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- PDB-2n48: EC-NMR Structure of Escherichia coli YiaD Determined by Combining... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2n48 | ||||||
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Title | EC-NMR Structure of Escherichia coli YiaD Determined by Combining Evolutionary Couplings (EC) and Sparse NMR Data. Northeast Structural Genomics Consortium target ER553 | ||||||
![]() | Probable lipoprotein YiaD | ||||||
![]() | LIPID BINDING PROTEIN / EC-NMR / NORTHEAST STRUCTURAL GENOMICS CONSORTIUM / NESG / Protein Structure Initiative / PSI-Biology / Structural Genomics | ||||||
Function / homology | ![]() | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Model details | lowest energy, model1 | ||||||
![]() | Tang, Y. / Huang, Y.J. / Hopf, T.A. / Sander, C. / Marks, D. / Montelione, G.T. / Northeast Structural Genomics Consortium (NESG) | ||||||
![]() | ![]() Title: Protein structure determination by combining sparse NMR data with evolutionary couplings. Authors: Tang, Y. / Huang, Y.J. / Hopf, T.A. / Sander, C. / Marks, D.S. / Montelione, G.T. | ||||||
History |
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Remark 0 | THIS ENTRY 2N48 REFLECTS AN ALTERNATIVE MODELING OF THE ORIGINAL STRUCTURAL DATA IN 2K1S DETERMINED ...THIS ENTRY 2N48 REFLECTS AN ALTERNATIVE MODELING OF THE ORIGINAL STRUCTURAL DATA IN 2K1S DETERMINED BY AUTHORS: T.A.RAMELOT,L.ZHAO,K.HAMILTON,M.MAGLAQUI,R.XIAO,J.LIU,M.C.BARAN,G.SWAPNA,T.B.ACTON,B.ROST,G.T.MONTELIONE,M.A.KENNEDY,NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 865 KB | Display | ![]() |
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PDB format | ![]() | 729.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 499 KB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 126 KB | Display | |
Data in CIF | ![]() | 138.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2n42C ![]() 2n44C ![]() 2n45C ![]() 2n46C ![]() 2n47C ![]() 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: 16055.984 Da / Num. of mol.: 1 / Fragment: C-terminal residues 59-199 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR Details: residues 59-199 of YiaD, lipoprotein, function unknown. Homolog of OmpA-like C-terminal domain. |
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NMR details | Text: AUTHOR USED THE EXPERIMENTAL DATA FROM ENTRY 2K1S. |
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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: lowest energy / Conformers calculated total number: 100 / Conformers submitted total number: 20 / Representative conformer: 1 |