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- PDB-4nmo: CFTR Associated Ligand (CAL) PDZ domain bound to peptide iCAL36(A... -
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Open data
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Basic information
Entry | Database: PDB / ID: 4nmo | ||||||
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Title | CFTR Associated Ligand (CAL) PDZ domain bound to peptide iCAL36(Ac-K-1)(ANSRWPTS[Ac-K]I) | ||||||
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![]() | protein transport/inhibitor / PDZ domain / CAL / FIG / PIST / GOPC / PDZ-peptide complex / CFTR / CFTR Associated Ligand / protein transport / protein transport-inhibitor complex | ||||||
Function / homology | ![]() negative regulation of anion channel activity / RHO GTPases regulate CFTR trafficking / negative regulation of protein localization to cell surface / Golgi-associated vesicle membrane / Golgi to plasma membrane transport / trans-Golgi network transport vesicle / molecular sequestering activity / apical protein localization / RHOQ GTPase cycle / endoplasmic reticulum to Golgi vesicle-mediated transport ...negative regulation of anion channel activity / RHO GTPases regulate CFTR trafficking / negative regulation of protein localization to cell surface / Golgi-associated vesicle membrane / Golgi to plasma membrane transport / trans-Golgi network transport vesicle / molecular sequestering activity / apical protein localization / RHOQ GTPase cycle / endoplasmic reticulum to Golgi vesicle-mediated transport / protein transport / transmembrane transporter binding / postsynaptic density / Golgi membrane / lysosomal membrane / dendrite / Golgi apparatus / protein-containing complex / identical protein binding / membrane / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Amacher, J.F. / Madden, D.R. | ||||||
![]() | ![]() Title: Chemically Modified Peptide Scaffolds Target the CFTR-Associated Ligand PDZ Domain. Authors: Amacher, J.F. / Zhao, R. / Spaller, M.R. / Madden, D.R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 86.9 KB | Display | ![]() |
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PDB format | ![]() | 65 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 4nmpC ![]() 4nmqC ![]() 4nmrC ![]() 4nmsC ![]() 4nmtC ![]() 4nmvC ![]() 4e34S C: citing same article ( S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 9353.722 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 284-370 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Protein/peptide | #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.99 Å3/Da / Density % sol: 38.19 % |
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7.5 Details: 27% (w/v) polyethylene glycol (PEG), 0.15 M sodium chloride, 0.1 M tris(hydroxymethyl)aminomethane (Tris), pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
-Data collection
Diffraction | Mean temperature: 100 K | ||||||||||||||||||||||||||||||||||||||||||
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Diffraction source | Source: ![]() ![]() ![]() | ||||||||||||||||||||||||||||||||||||||||||
Detector | Type: ADSC QUANTUM 270 / Detector: CCD / Date: Oct 18, 2011 | ||||||||||||||||||||||||||||||||||||||||||
Radiation | Monochromator: S1 111 CHANNEL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | ||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 0.8856 Å / Relative weight: 1 | ||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 1.4→19.5 Å / Num. all: 34123 / Num. obs: 34205 / % possible obs: 99.8 % / Observed criterion σ(F): 7.2 / Observed criterion σ(I): 30.16 / Rsym value: 0.072 / Net I/σ(I): 30.16 | ||||||||||||||||||||||||||||||||||||||||||
Reflection shell |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB entry 4E34 Resolution: 1.4→19.471 Å / SU ML: 0.18 / σ(F): 1.99 / Phase error: 17.8 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.38 Å / VDW probe radii: 0.7 Å / Solvent model: FLAT BULK SOLVENT MODEL / Bsol: 43.986 Å2 / ksol: 0.441 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 1.4→19.471 Å
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Refine LS restraints |
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LS refinement shell |
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