+Open data
-Basic information
Entry | Database: PDB / ID: 1tqz | ||||||
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Title | Solution structure of NECAP1 protein | ||||||
Components | NECAP1 | ||||||
Keywords | ENDOCYTOSIS/EXOCYTOSIS / NECAP1 protein / endocytosis / structural genomics / ENDOCYTOSIS-EXOCYTOSIS COMPLEX | ||||||
Function / homology | Function and homology information clathrin vesicle coat / Golgi Associated Vesicle Biogenesis / Cargo recognition for clathrin-mediated endocytosis / Clathrin-mediated endocytosis / clathrin-coated pit / vesicle-mediated transport / endocytosis / protein transport Similarity search - Function | ||||||
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. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1tqz.cif.gz | 413.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1tqz.ent.gz | 355.5 KB | Display | PDB format |
PDBx/mmJSON format | 1tqz.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/tq/1tqz ftp://data.pdbj.org/pub/pdb/validation_reports/tq/1tqz | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#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 |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||
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NMR experiment |
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NMR details | Text: The structure was determined using triple-resonance NMR spectroscopy |
-Sample preparation
Details |
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Sample conditions | Ionic strength: 75mM NaCl / pH: 7.2 / Pressure: 1 atm / Temperature: 303 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: 600 MHz |
-Processing
NMR software |
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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 |