+Open data
-Basic information
Entry | Database: PDB / ID: 2iwn | ||||||
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Title | 3rd PDZ domain of Multiple PDZ Domain Protein MPDZ | ||||||
Components | MULTIPLE PDZ DOMAIN PROTEIN | ||||||
Keywords | SIGNALING PROTEIN / SGC / PDZ / MPDZ / MUPP1 / MUPP- 1 / PDZ DOMAIN / HOST-VIRUS INTERACTION / STRUCTURAL GENOMICS CONSORTIUM / SYNAPTOSOME / TIGHT JUNCTION / ALTERNATIVE SPLICING | ||||||
Function / homology | Function and homology information tight junction assembly / apicolateral plasma membrane / bicellular tight junction / apical part of cell / postsynaptic density / apical plasma membrane / dendrite / plasma membrane / cytoplasm Similarity search - Function | ||||||
Biological species | HOMO SAPIENS (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.35 Å | ||||||
Authors | Elkins, J.M. / Gileadi, C. / Savitsky, P. / Berridge, G. / Smee, C.E.A. / Pike, A.C.W. / Papagrigoriou, E. / Sundstrom, M. / Edwards, A. / Arrowsmith, C. ...Elkins, J.M. / Gileadi, C. / Savitsky, P. / Berridge, G. / Smee, C.E.A. / Pike, A.C.W. / Papagrigoriou, E. / Sundstrom, M. / Edwards, A. / Arrowsmith, C. / Weigelt, J. / Doyle, D.A. | ||||||
Citation | Journal: Protein Sci. / Year: 2007 Title: Structure of Pick1 and Other Pdz Domains Obtained with the Help of Self-Binding C-Terminal Extension. Authors: Elkins, J.M. / Papagrigoriou, E. / Berridge, G. / Yang, X. / Phillips, C. / Gileadi, C. / Savitsky, P. / Doyle, D.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2iwn.cif.gz | 55.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2iwn.ent.gz | 40.2 KB | Display | PDB format |
PDBx/mmJSON format | 2iwn.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2iwn_validation.pdf.gz | 418.4 KB | Display | wwPDB validaton report |
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Full document | 2iwn_full_validation.pdf.gz | 419.4 KB | Display | |
Data in XML | 2iwn_validation.xml.gz | 7.5 KB | Display | |
Data in CIF | 2iwn_validation.cif.gz | 10.2 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/iw/2iwn ftp://data.pdbj.org/pub/pdb/validation_reports/iw/2iwn | HTTPS FTP |
-Related structure data
Related structure data | 2bygC 2fcfC 2fneSC 2gzvC 2he2C 2he4C 2i1nC 2iwoC 2iwpC 2iwqC C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 10470.839 Da / Num. of mol.: 1 / Fragment: 3RD PDZ DOMAIN, RESIDUES 373-463 Source method: isolated from a genetically manipulated source Source: (gene. exp.) HOMO SAPIENS (human) / Plasmid: PNIC28-BSA4 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3)-R3ROSETTA / References: UniProt: O75970 |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.22 Å3/Da / Density % sol: 44.5 % / Description: NONE |
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Crystal grow | pH: 4.5 / Details: 30% PEG 10K, 0.2M LI2SO4, 0.1M ACETATE PH4.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 0.9538 |
Detector | Type: MARRESEARCH / Detector: CCD / Date: May 18, 2006 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9538 Å / Relative weight: 1 |
Reflection | Resolution: 1.35→53 Å / Num. obs: 21533 / % possible obs: 99.8 % / Observed criterion σ(I): 0 / Redundancy: 6 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 20.1 |
Reflection shell | Resolution: 1.35→1.42 Å / Redundancy: 2.7 % / Rmerge(I) obs: 0.18 / Mean I/σ(I) obs: 5 / % possible all: 99.1 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 2FNE Resolution: 1.35→38.9 Å / Cor.coef. Fo:Fc: 0.966 / Cor.coef. Fo:Fc free: 0.964 / SU B: 1.463 / SU ML: 0.028 / Cross valid method: THROUGHOUT / ESU R: 0.052 / ESU R Free: 0.048 / 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: 9.34 Å2
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Refinement step | Cycle: LAST / Resolution: 1.35→38.9 Å
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Refine LS restraints |
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