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- PDB-2n49: EC-NMR Structure of Erwinia carotovora ECA1580 N-terminal Domain ... -
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Open data
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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 | ||||||
![]() | Putative cold-shock protein | ||||||
![]() | Structural Genomics / Unknown Function / cold shock protein / GFT NMR / NESGC / EC-NMR / OB fold / protein structure / PSI / Northeast Structural Genomics Consortium | ||||||
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 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) |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 452 KB | Display | ![]() |
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PDB format | ![]() | 381.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 530.2 KB | Display | ![]() |
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Full document | ![]() | 863 KB | Display | |
Data in XML | ![]() | 95.5 KB | Display | |
Data in CIF | ![]() | 66.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2n42C ![]() 2n44C ![]() 2n45C ![]() 2n46C ![]() 2n47C ![]() 2n48C ![]() 2n4aC ![]() 2n4bC ![]() 2n4cC ![]() 2n4dC ![]() 2n4fC C: citing same article ( |
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Similar structure data | |
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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: 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.) ![]() Strain: SCRI 1043 / ATCC BAA-672 / Gene: ECA1580 / Production host: ![]() ![]() |
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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. |
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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 |