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Yorodumi- PDB-1dz5: The NMR structure of the 38KDa U1A protein-PIE RNA complex reveal... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1dz5 | ||||||
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Title | The NMR structure of the 38KDa U1A protein-PIE RNA complex reveals the basis of cooperativity in regulation of polyadenylation by human U1A protein | ||||||
Components |
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Keywords | RIBONUCLEOPROTEIN/RNA / RIBONUCLEOPROTEIN-RNA COMPLEX / POLYADENYLATION / PROTEIN PROTEIN INTERACTION / RNA PROTEIN INTERACTION | ||||||
Function / homology | Function and homology information U1 snRNP binding / U1 snRNP / U1 snRNA binding / U4/U6 x U5 tri-snRNP complex / mRNA Splicing - Major Pathway / spliceosomal complex / mRNA splicing, via spliceosome / DNA binding / RNA binding / nucleoplasm ...U1 snRNP binding / U1 snRNP / U1 snRNA binding / U4/U6 x U5 tri-snRNP complex / mRNA Splicing - Major Pathway / spliceosomal complex / mRNA splicing, via spliceosome / DNA binding / RNA binding / nucleoplasm / identical protein binding / nucleus Similarity search - Function | ||||||
Biological species | HOMO SAPIENS (human) | ||||||
Method | SOLUTION NMR / RESTRAINED MOLECULAR DYNAMICS | ||||||
Authors | Varani, L. / Gunderson, S.I. / Mattaj, I.W. / Kay, L.E. / Neuhaus, D. / Varani, G. | ||||||
Citation | Journal: Nat.Struct.Biol. / Year: 2000 Title: The NMR Structure of the 38kDa U1A Protein-Pie RNA Complex Reveals the Basis of Cooperativity in Regulation of Polyadenylation by Human U1A Protein Authors: Varani, L. / Gunderson, S.I. / Mattaj, I.W. / Kay, L.E. / Neuhaus, D. / Varani, G. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1dz5.cif.gz | 1.2 MB | Display | PDBx/mmCIF format |
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PDB format | pdb1dz5.ent.gz | 1 MB | Display | PDB format |
PDBx/mmJSON format | 1dz5.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/dz/1dz5 ftp://data.pdbj.org/pub/pdb/validation_reports/dz/1dz5 | HTTPS FTP |
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-Related structure data
Related structure data | |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 11613.582 Da / Num. of mol.: 2 / Fragment: RESIDUES 2-102 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PET13A / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P09012 #2: RNA chain | Mass: 7033.242 Da / Num. of mol.: 2 / Fragment: 3' UTR POLYADENYLATION INHIBITION ELEMENT / Mutation: YES / Source method: obtained synthetically / Details: PRODUCED BY IN VITRO TRANSCRIPTION / Source: (synth.) HOMO SAPIENS (human) Compound details | MUTATIONS IN CHAIN A,B: Y31H, Q36R MUTATIONS IN CHAIN C: U18C, A21G MUTATIONS IN CHAIN D: U47C | |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||
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NMR experiment |
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NMR details | Text: THE STRUCTURE WAS DETERMINED USING 15N, 13C AND 2D LABELED SAMPLES. DIFFERENT LABELLED SPECIES WERE MIXED IN DIFFERENT EXPERIMENTS. TRIPLE RESONANCE EXPERIMENTS COULD NOT BE USED DUE TO THE ...Text: THE STRUCTURE WAS DETERMINED USING 15N, 13C AND 2D LABELED SAMPLES. DIFFERENT LABELLED SPECIES WERE MIXED IN DIFFERENT EXPERIMENTS. TRIPLE RESONANCE EXPERIMENTS COULD NOT BE USED DUE TO THE SIZE OF THE COMPLEX; TROSY WAS NOT AVAILABLE WHEN MOST OF THE ASSIGNMENT WAS COMPLETED. |
-Sample preparation
Details | Contents: 10MM PHOSPHATE BUFFER |
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Sample conditions | Ionic strength: 10MM PHOSPHATE BUFFER / pH: 6.0 / Pressure: 1 atm / Temperature: 300 K |
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer | Type: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 600 MHz |
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-Processing
NMR software |
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Refinement | Method: RESTRAINED MOLECULAR DYNAMICS / Software ordinal: 1 / Details: DETAILS CAN BE FOUND IN THE JOURNAL CITATION ABOVE | ||||||||||||
NMR ensemble | Conformer selection criteria: AGREEMENT WITH EXPERIMENTAL DATA Conformers calculated total number: 50 / Conformers submitted total number: 13 |