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Yorodumi- PDB-2m26: NMR structure of the C-terminal domain of the protein HCFC1 from ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2m26 | ||||||
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Title | NMR structure of the C-terminal domain of the protein HCFC1 from Mus musculus | ||||||
Components | HCF C-terminal chain 1 | ||||||
Keywords | CELL CYCLE / JCSG / PSI-Biology / Structural Genomics / Joint Center for Structural Genomics / Partnership for Stem Cell Biology / STEMCELL | ||||||
Function / homology | Function and homology information : / : / : / : / DNA-binding transcription factor binding => GO:0140297 / SAGA-type complex / release from viral latency / UCH proteinases / HATs acetylate histones / blastocyst hatching ...: / : / : / : / DNA-binding transcription factor binding => GO:0140297 / SAGA-type complex / release from viral latency / UCH proteinases / HATs acetylate histones / blastocyst hatching / Set1C/COMPASS complex / MLL1 complex / transcription factor binding / cellular response to organic cyclic compound / histone acetyltransferase complex / regulation of protein-containing complex assembly / protein-macromolecule adaptor activity / collagen-containing extracellular matrix / transcription coactivator activity / protein stabilization / chromatin remodeling / cell cycle / RNA polymerase II cis-regulatory region sequence-specific DNA binding / axon / neuronal cell body / chromatin binding / dendrite / regulation of DNA-templated transcription / positive regulation of gene expression / positive regulation of DNA-templated transcription / negative regulation of transcription by RNA polymerase II / positive regulation of transcription by RNA polymerase II / protein-containing complex / identical protein binding / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | SOLUTION NMR / molecular dynamics | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Serrano, P. / Geralt, M. / Dutta, S.K. / Wuthrich, K. / Joint Center for Structural Genomics (JCSG) / Partnership for Stem Cell Biology (STEMCELL) | ||||||
Citation | Journal: To be Published Title: NMR structure of the C-terminal domain of the protein HCFC1 from Mus musculus Authors: Serrano, P. / Wuthrich, K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2m26.cif.gz | 763.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2m26.ent.gz | 646.5 KB | Display | PDB format |
PDBx/mmJSON format | 2m26.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/m2/2m26 ftp://data.pdbj.org/pub/pdb/validation_reports/m2/2m26 | HTTPS FTP |
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-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: 13347.041 Da / Num. of mol.: 1 / Fragment: UNP residues 1896-2020 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Hcfc1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21 / References: UniProt: Q61191 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 1.2 mM [U-98% 13C; U-98% 15N] protein, 50 mM sodium chloride, 20 mM sodium phosphate, 5 mM sodium azide, 95% H2O/5% D2O Solvent system: 95% H2O/5% D2O | ||||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 0.220 / pH: 6.5 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: molecular dynamics / Software ordinal: 1 | |||||||||||||||
NMR representative | Selection criteria: lowest energy | |||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 80 / Conformers submitted total number: 20 |