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Yorodumi- PDB-1fv5: SOLUTION STRUCTURE OF THE FIRST ZINC FINGER FROM THE DROSOPHILA U... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1fv5 | ||||||
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Title | SOLUTION STRUCTURE OF THE FIRST ZINC FINGER FROM THE DROSOPHILA U-SHAPED TRANSCRIPTION FACTOR | ||||||
Components | FIRST ZINC FINGER OF U-SHAPED | ||||||
Keywords | TRANSCRIPTION / ZINC FINGER / CCHC / PROTEIN INTERACTION | ||||||
Function / homology | Function and homology information lymph gland plasmatocyte differentiation / lymph gland crystal cell differentiation / negative regulation of hemocyte differentiation / amnioserosa maintenance / positive regulation of antibacterial peptide biosynthetic process / germ-band shortening / Factors involved in megakaryocyte development and platelet production / lymph gland development / larval lymph gland hemopoiesis / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function ...lymph gland plasmatocyte differentiation / lymph gland crystal cell differentiation / negative regulation of hemocyte differentiation / amnioserosa maintenance / positive regulation of antibacterial peptide biosynthetic process / germ-band shortening / Factors involved in megakaryocyte development and platelet production / lymph gland development / larval lymph gland hemopoiesis / RUNX1 regulates genes involved in megakaryocyte differentiation and platelet function / compound eye development / chaeta development / DNA-binding transcription repressor activity / negative regulation of insulin receptor signaling pathway / heart development / RNA polymerase II-specific DNA-binding transcription factor binding / cell differentiation / negative regulation of DNA-templated transcription / regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / DNA binding / nucleus / metal ion binding Similarity search - Function | ||||||
Biological species | Drosophila melanogaster (fruit fly) | ||||||
Method | SOLUTION NMR / distance geometry simulated annealing cartesian dynamics | ||||||
Authors | Liew, C.K. / Kowalski, K. / Fox, A.H. / Newton, A. / Sharpe, B.K. / Crossley, M. / Mackay, J.P. | ||||||
Citation | Journal: Structure Fold.Des. / Year: 2000 Title: Solution structures of two CCHC zinc fingers from the FOG family protein U-shaped that mediate protein-protein interactions. Authors: Liew, C.K. / Kowalski, K. / Fox, A.H. / Newton, A. / Sharpe, B.K. / Crossley, M. / Mackay, J.P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1fv5.cif.gz | 219.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1fv5.ent.gz | 179.2 KB | Display | PDB format |
PDBx/mmJSON format | 1fv5.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1fv5_validation.pdf.gz | 339.8 KB | Display | wwPDB validaton report |
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Full document | 1fv5_full_validation.pdf.gz | 457.4 KB | Display | |
Data in XML | 1fv5_validation.xml.gz | 12.4 KB | Display | |
Data in CIF | 1fv5_validation.cif.gz | 20.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fv/1fv5 ftp://data.pdbj.org/pub/pdb/validation_reports/fv/1fv5 | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein/peptide | Mass: 3961.636 Da / Num. of mol.: 1 / Fragment: FIRST ZINC FINGER DOMAIN (RESIDUES 202-235) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Drosophila melanogaster (fruit fly) / Plasmid: PGEX-2T / Production host: Escherichia coli (E. coli) / References: UniProt: Q9VPQ6 |
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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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NMR details | Text: The structure was determined using 2D homonuclear and heteronuclear techniques on unlabelled and 15N-labelled peptide. |
-Sample preparation
Details |
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Sample conditions | Ionic strength: 0 / pH: 5.5 / Pressure: ambient / Temperature: 298 K | |||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: distance geometry simulated annealing cartesian dynamics Software ordinal: 1 Details: The structures are based on a total of 356 restraints, 324 are NOE-derived distance constraints and 32 are dihedral angle restraints | ||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 500 / Conformers submitted total number: 20 |