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- PDB-2l1b: Solution NMR structure of the chromobox protein Cbx7 with H3K27me3 -
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Open data
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Basic information
Entry | Database: PDB / ID: 2l1b | ||||||
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Title | Solution NMR structure of the chromobox protein Cbx7 with H3K27me3 | ||||||
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![]() | TRANSCRIPTION REGULATOR / chromodomain / Structural Genomics / Structural Genomics Consortium / SGC | ||||||
Function / homology | ![]() PRC1 complex / PcG protein complex / structural constituent of chromatin / nucleosome / chromatin organization / protein heterodimerization activity / chromatin / negative regulation of transcription by RNA polymerase II / DNA binding / nucleoplasm ...PRC1 complex / PcG protein complex / structural constituent of chromatin / nucleosome / chromatin organization / protein heterodimerization activity / chromatin / negative regulation of transcription by RNA polymerase II / DNA binding / nucleoplasm / nucleus / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / molecular dynamics | ||||||
Model details | lowest energy, model 1 | ||||||
![]() | Kaustov, L. / Lemak, A. / Fares, C. / Gutmanas, A. / Muhandiram, R. / Quang, H. / Loppnau, P. / Min, J. / Edwards, A. / Arrowsmith, C. / Structural Genomics Consortium (SGC) | ||||||
![]() | ![]() Title: Recognition and specificity determinants of the human cbx chromodomains. Authors: Kaustov, L. / Ouyang, H. / Amaya, M. / Lemak, A. / Nady, N. / Duan, S. / Wasney, G.A. / Li, Z. / Vedadi, M. / Schapira, M. / Min, J. / Arrowsmith, C.H. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 460.7 KB | Display | ![]() |
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PDB format | ![]() | 404.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Summary document | ![]() | 400.9 KB | Display | ![]() |
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Full document | ![]() | 533.1 KB | Display | |
Data in XML | ![]() | 21.9 KB | Display | |
Data in CIF | ![]() | 39.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2l11C ![]() 2l12C ![]() 3fdtC ![]() 3gv6C ![]() 3h91C ![]() 3i90C ![]() 3i91C C: citing same article ( |
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Similar structure data | |
Other databases |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 6816.852 Da / Num. of mol.: 1 / Fragment: UNP Residues 7-62 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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#2: Protein/peptide | Mass: 1515.776 Da / Num. of mol.: 1 / Fragment: UNP Residues 20-34 / Source method: obtained synthetically / Details: H3K27me3 15-mer peptide / Source: (synth.) ![]() |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details | Contents: 0.5 mM [U-13C; U-15N] protein, 2.7 mM peptide, 10 mM sodium phosphate, 300 mM sodium chloride, 0.5 mM PMSF, 0.5 mM TCEP, 1 mM Benzamidine, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O | ||||||||||||||||||||||||||||||||
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Sample |
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Sample conditions | Ionic strength: 300 / pH: 7.4 / 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: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |