+Open data
-Basic information
Entry | Database: PDB / ID: 6l1r | ||||||
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Title | Crystal structure of N-terminal domain of human SSRP1 | ||||||
Components | FACT complex subunit SSRP1FACT (biology) | ||||||
Keywords | CHAPERONE / Histone chaperone | ||||||
Function / homology | Function and homology information FACT complex / regulation of chromatin organization / nucleosome disassembly / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat / Formation of HIV elongation complex in the absence of HIV Tat ...FACT complex / regulation of chromatin organization / nucleosome disassembly / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat / Formation of HIV elongation complex in the absence of HIV Tat / nucleosome binding / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / RNA Polymerase II Pre-transcription Events / TP53 Regulates Transcription of DNA Repair Genes / nucleosome assembly / histone binding / Regulation of TP53 Activity through Phosphorylation / DNA replication / DNA repair / nucleolus / DNA binding / RNA binding / nucleoplasm / nucleus Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 1.79843948699 Å | ||||||
Authors | Li, H.Y. / Hu, T.T. / Dou, Y.S. / Su, D. | ||||||
Funding support | China, 1items
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Citation | Journal: To Be Published Title: Crystal structure of N-terminal domain of human SSRP1 Authors: Li, H.Y. / Hu, T.T. / Dou, Y.S. / Su, D. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6l1r.cif.gz | 40.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6l1r.ent.gz | 24.4 KB | Display | PDB format |
PDBx/mmJSON format | 6l1r.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/l1/6l1r ftp://data.pdbj.org/pub/pdb/validation_reports/l1/6l1r | HTTPS FTP |
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-Related structure data
Related structure data | 4khbS 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
#1: Protein | Mass: 11833.473 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SSRP1, FACT80 / Production host: Escherichia coli (E. coli) / References: UniProt: Q08945 |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.07 Å3/Da / Density % sol: 40.52 % |
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Crystal grow | Temperature: 287 K / Method: vapor diffusion, hanging drop / Details: 30%(w/v) PEG 1500, 40% 1,2-Butanediol |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU MICROMAX-002+ / Wavelength: 1.5418 Å |
Detector | Type: AGILENT EOS CCD / Detector: CCD / Date: May 23, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.798→16.417 Å / Num. obs: 8686 / % possible obs: 95.7 % / Redundancy: 3.4 % / Biso Wilson estimate: 10.7597929655 Å2 / CC1/2: 0.423 / Net I/σ(I): 18.16 |
Reflection shell | Resolution: 1.8→1.88 Å / Num. unique obs: 873 / CC1/2: 0.36 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 4KHB Resolution: 1.79843948699→16.4166396232 Å / SU ML: 0.138150384822 / Cross valid method: FREE R-VALUE / σ(F): 1.38290989401 / Phase error: 20.704718731
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | ||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 15.5626470588 Å2 | ||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.79843948699→16.4166396232 Å
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Refine LS restraints |
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LS refinement shell |
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