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Open data
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Basic information
Entry | Database: PDB / ID: 1cn7 | |||||||||
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Title | Yeast ribosomal protein L30 | |||||||||
![]() | 60S RIBOSOMAL PROTEIN L30E | |||||||||
![]() | RIBOSOME / RIBOSOMAL PROTEIN / AUTO-REGULATION OF PRE-MRNA SPLICING AND MRNA TRANSLATION | |||||||||
Function / homology | ![]() pre-mRNA 5'-splice site binding / SRP-dependent cotranslational protein targeting to membrane / GTP hydrolysis and joining of the 60S ribosomal subunit / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / negative regulation of mRNA splicing, via spliceosome / Formation of a pool of free 40S subunits / L13a-mediated translational silencing of Ceruloplasmin expression / rRNA processing / cytosolic large ribosomal subunit ...pre-mRNA 5'-splice site binding / SRP-dependent cotranslational protein targeting to membrane / GTP hydrolysis and joining of the 60S ribosomal subunit / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / negative regulation of mRNA splicing, via spliceosome / Formation of a pool of free 40S subunits / L13a-mediated translational silencing of Ceruloplasmin expression / rRNA processing / cytosolic large ribosomal subunit / cytoplasmic translation / structural constituent of ribosome / RNA binding / cytosol / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | SOLUTION NMR / SIMULATED ANNEALING, MOLECULAR DYNAMIC | |||||||||
![]() | Mao, H. / Willamson, J.R. | |||||||||
![]() | ![]() Title: Local folding coupled to RNA binding in the yeast ribosomal protein L30. Authors: Mao, H. / Williamson, J.R. #1: ![]() Title: The Yeast Ribosomal Protein L32 and its Gene Authors: Dabeva, M.D. / Warner, J.R. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 645 KB | Display | ![]() |
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PDB format | ![]() | 537.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
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-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 11299.168 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Description: RECOMBINANT EXPRESSION AS A C-TERMINAL MALTOSE-BINDING PROTEIN FUSION IN ESCHERICHIA COLI STRAIN JM109 HOSTING PLASMID PMALC-30 Cellular location: CYTOPLASM / Gene: RPL30 / Organelle: RIBOSOME,60S SUBUNIT / Plasmid: PMALC-L30 / Cellular location (production host): CYTOPLASM / Gene (production host): L30 / Production host: ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: THIS STRUCTURE WAS DETERMINED USING TRIPLE-RESONANCE NMR SPECTROSCOPY ON 13C, 15N-LABELED L30 PROTEIN. |
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Sample preparation
Details | Contents: 10% WATER/90% D2O |
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Sample conditions | Ionic strength: 300 mM / pH: 6.5 / Pressure: 1 atm / Temperature: 283 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: SIMULATED ANNEALING, MOLECULAR DYNAMIC / Software ordinal: 1 Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE. DISTANCE INTRARESIDUE NOES 720;INTERRESIDUE NOES 698 SEQUENTIAL (|I-J|=1) 291; SHORT- RANGE (|I-J|4) 258; HYDROGEN BONDS 62; TOTAL ...Details: REFINEMENT DETAILS CAN BE FOUND IN THE JRNL CITATION ABOVE. DISTANCE INTRARESIDUE NOES 720;INTERRESIDUE NOES 698 SEQUENTIAL (|I-J|=1) 291; SHORT- RANGE (|I-J|<=4) 149;LONG-RANGE (|I-J|>4) 258; HYDROGEN BONDS 62; TOTAL 1418 TORSION BACKBONE PHI 80; SIDECHAIN KAI1 59; TOTAL 139 | ||||||||||||
NMR ensemble | Conformer selection criteria: LOWEST TOTAL ENERGY / Conformers calculated total number: 50 / Conformers submitted total number: 20 |