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Yorodumi- PDB-2efi: Solution structure of the chromo domain of Mortality factor 4-lik... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2efi | ||||||
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Title | Solution structure of the chromo domain of Mortality factor 4-like protein 1 from human | ||||||
Components | Mortality factor 4-like protein 1 | ||||||
Keywords | TRANSCRIPTION / Chromo domain / Mortality factor 4-like protein 1 / 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 double-strand break repair / NuA4 histone acetyltransferase complex / Sin3-type complex / positive regulation of double-strand break repair via homologous recombination / double-strand break repair via homologous recombination / nucleosome / chromatin organization / HATs acetylate histones / regulation of apoptotic process / regulation of cell cycle ...regulation of double-strand break repair / NuA4 histone acetyltransferase complex / Sin3-type complex / positive regulation of double-strand break repair via homologous recombination / double-strand break repair via homologous recombination / nucleosome / chromatin organization / HATs acetylate histones / regulation of apoptotic process / regulation of cell cycle / nuclear speck / positive regulation of DNA-templated transcription / nucleoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Authors | Li, H. / Sato, M. / Tochio, N. / Tomizawa, T. / Koshiba, S. / Harada, T. / Watanabe, S. / Kigawa, T. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: Solution structure of the chromo domain of Mortality factor 4-like protein 1 from human Authors: Li, H. / Sato, M. / Tochio, N. / Tomizawa, T. / Koshiba, S. / Harada, T. / Watanabe, S. / Kigawa, T. / Yokoyama, S. | ||||||
History |
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Remark 650 | HELIX Determination method: Author determined | ||||||
Remark 700 | SHEET Determination method: Author determined | ||||||
Remark 999 | SEQUENCE The sequence database is Q9UBU8-2, Isoform 2 of Q9UBU8. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2efi.cif.gz | 628.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2efi.ent.gz | 526.1 KB | Display | PDB format |
PDBx/mmJSON format | 2efi.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2efi_validation.pdf.gz | 342.5 KB | Display | wwPDB validaton report |
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Full document | 2efi_full_validation.pdf.gz | 484.1 KB | Display | |
Data in XML | 2efi_validation.xml.gz | 35.6 KB | Display | |
Data in CIF | 2efi_validation.cif.gz | 53.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ef/2efi ftp://data.pdbj.org/pub/pdb/validation_reports/ef/2efi | 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: 11524.102 Da / Num. of mol.: 1 / Fragment: Chromo domain Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Description: Cell-free protein synthesis / Gene: MORF4L1 / Plasmid: P060522-07 / References: UniProt: Q9UBU8 |
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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: 1.13mM Chromo domain U-15N, 13C; 20mM d-Tris-HCl(pH 7.0); 100mM NaCl; 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: 296 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 |