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- PDB-2rux: Solution structures of the DNA-binding domain (ZF6) of immune-rel... -
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Basic information
Entry | Database: PDB / ID: 2rux | ||||||
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Title | Solution structures of the DNA-binding domain (ZF6) of immune-related zinc-finger protein ZFAT | ||||||
![]() | Zinc finger protein ZFAT | ||||||
![]() | TRANSCRIPTION / ZFAT / zinc finger | ||||||
Function / homology | ![]() hematopoietic progenitor cell differentiation / DNA-binding transcription activator activity, RNA polymerase II-specific / DNA-binding transcription factor activity, RNA polymerase II-specific / RNA polymerase II cis-regulatory region sequence-specific DNA binding / regulation of DNA-templated transcription / nucleus / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / DGSA-distance geometry simulated annealing | ||||||
Model details | lowest energy, model1 | ||||||
![]() | Tochio, N. / Umehara, T. / Kigawa, T. / Yokoyama, S. | ||||||
![]() | ![]() Title: Solution structures of the DNA-binding domains of immune-related zinc-finger protein ZFAT Authors: Tochio, N. / Umehara, T. / Nakabayashi, K. / Yoneyama, M. / Tsuda, K. / Shirouzu, M. / Koshiba, S. / Watanabe, S. / Kigawa, T. / Sasazuki, T. / Shirasawa, S. / Yokoyama, S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 228.5 KB | Display | ![]() |
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PDB format | ![]() | 187.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 386.7 KB | Display | ![]() |
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Full document | ![]() | 472 KB | Display | |
Data in XML | ![]() | 12.1 KB | Display | |
Data in CIF | ![]() | 20.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2rutC ![]() 2ruuC ![]() 2ruvC ![]() 2ruwC ![]() 2ruyC ![]() 2ruzC ![]() 2rv0C ![]() 2rv1C ![]() 2rv2C ![]() 2rv3C ![]() 2rv4C ![]() 2rv5C ![]() 2rv6C ![]() 2rv7C 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/peptide | Mass: 4199.735 Da / Num. of mol.: 1 / Fragment: UNP residues 402-430 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() |
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#2: Chemical | ChemComp-ZN / |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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Sample preparation
Details | Contents: 1.09 mM [U-13C; U-15N] protein-1, 20 mM [U-2H] TRIS-2, 100 mM sodium chloride-3, 1 mM [U-2H] DTT-4, 0.02 % sodium azide-5, 50 uM zinc chloride-6, 90 % H2O-7, 10 % [U-2H] D2O-8, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||||||||||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 120 / pH: 7 / Pressure: 1 atm / Temperature: 296 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz |
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Processing
NMR software |
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Refinement | Method: DGSA-distance geometry simulated annealing / Software ordinal: 1 | ||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 20 / Conformers submitted total number: 20 / Representative conformer: 1 |