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- PDB-2kw5: Solution NMR Structure of the Slr1183 protein from Synechocystis ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2kw5 | ||||||
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Title | Solution NMR Structure of the Slr1183 protein from Synechocystis sp. PCC 6803, Northeast Structural Genomics Consortium Target SgR145 | ||||||
![]() | Slr1183 protein | ||||||
![]() | Structural Genomics / Unknown function / NORTHEAST STRUCTURAL GENOMICS CONSORTIUM (NESG) / PSI-2 / Protein Structure Initiative | ||||||
Function / homology | Methyltransferase domain 25 / Methyltransferase domain / Vaccinia Virus protein VP39 / transferase activity / S-adenosyl-L-methionine-dependent methyltransferase superfamily / Rossmann fold / 3-Layer(aba) Sandwich / Alpha Beta / Slr1183 protein![]() | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR | ||||||
Model details | lowest energy, model 1 | ||||||
![]() | Rossi, P. / Forouhar, F. / Lee, H. / Lange, O. / Mao, B. / Lemak, A. / Maglaqui, M. / Belote, R. / Ciccosanti, C. / Foote, E. ...Rossi, P. / Forouhar, F. / Lee, H. / Lange, O. / Mao, B. / Lemak, A. / Maglaqui, M. / Belote, R. / Ciccosanti, C. / Foote, E. / Sahdev, S. / Acton, T. / Xiao, R. / Everett, J. / Baker, D. / Montelione, G.T. / Northeast Structural Genomics Consortium (NESG) | ||||||
![]() | ![]() Title: Determination of solution structures of proteins up to 40 kDa using CS-Rosetta with sparse NMR data from deuterated samples. Authors: Lange, O.F. / Rossi, P. / Sgourakis, N.G. / Song, Y. / Lee, H.W. / Aramini, J.M. / Ertekin, A. / Xiao, R. / Acton, T.B. / Montelione, G.T. / Baker, D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1.2 MB | Display | ![]() |
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PDB format | ![]() | 1019.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 2kznC ![]() 2lmdC ![]() 2lnuC ![]() 2lokC ![]() 2loyC ![]() 2mv0C 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: 22403.258 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 experiment |
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Sample preparation
Details | Contents: 1.1 mM [U-100% 13C; U-100% 15N] SgR145, 95% H2O/5% D2O Solvent system: 95% H2O/5% D2O |
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Sample | Conc.: 1.1 mM / Component: SgR145-1 / Isotopic labeling: [U-100% 13C; U-100% 15N] |
Sample conditions | pH: 6.5 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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Processing
NMR software |
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NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |