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Yorodumi- PDB-2n4f: EC-NMR Structure of Arabidopsis thaliana At2g32350 Determined by ... -
+Open data
-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 | ||||||
Components | uncharacterized protein AR3433A | ||||||
Keywords | STRUCTURAL GENOMICS / UNKNOWN FUNCTION / alpha / beta / ubiquitin fold / EC-NMR / NORTHEAST STRUCTURAL GENOMICS CONSORTIUM / NESG / Protein Structure Initiative / PSI-Biology | ||||||
Function / homology | Function and homology information proteasome binding / polyubiquitin modification-dependent protein binding / ubiquitin binding / proteasome-mediated ubiquitin-dependent protein catabolic process / nucleoplasm / cytosol Similarity search - Function | ||||||
Biological species | Arabidopsis thaliana (thale cress) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Model details | lowest energy, model1 | ||||||
Authors | Tang, Y. / Huang, Y.J. / Hopf, T.A. / Sander, C. / Marks, D. / Montelione, G.T. / Northeast Structural Genomics Consortium (NESG) | ||||||
Citation | Journal: Nat.Methods / Year: 2015 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) |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2n4f.cif.gz | 537.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2n4f.ent.gz | 450.9 KB | Display | PDB format |
PDBx/mmJSON format | 2n4f.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/n4/2n4f ftp://data.pdbj.org/pub/pdb/validation_reports/n4/2n4f | HTTPS FTP |
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-Related structure data
Related structure data | 2n42C 2n44C 2n45C 2n46C 2n47C 2n48C 2n49C 2n4aC 2n4bC 2n4cC 2n4dC 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: 11005.522 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Arabidopsis thaliana (thale cress) / Gene: At2g32350 / Plasmid: pET 14-15C / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)+ Magic / References: UniProt: Q9ZV63, UniProt: F4ITP6*PLUS |
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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. |
-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 |