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Open data
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Basic information
Entry | Database: PDB / ID: 2jma | ||||||
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Title | R21A Spc-SH3:P41 complex | ||||||
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![]() | STRUCTURAL PROTEIN / SH3 domain / p41-bound | ||||||
Function / homology | ![]() actin filament capping / costamere / cortical actin cytoskeleton / cell projection / actin filament binding / cell junction / actin cytoskeleton organization / calmodulin binding / calcium ion binding / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() synthetic construct (others) | ||||||
Method | SOLUTION NMR / torsion angle dynamics | ||||||
Model details | The R21A mutant of the alpha-spectrin SH3 domain (R21A Spc-SH3) in complex with P41 | ||||||
![]() | van Nuland, N.A.J. / Casares, S. / Ab, E. / Eshuis, H. / Lopez-Mayorga, O. / Conejero-Lara, F. | ||||||
![]() | ![]() Title: The high-resolution NMR structure of the R21A Spc-SH3:P41 complex: Understanding the determinants of binding affinity by comparison with Abl-SH3 Authors: Casares, S. / Ab, E. / Eshuis, H. / Lopez-Mayorga, O. / van Nuland, N.A.J. / Conejero-Lara, F. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 486.9 KB | Display | ![]() |
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PDB format | ![]() | 412.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 348.8 KB | Display | ![]() |
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Full document | ![]() | 540.7 KB | Display | |
Data in XML | ![]() | 23.9 KB | Display | |
Data in CIF | ![]() | 40.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2jm8C ![]() 2jm9C C: citing same article ( |
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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: 7143.128 Da / Num. of mol.: 1 / Fragment: SH3 domain, residues 965-1025 / Mutation: R21A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() |
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#2: Protein/peptide | Mass: 1035.149 Da / Num. of mol.: 1 / Source method: obtained synthetically / Source: (synth.) synthetic construct (others) |
-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR Details: The R21A mutant of the alpha-spectrin SH3 domain (R21A Spc-SH3) in complex with P41 | ||||||||||||
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NMR experiment |
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Sample preparation
Details | Contents: 2 mM R21A Spc-SH3, 5.2 mM P41, 90 % H2O, 10 % D2O, 20 mM d5-glycine Solvent system: 90% H2O/10% D2O | ||||||||||||||||||
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Sample |
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Sample conditions | pH: 3.5 / Temperature: 300 K |
-NMR measurement
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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Radiation wavelength | Relative weight: 1 |
NMR spectrometer | Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 750 MHz |
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Processing
NMR software |
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Refinement | Method: torsion angle dynamics / Software ordinal: 1 / Details: Final refinement in explicit solvent within ARIA | ||||||||||||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest interaction energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |