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- PDB-6n1d: X-ray Crystal complex showing Spontaneous Ribosomal Translocation... -
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Open data
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Basic information
Entry | Database: PDB / ID: 6n1d | |||||||||
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Title | X-ray Crystal complex showing Spontaneous Ribosomal Translocation of mRNA and tRNAs into a Chimeric Hybrid State | |||||||||
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![]() | RIBOSOME | |||||||||
Function / homology | ![]() regulation of translation / large ribosomal subunit / transferase activity / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / small ribosomal subunit rRNA binding / 5S rRNA binding / ribosomal large subunit assembly / cytosolic small ribosomal subunit ...regulation of translation / large ribosomal subunit / transferase activity / ribosomal small subunit biogenesis / ribosomal small subunit assembly / small ribosomal subunit / small ribosomal subunit rRNA binding / 5S rRNA binding / ribosomal large subunit assembly / cytosolic small ribosomal subunit / 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 / zinc ion binding / metal ion binding / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() ![]() ![]() ![]() ![]() ![]() synthetic construct (others) | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Noller, H.F. / Donohue, J.P. / Lancaster, L. / Zhou, J. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Spontaneous ribosomal translocation of mRNA and tRNAs into a chimeric hybrid state. Authors: Zhou, J. / Lancaster, L. / Donohue, J.P. / Noller, H.F. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 7.4 MB | Display | ![]() |
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PDB format | ![]() | Display | ![]() | |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.5 MB | Display | ![]() |
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Full document | ![]() | 1.9 MB | Display | |
Data in XML | ![]() | 569.4 KB | Display | |
Data in CIF | ![]() | 864.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4v67S 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 , 6 types, 11 molecules A16SB16SA23SB23SA5SB5SAMRNBMRNAPTNBPTNBATN
#1: RNA chain | Mass: 492773.656 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#2: RNA chain | Mass: 937014.688 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#3: RNA chain | Mass: 38553.000 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#34: RNA chain | Mass: 5562.422 Da / Num. of mol.: 2 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
#35: RNA chain | Mass: 24616.760 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#56: RNA chain | Mass: 27544.652 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
+50S ribosomal protein ... , 30 types, 60 molecules AL01BL01AL02BL02AL03BL03AL04BL04AL05BL05AL06BL06AL09BL09AL13BL13AL14BL14AL15BL15AL16BL16AL17BL17AL18BL18AL19BL19AL20BL20...
-30S ribosomal protein ... , 20 types, 40 molecules AS02BS02AS03BS03AS04BS04AS05BS05AS06BS06AS07BS07AS08BS08AS09BS09AS10BS10AS11BS11AS12BS12AS13BS13AS14BS14AS15BS15AS16BS16...
#36: Protein | Mass: 29186.506 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
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#37: Protein | Mass: 26619.881 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#38: Protein | Mass: 24242.254 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() ![]() Strain: HB27 / ATCC BAA-163 / DSM 7039 / References: UniProt: P62664 |
#39: Protein | Mass: 17452.221 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#40: Protein | Mass: 11988.753 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() ![]() Strain: HB27 / ATCC BAA-163 / DSM 7039 / References: UniProt: P62666 |
#41: Protein | Mass: 17919.775 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() ![]() Strain: HB27 / ATCC BAA-163 / DSM 7039 / References: UniProt: P62667 |
#42: Protein | Mass: 15868.570 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() ![]() Strain: HB27 / ATCC BAA-163 / DSM 7039 / References: UniProt: P62668 |
#43: Protein | Mass: 14429.661 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#44: Protein | Mass: 11823.772 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#45: Protein | Mass: 13606.672 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#46: Protein | Mass: 14506.188 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#47: Protein | Mass: 14207.666 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#48: Protein | Mass: 7027.529 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() ![]() Strain: HB27 / ATCC BAA-163 / DSM 7039 / References: UniProt: P62656 |
#49: Protein | Mass: 10447.213 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() ![]() Strain: HB27 / ATCC BAA-163 / DSM 7039 / References: UniProt: P62657 |
#50: Protein | Mass: 10409.983 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#51: Protein | Mass: 12193.475 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#52: Protein | Mass: 10127.102 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#53: Protein | Mass: 10474.269 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#54: Protein | Mass: 11590.920 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
#55: Protein/peptide | Mass: 3218.835 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() |
-Non-polymers , 2 types, 361 molecules 


#57: Chemical | ChemComp-MG / |
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#58: Chemical |
-Details
Has protein modification | Y |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.23 Å3/Da / Density % sol: 61.87 % |
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Crystal grow | Temperature: 295 K / Method: liquid diffusion / pH: 7 Details: pH 7, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Nov 3, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.03315 Å / Relative weight: 1 |
Reflection | Resolution: 3.2→100 Å / Num. obs: 874708 / % possible obs: 95.5 % / Redundancy: 2.87 % / CC1/2: 0.987 / Rrim(I) all: 0.309 / Rsym value: 0.278 / Net I/av σ(I): 3.94 / Net I/σ(I): 3.94 |
Reflection shell | Resolution: 3.2→3.3 Å / Redundancy: 2.49 % / Mean I/σ(I) obs: 0.82 / CC1/2: 0.182 / % possible all: 95 |
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Processing
Software |
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Refinement | Method to determine structure: ![]() Starting model: 4V67 Resolution: 3.2→100 Å / SU ML: 0.59 / Data cutoff low absF: 1.34 / Cross valid method: FREE R-VALUE / Phase error: 34.93
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Solvent computation | VDW probe radii: 1.11 Å | ||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.2→100 Å
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LS refinement shell | Resolution: 3.2→3.3 Å
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