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Open data
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Basic information
Entry | Database: PDB / ID: 2v70 | ||||||
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Title | Third LRR domain of human Slit2 | ||||||
![]() | SLIT HOMOLOG 2 PROTEIN N-PRODUCT | ||||||
![]() | STRUCTURAL PROTEIN / NEUROGENESIS / GLYCOPROTEIN / SLIT2 / SECRETED / CHEMOTAXIS / LRR DOMAIN / DIFFERENTIATION / EGF-LIKE DOMAIN / LEUCINE-RICH REPEAT / DEVELOPMENTAL PROTEIN | ||||||
Function / homology | ![]() negative regulation of leukocyte chemotaxis / corticospinal neuron axon guidance through spinal cord / negative regulation of lamellipodium assembly / induction of negative chemotaxis / negative regulation of mononuclear cell migration / negative regulation of retinal ganglion cell axon guidance / apoptotic process involved in luteolysis / negative regulation of monocyte chemotaxis / chemorepulsion involved in postnatal olfactory bulb interneuron migration / Roundabout binding ...negative regulation of leukocyte chemotaxis / corticospinal neuron axon guidance through spinal cord / negative regulation of lamellipodium assembly / induction of negative chemotaxis / negative regulation of mononuclear cell migration / negative regulation of retinal ganglion cell axon guidance / apoptotic process involved in luteolysis / negative regulation of monocyte chemotaxis / chemorepulsion involved in postnatal olfactory bulb interneuron migration / Roundabout binding / negative regulation of smooth muscle cell chemotaxis / negative regulation of cellular response to growth factor stimulus / cellular response to heparin / negative regulation of small GTPase mediated signal transduction / negative regulation of chemokine-mediated signaling pathway / response to cortisol / laminin-1 binding / negative regulation of smooth muscle cell migration / axon extension involved in axon guidance / Formation of the ureteric bud / Netrin-1 signaling / GTPase inhibitor activity / Role of ABL in ROBO-SLIT signaling / Regulation of commissural axon pathfinding by SLIT and ROBO / negative regulation of neutrophil chemotaxis / SLIT2:ROBO1 increases RHOA activity / Roundabout signaling pathway / Inactivation of CDC42 and RAC1 / negative regulation of actin filament polymerization / Signaling by ROBO receptors / pulmonary valve morphogenesis / negative regulation of vascular permeability / aortic valve morphogenesis / cell migration involved in sprouting angiogenesis / Activation of RAC1 / motor neuron axon guidance / proteoglycan binding / negative regulation of endothelial cell migration / ureteric bud development / negative chemotaxis / positive regulation of axonogenesis / retinal ganglion cell axon guidance / branching morphogenesis of an epithelial tube / ventricular septum morphogenesis / cellular response to hormone stimulus / negative regulation of cell migration / negative regulation of protein phosphorylation / axon guidance / negative regulation of cell growth / Regulation of expression of SLITs and ROBOs / heparin binding / positive regulation of apoptotic process / calcium ion binding / protein homodimerization activity / extracellular space / extracellular exosome / extracellular region / identical protein binding / membrane / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Morlot, C. / Cusack, S. / McCarthy, A.A. | ||||||
![]() | ![]() Title: Production of Slit2 Lrr Domains in Mammalian Cells for Structural Studies and the Structure of Human Slit2 Domain 3. Authors: Morlot, C. / Hemrika, W. / Romijn, R.A. / Gros, P. / Cusack, S. / Mccarthy, A.A. | ||||||
History |
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Remark 650 | HELIX DETERMINATION METHOD: AUTHOR PROVIDED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 169.1 KB | Display | ![]() |
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PDB format | ![]() | 133.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 480.6 KB | Display | ![]() |
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Full document | ![]() | 495.7 KB | Display | |
Data in XML | ![]() | 31.2 KB | Display | |
Data in CIF | ![]() | 41.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1w8aS S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
NCS oper:
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Components
#1: Protein | Mass: 24886.449 Da / Num. of mol.: 4 / Fragment: THIRD LRR DOMAIN, RESIDUES 504-714 Source method: isolated from a genetically manipulated source Details: GLYCOSYLATION ON N623 / Source: (gene. exp.) ![]() ![]() #2: Sugar | ChemComp-NAG / |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.7 Å3/Da / Density % sol: 54.6 % / Description: NONE |
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Crystal grow | pH: 5.6 Details: 15% PEG 4000, 0.2M NH4 ACETATE, 0.1M NACITRATE, PH=5.6. |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Apr 22, 2005 / Details: TORODIAL |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9393 Å / Relative weight: 1 |
Reflection | Resolution: 3→30 Å / Num. obs: 45165 / % possible obs: 91.9 % / Observed criterion σ(I): 0 / Redundancy: 2.3 % / Rmerge(I) obs: 0.09 / Net I/σ(I): 11.1 |
Reflection shell | Resolution: 3→3.5 Å / Redundancy: 2.4 % / Rmerge(I) obs: 0.3 / Mean I/σ(I) obs: 3.2 / % possible all: 94.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: MODIFIED PDB ENTRY 1W8A Resolution: 3.01→30 Å / Cor.coef. Fo:Fc: 0.911 / Cor.coef. Fo:Fc free: 0.869 / SU B: 50.217 / SU ML: 0.396 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R Free: 0.501 / 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: 34.97 Å2
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Refinement step | Cycle: LAST / Resolution: 3.01→30 Å
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Refine LS restraints |
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