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Yorodumi- PDB-2n49: EC-NMR Structure of Erwinia carotovora ECA1580 N-terminal Domain ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2n49 | ||||||
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Title | EC-NMR Structure of Erwinia carotovora ECA1580 N-terminal Domain Determined by Combining Evolutionary Couplings (EC) and Sparse NMR Data. Northeast Structural Genomics Consortium target EwR156A | ||||||
Components | Putative cold-shock protein | ||||||
Keywords | Structural Genomics / Unknown Function / cold shock protein / GFT NMR / NESGC / EC-NMR / OB fold / protein structure / PSI / Northeast Structural Genomics Consortium | ||||||
Function / homology | Function and homology information | ||||||
Biological species | Pectobacterium atrosepticum SCRI1043 (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 2N49 REFLECTS AN ALTERNATIVE MODELING OF THE ORIGINAL STRUCTURAL DATA IN 2K5N DETERMINED ...THIS ENTRY 2N49 REFLECTS AN ALTERNATIVE MODELING OF THE ORIGINAL STRUCTURAL DATA IN 2K5N DETERMINED BY AUTHORS: J.L.MILLS, A.ELETSKY, Q.ZHANG, D.LEE, M.JIANG, C.CICCOSANTI, R.XIAO, J.LUI, J.K.EVERETT, 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 | 2n49.cif.gz | 452 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2n49.ent.gz | 381.1 KB | Display | PDB format |
PDBx/mmJSON format | 2n49.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2n49_validation.pdf.gz | 530.2 KB | Display | wwPDB validaton report |
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Full document | 2n49_full_validation.pdf.gz | 863 KB | Display | |
Data in XML | 2n49_validation.xml.gz | 95.5 KB | Display | |
Data in CIF | 2n49_validation.cif.gz | 66.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/n4/2n49 ftp://data.pdbj.org/pub/pdb/validation_reports/n4/2n49 | HTTPS FTP |
-Related structure data
Related structure data | 2n42C 2n44C 2n45C 2n46C 2n47C 2n48C 2n4aC 2n4bC 2n4cC 2n4dC 2n4fC C: citing same article (ref.) |
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Similar structure data | |
Other databases |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 8417.549 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: 100% U-15N, 13C labeled sample Source: (gene. exp.) Pectobacterium atrosepticum SCRI1043 (bacteria) Strain: SCRI 1043 / ATCC BAA-672 / Gene: ECA1580 / Production host: Escherichia coli (E. coli) / References: UniProt: Q6D6V0 |
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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 2K5N. |
-Sample preparation
Sample | Conc.: 1.07 mM / Component: EwR156A-1 / Isotopic labeling: [U-100% 13C; U-100% 15N] |
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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 |