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- PDB-4ph9: The structure of Ibuprofen bound to cyclooxygenase-2 -

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Basic information

Entry
Database: PDB / ID: 4ph9
TitleThe structure of Ibuprofen bound to cyclooxygenase-2
ComponentsProstaglandin G/H synthase 2Cyclooxygenase
KeywordsOXIDOREDUCTASE / membrane protein / cyclooxygenase / COX / COX-2 / Ibuprofen / monotopic / prostaglandin / NSAID
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 / Synthesis of Prostaglandins (PG) and Thromboxanes (TX) / hair cycle / 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 / Synthesis of Prostaglandins (PG) and Thromboxanes (TX) / hair cycle / Nicotinamide salvaging / 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 / oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen / response to fructose / positive regulation of smooth muscle contraction / response to fatty acid / cyclooxygenase pathway / positive regulation of fever generation / response to vitamin D / prostaglandin secretion / cellular response to fluid shear stress / nuclear outer membrane / response to angiotensin / response to manganese ion / prostaglandin biosynthetic process / nuclear inner membrane / cellular response to ATP / negative regulation of smooth muscle contraction / maintenance of blood-brain barrier / positive regulation of cell migration involved in sprouting angiogenesis / 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 / positive regulation of vasoconstriction / response to glucocorticoid / keratinocyte differentiation / embryo implantation / positive regulation of brown fat cell differentiation / positive regulation of synaptic transmission, glutamatergic / learning / response to cytokine / caveola / peroxidase activity / 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 / cellular response to mechanical stimulus / positive regulation of nitric oxide biosynthetic process / response to estradiol / cellular response to heat / positive regulation of peptidyl-serine phosphorylation / regulation of cell population proliferation / cellular response to hypoxia / angiogenesis / response to oxidative stress / response to lipopolysaccharide / neuron projection / response to xenobiotic stimulus / positive regulation of apoptotic process / negative regulation of cell population proliferation / positive regulation of cell population proliferation / heme binding / endoplasmic reticulum membrane / negative regulation of apoptotic process / enzyme binding / endoplasmic reticulum / 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
ACRYLIC ACID / PROTOPORPHYRIN IX CONTAINING FE / IBUPROFEN / Prostaglandin G/H synthase 2
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 1.81 Å
AuthorsOrlando, B.J. / Lucido, M.J. / Malkowski, M.G.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)R01 GM077176 United States
CitationJournal: J.Struct.Biol. / Year: 2015
Title: The structure of ibuprofen bound to cyclooxygenase-2.
Authors: Orlando, B.J. / Lucido, M.J. / Malkowski, M.G.
History
DepositionMay 5, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 26, 2014Provider: repository / Type: Initial release
Revision 1.1Dec 17, 2014Group: Database references
Revision 1.2Jan 7, 2015Group: Database references
Revision 1.3Feb 25, 2015Group: Derived calculations
Revision 2.0Sep 6, 2017Group: Atomic model / Author supporting evidence ...Atomic model / Author supporting evidence / Database references / Derived calculations / Other / Source and taxonomy / Structure summary
Category: atom_site / citation ...atom_site / citation / entity / entity_src_gen / pdbx_audit_support / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_assembly_gen / pdbx_struct_conn_angle / pdbx_struct_oper_list / struct_conn / struct_site_gen
Item: _atom_site.label_asym_id / _atom_site.label_entity_id ..._atom_site.label_asym_id / _atom_site.label_entity_id / _citation.journal_id_CSD / _entity_src_gen.pdbx_alt_source_flag / _pdbx_audit_support.funding_organization / _pdbx_database_status.pdb_format_compatible / _pdbx_struct_assembly.oligomeric_details / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_oper_list.symmetry_operation / _struct_conn.ptnr1_label_asym_id / _struct_conn.ptnr2_label_asym_id / _struct_site_gen.label_asym_id
Revision 2.1Nov 22, 2017Group: Refinement description / Category: software
Revision 2.2Dec 25, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 3.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Refinement description / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / diffrn_radiation_wavelength / 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 / refine_hist / 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.mon_nstd_flag / _chem_comp.name / _chem_comp.type / _pdbx_struct_assembly_gen.asym_id_list / _pdbx_struct_conn_angle.ptnr1_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _refine_hist.number_atoms_total / _refine_hist.pdbx_number_atoms_nucleic_acid / _refine_hist.pdbx_number_atoms_protein / _struct_conn.conn_type_id / _struct_conn.id / _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 3.1Sep 27, 2023Group: Data collection / Database references ...Data collection / Database references / Refinement description / Structure summary
Category: chem_comp / chem_comp_atom ...chem_comp / chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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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
hetero molecules


Theoretical massNumber of molelcules
Total (without water)132,63832
Polymers126,9212
Non-polymers5,71730
Water20,3031127
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area16590 Å2
ΔGint47 kcal/mol
Surface area40950 Å2
MethodPISA
Unit cell
Length a, b, c (Å)120.941, 132.228, 180.462
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number23
Space group name H-MI222

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Components

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Protein , 1 types, 2 molecules AB

#1: Protein Prostaglandin G/H synthase 2 / Cyclooxygenase / 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 / PGHS-2 / Prostaglandin-endoperoxide synthase 2 / TIS10 protein


Mass: 63460.406 Da / Num. of mol.: 2 / Fragment: UNP residues 20-568
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Ptgs2, Cox-2, Cox2, Pghs-b, Tis10 / Production host: Spodoptera frugiperda (fall armyworm)
References: UniProt: Q05769, prostaglandin-endoperoxide synthase

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Sugars , 4 types, 9 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.: 2 / 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
#3: Polysaccharide alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta- ...alpha-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: obtained synthetically
DescriptorTypeProgram
DManpa1-4DGlcpNAcb1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,3,2/[a2122h-1b_1-5_2*NCC/3=O][a1122h-1a_1-5]/1-1-2/a4-b1_b4-c1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][b-D-GlcpNAc]{[(4+1)][a-D-Manp]{}}}}LINUCSPDB-CARE
#6: Sugar ChemComp-BOG / octyl beta-D-glucopyranoside / Beta-Octylglucoside / octyl beta-D-glucoside / octyl D-glucoside / octyl glucoside / Octyl glucoside


Type: D-saccharide / Mass: 292.369 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C14H28O6 / Comment: detergent*YM
IdentifierTypeProgram
b-octylglucosideIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
#7: 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 / N-Acetylglucosamine


Type: D-saccharide, beta linking / Mass: 221.208 Da / Num. of mol.: 3 / 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 , 5 types, 1148 molecules

#4: Chemical ChemComp-IBP / IBUPROFEN / 2-(4-ISOBUTYLPHENYL)PROPIONIC ACID / Dexibuprofen


Mass: 206.281 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C13H18O2 / Comment: antiinflammatory, medication*YM
#5: Chemical ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME / Heme B


Mass: 616.487 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C34H32FeN4O4
#8: Chemical
ChemComp-AKR / ACRYLIC ACID / Acrylic acid


Mass: 72.063 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C3H4O2
#9: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL / Ethylene glycol


Mass: 62.068 Da / Num. of mol.: 13 / Source method: isolated from a natural source / Formula: C2H6O2
#10: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 1127 / 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: 55.28 % / Description: rectangular
Crystal growTemperature: 296 K / Method: vapor diffusion, sitting drop / pH: 7.5
Details: 23-34% PAA-5100, 100mM HEPES (pH 7.5), 20mM MgCl2, 0.6% BoG

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: CHESS / Beamline: A1 / Wavelength: 0.9759 Å
DetectorType: ADSC QUANTUM 210 / Detector: CCD / Date: Sep 12, 2012
RadiationMonochromator: Horizontal focusing 5.05iN asymmetric cut Si(111)
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9759 Å / Relative weight: 1
ReflectionResolution: 1.81→40 Å / Num. all: 128926 / Num. obs: 128926 / % possible obs: 98.43 % / Observed criterion σ(I): -3 / Redundancy: 4.7 % / Biso Wilson estimate: 24.49 Å2 / Rmerge(I) obs: 0.056 / Χ2: 1.044 / Net I/av σ(I): 22.395 / Net I/σ(I): 13.6 / Num. measured all: 605910
Reflection shell

Diffraction-ID: 1 / Rejects: 0

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. unique allΧ2% possible all
1.81-1.8752.490.40372.4958351.08990.8
1.84-1.872.70.38460201.09792.8
1.87-1.9130.33161331.09294.8
1.91-1.953.50.25562681.09296.4
1.95-1.994.10.2264121.07698.8
1.99-2.044.40.18564761.04899.9
2.04-2.094.70.16665211.091100
2.09-2.155.20.14464721.087100
2.15-2.215.20.1265051.065100
2.21-2.285.20.10665351.061100
2.28-2.365.30.09565151.09799.9
2.36-2.465.30.08265291.04999.9
2.46-2.575.30.07465231.02999.9
2.57-2.75.40.0676547199.9
2.7-2.875.40.05965211.0499.9
2.87-3.095.40.05365671.00299.9
3.09-3.415.40.04965531.09399.9
3.41-3.950.03565950.95499.6
3.9-4.915.30.04366440.96599.7
4.91-405.20.04467600.9898.5

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Phasing

PhasingMethod: molecular replacement
Phasing MRModel details: Phaser MODE: MR_AUTO
Highest resolutionLowest resolution
Rotation6.79 Å38.56 Å
Translation6.79 Å38.56 Å

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Processing

Software
NameVersionClassification
PHENIX(PHENIX.REFINE: 1.8.4_1496)refinement
HKL-2000v704udata collection
HKL-2000v704udata reduction
PHASER2.5.6phasing
PDB_EXTRACT3.14data extraction
Coot0.7.2model building
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 3HS5

3hs5


Resolution: 1.81→35.55 Å / SU ML: 0.17 / Cross valid method: FREE R-VALUE / Phase error: 22.47
RfactorNum. reflection% reflectionSelection details
Rfree0.197 6401 4.99 %Random selection
Rwork0.16 ---
obs0.162 128316 98 %-
Solvent computationSolvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 29.97 Å2
Refine analyzeLuzzati coordinate error obs: 0.188 Å
Refinement stepCycle: final / Resolution: 1.81→35.55 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8944 0 72 1128 10144
Biso mean--37.6 39.34 -
Num. residues----1118
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0139687
X-RAY DIFFRACTIONf_angle_d1.3113131
X-RAY DIFFRACTIONf_dihedral_angle_d14.9293656
X-RAY DIFFRACTIONf_chiral_restr0.0611378
X-RAY DIFFRACTIONf_plane_restr0.0071676
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
1.81-1.83110.26422020.23663565X-RAY DIFFRACTION88
1.8311-1.85270.26481700.22853800X-RAY DIFFRACTION92
1.8527-1.87530.29451750.22073845X-RAY DIFFRACTION93
1.8753-1.8990.24171800.21023923X-RAY DIFFRACTION95
1.899-1.9240.26141570.20223950X-RAY DIFFRACTION95
1.924-1.95030.25522260.19363970X-RAY DIFFRACTION96
1.9503-1.97820.23062180.18854030X-RAY DIFFRACTION98
1.9782-2.00770.24142110.17924087X-RAY DIFFRACTION99
2.0077-2.03910.22662120.17994107X-RAY DIFFRACTION100
2.0391-2.07250.21572420.17864082X-RAY DIFFRACTION100
2.0725-2.10830.19952160.1774101X-RAY DIFFRACTION99
2.1083-2.14660.22712050.17264098X-RAY DIFFRACTION100
2.1466-2.18790.21952250.17294122X-RAY DIFFRACTION99
2.1879-2.23250.24672340.17114076X-RAY DIFFRACTION99
2.2325-2.28110.21982270.16794075X-RAY DIFFRACTION99
2.2811-2.33410.22282000.16624085X-RAY DIFFRACTION99
2.3341-2.39250.20582040.16354127X-RAY DIFFRACTION99
2.3925-2.45710.21632330.16634074X-RAY DIFFRACTION99
2.4571-2.52940.21062250.16244080X-RAY DIFFRACTION99
2.5294-2.6110.22012160.17244100X-RAY DIFFRACTION99
2.611-2.70430.20192510.16834109X-RAY DIFFRACTION99
2.7043-2.81260.19442430.15924061X-RAY DIFFRACTION99
2.8126-2.94050.21892310.16514118X-RAY DIFFRACTION99
2.9405-3.09550.22622240.16854129X-RAY DIFFRACTION99
3.0955-3.28930.19452230.1594152X-RAY DIFFRACTION100
3.2893-3.5430.18152400.14864121X-RAY DIFFRACTION99
3.543-3.89920.16392350.13594149X-RAY DIFFRACTION99
3.8992-4.46250.16322190.12884188X-RAY DIFFRACTION100
4.4625-5.61860.15931940.13294258X-RAY DIFFRACTION100
5.6186-35.56040.1541630.16314333X-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)
10.0065-0.01610.05430.0611-0.13670.47990.06650.1232-0.1043-0.3017-0.02640.06480.52270.0322-0.01810.4990.0122-0.04880.2281-0.02910.303927.67070.850732.201
20.17550.0645-0.06660.08280.07610.19450.05820.0412-0.2399-0.0238-0.00690.15860.2591-0.1278-0.01030.2475-0.0659-0.0630.271-0.01650.31885.024617.662827.39
30.16170.0716-0.00540.1280.03050.06980.06640.1187-0.0124-0.1344-0.0818-0.02170.18850.1159-0.00620.25090.08840.01180.22090.00960.17436.121819.631125.511
40.1046-0.1312-0.00510.1848-0.03840.07980.05470.13680.0134-0.1141-0.05150.01550.04940.047500.20480.0167-0.00130.23360.02230.210123.930634.481226.5913
50.4015-0.2283-0.07190.6159-0.09130.81090.05050.10420.037-0.08590.00610.02620.0435-0.0430.00050.13150.0096-0.00620.16490.02530.159518.885736.180227.4132
60.0703-0.02590.02290.0119-0.0410.4456-0.0268-0.1337-0.07330.09990.10420.1676-0.1005-0.3621-0.00520.2040.02190.04620.34250.06360.3313-0.388532.464660.9339
70.0875-0.0239-0.03890.07180.05540.0629-0.0196-0.0216-0.11160.03430.01250.2030.0875-0.17-0.00760.2327-0.04060.03090.23920.0380.335212.46716.375166.175
80.3323-0.12990.03340.2427-0.08680.1809-0.0545-0.09740.03050.09070.0645-0.0055-0.0812-0.024800.19960.02720.00850.19230.00180.188124.380231.81667.6662
90.4799-0.2147-0.07440.3949-0.15620.38630.0378-0.04740.0237-0.0399-0.0263-0.0670.09840.095300.17390.01620.0080.17780.00650.202842.01515.549658.4735
100.5202-0.2418-0.02790.4881-0.01010.5723-0.0418-0.152-0.02920.07760.07930.02640.0243-0.037500.18250.0130.01540.190.01750.175627.09420.284571.762
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1(CHAIN A AND RESID 33:83)
2X-RAY DIFFRACTION2(CHAIN A AND RESID 84:128)
3X-RAY DIFFRACTION3(CHAIN A AND RESID 129:186)
4X-RAY DIFFRACTION4(CHAIN A AND RESID 187:229)
5X-RAY DIFFRACTION5(CHAIN A AND RESID 230:582)
6X-RAY DIFFRACTION6(CHAIN B AND RESID 33:83)
7X-RAY DIFFRACTION7(CHAIN B AND RESID 84:125)
8X-RAY DIFFRACTION8(CHAIN B AND RESID 126:228)
9X-RAY DIFFRACTION9(CHAIN B AND RESID 229:367)
10X-RAY DIFFRACTION10(CHAIN B AND RESID 368:582)

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