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Open data
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Basic information
Entry | Database: PDB / ID: 1n9j | ||||||
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Title | Solution Structure of the 3D domain swapped dimer of Stefin A | ||||||
![]() | Cystatin A![]() | ||||||
![]() | HYDROLASE INHIBITOR / domain swapped / ![]() ![]() | ||||||
Function / homology | ![]() negative regulation of peptidase activity / ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
Model type details | minimized average | ||||||
![]() | Staniforth, R.A. / Giannini, S. / Higgins, L.D. / Conroy, M.J. / Hounslow, A.M. / Jerala, R. / Craven, C.J. / Waltho, J.P. | ||||||
![]() | ![]() Title: Three-dimensional domain swapping in the folded and molten-globule states of cystatins, an amyloid-forming structural superfamily Authors: Staniforth, R.A. / Giannini, S. / Higgins, L.D. / Conroy, M.J. / Hounslow, A.M. / Jerala, R. / Craven, C.J. / Waltho, J.P. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 73 KB | Display | ![]() |
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PDB format | ![]() | 56.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | |
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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: 11020.464 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() | ||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details |
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Sample conditions | pH: 5.5 / Pressure: ambient / Temperature: 308 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 |
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Processing
NMR software |
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Refinement | Method: ![]() Details: Distance restraints (NOEs and hydrogen bonds) were taken from the data used for the stefin A monomer structure (Martin et al., 1995), except those involving residues V48-G50 and N77-L80 ...Details: Distance restraints (NOEs and hydrogen bonds) were taken from the data used for the stefin A monomer structure (Martin et al., 1995), except those involving residues V48-G50 and N77-L80 where chemical shift perturbation was observed following resonance assignment. The NOEs were specified as intermolecular and intramolecular according to domain-swapped topology inferred from isotope filtering experiments. An additional hydrogen bond restraint was included between 48 and 50 based on evidence from protection experiments on the dimer (Jerala and Zerovnik, 1999). Dihedral restraints (phi and psi) were determined using the 1H-alpha, 15N, 13C-alpha, 13C-beta and 13C' chemical shifts and the program TALOS (Cornilescu et al., 1999). Where TALOS gave a `poor' match, the experimental phi dihedral angle was taken from the data used for the stefin A monomer structure calculation. | ||||||||||||||||
NMR representative | Selection criteria: minimized average structure | ||||||||||||||||
NMR ensemble | Conformers submitted total number: 1 |