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- PDB-4grw: Structure of a complex of human IL-23 with 3 Nanobodies (Llama vHHs) -

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Basic information

Entry
Database: PDB / ID: 4grw
TitleStructure of a complex of human IL-23 with 3 Nanobodies (Llama vHHs)
Components
  • Interleukin-12 subunit beta
  • Interleukin-23 subunit alphaInterleukin 23
  • Nanobody 124C4
  • Nanobody 22E11
  • Nanobody 37D5
KeywordsIMMUNE SYSTEM / Cytokine / immunoglobulin fold / VHH domain
Function / homology
Function and homology information


late endosome lumen / interleukin-23 receptor binding / 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 ...late endosome lumen / interleukin-23 receptor binding / 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 / 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 / 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 / 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 / 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 subunit alpha
Similarity search - Component
Biological speciesHomo sapiens (human)
Lama glama (llama)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.55 Å
AuthorsDesmyter, A. / Spinelli, S. / Button, C. / Saunders, M. / de Haard, H. / Rommelaere, H. / Union, A. / Cambillau, C.
CitationJournal: Front Immunol / Year: 2017
Title: Neutralization of Human Interleukin 23 by Multivalent Nanobodies Explained by the Structure of Cytokine-Nanobody Complex.
Authors: Desmyter, A. / Spinelli, S. / Boutton, C. / Saunders, M. / Blachetot, C. / de Haard, H. / Denecker, G. / Van Roy, M. / Cambillau, C. / Rommelaere, H.
History
DepositionAug 27, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 19, 2014Provider: repository / Type: Initial release
Revision 1.1Dec 6, 2017Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
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 / database_PDB_caveat / 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 / struct_asym / struct_conn / 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_seq_id / _atom_site.label_asym_id / _atom_site.label_entity_id / _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.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 / _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.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
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Sep 13, 2023Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession
Revision 2.2Dec 27, 2023Group: Advisory / Derived calculations / Category: pdbx_validate_close_contact / struct_conn

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Interleukin-23 subunit alpha
B: Interleukin-12 subunit beta
C: Interleukin-23 subunit alpha
D: Interleukin-12 subunit beta
E: Nanobody 124C4
F: Nanobody 37D5
G: Nanobody 124C4
H: Nanobody 22E11
I: Nanobody 22E11
J: Nanobody 37D5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)199,00212
Polymers197,18010
Non-polymers1,8222
Water12,791710
1
A: Interleukin-23 subunit alpha
B: Interleukin-12 subunit beta
G: Nanobody 124C4
H: Nanobody 22E11
J: Nanobody 37D5
hetero molecules


Theoretical massNumber of molelcules
Total (without water)99,5016
Polymers98,5905
Non-polymers9111
Water905
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
C: Interleukin-23 subunit alpha
D: Interleukin-12 subunit beta
E: Nanobody 124C4
F: Nanobody 37D5
I: Nanobody 22E11
hetero molecules


Theoretical massNumber of molelcules
Total (without water)99,5016
Polymers98,5905
Non-polymers9111
Water905
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)102.270, 135.140, 139.010
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number19
Space group name H-MP212121

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Components

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Antibody , 4 types, 8 molecules BDEGFJHI

#2: 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.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: IL12 p40, IL12B, NKSF2 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: P29460
#3: Antibody Nanobody 124C4


Mass: 13402.756 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Lama glama (llama) / Production host: Escherichia coli (E. coli) / Strain (production host): BL21
#4: Antibody Nanobody 37D5


Mass: 13847.148 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Lama glama (llama) / Production host: Escherichia coli (E. coli) / Strain (production host): BL21
#5: Antibody Nanobody 22E11


Mass: 13377.733 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Lama glama (llama) / Production host: Escherichia coli (E. coli) / Strain (production host): BL21

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Protein / Sugars / Non-polymers , 3 types, 714 molecules AC

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


Mass: 20749.688 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: IL23 p19, IL23A, SGRF, UNQ2498/PRO5798 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: Q9NPF7
#6: Polysaccharide alpha-D-mannopyranose-(1-3)-[alpha-D-mannopyranose-(1-6)]beta-D-mannopyranose-(1-4)-2-acetamido-2- ...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: 910.823 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DManpa1-3[DManpa1-6]DManpb1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/3,5,4/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5]/1-1-2-3-3/a4-b1_b4-c1_c3-d1_c6-e1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(3+1)][a-D-Manp]{}[(6+1)][a-D-Manp]{}}}}}LINUCSPDB-CARE
#7: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 710 / 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: 2.43 Å3/Da / Density % sol: 49.48 %
Crystal growTemperature: 277 K / pH: 5.9
Details: 16.5 % PEG 20K and 0.1M MES, pH 5.9, VAPOR DIFFUSION, SITTING DROP, temperature 277K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: ESRF / Beamline: ID29 / Wavelength: 0.931
DetectorType: ADSC QUANTUM 4 / Detector: CCD / Date: Mar 7, 2009
RadiationMonochromator: HIGH RESOLUTION SI(311) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.931 Å / Relative weight: 1
ReflectionResolution: 2.54→45 Å / Num. obs: 63755 / % possible obs: 99.8 % / Observed criterion σ(I): 0 / Redundancy: 4 % / Biso Wilson estimate: 55.41 Å2 / Rmerge(I) obs: 0.082 / Net I/σ(I): 13.5
Reflection shellResolution: 2.55→2.61 Å / Redundancy: 4.1 % / Rmerge(I) obs: 0.601 / Mean I/σ(I) obs: 2.65 / % possible all: 99.8

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Processing

Software
NameVersionClassification
ADSCQuantumdata collection
PHASERphasing
BUSTER2.9.2refinement
MOSFLMdata reduction
SCALAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3D85

3d85


Resolution: 2.55→43.83 Å / Cor.coef. Fo:Fc: 0.923 / Cor.coef. Fo:Fc free: 0.9 / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
RfactorNum. reflection% reflectionSelection details
Rfree0.218 1940 3.06 %RANDOM
Rwork0.183 ---
obs0.184 63328 --
all-63328 --
Displacement parametersBiso mean: 50.5 Å2
Baniso -1Baniso -2Baniso -3
1-11.3457 Å20 Å20 Å2
2--1.1144 Å20 Å2
3----12.4602 Å2
Refine analyzeLuzzati coordinate error obs: 0.28 Å
Refinement stepCycle: LAST / Resolution: 2.55→43.83 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12299 0 122 710 13131
Refine LS restraints
Refine-IDTypeDev idealNumberRestraint functionWeight
X-RAY DIFFRACTIONt_bond_d0.0112727HARMONIC2
X-RAY DIFFRACTIONt_angle_deg1.2117302HARMONIC2
X-RAY DIFFRACTIONt_dihedral_angle_d4196SINUSOIDAL2
X-RAY DIFFRACTIONt_incorr_chiral_ct
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_trig_c_planes290HARMONIC2
X-RAY DIFFRACTIONt_gen_planes1838HARMONIC5
X-RAY DIFFRACTIONt_it12597HARMONIC20
X-RAY DIFFRACTIONt_nbd
X-RAY DIFFRACTIONt_omega_torsion3.25
X-RAY DIFFRACTIONt_other_torsion23.02
X-RAY DIFFRACTIONt_improper_torsion
X-RAY DIFFRACTIONt_chiral_improper_torsion01650SEMIHARMONIC5
X-RAY DIFFRACTIONt_sum_occupancies
X-RAY DIFFRACTIONt_utility_distance
X-RAY DIFFRACTIONt_utility_angle
X-RAY DIFFRACTIONt_utility_torsion
X-RAY DIFFRACTIONt_ideal_dist_contact013635SEMIHARMONIC4
LS refinement shellResolution: 2.55→2.62 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.2498 140 3.02 %
Rwork0.2223 4494 -
all0.2231 4634 -
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)
10.1465-0.1154-0.098400.05540.07460.0006-0.0005-0.00250.0007-0.00070.0064-0.0014-0.00050.0001-0.00380.00690.00420.00050.00070.0053-3.208940.6262-51.7767
20.04510.1564-0.04110.1347-0.20030.1213-0.0013-0.0061-0.0034-0.0044-0.001-0.00410.00310.00010.00240.0057-0.01160.0099-0.01010.00870.0084.285126.7887-53.3973
300.24280.14720.0816-0.08020.0383-0.0036-0.0139-0.00220.00050.0009-0.00460.0036-0.00560.0027-0.0035-0.0026-0.0010.00860.0364-0.0006-1.828134.6319-37.8275
40.02070.3611-0.33270-0.24220.1886-0.00170.0009-0.00620.00850.0005-0.00350.0034-0.00350.0012-0.0052-0.01080.01140.00590.011-0.0011-3.557138.5075-38.357
50.4517-0.0211-0.347600.080.0708-0.00270.0018-0.00450.00120.0037-0.00090.0026-0.004-0.001-0.01130.00530.00050.00450.01760.0043.747436.6044-48.351
60.0557-0.2369-0.52310.3305-0.730400.0021-0.0045-0.0139-0.0039-0.00360.00220.0041-0.00770.0016-0.0134-0.0290.00250.01160.05750.001153.204130.3009-35.0376
70.0202-0.50830.10720.0273-0.90340.31330.0014-0.0073-0.00860.0015-0.000800.0169-0.025-0.0006-0.00590.0141-0.01670.01320.0727-0.009153.502833.5607-36.1041
80.3-0.01440.78360.0779-0.68710.21450.0015-0.0025-0.0004-0.0009-0.0040.00830.0010.00580.0025-0.0170.0289-0.01570.01860.0312-0.003430.976343.869-50.1851
90.5819-0.16120.66380.1306-0.73320.29280.0018-0.0046-0.0153-0.0029-0.00970.0086-0.00340.01360.0079-0.01760.0303-0.03380.01290.052-0.005132.157539.25-50.808
101.14180.1896-0.20880.3474-0.95640.15560.0052-0.0070.00250.00140.00270.0034-0.00560.0059-0.0079-0.0230.0455-0.0021-0.02260.01740.02697.927351.0419-65.1998
110.7262-0.18440.08380.034-0.321700.0003-0.00520.0031-0.00470.00310.0021-0.00550.0035-0.0035-0.00090.0070.0066-0.00740.00930.01310.790855.6935-62.508
120.0046-0.0239-0.07060.15030.18730.0473-0.00040.0013-0.0024-0.0009-0.00170.0043-0.0093-0.00130.0020.00260.00160.0102-0.0077-0.02910.004912.647618.8677-1.8189
130-0.1211-0.36070.23520.35180.25450-0.0039-0.00030.0048-0.0013-0.00110.0069-0.00180.00130.011-0.0070.0227-0.0048-0.00850.001618.10995.40025.4532
1400.1531-0.923400.4030.23370.0008-0.00620.00750.0072-0.0013-0.0024-0.0114-0.00390.00050.0193-0.01680.0286-0.0019-0.0146-0.016220.037723.705210.2756
150-0.2868-0.15490.31860.40030-0.0016-0.00340.00080.0111-0.0044-0.00080.0025-0.00020.006-0.0020.01710.0143-0.0115-0.01650.00918.513326.59887.4117
160.2078-0.5498-0.14870.22990.73180-0.00160.0032-0.00970.0059-0.00460.0073-0.005-0.00150.0061-0.00530.01030.0193-0.0028-0.01210.005819.08415.36790.8832
170.1704-0.38780.17380.2287-0.39620.6325-0.0032-0.0053-0.0080.00610.00070.00070.00330.01030.00260.01550.0060.0177-0.02080.0230.00670.95710.8472-0.007
180.54210.44230.19170.198-0.10030-0.0018-0.006-0.00550.0017-0.00690.00140.00050.01050.00870.00570.0007-0.0055-0.03690.00780.01670.66682.3292-3.1993
190.37710.45980.25560.07430.18320.1678-0.00060.00520.00090.00320.0002-0.0036-0.0072-0.00140.0004-0.00490.00940.0129-0.0004-0.01770.00444.2018.9863-12.1581
200.44240.1280.03250.50170.09550-0.00250.0011-0.01170.0050.01030.0141-0.00840.0099-0.0078-0.008-0.01610.0064-0.0082-0.02030.001844.55295.3512-9.4603
210.2506-0.2745-0.086700.05610.3613-0.0003-0.00370.0065-0.02960.00250.017-0.00840.0015-0.00220.00630.0203-0.0151-0.01010.0331-0.003318.459912.2181-19.5904
220.1512-0.1403-0.07640.2687-0.05870.02530.00110.00990.0031-0.0029-0.00030.0038-0.0023-0.0022-0.00080.0104-0.00450.00590.00370.0161-0.00921.326216.697-23.2207
230.01160.1336-0.18441.27920.44510.59260.00430.026-0.00630.0207-0.0037-0.00380.01340.0004-0.0006-0.00410.0043-0.0177-0.0095-0.05-0.018717.2343-13.0182-18.9322
2400.0652-0.320600.21630.37080.0020.0118-0.0016-0.0077-0.00340.0020.0017-0.00170.00130.01120.00670.0265-0.00130.0083-0.010324.444839.888-17.7637
250.0305-0.3529-0.28860.3582-0.24560.43480.00060.00980.00370.0006-0.0036-0.0034-0.00060.01390.0030.01310.00690.0339-0.00890.0109-0.000524.744145.8256-12.1597
260.0542-0.5811-0.56570.25360.14690.17020.00170.0104-0.00670.0050.0012-0.00390.00150.0032-0.00280.01160.00870.04570.0007-0.0002-0.011531.678439.1262-11.952
270.0391-0.9781-0.40210.86270.71250.69580.0041-0.00080.002-0.0054-0.00730.01550.03860.01440.00310.04640.0429-0.0347-0.0541-0.0091-0.018917.233331.9421-80.6759
280.150.3821-0.26950.0934-0.94180.2686-0.0001-0.00510.0086-0.00180.0052-0.0004-0.0070.0025-0.0051-0.0136-0.0229-0.01930.0190.0345-0.011261.041360.8562-35.6226
290.34610.1637-0.254700.10350.6450.0021-0.0127-0.00190.00520.0029-0.001-0.01350.0069-0.005-0.0130.0026-0.01260.03990.0215-0.027359.674257.611-28.2989
300.2235-0.0520.21640.057-0.63480.20690.001-0.001-0.00060.00160.0036-0.0007-0.00660.0032-0.0045-0.0235-0.0135-0.02960.01460.02520.008863.428954.3133-35.9968
310.5501-0.2056-0.45020.782-0.10480.74570.00070.00960.0118-0.0224-0.01-0.02850.01030.00270.0093-0.0662-0.00820.016-0.0230.03170.053180.106417.0273-20.9272
320.62140.5545-0.60850.50890.28870.13680.0038-0.01470.0066-0.0017-0.0032-0.0002-0.00460.0071-0.0006-0.0323-0.0497-0.01350.0223-0.0580.00358.846163.8855-34.0901
330-0.0003-0.01120.0177-0.00010.020400.0001-0.0007-0.0006-0.0002-0.0014-0.00080.00020.00020.0065-0.00140.00130.0026-0.0014-0.004258.53496.92987.2253
340.05060.05070.02020.0007-0.02080-0.00060.00140.00060.00140.000600.00120.00110-0.0005-0.007-0.00470.00390.00480.00238.63428.7456-32.3127
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1A 8 A 29
2X-RAY DIFFRACTION2A 30 A 69
3X-RAY DIFFRACTION3A 70 A 98
4X-RAY DIFFRACTION4A 99 A 140
5X-RAY DIFFRACTION5A 141 A 168
6X-RAY DIFFRACTION6B 1 B 45
7X-RAY DIFFRACTION7B 46 B 93
8X-RAY DIFFRACTION8B 94 B 139
9X-RAY DIFFRACTION9B 143 B 204
10X-RAY DIFFRACTION10B 205 B 277
11X-RAY DIFFRACTION11B 278 B 305
12X-RAY DIFFRACTION12C 9 C 29
13X-RAY DIFFRACTION13C 30 C 69
14X-RAY DIFFRACTION14C 70 C 98
15X-RAY DIFFRACTION15C 99 C 140
16X-RAY DIFFRACTION16C 141 C 170
17X-RAY DIFFRACTION17D 1 D 45
18X-RAY DIFFRACTION18D 46 D 93
19X-RAY DIFFRACTION19D 94 D 140
20X-RAY DIFFRACTION20D 141 D 204
21X-RAY DIFFRACTION21D 205 D 277
22X-RAY DIFFRACTION22D 278 D 305
23X-RAY DIFFRACTION23E 1 E 125
24X-RAY DIFFRACTION24F 2 F 40
25X-RAY DIFFRACTION25F 41 F 90
26X-RAY DIFFRACTION26F 91 F 126
27X-RAY DIFFRACTION27G 1 G 121
28X-RAY DIFFRACTION28H 1 H 39
29X-RAY DIFFRACTION29H 40 H 90
30X-RAY DIFFRACTION30H 91 H 123
31X-RAY DIFFRACTION31I 1 I 123
32X-RAY DIFFRACTION32J 3 J 126
33X-RAY DIFFRACTION33D 401 D 405
34X-RAY DIFFRACTION34B 401 B 405

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