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- PDB-5mzv: IL-23:IL-23R:Nb22E11 complex -

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Basic information

Entry
Database: PDB / ID: 5mzv
TitleIL-23:IL-23R:Nb22E11 complex
Components
  • (Interleukin-23 ...Interleukin 23) x 2
  • Interleukin-12 subunit beta
  • Nanobody 22E11
KeywordsCYTOKINE / inflammation / extracellular / fibronectin type III
Function / homology
Function and homology information


late endosome lumen / interleukin-23 receptor binding / interleukin-23-mediated signaling pathway / interleukin-12 alpha subunit binding / interleukin-12 complex / interleukin-23 complex / regulation of tyrosine phosphorylation of STAT protein / natural killer cell activation involved in immune response / positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target / negative regulation of vascular endothelial growth factor signaling pathway ...late endosome lumen / interleukin-23 receptor binding / interleukin-23-mediated signaling pathway / interleukin-12 alpha subunit binding / interleukin-12 complex / interleukin-23 complex / regulation of tyrosine phosphorylation of STAT protein / natural killer cell activation involved in immune response / positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target / negative regulation of vascular endothelial growth factor signaling pathway / negative regulation of blood vessel endothelial cell proliferation involved in sprouting angiogenesis / positive regulation of tissue remodeling / positive regulation of lymphocyte proliferation / positive regulation of activation of Janus kinase activity / tissue remodeling / sexual reproduction / positive regulation of T-helper 1 type immune response / positive regulation of smooth muscle cell apoptotic process / positive regulation of NK T cell activation / positive regulation of mononuclear cell proliferation / interleukin-12 receptor binding / positive regulation of memory T cell differentiation / natural killer cell activation / T-helper cell differentiation / interleukin-23 receptor complex / negative regulation of interleukin-17 production / positive regulation of osteoclast differentiation / Interleukin-23 signaling / positive regulation of T-helper 17 type immune response / positive regulation of NK T cell proliferation / interleukin-12-mediated signaling pathway / positive regulation of neutrophil chemotaxis / positive regulation of granulocyte macrophage colony-stimulating factor production / Interleukin-12 signaling / response to UV-B / cytokine receptor activity / positive regulation of natural killer cell activation / T-helper 1 type immune response / negative regulation of interleukin-10 production / cytokine binding / positive regulation of activated T cell proliferation / response to type II interferon / defense response to protozoan / positive regulation of interleukin-17 production / Interleukin-10 signaling / positive regulation of natural killer cell proliferation / positive regulation of interleukin-10 production / negative regulation of protein secretion / positive regulation of cell adhesion / positive regulation of T-helper 17 cell lineage commitment / T cell proliferation / positive regulation of tyrosine phosphorylation of STAT protein / regulation of cytokine production / negative regulation of inflammatory response to antigenic stimulus / positive regulation of defense response to virus by host / positive regulation of T cell proliferation / positive regulation of interleukin-12 production / cytokine activity / negative regulation of smooth muscle cell proliferation / positive regulation of inflammatory response / positive regulation of T cell mediated cytotoxicity / cellular response to type II interferon / cytokine-mediated signaling pathway / positive regulation of non-canonical NF-kappaB signal transduction / cell migration / positive regulation of type II interferon production / positive regulation of tumor necrosis factor production / defense response to virus / Interleukin-4 and Interleukin-13 signaling / cellular response to lipopolysaccharide / defense response to Gram-negative bacterium / response to lipopolysaccharide / receptor complex / inflammatory response / protein heterodimerization activity / endoplasmic reticulum lumen / external side of plasma membrane / innate immune response / protein-containing complex binding / positive regulation of transcription by RNA polymerase II / extracellular space / extracellular region / identical protein binding / plasma membrane / cytosol
Similarity search - Function
Interleukin-23 alpha / Interleukin 23 subunit alpha / Interleukin-12 beta / Interleukin-12 beta, central domain / Cytokine interleukin-12p40 C-terminus / Long hematopoietin receptor, soluble alpha chain, conserved site / Long hematopoietin receptor, soluble alpha chains family signature. / Growth Hormone; Chain: A; - #10 / Four-helical cytokine-like, core / Growth Hormone; Chain: A; ...Interleukin-23 alpha / Interleukin 23 subunit alpha / Interleukin-12 beta / Interleukin-12 beta, central domain / Cytokine interleukin-12p40 C-terminus / Long hematopoietin receptor, soluble alpha chain, conserved site / Long hematopoietin receptor, soluble alpha chains family signature. / Growth Hormone; Chain: A; - #10 / Four-helical cytokine-like, core / Growth Hormone; Chain: A; / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / Fibronectin type-III domain profile. / Fibronectin type III / Fibronectin type III superfamily / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulins / Immunoglobulin-like fold / Up-down Bundle / Immunoglobulin-like / Sandwich / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
Interleukin-12 subunit beta / Interleukin-23 receptor / Interleukin-23 subunit alpha
Similarity search - Component
Biological speciesHomo sapiens (human)
Lama glama (llama)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.8 Å
AuthorsBloch, Y. / Savvides, S.N.
Funding support Belgium, 1items
OrganizationGrant numberCountry
VLAIO Belgium
CitationJournal: Immunity / Year: 2018
Title: Structural Activation of Pro-inflammatory Human Cytokine IL-23 by Cognate IL-23 Receptor Enables Recruitment of the Shared Receptor IL-12R beta 1.
Authors: Bloch, Y. / Bouchareychas, L. / Merceron, R. / Skladanowska, K. / Van den Bossche, L. / Detry, S. / Govindarajan, S. / Elewaut, D. / Haerynck, F. / Dullaers, M. / Adamopoulos, I.E. / Savvides, S.N.
History
DepositionFeb 1, 2017Deposition site: PDBE / Processing site: PDBE
Revision 1.0Jan 3, 2018Provider: repository / Type: Initial release
Revision 1.1Jan 10, 2018Group: Database references / Category: citation / citation_author
Item: _citation.journal_id_ISSN / _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.2Jan 31, 2018Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation.year
Revision 1.3Feb 7, 2018Group: Structure summary / Category: entity / Item: _entity.details
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / chem_comp / entity / 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_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_struct_conn_angle / pdbx_validate_close_contact / 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 / _atom_site_anisotrop.U[1][1] / _atom_site_anisotrop.U[1][2] / _atom_site_anisotrop.U[1][3] / _atom_site_anisotrop.U[2][2] / _atom_site_anisotrop.U[2][3] / _atom_site_anisotrop.U[3][3] / _atom_site_anisotrop.id / _atom_site_anisotrop.pdbx_auth_asym_id / _atom_site_anisotrop.pdbx_auth_seq_id / _atom_site_anisotrop.pdbx_label_asym_id / _chem_comp.name / _chem_comp.type / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_validate_close_contact.auth_asym_id_2 / _pdbx_validate_close_contact.auth_seq_id_2 / _struct_conn.conn_type_id / _struct_conn.id / _struct_conn.pdbx_dist_value / _struct_conn.pdbx_leaving_atom_flag / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_comp_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr1_label_atom_id / _struct_conn.ptnr1_label_comp_id / _struct_conn.ptnr1_label_seq_id / _struct_conn.ptnr1_symmetry / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_comp_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_conn.ptnr2_label_atom_id / _struct_conn.ptnr2_label_comp_id / _struct_conn.ptnr2_label_seq_id / _struct_conn.ptnr2_symmetry / _struct_conn_type.id
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Jan 17, 2024Group: Data collection / Database references ...Data collection / Database references / Derived calculations / 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_conn
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_conn.pdbx_leaving_atom_flag

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Interleukin-12 subunit beta
B: Interleukin-23 subunit alpha
C: Interleukin-23 receptor
D: Nanobody 22E11
hetero molecules


Theoretical massNumber of molelcules
Total (without water)117,95615
Polymers114,2894
Non-polymers3,66711
Water1,35175
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10750 Å2
ΔGint3 kcal/mol
Surface area44980 Å2
MethodPISA
Unit cell
Length a, b, c (Å)67.219, 112.190, 109.870
Angle α, β, γ (deg.)90.00, 106.24, 90.00
Int Tables number4
Space group name H-MP1211

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Components

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Interleukin-23 ... , 2 types, 2 molecules BC

#2: Protein Interleukin-23 subunit alpha / Interleukin 23 / IL-23-A / Interleukin-23 subunit p19 / IL-23p19


Mass: 21865.904 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: The native secretion signal is likely cleaved off between residues 27 and 28
Source: (gene. exp.) Homo sapiens (human) / Gene: IL23A, SGRF, UNQ2498/PRO5798 / Plasmid: pCDNA4TO / Details (production host): stable transfection / Cell line (production host): HEK293S MGAT1-/- TetR / Production host: Homo sapiens (human) / References: UniProt: Q9NPF7
#3: Protein Interleukin-23 receptor / / IL-23R


Mass: 38377.613 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: The native secretion signal is likely cleaved off between residues 23 and 24
Source: (gene. exp.) Homo sapiens (human) / Gene: IL23R / Plasmid: pCDNA4TO / Details (production host): stable transfection / Cell line (production host): HEK293S MGAT1-/- TetR / Production host: Homo sapiens (human) / References: UniProt: Q5VWK5

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Antibody , 2 types, 2 molecules AD

#1: Antibody Interleukin-12 subunit beta / / IL-12B / Cytotoxic lymphocyte maturation factor 40 kDa subunit / CLMF p40 / IL-12 subunit p40 / NK ...IL-12B / Cytotoxic lymphocyte maturation factor 40 kDa subunit / CLMF p40 / IL-12 subunit p40 / NK cell stimulatory factor chain 2 / NKSF2


Mass: 37212.918 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: The native secretion signal is likely cleaved off between residues 22 and 23
Source: (gene. exp.) Homo sapiens (human) / Gene: IL12B, NKSF2 / Plasmid: pCDNA4TO / Details (production host): stable transfection / Cell line (production host): HEK293S MGAT1-/- TetR / Production host: Homo sapiens (human) / References: UniProt: P29460
#4: Antibody Nanobody 22E11


Mass: 16832.816 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: The PelB secretion signal is likely cleaved off between residues -1 and 1
Source: (gene. exp.) Lama glama (llama) / Plasmid: pMECS / Production host: Escherichia coli (E. coli) / Variant (production host): WK6

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Sugars , 4 types, 7 molecules

#5: Polysaccharide alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-alpha-D- ...alpha-D-mannopyranose-(1-2)-alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-3)-alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 1235.105 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-2DManpa1-3[DManpa1-3DManpa1-6]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,7,6/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3-3-3/a4-b1_b4-c1_c3-d1_c6-f1_d2-e1_f3-g1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{[(2+1)][a-D-Manp]{}}[(6+1)][a-D-Manp]{[(3+1)][a-D-Manp]{}}}}}}LINUCSPDB-CARE
#6: 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.: 3
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
#7: Polysaccharide beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 586.542 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5]/1-1-2/a4-b1_b4-c1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{}}}}LINUCSPDB-CARE
#10: 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.: 2
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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Non-polymers , 3 types, 79 molecules

#8: Chemical ChemComp-CL / CHLORIDE ION / Chloride


Mass: 35.453 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Cl
#9: Chemical ChemComp-NA / SODIUM ION


Mass: 22.990 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: Na
#11: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 75 / 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: 3.48 Å3/Da / Density % sol: 64.66 %
Crystal growTemperature: 287 K / Method: vapor diffusion, hanging drop / pH: 6.6
Details: 200 mM magnesium chloride, 100 mM Tris, 11 % (w/v) PEG8000
Temp details: Molecular Dimensions Cooled crystallization incubator

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: PETRA III, EMBL c/o DESY / Beamline: P14 (MX2) / Wavelength: 0.97625 Å
DetectorType: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Sep 22, 2015
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97625 Å / Relative weight: 1
ReflectionResolution: 2.8→79 Å / Num. obs: 38061 / % possible obs: 98.4 % / Redundancy: 3.45 % / Biso Wilson estimate: 72.2 Å2 / CC1/2: 0.997 / Rrim(I) all: 0.081 / Net I/σ(I): 12.45
Reflection shellResolution: 2.8→2.87 Å / Redundancy: 3.53 % / Mean I/σ(I) obs: 2.71 / Num. unique obs: 2797 / CC1/2: 0.565 / Rrim(I) all: 0.547 / % possible all: 99.1

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Processing

Software
NameVersionClassification
PHENIX(dev_2614: ???)refinement
BUSTERrefinement
XDSdata reduction
XDSdata scaling
PHASER2.6.0phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: hybrid model of IL23 from 4OE8 in complex with nanobody 22E11 from 4GRW

4oe8
PDB Unreleased entry

4grw


Resolution: 2.8→76.851 Å / SU ML: 0.38 / Cross valid method: FREE R-VALUE / σ(F): 1.38 / Phase error: 25.72
Details: Early refinement done against anisotropy corrected data.
RfactorNum. reflection% reflectionSelection details
Rfree0.2504 1594 4.19 %Phenix reflection tool editor
Rwork0.2121 ---
obs0.2137 38058 98.5 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Displacement parametersBiso mean: 84.47 Å2
Refinement stepCycle: LAST / Resolution: 2.8→76.851 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6786 0 238 75 7099
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0037239
X-RAY DIFFRACTIONf_angle_d0.6359875
X-RAY DIFFRACTIONf_dihedral_angle_d9.8914320
X-RAY DIFFRACTIONf_chiral_restr0.0441129
X-RAY DIFFRACTIONf_plane_restr0.0031226
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.8-2.89040.31541390.31973304X-RAY DIFFRACTION99
2.8904-2.99370.35511380.30813300X-RAY DIFFRACTION99
2.9937-3.11360.34751480.30073321X-RAY DIFFRACTION99
3.1136-3.25530.29211420.26653308X-RAY DIFFRACTION99
3.2553-3.42690.26691420.23813318X-RAY DIFFRACTION98
3.4269-3.64160.27481450.22973314X-RAY DIFFRACTION99
3.6416-3.92280.27611460.21973294X-RAY DIFFRACTION98
3.9228-4.31750.21241460.18893301X-RAY DIFFRACTION98
4.3175-4.94210.21031460.16493296X-RAY DIFFRACTION98
4.9421-6.22620.21591540.17963370X-RAY DIFFRACTION99
6.2262-76.850.24321480.2033338X-RAY DIFFRACTION97
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)
10.008800.00380.00740.00430.006-0.02240.02-0.05210.0154-0.05220.01910.00550.006501.58030.224-0.05641.2761-0.00820.8103-39.5035-10.11124.7001
20.01170.00980.00520.01730.02260.027-0.02360.0810.16070.01730.1503-0.12760.07640.122301.19930.19330.15791.42170.07620.8056-29.0534-0.82088.1418
30.0027-0.0081-0.0020.01250.00510.00470.08780.1047-0.15190.01830.0893-0.06290.01960.0511-01.54080.4486-0.01671.2402-0.00831.0486-31.3681-16.434211.2145
40.0169-0.0025-0.0132-0.0008-0.00360.01450.01690.0267-0.0847-0.12130.0172-0.1693-0.0373-0.0046-00.96540.27250.05090.94110.11290.5815-34.0954-6.614515.195
50.1548-0.0683-0.02070.1031-0.02760.21330.10280.09730.2035-0.1026-0.0669-0.18850.15590.14940.00120.4424-0.03740.04220.4790.04840.7811-46.935822.840951.4194
60.4571-0.0562-0.00610.02540.0260.09550.10140.15770.3624-0.1668-0.0718-0.06720.09120.00170.12540.67250.13660.01490.47120.21860.216-54.48175.113618.9276
70.10820.0159-0.06850.086-0.03940.0790.0702-0.09470.00930.0982-0.03060.1069-0.0518-0.02810.05330.4673-0.048-0.03620.51270.07670.6891-66.403711.320262.2357
80.00590.00080.00120.0017-0.00040.0019-0.0028-0.0202-0.0060.01710.0281-0.038-0.03890.0549-00.8269-0.1421-0.00740.94690.1240.9604-57.59698.470471.7201
90.0969-0.0271-0.02580.06710.01010.02620.0358-0.0221-0.1493-0.07280.02-0.10.0025-0.128100.4955-0.07120.0270.4670.08690.6359-66.482511.974364.3877
100.0518-0.0136-0.02330.01720.01690.01780.0382-0.037-0.0220.11760.0494-0.1575-0.04450.189-00.61680.05230.03790.62020.07480.9143-24.4923-16.091844.5425
110.0678-0.01950.01110.0246-0.01060.0553-0.0115-0.0791-0.08050.0614-0.02410.3686-0.20630.191600.63160.0123-0.03480.52280.05750.7108-31.7217-10.925548.0675
120.0113-0.0106-0.02340.01020.01350.03230.1851-0.02230.0111-0.10910.05510.0298-0.16690.0299-00.48870.06030.04950.40080.0220.6164-32.5235-8.251238.613
130.044-0.01910.03040.0490.05030.11030.18250.04470.1105-0.1531-0.1081-0.1143-0.10250.0837-00.53370.05970.00180.73030.13050.7413-0.1285-37.416932.9664
140.0205-0.0341-0.00460.05270.00750-0.116-0.05540.1047-0.15090.0548-0.070.3385-0.0137-01.11780.0286-0.0171.067-0.03290.5276-5.4168-65.436718.2658
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'B' and (resid 28 :48 )
2X-RAY DIFFRACTION2chain 'B' and (resid 67 :110 )
3X-RAY DIFFRACTION3chain 'B' and (resid 111:137 )
4X-RAY DIFFRACTION4chain 'B' and (resid 151:188 )
5X-RAY DIFFRACTION5chain 'A' and (resid 23 through 127 )
6X-RAY DIFFRACTION6(chain 'A' and resid 128:327)
7X-RAY DIFFRACTION7chain 'D' and (resid 1 through 61)
8X-RAY DIFFRACTION8chain 'D' and (resid 62 through 69 )
9X-RAY DIFFRACTION9chain 'D' and (resid 70 through 123 )
10X-RAY DIFFRACTION10(chain 'C' and resid 24 through 47 ) or (chain 'C' and resid 410:411)
11X-RAY DIFFRACTION11(chain 'C' and resid 48 through 95 )
12X-RAY DIFFRACTION12(chain 'C' and (resid 96 through 123 )) or (chain 'B' and resid 54:60)
13X-RAY DIFFRACTION13(chain 'C' and resid 124 through 213 )
14X-RAY DIFFRACTION14(chain 'C' and resid 214 through 316 )

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