|Entry||Database: PDB / ID: 1eqk|
|Title||SOLUTION STRUCTURE OF ORYZACYSTATIN-I, A CYSTEINE PROTEINASE INHIBITOR OF THE RICE, ORYZA SATIVA L. JAPONICA|
|Keywords||HYDROLASE INHIBITOR / alpha and beta proteins / cystatin-like fold / cystatin/monellin superfamily / phytocystatin family|
|Function / homology|
Function and homology information
cysteine-type endopeptidase inhibitor activity / defense response / extracellular region
Similarity search - Function
Aspartic acid proteinase inhibitor / Cystatin / Proteinase inhibitor I25, cystatin, conserved site / Cysteine proteases inhibitors signature. / Cystatin-like domain / Cystatin domain / Nuclear Transport Factor 2; Chain: A, - #10 / Nuclear Transport Factor 2; Chain: A, / Roll / Alpha Beta
Similarity search - Domain/homology
Cysteine proteinase inhibitor 1
Similarity search - Component
|Biological species||Oryza sativa Japonica Group (Japanese rice)|
|Method||SOLUTION NMR / torsion angle dynamics|
|Model type details||minimized average|
|Authors||Nagata, K. / Kudo, N. / Abe, K. / Arai, S. / Tanokura, M.|
|Citation||Journal: Biochemistry / Year: 2000|
Title: Three-dimensional solution structure of oryzacystatin-I, a cysteine proteinase inhibitor of the rice, Oryza sativa L. japonica.
Authors: Nagata, K. / Kudo, N. / Abe, K. / Arai, S. / Tanokura, M.
|Structure viewer||Molecule: |
Downloads & links
|#1: Protein|| |
Mass: 11398.888 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Oryza sativa Japonica Group (Japanese rice)
Species: Oryza sativa / Strain: Japonica Group / Tissue: SEED / Plasmid: PLASMID PET-26B(+) / Production host: Escherichia coli (E. coli) / References: UniProt: P09229
|Experiment||Method: SOLUTION NMR|
|NMR details||Text: The structure was determined using 1H and 15N NMR spectroscopy.|
|Sample conditions||pH: 6.8 / Pressure: ambient / Temperature: 298 K|
*PLUSMethod: other / Details: NMR
|NMR spectrometer||Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 500 MHz|
|Refinement||Method: torsion angle dynamics / Software ordinal: 1 |
Details: A total of 1383 restraints, consisting of 1183 interproton distance restraints (338 long-range (|i - j| >= 6), 228 medium-range (2 <= |i - j| <= 5), 351 sequential (|i - j| = 1) and 266 intraresidual (|i - j| = 0)), 108 hydrogen bond restraints (representing 54 hydrogen bonds) and 92 torsion angle restraints (54 phi and 38 chi1), were used in the structure calculations by torsion angle dynamics using DYANA (ver. 1.4). A final set of 20 structures was selected from 100 calculations on the basis of agreement with the experimental data and van der Waals' energy. The average coordinates of the 20 DYANA structures were subjected to energy-minimization using CNS (ver. 0.9).
|NMR representative||Selection criteria: minimized average structure|
|NMR ensemble||Conformer selection criteria: structures with favorable non-bond energy|
Conformers calculated total number: 100 / Conformers submitted total number: 21
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