+Open data
-Basic information
Entry | Database: PDB / ID: 2bym | ||||||
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Title | Histone fold heterodimer of the Chromatin Accessibility Complex | ||||||
Components |
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Keywords | DNA BINDING PROTEIN / CHRAC-14 / NUCLEOSOME SLIDING / HISTONE FOLD / CHRAC-16 / DNA-BINDING PROTEIN | ||||||
Function / homology | Function and homology information DNA replication initiation / PCNA-Dependent Long Patch Base Excision Repair / Termination of translesion DNA synthesis / Recognition of DNA damage by PCNA-containing replication complex / Dual Incision in GG-NER / Dual incision in TC-NER / CHRAC / Activation of the pre-replicative complex / epsilon DNA polymerase complex / CENP-A containing chromatin assembly ...DNA replication initiation / PCNA-Dependent Long Patch Base Excision Repair / Termination of translesion DNA synthesis / Recognition of DNA damage by PCNA-containing replication complex / Dual Incision in GG-NER / Dual incision in TC-NER / CHRAC / Activation of the pre-replicative complex / epsilon DNA polymerase complex / CENP-A containing chromatin assembly / ATAC complex / leading strand elongation / heterochromatin formation / cellular response to gamma radiation / chromatin DNA binding / DNA-templated DNA replication / nucleic acid binding / molecular adaptor activity / chromatin remodeling / protein heterodimerization activity / DNA damage response / nucleus Similarity search - Function | ||||||
Biological species | DROSOPHILA MELANOGASTER (fruit fly) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SIRAS / Resolution: 2.8 Å | ||||||
Authors | Fernandez-Tornero, C. / Hartlepp, K.F. / Grune, T. / Eberharter, A. / Becker, P.B. / Muller, C.W. | ||||||
Citation | Journal: Mol.Cell.Biol. / Year: 2005 Title: The Histone Fold Subunits of Drosophila Chrac Facilitate Nucleosome Sliding Through Dynamic DNA Interactions. Authors: Hartlepp, K.F. / Fernandez-Tornero, C. / Eberharter, A. / Grune, T. / Muller, C.W. / Becker, P.B. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2bym.cif.gz | 72.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2bym.ent.gz | 54 KB | Display | PDB format |
PDBx/mmJSON format | 2bym.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/by/2bym ftp://data.pdbj.org/pub/pdb/validation_reports/by/2bym | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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-Components
#1: Protein | Mass: 16020.667 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) DROSOPHILA MELANOGASTER (fruit fly) / Plasmid: PGEX2T-CHRAC14/16 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q9V452 #2: Protein | Mass: 13862.586 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) DROSOPHILA MELANOGASTER (fruit fly) / Plasmid: PGEX2T-CHRAC14/16 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q9V444 #3: Chemical | #4: Water | ChemComp-HOH / | Sequence details | PROTEOLYTIC CLEAVAGE IN THE CRYSTALLIZATION DROP MIGHT HAVE OCCURRED BUT ATTEMPTS TO CHARACTERIZE ...PROTEOLYTI | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.12 Å3/Da / Density % sol: 41.5 % |
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Crystal grow | pH: 7.5 / Details: 12% PEG 3350, 0.1M HEPES PH 7.5, 5MM CDCL2 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 0.9795 |
Detector | Type: ADSC CCD / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9795 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→30 Å / Num. obs: 13325 / % possible obs: 99.9 % / Observed criterion σ(I): 2 / Redundancy: 14 % / Biso Wilson estimate: 72.1 Å2 / Rmerge(I) obs: 0.13 / Net I/σ(I): 5.6 |
Reflection shell | Resolution: 2.8→2.95 Å / Redundancy: 14.3 % / Rmerge(I) obs: 0.48 / Mean I/σ(I) obs: 1.6 / % possible all: 99.9 |
-Processing
Software |
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Refinement | Method to determine structure: SIRAS / Resolution: 2.8→33.96 Å / Rfactor Rfree error: 0.008 / Data cutoff high absF: 1824194.32 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 31.0043 Å2 / ksol: 0.385781 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 39 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.8→33.96 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.8→2.98 Å / Rfactor Rfree error: 0.025 / Total num. of bins used: 6
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Xplor file |
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