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- PDB-9b9f: Zebrafish Betaglycan Orphan Domain (zfBGo) in complex with TGF-B3... -

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Basic information

Entry
Database: PDB / ID: 9b9f
TitleZebrafish Betaglycan Orphan Domain (zfBGo) in complex with TGF-B3 and extracellular domains of TGFBRI and TGFBRII
Components
  • Transforming growth factor beta receptor type-1
  • Transforming growth factor beta receptor type-2
  • Transforming growth factor beta receptor type-3
  • Transforming growth factor beta-3
  • Transforming growth factor beta-3 triple mutant
KeywordsMEMBRANE PROTEIN / Complex / Betaglycan / TGFBR3 / TGFb / TGFBR1 / TGFBR2
Function / homology
Function and homology information


FGFR1b ligand binding and activation / FGFR1c ligand binding and activation / TGF-beta receptor signaling activates SMADs / TGFBR3 PTM regulation / TGFBR3 regulates TGF-beta signaling / TGFBR3 regulates FGF2 signaling / uterine wall breakdown / positive regulation of tolerance induction to self antigen / positive regulation of B cell tolerance induction / inferior endocardial cushion morphogenesis ...FGFR1b ligand binding and activation / FGFR1c ligand binding and activation / TGF-beta receptor signaling activates SMADs / TGFBR3 PTM regulation / TGFBR3 regulates TGF-beta signaling / TGFBR3 regulates FGF2 signaling / uterine wall breakdown / positive regulation of tolerance induction to self antigen / positive regulation of B cell tolerance induction / inferior endocardial cushion morphogenesis / transforming growth factor beta receptor activity, type II / bronchus morphogenesis / mammary gland morphogenesis / lens fiber cell apoptotic process / detection of hypoxia / growth plate cartilage chondrocyte growth / extracellular structure organization / epicardium morphogenesis / tricuspid valve morphogenesis / vascular endothelial cell proliferation / TGFBR2 MSI Frameshift Mutants in Cancer / miRNA transport / parathyroid gland development / regulation of cardiac muscle cell proliferation / transforming growth factor beta ligand-receptor complex / type III transforming growth factor beta receptor binding / myofibroblast differentiation / positive regulation of epithelial to mesenchymal transition involved in endocardial cushion formation / aorta morphogenesis / Langerhans cell differentiation / TGFBR2 Kinase Domain Mutants in Cancer / transforming growth factor beta receptor activity / cardiac left ventricle morphogenesis / regulation of transforming growth factor beta receptor signaling pathway / secondary palate development / negative regulation of macrophage cytokine production / angiogenesis involved in coronary vascular morphogenesis / trophoblast cell migration / SMAD2/3 Phosphorylation Motif Mutants in Cancer / TGFBR1 KD Mutants in Cancer / positive regulation of mesenchymal stem cell proliferation / endocardial cushion fusion / ventricular compact myocardium morphogenesis / positive regulation of extracellular matrix assembly / positive regulation of tight junction disassembly / positive regulation of T cell tolerance induction / positive regulation of NK T cell differentiation / cardiac epithelial to mesenchymal transition / membranous septum morphogenesis / somite development / transforming growth factor beta receptor activity, type I / mesenchymal cell differentiation / TGFBR3 regulates TGF-beta signaling / neuron fate commitment / positive regulation of vasculature development / activin receptor activity, type I / activin receptor complex / regulation of stem cell proliferation / regulation of epithelial to mesenchymal transition / lung lobe morphogenesis / type II transforming growth factor beta receptor binding / pharyngeal system development / receptor protein serine/threonine kinase / activin binding / TGFBR1 LBD Mutants in Cancer / transmembrane receptor protein serine/threonine kinase activity / SMAD protein signal transduction / primordial germ cell migration / coronary artery morphogenesis / filopodium assembly / embryonic cranial skeleton morphogenesis / type I transforming growth factor beta receptor binding / glycosaminoglycan binding / myeloid dendritic cell differentiation / activin receptor signaling pathway / ventricular trabecula myocardium morphogenesis / positive regulation of CD4-positive, alpha-beta T cell proliferation / regulation of stem cell differentiation / mammary gland development / outflow tract septum morphogenesis / cell-cell junction organization / response to cholesterol / transforming growth factor beta binding / I-SMAD binding / sprouting angiogenesis / collagen fibril organization / negative regulation of chondrocyte differentiation / lens development in camera-type eye / atrioventricular valve morphogenesis / aortic valve morphogenesis / kinase activator activity / endothelial cell activation / anterior/posterior pattern specification / positive regulation of filopodium assembly / face morphogenesis / artery morphogenesis / embryonic hemopoiesis / positive regulation of mesenchymal cell proliferation / odontogenesis / Molecules associated with elastic fibres
Similarity search - Function
Transforming growth factor beta-3 / : / TGFBR3-like, N-terminal domain / Transforming growth factor beta receptor 2 ectodomain / Transforming growth factor-beta receptor, type II / Transforming growth factor beta receptor 2 ectodomain / Zona pellucida domain, conserved site / ZP domain signature. / Transforming growth factor-beta / : ...Transforming growth factor beta-3 / : / TGFBR3-like, N-terminal domain / Transforming growth factor beta receptor 2 ectodomain / Transforming growth factor-beta receptor, type II / Transforming growth factor beta receptor 2 ectodomain / Zona pellucida domain, conserved site / ZP domain signature. / Transforming growth factor-beta / : / : / ZP-N domain / Zona pellucida, ZP-C domain / ZP-C domain / Zona pellucida (ZP) domain / ZP domain profile. / Zona pellucida domain / GS domain / Transforming growth factor beta type I GS-motif / GS domain profile. / GS motif / TGF-beta, propeptide / TGF-beta propeptide / Transforming growth factor beta, conserved site / TGF-beta family signature. / Activin types I and II receptor domain / Transforming growth factor-beta-related / Activin types I and II receptor domain / Transforming growth factor-beta (TGF-beta) family / Transforming growth factor-beta, C-terminal / Transforming growth factor beta like domain / TGF-beta family profile. / Ser/Thr protein kinase, TGFB receptor / Cystine-knot cytokine / Snake toxin-like superfamily / Protein tyrosine and serine/threonine kinase / Serine-threonine/tyrosine-protein kinase, catalytic domain / Serine/threonine-protein kinase, active site / Serine/Threonine protein kinases active-site signature. / Protein kinase domain / Serine/Threonine protein kinases, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily
Similarity search - Domain/homology
Transforming growth factor beta receptor III / Transforming growth factor beta-3 proprotein / TGF-beta receptor type-1 / TGF-beta receptor type-2
Similarity search - Component
Biological speciesHomo sapiens (human)
Danio rerio (zebrafish)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3 Å
AuthorsWieteska, L. / Taylor, A.B. / Hinck, A.P.
Funding support United States, European Union, 3items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)GM058670 United States
H2020 Marie Curie Actions of the European Commission893196European Union
National Institutes of Health/Office of the DirectorOD030374 United States
CitationJournal: Nat Commun / Year: 2025
Title: Structures of TGF-β with betaglycan and signaling receptors reveal mechanisms of complex assembly and signaling.
Authors: Łukasz Wieteska / Alexander B Taylor / Emma Punch / Jonathan A Coleman / Isabella O Conway / Yeu-Farn Lin / Chang-Hyeock Byeon / Cynthia S Hinck / Troy Krzysiak / Rieko Ishima / Fernando ...Authors: Łukasz Wieteska / Alexander B Taylor / Emma Punch / Jonathan A Coleman / Isabella O Conway / Yeu-Farn Lin / Chang-Hyeock Byeon / Cynthia S Hinck / Troy Krzysiak / Rieko Ishima / Fernando López-Casillas / Peter Cherepanov / Daniel J Bernard / Caroline S Hill / Andrew P Hinck /
Abstract: Betaglycan (BG) is a transmembrane co-receptor of the transforming growth factor-β (TGF-β) family of signaling ligands. It is essential for embryonic development, tissue homeostasis and fertility ...Betaglycan (BG) is a transmembrane co-receptor of the transforming growth factor-β (TGF-β) family of signaling ligands. It is essential for embryonic development, tissue homeostasis and fertility in adults. It functions by enabling binding of the three TGF-β isoforms to their signaling receptors and is additionally required for inhibin A (InhA) activity. Despite its requirement for the functions of TGF-βs and InhA in vivo, structural information explaining BG ligand selectivity and its mechanism of action is lacking. Here, we determine the structure of TGF-β bound both to BG and the signaling receptors, TGFBR1 and TGFBR2. We identify key regions responsible for ligand engagement, which has revealed binding interfaces that differ from those described for the closely related co-receptor of the TGF-β family, endoglin, thus demonstrating remarkable evolutionary adaptation to enable ligand selectivity. Finally, we provide a structural explanation for the hand-off mechanism underlying TGF-β signal potentiation.
History
DepositionApr 2, 2024Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 12, 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: Transforming growth factor beta-3
B: Transforming growth factor beta-3 triple mutant
C: Transforming growth factor beta receptor type-1
D: Transforming growth factor beta receptor type-2
E: Transforming growth factor beta receptor type-3
F: Transforming growth factor beta-3
G: Transforming growth factor beta-3 triple mutant
H: Transforming growth factor beta receptor type-1
I: Transforming growth factor beta receptor type-2
J: Transforming growth factor beta receptor type-3


Theoretical massNumber of molelcules
Total (without water)170,89910
Polymers170,89910
Non-polymers00
Water00
1
A: Transforming growth factor beta-3
B: Transforming growth factor beta-3 triple mutant
C: Transforming growth factor beta receptor type-1
D: Transforming growth factor beta receptor type-2
E: Transforming growth factor beta receptor type-3


Theoretical massNumber of molelcules
Total (without water)85,4495
Polymers85,4495
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
F: Transforming growth factor beta-3
G: Transforming growth factor beta-3 triple mutant
H: Transforming growth factor beta receptor type-1
I: Transforming growth factor beta receptor type-2
J: Transforming growth factor beta receptor type-3


Theoretical massNumber of molelcules
Total (without water)85,4495
Polymers85,4495
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)195.136, 200.923, 47.436
Angle α, β, γ (deg.)90.000, 90.000, 90.000
Int Tables number18
Space group name H-MP21212
Space group name HallP22ab
Symmetry operation#1: x,y,z
#2: x+1/2,-y+1/2,-z
#3: -x+1/2,y+1/2,-z
#4: -x,-y,z
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails (eV)
d_1ens_1(chain "A" and (resid 301 through 324 or resid 326...
d_2ens_1(chain "B" and (resid 301 through 324 or resid 326...
d_3ens_1(chain "F" and (resid 301 through 324 or resid 326...
d_4ens_1(chain "G" and (resid 301 through 324 or resid 326...
d_1ens_2(chain "C" and (resid 31 through 89 or resid 92 through 107))
d_2ens_2chain "H"
d_1ens_3chain "D"
d_2ens_3chain "I"

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
d_11ens_1ALAALAPHEPHEAA301 - 3241 - 24
d_12ens_1GLNGLNLEULEUAA326 - 38926 - 89
d_13ens_1TYRTYRGLYGLYAA391 - 39391 - 93
d_14ens_1THRTHRSERSERAA395 - 41295 - 112
d_21ens_1ALAALAPHEPHEBB301 - 3241 - 24
d_22ens_1GLNGLNLEULEUBB326 - 38926 - 89
d_23ens_1TYRTYRGLYGLYBB391 - 39391 - 93
d_24ens_1THRTHRSERSERBB395 - 41295 - 112
d_31ens_1ALAALAPHEPHEFF301 - 3241 - 24
d_32ens_1GLNGLNLEULEUFF326 - 38926 - 89
d_33ens_1TYRTYRGLYGLYFF391 - 39391 - 93
d_34ens_1THRTHRSERSERFF395 - 41295 - 112
d_41ens_1ALAALAPHEPHEGG301 - 3241 - 24
d_42ens_1GLNGLNLEULEUGG326 - 38926 - 89
d_43ens_1TYRTYRGLYGLYGG391 - 39391 - 93
d_44ens_1THRTHRSERSERGG395 - 41295 - 112
d_11ens_2ALAALALYSLYSCC31 - 895 - 63
d_12ens_2SERSERILEILECC92 - 10766 - 81
d_21ens_2ALAALAILEILEHH31 - 1075 - 81
d_11ens_3VALVALPHEPHEDD45 - 1495 - 109
d_21ens_3VALVALPHEPHEII45 - 1495 - 109

NCS ensembles :
ID
ens_1
ens_2
ens_3

NCS oper:
IDCodeMatrixVector
1given(-0.852921964177, -0.346336071214, -0.390609074139), (-0.336889307008, -0.206414208009, 0.918639629863), (-0.398785302949, 0.915119937772, 0.0593782927061)238.507682365, 34.0205392465, 59.5016392445
2given(-0.918986062343, 0.162150377349, -0.359404886369), (0.213889791669, -0.560735024602, -0.799892110978), (-0.331233715433, -0.811962737637, 0.480625361846)149.449665352, 34.8997139007, 53.3594041238
3given(0.888452670137, -0.0419196508605, 0.457049883271), (0.318308074576, -0.661139477068, -0.679392788836), (0.330653629324, 0.749091005642, -0.574047770382)-85.9228035203, 20.897355036, -22.20958426
4given(-0.913827737441, 0.111427334984, -0.390516088404), (0.256395674676, -0.587423140258, -0.767590588984), (-0.314928760661, -0.80157220717, 0.508234072451)151.588898309, 30.8365170567, 50.9848093384
5given(-0.889766345197, 0.198726069608, -0.410881735069), (0.223912080387, -0.594399248568, -0.77236837944), (-0.397717526911, -0.779228774212, 0.484379279313)147.195334278, 34.3794171559, 58.301224277

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Components

#1: Protein Transforming growth factor beta-3 / TGF-beta-3


Mass: 12734.504 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TGFB3 / Production host: Escherichia coli (E. coli) / References: UniProt: P10600
#2: Protein Transforming growth factor beta-3 triple mutant / TGF-beta-3


Mass: 12586.247 Da / Num. of mol.: 2 / Mutation: R325E,Y390A,R394E
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TGFB3 / Production host: Escherichia coli (E. coli) / References: UniProt: P10600
#3: Protein Transforming growth factor beta receptor type-1 / TGFR-1 / Activin A receptor type II-like protein kinase of 53kD / Activin receptor-like kinase 5 / ...TGFR-1 / Activin A receptor type II-like protein kinase of 53kD / Activin receptor-like kinase 5 / ALK-5 / ALK5 / Serine/threonine-protein kinase receptor R4 / SKR4 / TGF-beta type I receptor / Transforming growth factor-beta receptor type I / TGF-beta receptor type I / TbetaR-I


Mass: 9474.826 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TGFBR1, ALK5, SKR4 / Production host: Escherichia coli (E. coli)
References: UniProt: P36897, receptor protein serine/threonine kinase
#4: Protein Transforming growth factor beta receptor type-2


Mass: 12926.812 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: TGFBR2 / Production host: Escherichia coli (E. coli) / References: UniProt: P37173
#5: Protein Transforming growth factor beta receptor type-3 / Transforming growth factor beta receptor type 3 precursor


Mass: 37727.000 Da / Num. of mol.: 2 / Mutation: C150G,C277G
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Danio rerio (zebrafish) / Gene: tgfbr3, si:ch73-18k18.1 / Production host: Homo sapiens (human) / References: UniProt: A0A0H3UK16
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: 2.72 Å3/Da / Density % sol: 54.79 %
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop
Details: 0.2 M lithium sulfate, 0.1 M tris pH 8.5, 30 %(w/v) polyethylene glycol 4000

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.97918 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Mar 23, 2022
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97918 Å / Relative weight: 1
ReflectionResolution: 3→139.98 Å / Num. obs: 38615 / % possible obs: 100 % / Redundancy: 13.4 % / Biso Wilson estimate: 105.95 Å2 / CC1/2: 0.99 / Rpim(I) all: 0.045 / Net I/σ(I): 10.5
Reflection shellResolution: 3→3.16 Å / Redundancy: 13.9 % / Mean I/σ(I) obs: 0.6 / Num. unique obs: 5562 / CC1/2: 0.407 / Rpim(I) all: 1.427 / % possible all: 100

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Processing

Software
NameVersionClassification
PHENIX1.21_5207refinement
autoPROCdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 3→63.35 Å / SU ML: 0.4918 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 34.5241
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.2779 2011 5.22 %
Rwork0.2353 36497 -
obs0.2375 38508 99.86 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 156.18 Å2
Refinement stepCycle: LAST / Resolution: 3→63.35 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms11078 0 0 0 11078
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.003911334
X-RAY DIFFRACTIONf_angle_d0.732715402
X-RAY DIFFRACTIONf_chiral_restr0.06271754
X-RAY DIFFRACTIONf_plane_restr0.0041978
X-RAY DIFFRACTIONf_dihedral_angle_d15.31234163
Refine LS restraints NCS
Ens-IDDom-IDAsym-IDAuth asym-IDRefine-IDTypeRms dev position (Å)
ens_1d_2AAX-RAY DIFFRACTIONTorsion NCS0.81756078523
ens_1d_3AAX-RAY DIFFRACTIONTorsion NCS0.491682567932
ens_1d_4AAX-RAY DIFFRACTIONTorsion NCS0.875006761952
ens_2d_2CCX-RAY DIFFRACTIONTorsion NCS0.798432985765
ens_3d_2DDX-RAY DIFFRACTIONTorsion NCS0.509781700708
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3-3.080.42711390.39052535X-RAY DIFFRACTION99.78
3.08-3.160.38691500.36442589X-RAY DIFFRACTION99.89
3.16-3.250.38171290.34622526X-RAY DIFFRACTION99.74
3.25-3.360.39841470.32632579X-RAY DIFFRACTION99.82
3.36-3.480.35571370.31082541X-RAY DIFFRACTION99.81
3.48-3.620.32951460.26032594X-RAY DIFFRACTION99.78
3.62-3.780.30391370.25322576X-RAY DIFFRACTION99.96
3.78-3.980.32561430.2542607X-RAY DIFFRACTION99.93
3.98-4.230.24051430.22542576X-RAY DIFFRACTION99.93
4.23-4.550.21561390.18732591X-RAY DIFFRACTION99.85
4.55-5.010.21871440.18832634X-RAY DIFFRACTION100
5.01-5.740.27261500.2132643X-RAY DIFFRACTION100
5.74-7.230.31741470.26732677X-RAY DIFFRACTION99.89
7.23-63.350.25321600.21082829X-RAY DIFFRACTION99.7
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)
18.44613167159-0.44514466242-8.24238489769.36860470141-0.127256675488.177879681210.210702040801-0.153932255363-2.202301338571.30683650658-0.7040131057150.724471035764-1.00713656538-0.4602119487430.7248434593771.45109493731-0.0443714673615-0.1849650769611.210716133520.02474585740940.990259581336105.14138544215.408327080351.0295687199
29.00487814309-1.65496992173-0.3504852867014.264202158452.55180172343.336429784380.187808161873-3.580143945222.447938340714.27802153414-0.04109681263020.557386607763-2.334447199862.103612481770.1902273220471.39197661163-0.312315027168-0.1684578229911.63133371144-0.1083433591531.01907139066107.95138532321.913919122157.0956857102
35.424257298151.40762613748-2.415428453122.69708903190.1371960681643.370295932570.0689735920742-0.4998682584770.1220854261410.509804116546-0.142470861836-0.2133744912590.02334635849650.201235529241-0.02782114649691.175127271510.0170650833031-0.02332160663971.12862381264-0.03000535871220.756626882065105.44661867527.082398063244.4137401458
42.29440554262-0.8758400714163.330031730183.15577679283-0.6566274348165.639963906891.54541978632-0.6345925698511.098600168611.68200724099-0.356358705404-1.09743184856-1.321658816820.1362744129050.2994183352661.750573442780.05516815838790.2457046726832.263884916260.144195483951.59766060362121.90845756235.514811297455.1682098664
56.023953515661.423093101585.946808448062.433089688061.356160101825.86897528173-0.2914121369460.579297533319-3.81613455366-0.6283172218321.09605063771-3.72624757205-0.1677103148551.86890013717-0.3153409059731.30839951841-0.269472955451-0.01726105842871.322727422020.004378071550681.31438632826109.03392750821.947969330241.2285912365
67.39873179832-2.082743063563.349381101260.480283815331-1.10444421458.39976744571-0.1713454330551.204062153890.2482337538650.1078286276240.0548547268134-0.04778186008410.1878726848931.69208378068-0.09087790693621.19328860752-0.133757210906-0.08676214362280.890213147983-0.06318367956841.0728247770297.582989749322.573184044130.7695464093
79.25782189968-1.15855406036-1.233791870657.897873979163.803804432445.26453457041.530210036221.24022516255-1.71275527776-1.17680769225-1.38304307192-0.0250500340354-0.561858680283-1.07790740013-0.1634185240221.51359994725-0.332857109244-0.4235782767881.028956799980.2345306182832.05336220959123.34692429742.409295541534.6240522366
81.37111988064-0.136226440962.130132443420.217926484988-1.139155408655.519399651770.288131565309-0.8566138461171.284161108160.270003623568-0.4761096090460.588099291213-1.30234085308-0.222588192033-0.1135017211741.61314227513-0.239338047597-0.2717654899890.947187821679-0.03393025155551.88558406057119.53569205743.325568480141.5345548298
91.9676448675-1.88307509232-1.893487184347.514679048091.987617498042.05030732374-1.11059229267-0.9084289974140.04186904712590.05652501760170.494336695642-2.31635713355-0.326743698823.0928782145-0.8381977734191.69596763876-0.332770121352-0.3999392160141.982191715720.1350134534231.29988176943135.20640614633.170525790753.671055683
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592.4168632377-0.734423206299-2.458833215352.55215966095-2.027170576548.14537144022-0.07659197987890.586071240657-1.03169210306-2.27060140427-1.72074464438-0.3135737397730.2087711405610.3412788175111.603742323331.631915027060.00757095902390.1641990558761.3323023707-0.2284118469921.1964555921484.686443850716.4710492220.00678797587058
608.01214485062-2.662843674230.885131528163.36327421844-4.066724226075.948816450840.174692283939-0.156768728334-1.11080212572-1.27854049063-1.738761690641.98396336626-0.6011159192220.6658943864810.5353747863111.40759982440.0505874742271-0.03601386466371.56876955785-0.2670398493951.4897060498480.15806614266.421149315863.5521769433
612.830240190134.543706103053.098721660078.313220976295.414570554843.67281382685-0.743291971176-1.034397156310.128712785674-0.941537629451-1.14584752080.207236369351-0.36981620697-1.782663162981.279200056051.32401383602-0.1741931699970.1291798584181.12229328574-0.09050714500160.97535200257294.242612848113.48237285546.26697879433
623.592511338154.758150891381.612878173486.955952414690.9901276852642.106953557-1.4009047243-0.399681717976-0.712172992283-0.744497285790.809145980515-0.958691837191-1.210866863820.1766035056551.29584781241.06562508074-0.01411427866270.002287092601051.56158230891-0.06577215226551.0470674280887.469695648512.49755715267.53287122657
635.23174163226-4.561744499090.08313388779614.171044391730.6044236706637.704268452510.5680113375461.77933957572-3.06649410796-0.977428308831-0.01084580910540.9480661880920.505186601524-2.30668268616-0.3786380337791.45888369731-0.249043243824-0.06699532654310.923479300546-0.1383299903411.3449488169175.80797577857.774665469817.69512647418
643.286299855481.457342663074.89722569554-1.07994610003-0.2033364590033.573391206010.3180654035650.461023236775-1.087867650470.01382338627680.834425097554-0.256541701797-0.346946640062-0.639165101375-0.3969708164561.173271012270.05999900136960.09261824898911.942902342240.160522011982.445104010213.3494786052829.37559816421.35743806008
652.89066133569-0.4927194303831.974767981543.209152780430.7142564188362.056231643810.6907037199681.59228891327-0.157637737819-0.435386611001-0.2669973872820.364259780832-0.0206763870951-0.137682411703-0.387486916281.49054484280.1469900192760.01140953801242.380041963540.2870721340072.09784841819-0.13321464304926.7426767877-5.1956825277
661.135678179452.18171531174-0.197428429398.39680589789-0.1967442176692.36326770751-0.3504546470090.156401326627-0.360855908083-0.1065558041810.934803563529-0.776756575478-0.0350879637177-0.11450611793-0.4955032412851.222029597810.1706571899580.1047890151651.81690538440.09534628230991.9617374325426.640714031233.717755532911.537941529
Refinement TLS group

Refine-ID: X-RAY DIFFRACTION

IDRefine TLS-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11chain 'A' and (resid 301 through 309 )AA301 - 3091 - 9
22chain 'A' and (resid 310 through 315 )AA310 - 31510 - 15
33chain 'A' and (resid 316 through 368 )AA316 - 36816 - 68
44chain 'A' and (resid 369 through 376 )AA369 - 37669 - 76
55chain 'A' and (resid 377 through 385 )AA377 - 38577 - 85
66chain 'A' and (resid 386 through 412 )AA386 - 41286 - 112
77chain 'B' and (resid 301 through 309 )BB301 - 3091 - 9
88chain 'B' and (resid 310 through 320 )BB310 - 32010 - 20
99chain 'B' and (resid 321 through 328 )BB321 - 32821 - 28
1010chain 'B' and (resid 329 through 337 )BB329 - 33729 - 37
1111chain 'B' and (resid 338 through 368 )BB338 - 36838 - 68
1212chain 'B' and (resid 369 through 377 )BB369 - 37769 - 77
1313chain 'B' and (resid 378 through 385 )BB378 - 38578 - 85
1414chain 'B' and (resid 386 through 392 )BB386 - 39286 - 92
1515chain 'B' and (resid 393 through 412 )BB393 - 41293 - 112
1616chain 'C' and (resid 31 through 59 )CC31 - 591 - 29
1717chain 'C' and (resid 60 through 70 )CC60 - 7030 - 40
1818chain 'C' and (resid 71 through 80 )CC71 - 8041 - 50
1919chain 'C' and (resid 81 through 94 )CC81 - 9451 - 64
2020chain 'C' and (resid 95 through 107 )CC95 - 10765 - 77
2121chain 'D' and (resid 45 through 58 )DD45 - 581 - 14
2222chain 'D' and (resid 59 through 65 )DD59 - 6515 - 21
2323chain 'D' and (resid 66 through 81 )DD66 - 8122 - 37
2424chain 'D' and (resid 82 through 91 )DD82 - 9138 - 47
2525chain 'D' and (resid 92 through 113 )DD92 - 11348 - 69
2626chain 'D' and (resid 114 through 123 )DD114 - 12370 - 79
2727chain 'D' and (resid 124 through 130 )DD124 - 13080 - 86
2828chain 'D' and (resid 131 through 138 )DD131 - 13887 - 94
2929chain 'D' and (resid 139 through 149 )DD139 - 14995 - 105
3030chain 'E' and (resid 30 through 203 )EE30 - 2031 - 142
3131chain 'E' and (resid 204 through 241 )EE204 - 241143 - 180
3232chain 'E' and (resid 242 through 315 )EE242 - 315181 - 254
3333chain 'E' and (resid 316 through 359 )EE316 - 359255 - 298
3434chain 'F' and (resid 301 through 309 )FF301 - 3091 - 9
3535chain 'F' and (resid 310 through 315 )FF310 - 31510 - 15
3636chain 'F' and (resid 316 through 356 )FF316 - 35616 - 56
3737chain 'F' and (resid 357 through 376 )FF357 - 37657 - 76
3838chain 'F' and (resid 377 through 392 )FF377 - 39277 - 92
3939chain 'F' and (resid 393 through 401 )FF393 - 40193 - 101
4040chain 'F' and (resid 402 through 412 )FF402 - 412102 - 112
4141chain 'G' and (resid 301 through 308 )GG301 - 3081 - 8
4242chain 'G' and (resid 309 through 315 )GG309 - 3159 - 15
4343chain 'G' and (resid 316 through 356 )GG316 - 35616 - 56
4444chain 'G' and (resid 357 through 376 )GG357 - 37657 - 76
4545chain 'G' and (resid 377 through 385 )GG377 - 38577 - 85
4646chain 'G' and (resid 386 through 401 )GG386 - 40186 - 101
4747chain 'G' and (resid 402 through 412 )GG402 - 412102 - 112
4848chain 'H' and (resid 31 through 59 )HH31 - 591 - 29
4949chain 'H' and (resid 60 through 80 )HH60 - 8030 - 50
5050chain 'H' and (resid 81 through 94 )HH81 - 9451 - 62
5151chain 'H' and (resid 95 through 107 )HH95 - 10763 - 75
5252chain 'I' and (resid 45 through 58 )II45 - 581 - 14
5353chain 'I' and (resid 59 through 65 )II59 - 6515 - 21
5454chain 'I' and (resid 66 through 73 )II66 - 7322 - 29
5555chain 'I' and (resid 74 through 81 )II74 - 8130 - 37
5656chain 'I' and (resid 82 through 91 )II82 - 9138 - 47
5757chain 'I' and (resid 92 through 103 )II92 - 10348 - 59
5858chain 'I' and (resid 104 through 108 )II104 - 10860 - 64
5959chain 'I' and (resid 109 through 118 )II109 - 11865 - 74
6060chain 'I' and (resid 119 through 123 )II119 - 12375 - 79
6161chain 'I' and (resid 124 through 130 )II124 - 13080 - 86
6262chain 'I' and (resid 131 through 138 )II131 - 13887 - 94
6363chain 'I' and (resid 139 through 149 )II139 - 14995 - 105
6464chain 'J' and (resid 31 through 91 )JJ31 - 911 - 52
6565chain 'J' and (resid 92 through 233 )JJ92 - 23353 - 174
6666chain 'J' and (resid 234 through 359 )JJ234 - 359175 - 300

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