+Open data
-Basic information
Entry | Database: PDB / ID: 2m0e | ||||||
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Title | Solution Structure of Miz-1 zinc finger 6 | ||||||
Components | Zinc finger and BTB domain-containing protein 17 | ||||||
Keywords | TRANSCRIPTION / C2H2 zinc fingers | ||||||
Function / homology | Function and homology information ectoderm development / XBP1(S) activates chaperone genes / regulation of immune system process / gastrulation with mouth forming second / G1 to G0 transition / negative regulation of cell cycle / core promoter sequence-specific DNA binding / regulation of cytokine production / protein-DNA complex / transcription coactivator binding ...ectoderm development / XBP1(S) activates chaperone genes / regulation of immune system process / gastrulation with mouth forming second / G1 to G0 transition / negative regulation of cell cycle / core promoter sequence-specific DNA binding / regulation of cytokine production / protein-DNA complex / transcription coactivator binding / DNA-binding transcription repressor activity, RNA polymerase II-specific / DNA-binding transcription activator activity, RNA polymerase II-specific / DNA-binding transcription factor binding / RNA polymerase II cis-regulatory region sequence-specific DNA binding / DNA-binding transcription factor activity / negative regulation of cell population proliferation / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / protein-containing complex / nucleoplasm / metal ion binding Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | lowest energy, model2 | ||||||
Authors | Bernard, D. / Bedard, M. / Bilodeau, J. / Lavigne, P. | ||||||
Citation | Journal: To be Published Title: NMR Structure Note: Solution Structure of Miz-1 Zinc Fingers 5 to 7 Authors: Bernard, D. / Bedard, M. / Bilodeau, J. / Lavigne, P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2m0e.cif.gz | 217.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2m0e.ent.gz | 175.6 KB | Display | PDB format |
PDBx/mmJSON format | 2m0e.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/m0/2m0e ftp://data.pdbj.org/pub/pdb/validation_reports/m0/2m0e | HTTPS FTP |
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-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 | Mass: 12964.952 Da / Num. of mol.: 1 / Fragment: C2H2-TYPE 5-8, ZINC FINGER RESIDUES 416-526 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: MIZ1, ZBTB17, ZNF151, ZNF60 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 star (DE3) / References: UniProt: Q13105 |
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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: 0.65 mM [U-13C; U-15N] Miz58, 90% H2O/10% D2O / Solvent system: 90% H2O/10% D2O |
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Sample | Conc.: 0.65 mM / Component: Miz58-1 / Isotopic labeling: [U-13C; U-15N] |
Sample conditions | Ionic strength: 0.05 / pH: 7 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | ||||||||||||||||||||||||
NMR constraints | NOE constraints total: 400 / NOE intraresidue total count: 219 / NOE long range total count: 10 / NOE medium range total count: 77 / NOE sequential total count: 94 / Protein chi angle constraints total count: 1 / Protein other angle constraints total count: 0 | ||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 300 / Conformers submitted total number: 20 |