regulation of granulocyte macrophage colony-stimulating factor production / regulation of interleukin-2 production / positive regulation of lymphotoxin A production / regulation of interleukin-8 production / positive regulation of antimicrobial peptide production / Interleukin-17 signaling / positive regulation of chemokine (C-X-C motif) ligand 1 production / interleukin-17-mediated signaling pathway / regulation of transforming growth factor beta receptor signaling pathway / cytokine receptor binding ...regulation of granulocyte macrophage colony-stimulating factor production / regulation of interleukin-2 production / positive regulation of lymphotoxin A production / regulation of interleukin-8 production / positive regulation of antimicrobial peptide production / Interleukin-17 signaling / positive regulation of chemokine (C-X-C motif) ligand 1 production / interleukin-17-mediated signaling pathway / regulation of transforming growth factor beta receptor signaling pathway / cytokine receptor binding / positive regulation of cytokine production involved in inflammatory response / cartilage development / regulation of interleukin-6 production / cytokine binding / negative regulation of angiogenesis / positive regulation of cytokine production / cytokine activity / positive regulation of interleukin-6 production / Interleukin-4 and Interleukin-13 signaling / defense response to Gram-negative bacterium / adaptive immune response / defense response to Gram-positive bacterium / inflammatory response / protein heterodimerization activity / innate immune response / 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
The biologically active unit is a dimer. The assymetric unit is formed of two dimers.
-
Components
-
Protein , 1 types, 4 molecules ABXY
#1: Protein
interleukin17F / IL-17F
Mass: 15335.575 Da / Num. of mol.: 4 / Fragment: Secreted IL-17F Source method: isolated from a genetically manipulated source Details: the first four residues, GSHM, are from the vector / Source: (gene. exp.) Homo sapiens (human) / Gene: IL-17F Plasmid details: A modified plasmid was used which incorporated an N-terminal his tag and thrombin site under the control of the viral coat protein promotor Production host: unidentified baculovirus / Strain (production host): Hi5 cells / References: GenBank: 15077800, UniProt: Q96PD4*PLUS
Method to determine structure: MAD / Resolution: 2.85→30 Å / Rfactor Rfree error: 0.008 / Data cutoff high absF: 10000000 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0.2 / σ(I): 0 / Stereochemistry target values: Engh & Huber Details: The structure was solved using data collected at three different wavelenghts from crystals that had been soaked in the Hg containing compound thimerosal but was refined against a native data ...Details: The structure was solved using data collected at three different wavelenghts from crystals that had been soaked in the Hg containing compound thimerosal but was refined against a native data set collected on a crystal that was not derivatized. The crystollgraphic statistics presented here are for the native data set. Used maximum likelihood residual. The program REFMAC was used at the initial stages of refinement. A bulk solvent corrections was applied in Xplor98.1 as part of the refinement process. This correction has not been applied to the depositted structure factors
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.284
1127
5.9 %
SHELLS
Rwork
0.238
-
-
-
all
0.24
19258
-
-
obs
0.238
19202
100 %
-
Solvent computation
Solvent model: BULK SOLVENT MODEL
Displacement parameters
Biso mean: 47.9 Å2
Baniso -1
Baniso -2
Baniso -3
1-
0.22 Å2
-0.25 Å2
0 Å2
2-
-
0.22 Å2
0 Å2
3-
-
-
-0.44 Å2
Refine analyze
Free
Obs
Luzzati coordinate error
0.43 Å
0.36 Å
Luzzati d res low
-
5 Å
Luzzati sigma a
0.48 Å
0.42 Å
Refinement step
Cycle: LAST / Resolution: 2.85→30 Å
Protein
Nucleic acid
Ligand
Solvent
Total
Num. atoms
3725
0
89
27
3841
Refine LS restraints
Refine-ID
Type
Dev ideal
Dev ideal target
X-RAY DIFFRACTION
x_bond_d
0.012
X-RAY DIFFRACTION
x_angle_deg
1.6
X-RAY DIFFRACTION
x_dihedral_angle_d
28.7
X-RAY DIFFRACTION
x_improper_angle_d
0.87
X-RAY DIFFRACTION
x_mcbond_it
3.69
1.5
X-RAY DIFFRACTION
x_mcangle_it
6.24
2
X-RAY DIFFRACTION
x_scbond_it
4.15
2
X-RAY DIFFRACTION
x_scangle_it
6.09
2.5
LS refinement shell
Resolution: 2.85→3.03 Å / Rfactor Rfree error: 0.028 / Total num. of bins used: 6
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