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Open data
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Basic information
Entry | Database: PDB / ID: 1ev0 | ||||||
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Title | SOLUTION STRUCTURE OF THE MINE TOPOLOGICAL SPECIFICITY DOMAIN | ||||||
![]() | MINE | ||||||
![]() | CELL CYCLE / MinE / topological specificity / cell division / MinCD / minicell | ||||||
Function / homology | ![]() division septum site selection / regulation of division septum assembly / regulation of cell division / identical protein binding / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / torsion angle dynamics, dynamical simulated annealing | ||||||
![]() | King, G.F. / Maciejewski, M.W. / Pan, B. / Mullen, G.P. | ||||||
![]() | ![]() Title: Structural basis for the topological specificity function of MinE. Authors: King, G.F. / Shih, Y.L. / Maciejewski, M.W. / Bains, N.P. / Pan, B. / Rowland, S.L. / Mullen, G.P. / Rothfield, L.I. #1: ![]() Title: A Division Inhibitor and a Topological Specificity Factor Coded for by the Minicell Locus Determine Proper Placement of the Division Septum in E. coli Authors: de Boer, P.A.J. / Crossley, R.E. / Rothfield, L.I. #2: ![]() Title: Proper Placement of the Escherichia coli Division Site Requires Two Functions that are Associated with Different Domains of the MinE Protein Authors: Zhao, C.R. / de Boer, P.A.J. / Rothfield, L.I. #3: ![]() Title: The MinE ring: An FtsZ-Independent Cell Structure Required for Selection of the Correct Division Site in E. coli Authors: Raskin, D.M. / de Boer, P.A.J. #4: ![]() Title: The Dimerization and Topological Specificity Functions of MinE Reside in a Structurally Autonomous C-terminal Domain Authors: King, G.F. / Rowland, S.L. / Pan, B. / Mackay, J.P. / Mullen, G.P. / Rothfield, L.I. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 735.4 KB | Display | ![]() |
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PDB format | ![]() | 618.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 347 KB | Display | ![]() |
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Full document | ![]() | 535.6 KB | Display | |
Data in XML | ![]() | 43.6 KB | Display | |
Data in CIF | ![]() | 67.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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: 6713.656 Da / Num. of mol.: 2 / Fragment: MINE TOPOLOGICAL SPECIFICITY DOMAIN 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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NMR details | Text: The structure was determined using triple-resonance NMR spectroscopy. Intermonomer NOEs were determined using a heterolabeled protein sample. |
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Sample preparation
Details |
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Sample conditions | Ionic strength: 0.075 / pH: 5.7 / Pressure: ambient / Temperature: 298 K | |||||||||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: torsion angle dynamics, dynamical simulated annealing Software ordinal: 1 Details: 900 structures were calculated using torsion angle dynamics (DYANA). The best 60 structures were then refined using dynamical simulated annealing in X-PLOR. | ||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: Lowest energy and least restraint violations Conformers calculated total number: 60 / Conformers submitted total number: 20 |