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Open data
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Basic information
Entry | Database: PDB / ID: 2l2g | ||||||
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Title | Solution structure of Opossum Domain 11 | ||||||
![]() | IGF2R DOMAIN 11 | ||||||
![]() | SIGNALING PROTEIN / Insulin-like growth factor 2 / mannose 6 phosphate receptor / Genomic imprinting / protein evolution | ||||||
Function / homology | ![]() retromer complex binding / insulin-like growth factor binding / trans-Golgi network transport vesicle / positive regulation by host of viral process / lysosomal transport / nuclear envelope lumen / D-mannose binding / endocytic vesicle / phosphoprotein binding / trans-Golgi network ...retromer complex binding / insulin-like growth factor binding / trans-Golgi network transport vesicle / positive regulation by host of viral process / lysosomal transport / nuclear envelope lumen / D-mannose binding / endocytic vesicle / phosphoprotein binding / trans-Golgi network / late endosome / signaling receptor activity / membrane => GO:0016020 / early endosome / endosome membrane / endosome / cell surface / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / simulated annealing, simulated annealing | ||||||
Model details | lowest energy, model 1 | ||||||
![]() | Williams, C. / Hoppe, H. / Rezgui, D. / Rezgui, M. / Frago, S. / Ellis, R.Z. / Wattana-Amorn, P. / Prince, S.N. / Zaccheo, O.J. / Forbes, B. ...Williams, C. / Hoppe, H. / Rezgui, D. / Rezgui, M. / Frago, S. / Ellis, R.Z. / Wattana-Amorn, P. / Prince, S.N. / Zaccheo, O.J. / Forbes, B. / Jones, E.Y. / Crump, M.P. / Bassim, A.H. | ||||||
![]() | ![]() Title: An exon splice enhancer primes IGF2:IGF2R binding site structure and function evolution. Authors: Williams, C. / Hoppe, H.J. / Rezgui, D. / Strickland, M. / Forbes, B.E. / Grutzner, F. / Frago, S. / Ellis, R.Z. / Wattana-Amorn, P. / Prince, S.N. / Zaccheo, O.J. / Nolan, C.M. / Mungall, A. ...Authors: Williams, C. / Hoppe, H.J. / Rezgui, D. / Strickland, M. / Forbes, B.E. / Grutzner, F. / Frago, S. / Ellis, R.Z. / Wattana-Amorn, P. / Prince, S.N. / Zaccheo, O.J. / Nolan, C.M. / Mungall, A.J. / Jones, E.Y. / Crump, M.P. / Hassan, A.B. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 857.1 KB | Display | ![]() |
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PDB format | ![]() | 741.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 352.9 KB | Display | ![]() |
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Full document | ![]() | 485.2 KB | Display | |
Data in XML | ![]() | 62.4 KB | Display | |
Data in CIF | ![]() | 83.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2l29C ![]() 2l2aC ![]() 2llaC ![]() 2l2h 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 | Mass: 16655.783 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Plasmid: pET26a / Production host: ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR Details: Domain 11 of the IGF2R from Monodelphis domestica (Gray Short-tailed Opossum) | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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Sample preparation
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Sample conditions | Ionic strength: 0 / pH: 5.5 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz |
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Processing
NMR software |
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Refinement | Method: simulated annealing, simulated annealing / Software ordinal: 1 Details: ARIA1.2 protocol. Cool_1 and cool_2 steps increased to 40K and cool_2, ARIA1.2 water refinement modified with RECOORD water refinement parameters | ||||||||||||||||||||||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 20 |