[English] 日本語
Yorodumi- PDB-2ld5: Solution NMR-derived complex structure of Hoxa13 DNA binding doma... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2ld5 | ||||||
---|---|---|---|---|---|---|---|
Title | Solution NMR-derived complex structure of Hoxa13 DNA binding domain bound to DNA | ||||||
Components |
| ||||||
Keywords | TRANSCRIPTION/DNA / TRANSCRIPTION-DNA complex | ||||||
Function / homology | Function and homology information endothelial cell fate specification / positive regulation of mesenchymal cell apoptotic process / regulation of BMP signaling pathway / branching involved in prostate gland morphogenesis / endothelial cell morphogenesis / male genitalia development / tissue homeostasis / embryonic forelimb morphogenesis / intermediate filament cytoskeleton / ventricular septum development ...endothelial cell fate specification / positive regulation of mesenchymal cell apoptotic process / regulation of BMP signaling pathway / branching involved in prostate gland morphogenesis / endothelial cell morphogenesis / male genitalia development / tissue homeostasis / embryonic forelimb morphogenesis / intermediate filament cytoskeleton / ventricular septum development / artery morphogenesis / inner ear development / anatomical structure morphogenesis / vasculogenesis / cis-regulatory region sequence-specific DNA binding / positive regulation of mitotic nuclear division / animal organ morphogenesis / sequence-specific double-stranded DNA binding / DNA-binding transcription activator activity, RNA polymerase II-specific / sequence-specific DNA binding / transcription cis-regulatory region binding / RNA polymerase II cis-regulatory region sequence-specific DNA binding / DNA-binding transcription factor activity / positive regulation of transcription by RNA polymerase II / DNA binding / nucleoplasm / nucleus / cytosol Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Zhang, Y. | ||||||
Citation | Journal: Plos One / Year: 2011 Title: Structural basis for sequence specific DNA binding and protein dimerization of HOXA13. Authors: Zhang, Y. / Larsen, C.A. / Stadler, H.S. / Ames, J.B. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 2ld5.cif.gz | 291.5 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb2ld5.ent.gz | 238.1 KB | Display | PDB format |
PDBx/mmJSON format | 2ld5.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2ld5_validation.pdf.gz | 428.5 KB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 2ld5_full_validation.pdf.gz | 573 KB | Display | |
Data in XML | 2ld5_validation.xml.gz | 16.9 KB | Display | |
Data in CIF | 2ld5_validation.cif.gz | 29.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ld/2ld5 ftp://data.pdbj.org/pub/pdb/validation_reports/ld/2ld5 | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
1 |
| |||||||||
NMR ensembles |
|
-Components
#1: Protein | Mass: 8670.194 Da / Num. of mol.: 1 / Fragment: Homeobox DNA binding residues 320-386 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Hox-1.10, Hoxa13 / Production host: Escherichia coli (E. coli) / References: UniProt: Q62424 |
---|---|
#2: DNA chain | Mass: 3334.239 Da / Num. of mol.: 1 / Source method: obtained synthetically |
#3: DNA chain | Mass: 3369.217 Da / Num. of mol.: 1 / Source method: obtained synthetically |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR |
---|---|
NMR experiment | Type: 3D 1H-13C NOESY |
-Sample preparation
Details | Contents: 0.5 mM [U-100% 13C; U-100% 15N] sodium phosphate, 100% D2O Solvent system: 100% D2O |
---|---|
Sample | Conc.: 0.5 mM / Component: sodium phosphate-1 / Isotopic labeling: [U-100% 13C; U-100% 15N] |
Sample conditions | Ionic strength: 0.025 / pH: 6.0 / Pressure: ambient / Temperature: 310 K |
-NMR measurement
NMR spectrometer | Type: Bruker Avance / Manufacturer: Bruker / Model: AVANCE / Field strength: 800 MHz |
---|
-Processing
NMR software |
| |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method: 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: 200 / Conformers submitted total number: 10 |