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- PDB-1tqz: Solution structure of NECAP1 protein -

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Database: PDB / ID: 1tqz
TitleSolution structure of NECAP1 protein
KeywordsENDOCYTOSIS/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 speciesMus musculus (house mouse)
MethodSOLUTION NMR / simulated annealing
AuthorsDenisov, A.Y. / Ritter, B. / McPherson, P.S. / Gehring, K.
CitationJournal: To be Published
Title: Solution structure of NECAP1 protein
Authors: Denisov, A.Y. / Ritter, B. / McPherson, P.S. / Gehring, K.
Validation Report
SummaryFull reportAbout validation report
DepositionJun 18, 2004Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jul 26, 2005Provider: repository / Type: Initial release
Revision 1.1Apr 30, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance

Structure visualization

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Deposited unit

Theoretical massNumber of molelcules
Total (without water)15,1021
NMR ensembles
Number of conformers (submitted / calculated)10 / 200structures with the least restraint violations,structures with the lowest energy
RepresentativeModel #1lowest energy


#1: Protein NECAP1

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

Experimental details


ExperimentMethod: SOLUTION NMR
NMR experiment
13113C,15N-edited NOESY
14215N-edited NOESY
NMR detailsText: The structure was determined using triple-resonance NMR spectroscopy

Sample preparation

Solution-IDContentsSolvent system
11.5 mM NECAP1 protein U-15N,13C, 25 mM phosphate buffer, 90% H2O, 10% D2O90% H2O/10% D2O
21.5 mM NECAP1 protein U-15N, 25 mM phosphate buffer, 90% H2O, 10% D2O90% H2O/10% D2O
30.6 mM NECAP1 protein U-15N, 8 mg/ml Pf1-bacteriophages, 90% H2O, 10% D2O90% H2O/10% D2O
Sample conditionsIonic strength: 75mM NaCl / pH: 7.2 / Pressure: 1 atm / Temperature: 303 K

NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometerType: Bruker DRX / Manufacturer: Bruker / Model: DRX / Field strength: 600 MHz


NMR software
NMRPipe2Delargio et al.processing
XEASY1.3.13Bartels et al.data analysis
CNS1.1Brunger et al.refinement
RefinementMethod: 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 representativeSelection criteria: lowest energy
NMR ensembleConformer 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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