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- PDB-1qey: NMR Structure Determination of the Tetramerization Domain of the ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1qey | ||||||
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Title | NMR Structure Determination of the Tetramerization Domain of the MNT Repressor: An Asymmetric A-Helical Assembly in Slow Exchange | ||||||
![]() | PROTEIN (REGULATORY PROTEIN MNT) | ||||||
![]() | GENE REGULATION / OLIGOMERIZATION / TRANSCRIPTIONAL CONTROL / P22 MNT REPRESSOR | ||||||
Function / homology | Bacteriophage P22, Mnt / Regulatory protein Mnt / Arc-like DNA binding domain / Arc-like DNA binding domain / Arc-type ribbon-helix-helix / Ribbon-helix-helix / regulation of DNA-templated transcription / DNA binding / Regulatory protein mnt![]() | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
![]() | Nooren, I.M.A. / George, A.V.E. / Kaptein, R. / Sauer, R.T. / Boelens, R. | ||||||
![]() | ![]() Title: The tetramerization domain of the Mnt repressor consists of two right-handed coiled coils. Authors: Nooren, I.M. / Kaptein, R. / Sauer, R.T. / Boelens, R. #1: Journal: J.Biomol.Nmr / Year: 1999 Title: NMR structure determination of the tetramerization domain of the Mnt repressor: An asymmetric alpha-helical assembly in slow exchange. Authors: Nooren, I.M. / George, A.V. / Kaptein, R. / Sauer, R.T. / Boelens, R. #2: Journal: J.Biomol.Struct.Dyn. / Year: 2000 Title: Structure and dynamics of the tetrameric mnt repressor and a model for its DNA complex. Authors: Nooren, I.M. / Folkers, G.E. / Kaptein, R. / Sauer, R.T. / Boelens, R. #3: Journal: Biochemistry / Year: 1995 Title: Domains of Mnt repressor: roles in tetramer formation, protein stability, and operator DNA binding. Authors: Waldburger, C.D. / Sauer, R.T. | ||||||
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 | ![]() | 1.1 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 361.2 KB | Display | ![]() |
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Full document | ![]() | 795.7 KB | Display | |
Data in XML | ![]() | 50.8 KB | Display | |
Data in CIF | ![]() | 83.8 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/peptide | Mass: 3693.208 Da / Num. of mol.: 4 / Fragment: C-TERMINAL TETRAMERIZATION DOMAIN Source method: isolated from a genetically manipulated source Details: CHYMOTRYPTIC FRAGMENT OF WILD-TYPE PROTEIN / Source: (gene. exp.) ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
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Sample preparation
Sample conditions | Ionic strength: 50 mM KPI, 200 mM NACL / pH: 5.2 / Temperature: 298.0 K |
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Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 / Details: SEE LITERATURE | ||||||||||||
NMR ensemble | Conformer selection criteria: LOWEST ENERGY, LEAST RESTRAINT VIOLATION Conformers calculated total number: 30 / Conformers submitted total number: 27 |