|Entry||Database: PDB / ID: 1tqz|
|Title||Solution structure of NECAP1 protein|
|Keywords||ENDOCYTOSIS/EXOCYTOSIS / NECAP1 protein / endocytosis / structural genomics / ENDOCYTOSIS-EXOCYTOSIS COMPLEX|
|Function / homology|
Function and homology information
clathrin vesicle coat / clathrin-coated pit / vesicle-mediated transport / protein transport / endocytosis
NECAP, PHear domain / PH-like domain superfamily / Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB) / PH-domain like / Roll / Mainly Beta
Adaptin ear-binding coat-associated protein 1
|Biological species||Mus musculus (house mouse)|
|Method||SOLUTION NMR / simulated annealing|
|Authors||Denisov, A.Y. / Ritter, B. / McPherson, P.S. / Gehring, K.|
|Citation||Journal: To be Published|
Title: Solution structure of NECAP1 protein
Authors: Denisov, A.Y. / Ritter, B. / McPherson, P.S. / Gehring, K.
SummaryFull reportAbout validation report
|Structure viewer||Molecule: |
Downloads & links
|#1: Protein|| |
Mass: 15101.970 Da / Num. of mol.: 1 / Fragment: residues 1-133
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Plasmid: pGEX-4T1 / Species (production host): Escherichia coli / Production host: Escherichia coli BL21 (bacteria) / Strain (production host): BL21 / References: UniProt: Q9CR95
|Experiment||Method: SOLUTION NMR|
|NMR details||Text: The structure was determined using triple-resonance NMR spectroscopy|
|Sample conditions||Ionic strength: 75mM NaCl / pH: 7.2 / Pressure: 1 atm / Temperature: 303 K|
|Radiation||Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M|
|Radiation wavelength||Relative weight: 1|
|NMR spectrometer||Type: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz|
|Refinement||Method: simulated annealing / Software ordinal: 1 |
Details: Structure was refined by using standard protocol in CNS with restraints from NOE distances, backbone torsion angles, hydrogen bonds and residual dipolar couplings
|NMR representative||Selection criteria: lowest energy|
|NMR ensemble||Conformer selection criteria: structures with the least restraint violations,structures with the lowest energy|
Conformers calculated total number: 200 / Conformers submitted total number: 10
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