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Yorodumi- PDB-4a3f: RNA Polymerase II initial transcribing complex with a 6nt DNA-RNA... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 4a3f | ||||||
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| Title | RNA Polymerase II initial transcribing complex with a 6nt DNA-RNA hybrid and soaked with AMPCPP | ||||||
 Components | 
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 Keywords | TRANSCRIPTION / TRANSCRIPTION INITIATION | ||||||
| Function / homology |  Function and homology informationRPB4-RPB7 complex / nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / RNA Polymerase I Transcription Initiation / Processing of Capped Intron-Containing Pre-mRNA / RNA Polymerase III Transcription Initiation From Type 2 Promoter / RNA Pol II CTD phosphorylation and interaction with CE / Formation of the Early Elongation Complex / mRNA Capping / RNA polymerase II transcribes snRNA genes / termination of RNA polymerase II transcription ...RPB4-RPB7 complex / nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay / RNA Polymerase I Transcription Initiation / Processing of Capped Intron-Containing Pre-mRNA / RNA Polymerase III Transcription Initiation From Type 2 Promoter / RNA Pol II CTD phosphorylation and interaction with CE / Formation of the Early Elongation Complex / mRNA Capping / RNA polymerase II transcribes snRNA genes / termination of RNA polymerase II transcription / TP53 Regulates Transcription of DNA Repair Genes / RNA Polymerase II Promoter Escape / RNA Polymerase II Transcription Pre-Initiation And Promoter Opening / RNA Polymerase II Transcription Initiation / RNA Polymerase II Transcription Initiation And Promoter Clearance / termination of RNA polymerase III transcription / RNA Polymerase II Pre-transcription Events / RNA-templated transcription / positive regulation of nuclear-transcribed mRNA poly(A) tail shortening / Formation of TC-NER Pre-Incision Complex / transcription initiation at RNA polymerase III promoter / RNA Polymerase I Promoter Escape / termination of RNA polymerase I transcription / nucleolar large rRNA transcription by RNA polymerase I / Gap-filling DNA repair synthesis and ligation in TC-NER / transcription initiation at RNA polymerase I promoter / Estrogen-dependent gene expression / maintenance of transcriptional fidelity during transcription elongation by RNA polymerase II / nuclear-transcribed mRNA catabolic process / transcription by RNA polymerase III / positive regulation of translational initiation / Dual incision in TC-NER / translesion synthesis / RNA polymerase I complex / transcription elongation by RNA polymerase I / RNA polymerase III complex / RNA polymerase II, core complex / tRNA transcription by RNA polymerase III / transcription by RNA polymerase I / translation initiation factor binding / transcription-coupled nucleotide-excision repair / transcription initiation at RNA polymerase II promoter / transcription elongation by RNA polymerase II / P-body / DNA-templated transcription initiation / ribonucleoside binding / mRNA processing / DNA-directed RNA polymerase / cytoplasmic stress granule / DNA-directed RNA polymerase activity / peroxisome / ribosome biogenesis / single-stranded DNA binding / nucleic acid binding / transcription by RNA polymerase II / single-stranded RNA binding / protein dimerization activity / nucleotide binding / mRNA binding / nucleolus / mitochondrion / DNA binding / zinc ion binding / nucleoplasm / metal ion binding / nucleus / cytoplasm Similarity search - Function  | ||||||
| Biological species | ![]()  | ||||||
| Method |  X-RAY DIFFRACTION /  SYNCHROTRON /  MOLECULAR REPLACEMENT / Resolution: 3.5 Å  | ||||||
 Authors | Cheung, A.C.M. / Sainsbury, S. / Cramer, P. | ||||||
 Citation |  Journal: EMBO J. / Year: 2011Title: Structural basis of initial RNA polymerase II transcription. Authors: Cheung, A.C. / Sainsbury, S. / Cramer, P.  | ||||||
| History | 
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| Remark 700 | SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AG" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AG" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN -2-STRANDED BARREL THIS IS REPRESENTED BY A -1-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. THE SHEETS PRESENTED AS "GA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN -1-STRANDED BARREL THIS IS REPRESENTED BY A 0-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. | 
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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 |  4a3f.cif.gz | 1.6 MB | Display |  PDBx/mmCIF format | 
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| PDB format |  pdb4a3f.ent.gz | 1.3 MB | Display |  PDB format | 
| PDBx/mmJSON format |  4a3f.json.gz | Tree view |  PDBx/mmJSON format | |
| Others |  Other downloads | 
-Validation report
| Summary document |  4a3f_validation.pdf.gz | 889.5 KB | Display |  wwPDB validaton report | 
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| Full document |  4a3f_full_validation.pdf.gz | 983.4 KB | Display | |
| Data in XML |  4a3f_validation.xml.gz | 135.2 KB | Display | |
| Data in CIF |  4a3f_validation.cif.gz | 187.2 KB | Display | |
| Arichive directory |  https://data.pdbj.org/pub/pdb/validation_reports/a3/4a3f ftp://data.pdbj.org/pub/pdb/validation_reports/a3/4a3f | HTTPS FTP  | 
-Related structure data
| Related structure data | ![]() 4a3bC ![]() 4a3cC ![]() 4a3dC ![]() 4a3eC ![]() 4a3gC ![]() 4a3iC ![]() 4a3jC ![]() 4a3kC ![]() 4a3lC ![]() 4a3mC C: citing same article (  | 
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| Similar structure data | 
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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
-DNA-DIRECTED RNA POLYMERASE II SUBUNIT  ... , 6 types, 6 molecules ABCDIK     
| #1: Protein |   Mass: 191664.391 Da / Num. of mol.: 1 / Fragment: RESIDUES 1-1732 / Source method: isolated from a natural source / Source: (natural)  ![]()  | 
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| #2: Protein |   Mass: 138937.297 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)  ![]()  | 
| #3: Protein |   Mass: 35330.457 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)  ![]()  | 
| #4: Protein |   Mass: 25451.191 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)  ![]()  | 
| #9: Protein |   Mass: 14308.161 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)  ![]()  | 
| #11: Protein |   Mass: 13633.493 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)  ![]()  | 
-DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC  ... , 5 types, 5 molecules EFHJL    
| #5: Protein |   Mass: 25117.094 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)  ![]()  | 
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| #6: Protein |   Mass: 17931.834 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)  ![]()  | 
| #8: Protein |   Mass: 16525.363 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)  ![]()  | 
| #10: Protein |   Mass: 8290.732 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)  ![]()  | 
| #12: Protein |   Mass: 7729.969 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)  ![]()  | 
-DNA chain , 2 types, 2 molecules NT 
| #13: DNA chain |   Mass: 4294.814 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.)  ![]()  | 
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| #15: DNA chain |   Mass: 7983.981 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.)  ![]()  | 
-Protein / RNA chain , 2 types, 2 molecules GP 
| #14: RNA chain |   Mass: 1914.229 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.)  ![]()  | 
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| #7: Protein |   Mass: 19081.053 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural)  ![]()  | 
-Non-polymers , 3 types, 10 molecules 




| #16: Chemical |  ChemComp-APC /  | ||
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| #17: Chemical | ChemComp-ZN / #18: Chemical |  ChemComp-MG /  |  | 
-Experimental details
-Experiment
| Experiment | Method:  X-RAY DIFFRACTION / Number of used crystals: 1  | 
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Sample preparation
| Crystal | Density Matthews: 6.89 Å3/Da / Density % sol: 82 % / Description: NONE | 
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| Crystal grow | Method: vapor diffusion, hanging drop / pH: 7 / Details: pH 7 | 
-Data collection
| Diffraction | Mean temperature: 100 K | 
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| Diffraction source | Source:  SYNCHROTRON / Site:  SLS   / Beamline: X06SA / Wavelength: 0.9188  | 
| Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL | 
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | 
| Radiation wavelength | Wavelength: 0.9188 Å / Relative weight: 1 | 
| Reflection | Resolution: 3.5→50 Å / Num. obs: 151373 / % possible obs: 90 % / Observed criterion σ(I): 2.1 / Redundancy: 3 % / Biso Wilson estimate: 83.13 Å2 / Rmerge(I) obs: 0.68 / Net I/σ(I): 8 | 
| Reflection shell | Resolution: 3.5→3.59 Å | 
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Processing
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| Refinement | Method to determine structure:  MOLECULAR REPLACEMENT / Resolution: 3.5→49.89 Å / Cor.coef. Fo:Fc: 0.9462  / Cor.coef. Fo:Fc free: 0.9278  / SU R Cruickshank DPI: 0.642  / Cross valid method: THROUGHOUT / σ(F): 0  / SU R Blow DPI: 0.563  / SU Rfree Blow DPI: 0.288  / SU Rfree Cruickshank DPI: 0.299 
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| Displacement parameters | Biso  mean: 124.59 Å2
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| Refine analyze | Luzzati coordinate error obs: 0.754 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 3.5→49.89 Å
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| Refine LS restraints | 
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| LS refinement shell | Resolution: 3.5→3.59 Å / Total num. of bins used: 20 
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| Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION 
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| Refinement TLS group | 
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