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Yorodumi- PDB-8cmp: DNA-binding bacterial histone protein HBB from Bdellovibrio bacte... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 8cmp | ||||||
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| Title | DNA-binding bacterial histone protein HBB from Bdellovibrio bacteriovorus | ||||||
Components | CBFD_NFYB_HMF domain-containing protein | ||||||
Keywords | DNA BINDING PROTEIN / Bacterial Histone | ||||||
| Function / homology | Transcription factor CBF/NF-Y/archaeal histone domain / Histone-like transcription factor (CBF/NF-Y) and archaeal histone / Histone-fold / protein heterodimerization activity / Transcription factor CBF/NF-Y/archaeal histone domain-containing protein Function and homology information | ||||||
| Biological species | Bdellovibrio bacteriovorus (bacteria) | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.06 Å | ||||||
Authors | Hu, Y. / Joiner, J.D. / Albrecht, R. / Hartmann, M.D. | ||||||
| Funding support | Germany, 1items
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Citation | Journal: Nucleic Acids Res. / Year: 2024Title: Bacterial histone HBb from Bdellovibrio bacteriovorus compacts DNA by bending. Authors: Hu, Y. / Schwab, S. / Deiss, S. / Escudeiro, P. / van Heesch, T. / Joiner, J.D. / Vreede, J. / Hartmann, M.D. / Lupas, A.N. / Alvarez, B.H. / Alva, V. / Dame, R.T. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 8cmp.cif.gz | 36.8 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb8cmp.ent.gz | 23.9 KB | Display | PDB format |
| PDBx/mmJSON format | 8cmp.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 8cmp_validation.pdf.gz | 408.4 KB | Display | wwPDB validaton report |
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| Full document | 8cmp_full_validation.pdf.gz | 408.3 KB | Display | |
| Data in XML | 8cmp_validation.xml.gz | 4.4 KB | Display | |
| Data in CIF | 8cmp_validation.cif.gz | 5.5 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cm/8cmp ftp://data.pdbj.org/pub/pdb/validation_reports/cm/8cmp | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 9ezzC ![]() 9f0eC C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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| 1 | ![]()
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| Unit cell |
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Components
| #1: Protein | Mass: 7189.504 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Bdellovibrio bacteriovorus (bacteria) / Gene: AZI86_06880 / Production host: ![]() |
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| #2: Water | ChemComp-HOH / |
| Has protein modification | N |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 1.8 Å3/Da / Density % sol: 31.78 % |
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| Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / Details: 0.1 M Sodium acetate, pH 4.5 and 25% PEG3350 |
-Data collection
| Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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| Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 1 Å |
| Detector | Type: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Sep 11, 2020 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
| Reflection | Resolution: 1.06→28.2 Å / Num. obs: 23226 / % possible obs: 96.3 % / Redundancy: 10.8 % / CC1/2: 1 / Rrim(I) all: 0.047 / Net I/σ(I): 23.8 |
| Reflection shell | Resolution: 1.06→1.13 Å / Redundancy: 3.88 % / Mean I/σ(I) obs: 1.66 / Num. unique obs: 3028 / CC1/2: 0.688 / Rrim(I) all: 0.921 / % possible all: 79.4 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 1.06→28.19 Å / Cor.coef. Fo:Fc: 0.975 / Cor.coef. Fo:Fc free: 0.971 / SU B: 0.778 / SU ML: 0.017 / Cross valid method: THROUGHOUT / ESU R: 0.025 / ESU R Free: 0.027 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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| Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | Biso mean: 17.722 Å2
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| Refinement step | Cycle: 1 / Resolution: 1.06→28.19 Å
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Bdellovibrio bacteriovorus (bacteria)
X-RAY DIFFRACTION
Germany, 1items
Citation

PDBj



