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Yorodumi- PDB-2n48: EC-NMR Structure of Escherichia coli YiaD Determined by Combining... -
+Open data
-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 | ||||||
Components | Probable lipoprotein YiaD | ||||||
Keywords | LIPID BINDING PROTEIN / EC-NMR / NORTHEAST STRUCTURAL GENOMICS CONSORTIUM / NESG / Protein Structure Initiative / PSI-Biology / Structural Genomics | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Escherichia coli K-12 (bacteria) | ||||||
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 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) |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2n48.cif.gz | 865 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2n48.ent.gz | 729.9 KB | Display | PDB format |
PDBx/mmJSON format | 2n48.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2n48_validation.pdf.gz | 499 KB | Display | wwPDB validaton report |
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Full document | 2n48_full_validation.pdf.gz | 1.1 MB | Display | |
Data in XML | 2n48_validation.xml.gz | 126 KB | Display | |
Data in CIF | 2n48_validation.cif.gz | 138.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/n4/2n48 ftp://data.pdbj.org/pub/pdb/validation_reports/n4/2n48 | HTTPS FTP |
-Related structure data
Related structure data | 2n42C 2n44C 2n45C 2n46C 2n47C 2n49C 2n4aC 2n4bC 2n4cC 2n4dC 2n4fC 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: 16055.984 Da / Num. of mol.: 1 / Fragment: C-terminal residues 59-199 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli K-12 (bacteria) / Strain: K12 / Gene: yiaD, b3552, JW5657 / Production host: Escherichia coli (E. coli) / References: UniProt: P37665 |
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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. |
-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 |