+Open data
-Basic information
Entry | Database: PDB / ID: 1fi6 | ||||||
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Title | SOLUTION STRUCTURE OF THE REPS1 EH DOMAIN | ||||||
Components | EH DOMAIN PROTEIN REPS1 | ||||||
Keywords | endocytosis/exocytosis / EPS15 HOMOLOGY DOMAIN / EF HAND / CALCIUM / RAS SIGNAL TRANSDUCTION / endocytosis-exocytosis COMPLEX | ||||||
Function / homology | Function and homology information Cargo recognition for clathrin-mediated endocytosis / Clathrin-mediated endocytosis / endosomal transport / clathrin-coated pit / receptor-mediated endocytosis / SH3 domain binding / endocytosis / calcium ion binding / plasma membrane Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Authors | Kim, S. / Baleja, J.D. | ||||||
Citation | Journal: Biochemistry / Year: 2001 Title: Solution structure of the Reps1 EH domain and characterization of its binding to NPF target sequences. Authors: Kim, S. / Cullis, D.N. / Feig, L.A. / Baleja, J.D. #1: Journal: Thesis / Year: 2000 Title: Chapter 3: Studies of Protein Structure and Interaction using Nuclear Magnetic Resonance Spectroscopy:Applications to the Reps1 EH Domain and MicrocinB17 Propeptide Authors: Kim, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1fi6.cif.gz | 868.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1fi6.ent.gz | 724.1 KB | Display | PDB format |
PDBx/mmJSON format | 1fi6.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1fi6_validation.pdf.gz | 343.6 KB | Display | wwPDB validaton report |
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Full document | 1fi6_full_validation.pdf.gz | 615.2 KB | Display | |
Data in XML | 1fi6_validation.xml.gz | 69.1 KB | Display | |
Data in CIF | 1fi6_validation.cif.gz | 105 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fi/1fi6 ftp://data.pdbj.org/pub/pdb/validation_reports/fi/1fi6 | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
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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: 10647.128 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Plasmid: PGEX2T / Production host: Escherichia coli (E. coli) / References: UniProt: O54916 |
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#2: Chemical | ChemComp-CA / |
-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 heteronuclear 2D and 3D NMR spectroscopy. |
-Sample preparation
Details |
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Sample conditions | Ionic strength: 10mM NaCl / pH: 6.8 / Pressure: ambient / Temperature: 30 K | ||||||||||||
Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 Details: The structures are based on a total of 1265 restraints, 1143 are NOE-derived distance constraints, 122 dihedral angle restraints. | ||||||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 40 / Conformers submitted total number: 30 |