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- PDB-4v8p: T.thermophila 60S ribosomal subunit in complex with initiation fa... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4v8p | |||||||||
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Title | T.thermophila 60S ribosomal subunit in complex with initiation factor 6. | |||||||||
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![]() | RIBOSOME / EUKARYOTIC INITIATION FACTOR 6 / EIF6 / 60S / TRANSLATION / LARGE RIBOSOMAL SUBUNIT / RRNA / RIBOSOMAL PROTEIN | |||||||||
Function / homology | ![]() ribosomal large subunit binding / protein-RNA complex assembly / translation initiation factor activity / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / cytosolic ribosome assembly / ribosomal large subunit biogenesis / ribosome biogenesis / large ribosomal subunit / 5S rRNA binding / ribosomal large subunit assembly ...ribosomal large subunit binding / protein-RNA complex assembly / translation initiation factor activity / maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) / cytosolic ribosome assembly / ribosomal large subunit biogenesis / ribosome biogenesis / large ribosomal subunit / 5S rRNA binding / ribosomal large subunit assembly / large ribosomal subunit rRNA binding / cytosolic large ribosomal subunit / cytoplasmic translation / tRNA binding / negative regulation of translation / rRNA binding / ribosome / structural constituent of ribosome / translation / ribonucleoprotein complex / mRNA binding / nucleolus / RNA binding / metal ion binding / nucleus / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Klinge, S. / Voigts-Hoffmann, F. / Leibundgut, M. / Arpagaus, S. / Ban, N. | |||||||||
![]() | ![]() Title: Crystal Structure of the Eukaryotic 60S Ribosomal Subunit in Complex with Initiation Factor 6. Authors: Klinge, S. / Voigts-Hoffmann, F. / Leibundgut, M. / Arpagaus, S. / Ban, N. | |||||||||
History |
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Remark 700 | SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "HA" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "HA" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 14.7 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1jj2S 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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Unit cell |
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Components
-RNA chain , 3 types, 12 molecules A1D1F1H1B2C2E2G2B3C3E3G3
#1: RNA chain | Mass: 1084310.250 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #20: RNA chain | Mass: 49800.582 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #21: RNA chain | Mass: 38740.992 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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-RIBOSOMAL PROTEIN ... , 4 types, 16 molecules AADAFAHAAMDMFMHMBBCBEBGBBLCLELGL
#2: Protein | Mass: 10703.564 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #12: Protein | Mass: 13804.006 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #23: Protein | Mass: 44348.539 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #33: Protein | Mass: 24134.201 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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+Protein , 28 types, 108 molecules ABDBFBHBAEDEFEHEAFDFFFHFAGDGFGHGAHDHFHHHAJDJFJHJAKDKFKHKALDL...
-60S RIBOSOMAL PROTEIN ... , 12 types, 48 molecules ACDCFCHCAQDQFQHQBDCDEDGDBECEEEGEBHCHEHGHBICIEIGIBKCKEKGKBMCM...
#4: Protein | Mass: 12786.319 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #16: Protein | Mass: 11703.105 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #25: Protein | Mass: 19754.959 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #26: Protein | Mass: 21373.016 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #29: Protein | Mass: 24511.777 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #30: Protein | Mass: 22641.775 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #32: Protein | Mass: 16662.867 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #34: Protein | Mass: 34525.941 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #37: Protein | Mass: 18164.055 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #43: Protein | Mass: 27670.322 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #44: Protein | Mass: 12990.064 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() #45: Protein | Mass: 15347.117 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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-Non-polymers , 3 types, 6075 molecules 




#48: Chemical | ChemComp-MG / #49: Chemical | ChemComp-ZN / #50: Water | ChemComp-HOH / | |
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-Details
Sequence details | UBIQUITIN FUSION, UBIQUITIN NOT VISIBLE IN STRUCTURE FOR CHAIN K. THE ENTRY 4A18 CONTAINS THE ...UBIQUITIN FUSION, UBIQUITIN NOT VISIBLE IN STRUCTURE FOR CHAIN K. THE ENTRY 4A18 CONTAINS THE PROTEINS THAT ARE DESCRIBED WITH LOWER CASE CHAIN IDS IN THE CITATION. |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.11 Å3/Da / Density % sol: 55 % / Description: NONE |
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Aug 26, 2011 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 3.52→40 Å / Num. obs: 1192534 / % possible obs: 99.3 % / Observed criterion σ(I): -3 / Redundancy: 3.7 % / Biso Wilson estimate: 96.88 Å2 / Rmerge(I) obs: 0.13 / Net I/σ(I): 8.8 |
Reflection shell | Resolution: 3.52→3.72 Å / Redundancy: 3.6 % / Rmerge(I) obs: 0.81 / Mean I/σ(I) obs: 1.6 / % possible all: 99.6 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1JJ2 Resolution: 3.52→19.998 Å / SU ML: 0.89 / σ(F): 1.99 / Phase error: 24.46 / Stereochemistry target values: ML / Details: CHAIN G IS MODELLED AS UNK OF PDB ENTRY 1ZAX
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Solvent computation | Shrinkage radii: 0.16 Å / VDW probe radii: 0.5 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 63.324 Å2 / ksol: 0.316 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 108.2 Å2
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Refinement step | Cycle: LAST / Resolution: 3.52→19.998 Å
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Refine LS restraints |
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LS refinement shell |
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