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Yorodumi- PDB-4v4g: Crystal structure of five 70s ribosomes from Escherichia Coli in ... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 4v4g | |||||||||
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| Title | Crystal structure of five 70s ribosomes from Escherichia Coli in complex with protein Y. | |||||||||
Components |
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Keywords | RIBOSOME / 30S RIBOSOMAL SUBUNIT / PROTEIN-RNA COMPLEX / PROTEIN-PROTEIN COMPLEX / RNA-RNA COMPLEX | |||||||||
| Function / homology | RNA / RNA (> 10) / RNA (> 100) / RNA (> 1000) Function and homology information | |||||||||
| Biological species | ![]() | |||||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 11.5 Å | |||||||||
Authors | Vila-Sanjurjo, A. / Schuwirth, B.S. / Hau, C.W. / Cate, J.H. | |||||||||
Citation | Journal: Nat.Struct.Mol.Biol. / Year: 2004Title: Structural basis for the control of translation initiation during stress. Authors: Vila-Sanjurjo, A. / Schuwirth, B.S. / Hau, C.W. / Cate, J.H. | |||||||||
| History |
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| Remark 400 | COMPOUND THIS FILE, 1VOQ, CONTAINS THE 30S SUBUNIT OF ONE 70S RIBOSOME. THE ENTIRE CRYSTAL ...COMPOUND THIS FILE, 1VOQ, CONTAINS THE 30S SUBUNIT OF ONE 70S RIBOSOME. THE ENTIRE CRYSTAL STRUCTURE CONTAINS FIVE 70S RIBOSOMES AND ARE DEPOSITED UNDER: 70S RIBOSOME ONE: 1VOQ (30S SUBUNIT), 1VOR (50S SUBUNIT) 70S RIBOSOME TWO: 1VOS (30S SUBUNIT), 1VOU (50S SUBUNIT) 70S RIBOSOME THREE: 1VOV (30S SUBUNIT), 1VOW (50S SUBUNIT) 70S RIBOSOME FOUR: 1VOX (30S SUBUNIT), 1VOY (50S SUBUNIT) 70S RIBOSOME FIVE: 1VOZ (30S SUBUNIT), 1VP0 (50S SUBUNIT) | |||||||||
| Remark 999 | SEQUENCE The 30S subunit is modelled based on 1PNS which are derived mainly from 1J5E, the T. ...SEQUENCE The 30S subunit is modelled based on 1PNS which are derived mainly from 1J5E, the T. thermophilus 30S subunit, with modifications to the rRNA to make it match E. coli insertions and deletions. The sequence of this subunit represent that of pdb entry, 1J5E. As a result, no dbref was provided. Some residues are not at link distance. Distance of O3*-P bond is 3.20 for residue (A A 919 ) and residue (A U 920 ). Distance of O3*-P bond is 3.21 for residue (A U 1393 ) and residue (A A 1394 ). Distance of O3*-P bond is 5.27 for residue (A G 1443 ) and residue (A U 1445 ). Distance of O3*-P bond is 6.64 for residue (A G 1458 ) and residue (A A 1460 ). Distance of C-N bond is 5.58 for residue (L SER 22 ) and residue (L LYS 23 ). Distance of C-N bond is 4.55 for residue (M GLY 89 ) and residue (M LEU 90 ). The short contacts listed at remark 500 may not be complete since this file only represents one tenth of the entire crystal structure. |
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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 | 4v4g.cif.gz | 15.4 MB | Display | PDBx/mmCIF format |
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| PDB format | pdb4v4g.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 4v4g.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 4v4g_validation.pdf.gz | 2.7 MB | Display | wwPDB validaton report |
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| Full document | 4v4g_full_validation.pdf.gz | 9.9 MB | Display | |
| Data in XML | 4v4g_validation.xml.gz | 1.9 MB | Display | |
| Data in CIF | 4v4g_validation.cif.gz | 2.7 MB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v4/4v4g ftp://data.pdbj.org/pub/pdb/validation_reports/v4/4v4g | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 1pns ![]() 1pnu 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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| 3 | ![]()
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| 4 | ![]()
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| 5 | ![]()
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| Unit cell |
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Components
-RNA chain , 3 types, 15 molecules AACAEAGAIABBDBFBHBJBBADAFAHAJA
| #1: RNA chain | Mass: 495435.469 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) ![]() #22: RNA chain | Mass: 915854.875 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) ![]() #23: RNA chain | Mass: 38374.984 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-30S ribosomal protein ... , 19 types, 95 molecules ABCBEBGBIBACCCECGCICADCDEDGDIDAECEEEGEIEAFCFEFGFIFAGCGEGGGIG...
| #2: Protein | Mass: 26987.271 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) ![]() #3: Protein | Mass: 22862.430 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) ![]() #4: Protein | Mass: 24242.254 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) ![]() #5: Protein | Mass: 16331.079 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) ![]() #6: Protein | Mass: 11988.753 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) ![]() #7: Protein | Mass: 17919.775 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) ![]() #8: Protein | Mass: 15868.570 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) ![]() #9: Protein | Mass: 14298.466 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) ![]() #10: Protein | Mass: 11299.176 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) ![]() #11: Protein | Mass: 12606.369 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) ![]() #12: Protein | Mass: 13804.311 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) ![]() #13: Protein | Mass: 14207.666 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) ![]() #14: Protein | Mass: 7027.529 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) ![]() #15: Protein | Mass: 10447.213 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) ![]() #16: Protein | Mass: 9924.469 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) ![]() #17: Protein | Mass: 12193.475 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) ![]() #18: Protein | Mass: 8483.172 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) ![]() #19: Protein | Mass: 9203.743 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) ![]() #20: Protein | Mass: 10907.060 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) ![]() |
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-Protein , 2 types, 10 molecules AaCaEaGaIaBWDWFWHWJW
| #21: Protein | Mass: 10250.834 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) ![]() #43: Protein | Mass: 18929.711 Da / Num. of mol.: 5 / Source method: isolated from a natural source / Source: (natural) ![]() |
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+50S ribosomal protein ... , 29 types, 145 molecules BDDDFDHDJDBEDEFEHEJEBFDFFFHFJFBGDGFGHGJGBHDHFHHHJHBIDIFIHIJI...
-Details
| Has protein modification | Y |
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-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 3 |
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Sample preparation
| Crystal | Density Matthews: 5.38 Å3/Da / Density % sol: 77.12 % | ||||||||||||||||||||||||||||||||||||||||||||
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| Crystal grow | pH: 6.5 Details: 18-22% 2-methyl-2,4-pentanediol (MPD), 0-5% ethanol, 20-25mM MgCl2, 200-320mM NH4Cl, 1mM spermine, 0-0.5mM spermidine, pH 6.0-6.5, pH 6.50 | ||||||||||||||||||||||||||||||||||||||||||||
| Components of the solutions |
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-Data collection
| Diffraction |
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| Detector |
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| Radiation | Monochromator: SI 111 / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||
| Radiation wavelength |
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| Reflection | Resolution: 11.5→500 Å / Num. obs: 62383 / % possible obs: 93.9 % / Observed criterion σ(I): -3 / Redundancy: 6.1 % / Rsym value: 0.181 / Net I/σ(I): 7.4 | ||||||||||||||||||||
| Reflection shell | Resolution: 11.5→11.8 Å / Redundancy: 2.6 % / Mean I/σ(I) obs: 2 / Rsym value: 0.462 / % possible all: 77.9 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: PDB ENTRIES 1PNS, 1PNU Resolution: 11.5→500 Å / Isotropic thermal model: ANISOTROPIC / Cross valid method: THROUGHOUT / σ(F): 0 Details: 235 RIGID BODIES REFINEMENT, GROUPED THIS ENTRY. COORDINATES USED FOR SOLVING AND REFINING THIS SUBUNIT COMES FROM PDB ENTRY, 1PNS, WHERE THE SEQUENCE REPRESENTS THAT OF T. THERMOPHILUS.
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| Refinement step | Cycle: LAST / Resolution: 11.5→500 Å
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