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Open data
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Basic information
Entry | Database: PDB / ID: 1j6y | ||||||
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Title | Solution structure of Pin1At from Arabidopsis thaliana | ||||||
![]() | peptidyl-prolyl cis-trans isomerase | ||||||
![]() | ISOMERASE / prolyl cis/trans isomerase / parvulin / PIN1 / phosphorylation | ||||||
Function / homology | ![]() regulation of flower development / gravitropism / plasmodesma / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / regulation of protein localization / regulation of cell cycle / endoplasmic reticulum / mitochondrion / nucleus ...regulation of flower development / gravitropism / plasmodesma / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / regulation of protein localization / regulation of cell cycle / endoplasmic reticulum / mitochondrion / nucleus / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / distance geometry simulated annealing | ||||||
![]() | Landrieu, I. / Wieruszeski, J.M. / Wintjens, R. / Inze, D. / Lippens, G. | ||||||
![]() | ![]() Title: Solution Structure of the Single-domain Prolyl Cis/Trans Isomerase PIN1At from Arabidopsis thaliana Authors: Landrieu, I. / Wieruszeski, J.M. / Wintjens, R. / Inze, D. / Lippens, G. #1: ![]() Title: Letter to the editor : sequence-specific 1H, 13C and 15N chemical shift backbone NMR assigment and secondary structure of the Arabidopsis thaliana PIN1At protein Authors: Landrieu, I. / Wieruszeski, J.M. / Odaert, B. / Inze, D. / Grzesiek, S. / Lippens, G. #2: ![]() Title: The Arabidopsis thaliana PIN1At gene encodes a single-domain phosphorylation-dependent peptidyl prolyl cis/trans isomerase Authors: Landrieu, I. / De Veylder, L. / Fruchart, J.-S. / Odaert, B. / Casteels, P. / Portetelle, D. / Van Montagu, M. / Inze, D. / Lippens, G. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 729.4 KB | Display | ![]() |
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PDB format | ![]() | 600.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 360.2 KB | Display | ![]() |
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Full document | ![]() | 616.2 KB | Display | |
Data in XML | ![]() | 87.1 KB | Display | |
Data in CIF | ![]() | 115.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data | |
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Links
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Assembly
Deposited unit | ![]()
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NMR ensembles |
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Components
#1: Protein | Mass: 15209.109 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
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Sample conditions | Ionic strength: 100 mM NaCl / pH: 6.3 / Pressure: ambient / Temperature: 293 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 | Type: Bruker DMX / Manufacturer: Bruker / Model: DMX / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: distance geometry simulated annealing / Software ordinal: 1 | ||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with acceptable covalent geometry,structures with the least restraint violations,structures with the lowest energy Conformers calculated total number: 150 / Conformers submitted total number: 20 |