+Open data
-Basic information
Entry | Database: PDB / ID: 1eq3 | ||||||
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Title | NMR STRUCTURE OF HUMAN PARVULIN HPAR14 | ||||||
Components | PEPTIDYL-PROLYL CIS/TRANS ISOMERASE (PPIASE) | ||||||
Keywords | ISOMERASE / PEPTIDYL-PROLYL CIS-TRANS ISOMERASE / PARVULIN | ||||||
Function / homology | Function and homology information preribosome / bent DNA binding / localization / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / spindle / rRNA processing / chromosome / double-stranded DNA binding / mitochondrial matrix ...preribosome / bent DNA binding / localization / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / spindle / rRNA processing / chromosome / double-stranded DNA binding / mitochondrial matrix / nucleolus / DNA binding / RNA binding / nucleoplasm / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | SOLUTION NMR / Refinement was done using X-PLOR98 simulated annealing protocol. | ||||||
Authors | Sekerina, E. / Rahfeld, U.J. / Muller, J. / Fischer, G. / Bayer, P. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2000 Title: NMR solution structure of hPar14 reveals similarity to the peptidyl prolyl cis/trans isomerase domain of the mitotic regulator hPin1 but indicates a different functionality of the protein. Authors: Sekerina, E. / Rahfeld, J.U. / Muller, J. / Fanghanel, J. / Rascher, C. / Fischer, G. / Bayer, P. #1: Journal: FEBS Lett. / Year: 1999 Title: Identification and characterization of a 14kDa human protein as a novel parvulin-like peptidyl-prolyl cis/trans isomerase Authors: Uchida, T. / Fujimori, F. / Tradler, T. / Fischer, G. / Rahfeld, J.U. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1eq3.cif.gz | 733.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1eq3.ent.gz | 636.9 KB | Display | PDB format |
PDBx/mmJSON format | 1eq3.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/eq/1eq3 ftp://data.pdbj.org/pub/pdb/validation_reports/eq/1eq3 | 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: 10731.549 Da / Num. of mol.: 1 / Fragment: PPIASE DOMAIN (RESIDUES 36-131) Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Description: HOMO SAPIENS / Cell: ENDOTHELIAL CELLS / Organ: LUNG / Production host: Escherichia coli (E. coli) / References: UniProt: Q9Y237 |
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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 |
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-NMR measurement
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 500 MHz |
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-Processing
NMR software |
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Refinement | Method: Refinement was done using X-PLOR98 simulated annealing protocol. Software ordinal: 1 Details: Constraints used for calculation: Total number of NOEs = 1042, Intra-residual = 120, Long-range = 397, Medium-range = 167, Sequential = 358; Coupling constants = 71, Hydrogen bonds = 38. | ||||||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 50 / Conformers submitted total number: 25 |