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- PDB-4otj: The complex of murine cyclooxygenase-2 with a conjugate of indome... -

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Basic information

Entry
Database: PDB / ID: 4otj
TitleThe complex of murine cyclooxygenase-2 with a conjugate of indomefathin and podophyllotoxin, N-{(succinylpodophyllotoxinyl)but-4-yl}-2-{1-(4-chlorobenzoyl)-5-methoxy-2-methyl-1H-indol-3-yl}acetamide
ComponentsProstaglandin G/H synthase 2
KeywordsOxidoreductase/Oxidoreductase inhibitor / OXIDOREDUCTASE / NSAIDs / GLYCOSYLATION / Membrane / Oxidoreductase-Oxidoreductase inhibitor complex
Function / homology
Function and homology information


Biosynthesis of DHA-derived SPMs / Biosynthesis of EPA-derived SPMs / Biosynthesis of DPAn-3 SPMs / Biosynthesis of electrophilic ω-3 PUFA oxo-derivatives / Synthesis of 15-eicosatetraenoic acid derivatives / cellular response to non-ionic osmotic stress / positive regulation of platelet-derived growth factor production / hair cycle / cellular response to homocysteine / Nicotinamide salvaging ...Biosynthesis of DHA-derived SPMs / Biosynthesis of EPA-derived SPMs / Biosynthesis of DPAn-3 SPMs / Biosynthesis of electrophilic ω-3 PUFA oxo-derivatives / Synthesis of 15-eicosatetraenoic acid derivatives / cellular response to non-ionic osmotic stress / positive regulation of platelet-derived growth factor production / hair cycle / cellular response to homocysteine / Nicotinamide salvaging / Synthesis of Prostaglandins (PG) and Thromboxanes (TX) / positive regulation of fibroblast growth factor production / prostaglandin-endoperoxide synthase / prostaglandin-endoperoxide synthase activity / negative regulation of synaptic transmission, dopaminergic / cellular response to lead ion / response to nematode / positive regulation of transforming growth factor beta production / negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress / positive regulation of prostaglandin biosynthetic process / regulation of neuroinflammatory response / positive regulation of synaptic plasticity / positive regulation of smooth muscle contraction / oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen / cyclooxygenase pathway / response to fatty acid / response to fructose / positive regulation of fever generation / prostaglandin secretion / response to vitamin D / cellular response to fluid shear stress / nuclear outer membrane / response to angiotensin / response to manganese ion / prostaglandin biosynthetic process / nuclear inner membrane / negative regulation of smooth muscle contraction / cellular response to ATP / positive regulation of cell migration involved in sprouting angiogenesis / maintenance of blood-brain barrier / bone mineralization / negative regulation of calcium ion transport / decidualization / negative regulation of cell cycle / positive regulation of vascular endothelial growth factor production / response to tumor necrosis factor / brown fat cell differentiation / response to glucocorticoid / keratinocyte differentiation / positive regulation of vasoconstriction / positive regulation of brown fat cell differentiation / embryo implantation / positive regulation of synaptic transmission, glutamatergic / learning / response to cytokine / caveola / positive regulation of smooth muscle cell proliferation / negative regulation of cysteine-type endopeptidase activity involved in apoptotic process / memory / regulation of blood pressure / positive regulation of protein import into nucleus / peroxidase activity / cellular response to mechanical stimulus / positive regulation of nitric oxide biosynthetic process / positive regulation of peptidyl-serine phosphorylation / response to estradiol / cellular response to heat / regulation of cell population proliferation / cellular response to hypoxia / angiogenesis / response to oxidative stress / response to lipopolysaccharide / response to xenobiotic stimulus / neuron projection / positive regulation of apoptotic process / negative regulation of cell population proliferation / heme binding / positive regulation of cell population proliferation / endoplasmic reticulum membrane / negative regulation of apoptotic process / enzyme binding / protein homodimerization activity / protein-containing complex / metal ion binding / cytoplasm
Similarity search - Function
Myeloperoxidase, subunit C / Haem peroxidase domain superfamily, animal type / Haem peroxidase, animal-type / Haem peroxidase domain superfamily, animal type / Animal haem peroxidase / Animal heme peroxidase superfamily profile. / Laminin / Laminin / EGF-like domain / Haem peroxidase superfamily ...Myeloperoxidase, subunit C / Haem peroxidase domain superfamily, animal type / Haem peroxidase, animal-type / Haem peroxidase domain superfamily, animal type / Animal haem peroxidase / Animal heme peroxidase superfamily profile. / Laminin / Laminin / EGF-like domain / Haem peroxidase superfamily / EGF-like domain profile. / EGF-like domain / Ribbon / Orthogonal Bundle / Mainly Beta / Mainly Alpha
Similarity search - Domain/homology
PROTOPORPHYRIN IX CONTAINING FE / Chem-IXP / Prostaglandin G/H synthase 2
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.11 Å
AuthorsXu, S. / Uddin, M.J. / Banerjee, S. / Marnett, L.J.
CitationJournal: Acs Chem.Biol. / Year: 2016
Title: Antitumor Activity of Cytotoxic Cyclooxygenase-2 Inhibitors.
Authors: Uddin, M.J. / Crews, B.C. / Xu, S. / Ghebreselasie, K. / Daniel, C.K. / Kingsley, P.J. / Banerjee, S. / Marnett, L.J.
History
DepositionFeb 13, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 8, 2015Provider: repository / Type: Initial release
Revision 1.1Dec 7, 2016Group: Database references
Revision 1.2Feb 15, 2017Group: Database references
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / chem_comp / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / pdbx_struct_conn_angle / pdbx_unobs_or_zero_occ_atoms / 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.occupancy / _atom_site.type_symbol / _atom_site_anisotrop.U[1][1] / _atom_site_anisotrop.U[1][2] / _atom_site_anisotrop.U[1][3] / _atom_site_anisotrop.U[2][2] / _atom_site_anisotrop.U[2][3] / _atom_site_anisotrop.U[3][3] / _atom_site_anisotrop.id / _atom_site_anisotrop.pdbx_auth_asym_id / _atom_site_anisotrop.pdbx_auth_seq_id / _atom_site_anisotrop.pdbx_label_asym_id / _chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.type / _pdbx_entity_nonpoly.entity_id / _pdbx_entity_nonpoly.name / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_conn_angle.ptnr1_auth_asym_id / _pdbx_struct_conn_angle.ptnr1_auth_seq_id / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_seq_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_seq_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _pdbx_struct_conn_angle.value / _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
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Sep 20, 2023Group: Advisory / Data collection ...Advisory / 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 / pdbx_unobs_or_zero_occ_atoms
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Prostaglandin G/H synthase 2
B: Prostaglandin G/H synthase 2
C: Prostaglandin G/H synthase 2
D: Prostaglandin G/H synthase 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)279,54626
Polymers269,3314
Non-polymers10,21622
Water27,5811531
1
A: Prostaglandin G/H synthase 2
B: Prostaglandin G/H synthase 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)139,77313
Polymers134,6652
Non-polymers5,10811
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10510 Å2
ΔGint-26 kcal/mol
Surface area41990 Å2
MethodPISA
2
C: Prostaglandin G/H synthase 2
D: Prostaglandin G/H synthase 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)139,77313
Polymers134,6652
Non-polymers5,10811
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10480 Å2
ΔGint-24 kcal/mol
Surface area41890 Å2
MethodPISA
Unit cell
Length a, b, c (Å)180.712, 133.943, 122.223
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21212

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Components

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Protein , 1 types, 4 molecules ABCD

#1: Protein
Prostaglandin G/H synthase 2 / Cyclooxygenase-2 / COX-2 / Glucocorticoid-regulated inflammatory cyclooxygenase / Gripghs / ...Cyclooxygenase-2 / COX-2 / Glucocorticoid-regulated inflammatory cyclooxygenase / Gripghs / Macrophage activation-associated marker protein P71/73 / PES-2 / PHS II / Prostaglandin H2 synthase 2 / PGH synthase 2 / PGHS-2 / Prostaglandin-endoperoxide synthase 2 / TIS10 protein


Mass: 67332.711 Da / Num. of mol.: 4 / Fragment: PROSTAGLANDIN G/H SYNTHASE 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Ptgs2, Cox-2, Cox2, Pghs-b, Tis10 / Plasmid: pVL1393 / Production host: Spodoptera frugiperda (fall armyworm)
References: UniProt: Q05769, prostaglandin-endoperoxide synthase

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Sugars , 3 types, 14 molecules

#2: 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.: 4
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/1,2,1/[a2122h-1b_1-5_2*NCC/3=O]/1-1/a4-b1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{}}}LINUCSPDB-CARE
#3: 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.: 8
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
#6: Sugar ChemComp-BOG / octyl beta-D-glucopyranoside / Beta-Octylglucoside / octyl beta-D-glucoside / octyl D-glucoside / octyl glucoside


Type: D-saccharide / Mass: 292.369 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Formula: C14H28O6 / Comment: detergent*YM
IdentifierTypeProgram
b-octylglucosideIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0

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Non-polymers , 3 types, 1539 molecules

#4: Chemical
ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME


Mass: 616.487 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C34H32FeN4O4
#5: Chemical
ChemComp-IXP / (5S,5aS,8aS,9S)-8-oxo-9-(3,4,5-trimethoxyphenyl)-5,5a,6,8,8a,9-hexahydrofuro[3',4':6,7]naphtho[2,3-d][1,3]dioxol-5-yl 4-{[4-({[1-(4-chlorobenzoyl)-5-methoxy-2-methyl-1H-indol-3-yl]acetyl}amino)butyl]amino}-4-oxobutanoate


Mass: 924.387 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C49H50ClN3O13
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1531 / 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: 2.75 Å3/Da / Density % sol: 55.21 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 8
Details: mCOX-2 protein reconstituted with a 2-fold molar excess of heme in phosphtate buffer, pH 6.7, 100 mM NaCl, 1.2% (w/v) -OG, and 0.1% NaN3, and 10-fold molar excess of inhibitors from 25 mM ...Details: mCOX-2 protein reconstituted with a 2-fold molar excess of heme in phosphtate buffer, pH 6.7, 100 mM NaCl, 1.2% (w/v) -OG, and 0.1% NaN3, and 10-fold molar excess of inhibitors from 25 mM DMSO stocks were added to protein samples. Mixing 3 uL of the protein-inhibitor complex with 3 uL crystallization solution containing 50 mM EPPS, pH 8.0, 120 mM MgCl2, 22-26% PEG MME-550 against reservoir solutions comprised of 50 mM EPPS pH 8.0, 120 mM MgCl2, 22-26% PEG MME-550, VAPOR DIFFUSION, HANGING DROP, temperature 291K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.9792
DetectorType: PSI PILATUS 6M / Detector: PIXEL / Date: Jan 31, 2013
RadiationMonochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9792 Å / Relative weight: 1
ReflectionResolution: 2.11→50.11 Å / Num. obs: 170000 / % possible obs: 99.7 % / Observed criterion σ(I): 0 / Redundancy: 6.8 % / Biso Wilson estimate: 29.46 Å2 / Rmerge(I) obs: 0.078 / Rsym value: 0.035 / Net I/σ(I): 17.5
Reflection shellResolution: 2.11→2.22 Å / Redundancy: 6.9 % / Rmerge(I) obs: 0.561 / Mean I/σ(I) obs: 3.5 / Rsym value: 0.248 / % possible all: 99.5

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Processing

Software
NameVersionClassification
HKL-2000data collection
PHASESphasing
PHENIX(phenix.refine: 1.8.4_1496)refinement
XDSdata reduction
SCALEPACKdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 3NT1

3nt1


Resolution: 2.11→50.11 Å / SU ML: 0.2 / Isotropic thermal model: Isotropic / σ(F): 1.35 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.199 5131 3.02 %
Rwork0.177 --
obs0.177 169740 99.5 %
all-170113 -
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.11→50.11 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17878 0 700 1531 20109
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00719203
X-RAY DIFFRACTIONf_angle_d1.36326119
X-RAY DIFFRACTIONf_dihedral_angle_d13.6447093
X-RAY DIFFRACTIONf_chiral_restr0.0782751
X-RAY DIFFRACTIONf_plane_restr0.0083334
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.1093-2.13330.28671510.2315396X-RAY DIFFRACTION98
2.1333-2.15840.2711680.22815412X-RAY DIFFRACTION99
2.1584-2.18470.26761790.22025446X-RAY DIFFRACTION100
2.1847-2.21230.26191630.21325391X-RAY DIFFRACTION100
2.2123-2.24140.2411640.22115474X-RAY DIFFRACTION100
2.2414-2.27210.24591620.20935467X-RAY DIFFRACTION99
2.2721-2.30460.23021740.19965426X-RAY DIFFRACTION100
2.3046-2.3390.26911550.20215446X-RAY DIFFRACTION100
2.339-2.37560.23971420.1915485X-RAY DIFFRACTION100
2.3756-2.41450.23151740.18655461X-RAY DIFFRACTION100
2.4145-2.45610.21421770.18735430X-RAY DIFFRACTION100
2.4561-2.50080.22691790.18695475X-RAY DIFFRACTION100
2.5008-2.54890.19911730.18275431X-RAY DIFFRACTION99
2.5489-2.60090.22531600.18845477X-RAY DIFFRACTION100
2.6009-2.65750.20981730.18255483X-RAY DIFFRACTION100
2.6575-2.71930.22261760.17795457X-RAY DIFFRACTION100
2.7193-2.78730.20471770.18035506X-RAY DIFFRACTION100
2.7873-2.86260.21321540.18285437X-RAY DIFFRACTION100
2.8626-2.94690.22131890.18245495X-RAY DIFFRACTION100
2.9469-3.0420.22661710.1875487X-RAY DIFFRACTION100
3.042-3.15070.21681730.19015486X-RAY DIFFRACTION100
3.1507-3.27680.20171690.18055524X-RAY DIFFRACTION100
3.2768-3.42590.20361940.18585456X-RAY DIFFRACTION99
3.4259-3.60650.18741740.16875496X-RAY DIFFRACTION100
3.6065-3.83230.18581840.1585536X-RAY DIFFRACTION100
3.8323-4.12810.1541830.15055519X-RAY DIFFRACTION100
4.1281-4.54330.14561710.1415572X-RAY DIFFRACTION100
4.5433-5.20010.14981810.14325502X-RAY DIFFRACTION99
5.2001-6.54930.21121700.17955646X-RAY DIFFRACTION100
6.5493-50.12240.17151710.18015790X-RAY DIFFRACTION98
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)
11.2635-0.3842-0.21480.68150.110.0414-0.2266-0.0156-0.69270.36850.02490.36760.2288-0.13060.07330.5054-0.04290.17450.2874-0.03210.690137.18592.5372125.0995
21.02860.1722-0.14980.4403-0.18730.6301-0.1068-0.3468-0.52160.118-0.0333-0.14130.3596-0.1690.04910.55510.01910.07860.44860.15420.52735.207716.6504149.5376
31.52740.309-0.1221.2136-0.360.3457-0.00450.2423-0.2830.0008-0.20970.17790.1693-0.04680.16160.23470.00010.02210.1922-0.07270.256144.595319.5296117.2127
41.4238-0.2707-0.30050.7330.48231.0928-0.05020.006-0.08430.0342-0.04680.1269-0.0135-0.140.08510.22750.00660.01630.2115-0.00890.195333.042334.3258132.117
51.2271-0.2719-0.46110.08180.24491.1041-0.2597-0.7028-0.02560.27650.2281-0.13130.39780.41730.15950.45170.1667-0.0330.8140.0060.275769.697426.5811151.1889
60.7640.1570.24110.5529-0.31530.51540.0397-0.3311-0.33060.16810.0896-0.0770.38940.1993-0.16260.60820.21470.07580.57450.20540.545771.48282.6977136.1286
71.011-0.43-0.0880.454-0.090.35420.0008-0.4180.26140.09770.1067-0.1047-0.07230.2823-0.06420.26140.0035-0.00520.4367-0.10360.290371.859837.4824134.9792
81.2844-0.1176-0.19480.54860.33751.0053-0.0418-0.0107-0.09860.00060.0767-0.10920.06220.2976-0.0270.22890.04260.00430.2935-0.02160.230873.578420.962116.1317
91.28020.21120.18120.36760.10520.4730.0891-0.2856-0.12550.33910.0726-0.26370.17380.5148-0.1050.29720.0812-0.05820.5905-0.06890.313383.604624.7275134.9912
100.9283-0.08680.10530.59460.190.9762-0.0451-0.152-0.16150.18490.0502-0.00060.20390.2338-0.01890.32110.05960.04680.2801-0.00730.325667.345412.6672119.9984
110.9368-0.1950.37110.6217-0.36880.7758-0.1171-0.1130.51820.2827-0.0071-0.2653-0.23760.13010.00280.4307-0.0262-0.06930.2465-0.080.472759.8861.881870.2786
120.39590.07640.41370.2303-0.69092.88080.0154-0.13370.30350.14120.0146-0.027-0.36680.1119-0.05690.31580.00420.01680.2336-0.05550.352853.460750.428572.7751
130.7531-0.15440.1670.41-0.20930.46170.04690.0540.0165-0.0589-0.0563-0.0370.06460.08560.01310.2410.00560.00640.16970.01660.213960.612232.439663.8961
141.58150.053-0.3141.13460.10321.1368-0.0512-0.0057-0.2538-0.10310.0159-0.12790.19180.01970.07030.2770.0119-0.01240.16640.02740.254958.007217.672271.6539
151.0305-0.1366-0.06320.5326-0.27940.5042-0.0274-0.10310.08830.0399-0.0224-0.1119-0.02860.08690.04460.2309-0.0152-0.02170.1982-0.00460.207864.5337.044573.5251
160.9989-0.64390.32770.8663-0.49940.7722-0.1509-0.48070.06650.24650.23050.1105-0.3321-0.1838-0.04870.35340.05630.04240.4327-0.04730.257924.654944.733487.0369
170.2987-0.36290.02922.4467-0.81810.2583-0.0628-0.38070.14890.33750.13350.1725-0.2034-0.0657-0.01950.31790.0062-0.0010.2999-0.06430.316731.089647.401275.705
180.7086-0.26760.16430.16820.06030.3473-0.0042-0.2415-0.36070.0320.02540.08620.1469-0.1246-0.03660.2508-0.0349-0.01570.25680.08630.301920.865527.474373.0129
190.9931-0.09110.01880.305-0.19280.76660.01560.06270.0628-0.05650.00440.02510.0114-0.0716-0.01870.23080.0156-0.00290.1681-0.00040.209827.698647.460352.653
201.00240.12340.04950.5985-0.27190.66650.0085-0.08310.0443-0.00730.04350.0825-0.0145-0.2203-0.03410.19990.0220.00940.2209-0.00010.20616.020945.968862.3625
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(CHAIN A AND RESID 33:93 )
2X-RAY DIFFRACTION2(CHAIN A AND RESID 94:123 )
3X-RAY DIFFRACTION3(CHAIN A AND RESID 124:158 )
4X-RAY DIFFRACTION4(CHAIN A AND RESID 159:583 )
5X-RAY DIFFRACTION5(CHAIN B AND RESID 33:93 )
6X-RAY DIFFRACTION6(CHAIN B AND RESID 94:123 )
7X-RAY DIFFRACTION7(CHAIN B AND RESID 124:181 )
8X-RAY DIFFRACTION8(CHAIN B AND RESID 182:485 )
9X-RAY DIFFRACTION9(CHAIN B AND RESID 486:535 )
10X-RAY DIFFRACTION10(CHAIN B AND RESID 536:582 )
11X-RAY DIFFRACTION11(CHAIN C AND RESID 33:105 )
12X-RAY DIFFRACTION12(CHAIN C AND RESID 106:138 )
13X-RAY DIFFRACTION13(CHAIN C AND RESID 139:269 )
14X-RAY DIFFRACTION14(CHAIN C AND RESID 270:319 )
15X-RAY DIFFRACTION15(CHAIN C AND RESID 320:582 )
16X-RAY DIFFRACTION16(CHAIN D AND RESID 33:105 )
17X-RAY DIFFRACTION17(CHAIN D AND RESID 106:138 )
18X-RAY DIFFRACTION18(CHAIN D AND RESID 139:181 )
19X-RAY DIFFRACTION19(CHAIN D AND RESID 182:390 )
20X-RAY DIFFRACTION20(CHAIN D AND RESID 391:582 )

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