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- PDB-8dpu: The crystal structure of the IL-11 signalling complex -

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Basic information

Entry
Database: PDB / ID: 8dpu
TitleThe crystal structure of the IL-11 signalling complex
Components
  • Interleukin-11
  • Interleukin-11 receptor subunit alpha
  • Interleukin-6 receptor subunit beta
KeywordsCYTOKINE / Complex / GP130 / glycoprotein 130 / signalling / cancer / CYTOKINE-RECEPTOR complex
Function / homology
Function and homology information


interleukin-11 receptor binding / oncostatin-M-mediated signaling pathway / ciliary neurotrophic factor receptor activity / negative regulation of interleukin-6-mediated signaling pathway / leukemia inhibitory factor signaling pathway / interleukin-27 receptor activity / oncostatin-M receptor complex / ciliary neurotrophic factor receptor binding / interleukin-11 receptor activity / interleukin-11 binding ...interleukin-11 receptor binding / oncostatin-M-mediated signaling pathway / ciliary neurotrophic factor receptor activity / negative regulation of interleukin-6-mediated signaling pathway / leukemia inhibitory factor signaling pathway / interleukin-27 receptor activity / oncostatin-M receptor complex / ciliary neurotrophic factor receptor binding / interleukin-11 receptor activity / interleukin-11 binding / interleukin-6 receptor activity / interleukin-6 binding / ciliary neurotrophic factor-mediated signaling pathway / ciliary neurotrophic factor receptor complex / interleukin-27-mediated signaling pathway / interleukin-6 receptor complex / head development / megakaryocyte differentiation / negative regulation of hormone secretion / interleukin-11-mediated signaling pathway / T-helper 17 cell lineage commitment / positive regulation of adaptive immune response / developmental process / positive regulation of acute inflammatory response / positive regulation of astrocyte differentiation / intestinal epithelial cell development / positive regulation of platelet aggregation / Interleukin-27 signaling / IL-6-type cytokine receptor ligand interactions / Interleukin-35 Signalling / cytokine receptor activity / glycogen metabolic process / interleukin-6-mediated signaling pathway / Interleukin-6 signaling / positive regulation of Notch signaling pathway / protein tyrosine kinase activator activity / positive regulation of cardiac muscle hypertrophy / cytokine binding / fat cell differentiation / MAPK3 (ERK1) activation / growth factor binding / MAPK1 (ERK2) activation / positive regulation of vascular endothelial growth factor production / positive regulation of osteoblast differentiation / coreceptor activity / positive regulation of T cell proliferation / positive regulation of tyrosine phosphorylation of STAT protein / B cell differentiation / response to cytokine / cytokine activity / growth factor activity / cytokine-mediated signaling pathway / transmembrane signaling receptor activity / positive regulation of peptidyl-tyrosine phosphorylation / positive regulation of peptidyl-serine phosphorylation / scaffold protein binding / negative regulation of neuron apoptotic process / cell population proliferation / positive regulation of MAPK cascade / receptor complex / membrane raft / external side of plasma membrane / neuronal cell body / dendrite / positive regulation of cell population proliferation / negative regulation of apoptotic process / positive regulation of transcription by RNA polymerase II / extracellular space / extracellular exosome / extracellular region / identical protein binding / membrane / plasma membrane / cytoplasm
Similarity search - Function
Interleukin-11, mammalian / Interleukin-11 / Interleukin 11 / Type I cytokine receptor, cytokine-binding domain / Interleukin-6 receptor alpha chain, binding / Immunoglobulin C2-set-like, ligand-binding / Ig-like C2-type domain / Long hematopoietin receptor, soluble alpha chain, conserved site / Long hematopoietin receptor, soluble alpha chains family signature. / Long hematopoietin receptor, Gp130 family 2, conserved site ...Interleukin-11, mammalian / Interleukin-11 / Interleukin 11 / Type I cytokine receptor, cytokine-binding domain / Interleukin-6 receptor alpha chain, binding / Immunoglobulin C2-set-like, ligand-binding / Ig-like C2-type domain / Long hematopoietin receptor, soluble alpha chain, conserved site / Long hematopoietin receptor, soluble alpha chains family signature. / Long hematopoietin receptor, Gp130 family 2, conserved site / Long hematopoietin receptor, gp130 family signature. / Four-helical cytokine-like, core / Fibronectin type III domain / Fibronectin type 3 domain / Fibronectin type-III domain profile. / Fibronectin type III / Fibronectin type III superfamily / Immunoglobulin subtype / Immunoglobulin / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulin-like fold
Similarity search - Domain/homology
Interleukin-11 / Interleukin-6 receptor subunit beta / Interleukin-11 receptor subunit alpha
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.78 Å
AuthorsMetcalfe, R.D. / Aizel, K. / Griffin, M.D.W.
Funding support Australia, 1items
OrganizationGrant numberCountry
National Health and Medical Research Council (NHMRC, Australia)APP1147621 Australia
CitationJournal: Nat Commun / Year: 2023
Title: Structures of the interleukin 11 signalling complex reveal gp130 dynamics and the inhibitory mechanism of a cytokine variant.
Authors: Riley D Metcalfe / Eric Hanssen / Ka Yee Fung / Kaheina Aizel / Clara C Kosasih / Courtney O Zlatic / Larissa Doughty / Craig J Morton / Andrew P Leis / Michael W Parker / Paul R Gooley / ...Authors: Riley D Metcalfe / Eric Hanssen / Ka Yee Fung / Kaheina Aizel / Clara C Kosasih / Courtney O Zlatic / Larissa Doughty / Craig J Morton / Andrew P Leis / Michael W Parker / Paul R Gooley / Tracy L Putoczki / Michael D W Griffin /
Abstract: Interleukin (IL-)11, an IL-6 family cytokine, has pivotal roles in autoimmune diseases, fibrotic complications, and solid cancers. Despite intense therapeutic targeting efforts, structural ...Interleukin (IL-)11, an IL-6 family cytokine, has pivotal roles in autoimmune diseases, fibrotic complications, and solid cancers. Despite intense therapeutic targeting efforts, structural understanding of IL-11 signalling and mechanistic insights into current inhibitors are lacking. Here we present cryo-EM and crystal structures of the human IL-11 signalling complex, including the complex containing the complete extracellular domains of the shared IL-6 family β-receptor, gp130. We show that complex formation requires conformational reorganisation of IL-11 and that the membrane-proximal domains of gp130 are dynamic. We demonstrate that the cytokine mutant, IL-11 Mutein, competitively inhibits signalling in human cell lines. Structural shifts in IL-11 Mutein underlie inhibition by altering cytokine binding interactions at all three receptor-engaging sites and abrogating the final gp130 binding step. Our results reveal the structural basis of IL-11 signalling, define the molecular mechanisms of an inhibitor, and advance understanding of gp130-containing receptor complexes, with potential applications in therapeutic development.
History
DepositionJul 17, 2022Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 29, 2023Provider: repository / Type: Initial release
Revision 1.1May 1, 2024Group: Database references / Category: citation
Item: _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Interleukin-6 receptor subunit beta
B: Interleukin-11
C: Interleukin-11 receptor subunit alpha
D: Interleukin-6 receptor subunit beta
E: Interleukin-11
F: Interleukin-11 receptor subunit alpha
G: Interleukin-6 receptor subunit beta
H: Interleukin-11
I: Interleukin-11 receptor subunit alpha
J: Interleukin-6 receptor subunit beta
K: Interleukin-11
L: Interleukin-11 receptor subunit alpha
M: Interleukin-6 receptor subunit beta
N: Interleukin-11
O: Interleukin-11 receptor subunit alpha
P: Interleukin-6 receptor subunit beta
Q: Interleukin-11
R: Interleukin-11 receptor subunit alpha
hetero molecules


Theoretical massNumber of molelcules
Total (without water)561,23148
Polymers551,18318
Non-polymers10,04730
Water00
1
A: Interleukin-6 receptor subunit beta
B: Interleukin-11
C: Interleukin-11 receptor subunit alpha
D: Interleukin-6 receptor subunit beta
E: Interleukin-11
F: Interleukin-11 receptor subunit alpha
hetero molecules


Theoretical massNumber of molelcules
Total (without water)187,07716
Polymers183,7286
Non-polymers3,34910
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
G: Interleukin-6 receptor subunit beta
H: Interleukin-11
I: Interleukin-11 receptor subunit alpha
J: Interleukin-6 receptor subunit beta
K: Interleukin-11
L: Interleukin-11 receptor subunit alpha
hetero molecules


Theoretical massNumber of molelcules
Total (without water)187,07716
Polymers183,7286
Non-polymers3,34910
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
M: Interleukin-6 receptor subunit beta
N: Interleukin-11
O: Interleukin-11 receptor subunit alpha
P: Interleukin-6 receptor subunit beta
Q: Interleukin-11
R: Interleukin-11 receptor subunit alpha
hetero molecules


Theoretical massNumber of molelcules
Total (without water)187,07716
Polymers183,7286
Non-polymers3,34910
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)163.411, 163.411, 506.623
Angle α, β, γ (deg.)90.000, 90.000, 120.000
Int Tables number151
Space group name H-MP3112
Space group name HallP312(x,y,z+1/3)
Symmetry operation#1: x,y,z
#2: -y,x-y,z+1/3
#3: -x+y,-x,z+2/3
#4: -y,-x,-z+2/3
#5: -x+y,y,-z+1/3
#6: x,x-y,-z
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
d_1ens_1chain "G"
d_2ens_1chain "D"
d_3ens_1chain "A"
d_4ens_1chain "J"
d_5ens_1chain "M"
d_6ens_1chain "P"
d_1ens_2chain "N"
d_2ens_2chain "E"
d_3ens_2chain "H"
d_4ens_2chain "K"
d_5ens_2chain "B"
d_6ens_2chain "Q"
d_1ens_3chain "R"
d_2ens_3chain "F"
d_3ens_3chain "I"
d_4ens_3chain "L"
d_5ens_3chain "O"
d_6ens_3chain "C"

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg label comp-IDEnd label comp-IDLabel asym-IDLabel seq-ID
d_11ens_1ASPGLUE1 - 298
d_12ens_1NAGNAGX
d_13ens_1NAGNAGX
d_14ens_1NAGNAGY
d_15ens_1NAGNAGY
d_21ens_1ASPGLUD1 - 298
d_22ens_1NAGNAGV
d_23ens_1NAGNAGV
d_24ens_1NAGNAGW
d_25ens_1NAGNAGW
d_31ens_1ASPGLUA1 - 298
d_32ens_1NAGNAGS
d_33ens_1NAGNAGS
d_34ens_1NAGNAGT
d_35ens_1NAGNAGT
d_41ens_1ASPGLUF1 - 298
d_42ens_1NAGNAGZ
d_43ens_1NAGNAGZ
d_44ens_1NAGNAGAA
d_45ens_1NAGNAGAA
d_51ens_1ASPGLUG1 - 298
d_52ens_1NAGNAGBA
d_53ens_1NAGNAGBA
d_54ens_1NAGNAGCA
d_55ens_1NAGNAGCA
d_61ens_1ASPGLUH1 - 298
d_62ens_1NAGNAGDA
d_63ens_1NAGNAGDA
d_64ens_1NAGNAGEA
d_65ens_1NAGNAGEA
d_11ens_2ARGLEUL1 - 164
d_21ens_2ARGLEUI1 - 164
d_31ens_2ARGLEUJ1 - 164
d_41ens_2ARGLEUK1 - 164
d_51ens_2ARGLEUB1 - 164
d_61ens_2ARGLEUM1 - 164
d_11ens_3PROSERR1 - 283
d_12ens_3NAGNAGVA
d_13ens_3NAGNAGJA
d_14ens_3NAGNAGJA
d_15ens_3BMABMAJA
d_21ens_3PROSERN1 - 283
d_22ens_3NAGNAGRA
d_23ens_3NAGNAGFA
d_24ens_3NAGNAGFA
d_25ens_3BMABMAFA
d_31ens_3PROSERO1 - 283
d_32ens_3NAGNAGSA
d_33ens_3NAGNAGGA
d_34ens_3NAGNAGGA
d_35ens_3BMABMAGA
d_41ens_3PROSERP1 - 283
d_42ens_3NAGNAGTA
d_43ens_3NAGNAGHA
d_44ens_3NAGNAGHA
d_45ens_3BMABMAHA
d_51ens_3PROSERQ1 - 283
d_52ens_3NAGNAGUA
d_53ens_3NAGNAGIA
d_54ens_3NAGNAGIA
d_55ens_3BMABMAIA
d_61ens_3PROSERC1 - 283
d_62ens_3NAGNAGLA
d_63ens_3NAGNAGU
d_64ens_3NAGNAGU
d_65ens_3BMABMAU

NCS ensembles :
ID
ens_1
ens_2
ens_3

NCS oper:
IDCodeMatrixVector
1given(-0.265502677675, -0.607468399371, -0.748659115962), (-0.494124936406, 0.752524864168, -0.435369815249), (0.827858004352, 0.254339286337, -0.499962650661)64.3196395708, 28.0701618481, -2.77641223555
2given(0.207530926847, 0.583564528786, 0.785100856671), (0.589169859717, -0.715245742134, 0.37590212125), (0.780903189136, 0.384546445961, -0.492254243349)-32.0944372553, 80.001359607, -9.42690200553
3given(0.305230767718, 0.52263165459, -0.796046689622), (0.515168696934, -0.793675965127, -0.323542386836), (-0.800896617634, -0.311343244668, -0.511497792626)-5.80309904303, 95.8581225286, 52.6418124918
4given(-0.264708655941, -0.473110354611, 0.840295138525), (-0.61484299365, 0.754094181011, 0.23088971247), (-0.742897988037, -0.455531073062, -0.490503843865)32.6795368088, 18.6717441804, 58.9286040231
5given(-0.997965627298, -0.00174258728427, -0.0637304489334), (-0.00712443167537, -0.990317081147, 0.138640979735), (-0.0633549461763, 0.138812975539, 0.988289992167)30.9926959637, 107.671478275, -6.73788040851
6given(-0.259679754212, -0.494293328862, 0.829602633973), (-0.617592094866, 0.745430581297, 0.250825143925), (-0.742392369042, -0.447221816897, -0.498844882584)33.4399713689, 18.52637232, 59.698583476
7given(-0.262262431744, -0.600122701799, -0.755692503391), (-0.487883457164, 0.758105359218, -0.432719304574), (0.832579214923, 0.255203854027, -0.491612493503)63.8896057244, 27.6011481879, -3.51719518762
8given(-0.997094342645, -0.00194371235277, -0.0761517816489), (-0.00806343742546, -0.991365093811, 0.130882511247), (-0.0757486161121, 0.131116256642, 0.988468853531)31.4997573263, 107.747502421, -6.31553693328
9given(0.296119546705, 0.510621020962, -0.807204674795), (0.510799794421, -0.798764593135, -0.317897302242), (-0.807091558671, -0.318184376902, -0.497354921778)-5.28763941826, 96.4068041566, 52.5687514727
10given(0.168127048406, 0.566182676873, 0.80695134426), (0.598334568756, -0.709174491051, 0.372917263042), (0.783408603109, 0.42012940584, -0.45799808179)-33.7182816613, 78.7812047954, -12.257861583
11given(0.359651129657, 0.474640526023, -0.803347643298), (0.524014615532, -0.815109215772, -0.246993216651), (-0.772049057797, -0.332134517055, -0.541873523006)-3.52213797283, 98.9104767687, 52.487046771
12given(-0.993964522421, -0.00336027702879, -0.109650520779), (-0.0117526444181, -0.990516456043, 0.136890560879), (-0.109070635453, 0.137353044549, 0.984498724039)29.6434415412, 107.608542679, -6.00569020228
13given(-0.223107972388, -0.627123184881, -0.746283688446), (-0.452268739193, 0.744787941913, -0.490656610196), (0.863525228471, 0.228051381414, -0.449796339725)64.5159651821, 26.6438332739, -0.476070901639
14given(0.169495466074, 0.606399440772, 0.776885451796), (0.563323891613, -0.706433768662, 0.428506153552), (0.808664009412, 0.365008285831, -0.461336613717)-32.8155660641, 81.0176723607, -7.67236481184
15given(-0.335286205015, -0.448112895716, 0.828720696869), (-0.610264981608, 0.773449966672, 0.171323674015), (-0.717746343042, -0.448296756343, -0.532794712157)31.1616174886, 15.4212891613, 57.0914501454

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Components

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Protein , 3 types, 18 molecules ADGJMPBEHKNQCFILOR

#1: Protein
Interleukin-6 receptor subunit beta / IL-6 receptor subunit beta / IL-6R subunit beta / IL-6R-beta / IL-6RB / CDw130 / Interleukin-6 ...IL-6 receptor subunit beta / IL-6R subunit beta / IL-6R-beta / IL-6RB / CDw130 / Interleukin-6 signal transducer / Membrane glycoprotein 130 / gp130 / Oncostatin-M receptor subunit alpha


Mass: 34563.961 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: IL6ST / Cell line (production host): Sf21 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P40189
#2: Protein
Interleukin-11 / IL-11 / Adipogenesis inhibitory factor / AGIF


Mass: 19226.416 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: IL11 / Production host: Escherichia coli BL21(DE3) (bacteria) / Strain (production host): BL21(DE3) / References: UniProt: P20809
#3: Protein
Interleukin-11 receptor subunit alpha / IL-11 receptor subunit alpha / IL-11R subunit alpha / IL-11R-alpha / IL-11RA


Mass: 38073.508 Da / Num. of mol.: 6 / Mutation: C226S
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: IL11RA / Cell line (production host): Sf21 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q14626

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Sugars , 3 types, 30 molecules

#4: Polysaccharide
2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}LINUCSPDB-CARE
#5: Polysaccharide
beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 586.542 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1WURCSPDB2Glycan 1.1.0
[][D-1-deoxy-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}LINUCSPDB-CARE
#6: Sugar
ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-acetyl-beta-D-glucosamine / 2-acetamido-2-deoxy-beta-D-glucose / 2-acetamido-2-deoxy-D-glucose / 2-acetamido-2-deoxy-glucose / N-ACETYL-D-GLUCOSAMINE


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 18
Source method: isolated from a genetically manipulated source
Formula: C8H15NO6
IdentifierTypeProgram
DGlcpNAcbCONDENSED IUPAC CARBOHYDRATE SYMBOLGMML 1.0
N-acetyl-b-D-glucopyranosamineCOMMON NAMEGMML 1.0
b-D-GlcpNAcIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
GlcNAcSNFG CARBOHYDRATE SYMBOLGMML 1.0

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Details

Has ligand of interestN

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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: 3.54 Å3/Da / Density % sol: 65.28 %
Crystal growTemperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.25
Details: 180 mM magnesium chloride, 15.3% PEG 3350, 100 mM potassium sodium tartrate, 90 mM sodium HEPES pH 7.25 and 1.8% tert-butanol

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 0.9537 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: May 8, 2018
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9537 Å / Relative weight: 1
ReflectionResolution: 3.779→49.275 Å / Num. obs: 48027 / % possible obs: 92.8 % / Redundancy: 20.9 % / Biso Wilson estimate: 126.31 Å2 / CC1/2: 0.998 / Rpim(I) all: 0.064 / Rrim(I) all: 0.294 / Rsym value: 0.286 / Net I/σ(I): 10.6
Reflection shellResolution: 3.779→4.197 Å / Mean I/σ(I) obs: 1.5 / Num. unique obs: 2262 / CC1/2: 0.548 / Rpim(I) all: 0.558 / Rrim(I) all: 2.584 / Rsym value: 2.522

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Processing

Software
NameVersionClassification
PHENIX1.19.2_4158refinement
XDSdata reduction
XDSdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 8DPS

8dps


Resolution: 3.78→40.86 Å / SU ML: 0.6282 / Cross valid method: FREE R-VALUE / σ(F): 1.35 / Phase error: 38.2385
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.2951 2054 4.54 %
Rwork0.2756 43181 -
obs0.2765 45235 58.04 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 175.3 Å2
Refinement stepCycle: LAST / Resolution: 3.78→40.86 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms34914 0 654 0 35568
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.005636546
X-RAY DIFFRACTIONf_angle_d1.203549956
X-RAY DIFFRACTIONf_chiral_restr0.05885682
X-RAY DIFFRACTIONf_plane_restr0.00726360
X-RAY DIFFRACTIONf_dihedral_angle_d9.68325160
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDRefine-IDTypeRms dev position (Å)
ens_1d_2GX-RAY DIFFRACTIONNCS constraints5.31069407811E-12
ens_1d_3GX-RAY DIFFRACTIONNCS constraints1.48377315684E-12
ens_1d_4GX-RAY DIFFRACTIONNCS constraints1.63812474458E-12
ens_1d_5GX-RAY DIFFRACTIONNCS constraints6.08173820582E-12
ens_1d_6GX-RAY DIFFRACTIONNCS constraints2.26776251009E-12
ens_2d_2NX-RAY DIFFRACTIONNCS constraints7.89311033029E-12
ens_2d_3NX-RAY DIFFRACTIONNCS constraints2.29790034744E-12
ens_2d_4NX-RAY DIFFRACTIONNCS constraints1.47088919813E-12
ens_2d_5NX-RAY DIFFRACTIONNCS constraints4.29345428365E-12
ens_2d_6NX-RAY DIFFRACTIONNCS constraints5.82794000469E-12
ens_3d_2RX-RAY DIFFRACTIONNCS constraints6.09787184976E-12
ens_3d_3RX-RAY DIFFRACTIONNCS constraints1.18757147017E-12
ens_3d_4RX-RAY DIFFRACTIONNCS constraints1.43696834152E-12
ens_3d_5RX-RAY DIFFRACTIONNCS constraints1.5985643932E-12
ens_3d_6RX-RAY DIFFRACTIONNCS constraints5.58443611491E-12
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.78-3.870.732710.4297137X-RAY DIFFRACTION2.69
3.87-3.960.4274200.3648403X-RAY DIFFRACTION8.27
3.96-4.070.4193530.3934632X-RAY DIFFRACTION13.31
4.07-4.190.368550.3883923X-RAY DIFFRACTION18.98
4.19-4.330.3815910.36881150X-RAY DIFFRACTION24.08
4.33-4.480.4545100.35271647X-RAY DIFFRACTION32.45
4.48-4.660.33691760.32962199X-RAY DIFFRACTION45.66
4.66-4.870.32221330.28962881X-RAY DIFFRACTION58.58
4.87-5.130.33921190.28273580X-RAY DIFFRACTION71.19
5.13-5.450.3021650.28844590X-RAY DIFFRACTION91.67
5.45-5.870.3232970.29174889X-RAY DIFFRACTION99.96
5.87-6.460.34742570.30634945X-RAY DIFFRACTION100
6.46-7.390.32131980.27955029X-RAY DIFFRACTION100
7.39-9.290.23212150.23975032X-RAY DIFFRACTION99.98
9.29-40.860.25242640.2455144X-RAY DIFFRACTION99.8

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