+Open data
-Basic information
Entry | Database: PDB / ID: 2v1q | ||||||
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Title | Atomic-resolution structure of the yeast Sla1 SH3 domain 3 | ||||||
Components | CYTOSKELETON ASSEMBLY CONTROL PROTEIN SLA1 | ||||||
Keywords | STRUCTURAL PROTEIN / STRUCTURAL GENOMICS / PHOSPHORYLATION / YEAST / SH3 DOMAIN / CYTOSKELETON / ACTIN-BINDING | ||||||
Function / homology | Function and homology information actin cytoskeleton-regulatory complex / SLAC complex / cargo adaptor activity / actin cortical patch assembly / regulation of Arp2/3 complex-mediated actin nucleation / negative regulation of Arp2/3 complex-mediated actin nucleation / actin cortical patch / regulation of actin filament polymerization / cellular bud neck / mating projection tip ...actin cytoskeleton-regulatory complex / SLAC complex / cargo adaptor activity / actin cortical patch assembly / regulation of Arp2/3 complex-mediated actin nucleation / negative regulation of Arp2/3 complex-mediated actin nucleation / actin cortical patch / regulation of actin filament polymerization / cellular bud neck / mating projection tip / ubiquitin binding / cell wall organization / endocytosis / actin binding / cell cortex / endosome membrane / identical protein binding / nucleus / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | SACCHAROMYCES CEREVISIAE (brewer's yeast) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.2 Å | ||||||
Authors | Kursula, I. / Kursula, P. / Zou, P. / Lehmann, F. / Song, Y.H. / Wilmanns, M. | ||||||
Citation | Journal: To be Published Title: Structural Genomics of Yeast SH3 Domains Authors: Kursula, P. / Kursula, I. / Pinotsis, N. / Lehmann, F. / Zou, P. / Song, Y.H. / Wilmanns, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2v1q.cif.gz | 70.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2v1q.ent.gz | 52.6 KB | Display | PDB format |
PDBx/mmJSON format | 2v1q.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/v1/2v1q ftp://data.pdbj.org/pub/pdb/validation_reports/v1/2v1q | HTTPS FTP |
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-Related structure data
Related structure data | 2v1rC 2vknC 1z9zS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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Components on special symmetry positions |
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-Components
#1: Protein | Mass: 6833.769 Da / Num. of mol.: 2 / Fragment: SH3 DOMAIN 3, RESIDUES 357-413 Source method: isolated from a genetically manipulated source Source: (gene. exp.) SACCHAROMYCES CEREVISIAE (brewer's yeast) Plasmid: PET24D / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21 / References: UniProt: P32790 #2: Chemical | ChemComp-NA / | #3: Chemical | #4: Chemical | ChemComp-CL / | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 1.67 Å3/Da / Density % sol: 39 % / Description: NONE |
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: EMBL/DESY, HAMBURG / Beamline: BW7A / Wavelength: 0.92 |
Detector | Type: MARRESEARCH / Detector: CCD |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.92 Å / Relative weight: 1 |
Reflection | Resolution: 1.2→20 Å / Num. obs: 33200 / % possible obs: 100 % / Observed criterion σ(I): -3 / Redundancy: 5.9 % / Rmerge(I) obs: 0.04 / Net I/σ(I): 19.4 |
Reflection shell | Resolution: 1.2→1.22 Å / Redundancy: 3.9 % / Rmerge(I) obs: 0.53 / Mean I/σ(I) obs: 2.8 / % possible all: 100 |
-Processing
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1Z9Z Resolution: 1.2→10 Å / Cor.coef. Fo:Fc: 0.975 / Cor.coef. Fo:Fc free: 0.965 / SU B: 1.656 / SU ML: 0.033 / Cross valid method: THROUGHOUT / ESU R: 0.041 / ESU R Free: 0.043 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 13.21 Å2
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Refinement step | Cycle: LAST / Resolution: 1.2→10 Å
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Refine LS restraints |
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