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- PDB-2n4f: EC-NMR Structure of Arabidopsis thaliana At2g32350 Determined by ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2n4f | ||||||
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Title | EC-NMR Structure of Arabidopsis thaliana At2g32350 Determined by Combining Evolutionary Couplings (EC) and Sparse NMR Data. Northeast Structural Genomics Consortium target AR3433A | ||||||
![]() | uncharacterized protein AR3433A | ||||||
![]() | STRUCTURAL GENOMICS / UNKNOWN FUNCTION / alpha / beta / ubiquitin fold / EC-NMR / NORTHEAST STRUCTURAL GENOMICS CONSORTIUM / NESG / Protein Structure Initiative / PSI-Biology | ||||||
Function / homology | ![]() proteasome binding / polyubiquitin modification-dependent protein binding / ubiquitin binding / proteasome-mediated ubiquitin-dependent protein catabolic process / nucleoplasm / cytosol Similarity search - Function | ||||||
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 2N4F REFLECTS AN ALTERNATIVE MODELING OF THE ORIGINAL STRUCTURAL DATA IN 2KAN DETERMINED ...THIS ENTRY 2N4F REFLECTS AN ALTERNATIVE MODELING OF THE ORIGINAL STRUCTURAL DATA IN 2KAN DETERMINED BY AUTHORS: A.ELETSKY,J.L.MILLS,D.SUKUMARAN,J.HUA,R.SHASTRY,M.JIANG,C.CICCOSANTI,R.XIAO,J.LIU,J.K.EVERRET,G.V.T.SWAPNA,T.B.ACTON,B.ROST,G.T.MONTELIONE,T.SZYPERSKI,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 | ![]() | 537.9 KB | Display | ![]() |
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PDB format | ![]() | 450.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 494.4 KB | Display | ![]() |
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Full document | ![]() | 856 KB | Display | |
Data in XML | ![]() | 66 KB | Display | |
Data in CIF | ![]() | 75.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2n42C ![]() 2n44C ![]() 2n45C ![]() 2n46C ![]() 2n47C ![]() 2n48C ![]() 2n49C ![]() 2n4aC ![]() 2n4bC ![]() 2n4cC ![]() 2n4dC 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: 11005.522 Da / Num. of mol.: 1 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: AUTHOR USED THE EXPERIMENTAL DATA FROM ENTRY 2KAN. |
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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 |