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- PDB-6e3k: Interferon gamma signalling complex with IFNGR1 and IFNGR2 -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 6e3k
TitleInterferon gamma signalling complex with IFNGR1 and IFNGR2
Components
  • (Interferon gamma receptor ...) x 2
  • Interferon gamma
KeywordsCYTOKINE / cytokine receptor / protein complex / protein engineering
Function / homology
Function and homology information


type II interferon receptor activity / : / : / positive regulation of peptidyl-serine phosphorylation of STAT protein / positive regulation of fructose 1,6-bisphosphate metabolic process / positive regulation of tumor necrosis factor (ligand) superfamily member 11 production / type II interferon receptor binding / positive regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation involved in immune response / positive regulation of protein deacetylation / positive regulation of vitamin D biosynthetic process ...type II interferon receptor activity / : / : / positive regulation of peptidyl-serine phosphorylation of STAT protein / positive regulation of fructose 1,6-bisphosphate metabolic process / positive regulation of tumor necrosis factor (ligand) superfamily member 11 production / type II interferon receptor binding / positive regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation involved in immune response / positive regulation of protein deacetylation / positive regulation of vitamin D biosynthetic process / positive regulation of cellular respiration / positive regulation of iron ion import across plasma membrane / positive regulation of interleukin-23 production / positive regulation of smooth muscle cell apoptotic process / type III interferon-mediated signaling pathway / RUNX1 and FOXP3 control the development of regulatory T lymphocytes (Tregs) / negative regulation of amyloid-beta clearance / positive regulation of core promoter binding / neuroinflammatory response / positive regulation of exosomal secretion / positive regulation of glutamate receptor signaling pathway / positive regulation of MHC class II biosynthetic process / macrophage activation involved in immune response / negative regulation of interleukin-17 production / positive regulation of osteoclast differentiation / cytokine receptor activity / cell surface receptor signaling pathway via STAT / positive regulation of membrane protein ectodomain proteolysis / positive regulation of neurogenesis / regulation of metabolic process / positive regulation of tyrosine phosphorylation of STAT protein / IFNG signaling activates MAPKs / positive regulation of amyloid-beta formation / negative regulation of epithelial cell differentiation / cytokine binding / Fc-gamma receptor signaling pathway involved in phagocytosis / humoral immune response / macrophage differentiation / positive regulation of epithelial cell migration / positive regulation of protein serine/threonine kinase activity / cell surface receptor signaling pathway via JAK-STAT / type II interferon-mediated signaling pathway / Regulation of IFNG signaling / positive regulation of chemokine production / extrinsic apoptotic signaling pathway / positive regulation of interleukin-12 production / positive regulation of autophagy / astrocyte activation / regulation of insulin secretion / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / positive regulation of phagocytosis / cytoplasmic vesicle membrane / positive regulation of glycolytic process / positive regulation of cytokine production / positive regulation of interleukin-1 beta production / cytokine activity / positive regulation of protein localization to plasma membrane / positive regulation of protein-containing complex assembly / negative regulation of smooth muscle cell proliferation / microglial cell activation / cellular response to virus / positive regulation of interleukin-6 production / positive regulation of protein import into nucleus / response to virus / cytokine-mediated signaling pathway / Interferon gamma signaling / positive regulation of inflammatory response / positive regulation of nitric oxide biosynthetic process / positive regulation of tumor necrosis factor production / defense response to virus / Potential therapeutics for SARS / adaptive immune response / cell surface receptor signaling pathway / Golgi membrane / negative regulation of gene expression / negative regulation of DNA-templated transcription / positive regulation of cell population proliferation / apoptotic process / positive regulation of gene expression / endoplasmic reticulum membrane / endoplasmic reticulum / negative regulation of transcription by RNA polymerase II / signal transduction / positive regulation of transcription by RNA polymerase II / extracellular space / extracellular region / membrane / plasma membrane
Similarity search - Function
Interferon gamma receptor 1, transmembrane region / Interferon gamma receptor, D2 domain, poxvirus/mammal / Interferon gamma receptor (IFNGR1), D2 domain / Interferon gamma receptor alpha subunit / Interferon gamma / Interferon gamma / Interferon/interleukin receptor domain / Interferon-alpha/beta receptor, fibronectin type III / : / Tissue factor ...Interferon gamma receptor 1, transmembrane region / Interferon gamma receptor, D2 domain, poxvirus/mammal / Interferon gamma receptor (IFNGR1), D2 domain / Interferon gamma receptor alpha subunit / Interferon gamma / Interferon gamma / Interferon/interleukin receptor domain / Interferon-alpha/beta receptor, fibronectin type III / : / Tissue factor / Growth Hormone; Chain: A; - #10 / Four-helical cytokine-like, core / Growth Hormone; Chain: A; / Fibronectin type-III domain profile. / Fibronectin type III / Fibronectin type III superfamily / Immunoglobulin-like fold / Immunoglobulins / Up-down Bundle / Immunoglobulin-like / Sandwich / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
CYSTEINE / Interferon gamma / Interferon gamma receptor 1 / Interferon gamma receptor 2
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.25 Å
AuthorsJude, K.M. / Mendoza, J.L. / Garcia, K.C.
Funding support United States, 2items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)RO1-AI51321 United States
National Institutes of Health/National Cancer Institute (NIH/NCI)K01CA175127 United States
CitationJournal: Nature / Year: 2019
Title: Structure of the IFN gamma receptor complex guides design of biased agonists.
Authors: Mendoza, J.L. / Escalante, N.K. / Jude, K.M. / Sotolongo Bellon, J. / Su, L. / Horton, T.M. / Tsutsumi, N. / Berardinelli, S.J. / Haltiwanger, R.S. / Piehler, J. / Engleman, E.G. / Garcia, K.C.
History
DepositionJul 14, 2018Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 27, 2019Provider: repository / Type: Initial release
Revision 1.1Mar 13, 2019Group: Data collection / Database references / Category: citation / citation_author / pdbx_database_proc / Item: _citation.pdbx_database_id_PubMed / _citation.title
Revision 1.2Mar 20, 2019Group: Data collection / Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.3Dec 4, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / chem_comp ...atom_site / 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 / 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_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.name / _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 / _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 2.1Oct 11, 2023Group: 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
Revision 2.2Nov 20, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Interferon gamma
B: Interferon gamma
C: Interferon gamma receptor 1
D: Interferon gamma receptor 1
E: Interferon gamma receptor 2
I: Interferon gamma receptor 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)146,38628
Polymers141,7826
Non-polymers4,60422
Water1448
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)78.284, 151.464, 211.301
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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Protein , 1 types, 2 molecules AB

#1: Protein Interferon gamma / IFN-gamma / Immune interferon


Mass: 17216.453 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: IFNG / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: P01579

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Interferon gamma receptor ... , 2 types, 4 molecules CDEI

#2: Protein Interferon gamma receptor 1 / IFN-gamma-R1 / CDw119 / Interferon gamma receptor alpha-chain / IFN-gamma-R-alpha


Mass: 27363.729 Da / Num. of mol.: 2 / Mutation: T149I, M161K, Q167K, K174N, Q182R, H205N
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: IFNGR1 / Cell line (production host): HEK 293 / Production host: Homo sapiens (human) / References: UniProt: P15260
#3: Protein Interferon gamma receptor 2 / IFN-gamma-R2 / Interferon gamma receptor accessory factor 1 / AF-1 / Interferon gamma receptor beta- ...IFN-gamma-R2 / Interferon gamma receptor accessory factor 1 / AF-1 / Interferon gamma receptor beta-chain / IFN-gamma-R-beta / Interferon gamma transducer 1


Mass: 26310.582 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: IFNGR2, IFNGT1 / Cell line (production host): HEK 293 / Production host: Homo sapiens (human) / References: UniProt: P38484

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Sugars , 3 types, 14 molecules

#4: 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.: 1 / Source method: obtained synthetically
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
#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.: 1
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: 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


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 12 / Source method: obtained synthetically / 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, 16 molecules

#7: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Formula: C2H6O2
#8: Chemical ChemComp-CYS / CYSTEINE


Type: L-peptide linking / Mass: 121.158 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H7NO2S
#9: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 8 / Source method: isolated from a natural source / Formula: H2O

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Details

Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION / Number of used crystals: 1

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Sample preparation

CrystalDensity Matthews: 4.42 Å3/Da / Density % sol: 72.16 %
Crystal growTemperature: 293 K / Method: vapor diffusion / pH: 7 / Details: 100 mM Bis Tris Propane pH 7.0, 2 M sodium formate

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: SSRL / Beamline: BL12-2 / Wavelength: 0.97946 Å
DetectorType: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jul 23, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97946 Å / Relative weight: 1
ReflectionResolution: 3.25→49.49 Å / Num. obs: 40393 / % possible obs: 99.9 % / Redundancy: 6.6 % / CC1/2: 0.994 / Rmerge(I) obs: 0.138 / Rpim(I) all: 0.058 / Rrim(I) all: 0.149 / Χ2: 0.88 / Net I/σ(I): 11.1
Reflection shellResolution: 3.25→3.38 Å / Redundancy: 6.8 % / Rmerge(I) obs: 1.454 / Mean I/σ(I) obs: 1.2 / Num. unique obs: 4469 / CC1/2: 0.7 / Rpim(I) all: 0.594 / Rrim(I) all: 1.573 / Χ2: 0.87 / % possible all: 99.9

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Processing

Software
NameVersionClassification
PHENIX1.14_3211refinement
XDSJune 1, 2017data reduction
Aimless0.5.3.2data scaling
PHASER2.8.0phasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 1fg9, 5eh1

1fg9

5eh1


Resolution: 3.25→37.188 Å / SU ML: 0.43 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 26.28
RfactorNum. reflection% reflectionSelection details
Rfree0.2321 1783 4.53 %random
Rwork0.1904 ---
obs0.1923 39329 97.41 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å
Refinement stepCycle: LAST / Resolution: 3.25→37.188 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8663 0 295 8 8966
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0039194
X-RAY DIFFRACTIONf_angle_d0.58912517
X-RAY DIFFRACTIONf_dihedral_angle_d11.2825486
X-RAY DIFFRACTIONf_chiral_restr0.0471423
X-RAY DIFFRACTIONf_plane_restr0.0041585
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
3.25-3.33780.36271370.33832903X-RAY DIFFRACTION100
3.3378-3.4360.32691340.28772825X-RAY DIFFRACTION97
3.436-3.54680.30991250.2672624X-RAY DIFFRACTION90
3.5468-3.67350.30951230.24272618X-RAY DIFFRACTION90
3.6735-3.82040.32051390.23812930X-RAY DIFFRACTION100
3.8204-3.99410.27181320.20392729X-RAY DIFFRACTION92
3.9941-4.20440.20581380.18182912X-RAY DIFFRACTION100
4.2044-4.46740.20941400.17072944X-RAY DIFFRACTION100
4.4674-4.81170.21451410.14972953X-RAY DIFFRACTION100
4.8117-5.29470.18541410.15272966X-RAY DIFFRACTION100
5.2947-6.05790.25491410.18092998X-RAY DIFFRACTION100
6.0579-7.62160.22281440.19663010X-RAY DIFFRACTION100
7.6216-37.190.20751480.18113134X-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)
18.45010.4536-1.93199.14815.07343.33470.00310.99410.1498-0.4072-0.1369-0.88390.33871.8161-0.20371.00510.25730.04331.39250.04850.8226-16.77817.0825-14.41
27.94691.599-1.00733.2375-3.61776.8416-0.08220.7775-0.3269-0.4269-0.0292-0.18790.81580.37390.02530.99610.3324-0.06240.9642-0.020.8318-19.761-2.2961-0.174
32.54843.5912-3.62697.8736-2.14598.504-0.7027-0.4264-0.16110.16550.8421-0.3738-0.41080.1669-0.28321.04510.1685-0.15460.8527-0.0760.8614-17.127114.6186-4.1778
46.4516-4.30154.95772.975-2.82995.432-0.13650.6341.48050.5472-0.79110.502-0.5829-0.3870.76851.06420.2487-0.05451.10460.00190.9762-23.249910.18739.5192
54.61230.78910.61878.40892.25852.8818-0.74620.74230.19890.14631.1825-0.1450.67291.7144-0.80441.31370.15630.07591.35360.15810.9268-15.60240.272123.0835
61.99992.000121.99992212.0388-40.08217.201712.9179-6.66682.894510.56181.4606-5.40483.2645-0.051-0.80942.0676-0.55821.152-35.5899-6.809719.2969
79.33871.9978-4.1119.2966-3.38329.80440.1603-1.529-0.53012.2501-0.16550.6433-0.27130.9867-0.37891.87050.3498-0.03691.28910.18511.2451-16.1411-10.540330.7046
82.88190.1820.77227.6035-1.01158.23710.123-1.60980.05220.5038-0.057-0.541-0.3556-0.4282-0.10311.1163-0.02830.12641.17880.06240.8466-18.54731.57419.729
97.44175.6353-1.67195.33060.18444.8047-0.51330.6658-0.0374-0.05080.8692-0.0790.64770.4836-0.31921.72580.4086-0.05350.8879-0.00991.1173-11.0482-12.711921.3091
101.30873.4113-1.21978.8555-3.13767.22990.31990.3303-0.5250.70280.0479-0.63430.91230.733-0.14341.43070.3538-0.22351.38890.08181.2783-15.8815-9.06695.5583
116.5458-1.84784.49136.6266-0.02438.01340.7620.3361-0.2785-1.0126-0.34540.33030.08040.1684-0.56481.00410.257-0.01050.8621-0.08230.6239-17.73941.0561-7.4759
126.55912.70693.47672.27151.37573.9698-1.23590.67420.583-2.2808-1.0797-0.6685-1.54690.2842.58274.31120.2099-0.4333.27070.02891.053-37.6397-1.6997-2.9916
136.5075-1.2855-4.4181.90612.62114.49320.01240.8760.0085-0.3286-0.0417-0.46750.7060.25660.0551.31610.3620.03931.3395-0.02740.896-15.3456-7.5216-30.7912
147.9274-2.9414-0.82035.321.40223.0676-0.57060.1598-0.71590.1859-0.07221.1280.5413-0.54550.56461.0803-0.16140.0491.1427-0.27621.2124-48.7262.4011-20.2911
159.2373-0.30746.28694.50750.36616.9473-0.0268-0.13-0.0464-0.307-0.17630.61040.4299-0.37090.18880.9830.15850.14241.2917-0.15461.2285-44.85265.3426-26.6093
161.99982.000121.99981.99991.9997-8.14721.0786-2.3823-27.85653.3511-13.44710.67890.38354.6992.3329-0.74060.19741.6788-0.00922.0535-71.89918.5101-29.1298
175.21071.81381.49354.96015.11915.04120.0046-0.57080.03220.36060.3149-0.1259-0.3909-0.9969-0.19451.52540.2023-0.02491.47390.25321.0065-18.27349.522748.1573
187.91214.40081.26338.98051.26474.8036-0.8838-0.7739-0.0339-1.04540.19951.83810.5145-1.5710.55511.3386-0.1122-0.14512.01630.17461.3219-42.1584-10.454638.1175
190.83290.96830.56861.05460.18870.57170.26020.0990.19030.1810.07290.63440.1432-0.801-0.51191.9215-0.3884-0.26291.97780.31491.7254-43.8556-18.05938.4182
204.0739-1.2109-2.12083.76590.33211.41020.19550.692-0.97560.26050.1817-0.59810.66240.137-0.31442.61180.325-0.55632.05620.10452.4949-12.3066-32.914823.9104
214.9053-1.7682-0.41941.45090.3521.86740.340.0774-2.28221.0761-0.52210.25310.89590.0305-0.17092.4264-0.5126-0.23561.69280.32422.2798-46.9876-33.999826.0083
229.85198.89565.66039.25944.47116.2152-0.40960.25221.443-0.4957-0.04691.0852-0.154-0.25240.5340.61460.0782-0.11290.91970.00630.9864-30.93936.273-4.5428
237.03611.6521-0.42054.50590.03855.821-0.12530.71690.7124-0.90710.18110.7196-0.03510.2998-0.11970.84790.05280.01271.07930.0770.9442-22.75233.7981-9.3043
244.38320.42330.30532.72530.3752.54250.0285-0.1016-0.6829-0.0759-0.23910.57820.3877-0.5670.09160.5022-0.01620.04740.9744-0.08960.8692-48.388221.8421-7.3079
252.89512.38644.30215.6332.95096.8979-0.924-0.30161.44030.318-0.65780.59890.1979-0.64211.19070.77410.01680.40881.2258-0.00570.9495-56.624421.2561-7.273
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid -1 through 23 )
2X-RAY DIFFRACTION2chain 'A' and (resid 24 through 59 )
3X-RAY DIFFRACTION3chain 'A' and (resid 60 through 80 )
4X-RAY DIFFRACTION4chain 'A' and (resid 81 through 97 )
5X-RAY DIFFRACTION5chain 'A' and (resid 98 through 122 )
6X-RAY DIFFRACTION6chain 'A' and (resid 123 through 123 )
7X-RAY DIFFRACTION7chain 'B' and (resid -1 through 14 )
8X-RAY DIFFRACTION8chain 'B' and (resid 15 through 59 )
9X-RAY DIFFRACTION9chain 'B' and (resid 60 through 80 )
10X-RAY DIFFRACTION10chain 'B' and (resid 81 through 102 )
11X-RAY DIFFRACTION11chain 'B' and (resid 103 through 122 )
12X-RAY DIFFRACTION12chain 'B' and (resid 123 through 124 )
13X-RAY DIFFRACTION13chain 'C' and (resid 11 through 113 )
14X-RAY DIFFRACTION14chain 'C' and (resid 114 through 204 )
15X-RAY DIFFRACTION15chain 'C' and (resid 205 through 222 )
16X-RAY DIFFRACTION16chain 'C' and (resid 223 through 223 )
17X-RAY DIFFRACTION17chain 'D' and (resid 11 through 103 )
18X-RAY DIFFRACTION18chain 'D' and (resid 104 through 161 )
19X-RAY DIFFRACTION19chain 'D' and (resid 162 through 221 )
20X-RAY DIFFRACTION20chain 'E' and (resid 28 through 146 )
21X-RAY DIFFRACTION21chain 'E' and (resid 147 through 240 )
22X-RAY DIFFRACTION22chain 'I' and (resid 28 through 48 )
23X-RAY DIFFRACTION23chain 'I' and (resid 49 through 105 )
24X-RAY DIFFRACTION24chain 'I' and (resid 106 through 218 )
25X-RAY DIFFRACTION25chain 'I' and (resid 219 through 240 )

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