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- PDB-5njd: Structure of Interleukin 23 in complex with Briakinumab FAb -

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Basic information

Entry
Database: PDB / ID: 5njd
TitleStructure of Interleukin 23 in complex with Briakinumab FAb
Components
  • (Briakinumab FAb ...) x 2
  • Interleukin-12 subunit beta
  • Interleukin-23 subunit alpha
KeywordsIMMUNE SYSTEM / antagonist / antibody / extracellular region
Function / homology
Function and homology information


late endosome lumen / regulation of tyrosine phosphorylation of STAT protein / interleukin-23 receptor binding / interleukin-12 alpha subunit binding / interleukin-12 complex / interleukin-23 complex / natural killer cell activation involved in immune response / positive regulation of natural killer cell activation / positive regulation of lymphocyte proliferation / positive regulation of natural killer cell mediated cytotoxicity directed against tumor cell target ...late endosome lumen / regulation of tyrosine phosphorylation of STAT protein / interleukin-23 receptor binding / interleukin-12 alpha subunit binding / interleukin-12 complex / interleukin-23 complex / natural killer cell activation involved in immune response / positive regulation of natural killer cell activation / positive regulation of lymphocyte proliferation / 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 activation of Janus kinase activity / tissue remodeling / sexual reproduction / positive regulation of T-helper 1 type immune response / positive regulation of NK T cell activation / positive regulation of smooth muscle cell apoptotic process / 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 / positive regulation of osteoclast differentiation / Interleukin-23 signaling / negative regulation of interleukin-17 production / 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 / Interleukin-12 signaling / response to UV-B / positive regulation of natural killer cell proliferation / positive regulation of granulocyte macrophage colony-stimulating factor production / cytokine receptor activity / 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 interleukin-10 production / positive regulation of cell adhesion / negative regulation of protein secretion / positive regulation of T-helper 17 cell lineage commitment / T cell proliferation / positive regulation of T cell proliferation / positive regulation of tyrosine phosphorylation of STAT protein / negative regulation of inflammatory response to antigenic stimulus / positive regulation of defense response to virus by host / regulation of cytokine production / positive regulation of interleukin-12 production / cytokine activity / negative regulation of smooth muscle cell proliferation / cytokine-mediated signaling pathway / cellular response to type II interferon / positive regulation of inflammatory response / positive regulation of non-canonical NF-kappaB signal transduction / positive regulation of T cell mediated cytotoxicity / positive regulation of tumor necrosis factor production / positive regulation of type II interferon production / cell migration / cellular response to lipopolysaccharide / Interleukin-4 and Interleukin-13 signaling / defense response to Gram-negative bacterium / defense response to virus / 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)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.9 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
DepositionMar 28, 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 1.3Sep 18, 2019Group: Data collection / Category: reflns_shell / Item: _reflns_shell.pdbx_Rrim_I_all
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Refinement description / 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 / refine_hist / struct_asym / struct_conn / struct_site / struct_site_gen
Item: _atom_site.auth_asym_id / _atom_site.auth_seq_id ..._atom_site.auth_asym_id / _atom_site.auth_seq_id / _atom_site.label_asym_id / _atom_site.label_entity_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 / _refine_hist.d_res_high / _refine_hist.d_res_low / _struct_conn.pdbx_role / _struct_conn.ptnr1_auth_asym_id / _struct_conn.ptnr1_auth_seq_id / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr2_auth_asym_id / _struct_conn.ptnr2_auth_seq_id / _struct_conn.ptnr2_label_asym_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-12 subunit beta
D: Interleukin-23 subunit alpha
E: Interleukin-12 subunit beta
F: Interleukin-23 subunit alpha
G: Interleukin-12 subunit beta
H: Interleukin-23 subunit alpha
I: Interleukin-12 subunit beta
J: Interleukin-23 subunit alpha
K: Interleukin-12 subunit beta
L: Interleukin-23 subunit alpha
M: Briakinumab FAb Light chain
N: Briakinumab FAb Heavy chain
O: Briakinumab FAb Light chain
P: Briakinumab FAb Heavy chain
Q: Briakinumab FAb Light chain
R: Briakinumab FAb Heavy chain
S: Briakinumab FAb Light chain
T: Briakinumab FAb Heavy chain
U: Briakinumab FAb Light chain
V: Briakinumab FAb Heavy chain
W: Briakinumab FAb Light chain
X: Briakinumab FAb Heavy chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)701,05643
Polymers694,34224
Non-polymers6,71419
Water00
1
A: Interleukin-12 subunit beta
B: Interleukin-23 subunit alpha
U: Briakinumab FAb Light chain
V: Briakinumab FAb Heavy chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)116,8277
Polymers115,7244
Non-polymers1,1033
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
C: Interleukin-12 subunit beta
D: Interleukin-23 subunit alpha
Q: Briakinumab FAb Light chain
R: Briakinumab FAb Heavy chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)116,8277
Polymers115,7244
Non-polymers1,1033
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
E: Interleukin-12 subunit beta
F: Interleukin-23 subunit alpha
W: Briakinumab FAb Light chain
X: Briakinumab FAb Heavy chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)116,8277
Polymers115,7244
Non-polymers1,1033
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
G: Interleukin-12 subunit beta
H: Interleukin-23 subunit alpha
S: Briakinumab FAb Light chain
T: Briakinumab FAb Heavy chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)116,9238
Polymers115,7244
Non-polymers1,1994
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
5
I: Interleukin-12 subunit beta
J: Interleukin-23 subunit alpha
O: Briakinumab FAb Light chain
P: Briakinumab FAb Heavy chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)116,8277
Polymers115,7244
Non-polymers1,1033
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
6
K: Interleukin-12 subunit beta
L: Interleukin-23 subunit alpha
M: Briakinumab FAb Light chain
N: Briakinumab FAb Heavy chain
hetero molecules


Theoretical massNumber of molelcules
Total (without water)116,8277
Polymers115,7244
Non-polymers1,1033
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)191.606, 191.606, 519.109
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number92
Space group name H-MP41212

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Components

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Antibody , 3 types, 18 molecules ACEGIKMOQSUWNPRTVX

#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.: 6
Source method: isolated from a genetically manipulated source
Details: First 22 amino acids form the signal peptide. / Source: (gene. exp.) Homo sapiens (human) / Gene: IL12B, NKSF2 / Plasmid: pCDNA4TO / Cell line (production host): HEK293S MGAT-/- TETR / Production host: Homo sapiens (human) / References: UniProt: P29460
#3: Antibody
Briakinumab FAb Light chain


Mass: 25925.178 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Details: first 28 amino acids form the signal peptide / Source: (gene. exp.) Homo sapiens (human) / Plasmid: pHLsec / Cell line (production host): HEK293T / Production host: Homo sapiens (human)
#4: Antibody
Briakinumab FAb Heavy chain


Mass: 30719.658 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Details: First 28 amino acids form the signal peptide. Last 41 amino acids are a cloning scar and the purification tag. Last 33 amino acids were removed by thrombin digestion.
Source: (gene. exp.) Homo sapiens (human) / Plasmid: pHLsec / Cell line (production host): HEK293T / Production host: Homo sapiens (human)

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Protein / Sugars / Non-polymers , 3 types, 25 molecules BDFHJL

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


Mass: 21865.904 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Details: First 19 amino acids form the signal peptide. Last 9 amino acids are a cloning scar and purification tag.
Source: (gene. exp.) Homo sapiens (human) / Gene: IL23A, SGRF, UNQ2498/PRO5798 / Plasmid: pCDNA4TO / Cell line (production host): HEK293S MGAT-/- TETR / Production host: Homo sapiens (human) / References: UniProt: Q9NPF7
#5: 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.: 6
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
#6: Chemical
ChemComp-SO4 / SULFATE ION


Mass: 96.063 Da / Num. of mol.: 13
Source method: isolated from a genetically manipulated source
Formula: SO4

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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: 3.83 Å3/Da / Density % sol: 67.87 %
Crystal growTemperature: 287 K / Method: vapor diffusion, sitting drop / pH: 6 / Details: 2 M (NH4)2SO4, 100 mM BisTris
Temp details: Molecular Dimensions Cooled Crystallisation Incubators

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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 PILATUS 6M / Detector: PIXEL / Date: May 1, 2016
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97625 Å / Relative weight: 1
ReflectionResolution: 3.9→95.8 Å / Num. obs: 86556 / % possible obs: 97.7 % / Redundancy: 5.1 % / Biso Wilson estimate: 69.81 Å2 / CC1/2: 0.96 / Rrim(I) all: 0.438 / Net I/σ(I): 4.2
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Mean I/σ(I) obsNum. unique obsCC1/2Rrim(I) all% possible all
11.64-94.814.6116.0235490.9950.08595.9
8.26-11.644.9113.7260690.9930.10897.8
6.75-8.265.126.4677480.9660.25598.1
5.85-6.754.993.6191140.8660.4798.7
5.24-5.855.093.22102580.830.53198.8
4.78-5.245.13.12113230.8050.56199.1
4.43-4.785.192.64122900.7490.66999.2
4.14-4.435.171.87131910.5990.91699.3
3.9-4.145.121.18130140.431.37892.5

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Processing

Software
NameVersionClassification
PHENIX(1.12_2829: ???)refinement
XDSdata reduction
XDSdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: composite model 4OE8 and homology model for FAb

4oe8
PDB Unreleased entry


Resolution: 3.9→95.8 Å / SU ML: 0.48 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 30.99 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.3118 1836 2.12 %
Rwork0.2715 --
obs0.2724 86488 97.63 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 3.9→95.8 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms39015 0 431 0 39446
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00440488
X-RAY DIFFRACTIONf_angle_d0.55255299
X-RAY DIFFRACTIONf_dihedral_angle_d9.12124122
X-RAY DIFFRACTIONf_chiral_restr0.0426318
X-RAY DIFFRACTIONf_plane_restr0.0046976
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.9048-4.01040.33511220.36045549X-RAY DIFFRACTION84
4.0104-4.12840.36821400.336485X-RAY DIFFRACTION99
4.1284-4.26170.3451420.31766520X-RAY DIFFRACTION99
4.2617-4.4140.33041420.29966523X-RAY DIFFRACTION99
4.414-4.59070.33571410.28946548X-RAY DIFFRACTION99
4.5907-4.79960.27561430.26636541X-RAY DIFFRACTION99
4.7996-5.05270.26731410.26236561X-RAY DIFFRACTION99
5.0527-5.36920.30311420.26216542X-RAY DIFFRACTION99
5.3692-5.78370.32791430.27726578X-RAY DIFFRACTION99
5.7837-6.36560.31621420.28476602X-RAY DIFFRACTION99
6.3656-7.28650.38311430.27586624X-RAY DIFFRACTION98
7.2865-9.1790.27951450.22566678X-RAY DIFFRACTION98
9.179-95.83180.28641500.2336901X-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)
11.5096-0.0682-0.00324.0824-0.49970.47020.11380.08380.01810.10930.0247-0.0984-0.2777-0.379-0.1320.94040.15080.04251.1986-0.05720.8173-40.490665.963377.2947
28.42642.7207-0.05025.2633-1.0722.1652-0.57560.45130.3522-0.16170.33160.124-0.02010.18890.21740.78690.0796-0.02880.8845-0.13650.8179-33.528633.356575.7071
32.7312-0.5102-1.15961.2847-0.24822.25210.0786-0.046-0.06490.25750.0937-0.2657-0.1402-0.0091-0.0550.64090.1223-0.14110.58810.01510.7949-57.655160.948555.1009
44.2516-0.12321.41143.5061-1.57386.9286-0.225-0.2670.00630.5867-0.12560.5474-0.5570.32210.31250.99680.13110.12240.88670.04951.1682-80.992978.45372.5641
51.4044-1.5334-0.78563.18162.32041.58850.20570.10120.2847-0.59270.062-0.4967-0.3933-0.0625-0.27241.26590.03370.16631.14950.04530.901128.701930.521312.5471
63.8075-1.79081.7943.3823-0.8113.5810.45810.5066-0.2366-0.4017-0.18030.0782-0.5571-0.1596-0.17041.13630.0420.14521.2328-0.06431.03487.674838.864136.5474
72.1244-1.5493-1.73421.67790.9622.0698-0.0029-0.25780.14140.00360.2491-0.4873-0.22510.4109-0.28030.7739-0.21490.03240.8425-0.3261.274733.633956.176469.7149
82.57461.27450.51863.88060.60746.2511-0.0322-0.34120.39750.04750.1038-0.28420.09960.2581-0.1750.8190.00230.08291.1111-0.29261.374151.059634.506251.7971
90.914-0.51260.18733.45730.20750.166-0.049-0.4033-0.13540.46930.2614-0.0169-0.1615-0.093-0.20611.09160.00480.07231.17760.14750.671-13.964224.4564116.4561
103.7091.2218-1.02523.5016-1.50675.85270.3419-0.2697-0.06440.4961-0.1533-0.2389-0.15760.2702-0.261.04360.0347-0.0281.0788-0.17311.0948-6.592655.7624106.6423
110.70280.2195-0.3911.6786-1.24881.3367-0.03760.0490.24130.0483-0.0812-0.8263-0.16830.27660.07250.72550.10760.08190.94910.09391.756324.191-28.866479.6691
121.56560.60521.41672.902-0.8211.796-0.22150.6851-0.0189-1.2578-0.0026-0.34020.45660.3750.33121.5184-0.14690.47171.49120.00961.10777.4226-10.119837.9518
131.0780.58790.41282.0992-0.48382.7065-0.19010.59720.1967-0.5751-0.1832-0.13020.13950.070.37341.0217-0.01220.21681.2033-0.08131.2452-3.1193.53445.8102
142.17480.99231.15891.47450.91712.3714-0.28070.3136-0.1261-0.60330.3048-0.1045-0.0704-0.1036-0.0241.1101-0.12670.04571.01090.18181.0736-24.278611.610564.5209
151.55891.27321.73493.36642.08642.0237-0.0075-0.1958-0.19840.03640.00060.34040.1186-0.26040.0380.8354-0.10070.09191.04610.14331.0646-35.76723.856477.2667
162.03330.11951.16482.5103-0.29661.26390.04550.4750.1306-0.7889-0.02890.05010.16680.08360.00241.0675-0.00010.07620.97480.01780.9023-80.598776.69918.6125
172.12550.08211.04831.2393-0.83641.30340.16140.671-0.3081-0.9962-0.034-0.2440.41460.104-0.26141.60820.02340.09571.3999-0.17251.2516-73.327759.54518.4997
184.5544-0.29571.49551.5621-0.37992.01110.3031-0.0734-0.1468-0.3786-0.28360.26120.4464-0.17560.03491.0551-0.00040.13410.8048-0.08260.9427-12.283733.592651.7323
194.8965-0.31521.02631.0920.38741.33530.2704-0.05930.6581-0.2651-0.2313-0.2161-0.0484-0.05670.03110.8730.02350.08550.86350.09131.0026-12.334351.970254.1617
202.51490.52251.08871.6296-0.19832.2102-0.1345-0.3190.00350.5374-0.0589-0.8731-0.26040.16230.18141.31320.115-0.13461.0425-0.09771.49879.409575.740797.0128
212.70440.9856-0.10220.3542-0.19161.48030.0992-0.77540.88620.3419-0.41520.0538-0.4315-0.26670.33481.48090.0763-0.11921.052-0.30181.2389-4.754186.1819103.4067
222.27330.27240.70032.0292-0.83512.04910.3463-0.328-0.10550.3471-0.4026-0.18940.38460.4720.07641.1838-0.07030.09131.2258-0.00411.138965.30868.688446.8243
233.0669-0.34140.05751.1574-0.88410.71170.07430.49220.12210.0783-0.2392-0.15030.24440.20610.24910.98990.01720.12381.0852-0.16251.127870.549319.558532.0129
245.591-0.18731.31263.9401-2.39223.0795-0.11720.3358-0.40290.27530.0843-0.715-0.09260.13660.0671.0461-0.0474-0.0241.2173-0.15051.1075-1.046-28.4239101.0711
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(chain 'A' and resid 23:328) or (chain 'A' and resi 401:405)
2X-RAY DIFFRACTION2chain 'B'
3X-RAY DIFFRACTION3(chain 'C' and resid 23:328) or (chain 'C' and resi 401:405)
4X-RAY DIFFRACTION4chain 'D'
5X-RAY DIFFRACTION5(chain 'E' and resid 23:328) or (chain 'E' and resi 401:405)
6X-RAY DIFFRACTION6chain 'F'
7X-RAY DIFFRACTION7(chain 'G' and resid 23:327) or (chain 'G' and resi 401:405)
8X-RAY DIFFRACTION8chain 'H'
9X-RAY DIFFRACTION9(chain 'I' and resid 23:328) or (chain 'I' and resi 401:405)
10X-RAY DIFFRACTION10chain 'J'
11X-RAY DIFFRACTION11(chain 'K' and resid 23:328) or (chain 'K' and resi 401:405)
12X-RAY DIFFRACTION12protein and chain 'N'
13X-RAY DIFFRACTION13protein and chain 'M'
14X-RAY DIFFRACTION14protein and chain 'O'
15X-RAY DIFFRACTION15protein and chain 'P'
16X-RAY DIFFRACTION16protein and chain 'Q'
17X-RAY DIFFRACTION17protein and chain 'R'
18X-RAY DIFFRACTION18protein and chain 'S'
19X-RAY DIFFRACTION19protein and chain 'T'
20X-RAY DIFFRACTION20protein and chain 'U'
21X-RAY DIFFRACTION21protein and chain 'V'
22X-RAY DIFFRACTION22protein and chain 'W'
23X-RAY DIFFRACTION23protein and chain 'X'
24X-RAY DIFFRACTION24chain 'L'

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