+Open data
-Basic information
Entry | Database: PDB / ID: 2k7n | ||||||
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Title | Solution structure of the PPIL1 bound to a fragment of SKIP | ||||||
Components | Peptidyl-prolyl cis-trans isomerase-like 1 | ||||||
Keywords | ISOMERASE / beta barrel / disorder-order transition / hook-like / mRNA processing / mRNA splicing / Rotamase / Spliceosome | ||||||
Function / homology | Function and homology information embryonic brain development / U2-type catalytic step 2 spliceosome / cyclosporin A binding / protein peptidyl-prolyl isomerization / catalytic step 2 spliceosome / mRNA Splicing - Major Pathway / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / mRNA splicing, via spliceosome / disordered domain specific binding ...embryonic brain development / U2-type catalytic step 2 spliceosome / cyclosporin A binding / protein peptidyl-prolyl isomerization / catalytic step 2 spliceosome / mRNA Splicing - Major Pathway / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / mRNA splicing, via spliceosome / disordered domain specific binding / protein folding / nucleoplasm / nucleus Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / CYANA, simulated annealin | ||||||
Authors | Wang, X. / Wu, J. / Shi, Y. | ||||||
Citation | Journal: To be Published Title: Solution Structure of PPIL1 Bound to the Fragment of SKIP Shown Disorder-Order Transition Induced by Protein Binding Authors: Wang, X. / Wu, J. / Shi, Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2k7n.cif.gz | 1.3 MB | Display | PDBx/mmCIF format |
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PDB format | pdb2k7n.ent.gz | 1.1 MB | Display | PDB format |
PDBx/mmJSON format | 2k7n.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/k7/2k7n ftp://data.pdbj.org/pub/pdb/validation_reports/k7/2k7n | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 21534.260 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PPIL1, CYPL1, CGI-124, UNQ2425/PRO4984 / Plasmid: pET22b / Production host: Escherichia coli (E. coli) / References: UniProt: Q9Y3C6, peptidylprolyl isomerase |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 100% D2O, 100% H2O / Solvent system: 100% D2O, 100% H2O |
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Sample conditions | Ionic strength: 50 mM NaCl / pH: 6.5 / Pressure: 1 atm / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 600 MHz |
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-Processing
NMR software | Name: CNS / Classification: refinement |
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Refinement | Method: CYANA, simulated annealin / Software ordinal: 1 / Details: using by CNS in explict water |
NMR representative | Selection criteria: lowest energy, fewest violation |
NMR ensemble | Conformer selection criteria: 20 structures for lowest energy Conformers calculated total number: 400 / Conformers submitted total number: 20 / Representative conformer: 1 |