+Open data
-Basic information
Entry | Database: PDB / ID: 4cnu | ||||||
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Title | CRYSTAL STRUCTURE OF WT HUMAN CRMP-4 from lattice translocation | ||||||
Components | DIHYDROPYRIMIDINASE-LIKE 3 | ||||||
Keywords | SIGNALING PROTEIN / NEUROGENESIS / AXONAL OUTGROWTH / DEVELOPMENTAL PROTEIN | ||||||
Function / homology | Function and homology information hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides / chondroitin sulfate binding / filamin binding / actin crosslink formation / exocytic vesicle / CRMPs in Sema3A signaling / positive regulation of filopodium assembly / cellular response to cytokine stimulus / filamentous actin / actin filament bundle assembly ...hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides / chondroitin sulfate binding / filamin binding / actin crosslink formation / exocytic vesicle / CRMPs in Sema3A signaling / positive regulation of filopodium assembly / cellular response to cytokine stimulus / filamentous actin / actin filament bundle assembly / neuron development / response to axon injury / negative regulation of cell migration / positive regulation of neuron projection development / SH3 domain binding / negative regulation of neuron projection development / lamellipodium / cell body / growth cone / synapse / extracellular space / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | HOMO SAPIENS (human) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.8 Å | ||||||
Authors | Ponnusamy, R. / Lebedev, A. / Lohkamp, B. | ||||||
Citation | Journal: Acta Crystallogr.,Sect.D / Year: 2014 Title: Crystal Structure of Human Crmp-4: Correction of Intensities for Lattice-Translocation Disorder Authors: Ponnusamy, R. / Lebedev, A. / Pahlow, S. / Lohkamp, B. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4cnu.cif.gz | 193.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4cnu.ent.gz | 155.1 KB | Display | PDB format |
PDBx/mmJSON format | 4cnu.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cn/4cnu ftp://data.pdbj.org/pub/pdb/validation_reports/cn/4cnu | HTTPS FTP |
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-Related structure data
Related structure data | 4cnsSC 4cntC 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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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: 0 / Ens-ID: 1 / Beg auth comp-ID: ILE / Beg label comp-ID: ILE / End auth comp-ID: TYR / End label comp-ID: TYR / Refine code: 0 / Auth seq-ID: 12 - 499 / Label seq-ID: 12 - 499
NCS oper: (Code: given) |
-Components
#1: Protein | Mass: 62049.148 Da / Num. of mol.: 2 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) / Variant (production host): PLYSS / References: UniProt: Q14195 Sequence details | ISOFORM 2 GENBANK REF NP_001378.1 | |
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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: 2.43 Å3/Da / Density % sol: 49.3 % / Description: NONE |
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Crystal grow | pH: 7 Details: 23% (W/V) PEG 3350, 200 MM NA TARTRATE, 100 MM BIS-TRIS PROPANE PH 7.0, 50 MM NA FLUORIDE |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: MAX II / Beamline: I911-3 / Wavelength: 1.07068 |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Feb 25, 2012 / Details: MIRRORS |
Radiation | Monochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.07068 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→39.4 Å / Num. obs: 28951 / % possible obs: 93.2 % / Observed criterion σ(I): -3 / Redundancy: 5.7 % / Biso Wilson estimate: 34.9 Å2 / Rmerge(I) obs: 0.24 / Net I/σ(I): 4.9 |
Reflection shell | Resolution: 2.8→2.95 Å / Redundancy: 5.8 % / Rmerge(I) obs: 1.21 / Mean I/σ(I) obs: 1.2 / % possible all: 84.4 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 4CNS Resolution: 2.8→39.43 Å / Cor.coef. Fo:Fc: 0.927 / Cor.coef. Fo:Fc free: 0.898 / SU B: 17.095 / SU ML: 0.329 / Cross valid method: THROUGHOUT / ESU R Free: 0.45 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY. DATA WERE CORRECTED FOR LATTICE TRANSLOCATION DISORDER ITERATIVELY BEFORE REFINEMENT.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 46.273 Å2
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Refinement step | Cycle: LAST / Resolution: 2.8→39.43 Å
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Refine LS restraints |
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