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- PDB-8t9b: Structure of the CK variant of Fab F1 (FabC-F1) in complex with t... -

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Basic information

Entry
Database: PDB / ID: 8t9b
TitleStructure of the CK variant of Fab F1 (FabC-F1) in complex with the C-terminal FN3 domain of EphA2
Components
  • CK variant of Fab F1 heavy chain
  • CK variant of Fab F1 light chain
  • Ephrin type-A receptor 2
KeywordsIMMUNE SYSTEM / enhanced crystallization / EphA2 binding / expressed protein / Fab / Complex / receptor clustering
Function / homology
Function and homology information


notochord cell development / notochord formation / lens fiber cell morphogenesis / blood vessel endothelial cell proliferation involved in sprouting angiogenesis / negative regulation of lymphangiogenesis / axial mesoderm formation / pericyte cell differentiation / cAMP metabolic process / regulation of blood vessel endothelial cell migration / leading edge membrane ...notochord cell development / notochord formation / lens fiber cell morphogenesis / blood vessel endothelial cell proliferation involved in sprouting angiogenesis / negative regulation of lymphangiogenesis / axial mesoderm formation / pericyte cell differentiation / cAMP metabolic process / regulation of blood vessel endothelial cell migration / leading edge membrane / negative regulation of chemokine production / post-anal tail morphogenesis / response to growth factor / bone remodeling / positive regulation of bicellular tight junction assembly / activation of GTPase activity / regulation of lamellipodium assembly / branching involved in mammary gland duct morphogenesis / EPH-Ephrin signaling / tight junction / RND1 GTPase cycle / RND2 GTPase cycle / neural tube development / RND3 GTPase cycle / mammary gland epithelial cell proliferation / RHOV GTPase cycle / EPHA-mediated growth cone collapse / growth factor binding / regulation of cell adhesion mediated by integrin / lamellipodium membrane / RHOU GTPase cycle / RHOG GTPase cycle / EPH-ephrin mediated repulsion of cells / ephrin receptor signaling pathway / RAC2 GTPase cycle / RAC3 GTPase cycle / regulation of angiogenesis / regulation of ERK1 and ERK2 cascade / vasculogenesis / keratinocyte differentiation / transmembrane receptor protein tyrosine kinase activity / RAC1 GTPase cycle / osteoclast differentiation / cell surface receptor protein tyrosine kinase signaling pathway / negative regulation of angiogenesis / molecular function activator activity / protein localization to plasma membrane / skeletal system development / cell chemotaxis / positive regulation of protein localization to plasma membrane / cell motility / placental growth factor receptor activity / insulin receptor activity / vascular endothelial growth factor receptor activity / hepatocyte growth factor receptor activity / macrophage colony-stimulating factor receptor activity / platelet-derived growth factor alpha-receptor activity / platelet-derived growth factor beta-receptor activity / stem cell factor receptor activity / boss receptor activity / protein tyrosine kinase collagen receptor activity / brain-derived neurotrophic factor receptor activity / transmembrane-ephrin receptor activity / GPI-linked ephrin receptor activity / epidermal growth factor receptor activity / fibroblast growth factor receptor activity / insulin-like growth factor receptor activity / receptor protein-tyrosine kinase / ruffle membrane / intrinsic apoptotic signaling pathway in response to DNA damage / neuron differentiation / osteoblast differentiation / cell migration / lamellipodium / virus receptor activity / angiogenesis / receptor complex / defense response to Gram-positive bacterium / cell adhesion / positive regulation of cell migration / cadherin binding / inflammatory response / focal adhesion / cell surface / ATP binding / plasma membrane
Similarity search - Function
Ephrin type-A receptor 2, ligand binding domain / Ephrin receptor type-A /type-B / Ephrin receptor ligand binding domain / Tyrosine-protein kinase, receptor class V, conserved site / Ephrin receptor, transmembrane domain / : / Ephrin receptor ligand binding domain / Ephrin type-A receptor 2 transmembrane domain / Receptor tyrosine kinase class V signature 1. / Receptor tyrosine kinase class V signature 2. ...Ephrin type-A receptor 2, ligand binding domain / Ephrin receptor type-A /type-B / Ephrin receptor ligand binding domain / Tyrosine-protein kinase, receptor class V, conserved site / Ephrin receptor, transmembrane domain / : / Ephrin receptor ligand binding domain / Ephrin type-A receptor 2 transmembrane domain / Receptor tyrosine kinase class V signature 1. / Receptor tyrosine kinase class V signature 2. / Eph receptor ligand-binding domain profile. / Ephrin receptor ligand binding domain / Putative ephrin-receptor like / SAM domain (Sterile alpha motif) / SAM domain profile. / Sterile alpha motif. / Sterile alpha motif domain / Sterile alpha motif/pointed domain superfamily / Growth factor receptor cysteine-rich domain superfamily / Fibronectin type III domain / Fibronectin type 3 domain / Fibronectin type-III domain profile. / Galactose-binding-like domain superfamily / Fibronectin type III / Fibronectin type III superfamily / Tyrosine-protein kinase, catalytic domain / Tyrosine kinase, catalytic domain / Tyrosine protein kinases specific active-site signature. / Tyrosine-protein kinase, active site / Serine-threonine/tyrosine-protein kinase, catalytic domain / Protein tyrosine and serine/threonine kinase / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Immunoglobulin-like fold / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily
Similarity search - Domain/homology
Ephrin type-A receptor 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 4.2 Å
AuthorsSinger, A.U. / Bruce, H.A. / Enderle, L. / Blazer, L. / Adams, J.J. / Sicheri, F. / Sidhu, S.S.
Funding support1items
OrganizationGrant numberCountry
Other private
Citation
Journal: Protein Sci. / Year: 2025
Title: Synthetic antibodies targeting EphA2 induce diverse signaling-competent clusters with differential activation.
Authors: Adams, J.J. / Bruce, H.A. / Subramania, S. / Ploder, L. / Garcia, J. / Pot, I. / Blazer, L.L. / Singer, A.U. / Sidhu, S.S.
#1: Journal: PloS One / Year: 2020
Title: Rapid and robust antibody Fab fragment crystallization utilizing edge-to-edge beta-sheet packing.
Authors: Lieu, R. / Antonysamy, S. / Druzina, Z. / Ho, C. / Kang, N.R. / Pustilnik, A. / Wang, J. / Atwell, S.
#2: Journal: Dev Comp Immunol / Year: 2003
Title: IMGT unique numbering for immunoglobulin and T cell receptor variable domains and Ig superfamily V-like domains.
Authors: Lefranc, M.P. / Pommie, C. / Ruiz, M. / Giudicelli, V. / Foulquier, E. / Truong, L. / Thouvenin-Contet, V. / Lefranc, G.
History
DepositionJun 23, 2023Deposition site: RCSB / Processing site: RCSB
Revision 1.0May 1, 2024Provider: repository / Type: Initial release
Revision 1.1Oct 9, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature
Revision 1.2May 7, 2025Group: Database references / Category: citation
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.title / _citation.year
Revision 1.3Jun 4, 2025Group: Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _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
C: CK variant of Fab F1 heavy chain
G: CK variant of Fab F1 light chain
A: CK variant of Fab F1 heavy chain
B: CK variant of Fab F1 light chain
D: CK variant of Fab F1 heavy chain
E: CK variant of Fab F1 light chain
F: CK variant of Fab F1 heavy chain
H: CK variant of Fab F1 light chain
I: Ephrin type-A receptor 2
J: Ephrin type-A receptor 2
K: Ephrin type-A receptor 2
L: Ephrin type-A receptor 2


Theoretical massNumber of molelcules
Total (without water)238,49312
Polymers238,49312
Non-polymers00
Water00
1
C: CK variant of Fab F1 heavy chain
G: CK variant of Fab F1 light chain
L: Ephrin type-A receptor 2


Theoretical massNumber of molelcules
Total (without water)59,6233
Polymers59,6233
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
A: CK variant of Fab F1 heavy chain
B: CK variant of Fab F1 light chain
K: Ephrin type-A receptor 2


Theoretical massNumber of molelcules
Total (without water)59,6233
Polymers59,6233
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
D: CK variant of Fab F1 heavy chain
E: CK variant of Fab F1 light chain
I: Ephrin type-A receptor 2


Theoretical massNumber of molelcules
Total (without water)59,6233
Polymers59,6233
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
F: CK variant of Fab F1 heavy chain
H: CK variant of Fab F1 light chain
J: Ephrin type-A receptor 2


Theoretical massNumber of molelcules
Total (without water)59,6233
Polymers59,6233
Non-polymers00
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)76.661, 130.650, 222.996
Angle α, β, γ (deg.)90.000, 89.760, 90.000
Int Tables number4
Space group name H-MP1211
Space group name HallP2yb
Symmetry operation#1: x,y,z
#2: -x,y+1/2,-z
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
d_1ens_1(chain "A" and (resid 1 through 47 or (resid 48...
d_2ens_1(chain "C" and (resid 1 through 47 or (resid 48...
d_3ens_1(chain "D" and (resid 1 through 153 or (resid 154...
d_4ens_1(chain "F" and (resid 1 through 47 or (resid 48...
d_1ens_2(chain "B" and (resid 5 or (resid 6 and (name...
d_2ens_2(chain "E" and (resid 5 through 50 or (resid 51...
d_3ens_2(chain "G" and (resid 5 or (resid 6 and (name...
d_4ens_2(chain "H" and (resid 5 through 66 or (resid 67...
d_1ens_3(chain "I" and (resid 438 through 461 or (resid 462...
d_2ens_3(chain "J" and (resid 438 through 462 or (resid 463...
d_3ens_3(chain "K" and (resid 438 through 461 or (resid 462...
d_4ens_3(chain "L" and (resid 438 through 461 or (resid 462...

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_1GLUGLULYSLYSAC1 - 2381 - 230
d_21ens_1GLUGLULYSLYSCA1 - 2381 - 230
d_31ens_1GLUGLULYSLYSDE1 - 2381 - 230
d_41ens_1GLUGLULYSLYSFG1 - 2381 - 230
d_11ens_2THRTHRCYSCYSBD5 - 2325 - 214
d_21ens_2THRTHRCYSCYSEF5 - 2325 - 214
d_31ens_2THRTHRCYSCYSGB5 - 2325 - 214
d_41ens_2THRTHRCYSCYSHH5 - 2325 - 214
d_11ens_3GLUGLUGLNGLNII438 - 5123 - 77
d_12ens_3GLYGLYLEULEUII516 - 52781 - 92
d_21ens_3GLUGLULEULEUJJ438 - 5273 - 92
d_31ens_3GLUGLUGLNGLNKK438 - 5123 - 77
d_32ens_3GLYGLYLEULEUKK516 - 52781 - 92
d_41ens_3GLUGLULEULEULL438 - 5273 - 92

NCS ensembles :
ID
ens_1
ens_2
ens_3

NCS oper:
IDCodeMatrixVector
1given(-0.99842010676, 0.0560321329983, -0.00420600624384), (0.0560985071446, 0.998266522254, -0.0178019112162), (0.00320123616872, -0.0180097367683, -0.999832686737)-39.9525582904, 0.60214260181, -111.727568698
2given(-0.999945926993, 0.00139164151967, 0.0103056501162), (-0.00139105668448, -0.999999030437, 6.39168327534E-5), (0.0103057290735, 4.95776330959E-5, 0.999946893335)-38.2520901348, 9.33371414912, 0.128966078114
3given(0.998909216798, -0.0465969302567, 0.003017065958), (-0.0466370397879, -0.998799706948, 0.0149710360667), (0.00231584027122, -0.0150954129372, -0.999883375895)1.08642413504, 8.72569042699, -111.787721708
4given(-0.999900922159, -0.0138470260496, 0.00253095553959), (0.0138632457583, -0.999882724844, 0.00650745544828), (0.00244054981627, 0.00654189796229, 0.999975623347)-38.8384583439, 9.6940034049, 0.372976270828
5given(-0.998250206466, 0.0591284930608, -0.000588726866659), (0.0591312759022, 0.998220505049, -0.0077016562933), (0.000132291899478, -0.00772299215569, -0.999970168501)-40.0125743942, 1.03899766636, -111.451347926
6given(0.999138510258, -0.0410624128265, -0.00600962329286), (-0.0410404993201, -0.999150538437, 0.00372544718143), (-0.00615749419899, -0.00347559980623, -0.999975002423)1.2579680814, 8.61885907881, -111.643845526
7given(-0.992950741028, 0.118124365111, 0.00977037661506), (0.118138331547, 0.99299677244, 0.000862868622276), (-0.0096000266361, 0.00201104202979, -0.999951896442)-38.8807642053, 2.84922848592, -111.838095307
8given(-0.999704605855, 0.00779062719244, 0.0230218843649), (-0.00808703376138, -0.999885244538, -0.0128100601529), (0.022919444075, -0.0129924548922, 0.999652887356)-37.4888172449, 8.38412798953, 0.979067715776
9given(0.9914242527, -0.129286018547, -0.0190545681056), (-0.12926045017, -0.991607340506, 0.00257260105387), (-0.0192272509513, -8.75370261922E-5, -0.999815135492)-0.329794613231, 6.47618625026, -111.992905659

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Components

#1: Antibody
CK variant of Fab F1 heavy chain / FabC-F1 heavy chain


Mass: 25332.188 Da / Num. of mol.: 4
Source method: isolated from a genetically manipulated source
Details: engineered Fab from phage display / Source: (gene. exp.) Homo sapiens (human) / Plasmid: pSCSTa / Cell line (production host): Expi293 / Production host: Homo sapiens (human)
#2: Antibody
CK variant of Fab F1 light chain / FabC-F1 light chain


Mass: 23267.811 Da / Num. of mol.: 4 / Mutation: HAGLSSP replaced by QGTTS
Source method: isolated from a genetically manipulated source
Details: Fab selected/engineered by phage display / Source: (gene. exp.) Homo sapiens (human) / Plasmid: pSCSTa / Cell line (production host): Expi293 / Production host: Homo sapiens (human)
#3: Protein
Ephrin type-A receptor 2 / Epithelial cell kinase / Tyrosine-protein kinase receptor ECK


Mass: 11023.206 Da / Num. of mol.: 4 / Fragment: C-termimal FN3 domain (UNP residues 436-529)
Source method: isolated from a genetically manipulated source
Details: residues 438-531 / Source: (gene. exp.) Homo sapiens (human) / Gene: EPHA2, ECK / Plasmid: pSCSTa
Details (production host): expressed with a C-terminal thrombin cleavage site and 6-his sequence. The residues LTPR at the C-terminus are derived from the thrombin cleavage site
Cell line (production host): Expi293 / Production host: Homo sapiens (human)
References: UniProt: P29317, receptor protein-tyrosine kinase
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: 4.86 Å3/Da / Density % sol: 74.72 % / Description: thin hexagonal plates
Crystal growTemperature: 298 K / Method: vapor diffusion, sitting drop / pH: 8 / Details: 1.5 M sodium formate, 100 mM Tris-HCl, pH 8.0

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-E / Wavelength: 0.97918 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Oct 20, 2021 / Details: Mirrors
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97918 Å / Relative weight: 1
ReflectionResolution: 4.2→131.33 Å / Num. obs: 31847 / % possible obs: 97.3 % / Redundancy: 3 % / Biso Wilson estimate: 101.35 Å2 / CC1/2: 0.997 / Rmerge(I) obs: 0.173 / Rpim(I) all: 0.119 / Rrim(I) all: 0.211 / Net I/σ(I): 4.2
Reflection shellResolution: 4.2→4.43 Å / Redundancy: 3 % / Rmerge(I) obs: 1.185 / Mean I/σ(I) obs: 1.2 / Num. unique obs: 4648 / CC1/2: 0.602 / Rpim(I) all: 0.813 / % possible all: 97.8

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Processing

Software
NameVersionClassification
PHENIX1.20.1_4487refinement
PHENIX1.20.1_4487refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 8T7F

8t7f


Resolution: 4.2→66.12 Å / SU ML: 0.5627 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 40.3085
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflection
Rfree0.315 1713 5.51 %
Rwork0.2957 29395 -
obs0.2968 31108 96.25 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 156.28 Å2
Refinement stepCycle: LAST / Resolution: 4.2→66.12 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms15657 0 0 0 15657
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.004916048
X-RAY DIFFRACTIONf_angle_d1.006221967
X-RAY DIFFRACTIONf_chiral_restr0.05682506
X-RAY DIFFRACTIONf_plane_restr0.02022820
X-RAY DIFFRACTIONf_dihedral_angle_d17.07885439
Refine LS restraints NCS
Ens-IDDom-IDAsym-IDAuth asym-IDRefine-IDTypeRms dev position (Å)
ens_1d_2CAX-RAY DIFFRACTIONTorsion NCS1.27511466564
ens_1d_3CAX-RAY DIFFRACTIONTorsion NCS1.05600153551
ens_1d_4CAX-RAY DIFFRACTIONTorsion NCS1.26981567014
ens_2d_2DBX-RAY DIFFRACTIONTorsion NCS1.85389334328
ens_2d_3DBX-RAY DIFFRACTIONTorsion NCS1.41475831148
ens_2d_4DBX-RAY DIFFRACTIONTorsion NCS1.95312198724
ens_3d_2IIX-RAY DIFFRACTIONTorsion NCS1.71164158135
ens_3d_3IIX-RAY DIFFRACTIONTorsion NCS1.53224374605
ens_3d_4IIX-RAY DIFFRACTIONTorsion NCS1.69206863884
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
4.2-4.320.40081400.37162474X-RAY DIFFRACTION97.65
4.32-4.460.36841450.3472465X-RAY DIFFRACTION97.1
4.46-4.620.35381410.32072387X-RAY DIFFRACTION95.54
4.62-4.810.33621320.30762288X-RAY DIFFRACTION89.2
4.81-5.030.33481350.28772418X-RAY DIFFRACTION95.47
5.03-5.290.29771420.28622458X-RAY DIFFRACTION97.71
5.29-5.620.35191480.29872513X-RAY DIFFRACTION98.37
5.62-6.060.35371470.3332482X-RAY DIFFRACTION98.35
6.06-6.670.39711500.33322503X-RAY DIFFRACTION98.85
6.67-7.630.32371470.31982522X-RAY DIFFRACTION98.34
7.63-9.60.24331450.26772437X-RAY DIFFRACTION94.75
9.61-66.120.24441410.22552448X-RAY DIFFRACTION93.8
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)
14.71915725414-2.42110505357-0.8932216210485.687285470831.812398401870.8439286626741.12444098102-0.251945466208-0.266250464677-3.79181328789-1.150529006841.19435306067-0.110674460226-1.670019070610.0198225231744-0.2921024901370.0494479481731-0.5221857686522.84816054208-0.4242883107791.36795292297-46.3834695549-7.8107037145-81.4996442256
23.29607462866-1.152198112323.129117774585.169162365340.3387963999033.800171635480.700792884556-0.24765367753-0.760918189582-0.07259540412390.0235321286162-0.03835878809311.32576693515-0.268396667709-0.558560058440.739276013967-0.129980486755-0.08955138843812.41303464163-0.1018287972081.20803800032-41.16994812-8.61568531637-77.7742517101
33.99138501633-0.3442883908024.531163496166.05407321525-0.3223468533066.488958436880.103535580254-0.369539425334-0.330916613829-1.79974493165-0.540772905350.608412598666-0.233130054547-1.274846958740.4022670696321.813440028720.0516978276296-0.2367793491122.30880188757-0.3703850454251.1577027743-36.250105229-30.7563048385-107.804857674
48.68541611988-5.20928635361-1.353686960248.630886869084.282908639996.322003547090.9349552440470.3452739193670.106823261638-0.7485189761960.520739429433-1.04844067091-0.6526586090310.50945884116-1.227294237321.125067010820.1563186344910.1316397626951.80083585107-0.1659921617351.05184853514-22.9340625696-13.9742970357-79.3436884397
58.108600326-4.66363078047-0.5261386390587.487637136942.751978057685.61510676370.785212862512-2.656924670530.3189250956511.444578633860.22683651081-0.7183924194320.2794092712070.608898672033-1.16855243507-0.8286103984580.309604931415-0.8718237427333.28640367086-0.01592924192250.964890947475-22.7716313194-18.0911520651-71.3140546629
62.30107805248-0.0287141231611-1.021809077151.454306205970.02477462194530.7875510069030.0615926895798-0.09724936219040.188864732513-0.2509357314670.172766070966-0.5033280488760.262296357331-0.178726656632-0.2307433946441.16078698930.0867451367043-0.08060791592361.25202651586-0.1330781356830.875542459597-25.2178454068-18.3948458398-99.5130111122
74.53781318902-0.9677373682722.482305713471.95544146867-2.154755233554.068481159380.2268876136230.758466090362-0.0999050275924-0.873094356544-0.8236114722490.01664769872680.3637441589190.1718186253450.3611093553721.605063675870.336265788532-0.03766644342191.99004287435-0.3247933429041.59628545995-23.3483167746-22.4314602179-112.259335592
81.975605417471.82518206556-0.1757566590513.96594088151-2.047907169941.436181854351.96437678878-0.758322755018-0.3753739985980.157707863314-1.01533392008-1.01498488074-0.2050109320851.430473741330.1387775576750.993017835777-0.0125969110305-0.6641150606052.298622833070.4358764818891.592899778799.49726901391-14.0162810212-24.9543786912
92.47258858441.547841233340.2053193337724.8331155491-1.824929539743.266725096640.5866174305660.5504242384890.2402411509540.475251472097-0.250694647194-1.046214891090.4184666462120.668749195175-0.09301167186530.6918077418880.0150135642402-0.1833123174892.282807355240.1332403451450.9966630921244.84104988194-7.94772194792-33.5727790081
102.196112270111.119514273161.092039451025.77474494307-1.770994894482.967372584430.599993351249-0.3226731252720.006769505812422.07911069651-0.51573209394-0.452688415151-0.9576217707720.7492079842510.08682022014991.281437601770.024203695642-0.3619639701912.148208889310.2979453379341.070879254157.68557097765-5.90604098088-22.5099099174
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Refinement TLS group

Refine-ID: X-RAY DIFFRACTION

IDRefine TLS-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11chain 'C' and (resid 1 through 106 )CA1 - 1061 - 98
22chain 'C' and (resid 107 through 143 )CA107 - 14399 - 135
33chain 'C' and (resid 144 through 238 )CA144 - 238136 - 230
44chain 'G' and (resid 5 through 49 )GB5 - 491 - 39
55chain 'G' and (resid 50 through 95 )GB50 - 9540 - 75
66chain 'G' and (resid 96 through 176 )GB96 - 17676 - 156
77chain 'G' and (resid 177 through 232 )GB177 - 232157 - 210
88chain 'A' and (resid 1 through 24 )AC1 - 241 - 23
99chain 'A' and (resid 25 through 85 )AC25 - 8524 - 77
1010chain 'A' and (resid 86 through 99 )AC86 - 9978 - 91
1111chain 'A' and (resid 100 through 120 )AC100 - 12092 - 112
1212chain 'A' and (resid 121 through 155 )AC121 - 155113 - 147
1313chain 'A' and (resid 156 through 167 )AC156 - 167148 - 159
1414chain 'A' and (resid 168 through 183 )AC168 - 183160 - 175
1515chain 'A' and (resid 184 through 209 )AC184 - 209176 - 201
1616chain 'A' and (resid 210 through 240 )AC210 - 240202 - 232
1717chain 'B' and (resid 5 through 95 )BD5 - 951 - 75
1818chain 'B' and (resid 96 through 232 )BD96 - 23276 - 210
1919chain 'D' and (resid 1 through 106 )DE1 - 1061 - 98
2020chain 'D' and (resid 107 through 148 )DE107 - 14899 - 140
2121chain 'D' and (resid 149 through 238 )DE149 - 238141 - 230
2222chain 'E' and (resid 4 through 49 )EF4 - 491 - 40
2323chain 'E' and (resid 50 through 131 )EF50 - 13141 - 112
2424chain 'E' and (resid 132 through 181 )EF132 - 181113 - 162
2525chain 'E' and (resid 182 through 232 )EF182 - 232163 - 211
2626chain 'F' and (resid 1 through 143 )FG1 - 1431 - 135
2727chain 'F' and (resid 144 through 238 )FG144 - 238136 - 230
2828chain 'H' and (resid 5 through 124 )HH5 - 1241 - 104
2929chain 'H' and (resid 125 through 232 )HH125 - 232105 - 210
3030chain 'I' and (resid 438 through 442 )II438 - 4421 - 5
3131chain 'I' and (resid 443 through 455 )II443 - 4556 - 18
3232chain 'I' and (resid 456 through 468 )II456 - 46819 - 31
3333chain 'I' and (resid 469 through 484 )II469 - 48432 - 47
3434chain 'I' and (resid 485 through 494 )II485 - 49448 - 57
3535chain 'I' and (resid 495 through 501 )II495 - 50158 - 64
3636chain 'I' and (resid 502 through 521 )II502 - 52165 - 83
3737chain 'I' and (resid 522 through 527 )II522 - 52784 - 89
3838chain 'J' and (resid 438 through 451 )JJ438 - 4511 - 14
3939chain 'J' and (resid 452 through 467 )JJ452 - 46715 - 30
4040chain 'J' and (resid 468 through 477 )JJ468 - 47731 - 40
4141chain 'J' and (resid 478 through 487 )JJ478 - 48741 - 50
4242chain 'J' and (resid 488 through 527 )JJ488 - 52751 - 87
4343chain 'K' and (resid 438 through 456 )KK438 - 4561 - 19
4444chain 'K' and (resid 457 through 467 )KK457 - 46720 - 30
4545chain 'K' and (resid 468 through 481 )KK468 - 48131 - 44
4646chain 'K' and (resid 482 through 501 )KK482 - 50145 - 64
4747chain 'K' and (resid 502 through 527 )KK502 - 52765 - 90
4848chain 'L' and (resid 438 through 444 )LL438 - 4441 - 7
4949chain 'L' and (resid 445 through 451 )LL445 - 4518 - 14
5050chain 'L' and (resid 452 through 456 )LL452 - 45615 - 19
5151chain 'L' and (resid 457 through 471 )LL457 - 47120 - 34
5252chain 'L' and (resid 472 through 484 )LL472 - 48435 - 47
5353chain 'L' and (resid 485 through 494 )LL485 - 49448 - 57
5454chain 'L' and (resid 495 through 509 )LL495 - 50958 - 72
5555chain 'L' and (resid 510 through 521 )LL510 - 52173 - 81
5656chain 'L' and (resid 522 through 527 )LL522 - 52782 - 87

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