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- PDB-2lf7: Intramolecular regulation of the ETS Domain within ETV6 sequence ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2lf7 | ||||||
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Title | Intramolecular regulation of the ETS Domain within ETV6 sequence R335 to Q436 | ||||||
![]() | Transcription factor ETV6 | ||||||
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Function / homology | ![]() mesenchymal cell apoptotic process / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
Model details | closest to the average, model 5 | ||||||
![]() | Coyne III, H. / Green, S.M. / Graves, B.J. / Mcintosh, L.P. | ||||||
![]() | ![]() Title: Autoinhibition of ETV6 (TEL) DNA Binding: Appended Helices Sterically Block the ETS Domain. Authors: Coyne, H.J. / De, S. / Okon, M. / Green, S.M. / Bhachech, N. / Graves, B.J. / McIntosh, L.P. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 775.7 KB | Display | ![]() |
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PDB format | ![]() | 659 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 |
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NMR ensembles |
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Components
#1: Protein | Mass: 13060.987 Da / Num. of mol.: 1 / Fragment: ETS DNA binding domain residues 335-436 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details | Contents: 50 mM sodium phosphate, 200 mM sodium chloride, 0.6 mM [U-99% 13C; U-99% 15N] protein, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 0.250 / pH: 5.8 / Pressure: ambient / Temperature: 303 K |
-NMR measurement
NMR spectrometer |
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Processing
NMR software |
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Refinement | Method: ![]() Details: iteration protocol used default values except iteration6 had the violation tolerance 0.09 violation threshold 0.5 and max_contribution 15, iteration7 set the violation threshold 0.07 ...Details: iteration protocol used default values except iteration6 had the violation tolerance 0.09 violation threshold 0.5 and max_contribution 15, iteration7 set the violation threshold 0.07 violation threshold 0.4 max_contributions 10. iteration 8 set the violation tolerance 0.05 violation threshold 0.3 max_contributions 5. The chemical shift tolerances were set to proton1=0.03 hetero1=0.4 proton2=0.3 and hetero2= 0.4. Violated restraints used in the calcuation were examined manually for correct identification as were restraints not used in the calculation over 3 angstroms. Long, medium, and short NOEs not used in the calcualtion were examined on refinement as were ambigous assigments with 3 or more contributions. | ||||||||||||||||||||||||
NMR constraints | NOE constraints total: 3787 / NOE intraresidue total count: 1397 / NOE long range total count: 1003 / NOE medium range total count: 665 / NOE sequential total count: 712 / Protein chi angle constraints total count: 0 / Protein other angle constraints total count: 0 / Protein phi angle constraints total count: 84 / Protein psi angle constraints total count: 84 | ||||||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: all calculated structures submitted Conformers calculated total number: 20 / Conformers submitted total number: 20 / Maximum lower distance constraint violation: 0.05 Å / Maximum upper distance constraint violation: 0.22 Å |