[English] 日本語
Yorodumi- PDB-6n1d: X-ray Crystal complex showing Spontaneous Ribosomal Translocation... -
+Open data
-Basic information
Entry | Database: PDB / ID: 6n1d | |||||||||
---|---|---|---|---|---|---|---|---|---|---|
Title | X-ray Crystal complex showing Spontaneous Ribosomal Translocation of mRNA and tRNAs into a Chimeric Hybrid State | |||||||||
Components |
| |||||||||
Keywords | RIBOSOME | |||||||||
Function / homology | Function and homology information large ribosomal subunit / regulation of translation / ribosomal small subunit assembly / large ribosomal subunit rRNA binding / 5S rRNA binding / transferase activity / small ribosomal subunit / cytosolic small ribosomal subunit / ribosomal large subunit assembly / cytosolic large ribosomal subunit ...large ribosomal subunit / regulation of translation / ribosomal small subunit assembly / large ribosomal subunit rRNA binding / 5S rRNA binding / transferase activity / small ribosomal subunit / cytosolic small ribosomal subunit / ribosomal large subunit assembly / cytosolic large ribosomal subunit / 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 | Thermus thermophilus HB27 (bacteria) Thermus thermophilus (bacteria) Escherichia coli (E. coli) synthetic construct (others) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.2 Å | |||||||||
Authors | Noller, H.F. / Donohue, J.P. / Lancaster, L. / Zhou, J. | |||||||||
Funding support | United States, 1items
| |||||||||
Citation | Journal: Proc. Natl. Acad. Sci. U.S.A. / Year: 2019 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 |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 6n1d.cif.gz | 7.4 MB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb6n1d.ent.gz | Display | PDB format | |
PDBx/mmJSON format | 6n1d.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6n1d_validation.pdf.gz | 1.5 MB | Display | wwPDB validaton report |
---|---|---|---|---|
Full document | 6n1d_full_validation.pdf.gz | 1.9 MB | Display | |
Data in XML | 6n1d_validation.xml.gz | 569.4 KB | Display | |
Data in CIF | 6n1d_validation.cif.gz | 864.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/n1/6n1d ftp://data.pdbj.org/pub/pdb/validation_reports/n1/6n1d | HTTPS FTP |
-Related structure data
Related structure data | 4v67S S: Starting model for refinement |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||||||
2 |
| ||||||||||||
Unit cell |
|
-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) Thermus thermophilus HB27 (bacteria) / References: GenBank: 46197919 #2: RNA chain | Mass: 937014.688 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus HB27 (bacteria) / Strain: HB27 / ATCC BAA-163 / DSM 7039 #3: RNA chain | Mass: 38553.000 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus HB27 (bacteria) / References: GenBank: 46197919 #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) Escherichia coli (E. coli) #56: RNA chain | | Mass: 27544.652 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) Escherichia coli (E. coli) |
---|
+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) Thermus thermophilus HB27 (bacteria) / References: UniProt: P62662 #37: Protein | Mass: 26619.881 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus HB27 (bacteria) / References: UniProt: P62663 #38: Protein | Mass: 24242.254 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) (bacteria) 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) Thermus thermophilus HB27 (bacteria) / References: UniProt: P62665 #40: Protein | Mass: 11988.753 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) (bacteria) 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) Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) (bacteria) 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) Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) (bacteria) 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) Thermus thermophilus HB27 (bacteria) / References: UniProt: P62669 #44: Protein | Mass: 11823.772 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus HB27 (bacteria) / References: UniProt: P62653 #45: Protein | Mass: 13606.672 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus HB27 (bacteria) / References: UniProt: P62654 #46: Protein | Mass: 14506.188 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus HB27 (bacteria) / References: UniProt: P61941 #47: Protein | Mass: 14207.666 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus HB27 (bacteria) / References: UniProt: P62655 #48: Protein | Mass: 7027.529 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) (bacteria) 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) Thermus thermophilus (strain HB27 / ATCC BAA-163 / DSM 7039) (bacteria) 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) Thermus thermophilus HB27 (bacteria) / References: UniProt: P62238 #51: Protein | Mass: 12193.475 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus HB27 (bacteria) / References: UniProt: P62658 #52: Protein | Mass: 10127.102 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus HB27 (bacteria) / References: UniProt: P62659 #53: Protein | Mass: 10474.269 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus HB27 (bacteria) / References: UniProt: P62660 #54: Protein | Mass: 11590.920 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus HB27 (bacteria) / References: UniProt: P62661 #55: Protein/peptide | Mass: 3218.835 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Thermus thermophilus HB27 (bacteria) / References: UniProt: P62613 |
---|
-Non-polymers , 2 types, 361 molecules
#57: Chemical | ChemComp-MG / #58: Chemical | |
---|
-Details
Has protein modification | Y |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 3.23 Å3/Da / Density % sol: 61.87 % |
---|---|
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 |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 23-ID-D / Wavelength: 1.03315 Å |
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 |
-Processing
Software |
| ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT 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
| ||||||||||||||||||||
Solvent computation | VDW probe radii: 1.11 Å | ||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.2→100 Å
| ||||||||||||||||||||
LS refinement shell | Resolution: 3.2→3.3 Å
|