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- PDB-5vi4: IL-33/ST2/IL-1RAcP ternary complex structure -

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Basic information

Entry
Database: PDB / ID: 5vi4
TitleIL-33/ST2/IL-1RAcP ternary complex structure
Components
  • Interleukin-1 receptor accessory protein
  • Interleukin-1 receptor-like 1
  • Interleukin-33Interleukin 33
KeywordsSIGNALING PROTEIN / cytokine / cytokine receptor / signaling
Function / homology
Function and homology information


interleukin-33 binding / Interleukin-33 signaling / interleukin-33 receptor binding / negative regulation of macrophage proliferation / positive regulation of CD86 production / positive regulation of CD80 production / Interleukin-36 pathway / positive regulation of cellular defense response / interleukin-33 receptor activity / positive regulation of MHC class I biosynthetic process ...interleukin-33 binding / Interleukin-33 signaling / interleukin-33 receptor binding / negative regulation of macrophage proliferation / positive regulation of CD86 production / positive regulation of CD80 production / Interleukin-36 pathway / positive regulation of cellular defense response / interleukin-33 receptor activity / positive regulation of MHC class I biosynthetic process / interleukin-1 receptor activity / negative regulation of immunoglobulin production / negative regulation of T-helper 1 type immune response / Receptor-type tyrosine-protein phosphatases / trans-synaptic signaling by trans-synaptic complex / microglial cell activation involved in immune response / regulation of postsynaptic density assembly / synaptic membrane adhesion / negative regulation of leukocyte migration / Interleukin-1 signaling / PIP3 activates AKT signaling / microglial cell proliferation / regulation of sensory perception of pain / interleukin-33-mediated signaling pathway / positive regulation of type 2 immune response / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / positive regulation of interleukin-5 production / ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase / Ub-specific processing proteases / macrophage activation involved in immune response / positive regulation of macrophage activation / NAD+ nucleotidase, cyclic ADP-ribose generating / NADP+ nucleosidase activity / positive regulation of MHC class II biosynthetic process / interleukin-1 receptor binding / positive regulation of synapse assembly / interleukin-1-mediated signaling pathway / positive regulation of interleukin-13 production / positive regulation of oligodendrocyte differentiation / positive regulation of nitric-oxide synthase biosynthetic process / regulation of presynapse assembly / negative regulation of type II interferon production / positive regulation of immunoglobulin production / positive regulation of interleukin-4 production / coreceptor activity / extrinsic apoptotic signaling pathway / positive regulation of chemokine production / transport vesicle / cytokine activity / positive regulation of cytokine production / positive regulation of inflammatory response / positive regulation of interleukin-6 production / cytokine-mediated signaling pathway / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / positive regulation of tumor necrosis factor production / chromosome / positive regulation of NF-kappaB transcription factor activity / defense response to virus / membrane => GO:0016020 / inflammatory response / negative regulation of cell population proliferation / external side of plasma membrane / focal adhesion / innate immune response / intracellular membrane-bounded organelle / glutamatergic synapse / synapse / positive regulation of gene expression / negative regulation of transcription by RNA polymerase II / cell surface / positive regulation of transcription by RNA polymerase II / protein-containing complex / extracellular space / extracellular region / nucleoplasm / nucleus / plasma membrane / cytosol / cytoplasm
Similarity search - Function
Interleukin-33 / Interleukin 33 / Interleukin-1 receptor type I/II / IL-1Ra-like, immunoglobulin domain / Immunoglobulin domain / Interleukin-1 receptor family / TIR domain / Toll - interleukin 1 - resistance / Immunoglobulin domain / TIR domain profile. ...Interleukin-33 / Interleukin 33 / Interleukin-1 receptor type I/II / IL-1Ra-like, immunoglobulin domain / Immunoglobulin domain / Interleukin-1 receptor family / TIR domain / Toll - interleukin 1 - resistance / Immunoglobulin domain / TIR domain profile. / Toll/interleukin-1 receptor homology (TIR) domain / Toll/interleukin-1 receptor homology (TIR) domain superfamily / Immunoglobulin domain / Trefoil (Acidic Fibroblast Growth Factor, subunit A) - #50 / Trefoil (Acidic Fibroblast Growth Factor, subunit A) / Trefoil / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / 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
Interleukin-1 receptor-like 1 / Interleukin-1 receptor accessory protein / Interleukin-33
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.792 Å
AuthorsGuenther, S. / Sundberg, E.J.
Funding support United States, 2items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of Arthritis and Musculoskeletal and Skin Diseases (NIH/NIAMS)R01AR068436 United States
American Asthma Foundation13-0066 United States
CitationJournal: Immunity / Year: 2017
Title: IL-1 Family Cytokines Use Distinct Molecular Mechanisms to Signal through Their Shared Co-receptor.
Authors: Gunther, S. / Deredge, D. / Bowers, A.L. / Luchini, A. / Bonsor, D.A. / Beadenkopf, R. / Liotta, L. / Wintrode, P.L. / Sundberg, E.J.
History
DepositionApr 13, 2017Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 27, 2017Provider: repository / Type: Initial release
Revision 1.1Dec 11, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.2Jul 29, 2020Group: Data collection / Derived calculations / Structure summary
Category: chem_comp / entity ...chem_comp / entity / pdbx_chem_comp_identifier / pdbx_entity_nonpoly / struct_conn / struct_site / struct_site_gen
Item: _chem_comp.name / _chem_comp.type ..._chem_comp.name / _chem_comp.type / _entity.pdbx_description / _pdbx_entity_nonpoly.name / _struct_conn.pdbx_role
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 1.3Oct 4, 2023Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Interleukin-33
B: Interleukin-1 receptor-like 1
C: Interleukin-1 receptor accessory protein
D: Interleukin-33
E: Interleukin-1 receptor-like 1
F: Interleukin-1 receptor accessory protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)185,6619
Polymers184,9986
Non-polymers6643
Water0
1
A: Interleukin-33
B: Interleukin-1 receptor-like 1
C: Interleukin-1 receptor accessory protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)92,7204
Polymers92,4993
Non-polymers2211
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7150 Å2
ΔGint-11 kcal/mol
Surface area34360 Å2
MethodPISA
2
D: Interleukin-33
E: Interleukin-1 receptor-like 1
F: Interleukin-1 receptor accessory protein
hetero molecules


Theoretical massNumber of molelcules
Total (without water)92,9415
Polymers92,4993
Non-polymers4422
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area7180 Å2
ΔGint-9 kcal/mol
Surface area35640 Å2
MethodPISA
Unit cell
Length a, b, c (Å)106.314, 107.332, 176.036
Angle α, β, γ (deg.)90.000, 107.270, 90.000
Int Tables number5
Space group name H-MI121
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain B and (resid 29 through 112 or (resid 113...
21(chain E and (resid 29 through 43 or resid 51...
12(chain A and (resid 114 through 135 or (resid 136...
22(chain D and (resid 114 through 197 or (resid 198...
13(chain C and (resid 23 through 255 or resid 263...
23(chain F and (resid 23 through 254 or resid 261 or resid 263 through 348))

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
111SERSERLYSLYS(chain B and (resid 29 through 112 or (resid 113...BB29 - 1126 - 89
121LYSLYSLYSLYS(chain B and (resid 29 through 112 or (resid 113...BB11390
131SERSERNAGNAG(chain B and (resid 29 through 112 or (resid 113...BB - G29 - 4016
141SERSERNAGNAG(chain B and (resid 29 through 112 or (resid 113...BB - G29 - 4016
151SERSERNAGNAG(chain B and (resid 29 through 112 or (resid 113...BB - G29 - 4016
161SERSERNAGNAG(chain B and (resid 29 through 112 or (resid 113...BB - G29 - 4016
211SERSERPROPRO(chain E and (resid 29 through 43 or resid 51...EE29 - 436 - 20
221PROPROTRPTRP(chain E and (resid 29 through 43 or resid 51...EE51 - 5428 - 31
231ARGARGARGARG(chain E and (resid 29 through 43 or resid 51...EE7047
241SERSERNAGNAG(chain E and (resid 29 through 43 or resid 51...EE - I27 - 4024
251SERSERNAGNAG(chain E and (resid 29 through 43 or resid 51...EE - I27 - 4024
261SERSERNAGNAG(chain E and (resid 29 through 43 or resid 51...EE - I27 - 4024
271SERSERNAGNAG(chain E and (resid 29 through 43 or resid 51...EE - I27 - 4024
112SERSERLEULEU(chain A and (resid 114 through 135 or (resid 136...AA114 - 1356 - 27
122GLUGLUGLUGLU(chain A and (resid 114 through 135 or (resid 136...AA13628
132SERSERLYSLYS(chain A and (resid 114 through 135 or (resid 136...AA114 - 2656 - 157
142SERSERLYSLYS(chain A and (resid 114 through 135 or (resid 136...AA114 - 2656 - 157
152SERSERLYSLYS(chain A and (resid 114 through 135 or (resid 136...AA114 - 2656 - 157
162SERSERLYSLYS(chain A and (resid 114 through 135 or (resid 136...AA114 - 2656 - 157
212SERSERASPASP(chain D and (resid 114 through 197 or (resid 198...DD114 - 1976 - 89
222LYSLYSLYSLYS(chain D and (resid 114 through 197 or (resid 198...DD19890
232SERSERLYSLYS(chain D and (resid 114 through 197 or (resid 198...DD114 - 2656 - 157
242SERSERLYSLYS(chain D and (resid 114 through 197 or (resid 198...DD114 - 2656 - 157
252SERSERLYSLYS(chain D and (resid 114 through 197 or (resid 198...DD114 - 2656 - 157
262SERSERLYSLYS(chain D and (resid 114 through 197 or (resid 198...DD114 - 2656 - 157
113ARGARGGLUGLU(chain C and (resid 23 through 255 or resid 263...CC23 - 2556 - 238
123VALVALLEULEU(chain C and (resid 23 through 255 or resid 263...CC263 - 316246 - 299
133PROPROVALVAL(chain C and (resid 23 through 255 or resid 263...CC323 - 347306 - 330
143LYSLYSLYSLYS(chain C and (resid 23 through 255 or resid 263...CC348331
153ARGARGLYSLYS(chain C and (resid 23 through 255 or resid 263...CC23 - 3486 - 331
163ARGARGLYSLYS(chain C and (resid 23 through 255 or resid 263...CC23 - 3486 - 331
173ARGARGLYSLYS(chain C and (resid 23 through 255 or resid 263...CC23 - 3486 - 331
183ARGARGLYSLYS(chain C and (resid 23 through 255 or resid 263...CC23 - 3486 - 331
213ARGARGTYRTYR(chain F and (resid 23 through 254 or resid 261 or resid 263 through 348))FF23 - 2546 - 237
223GLUGLUGLUGLU(chain F and (resid 23 through 254 or resid 261 or resid 263 through 348))FF261244
233VALVALLYSLYS(chain F and (resid 23 through 254 or resid 261 or resid 263 through 348))FF263 - 348246 - 331

NCS ensembles :
ID
1
2
3

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Components

#1: Protein Interleukin-33 / Interleukin 33 / IL-33


Mass: 17519.279 Da / Num. of mol.: 2 / Mutation: C139S, C165S, C231S, C256S
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Il33 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(D3)pLysS / References: UniProt: Q8BVZ5
#2: Protein Interleukin-1 receptor-like 1 / Interleukin-33 receptor alpha chain / Lymphocyte antigen 84 / Protein ST2 / Protein T1


Mass: 35509.023 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Il1rl1, Ly84, St2, Ste2 / Cell line (production host): HEK293T / Production host: Homo sapiens (human) / References: UniProt: P14719
#3: Protein Interleukin-1 receptor accessory protein / IL-1RAcP / Interleukin-33 receptot beta chain


Mass: 39470.613 Da / Num. of mol.: 2 / Mutation: N107Q, N111Q, N196Q,N209Q
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Il1rap / Cell line (production host): HEK293T / Production host: Homo sapiens (human) / References: UniProt: Q61730
#4: 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 / N-Acetylglucosamine


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 3
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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Experimental details

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Experiment

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

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Sample preparation

CrystalDensity Matthews: 2.59 Å3/Da / Density % sol: 52.55 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6
Details: 16% PEG 3350, 0.2 M NaMalonate, pH 6, 0.2 M NaThiocyanate

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 23-ID-D / Wavelength: 1.03322 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Jul 18, 2016
RadiationMonochromator: double crystal monochromator / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1.03322 Å / Relative weight: 1
ReflectionResolution: 2.79→29.681 Å / Num. obs: 46553 / % possible obs: 99 % / Redundancy: 6.9 % / Biso Wilson estimate: 65.02 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.108 / Rpim(I) all: 0.044 / Rrim(I) all: 0.117 / Net I/σ(I): 15
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsCC1/2Rpim(I) allRrim(I) all% possible all
2.79-2.896.81.130.6650.461.22293.9
10.81-29.686.50.0250.9990.0110.02795

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassification
Aimless0.3.11data scaling
PHASERphasing
PHENIXrefinement
PDB_EXTRACT3.22data extraction
XDSdata reduction
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4KC3, 4YFD

4kc3

4yfd


Resolution: 2.792→29.681 Å / SU ML: 0.39 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 28.56
RfactorNum. reflection% reflection
Rfree0.2672 2337 5.02 %
Rwork0.2121 --
obs0.2149 46538 99.02 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso max: 179.57 Å2 / Biso mean: 75.843 Å2 / Biso min: 25.69 Å2
Refinement stepCycle: final / Resolution: 2.792→29.681 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11262 0 42 0 11304
Biso mean--82.46 --
Num. residues----1405
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0111598
X-RAY DIFFRACTIONf_angle_d1.18515736
X-RAY DIFFRACTIONf_chiral_restr0.0661730
X-RAY DIFFRACTIONf_plane_restr0.0092004
X-RAY DIFFRACTIONf_dihedral_angle_d6.4376914
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11B2065X-RAY DIFFRACTION11.707TORSIONAL
12E2065X-RAY DIFFRACTION11.707TORSIONAL
21A1312X-RAY DIFFRACTION11.707TORSIONAL
22D1312X-RAY DIFFRACTION11.707TORSIONAL
31C2862X-RAY DIFFRACTION11.707TORSIONAL
32F2862X-RAY DIFFRACTION11.707TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 17

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.7919-2.84890.35951340.29792348248291
2.8489-2.91080.33351350.28092573270899
2.9108-2.97840.34531380.27122608274699
2.9784-3.05280.31781360.25826062742100
3.0528-3.13530.29981380.25562601273999
3.1353-3.22740.27631370.25362592272999
3.2274-3.33150.30381370.23862606274399
3.3315-3.45040.26471360.22262608274499
3.4504-3.58830.25761360.21032579271599
3.5883-3.75130.29411390.214626312770100
3.7513-3.94870.28241370.201826102747100
3.9487-4.19540.22391370.191526112748100
4.1954-4.51830.23931380.1726092747100
4.5183-4.97110.21441370.166526282765100
4.9711-5.6860.25651410.188326492790100
5.686-7.14730.29241370.2226482785100
7.1473-29.68230.26051440.231726942838100
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)
12.3768-2.21612.78287.5652-3.41083.4691-0.35740.09710.1548-0.4660.4881-0.74660.06390.9312-0.07580.42130.14370.12520.7496-0.16050.479535.638144.0741-27.0184
23.34154.62981.09946.45391.05964.56930.08771.34530.28841.03420.3110.572-0.68271.10470.00380.8384-0.01890.03430.7975-0.02060.735342.056755.7697-28.2922
35.5268-5.38915.91585.2328-5.76846.3413-0.33680.42620.46570.68590.6411-0.5853-0.63941.0068-0.54830.71870.041-0.02670.77930.0470.640337.092548.4181-38.4764
45.24011.074-4.68112.5244-1.48724.2383-0.05641.1977-0.47470.2068-0.04180.45360.3031-0.07810.22750.5260.06760.10780.6663-0.00880.585632.144934.561-14.7221
50.515-0.76981.14057.35012.02425.08920.10570.10210.17520.4451-0.0892-1.2882-0.57610.8346-0.020.3767-0.0002-0.09470.79060.07210.654438.910544.229-16.319
68.6862.7024-0.94466.6692-0.83063.1554-0.09250.0834-0.52960.2080.4143-1.1413-0.45981.10090.00750.37040.0123-0.0320.70810.02440.523134.786644.4555-17.3403
72.19710.4988-0.56569.5083-6.51774.51810.3357-0.34870.6910.6628-0.16420.6849-0.88070.687-0.31160.50980.0403-0.03180.6109-0.12980.565630.704952.6947-16.3441
85.8066-4.7658-6.95664.23996.4129.7483-0.50790.1173-0.05290.149-0.00751.18310.0058-0.26690.4280.36080.01660.02740.5415-0.02410.576824.444247.5699-23.3406
92.58750.91910.55883.97390.9620.9507-0.16940.61650.0848-0.67330.3389-0.1655-0.9370.6086-0.23530.7463-0.26540.14881.22130.22530.586834.086467.4802-42.2665
103.49171.8837-0.11348.9401-1.05825.8833-0.08410.49440.037-0.5935-0.2020.0171-0.1040.35220.29640.3634-0.0242-0.03440.61810.08230.261319.085952.8059-40.9535
116.0823-4.49471.07938.1138-0.17971.9223-0.0977-0.0617-0.31810.4050.4515-0.1220.70.9719-0.30880.5820.2591-0.07590.6576-0.14410.507832.896919.7957-18.6885
126.50043.4372-1.17595.4874-1.05683.8157-0.1990.40910.0117-0.43130.18970.717-0.019-0.38440.03420.47220.0473-0.03710.38340.03390.493-23.108942.973-9.7921
133.9069-3.6066-0.37235.49870.98871.0017-0.00590.194-0.1081-0.0605-0.01410.4043-0.088-0.12390.04610.2921-0.0367-0.05070.27560.020.32560.544849.1121-21.8382
144.1103-1.44451.97083.2898-2.13874.04450.0138-0.2493-0.3040.43870.237-0.09960.7221-0.0938-0.20320.84620.124-0.13650.4531-0.01560.499914.77211.7296-18.8613
154.44150.31952.39593.7018-0.17221.31350.3334-0.24670.5570.8889-0.3385-0.5186-0.94090.80890.35970.4584-0.1152-0.05830.5303-0.07050.482211.029731.9011-59.3671
162.6801-4.1015-2.17768.10131.66763.1502-0.15180.1449-0.10150.27090.0272-1.78270.95861.1841-0.00120.70170.1798-0.04460.7053-0.00980.78999.043816.392-54.4168
175.90423.5457-5.86617.001-2.87885.8850.7214-0.37090.3444-1.3569-0.2397-1.03920.46420.3097-0.52140.7260.2026-0.09470.67740.11960.61098.929520.0178-44.1907
182.6996-0.81841.41544.583-2.01188.06280.345-0.2508-0.08080.33920.0453-0.2493-0.71870.9425-0.23080.4628-0.2008-0.07880.66460.04550.464812.678731.9608-62.7052
193.97314.03013.78654.12524.1556.1689-1.0830.15560.9391-0.17450.25471.0109-0.3346-1.64670.4660.865-0.1389-0.28750.60570.15950.7142-3.23437.6913-73.1409
208.0357-2.03661.52716.44072.47047.6302-0.01970.9581-0.2576-0.5661-0.492-0.88410.17291.090.55060.3144-0.11110.11780.69560.07690.657311.565325.1984-67.3097
215.77534.2071-3.56393.7093-2.0872.61-0.44262.47861.6499-1.04321.3826-0.7256-0.13361.5214-1.11310.9660.10570.13871.60990.17251.127317.881219.9819-67.7333
226.2578-6.1372-0.67916.01020.50027.25231.18880.73871.4017-1.2626-0.5778-1.15420.01530.1018-0.76170.4712-0.04430.02940.4563-0.05420.60076.9827.3592-69.2765
235.4248-2.9349-4.44243.14822.27873.6090.0007-0.3292-0.2678-0.07160.6881-0.17410.02620.1843-0.63690.5298-0.040.01390.3949-0.02820.4157-0.791527.4525-61.9096
248.9322-0.73831.46139.3014-5.85964.2984-0.15710.325-1.2118-0.82040.561-0.56051.7541-0.2603-0.39030.6136-0.07590.00290.4384-0.19920.53783.199516.9995-67.2992
258.35244.43855.09776.53184.69454.18110.0750.7249-0.78050.00720.36270.3228-0.1677-0.4129-0.32670.3455-0.1696-0.08090.53190.0240.5645-2.918121.9698-60.2924
262.33252.0570.88163.89471.09064.68520.5557-0.0351-0.6278-0.14780.0286-0.37921.24091.1023-0.39530.66710.2234-0.2160.64410.07170.74149.22760.0043-44.139
277.9498-6.25498.064.7708-6.27848.4979-0.7457-0.65030.43331.00370.0992-0.2002-1.0862-0.42140.37890.5153-0.023-0.03450.5680.03440.4217-1.810119.7316-37.7128
284.6628-4.20490.4577.7541-0.16675.4897-0.0273-0.1671-0.26490.5179-0.04420.34150.2073-0.29650.14280.3342-0.06760.00170.36980.05520.3844-9.958715.0218-42.8192
295.29664.6314-1.25127.214-0.93173.786-0.05590.0528-0.0572-0.1255-0.0611-0.074-0.96530.80060.07570.6336-0.1842-0.10620.5686-0.0110.32937.430150.2917-65.9803
306.3715-1.86210.41178.7081-2.3854.80630.1509-0.24280.26780.6680.05940.9149-0.2317-0.5734-0.13770.5573-0.0646-0.070.4432-0.02480.6397-52.729127.1917-74.4861
310.861.5701-0.20883.98350.37510.9076-0.05470.10460.3301-0.30370.15140.3378-0.32140.0429-0.07680.50830.0478-0.06250.32980.05280.5536-20.476138.6159-64.3257
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 114 through 134 )A114 - 134
2X-RAY DIFFRACTION2chain 'A' and (resid 135 through 145 )A135 - 145
3X-RAY DIFFRACTION3chain 'A' and (resid 146 through 155 )A146 - 155
4X-RAY DIFFRACTION4chain 'A' and (resid 156 through 172 )A156 - 172
5X-RAY DIFFRACTION5chain 'A' and (resid 173 through 201 )A173 - 201
6X-RAY DIFFRACTION6chain 'A' and (resid 202 through 231 )A202 - 231
7X-RAY DIFFRACTION7chain 'A' and (resid 232 through 250 )A232 - 250
8X-RAY DIFFRACTION8chain 'A' and (resid 251 through 265 )A251 - 265
9X-RAY DIFFRACTION9chain 'B' and (resid 29 through 120 )B29 - 120
10X-RAY DIFFRACTION10chain 'B' and (resid 121 through 209 )B121 - 209
11X-RAY DIFFRACTION11chain 'B' and (resid 210 through 322 )B210 - 322
12X-RAY DIFFRACTION12chain 'C' and (resid 23 through 144 )C23 - 144
13X-RAY DIFFRACTION13chain 'C' and (resid 145 through 234 )C145 - 234
14X-RAY DIFFRACTION14chain 'C' and (resid 235 through 348 )C235 - 348
15X-RAY DIFFRACTION15chain 'D' and (resid 114 through 125 )D114 - 125
16X-RAY DIFFRACTION16chain 'D' and (resid 126 through 145 )D126 - 145
17X-RAY DIFFRACTION17chain 'D' and (resid 146 through 154 )D146 - 154
18X-RAY DIFFRACTION18chain 'D' and (resid 155 through 162 )D155 - 162
19X-RAY DIFFRACTION19chain 'D' and (resid 163 through 172 )D163 - 172
20X-RAY DIFFRACTION20chain 'D' and (resid 173 through 201 )D173 - 201
21X-RAY DIFFRACTION21chain 'D' and (resid 202 through 212 )D202 - 212
22X-RAY DIFFRACTION22chain 'D' and (resid 213 through 221 )D213 - 221
23X-RAY DIFFRACTION23chain 'D' and (resid 222 through 231 )D222 - 231
24X-RAY DIFFRACTION24chain 'D' and (resid 232 through 250 )D232 - 250
25X-RAY DIFFRACTION25chain 'D' and (resid 251 through 265 )D251 - 265
26X-RAY DIFFRACTION26chain 'E' and (resid 27 through 111 )E27 - 111
27X-RAY DIFFRACTION27chain 'E' and (resid 112 through 135 )E112 - 135
28X-RAY DIFFRACTION28chain 'E' and (resid 136 through 209 )E136 - 209
29X-RAY DIFFRACTION29chain 'E' and (resid 210 through 322 )E210 - 322
30X-RAY DIFFRACTION30chain 'F' and (resid 23 through 132 )F23 - 132
31X-RAY DIFFRACTION31chain 'F' and (resid 133 through 348 )F133 - 348

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