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- PDB-5oyj: Crystal structure of VEGFR-2 domains 4-5 in complex with DARPin D4b -

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Basic information

Entry
Database: PDB / ID: 5oyj
TitleCrystal structure of VEGFR-2 domains 4-5 in complex with DARPin D4b
Components
  • DARPin D4b
  • Vascular endothelial growth factor receptor 2VEGF receptor
KeywordsSIGNALING PROTEIN / glycoprotein receptor kinase designed ankyrin repeat protein angiogenesis
Function / homology
Function and homology information


blood vessel endothelial cell differentiation / cellular response to hydrogen sulfide / regulation of bone development / regulation of hematopoietic progenitor cell differentiation / Signaling by membrane-tethered fusions of PDGFRA or PDGFRB / endothelium development / Neurophilin interactions with VEGF and VEGFR / vascular endothelial growth factor binding / positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway / vascular endothelial growth factor receptor-2 signaling pathway ...blood vessel endothelial cell differentiation / cellular response to hydrogen sulfide / regulation of bone development / regulation of hematopoietic progenitor cell differentiation / Signaling by membrane-tethered fusions of PDGFRA or PDGFRB / endothelium development / Neurophilin interactions with VEGF and VEGFR / vascular endothelial growth factor binding / positive regulation of endothelial cell chemotaxis by VEGF-activated vascular endothelial growth factor receptor signaling pathway / vascular endothelial growth factor receptor-2 signaling pathway / VEGF binds to VEGFR leading to receptor dimerization / endocardium development / vascular wound healing / vascular endothelial growth factor receptor activity / post-embryonic camera-type eye morphogenesis / endothelial cell differentiation / mesenchymal cell proliferation / lymph vessel development / positive regulation of vasculogenesis / positive regulation of BMP signaling pathway / surfactant homeostasis / epithelial cell maturation / anchoring junction / cell migration involved in sprouting angiogenesis / positive regulation of positive chemotaxis / vascular endothelial growth factor signaling pathway / embryonic hemopoiesis / positive regulation of mesenchymal cell proliferation / positive regulation of mitochondrial depolarization / positive regulation of mitochondrial fission / branching involved in blood vessel morphogenesis / positive regulation of cell migration involved in sprouting angiogenesis / lung alveolus development / positive regulation of stem cell proliferation / positive regulation of nitric-oxide synthase biosynthetic process / growth factor binding / sorting endosome / positive regulation of focal adhesion assembly / regulation of MAPK cascade / semaphorin-plexin signaling pathway / positive regulation of macroautophagy / : / positive regulation of blood vessel endothelial cell migration / calcium ion homeostasis / cellular response to vascular endothelial growth factor stimulus / cell fate commitment / vasculogenesis / Integrin cell surface interactions / coreceptor activity / vascular endothelial growth factor receptor signaling pathway / negative regulation of endothelial cell apoptotic process / peptidyl-tyrosine autophosphorylation / ovarian follicle development / positive regulation of endothelial cell proliferation / transmembrane receptor protein tyrosine kinase activity / positive regulation of endothelial cell migration / VEGFR2 mediated cell proliferation / epithelial cell proliferation / stem cell proliferation / Hsp90 protein binding / receptor protein-tyrosine kinase / VEGFA-VEGFR2 Pathway / peptidyl-tyrosine phosphorylation / cell surface receptor protein tyrosine kinase signaling pathway / positive regulation of angiogenesis / cell migration / integrin binding / cell junction / regulation of cell shape / angiogenesis / protein tyrosine kinase activity / negative regulation of neuron apoptotic process / positive regulation of MAPK cascade / protein autophosphorylation / positive regulation of ERK1 and ERK2 cascade / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / early endosome / receptor complex / endosome / positive regulation of cell migration / cadherin binding / positive regulation of protein phosphorylation / membrane raft / external side of plasma membrane / negative regulation of gene expression / positive regulation of cell population proliferation / negative regulation of apoptotic process / Golgi apparatus / endoplasmic reticulum / extracellular region / ATP binding / identical protein binding / nucleus / plasma membrane
Similarity search - Function
Vascular endothelial growth factor receptor 2 (VEGFR2) / VEGFR-2, transmembrane domain / VEGFR-2 Transmembrane domain / Vascular endothelial growth factor receptor 1-like, Ig-like domain / Tyrosine-protein kinase, receptor class III, conserved site / Receptor tyrosine kinase class III signature. / Ankyrin repeat-containing domain / Immunoglobulin domain / Immunoglobulin / Immunoglobulin domain ...Vascular endothelial growth factor receptor 2 (VEGFR2) / VEGFR-2, transmembrane domain / VEGFR-2 Transmembrane domain / Vascular endothelial growth factor receptor 1-like, Ig-like domain / Tyrosine-protein kinase, receptor class III, conserved site / Receptor tyrosine kinase class III signature. / Ankyrin repeat-containing domain / Immunoglobulin domain / Immunoglobulin / Immunoglobulin domain / Immunoglobulin I-set / Immunoglobulin I-set domain / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat / Alpha Horseshoe / Tyrosine-protein kinase, catalytic domain / Tyrosine kinase, catalytic domain / Tyrosine protein kinases specific active-site signature. / Immunoglobulin subtype / Immunoglobulin / Tyrosine-protein kinase, active site / Protein tyrosine and serine/threonine kinase / Serine-threonine/tyrosine-protein kinase, catalytic domain / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulins / 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 / Immunoglobulin-like / Sandwich / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
trehalose / ACETATE ION / CACODYLATE ION / Vascular endothelial growth factor receptor 2
Similarity search - Component
Biological speciessynthetic construct (others)
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.38 Å
AuthorsPiscitelli, C.L. / Thieltges, K.M. / Markovic-Mueller, S. / Binz, H.K. / Ballmer-Hofer, K.
Funding support Switzerland, 1items
OrganizationGrant numberCountry
Switzerland
CitationJournal: Angiogenesis / Year: 2018
Title: Characterization of a drug-targetable allosteric site regulating vascular endothelial growth factor signaling.
Authors: Thieltges, K.M. / Avramovic, D. / Piscitelli, C.L. / Markovic-Mueller, S. / Binz, H.K. / Ballmer-Hofer, K.
History
DepositionSep 10, 2017Deposition site: PDBE / Processing site: PDBE
Revision 1.0Mar 14, 2018Provider: repository / Type: Initial release
Revision 1.1Jul 25, 2018Group: Data collection / Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Non-polymer description / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / entity_name_com / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_molecule_features / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_struct_conn_angle / pdbx_struct_special_symmetry / struct_asym / struct_conn / struct_conn_type / struct_site / struct_site_gen
Item: _atom_site.B_iso_or_equiv / _atom_site.Cartn_x ..._atom_site.B_iso_or_equiv / _atom_site.Cartn_x / _atom_site.Cartn_y / _atom_site.Cartn_z / _atom_site.auth_asym_id / _atom_site.auth_atom_id / _atom_site.auth_comp_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_atom_id / _atom_site.label_comp_id / _atom_site.label_entity_id / _atom_site.type_symbol / _chem_comp.formula / _chem_comp.formula_weight / _chem_comp.id / _chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.pdbx_synonyms / _chem_comp.type / _entity.formula_weight / _entity.pdbx_description / _entity.pdbx_number_of_molecules / _entity.src_method / _entity.type / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_comp_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr1_label_atom_id / _pdbx_struct_conn_angle.ptnr1_label_comp_id / _pdbx_struct_conn_angle.ptnr1_label_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_comp_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_atom_id / _pdbx_struct_conn_angle.ptnr3_label_comp_id / _pdbx_struct_conn_angle.ptnr3_label_seq_id / _pdbx_struct_conn_angle.value / _pdbx_struct_special_symmetry.label_asym_id / _struct_conn_type.id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Jan 17, 2024Group: 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
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: DARPin D4b
B: DARPin D4b
C: Vascular endothelial growth factor receptor 2
D: Vascular endothelial growth factor receptor 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)93,56321
Polymers89,1864
Non-polymers4,37717
Water4,864270
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area8800 Å2
ΔGint-8 kcal/mol
Surface area40460 Å2
MethodPISA
Unit cell
Length a, b, c (Å)109.489, 164.559, 70.759
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21212
Components on special symmetry positions
IDModelComponents
11C-610-

CAC

21C-754-

HOH

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Components

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Protein , 2 types, 4 molecules ABCD

#1: Protein DARPin D4b


Mass: 18339.438 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) synthetic construct (others) / Production host: Escherichia coli BL21 (bacteria)
#2: Protein Vascular endothelial growth factor receptor 2 / VEGF receptor / VEGFR-2 / Fetal liver kinase 1 / FLK-1 / Kinase insert domain receptor / KDR / Protein-tyrosine ...VEGFR-2 / Fetal liver kinase 1 / FLK-1 / Kinase insert domain receptor / KDR / Protein-tyrosine kinase receptor flk-1


Mass: 26253.711 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: KDR, FLK1, VEGFR2 / Cell line (production host): HEK-293 EBNA / Production host: Homo sapiens (human)
References: UniProt: P35968, receptor protein-tyrosine kinase

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Sugars , 2 types, 10 molecules

#3: 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.: 7
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-Glycam 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
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}}LINUCSPDB-CARE
#4: Polysaccharide alpha-D-glucopyranose-(1-1)-alpha-D-glucopyranose / trehalose /


Type: oligosaccharide, Oligosaccharide / Class: Nutrient / Mass: 342.297 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Details: oligosaccharide with reducing-end-to-reducing-end glycosidic bond
References: trehalose
DescriptorTypeProgram
DGlcpa1-1DGlcpaGlycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1a_1-5]/1-1/a1-b1WURCSPDB2Glycan 1.1.0
[][a-D-Glcp]{[(1+1)][a-D-Glcp]{}}LINUCSPDB-CARE

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Non-polymers , 5 types, 277 molecules

#5: Chemical
ChemComp-CA / CALCIUM ION


Mass: 40.078 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Ca
#6: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Na
#7: Chemical ChemComp-CAC / CACODYLATE ION / dimethylarsinate / Cacodylic acid


Mass: 136.989 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H6AsO2
#8: Chemical ChemComp-ACT / ACETATE ION / Acetate


Mass: 59.044 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C2H3O2
#9: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 270 / Source method: isolated from a natural source / Formula: H2O

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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: 3.64 Å3/Da / Density % sol: 66.25 %
Crystal growTemperature: 293.15 K / Method: vapor diffusion, hanging drop / pH: 6.4
Details: 0.2 M calcium acetate monohydrate, 15% PEG 4000, 0.1 M sodium cacodylate pH 6.4, cryoprotected with 15% trehalose

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SLS / Beamline: X06SA / Wavelength: 1 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: May 28, 2016
RadiationMonochromator: SI(111) MONOCHROMATOR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.38→55.9 Å / Num. obs: 52035 / % possible obs: 99.9 % / Redundancy: 13.2 % / Biso Wilson estimate: 50.83 Å2 / CC1/2: 0.998 / Rmerge(I) obs: 0.136 / Rpim(I) all: 0.038 / Net I/σ(I): 10.7
Reflection shellResolution: 2.38→2.44 Å / Redundancy: 13 % / Rmerge(I) obs: 2.37 / Mean I/σ(I) obs: 1.3 / Num. unique obs: 3808 / CC1/2: 0.675 / Rpim(I) all: 0.68 / % possible all: 100

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Processing

Software
NameVersionClassification
PHENIX(dev_2722: ???)refinement
XDSdata reduction
Aimless0.5.26data scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 4BSJ, 2QYJ

4bsj

2qyj


Resolution: 2.38→38.749 Å / SU ML: 0.36 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 25.46
RfactorNum. reflection% reflectionSelection details
Rfree0.2288 2582 5.01 %random
Rwork0.1779 ---
obs0.1804 51496 98.92 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 2.38→38.749 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms5915 0 279 270 6464
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0096390
X-RAY DIFFRACTIONf_angle_d1.068728
X-RAY DIFFRACTIONf_dihedral_angle_d18.1873764
X-RAY DIFFRACTIONf_chiral_restr0.061025
X-RAY DIFFRACTIONf_plane_restr0.0071109
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.38-2.42580.41371330.36122616X-RAY DIFFRACTION97
2.4258-2.47530.3691320.35142643X-RAY DIFFRACTION97
2.4753-2.52910.40051410.33612634X-RAY DIFFRACTION96
2.5291-2.58790.3191450.29312584X-RAY DIFFRACTION97
2.5879-2.65270.31341450.2592660X-RAY DIFFRACTION98
2.6527-2.72440.30971370.25112703X-RAY DIFFRACTION99
2.7244-2.80450.28731650.23392663X-RAY DIFFRACTION99
2.8045-2.8950.26131470.22712717X-RAY DIFFRACTION100
2.895-2.99840.25331360.21652707X-RAY DIFFRACTION100
2.9984-3.11840.25891510.19492725X-RAY DIFFRACTION100
3.1184-3.26030.24521350.18942728X-RAY DIFFRACTION100
3.2603-3.43210.24831480.17472736X-RAY DIFFRACTION100
3.4321-3.6470.25921360.17432735X-RAY DIFFRACTION99
3.647-3.92830.18381710.14722730X-RAY DIFFRACTION100
3.9283-4.32310.16111180.12572782X-RAY DIFFRACTION100
4.3231-4.94760.17321370.11792786X-RAY DIFFRACTION100
4.9476-6.22930.1611610.14982818X-RAY DIFFRACTION100
6.2293-38.75360.24191440.17192947X-RAY DIFFRACTION99
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)
13.19812.6733.6762.72941.45119.5240.7612-0.65210.05130.4244-0.6460.32220.3526-0.9685-0.10680.5837-0.02980.14080.5287-0.03240.8327-44.1167-10.22-25.5509
23.59275.49591.96478.50543.02085.3598-0.54241.0074-0.4477-0.50020.7504-0.68690.85330.3911-0.18990.7498-0.03710.16380.44220.02480.7954-38.5606-13.7473-33.2823
33.54640.88710.49164.6285-0.66331.3237-0.1809-0.0489-0.56080.21240.16030.19070.0734-0.07980.0270.3625-0.02960.11770.3558-0.05130.3088-38.05265.0974-33.2674
46.53822.3432.17387.7285-1.47412.4355-0.32510.19120.2849-0.07710.16350.1343-0.3065-0.09630.10340.3043-0.05330.02970.44430.01120.2594-31.159420.8501-36.9936
55.52573.55845.22426.98383.35175.51160.10110.84790.5511-1.00590.30460.6539-0.2551-0.1327-0.29910.4718-0.0383-0.00180.54540.04150.456-25.134223.3834-41.6465
68.61-4.9330.13643.31220.89962.386-0.0493-0.08480.65381.9052-0.39050.98250.3842-1.07740.41770.9195-0.10380.10590.75190.00720.5755-79.045327.6947-13.1695
75.4055.11-5.09495.8239-5.74075.72810.5688-1.7353-0.15281.9038-0.14740.12910.6942-0.0454-0.39271.452-0.06780.05931.21180.1430.8283-73.922930.4431-5.5252
85.00910.2090.11883.6918-1.3569.50770.2401-0.575-0.88111.27330.15570.92090.3795-0.7051-0.33480.7031-0.00760.0010.4480.18270.7803-73.207426.3924-17.8971
92.78860.1768-2.87793.5873-4.98259.41270.1592-1.1683-0.23612.3169-0.5356-1.01170.50190.79060.23120.9245-0.0027-0.2580.59930.12490.6209-64.664428.1226-10.2415
106.9924-1.5840.39765.44740.7287.670.5788-0.0013-1.2071.1914-0.15330.52710.60520.2998-0.30920.6081-0.0868-0.18450.40020.1410.9624-68.32922.597-25.3296
115.0898-3.53312.24813.6922-2.97922.7481-0.1301-0.50240.26620.9036-0.01130.01090.00290.13090.06370.6301-0.0285-0.18940.44860.04250.8875-60.976232.4239-21.6049
129.2368-1.44015.90345.6864-0.06593.91780.32690.0703-1.14670.19890.5316-0.7999-0.08890.0218-0.95260.6553-0.0171-0.16710.47050.0220.9099-61.206424.4329-29.9956
136.07-2.1017-2.10626.8572-2.18827.0452-0.1169-0.1994-0.23860.20360.3015-1.28340.04750.1969-0.16990.3523-0.0059-0.08060.2394-0.0980.7539-56.220135.3214-29.5647
146.0925-1.2571-0.28568.8888-0.62756.55390.04820.6615-0.9035-0.02370.4923-1.63340.3520.396-0.48450.4757-0.05350.00870.5921-0.23391.043-57.221827.4992-39.9864
156.5993-3.9878-3.63612.92781.67442.5560.27750.7321-1.0671-0.93390.4261-1.96340.3101-0.3137-0.66350.6222-0.04390.08060.7369-0.25540.9635-56.850438.6336-41.5932
164.2541-3.90261.35334.0743-0.98398.47730.67630.30511.544-0.8037-0.3261-2.5584-0.60581.559-0.27740.6302-0.14620.08460.9056-0.1441.197-48.641539.2224-37.1898
173.37521.5879-1.9422.81411.46827.6813-0.4422-1.29391.28510.30770.8569-0.95320.35221.0376-0.39160.44770.0185-0.04350.5318-0.1310.4799-5.791231.3103-33.7375
186.1753-3.9357-2.12215.0821.42561.90910.11860.13510.6001-0.36090.055-0.0722-0.3623-0.1313-0.15580.40970.0243-0.00650.36680.06530.4557-20.457441.9012-39.9675
198.3675-6.0976-6.11064.77284.91795.5999-0.1188-0.15560.27030.03060.1676-0.0530.0350.03930.04870.3293-0.0290.02060.3484-0.0110.4533-20.848935.3267-36.6101
204.9805-3.6984-3.59195.60083.65693.71921.27721.46630.952-1.3797-0.9106-0.6659-0.7246-0.06810.02470.60380.02170.11220.59710.09220.6648-45.888864.085-30.9266
214.0838-2.0753-0.96067.27282.36731.1384-0.26180.1114-0.1030.58170.268-0.0330.23830.04910.0350.45150.02370.0330.4859-0.01790.4588-49.70565.4499-20.8883
222.7199-1.6848-0.93459.5096-0.28672.1942-0.2505-0.40990.01510.32540.1564-0.9018-0.23420.1860.21720.4596-0.04070.03250.5478-0.04260.6408-44.412674.4872-19.1891
233.2685-1.6578-0.64033.69271.45261.839-0.1346-0.1311-0.55380.97950.15950.00950.20930.0721-0.00440.5311-0.00110.03060.4128-0.00690.5888-53.046259.1993-19.8968
241.05811.17470.97272.55731.04372.4728-0.0740.10350.11890.2847-0.13150.1587-0.09180.0933-0.06660.3666-0.00730.04810.4119-0.03290.455-50.001969.1277-23.4605
255.738-0.0964-2.4223.01470.77226.09910.071-0.3264-0.28580.44380.0368-0.3740.17370.3582-0.11570.50610.0267-0.03310.3899-0.00030.3487-21.38298.5636-23.1794
260.60820.6867-1.80412.1474-3.59257.1072-0.44350.4397-0.4911-0.5165-0.11920.47350.887-0.38030.62320.6859-0.11010.00520.7312-0.08190.5074-44.28048.375417.2493
272.1653-0.09-2.45553.20550.05866.49170.16340.280.2954-0.39690.02120.6777-0.0083-0.2481-0.17010.4833-0.041-0.08090.69240.01030.4835-45.240716.39314.0709
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 9 through 23 )
2X-RAY DIFFRACTION2chain 'A' and (resid 24 through 35 )
3X-RAY DIFFRACTION3chain 'A' and (resid 36 through 125 )
4X-RAY DIFFRACTION4chain 'A' and (resid 126 through 155 )
5X-RAY DIFFRACTION5chain 'A' and (resid 156 through 169 )
6X-RAY DIFFRACTION6chain 'B' and (resid 13 through 23 )
7X-RAY DIFFRACTION7chain 'B' and (resid 24 through 35 )
8X-RAY DIFFRACTION8chain 'B' and (resid 36 through 59 )
9X-RAY DIFFRACTION9chain 'B' and (resid 60 through 69 )
10X-RAY DIFFRACTION10chain 'B' and (resid 70 through 82 )
11X-RAY DIFFRACTION11chain 'B' and (resid 83 through 101 )
12X-RAY DIFFRACTION12chain 'B' and (resid 102 through 115 )
13X-RAY DIFFRACTION13chain 'B' and (resid 116 through 135 )
14X-RAY DIFFRACTION14chain 'B' and (resid 136 through 148 )
15X-RAY DIFFRACTION15chain 'B' and (resid 149 through 158 )
16X-RAY DIFFRACTION16chain 'B' and (resid 159 through 169 )
17X-RAY DIFFRACTION17chain 'C' and (resid 322 through 338 )
18X-RAY DIFFRACTION18chain 'C' and (resid 339 through 389 )
19X-RAY DIFFRACTION19chain 'C' and (resid 390 through 418 )
20X-RAY DIFFRACTION20chain 'C' and (resid 419 through 433 )
21X-RAY DIFFRACTION21chain 'C' and (resid 434 through 465 )
22X-RAY DIFFRACTION22chain 'C' and (resid 466 through 493 )
23X-RAY DIFFRACTION23chain 'C' and (resid 494 through 525 )
24X-RAY DIFFRACTION24chain 'C' and (resid 526 through 552 )
25X-RAY DIFFRACTION25chain 'D' and (resid 322 through 418 )
26X-RAY DIFFRACTION26chain 'D' and (resid 419 through 440 )
27X-RAY DIFFRACTION27chain 'D' and (resid 441 through 553 )

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