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Yorodumi- PDB-2bti: Structure-function studies of the RmsA CsrA post-transcriptional ... -
+Open data
-Basic information
Entry | Database: PDB / ID: 2bti | ||||||
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Title | Structure-function studies of the RmsA CsrA post-transcriptional global regulator protein family reveals a class of RNA-binding structure | ||||||
Components | CARBON STORAGE REGULATOR HOMOLOG | ||||||
Keywords | RNA BINDING PROTEIN / RMSA / CSRA | ||||||
Function / homology | Function and homology information regulation of carbohydrate metabolic process / mRNA catabolic process / positive regulation of translational initiation / negative regulation of translational initiation / mRNA 5'-UTR binding / cytoplasm Similarity search - Function | ||||||
Biological species | YERSINIA ENTEROCOLITICA (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MAD / Resolution: 2 Å | ||||||
Authors | Heeb, S. / Kuehne, S.A. / Bycroft, M. / Crivii, S. / Allen, M.D. / Haas, D. / Camara, M. / Williams, P. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2006 Title: Functional Analysis of the Post-Transcriptional Regulator Rsma Reveals a Novel RNA-Binding Site. Authors: Heeb, S. / Kuehne, S.A. / Bycroft, M. / Crivii, S. / Allen, M.D. / Haas, D. / Camara, M. / Williams, P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2bti.cif.gz | 31.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2bti.ent.gz | 24.3 KB | Display | PDB format |
PDBx/mmJSON format | 2bti.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2bti_validation.pdf.gz | 452.7 KB | Display | wwPDB validaton report |
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Full document | 2bti_full_validation.pdf.gz | 453.6 KB | Display | |
Data in XML | 2bti_validation.xml.gz | 7.3 KB | Display | |
Data in CIF | 2bti_validation.cif.gz | 9.1 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bt/2bti ftp://data.pdbj.org/pub/pdb/validation_reports/bt/2bti | HTTPS FTP |
-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 7085.812 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) YERSINIA ENTEROCOLITICA (bacteria) / Production host: ESCHERICHIA COLI BL21(DE3) (bacteria) / Variant (production host): C41 / References: UniProt: A1JK11*PLUS #2: Chemical | ChemComp-SO4 / | #3: Chemical | ChemComp-ACT / | #4: Water | ChemComp-HOH / | Sequence details | THE GENOMIC SEQUENCE FOR THIS ORGANISM ARE NOT YET PUBLISHED OR IN THE NCBI DATABASES, BUT CAN BE ...THE GENOMIC SEQUENCE FOR THIS ORGANISM ARE NOT YET PUBLISHED OR IN THE NCBI DATABASES, BUT CAN BE RETRIEVED FROM THE SANGER INSTITUTE. HTTP://WWW.SANGER.AC.UK/PROJECTS/Y_ENTEROCOLI | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.35 Å3/Da / Density % sol: 48 % |
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Crystal grow | pH: 4.6 Details: 0.16M AMMONIUM SULPHATE, 0.08M SODIUM ACETATE PH 4.6, 20% PEG 4000, 20% GLYCEROL, 10 MG/ML PROTEIN |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 0.979 |
Radiation | Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.979 Å / Relative weight: 1 |
Reflection | Resolution: 2→26.5 Å / Num. obs: 9675 / % possible obs: 98.4 % / Observed criterion σ(I): 1.5 / Redundancy: 6 % / Rmerge(I) obs: 0.09 / Net I/σ(I): 14.8 |
Reflection shell | Resolution: 2→2.1 Å / Redundancy: 5.4 % / Rmerge(I) obs: 0.3 / Mean I/σ(I) obs: 4.5 / % possible all: 95.1 |
-Processing
Software |
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Refinement | Method to determine structure: MAD / Resolution: 2→100 Å / Data cutoff high absF: 10000 / Cross valid method: THROUGHOUT / σ(F): 4.6
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Solvent computation | Bsol: 48.383 Å2 / ksol: 0.383018 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 2→100 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2→2.1 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Xplor file |
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