+Open data
-Basic information
Entry | Database: PDB / ID: 5ik7 | ||||||
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Title | Laminin A2LG45 I-form, Apo. | ||||||
Components | Laminin subunit alpha-2 | ||||||
Keywords | STRUCTURAL PROTEIN / Extracellular Matrix / Ligand binding / LG domain | ||||||
Function / homology | Function and homology information regulation of basement membrane organization / Schwann cell differentiation / positive regulation of synaptic transmission, cholinergic / positive regulation of integrin-mediated signaling pathway / tissue development / protein complex involved in cell-matrix adhesion / extracellular matrix structural constituent / positive regulation of muscle cell differentiation / regulation of embryonic development / basement membrane ...regulation of basement membrane organization / Schwann cell differentiation / positive regulation of synaptic transmission, cholinergic / positive regulation of integrin-mediated signaling pathway / tissue development / protein complex involved in cell-matrix adhesion / extracellular matrix structural constituent / positive regulation of muscle cell differentiation / regulation of embryonic development / basement membrane / positive regulation of cell adhesion / synaptic cleft / regulation of cell migration / axon guidance / animal organ morphogenesis / sarcolemma / neuromuscular junction / collagen-containing extracellular matrix / dendritic spine / cell adhesion / signaling receptor binding / extracellular region Similarity search - Function | ||||||
Biological species | Mus musculus (house mouse) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å | ||||||
Authors | Briggs, D.C. / Hohenester, E. / Campbell, K.P. | ||||||
Funding support | United Kingdom, 1items
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Citation | Journal: Nat.Chem.Biol. / Year: 2016 Title: Structural basis of laminin binding to the LARGE glycans on dystroglycan. Authors: Briggs, D.C. / Yoshida-Moriguchi, T. / Zheng, T. / Venzke, D. / Anderson, M.E. / Strazzulli, A. / Moracci, M. / Yu, L. / Hohenester, E. / Campbell, K.P. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5ik7.cif.gz | 442.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5ik7.ent.gz | 370 KB | Display | PDB format |
PDBx/mmJSON format | 5ik7.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ik/5ik7 ftp://data.pdbj.org/pub/pdb/validation_reports/ik/5ik7 | HTTPS FTP |
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-Related structure data
Related structure data | 5ik4C 5ik5C 5ik8C 1dykS 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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2 |
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Unit cell |
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-Components
-Protein / Sugars , 2 types, 4 molecules AB
#1: Protein | Mass: 41405.023 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mus musculus (house mouse) / Gene: Lama2 / Cell line (production host): HEK293 / Production host: Homo sapiens (human) / References: UniProt: Q60675 #4: Sugar | |
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-Non-polymers , 4 types, 460 molecules
#2: Chemical | ChemComp-CA / #3: Chemical | ChemComp-FLC / #5: Chemical | ChemComp-EDO / #6: 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: 3.21 Å3/Da / Density % sol: 61.7 % |
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Crystal grow | Temperature: 292 K / Method: vapor diffusion, hanging drop / Details: 100mM Ammonium Citrate dibasic 18% PEG3350 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I04-1 / Wavelength: 0.92 Å |
Detector | Type: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Nov 22, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.92 Å / Relative weight: 1 |
Reflection | Resolution: 2→89.1 Å / Num. obs: 68371 / % possible obs: 95 % / Redundancy: 11.9 % / CC1/2: 0.997 / Rmerge(I) obs: 0.133 / Net I/σ(I): 12.9 |
Reflection shell | Resolution: 2→2.07 Å / Redundancy: 12.1 % / Rmerge(I) obs: 4.26 / Mean I/σ(I) obs: 1.5 / CC1/2: 0.64 / % possible all: 95.7 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1DYK Resolution: 2→89.1 Å / SU ML: 0.26 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 24.97
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→89.1 Å
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Refine LS restraints |
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LS refinement shell |
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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