2N44 REFLECTS AN ALTERNATIVE MODELING OF THE ORIGINAL STRUCTURAL DATA IN PDB ENTRIES 2MV0 AND 1EZP DETERMINED BY AUTHORS: P.ROSSI,O.F.LANGE,N.G.SGOURAKIS,Y.SONG,H.LEE,J.M.ARAMINI,A.ERTEKIN,R.XIAO,T.B.ACTON,D.BAKER,G.T.MONTELIONE,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) (PDB ENTRY 2MV0); G.A.MUELLER,W.Y.CHOY,D.YANG,J.D.FORMAN-KAY,R.A.VENTERS,L.E.KAY (PDB ENTRY 1EZP). |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 2.1 MB | Display | ![]() |
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PDB format | ![]() | 1.8 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 560.5 KB | Display | ![]() |
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Full document | ![]() | 3.2 MB | Display | |
Data in XML | ![]() | 803.9 KB | Display | |
Data in CIF | ![]() | 454.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2n42C ![]() 2n45C ![]() 2n46C ![]() 2n47C ![]() 2n48C ![]() 2n49C ![]() 2n4aC ![]() 2n4bC ![]() 2n4cC ![]() 2n4dC ![]() 2n4fC C: citing same article ( |
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Similar structure data | |
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: 40753.152 Da / Num. of mol.: 1 / Fragment: UNP residues 27-396 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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NMR details | Text: AUTHORS USED THE CS DATA AND THE NOESY PEAK LIST DATA FROM PDB ENTRY 2MV0, AND THE RDC DATA FROM PDB ENTRY 1EZP. |
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Sample preparation
Sample | Conc.: 1.05 mM / Component: MBP-1 |
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Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 Details: PROTONS FROM THE ROSETTA MODELS WERE REMOVED AND ADDED BACK USING REDUCE. | |||||||||||||||||||||
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 |