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- PDB-9sg0: CJM112 Fv in complex with human IL-17A -

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Basic information

Entry
Database: PDB / ID: 9sg0
TitleCJM112 Fv in complex with human IL-17A
Components
  • CJM112 Fv heavy-chain
  • CJM112 Fv light-chain
  • Interleukin-17A
KeywordsCYTOKINE / MONOCLONAL ANTIBODY / THERAPEUTIC ANTIBODY / FV FRAGMENT
Function / homology
Function and homology information


positive regulation of interleukin-16 production / granulocyte migration / positive regulation of antimicrobial peptide production / Interleukin-17 signaling / cell death / interleukin-17A-mediated signaling pathway / positive regulation of interleukin-23 production / negative regulation of inflammatory response to wounding / positive regulation of chemokine (C-X-C motif) ligand 1 production / interleukin-17-mediated signaling pathway ...positive regulation of interleukin-16 production / granulocyte migration / positive regulation of antimicrobial peptide production / Interleukin-17 signaling / cell death / interleukin-17A-mediated signaling pathway / positive regulation of interleukin-23 production / negative regulation of inflammatory response to wounding / positive regulation of chemokine (C-X-C motif) ligand 1 production / interleukin-17-mediated signaling pathway / intestinal epithelial structure maintenance / fibroblast activation / positive regulation of bicellular tight junction assembly / positive regulation of osteoclast differentiation / positive regulation of cytokine production involved in inflammatory response / keratinocyte proliferation / cellular response to interleukin-1 / defense response to fungus / keratinocyte differentiation / Notch signaling pathway / positive regulation of interleukin-12 production / positive regulation of interleukin-1 beta production / cytokine activity / positive regulation of interleukin-6 production / response to wounding / positive regulation of tumor necrosis factor production / cell-cell signaling / Interleukin-4 and Interleukin-13 signaling / defense response to Gram-negative bacterium / gene expression / adaptive immune response / defense response to Gram-positive bacterium / immune response / inflammatory response / protein heterodimerization activity / innate immune response / external side of plasma membrane / apoptotic process / SARS-CoV-2 activates/modulates innate and adaptive immune responses / protein homodimerization activity / positive regulation of transcription by RNA polymerase II / extracellular space / extracellular region
Similarity search - Function
Interleukin-17, chordata / Interleukin-17 family / Interleukin-17 / Cystine-knot cytokine
Similarity search - Domain/homology
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.65 Å
AuthorsRondeau, J.-M. / Lehmann, S.
Funding support1items
OrganizationGrant numberCountry
Not funded
CitationJournal: Mabs / Year: 2025
Title: IL-17A complexes with therapeutic antibodies exhibit distinct size distributions, potentially contributing to clinically observed immunogenicity.
Authors: Ungan, D. / Be, C. / Baczyk, P. / Mittermeier, S. / Lehmann, S. / Wiesmann, C. / Huber, T. / Kolbinger, F. / Rondeau, J.M.
History
DepositionAug 21, 2025Deposition site: PDBE / Processing site: PDBE
Revision 1.0Oct 29, 2025Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Interleukin-17A
H: CJM112 Fv heavy-chain
L: CJM112 Fv light-chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)42,3924
Polymers42,2963
Non-polymers961
Water00
1
A: Interleukin-17A
H: CJM112 Fv heavy-chain
L: CJM112 Fv light-chain
hetero molecules

A: Interleukin-17A
H: CJM112 Fv heavy-chain
L: CJM112 Fv light-chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)84,7848
Polymers84,5926
Non-polymers1922
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation3_654-x+1,y,-z-1/21
Buried area11570 Å2
ΔGint-88 kcal/mol
Surface area27930 Å2
MethodPISA
Unit cell
Length a, b, c (Å)55.720, 87.030, 156.260
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number20
Space group name H-MC2221

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Components

#1: Protein Interleukin-17A / IL-17 / IL-17A / Cytotoxic T-lymphocyte-associated antigen 8 / CTLA-8


Mass: 15919.918 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: The construct included a non-cleavable, N-terminal APP6 tag (EFRHDS)
Source: (gene. exp.) Homo sapiens (human) / Gene: IL17A, CTLA8, IL17 / Cell line (production host): HEK 293-6E / Production host: Homo sapiens (human) / References: UniProt: Q16552
#2: Antibody CJM112 Fv heavy-chain


Mass: 13723.221 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: The construct included a non-cleavable, C-terminal His6 tag
Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / Strain (production host): TG1
#3: Antibody CJM112 Fv light-chain


Mass: 12653.034 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: The construct included a non-cleavable, C-terminal Strep tag (WSHPQFEK)
Source: (gene. exp.) Homo sapiens (human) / Production host: Escherichia coli (E. coli) / Strain (production host): TG1
#4: Chemical ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: SO4
Has ligand of interestN
Has protein modificationY

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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: 2.24 Å3/Da / Density % sol: 45.08 %
Crystal growTemperature: 292 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: 0.1M MES pH 6.5, 0.2M ammonium sulfate, 15% PEG 5,000 MME

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X10SA / Wavelength: 0.99984 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Feb 20, 2012
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.99984 Å / Relative weight: 1
ReflectionResolution: 2.65→78.13 Å / Num. obs: 11404 / % possible obs: 99.9 % / Redundancy: 6.5 % / CC1/2: 0.999 / Rmerge(I) obs: 0.073 / Rrim(I) all: 0.079 / Net I/σ(I): 13.2
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. unique obsCC1/2Rrim(I) all% possible all
2.65-2.726.773.7260.58440.334.037100
2.72-2.796.522.9260.647960.4473.18299.9
2.79-2.876.51.9650.957880.5812.137100
2.87-2.966.551.4371.367630.7851.56199.7
2.96-3.066.880.9822.087410.9451.063100
3.06-3.176.830.712.787090.9440.769100
3.17-3.296.670.4224.326990.9710.45899.9
3.29-3.426.410.2656.226700.9880.289100
3.42-3.576.30.1619.326330.9960.17699.8
3.57-3.756.560.13112.096290.9950.14399.8
3.75-3.956.690.09914.935950.9980.10899.8
3.95-4.196.650.07619.155430.9980.08399.8
4.19-4.486.350.05626.345270.9990.06299.8
4.48-4.846.280.04631.074880.9990.0599.8
4.84-5.36.720.0435.624570.9990.043100
5.3-5.936.490.04333.794200.9990.047100
5.93-6.846.060.0435.483720.9990.044100
6.84-8.386.060.03539.313190.9980.039100
8.38-11.855.750.02846.732590.9990.03100
11.85-78.135.140.02545.761520.9990.02898.7

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Processing

Software
NameVersionClassification
BUSTER2.11.7refinement
XSCALEdata scaling
XDSdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.65→78.13 Å / Cor.coef. Fo:Fc: 0.932 / Cor.coef. Fo:Fc free: 0.904 / Rfactor Rfree error: 0 / SU R Cruickshank DPI: 0.713 / Cross valid method: THROUGHOUT / σ(F): 0 / SU R Blow DPI: 0.706 / SU Rfree Blow DPI: 0.313 / SU Rfree Cruickshank DPI: 0.318
RfactorNum. reflection% reflectionSelection details
Rfree0.256 570 5 %RANDOM
Rwork0.195 ---
obs0.198 11398 99.8 %-
Displacement parametersBiso mean: 137.72 Å2
Baniso -1Baniso -2Baniso -3
1--3.6184 Å20 Å20 Å2
2---31.7467 Å20 Å2
3---35.3651 Å2
Refine analyzeLuzzati coordinate error obs: 0.46 Å
Refinement stepCycle: 1 / Resolution: 2.65→78.13 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms2515 0 5 0 2520
Refine LS restraints
Refine-IDTypeDev idealNumberRestraint functionWeight
X-RAY DIFFRACTIONt_bond_d0.012584HARMONIC2
X-RAY DIFFRACTIONt_angle_deg1.273513HARMONIC2
X-RAY DIFFRACTIONt_dihedral_angle_d866SINUSOIDAL2
X-RAY DIFFRACTIONt_incorr_chiral_ct
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_trig_c_planes61HARMONIC2
X-RAY DIFFRACTIONt_gen_planes373HARMONIC5
X-RAY DIFFRACTIONt_it2584HARMONIC20
X-RAY DIFFRACTIONt_nbd
X-RAY DIFFRACTIONt_omega_torsion3.24
X-RAY DIFFRACTIONt_other_torsion21.45
X-RAY DIFFRACTIONt_improper_torsion
X-RAY DIFFRACTIONt_chiral_improper_torsion325SEMIHARMONIC5
X-RAY DIFFRACTIONt_sum_occupancies
X-RAY DIFFRACTIONt_utility_distance
X-RAY DIFFRACTIONt_utility_angle
X-RAY DIFFRACTIONt_utility_torsion
X-RAY DIFFRACTIONt_ideal_dist_contact2755SEMIHARMONIC4
LS refinement shellResolution: 2.65→2.9 Å / Rfactor Rfree error: 0 / Total num. of bins used: 6
RfactorNum. reflection% reflection
Rfree0.39 133 4.97 %
Rwork0.277 2541 -
all0.282 2674 -
obs--99.7 %
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
13.22141.486-0.4317.3441-1.28073.73770.03510.33020.14490.08110.18590.46690.0444-0.7263-0.2210.09760.02-0.14430.25290.0173-0.282522.49150.1787-34.9619
27.39061.6308-1.70283.81353.93574.30710.26110.3929-0.50740.6465-0.44190.82871.0885-1.08850.18070.0929-0.304-0.02050.13650.1387-0.156410.9137-8.6685-10.1024
34.79410.1857-0.99213.7011.599812.1315-0.0043-0.3229-0.0220.40220.858-0.65121.08851.0885-0.85370.21660.2209-0.2182-0.2317-0.1143-0.128533.2261-11.1262-14.2305
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1{ A|* }
2X-RAY DIFFRACTION2{ H|* }
3X-RAY DIFFRACTION3{ L|* }

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