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Yorodumi- PDB-5eq1: Crystal structure of the human BRPF1 bromodomain in complex with ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5eq1 | ||||||
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Title | Crystal structure of the human BRPF1 bromodomain in complex with SEED12 | ||||||
Components | Peregrin | ||||||
Keywords | DNA BINDING PROTEIN / Bromodomain and PHD finger-containing protein 1(BRPF1) / monocytic leukemia zinc-finger (MOZ) / Inhibitor / transcription | ||||||
Function / homology | Function and homology information acetyltransferase activator activity / regulation of developmental process / regulation of hemopoiesis / MOZ/MORF histone acetyltransferase complex / histone acetyltransferase complex / Regulation of TP53 Activity through Acetylation / HATs acetylate histones / chromatin remodeling / regulation of transcription by RNA polymerase II / positive regulation of DNA-templated transcription ...acetyltransferase activator activity / regulation of developmental process / regulation of hemopoiesis / MOZ/MORF histone acetyltransferase complex / histone acetyltransferase complex / Regulation of TP53 Activity through Acetylation / HATs acetylate histones / chromatin remodeling / regulation of transcription by RNA polymerase II / positive regulation of DNA-templated transcription / regulation of DNA-templated transcription / DNA binding / nucleoplasm / nucleus / metal ion binding / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.55 Å | ||||||
Authors | Zhu, J. / Caflisch, A. | ||||||
Funding support | Switzerland, 1items
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Citation | Journal: J.Med.Chem. / Year: 2016 Title: Twenty Crystal Structures of Bromodomain and PHD Finger Containing Protein 1 (BRPF1)/Ligand Complexes Reveal Conserved Binding Motifs and Rare Interactions. Authors: Zhu, J. / Caflisch, A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5eq1.cif.gz | 66.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5eq1.ent.gz | 48.2 KB | Display | PDB format |
PDBx/mmJSON format | 5eq1.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5eq1_validation.pdf.gz | 450.4 KB | Display | wwPDB validaton report |
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Full document | 5eq1_full_validation.pdf.gz | 450.6 KB | Display | |
Data in XML | 5eq1_validation.xml.gz | 7.7 KB | Display | |
Data in CIF | 5eq1_validation.cif.gz | 9.8 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/eq/5eq1 ftp://data.pdbj.org/pub/pdb/validation_reports/eq/5eq1 | HTTPS FTP |
-Related structure data
Related structure data | 5c7nC 5c85C 5c87C 5dy7C 5dyaC 5dycC 5e3dC 5e3gC 5em3C 5eprC 5epsC 5etbC 5etdC 5ev9C 5evaC 5ewcC 5ewdC 5ewhC 4lc2S C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 13703.698 Da / Num. of mol.: 1 / Fragment: UNP residues 626-740 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: BRPF1, BR140 / Production host: Escherichia coli (E. coli) / References: UniProt: P55201 |
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#2: Chemical | ChemComp-BEA / |
#3: Chemical | ChemComp-NO3 / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.5 Å3/Da / Density % sol: 50.81 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop Details: 0.1 M Bis-tris propane, pH6.5, 0.2 M Sodium nitrate, 20% PEG3350 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 0.99987 Å |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jul 5, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.99987 Å / Relative weight: 1 |
Reflection | Resolution: 1.55→40.29 Å / Num. obs: 19761 / % possible obs: 99.9 % / Redundancy: 9.4 % / Rmerge(I) obs: 0.041 / Net I/σ(I): 25.9 |
Reflection shell | Resolution: 1.55→1.63 Å / Redundancy: 8.9 % / Rmerge(I) obs: 0.338 / Mean I/σ(I) obs: 6.1 / % possible all: 100 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 4LC2 Resolution: 1.55→40.288 Å / SU ML: 0.18 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 22.14 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.55→40.288 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Origin x: 14.7625 Å / Origin y: -22.5514 Å / Origin z: 0.394 Å
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Refinement TLS group | Selection details: all |