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- PDB-2l2p: Folding Intermediate of the Fyn SH3 A39V/N53P/V55L from NMR Relax... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2l2p | ||||||
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Title | Folding Intermediate of the Fyn SH3 A39V/N53P/V55L from NMR Relaxation Dispersion Experiments | ||||||
![]() | Tyrosine-protein kinase Fyn | ||||||
![]() | TRANSFERASE / amyloid fibril / chemical exchange / CPMG NMR relaxation dispersion / Fyn SH3 domain / protein folding intermediate | ||||||
Function / homology | ![]() forebrain development / extrinsic component of cytoplasmic side of plasma membrane / cell surface receptor protein tyrosine kinase signaling pathway / tubulin binding / non-specific protein-tyrosine kinase / neuron migration / non-membrane spanning protein tyrosine kinase activity / peptidyl-tyrosine phosphorylation / regulation of cell shape / perikaryon ...forebrain development / extrinsic component of cytoplasmic side of plasma membrane / cell surface receptor protein tyrosine kinase signaling pathway / tubulin binding / non-specific protein-tyrosine kinase / neuron migration / non-membrane spanning protein tyrosine kinase activity / peptidyl-tyrosine phosphorylation / regulation of cell shape / perikaryon / protein tyrosine kinase activity / cell differentiation / protein kinase activity / membrane raft / innate immune response / signaling receptor binding / ATP binding / nucleus / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | SOLUTION NMR / molecular dynamics | ||||||
Model details | lowest energy, model 1 | ||||||
![]() | Neudecker, P. / Robustelli, P. / Cavalli, A. / Vendruscolo, M. / Kay, L.E. | ||||||
![]() | ![]() Title: Structure of an intermediate state in protein folding and aggregation. Authors: Neudecker, P. / Robustelli, P. / Cavalli, A. / Walsh, P. / Lundstrom, P. / Zarrine-Afsar, A. / Sharpe, S. / Vendruscolo, M. / Kay, L.E. | ||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR DETERMINED | ||||||
Remark 700 | SHEET DETERMINATION METHOD: AUTHOR DETERMINED |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 175.8 KB | Display | ![]() |
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PDB format | ![]() | 145.4 KB | Display | ![]() |
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-Validation report
Summary document | ![]() | 426.6 KB | Display | ![]() |
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Full document | ![]() | 450.9 KB | Display | |
Data in XML | ![]() | 11.1 KB | Display | |
Data in CIF | ![]() | 18.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related 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: 7538.242 Da / Num. of mol.: 1 / Fragment: SH3 domain (unp residues 85-142) / Mutation: A122V, N136P, V138L Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: Q05876, non-specific protein-tyrosine kinase |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR Details: High-resolution structure of a low-populated folding intermediate of the Fyn SH3 domain mutant A39V/N53P/V55L determined from NMR relaxation dispersion experiments | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: The CPMG experiments were supplemented with sign determination experiments as appropriate. |
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