+Open data
-Basic information
Entry | Database: PDB / ID: 5fmt | ||||||
---|---|---|---|---|---|---|---|
Title | CrIFT54 CH-domain | ||||||
Components | FLAGELLAR ASSOCIATED PROTEIN | ||||||
Keywords | PROTEIN TRANSPORT / MOTOR PROTEIN / CALPONIN HOMOLOGY DOMAIN / IFT / TUBULIN-BINDING DOMAIN | ||||||
Function / homology | Function and homology information intraciliary transport particle B / cilium-dependent cell motility / intraciliary transport / post-transcriptional regulation of gene expression / axoneme / cilium assembly / regulation of microtubule cytoskeleton organization / ciliary basal body / microtubule binding Similarity search - Function | ||||||
Biological species | CHLAMYDOMONAS REINHARDTII (plant) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.878 Å | ||||||
Authors | Weber, K. / Lorentzen, E. | ||||||
Citation | Journal: Embo J. / Year: 2016 Title: Intraflagellar Transport Proteins 172, 80, 57, 54, 38, and 20 Form a Stable Tubulin-Binding Ift-B2 Complex. Authors: Taschner, M. / Weber, K. / Mourao, A. / Vetter, M. / Awasthi, M. / Stiegler, M. / Bhogaraju, S. / Lorentzen, E. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 5fmt.cif.gz | 67.9 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb5fmt.ent.gz | 51.5 KB | Display | PDB format |
PDBx/mmJSON format | 5fmt.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fm/5fmt ftp://data.pdbj.org/pub/pdb/validation_reports/fm/5fmt | HTTPS FTP |
---|
-Related structure data
-Links
-Assembly
Deposited unit |
| ||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||||||||||||
2 |
| ||||||||||||||||||
Unit cell |
| ||||||||||||||||||
Components on special symmetry positions |
| ||||||||||||||||||
Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
|
-Components
#1: Protein | Mass: 14740.996 Da / Num. of mol.: 2 / Fragment: CH-DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) CHLAMYDOMONAS REINHARDTII (plant) / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: A8JBY2 #2: Chemical | #3: Chemical | #4: Chemical | ChemComp-GOL / | #5: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 2.5 Å3/Da / Density % sol: 50.7 % / Description: NONE |
---|---|
Crystal grow | Details: 50 MM TRIS-HCL PH 8.3, 2% MPD, 80 MM AMMONIUM SULFATE, 30% PEG5000, 5% GLYCEROL |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X06DA / Wavelength: 1 |
Detector | Type: DECTRIS PILATUS / Detector: PIXEL |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.88→36.36 Å / Num. obs: 25144 / % possible obs: 98.2 % / Observed criterion σ(I): 1.7 / Redundancy: 4.7 % / Biso Wilson estimate: 23.45 Å2 / Rmerge(I) obs: 0.17 / Net I/σ(I): 11.16 |
Reflection shell | Resolution: 1.88→1.99 Å / Redundancy: 4 % / Rmerge(I) obs: 0.94 / Mean I/σ(I) obs: 1.73 / % possible all: 90.9 |
-Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: SAD Starting model: NONE Resolution: 1.878→36.365 Å / SU ML: 0.21 / σ(F): 2 / Phase error: 25.32 / Stereochemistry target values: ML
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Shrinkage radii: 1 Å / VDW probe radii: 1.2 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.878→36.365 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints NCS |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell |
|