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- PDB-5l5g: Plexin A2 full extracellular region, domains 1 to 8 modeled, data... -

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Basic information

Entry
Database: PDB / ID: 5l5g
TitlePlexin A2 full extracellular region, domains 1 to 8 modeled, data to 10 angstrom
ComponentsPlexin-A2
KeywordsSIGNALING PROTEIN / receptor / signaling / axon guidance
Function / homology
Function and homology information


cerebellar granule cell precursor tangential migration / CRMPs in Sema3A signaling / Sema3A PAK dependent Axon repulsion / SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion / semaphorin-plexin signaling pathway involved in axon guidance / semaphorin receptor complex / limb bud formation / pharyngeal system development / semaphorin receptor activity / negative regulation of cell adhesion ...cerebellar granule cell precursor tangential migration / CRMPs in Sema3A signaling / Sema3A PAK dependent Axon repulsion / SEMA3A-Plexin repulsion signaling by inhibiting Integrin adhesion / semaphorin-plexin signaling pathway involved in axon guidance / semaphorin receptor complex / limb bud formation / pharyngeal system development / semaphorin receptor activity / negative regulation of cell adhesion / neural tube development / positive regulation of axonogenesis / semaphorin-plexin signaling pathway / centrosome localization / somitogenesis / regulation of GTPase activity / regulation of cell migration / regulation of cell shape / collagen-containing extracellular matrix / cell surface receptor signaling pathway / integral component of plasma membrane / identical protein binding / plasma membrane
Similarity search - Function
Plexin-A2, sema domain / TIG domain found in plexin / Plexin, TIG domain 2 / Plexin, TIG domain 1 / TIG domain / Plexin cytoplasmic RasGAP domain / Plexin, cytoplasmic RasGAP domain / Plexin family / Plexin repeat / Plexin repeat ...Plexin-A2, sema domain / TIG domain found in plexin / Plexin, TIG domain 2 / Plexin, TIG domain 1 / TIG domain / Plexin cytoplasmic RasGAP domain / Plexin, cytoplasmic RasGAP domain / Plexin family / Plexin repeat / Plexin repeat / Sema domain / semaphorin domain / Sema domain / Sema domain profile. / Sema domain superfamily / IPT/TIG domain / Rho GTPase activation protein / ig-like, plexins, transcription factors / domain found in Plexins, Semaphorins and Integrins / PSI domain / IPT domain / Immunoglobulin E-set / WD40/YVTN repeat-like-containing domain superfamily / Immunoglobulin-like fold
Similarity search - Domain/homology
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 10 Å
AuthorsJanssen, B.J.C. / Kong, Y. / Malinauskas, T. / Vangoor, V.R. / Coles, C.H. / Kaufmann, R. / Ni, T. / Gilbert, R.J.C. / Padilla-Parra, S. / Pasterkamp, R.J. / Jones, E.Y.
CitationJournal: Neuron / Year: 2016
Title: Structural Basis for Plexin Activation and Regulation.
Authors: Kong, Y. / Janssen, B.J. / Malinauskas, T. / Vangoor, V.R. / Coles, C.H. / Kaufmann, R. / Ni, T. / Gilbert, R.J. / Padilla-Parra, S. / Pasterkamp, R.J. / Jones, E.Y.
History
DepositionMay 28, 2016Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jul 6, 2016Provider: repository / Type: Initial release
Revision 1.1Jul 20, 2016Group: Database references
Revision 1.2Aug 17, 2016Group: Database references
Revision 1.3Oct 24, 2018Group: Advisory / Data collection / Derived calculations
Category: pdbx_validate_close_contact / pdbx_validate_symm_contact ...pdbx_validate_close_contact / pdbx_validate_symm_contact / struct_conn / struct_conn_type

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Plexin-A2
B: Plexin-A2
C: Plexin-A2
D: Plexin-A2


Theoretical massNumber of molelcules
Total (without water)534,3174
Polymers534,3174
Non-polymers00
Water0
1
A: Plexin-A2
C: Plexin-A2


Theoretical massNumber of molelcules
Total (without water)267,1592
Polymers267,1592
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Plexin-A2
D: Plexin-A2


Theoretical massNumber of molelcules
Total (without water)267,1592
Polymers267,1592
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)238.400, 238.400, 642.180
Angle α, β, γ (deg.)90.00, 90.00, 120.00
Int Tables number154
Space group name H-MP3221

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Components

#1: Protein
Plexin-A2 / Plexin-2


Mass: 133579.266 Da / Num. of mol.: 4 / Fragment: UNP residues 33-1231
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Plxna2, Kiaa0463 / Cell line (production host): Hek293 / Production host: Homo sapiens (human) / References: UniProt: P70207

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity % sol: 85 %
Crystal growTemperature: 293.5 K / Method: vapor diffusion, hanging drop / pH: 7.5
Details: 0.68 M potassium/sodium tartrate, 85 mM HEPES, pH 7.5

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Diamond / Beamline: I03 / Wavelength: 0.97922 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Feb 26, 2011
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97922 Å / Relative weight: 1
ReflectionResolution: 10→63.055 Å / Num. obs: 11079 / % possible obs: 93.9 % / Redundancy: 3.3 % / Rmerge(I) obs: 0.187 / Net I/σ(I): 5.1
Reflection shellHighest resolution: 10 Å / Rmerge(I) obs: 0.882

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Processing

Software
NameVersionClassification
PHENIX1.8.2_1309refinement
iMOSFLMdata reduction
SCALAdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3OKT

3okt


Resolution: 10→63.055 Å / SU ML: 1.75 / Cross valid method: FREE R-VALUE / σ(F): 0.69 / Phase error: 41.78
Details: THE AUTHORS STATE THAT DUE TO THE LOW RESOLUTION OF THE DIFFRACTION DATA THE STRUCTURE WAS ONLY SUBJECTED TO RIGID BODY REFINEMENT WITH EACH DOMAIN AS RIGID BODY. THE STRUCTURE IS BASED ON ...Details: THE AUTHORS STATE THAT DUE TO THE LOW RESOLUTION OF THE DIFFRACTION DATA THE STRUCTURE WAS ONLY SUBJECTED TO RIGID BODY REFINEMENT WITH EACH DOMAIN AS RIGID BODY. THE STRUCTURE IS BASED ON PDB ENTRIES 3OKT AND 5L56. THE AUTHORS HAVE NOT FURTHER REFINED THE RESULTING COORDINATES NOR CORRECTED RESULTING CLASHES BETWEEN ATOMS AND DEVIATING PEPTIDE LINKAGES BETWEEN DOMAINS.
RfactorNum. reflection% reflection
Rfree0.3702 521 4.7 %
Rwork0.3351 --
obs0.3368 11079 92.53 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 10→63.055 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms28787 0 0 0 28787
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.01929564
X-RAY DIFFRACTIONf_angle_d1.72840054
X-RAY DIFFRACTIONf_dihedral_angle_d12.71410753
X-RAY DIFFRACTIONf_chiral_restr0.0814445
X-RAY DIFFRACTIONf_plane_restr0.0145210
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
10.0001-11.00160.35661410.37282608X-RAY DIFFRACTION95
11.0016-12.58260.31411410.34522659X-RAY DIFFRACTION94
12.5826-15.81130.35691210.33522670X-RAY DIFFRACTION93
15.8113-63.05610.40791180.31812621X-RAY DIFFRACTION88

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