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Yorodumi- PDB-2eme: Solution structure of the C2H2 type zinc finger (region 725-757) ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2eme | ||||||
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Title | Solution structure of the C2H2 type zinc finger (region 725-757) of human Zinc finger protein 473 | ||||||
Components | Zinc finger protein 473 | ||||||
Keywords | TRANSCRIPTION / zf-C2H2 / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information mRNA 3'-end processing by stem-loop binding and cleavage / SLBP independent Processing of Histone Pre-mRNAs / SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs / Generic Transcription Pathway / RNA Polymerase II Transcription Termination / Cajal body / DNA-binding transcription activator activity, RNA polymerase II-specific / RNA polymerase II cis-regulatory region sequence-specific DNA binding / regulation of transcription by RNA polymerase II / nucleoplasm ...mRNA 3'-end processing by stem-loop binding and cleavage / SLBP independent Processing of Histone Pre-mRNAs / SLBP Dependent Processing of Replication-Dependent Histone Pre-mRNAs / Generic Transcription Pathway / RNA Polymerase II Transcription Termination / Cajal body / DNA-binding transcription activator activity, RNA polymerase II-specific / RNA polymerase II cis-regulatory region sequence-specific DNA binding / regulation of transcription by RNA polymerase II / nucleoplasm / nucleus / metal ion binding Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Tomizawa, T. / Tochio, N. / Abe, H. / Saito, K. / Li, H. / Sato, M. / Koshiba, S. / Kobayashi, N. / Kigawa, T. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: Solution structure of the C2H2 type zinc finger (region 725-757) of human Zinc finger protein 473 Authors: Tochio, N. / Tomizawa, T. / Abe, H. / Saito, K. / Li, H. / Sato, M. / Koshiba, S. / Kobayashi, N. / Kigawa, T. / Yokoyama, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2eme.cif.gz | 252.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2eme.ent.gz | 209.4 KB | Display | PDB format |
PDBx/mmJSON format | 2eme.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2eme_validation.pdf.gz | 339 KB | Display | wwPDB validaton report |
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Full document | 2eme_full_validation.pdf.gz | 448 KB | Display | |
Data in XML | 2eme_validation.xml.gz | 15.8 KB | Display | |
Data in CIF | 2eme_validation.cif.gz | 24.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/em/2eme ftp://data.pdbj.org/pub/pdb/validation_reports/em/2eme | 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/peptide | Mass: 4676.104 Da / Num. of mol.: 1 / Fragment: zf-C2H2 domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Description: cell-free protein synthesis / Gene: ZNF473 / Plasmid: P070115-33 / References: UniProt: Q8WTR7 |
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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: about 1.0mM sample U-15N, 13C; 20mM d-Tris-HCl; 100mM NaCl; 0.05MM ZnCl2; 1mM IDA; 1mM d-DTT; 0.02% NaN3; 90% H2O, 10% D2O 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 dynamics / Software ordinal: 1 | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the least restraint violations, target function Conformers calculated total number: 100 / Conformers submitted total number: 20 |