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Yorodumi- PDB-2epp: Solution structure of the first C2H2 type zinc finger domain of Z... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2epp | ||||||
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Title | Solution structure of the first C2H2 type zinc finger domain of Zinc finger protein 278 | ||||||
Components | POZ-, AT hook-, and zinc finger-containing protein 1 | ||||||
Keywords | TRANSCRIPTION / C2H2 / zinc finger domain / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information regulation of immune system process / negative regulation of endothelial cell migration / T cell differentiation / regulation of cytokine production / male germ cell nucleus / DNA-binding transcription repressor activity, RNA polymerase II-specific / male gonad development / spermatogenesis / RNA polymerase II cis-regulatory region sequence-specific DNA binding / negative regulation of DNA-templated transcription ...regulation of immune system process / negative regulation of endothelial cell migration / T cell differentiation / regulation of cytokine production / male germ cell nucleus / DNA-binding transcription repressor activity, RNA polymerase II-specific / male gonad development / spermatogenesis / RNA polymerase II cis-regulatory region sequence-specific DNA binding / negative regulation of DNA-templated transcription / chromatin binding / ubiquitin protein ligase binding / regulation of DNA-templated transcription / positive regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / DNA binding / nucleoplasm / nucleus / metal ion binding Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dyanamics, simulated annealing | ||||||
Authors | Tanabe, W. / Suzuki, S. / Muto, Y. / Inoue, M. / Kigawa, T. / Terada, T. / Shirouzu, M. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: Solution structure of the first C2H2 type zinc finger domain of Zinc finger protein 278 Authors: Tanabe, W. / Suzuki, S. / Muto, Y. / Inoue, M. / Kigawa, T. / Terada, T. / Shirouzu, M. / Yokoyama, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2epp.cif.gz | 370.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2epp.ent.gz | 311.3 KB | Display | PDB format |
PDBx/mmJSON format | 2epp.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2epp_validation.pdf.gz | 338.2 KB | Display | wwPDB validaton report |
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Full document | 2epp_full_validation.pdf.gz | 439.5 KB | Display | |
Data in XML | 2epp_validation.xml.gz | 18.5 KB | Display | |
Data in CIF | 2epp_validation.cif.gz | 31 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ep/2epp ftp://data.pdbj.org/pub/pdb/validation_reports/ep/2epp | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 6734.532 Da / Num. of mol.: 1 / Fragment: zinc finger domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Description: Cell-free protein synthesis / Gene: PATZ1, PATZ, RIAZ, ZBTB19, ZNF278, ZSG / Plasmid: P061204-01 / References: UniProt: Q9HBE1 |
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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: 0.89mM 13C-15N PROTEIN, 20mM d-Tris-HCl(pH7.0), 100mM NaCl, 1mM d-DTT, 0.02% NaN3, 90% H2O, 10% D2O, 0.05mM ZnCl2, 1mM IDA Solvent system: 90% H2O/10% D2O |
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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 |
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-Processing
NMR software |
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Refinement | Method: torsion angle dyanamics, simulated annealing / Software ordinal: 1 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations, structures with the lowest energy, target function Conformers calculated total number: 100 / Conformers submitted total number: 20 |