+Open data
-Basic information
Entry | Database: PDB / ID: 1p0r | ||||||
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Title | Solution Structure of UBL5 a human Ubiquitin-Like Protein | ||||||
Components | ubiquitin-like 5 | ||||||
Keywords | PROTEIN BINDING / Ubiquitin-like fold | ||||||
Function / homology | Function and homology information positive regulation of protein targeting to mitochondrion / Cajal body / mRNA Splicing - Major Pathway / protein modification process / protein tag activity / mRNA splicing, via spliceosome / nucleoplasm / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model type details | minimized average | ||||||
Authors | McNally, T. / Huang, Q. / Janis, R.S. / Liu, Z. / Olejniczak, E.T. / Reilly, R.M. | ||||||
Citation | Journal: Protein Sci. / Year: 2003 Title: Structural analysis of UBL5, a novel ubiquitin-like modifier Authors: McNally, T. / Huang, Q. / Janis, R.S. / Liu, Z. / Olejniczak, E.T. / Reilly, R.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1p0r.cif.gz | 33.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1p0r.ent.gz | 26.1 KB | Display | PDB format |
PDBx/mmJSON format | 1p0r.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/p0/1p0r ftp://data.pdbj.org/pub/pdb/validation_reports/p0/1p0r | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 10732.312 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Plasmid: pet15b / Species (production host): Escherichia coli / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): bl21(DE3) / References: UniProt: Q9BZL1 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample conditions | Ionic strength: 50mM sodium phosphate / pH: 5.7 / Pressure: ambient / Temperature: 298 K | |||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M | |||||||||||||||
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Radiation wavelength | Relative weight: 1 | |||||||||||||||
NMR spectrometer |
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-Processing
NMR software | Name: CNX / Version: 2000 / Developer: Brunger, A.T. / Classification: refinement |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: Based on 952 NMR-derived distance and torsion angle restraints. |
NMR representative | Selection criteria: minimized average structure |
NMR ensemble | Conformers submitted total number: 1 |