[English] 日本語
![](img/lk-miru.gif)
- PDB-8ajr: The Solution Structure of the Triple Mutant Methyl-CpG-Binding Do... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 8ajr | ||||||
---|---|---|---|---|---|---|---|
Title | The Solution Structure of the Triple Mutant Methyl-CpG-Binding Domain from MeCP2 | ||||||
![]() | Methyl-CpG-binding protein 2 | ||||||
![]() | GENE REGULATION / Epigenetic modifications / Reader protein / Domain of MeCP2 | ||||||
Function / homology | ![]() double-stranded methylated DNA binding / negative regulation of transcription by RNA polymerase II / nucleus Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
![]() | Singh, H. | ||||||
Funding support | ![]()
| ||||||
![]() | ![]() Title: Epigenetic CpG duplex marks probed by an evolved DNA reader via a well-tempered conformational plasticity. Authors: Singh, H. / Das, C.K. / Buchmuller, B.C. / Schafer, L.V. / Summerer, D. / Linser, R. #1: ![]() Title: Epigenetic CpG Duplex Marks Probed by an Evolved DNA Reader via a Well-Tempered Conformational Plasticity Authors: Singh, H. / Das, C.K. / Buchmuller, B.C. / Eppmann, S. / Schafer, L.V. / Summerer, D. / Linser, R. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 367.7 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 308.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 404.9 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 454.3 KB | Display | |
Data in XML | ![]() | 17.9 KB | Display | |
Data in CIF | ![]() | 29.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 8alqC C: citing same article ( |
---|---|
Similar structure data | Similarity search - Function & homology ![]() |
Other databases |
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-
Components
#1: Protein | Mass: 11905.288 Da / Num. of mol.: 1 / Mutation: T, A, N Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-
Sample preparation
Details |
| |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Sample |
| |||||||||||||||
Sample conditions | Ionic strength: 100 mM / Label: 13C and 15N / pH: 6 Not defined / Pressure: 1 atm / Temperature: 283 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE III HD / Manufacturer: Bruker / Model: AVANCE III HD / Field strength: 800 MHz |
---|
-
Processing
NMR software |
| |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: simulated annealing / Software ordinal: 1 / Details: total restraints 658 | |||||||||||||||
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: 10 |