[English] 日本語
Yorodumi- PDB-2dmn: The solution structure of the homeobox domain of human homeobox p... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2dmn | ||||||
---|---|---|---|---|---|---|---|
Title | The solution structure of the homeobox domain of human homeobox protein TGIF2LX | ||||||
Components | Homeobox protein TGIF2LX | ||||||
Keywords | TRANSCRIPTION / TGFB-induced factor 2-like protein / X-linked TGF(beta)induced transcription factor 2-like protein / TGIF-like on the X / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information DNA-binding transcription repressor activity, RNA polymerase II-specific / sequence-specific double-stranded DNA binding / DNA-binding transcription factor activity, RNA polymerase II-specific / RNA polymerase II cis-regulatory region sequence-specific DNA binding / chromatin / negative regulation of transcription by RNA polymerase II / nucleus Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Tochio, N. / Ohnishi, S. / Sasagawa, A. / Saito, K. / Koshiba, S. / Inoue, M. / Kigawa, T. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: The solution structure of the homeobox domain of human homeobox protein TGIF2LX Authors: Tochio, N. / Ohnishi, S. / Sasagawa, A. / Saito, K. / Koshiba, S. / Inoue, M. / Kigawa, T. / Yokoyama, S. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 2dmn.cif.gz | 521.9 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb2dmn.ent.gz | 438.1 KB | Display | PDB format |
PDBx/mmJSON format | 2dmn.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2dmn_validation.pdf.gz | 341.5 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 2dmn_full_validation.pdf.gz | 477.3 KB | Display | |
Data in XML | 2dmn_validation.xml.gz | 31.8 KB | Display | |
Data in CIF | 2dmn_validation.cif.gz | 48 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/dm/2dmn ftp://data.pdbj.org/pub/pdb/validation_reports/dm/2dmn | HTTPS FTP |
-Related structure data
Similar structure data | |
---|---|
Other databases |
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 9551.891 Da / Num. of mol.: 1 / Fragment: homeobox domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Description: cell-free protein synthesis / Gene: TGIF2LX, TGIFLX / Plasmid: P050530-26 / Production host: Cell free synthesis / References: UniProt: Q8IUE1 |
---|
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
NMR experiment |
|
-Sample preparation
Details | Contents: 1.1mM homeobox domain U-15N,13C; 20mM d-Tris-HCl; 100mM NaCl; 1mM d-DTT; 0.02% NaN3; 10% D2O Solvent system: 90% H2O/10% D2O |
---|---|
Sample conditions | Ionic strength: 120mM / pH: 7 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz |
---|
-Processing
NMR software |
| ||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: torsion angle dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: target function,structures with the least restraint violations Conformers calculated total number: 100 / Conformers submitted total number: 20 |