+Open data
-Basic information
Entry | Database: PDB / ID: 2lj4 | ||||||
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Title | Solution structure of the TbPIN1 | ||||||
Components | Peptidyl-prolyl cis-trans isomerase/rotamase, putative | ||||||
Keywords | ISOMERASE / TbPIN1 | ||||||
Function / homology | Function and homology information nuclear lumen / ciliary plasm / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / protein folding / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Trypanosoma brucei (eukaryote) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Sun, L. / Lin, D. / Zhao, Y. | ||||||
Citation | Journal: Plos One / Year: 2012 Title: Solution structural analysis of the single-domain parvulin TbPin1. Authors: Sun, L. / Wu, X. / Peng, Y. / Goh, J.Y. / Liou, Y.-C. / Lin, D. / Zhao, Y. #1: Journal: Plos One / Year: 2012 Title: Solution Structural Analysis of the Single-Domain Parvulin TbPin1 Authors: Sun, L. / Wu, X. / Peng, Y. / Goh, J.Y. / Liou, T.-C. / Lin, D. / Zhao, Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2lj4.cif.gz | 737.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2lj4.ent.gz | 625 KB | Display | PDB format |
PDBx/mmJSON format | 2lj4.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2lj4_validation.pdf.gz | 467.8 KB | Display | wwPDB validaton report |
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Full document | 2lj4_full_validation.pdf.gz | 1.5 MB | Display | |
Data in XML | 2lj4_validation.xml.gz | 145.2 KB | Display | |
Data in CIF | 2lj4_validation.cif.gz | 162.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lj/2lj4 ftp://data.pdbj.org/pub/pdb/validation_reports/lj/2lj4 | HTTPS FTP |
-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: 12515.032 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Trypanosoma brucei (eukaryote) / Gene: TbPIN1 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: Q57YG1, 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: 0.8-1.0 mM [U-99% 13C; U-99% 15N] Prolyl Cis/trans Isomerase TbPIN1-1, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O |
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Sample | Units: mM / Component: Prolyl Cis/trans Isomerase TbPIN1-1 / Isotopic labeling: [U-99% 13C; U-99% 15N] / Conc. range: 0.8-1.0 |
Sample conditions | Ionic strength: 20 / pH: 7.0 / Pressure: 10132 5 / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz |
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-Processing
NMR software | Name: CNS / Version: 1.2 / Developer: Brunger A. T. et.al. / Classification: refinement |
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Refinement | Method: simulated annealing / Software ordinal: 1 |
NMR constraints | NOE constraints total: 1898 / NOE intraresidue total count: 711 / NOE long range total count: 447 / NOE medium range total count: 293 / NOE sequential total count: 447 |
NMR representative | Selection criteria: lowest energy |
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 20 / Representative conformer: 1 |