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- PDB-6a77: Crystal structure of the fifth immunoglobulin domain (Ig5) of hum... -

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Basic information

Entry
Database: PDB / ID: 6a77
TitleCrystal structure of the fifth immunoglobulin domain (Ig5) of human Robo1 in complex with the Fab fragment of murine monoclonal antibody B5209B
Components
  • Heavy chain of the anti-human Robo1 antibody B5209B Fab
  • Light chain of the anti-human Robo1 antibody B5209B Fab
  • Roundabout homolog 1
KeywordsIMMUNE SYSTEM / hepatocellular carcinoma antigen / angiogenesis / antibody drug
Function / homology
Function and homology information


chemorepulsion involved in postnatal olfactory bulb interneuron migration / negative regulation of negative chemotaxis / Regulation of cortical dendrite branching / negative regulation of mammary gland epithelial cell proliferation / LRR domain binding / negative regulation of chemokine-mediated signaling pathway / heart induction / axon guidance receptor activity / Netrin-1 signaling / positive regulation of vascular endothelial growth factor signaling pathway ...chemorepulsion involved in postnatal olfactory bulb interneuron migration / negative regulation of negative chemotaxis / Regulation of cortical dendrite branching / negative regulation of mammary gland epithelial cell proliferation / LRR domain binding / negative regulation of chemokine-mediated signaling pathway / heart induction / axon guidance receptor activity / Netrin-1 signaling / positive regulation of vascular endothelial growth factor signaling pathway / Regulation of commissural axon pathfinding by SLIT and ROBO / Role of ABL in ROBO-SLIT signaling / SLIT2:ROBO1 increases RHOA activity / Roundabout signaling pathway / Inactivation of CDC42 and RAC1 / outflow tract septum morphogenesis / endocardial cushion formation / Signaling by ROBO receptors / pulmonary valve morphogenesis / positive regulation of vascular endothelial growth factor receptor signaling pathway / cell migration involved in sprouting angiogenesis / Activation of RAC1 / aortic valve morphogenesis / axon midline choice point recognition / aorta development / positive regulation of axonogenesis / positive regulation of Rho protein signal transduction / ventricular septum morphogenesis / positive regulation of Notch signaling pathway / homophilic cell adhesion via plasma membrane adhesion molecules / endoplasmic reticulum-Golgi intermediate compartment membrane / negative regulation of cell migration / positive regulation of MAP kinase activity / : / Regulation of expression of SLITs and ROBOs / nervous system development / cell adhesion / neuron projection / axon / negative regulation of gene expression / positive regulation of gene expression / cell surface / identical protein binding / plasma membrane / cytoplasm
Similarity search - Function
Roundabout homologue 1 / : / Immunoglobulin domain / Immunoglobulin I-set / Immunoglobulin I-set domain / Fibronectin type III domain / Fibronectin type 3 domain / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / Immunoglobulin V-Type ...Roundabout homologue 1 / : / Immunoglobulin domain / Immunoglobulin I-set / Immunoglobulin I-set domain / Fibronectin type III domain / Fibronectin type 3 domain / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / Immunoglobulin V-Type / Fibronectin type-III domain profile. / Fibronectin type III / Fibronectin type III superfamily / Immunoglobulin V-set domain / Immunoglobulin subtype / Immunoglobulin / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulins / Immunoglobulin-like fold / Immunoglobulin-like / Sandwich / Mainly Beta
Similarity search - Domain/homology
Roundabout homolog 1
Similarity search - Component
Biological speciesHomo sapiens (human)
Mus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2 Å
AuthorsMizohata, E. / Nakayama, T. / Kado, Y. / Inoue, T.
Funding support Japan, 1items
OrganizationGrant numberCountry
FIRST Program-MDADD Japan
CitationJournal: Structure / Year: 2019
Title: Affinity Improvement of a Cancer-Targeted Antibody through Alanine-Induced Adjustment of Antigen-Antibody Interface.
Authors: Yamashita, T. / Mizohata, E. / Nagatoishi, S. / Watanabe, T. / Nakakido, M. / Iwanari, H. / Mochizuki, Y. / Nakayama, T. / Kado, Y. / Yokota, Y. / Matsumura, H. / Kawamura, T. / Kodama, T. / ...Authors: Yamashita, T. / Mizohata, E. / Nagatoishi, S. / Watanabe, T. / Nakakido, M. / Iwanari, H. / Mochizuki, Y. / Nakayama, T. / Kado, Y. / Yokota, Y. / Matsumura, H. / Kawamura, T. / Kodama, T. / Hamakubo, T. / Inoue, T. / Fujitani, H. / Tsumoto, K.
History
DepositionJul 2, 2018Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Jan 30, 2019Provider: repository / Type: Initial release
Revision 1.1Mar 20, 2019Group: Data collection / Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.year

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Roundabout homolog 1
L: Light chain of the anti-human Robo1 antibody B5209B Fab
H: Heavy chain of the anti-human Robo1 antibody B5209B Fab


Theoretical massNumber of molelcules
Total (without water)56,3743
Polymers56,3743
Non-polymers00
Water2,864159
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5070 Å2
ΔGint-31 kcal/mol
Surface area23040 Å2
MethodPISA
Unit cell
Length a, b, c (Å)100.566, 100.566, 122.756
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number96
Space group name H-MP43212

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Components

#1: Protein Roundabout homolog 1 / Deleted in U twenty twenty / H-Robo-1


Mass: 9776.106 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ROBO1, DUTT1 / Production host: Escherichia coli (E. coli) / References: UniProt: Q9Y6N7
#2: Antibody Light chain of the anti-human Robo1 antibody B5209B Fab


Mass: 23098.506 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Cell line (production host): HEK293 / Production host: Homo sapiens (human)
#3: Antibody Heavy chain of the anti-human Robo1 antibody B5209B Fab


Mass: 23499.217 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Cell line (production host): HEK293 / Production host: Homo sapiens (human)
#4: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 159 / Source method: isolated from a natural source / Formula: H2O

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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 Matthews: 2.75 Å3/Da / Density % sol: 55.32 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 5.6
Details: 100 mM sodium citrate tribasic dihydrate (pH 5.6), 10% (w/v) PEG 8000, 10% (v/v) 2-propanol

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SPring-8 / Beamline: BL38B1 / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Nov 1, 2010
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2→50 Å / Num. obs: 42067 / % possible obs: 97.1 % / Redundancy: 10.4 % / Net I/σ(I): 56.9
Reflection shellResolution: 2→2.07 Å

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Processing

Software
NameVersionClassification
REFMAC5.8.0158refinement
HKL-2000data reduction
Cootmodel building
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2→50 Å / Cor.coef. Fo:Fc: 0.955 / Cor.coef. Fo:Fc free: 0.939 / SU B: 7.349 / SU ML: 0.182 / Cross valid method: THROUGHOUT / ESU R: 0.204 / ESU R Free: 0.183 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.2782 2048 4.9 %RANDOM
Rwork0.23801 ---
obs0.23994 39899 97.16 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å
Displacement parametersBiso mean: 56.661 Å2
Baniso -1Baniso -2Baniso -3
1--1.87 Å20 Å20 Å2
2---1.87 Å20 Å2
3---3.74 Å2
Refinement stepCycle: 1 / Resolution: 2→50 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms3931 0 0 159 4090
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0190.024039
X-RAY DIFFRACTIONr_bond_other_d0.0020.023624
X-RAY DIFFRACTIONr_angle_refined_deg2.1021.9525501
X-RAY DIFFRACTIONr_angle_other_deg1.11838459
X-RAY DIFFRACTIONr_dihedral_angle_1_deg7.9965519
X-RAY DIFFRACTIONr_dihedral_angle_2_deg37.74324.079152
X-RAY DIFFRACTIONr_dihedral_angle_3_deg18.58315647
X-RAY DIFFRACTIONr_dihedral_angle_4_deg17.351519
X-RAY DIFFRACTIONr_chiral_restr0.130.2632
X-RAY DIFFRACTIONr_gen_planes_refined0.010.0214461
X-RAY DIFFRACTIONr_gen_planes_other0.0020.02794
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it5.4695.6352079
X-RAY DIFFRACTIONr_mcbond_other5.4685.6332078
X-RAY DIFFRACTIONr_mcangle_it7.3328.4182594
X-RAY DIFFRACTIONr_mcangle_other7.3318.422595
X-RAY DIFFRACTIONr_scbond_it5.5865.911960
X-RAY DIFFRACTIONr_scbond_other5.5845.9121961
X-RAY DIFFRACTIONr_scangle_it
X-RAY DIFFRACTIONr_scangle_other7.5998.7152906
X-RAY DIFFRACTIONr_long_range_B_refined10.52416281
X-RAY DIFFRACTIONr_long_range_B_other10.52216230
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2→2.052 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.466 145 -
Rwork0.451 2975 -
obs--99.46 %

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