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Yorodumi- PDB-4v50: Crystal Structure of Ribosome with messenger RNA and the Anticodo... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 4v50 | |||||||||
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| Title | Crystal Structure of Ribosome with messenger RNA and the Anticodon stem-loop of P-site tRNA. | |||||||||
Components |
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Keywords | RIBOSOME / 30S ribosomal subunit / protein-nucleic acid complexes | |||||||||
| Function / homology | Function and homology informationstringent response / ornithine decarboxylase inhibitor activity / transcription antitermination factor activity, RNA binding / misfolded RNA binding / Group I intron splicing / RNA folding / transcriptional attenuation / endoribonuclease inhibitor activity / positive regulation of ribosome biogenesis / RNA-binding transcription regulator activity ...stringent response / ornithine decarboxylase inhibitor activity / transcription antitermination factor activity, RNA binding / misfolded RNA binding / Group I intron splicing / RNA folding / transcriptional attenuation / endoribonuclease inhibitor activity / positive regulation of ribosome biogenesis / RNA-binding transcription regulator activity / translational termination / negative regulation of cytoplasmic translation / four-way junction DNA binding / DnaA-L2 complex / translation repressor activity / regulation of mRNA stability / negative regulation of translational initiation / negative regulation of DNA-templated DNA replication initiation / mRNA regulatory element binding translation repressor activity / positive regulation of RNA splicing / assembly of large subunit precursor of preribosome / cytosolic ribosome assembly / regulation of DNA-templated transcription elongation / response to reactive oxygen species / ribosome assembly / transcription elongation factor complex / DNA endonuclease activity / transcription antitermination / regulation of cell growth / DNA-templated transcription termination / response to radiation / maintenance of translational fidelity / mRNA 5'-UTR binding / regulation of translation / large ribosomal subunit / ribosome biogenesis / ribosome binding / transferase activity / ribosomal small subunit biogenesis / ribosomal small subunit assembly / 5S rRNA binding / ribosomal large subunit assembly / small ribosomal subunit / small ribosomal subunit rRNA binding / large ribosomal subunit rRNA binding / cytosolic small ribosomal subunit / cytosolic large ribosomal subunit / cytoplasmic translation / tRNA binding / negative regulation of translation / rRNA binding / structural constituent of ribosome / ribosome / translation / response to antibiotic / negative regulation of DNA-templated transcription / mRNA binding / DNA binding / RNA binding / zinc ion binding / membrane / cytosol / cytoplasm Similarity search - Function | |||||||||
| Biological species | ![]() | |||||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.22 Å | |||||||||
Authors | Berk, V. / Zhang, W. / Pai, R.D. / Cate, J.H.D. | |||||||||
Citation | Journal: Proc.Natl.Acad.Sci.Usa / Year: 2006Title: Structural basis for mRNA and tRNA positioning on the ribosome. Authors: Berk, V. / Zhang, W. / Pai, R.D. / Cate, J.H.D. | |||||||||
| History |
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| Remark 300 | BIOMOLECULE: 1, 2 THIS ENTRY CONTAINS PART OF THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT. THE BIOLOGICAL ...BIOMOLECULE: 1, 2 THIS ENTRY CONTAINS PART OF THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT. THE BIOLOGICAL UNIT CONSISTS OF TWO SUBUNITS. THERE ARE 2 BIOLOGICAL UNITS IN THE ASYMMETRIC UNIT. | |||||||||
| Remark 400 | COMPOUND THIS FILE, 2I2P, CONTAINS THE 30S SUBUNIT OF ONE 70S RIBOSOME. THE ENTIRE CRYSTAL ...COMPOUND THIS FILE, 2I2P, CONTAINS THE 30S SUBUNIT OF ONE 70S RIBOSOME. THE ENTIRE CRYSTAL STRUCTURE CONTAINS TWO 70S RIBOSOMES AND ARE DEPOSITED UNDER: 70S RIBOSOME ONE: 2I2P (30S SUBUNIT), 2I2T (50S SUBUNIT) 70S RIBOSOME TWO: 2I2U (30S SUBUNIT), 2I2V (50S SUBUNIT) | |||||||||
| Remark 600 | HETEROGEN MO4 38 HAS SQUARE-PLANAR HYDRATION OF MG2+ MO4 10,16,30,31,34,40,43,44,51 HAVE 2 VICINAL ...HETEROGEN MO4 38 HAS SQUARE-PLANAR HYDRATION OF MG2+ MO4 10,16,30,31,34,40,43,44,51 HAVE 2 VICINAL WATERS MISSING FROM HYDRATION OF MG2+ MO3 11,48 HAVE ALL WATER BONDS MUTUALLY ORTHOGONAL TO OTHER MG2+-WATER BONDS MO3 4,9,53,61 HAVE ALL WATERS AND MG2+ IN-PLANE MO2 35 HAS ALL WATERS AND MG2+ ORTHOGONAL |
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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 | 4v50.cif.gz | 6.4 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb4v50.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 4v50.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 4v50_validation.pdf.gz | 1.7 MB | Display | wwPDB validaton report |
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| Full document | 4v50_full_validation.pdf.gz | 3.6 MB | Display | |
| Data in XML | 4v50_validation.xml.gz | 841.3 KB | Display | |
| Data in CIF | 4v50_validation.cif.gz | 1.2 MB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v5/4v50 ftp://data.pdbj.org/pub/pdb/validation_reports/v5/4v50 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 2avy ![]() 2aw4 ![]() 2aw7 ![]() 2awb S: Starting model for refinement |
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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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| 2 | ![]()
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| Unit cell |
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Components
-RNA chain , 5 types, 10 molecules AACAAWCWAXCXBADABBDB
| #1: RNA chain | Mass: 499690.031 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #2: RNA chain | Mass: 5402.276 Da / Num. of mol.: 2 / Source method: obtained synthetically #3: RNA chain | Mass: 1854.118 Da / Num. of mol.: 2 / Source method: obtained synthetically #24: RNA chain | Mass: 38790.090 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #25: RNA chain | Mass: 941612.375 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-30S ribosomal protein ... , 20 types, 40 molecules ABCBACCCADCDAECEAFCFAGCGAHCHAICIAJCJAKCKALCLAMCMANCNAOCOAPCP...
| #4: Protein | Mass: 26650.475 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #5: Protein | Mass: 25900.117 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #6: Protein | Mass: 23383.002 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #7: Protein | Mass: 17498.203 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #8: Protein | Mass: 15727.512 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #9: Protein | Mass: 19923.959 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #10: Protein | Mass: 14015.361 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #11: Protein | Mass: 14755.074 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #12: Protein | Mass: 11755.597 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #13: Protein | Mass: 13739.778 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #14: Protein | Mass: 13636.961 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #15: Protein | Mass: 12997.271 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #16: Protein | Mass: 11475.364 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #17: Protein | Mass: 10188.687 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #18: Protein | Mass: 9207.572 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #19: Protein | Mass: 9593.296 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #20: Protein | Mass: 8874.276 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #21: Protein | Mass: 10324.160 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #22: Protein | Mass: 9577.268 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() #23: Protein | Mass: 8392.844 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() |
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+50S ribosomal protein ... , 29 types, 58 molecules BCDCBDDDBEDEBFDFBGDGBHDHBIDIBJDJBKDKBLDLBMDMBNDNBODOBPDPBQDQ...
-Non-polymers , 3 types, 2065 molecules 




| #55: Chemical | ChemComp-MG / #56: Chemical | #57: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 13 |
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Sample preparation
| Crystal | Density Matthews: 3.62 Å3/Da / Density % sol: 66.04 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Crystal grow | Temperature: 277 K / Method: batch / pH: 7.5 Details: MPD, PEG 8000, MGCL2, NH4CL, SPERMINE, SPERMIDINE, TRIS, EDTA, pH 7.5, batch, temperature 277K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Components of the solutions |
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-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 12.3.1 / Wavelength: 1.116 Å |
| Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Jun 30, 2006 |
| Radiation | Monochromator: double crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 1.116 Å / Relative weight: 1 |
| Reflection | Resolution: 3.22→70 Å / Num. all: 997175 / Num. obs: 753057 / % possible obs: 75.5 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 |
| Reflection shell | Resolution: 3.22→3.26 Å / % possible all: 11.8 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: pdb entries 2AVY, 2AW4, 2AW7, 2AWB Resolution: 3.22→70 Å / FOM work R set: 0.65 / σ(F): 2 / Stereochemistry target values: Engh & Huber
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| Displacement parameters | Biso mean: 105.753 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 3.22→70 Å
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| Refine LS restraints |
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| LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 50
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