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Open data
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Basic information
Entry | Database: PDB / ID: 7jia | ||||||
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Title | Structure of truncated zebrafish granulin AaE | ||||||
![]() | Granulin-A | ||||||
![]() | SIGNALING PROTEIN / disulfide-rich / growth factor | ||||||
Function / homology | ![]() skeletal muscle acetylcholine-gated channel clustering / axon extension / liver development / extracellular region / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
![]() | Takjoo, R. / Daly, N.L. | ||||||
![]() | ![]() Title: Folding of Truncated Granulin Peptides. Authors: Takjoo, R. / Wilson, D. / Bansal, P.S. / Loukas, A. / Smout, M.J. / Daly, N.L. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 121.3 KB | Display | ![]() |
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PDB format | ![]() | 97 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 437.7 KB | Display | ![]() |
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Full document | ![]() | 568.6 KB | Display | |
Data in XML | ![]() | 20.7 KB | Display | |
Data in CIF | ![]() | 21.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7jiyC C: citing same article ( |
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Similar structure data | |
Other databases |
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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/peptide | Mass: 2441.677 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
Details | Type: solution / Contents: 0.2 mM ZF-N24_3s, 90% H2O/10% D2O / Label: 1 / Solvent system: 90% H2O/10% D2O |
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Sample | Conc.: 0.2 mM / Component: ZF-N24_3s / Isotopic labeling: natural abundance |
Sample conditions | Ionic strength: 0 M / Label: 1 / pH: 3 / Pressure: ambient / Temperature: 290 K |
-NMR measurement
NMR spectrometer | Type: Bruker AVANCE / Manufacturer: Bruker / Model: AVANCE / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 2 | ||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||
NMR ensemble | Conformer selection criteria: target function / Conformers calculated total number: 50 / Conformers submitted total number: 20 |