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- PDB-4zxb: Structure of the human insulin receptor ectodomain, IRDeltabeta c... -

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Basic information

Entry
Database: PDB / ID: 4zxb
TitleStructure of the human insulin receptor ectodomain, IRDeltabeta construct, in complex with four Fab molecules
Components
  • Fab 83-14 heavy chain
  • Fab 83-14 light chain
  • Fab 83-7 heavy chain
  • Fab 83-7 light chain
  • Insulin receptor
KeywordsHORMONE RECEPTOR/IMMUNE SYSTEM / receptor tyrosine kinase extracellular domain antibody fragments / HORMONE RECEPTOR-IMMUNE SYSTEM complex
Function / homology
Function and homology information


regulation of female gonad development / positive regulation of B cell activation / positive regulation of meiotic cell cycle / positive regulation of developmental growth / insulin-like growth factor II binding / humoral immune response mediated by circulating immunoglobulin / early endosome to late endosome transport / phagocytosis, recognition / male sex determination / exocrine pancreas development ...regulation of female gonad development / positive regulation of B cell activation / positive regulation of meiotic cell cycle / positive regulation of developmental growth / insulin-like growth factor II binding / humoral immune response mediated by circulating immunoglobulin / early endosome to late endosome transport / phagocytosis, recognition / male sex determination / exocrine pancreas development / insulin receptor complex / positive regulation of type IIa hypersensitivity / insulin-like growth factor I binding / insulin receptor activity / regulation of proteolysis / positive regulation of type I hypersensitivity / positive regulation of protein-containing complex disassembly / cargo receptor activity / antibody-dependent cellular cytotoxicity / Fc-gamma receptor I complex binding / dendritic spine maintenance / insulin binding / PTB domain binding / phagocytosis, engulfment / adrenal gland development / IgG immunoglobulin complex / neuronal cell body membrane / Signaling by Insulin receptor / endosome to lysosome transport / IRS activation / activation of protein kinase activity / amyloid-beta clearance / positive regulation of respiratory burst / positive regulation of endocytosis / regulation of embryonic development / positive regulation of receptor internalization / transport across blood-brain barrier / antigen processing and presentation / insulin receptor substrate binding / immunoglobulin mediated immune response / positive regulation of glycogen biosynthetic process / epidermis development / immunoglobulin complex, circulating / Signal attenuation / immunoglobulin receptor binding / phosphatidylinositol 3-kinase binding / positive regulation of phagocytosis / heart morphogenesis / dendrite membrane / Insulin receptor recycling / insulin-like growth factor receptor binding / neuron projection maintenance / positive regulation of glycolytic process / activation of protein kinase B activity / multivesicular body / positive regulation of mitotic nuclear division / receptor-mediated endocytosis / Insulin receptor signalling cascade / B cell differentiation / complement activation, classical pathway / learning / antigen binding / caveola / positive regulation of glucose import / response to bacterium / positive regulation of MAP kinase activity / receptor internalization / receptor protein-tyrosine kinase / memory / cellular response to growth factor stimulus / peptidyl-tyrosine phosphorylation / cellular response to insulin stimulus / positive regulation of nitric oxide biosynthetic process / male gonad development / positive regulation of immune response / late endosome / insulin receptor signaling pathway / glucose homeostasis / amyloid-beta binding / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / antibacterial humoral response / protein tyrosine kinase activity / positive regulation of MAPK cascade / protein autophosphorylation / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / lysosome / receptor complex / endosome membrane / positive regulation of cell migration / symbiont entry into host cell / positive regulation of protein phosphorylation / G protein-coupled receptor signaling pathway / protein domain specific binding / external side of plasma membrane / axon / protein phosphorylation / positive regulation of cell population proliferation / protein-containing complex binding / regulation of DNA-templated transcription / GTP binding
Similarity search - Function
24 nucleotide stem-loop, u2 snrnp hairpin iv. U2 a'; Chain A / Receptor L-domain / Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A domain 2 / Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A, domain 2 / Insulin receptor, trans-membrane domain / Insulin receptor trans-membrane segment / Tyrosine-protein kinase, insulin-like receptor / Tyrosine-protein kinase, receptor class II, conserved site / Receptor tyrosine kinase class II signature. / Alpha-Beta Horseshoe ...24 nucleotide stem-loop, u2 snrnp hairpin iv. U2 a'; Chain A / Receptor L-domain / Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A domain 2 / Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A, domain 2 / Insulin receptor, trans-membrane domain / Insulin receptor trans-membrane segment / Tyrosine-protein kinase, insulin-like receptor / Tyrosine-protein kinase, receptor class II, conserved site / Receptor tyrosine kinase class II signature. / Alpha-Beta Horseshoe / Receptor L-domain / Furin-like cysteine-rich domain / Receptor L-domain superfamily / Furin-like cysteine rich region / Receptor L domain / Furin-like repeat / Furin-like repeats / Growth factor receptor cysteine-rich domain superfamily / Fibronectin type III domain / Fibronectin type 3 domain / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / Immunoglobulin V-Type / Fibronectin type-III domain profile. / Fibronectin type III / Fibronectin type III superfamily / Immunoglobulin V-set domain / Immunoglobulin V-set domain / Ribbon / Tyrosine-protein kinase, catalytic domain / Tyrosine kinase, catalytic domain / Tyrosine protein kinases specific active-site signature. / Immunoglobulin subtype / Immunoglobulin / Immunoglobulin/major histocompatibility complex, conserved site / Immunoglobulins and major histocompatibility complex proteins signature. / Tyrosine-protein kinase, active site / Immunoglobulin C-Type / Immunoglobulin C1-set / Immunoglobulin C1-set domain / Protein tyrosine and serine/threonine kinase / Serine-threonine/tyrosine-protein kinase, catalytic domain / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulins / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Immunoglobulin-like fold / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily / Immunoglobulin-like / Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
Kappa light chain / Immunoglobulin kappa constant / Ig gamma-2A chain C region, membrane-bound form / Insulin receptor / Anti-H5N1 hemagglutinin monoclonal anitbody H5M9 heavy chain
Similarity search - Component
Biological speciesMus musculus (house mouse)
Homo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / Resolution: 3.3 Å
AuthorsCroll, T. / Smith, B.J. / Margetts, M.B. / Whittaker, J. / Weiss, M.A. / Ward, C.W. / Lawrence, M.C.
Funding support Australia, 5items
OrganizationGrant numberCountry
National Health and Medical Research Council (NHMRC, Australia)1005896 Australia
National Health and Medical Research Council (NHMRC, Australia)1058233 Australia
Hazel and Pip Appel Fund Australia
National Health and Medical Research Council (NHMRC, Australia)361646 Australia
Victorian State Government Operational Infrastructure Support Grant Australia
CitationJournal: Structure / Year: 2016
Title: Higher-Resolution Structure of the Human Insulin Receptor Ectodomain: Multi-Modal Inclusion of the Insert Domain.
Authors: Croll, T.I. / Smith, B.J. / Margetts, M.B. / Whittaker, J. / Weiss, M.A. / Ward, C.W. / Lawrence, M.C.
History
DepositionMay 20, 2015Deposition site: RCSB / Processing site: RCSB
SupersessionFeb 24, 2016ID: 2DTG, 3LOH
Revision 1.0Feb 24, 2016Provider: repository / Type: Initial release
Revision 1.1Mar 9, 2016Group: Database references
Revision 1.2Sep 6, 2017Group: Author supporting evidence / Data collection ...Author supporting evidence / Data collection / Database references / Derived calculations
Category: citation / diffrn_source ...citation / diffrn_source / pdbx_audit_support / pdbx_struct_oper_list
Item: _citation.journal_id_CSD / _diffrn_source.pdbx_synchrotron_site ..._citation.journal_id_CSD / _diffrn_source.pdbx_synchrotron_site / _pdbx_audit_support.funding_organization / _pdbx_struct_oper_list.symmetry_operation
Revision 1.3Jan 8, 2020Group: Author supporting evidence / Data collection / Category: chem_comp / pdbx_audit_support
Item: _chem_comp.type / _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 / 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 / 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 / _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_atom_id / _atom_site_anisotrop.pdbx_auth_comp_id / _atom_site_anisotrop.pdbx_auth_seq_id / _atom_site_anisotrop.pdbx_label_asym_id / _atom_site_anisotrop.pdbx_label_atom_id / _atom_site_anisotrop.pdbx_label_comp_id / _atom_site_anisotrop.type_symbol / _chem_comp.name / _chem_comp.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

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Fab 83-7 heavy chain
B: Fab 83-7 light chain
C: Fab 83-14 heavy chain
D: Fab 83-14 light chain
E: Insulin receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)202,01115
Polymers197,2175
Non-polymers4,79510
Water0
1
A: Fab 83-7 heavy chain
B: Fab 83-7 light chain
C: Fab 83-14 heavy chain
D: Fab 83-14 light chain
E: Insulin receptor
hetero molecules

A: Fab 83-7 heavy chain
B: Fab 83-7 light chain
C: Fab 83-14 heavy chain
D: Fab 83-14 light chain
E: Insulin receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)404,02330
Polymers394,43410
Non-polymers9,58920
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation3_555-x,y,-z+1/21
Unit cell
Length a, b, c (Å)121.870, 321.250, 199.400
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number20
Space group name H-MC2221
SymmetryPoint symmetry: (Schoenflies symbol: C2 (2 fold cyclic))

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Components

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Protein , 1 types, 1 molecules E

#5: Protein Insulin receptor /


Mass: 102279.945 Da / Num. of mol.: 1
Mutation: Y144H, V731A, T732G, V733N, A734N, residues 735-753 deleted
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Plasmid: pEE14 / Cell line (production host): Lec8 / Production host: Cricetulus griseus (Chinese hamster) / References: UniProt: P06213

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Antibody , 4 types, 4 molecules ABCD

#1: Antibody Fab 83-7 heavy chain


Mass: 23414.266 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: Original Mab obtained from a mouse hybridoma cell line
Source: (gene. exp.) Mus musculus (house mouse) / Production host: Mus musculus (house mouse) / References: UniProt: U5LP42
#2: Antibody Fab 83-7 light chain


Mass: 24385.072 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: The original Mab was obtained from a mouse hybridoma
Source: (gene. exp.) Mus musculus (house mouse) / Production host: Mus musculus (house mouse) / References: UniProt: P01837
#3: Antibody Fab 83-14 heavy chain


Mass: 23622.672 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: The original mAb was obtained from a mouse hybridoma
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Igh-1a / Production host: Mus musculus (house mouse) / References: UniProt: P01865
#4: Antibody Fab 83-14 light chain


Mass: 23514.807 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Details: The original mAb was obtained form a mouse hybridoma
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Igkc, Igk-C / Production host: Mus musculus (house mouse) / References: UniProt: A2P1G9

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Sugars , 5 types, 10 molecules

#6: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta- ...2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 570.542 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4[LFucpa1-6]DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1221m-1a_1-5]/1-1-2/a4-b1_a6-c1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}[(6+1)][a-L-Fucp]{}}}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
#8: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1- ...2-acetamido-2-deoxy-beta-D-glucopyranose-(1-2)-alpha-D-mannopyranose-(1-6)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 1098.016 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-2DManpa1-6DManpb1-4DGlcpNAcb1-4[LFucpa1-6]DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/4,6,5/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1b_1-5][a1122h-1a_1-5][a1221m-1a_1-5]/1-1-2-3-1-4/a4-b1_a6-f1_b4-c1_c6-d1_d2-e1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-Manp]{[(6+1)][a-D-Manp]{[(2+1)][b-D-GlcpNAc]{}}}}[(6+1)][a-L-Fucp]{}}}LINUCSPDB-CARE
#9: Polysaccharide alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 367.349 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
LFucpa1-6DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,2,1/[a2122h-1b_1-5_2*NCC/3=O][a1221m-1a_1-5]/1-2/a6-b1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(6+1)][a-L-Fucp]{}}}LINUCSPDB-CARE
#10: Sugar ChemComp-NAG / 2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 3
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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Experimental details

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Experiment

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

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Sample preparation

CrystalDensity Matthews: 4.95 Å3/Da / Density % sol: 75.15 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 6.5
Details: Crystals were produced by vapour diffusion using 1 microlitre of the complex (2.6 mg/ml) in 10 mM HEPES (pH 7.5), 0.02% sodium azide and 10% D-trehalose solution and 1 microlitres of well ...Details: Crystals were produced by vapour diffusion using 1 microlitre of the complex (2.6 mg/ml) in 10 mM HEPES (pH 7.5), 0.02% sodium azide and 10% D-trehalose solution and 1 microlitres of well solution containing 10% PEG 8000, 0.1 M MES (pH 6.5) and 0.1 M MgAc2.

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: Photon Factory / Beamline: BL-5A / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Jun 22, 2006
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 3.3→35 Å / Num. obs: 57953 / % possible obs: 97.9 % / Redundancy: 7 % / Biso Wilson estimate: 90.48 Å2 / Net I/σ(I): 11.39
Reflection shellResolution: 3.3→3.4 Å / Redundancy: 3.6 % / Mean I/σ(I) obs: 0.78 / % possible all: 86.6

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Processing

Software
NameVersionClassification
BUSTER2.10.2refinement
XDSdata reduction
XSCALEdata scaling
BUSTERphasing
RefinementResolution: 3.3→34.46 Å / Cor.coef. Fo:Fc: 0.9258 / Cor.coef. Fo:Fc free: 0.9127 / SU R Cruickshank DPI: 0.978 / Cross valid method: THROUGHOUT / σ(F): 0 / SU R Blow DPI: 0.854 / SU Rfree Blow DPI: 0.359 / SU Rfree Cruickshank DPI: 0.37
RfactorNum. reflection% reflectionSelection details
Rfree0.2368 2911 5.03 %RANDOM
Rwork0.2054 ---
obs0.207 57926 98.01 %-
Displacement parametersBiso mean: 134.12 Å2
Baniso -1Baniso -2Baniso -3
1--13.5969 Å20 Å20 Å2
2--16.8154 Å20 Å2
3----3.2185 Å2
Refine analyzeLuzzati coordinate error obs: 0.912 Å
Refinement stepCycle: LAST / Resolution: 3.3→34.46 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms12601 0 317 0 12918
Refine LS restraints
Refine-IDTypeDev idealNumberRestraint functionWeight
X-RAY DIFFRACTIONt_bond_d0.0113273HARMONIC2
X-RAY DIFFRACTIONt_angle_deg1.3318079HARMONIC2
X-RAY DIFFRACTIONt_dihedral_angle_d4561SINUSOIDAL20
X-RAY DIFFRACTIONt_incorr_chiral_ct
X-RAY DIFFRACTIONt_pseud_angle
X-RAY DIFFRACTIONt_trig_c_planes296HARMONIC2
X-RAY DIFFRACTIONt_gen_planes1888HARMONIC5
X-RAY DIFFRACTIONt_it13273HARMONIC5
X-RAY DIFFRACTIONt_nbd
X-RAY DIFFRACTIONt_omega_torsion3.8
X-RAY DIFFRACTIONt_other_torsion10.22
X-RAY DIFFRACTIONt_improper_torsion
X-RAY DIFFRACTIONt_chiral_improper_torsion1804SEMIHARMONIC5
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_contact14752SEMIHARMONIC4
LS refinement shellResolution: 3.3→3.39 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.2253 187 5.08 %
Rwork0.2317 3492 -
all0.2314 3679 -
obs--98.01 %
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)
12.3673-0.36530.28082.51280.92644.4298-0.0918-0.2473-0.17980.30170.2361-0.126-0.86170.0831-0.14430.5568-0.2862-0.1189-0.01430.0293-0.435839.0482120.17438.395
22.57262.2125-0.09755.3161-1.03194.2521-0.1527-0.3018-0.13090.65630.21630.0679-0.3692-0.1664-0.06350.4308-0.3040.05960.06940.0531-0.341531.7307110.87615.1132
35.81860.50610.29644.94120.60058.2918-0.38090.7786-0.1162-0.0643-0.0723-0.4277-0.6040.89280.4532-0.3092-0.10840.11710.25540.0186-0.15589.740775.488434.4809
44.6001-1.94010.88852.3341-0.18046.50670.3116-0.4383-0.4478-0.1637-0.1606-0.552-0.1129-0.2055-0.1511-0.34510.1209-0.0444-0.1231-0.0645-0.0409-22.336473.634442.0641
50.1532-1.86620.39098.22550.29012.62910.28740.40110.1506-0.9266-0.3907-0.6432-0.17740.03240.10330.45430.29110.0039-0.2286-0.0276-0.3066-38.2847122.63234.6693
65.1623-4.2455-3.543401.37011.00480.00440.2138-0.09580.109-0.1712-0.2463-0.12020.13640.16680.23080.26490.18880.231-0.1165-0.3447-24.383109.83952.9279
75.0274-0.8554-0.23357.43230.76991.99060.20030.1802-0.3207-0.6632-0.3563-0.05480.26290.37610.15610.58270.265-0.2514-0.25260.0218-0.4138-49.3398159.98836.749
81.71410.5916-1.58933.6610.12155.21150.3917-0.2938-0.23230.3628-0.3645-0.5726-0.15630.1441-0.0272-0.0282-0.22650.0297-0.03420.0214-0.079243.0115116.431-9.7451
91.9931-1.80930.16476.9263-1.89995.43080.46930.08090.39320.5535-0.13990.2656-0.7851-0.8693-0.3294-0.0306-0.13190.2392-0.0017-0.0363-0.166224.4946126.699-6.9001
103.43641.6755-0.96945.1925-1.3142.72760.1946-0.24540.12210.0467-0.08050.4966-0.68010.3843-0.11410.323-0.11380.304-0.09080.0089-0.272649.5995139.179-29.0461
116.1173-0.636-4.61021.4727-0.38215.11050.35510.57240.1421-0.24460.080.5383-0.1018-0.571-0.43510.37770.04710.2276-0.2810.0887-0.100437.8926143.646-39.5123
123.04770.6931-0.79384.46430.98261.6356-0.0375-0.82440.24390.2951-0.53291.0615-0.6162-0.89640.5704-0.41660.3040.14170.5208-0.2674-0.0826-49.727777.080339.3958
1310.35483.56612.1120.76345.11213.7571-0.0750.2787-0.27510.27180.06840.15070.063-0.35620.0066-0.6080.28440.04950.608-0.24170.5805-74.685859.738224.9776
145.00961.39362.54136.02514.17386.76640.01670.4848-0.1526-0.5792-0.14570.3425-0.5303-0.55310.129-0.31060.18580.13430.236-0.0694-0.1355-38.163666.173724.0044
1511.70.22082.91070.9430.16149.4792-0.11560.7288-0.0349-0.662-0.09440.4477-0.0845-0.63170.21-0.6080.304-0.17410.608-0.27220.0653-67.090258.88839.9081
160.0105-0.1581-0.108800.40450.2055-0.0008-0.00150.01150.0028-0.01010.00340.0050.0130.0109-0.0872-0.1831-0.03150.1682-0.21020.049748.840798.316345.4003
170-0.46050.43530.1488-0.02380.45570.0069-0.0438-0.00810.0028-0.0507-0.0120.01350.01040.04380.1675-0.05790.0750.1433-0.0445-0.138156.1411104.11124.7759
1802.20280.27240.0683-2.21970.1148-0.0050.0279-0.05890.0456-0.01450.0071-0.1061-0.02890.01950.3317-0.09710.0875-0.06580.1656-0.165425.1793124.52222.7587
190.0331-0.19610.1330.07050.214100.0049-0.0213-0.00730.0116-0.039-0.01540.0420.02110.03410.1061-0.1002-0.0484-0.0594-0.13070.011947.2529128.54324.9909
200.176-0.2187-0.23130.1712-0.53570.1776-0.0030.014-0.0177-0.05580.0324-0.01970.04740.0515-0.02940.0977-0.20030.05480.00390.19170.023543.7815103.73310.161
210.1375-0.1776-0.71990.0595-1.113200.0082-0.0008-0.00830.07290.0075-0.02360.07550.0454-0.0157-0.33140.04140.30290.1715-0.07470.187727.195656.421832.2473
220.1007-0.19180.10570.1958-0.05220.39350.0031-0.0019-0.01040.0097-0.01160.01410.022-0.02140.00850.0339-0.186-0.0730.07340.09480.03367.887470.944516.8348
230.1669-0.2181-0.40850-0.04320.07230.00530.0046-0.01960.0198-0.0018-0.0073-0.0024-0.0215-0.0035-0.06410.18220.17450.21790.00030.0315-10.361990.875628.3903
2400.0573-1.34910-0.31130.34470.00980.0009-0.02650.0161-0.0114-0.0005-0.03860.03930.00160.1794-0.01170.2707-0.04390.21430.0562-28.5665126.56921.2713
250.08250.03590.550200.60850.40810.0016-0.01560.0063-0.0342-0.0266-0.0118-0.0215-0.02190.02490.03660.1072-0.0047-0.05370.11280.1979-44.408173.28226.2346
260.69571.8179-1.60831.73381.07981.3618-0.0029-0.0135-0.00070.03070.05810.05690.0237-0.0622-0.0552-0.1928-0.07030.13720.1561-0.20750.182730.682757.288329.1719
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1{ E|1 - E|162 E|168 - E|172 E|177 - E|191 }
2X-RAY DIFFRACTION2{ E|192 - E|267 E|274 - E|311 }
3X-RAY DIFFRACTION3{ E|312 - E|464 }
4X-RAY DIFFRACTION4{ E|465 - E|515 E|531 - E|594 }
5X-RAY DIFFRACTION5{ E|595 - E|656 E|754 - E|817 }
6X-RAY DIFFRACTION6{ E|694 - E|710 }
7X-RAY DIFFRACTION7{ E|818 - E|910 }
8X-RAY DIFFRACTION8{ A|1 - A|112 }
9X-RAY DIFFRACTION9{ B|1 - B|109 }
10X-RAY DIFFRACTION10{ A|113 - A|133 A|139 - A|219 }
11X-RAY DIFFRACTION11{ B|110 - B|218 }
12X-RAY DIFFRACTION12{ C|1 - C|84 C|89 - C|109 }
13X-RAY DIFFRACTION13{ C|110 - C|126 C|135 - C|183 C|194 - C|209 }
14X-RAY DIFFRACTION14{ D|1 - D|106 }
15X-RAY DIFFRACTION15{ D|107 - D|147 D|159 - D|179 D|196 - D|209 }
16X-RAY DIFFRACTION16{ E|1001 }
17X-RAY DIFFRACTION17{ E|1002 - E|1003 E|1004 }
18X-RAY DIFFRACTION18{ E|1005 - E|1007 }
19X-RAY DIFFRACTION19{ E|1008 }
20X-RAY DIFFRACTION20{ E|1009 - E|1010 E|1011 }
21X-RAY DIFFRACTION21{ E|1012 - E|1014 }
22X-RAY DIFFRACTION22{ E|1018 E|1019 }
23X-RAY DIFFRACTION23{ E|1020 }
24X-RAY DIFFRACTION24{ E|1021 - E|1022 E|1023 }
25X-RAY DIFFRACTION25{ E|1024 E|1025 }
26X-RAY DIFFRACTION26{ E|1015 - E|1016 E|1017 }

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