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- PDB-4rut: crystal structure of murine cyclooxygenase-2 with 13-methyl-arach... -

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Basic information

Entry
Database: PDB / ID: 4rut
Titlecrystal structure of murine cyclooxygenase-2 with 13-methyl-arachidonic Acid
ComponentsProstaglandin G/H synthase 2
KeywordsOXIDOREDUCTASE / PROTEIN-LIGAND COMPLEX / PROSTAGLANDIN-ENDOPEROXIDE SYNTHASE / FATTY ACID ANALOG / GLYCOSYLATION / MEMBRANE
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 / oxidoreductase activity, acting on single donors with incorporation of molecular oxygen / Synthesis of Prostaglandins (PG) and Thromboxanes (TX) / positive regulation of fibroblast growth factor production ...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 / oxidoreductase activity, acting on single donors with incorporation of molecular oxygen / 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 / positive regulation of transforming growth factor beta production / negative regulation of intrinsic apoptotic signaling pathway in response to osmotic stress / prostanoid biosynthetic process / regulation of neuroinflammatory response / cyclooxygenase pathway / cellular response to fluid shear stress / positive regulation of prostaglandin biosynthetic process / positive regulation of fever generation / response to selenium ion / oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen / positive regulation of smooth muscle contraction / prostaglandin secretion / positive regulation of synaptic plasticity / response to nematode / prostaglandin biosynthetic process / negative regulation of smooth muscle contraction / nuclear inner membrane / positive regulation of cell migration involved in sprouting angiogenesis / bone mineralization / decidualization / maintenance of blood-brain barrier / negative regulation of cell cycle / negative regulation of calcium ion transport / nuclear outer membrane / oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen / positive regulation of vascular endothelial growth factor production / keratinocyte differentiation / positive regulation of vasoconstriction / positive regulation of brown fat cell differentiation / embryo implantation / positive regulation of synaptic transmission, glutamatergic / response to cytokine / positive regulation of smooth muscle cell proliferation / brown fat cell differentiation / learning / peroxidase activity / positive regulation of protein import into nucleus / caveola / regulation of blood pressure / memory / positive regulation of nitric oxide biosynthetic process / regulation of cell population proliferation / angiogenesis / response to oxidative stress / response to lipopolysaccharide / cellular response to hypoxia / neuron projection / positive regulation of apoptotic process / endoplasmic reticulum lumen / negative regulation of cell population proliferation / heme binding / positive regulation of cell population proliferation / negative regulation of apoptotic process / endoplasmic reticulum membrane / enzyme binding / endoplasmic reticulum / protein homodimerization activity / protein-containing complex / metal ion binding / cytosol / 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 ...: / 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 CO / Chem-LM8 / Prostaglandin G/H synthase 2
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.16 Å
AuthorsXu, S. / Kudalkar, S.N. / Banerjee, S. / Makriyannis, A. / Nikas, S.P. / Marnett, L.J.
CitationJournal: J.Biol.Chem. / Year: 2015
Title: 13-methylarachidonic Acid is a positive allosteric modulator of endocannabinoid oxygenation by cyclooxygenase.
Authors: Kudalkar, S.N. / Nikas, S.P. / Kingsley, P.J. / Xu, S. / Galligan, J.J. / Rouzer, C.A. / Banerjee, S. / Ji, L. / Eno, M.R. / Makriyannis, A. / Marnett, L.J.
History
DepositionNov 21, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 11, 2015Provider: repository / Type: Initial release
Revision 1.1Apr 15, 2015Group: Database references
Revision 1.2Nov 20, 2019Group: Derived calculations / Category: pdbx_struct_conn_angle / struct_conn
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 / pdbx_struct_conn_angle / 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.pdbx_formal_charge / _atom_site.type_symbol / _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_label_asym_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_label_asym_id / _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 2.1Sep 20, 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
Revision 2.2Nov 20, 2024Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_entry_details / pdbx_modification_feature / pdbx_validate_chiral
Item: _chem_comp_atom.pdbx_aromatic_flag / _chem_comp_atom.pdbx_stereo_config / _chem_comp_bond.pdbx_aromatic_flag

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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)277,13526
Polymers269,3314
Non-polymers7,80422
Water20,5011138
1
A: Prostaglandin G/H synthase 2
B: Prostaglandin G/H synthase 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)138,56813
Polymers134,6652
Non-polymers3,90211
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10480 Å2
ΔGint-19 kcal/mol
Surface area42040 Å2
MethodPISA
2
C: Prostaglandin G/H synthase 2
D: Prostaglandin G/H synthase 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)138,56813
Polymers134,6652
Non-polymers3,90211
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10490 Å2
ΔGint-17 kcal/mol
Surface area41900 Å2
MethodPISA
Unit cell
Length a, b, c (Å)215.796, 121.539, 134.943
Angle α, β, γ (deg.)90.00, 123.60, 90.00
Int Tables number5
Space group name H-MC121

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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
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Ptgs2, Cox-2, Cox2, Pghs-b, Tis10 / Plasmid: PLV1393 / 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, 1146 molecules

#4: Chemical
ChemComp-COH / PROTOPORPHYRIN IX CONTAINING CO


Mass: 619.575 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C34H32CoN4O4
#5: Chemical
ChemComp-LM8 / (5Z,8Z,11Z,13S,14Z)-13-methylicosa-5,8,11,14-tetraenoic acid / (5Z,8Z,11Z,14Z)-13S-methyl-5,8,11,14-eicosatetraenoic acid


Mass: 318.493 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C21H34O2
#7: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 1138 / 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: 2.74 Å3/Da / Density % sol: 55.05 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 8
Details: 50 mM EPPS pH 8.0, 20~25% PEG MME 550, 80~120 mM MgCl2, 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: 0.97918 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Jul 24, 2014
RadiationMonochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97918 Å / Relative weight: 1
ReflectionResolution: 2.16→112.4 Å / Num. all: 152423 / Num. obs: 152390 / % possible obs: 98.12 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 5.7 % / Biso Wilson estimate: 39.46 Å2 / Rmerge(I) obs: 0.136 / Net I/σ(I): 10.12
Reflection shellResolution: 2.16→2.24 Å / Redundancy: 5.7 % / Rmerge(I) obs: 1.35 / Mean I/σ(I) obs: 1.48 / Num. unique all: 15303 / % possible all: 95.94

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Processing

Software
NameVersionClassification
HKL-2000data collection
PHASESphasing
PHENIX(phenix.refine: 1.9_1692)refinement
XDSdata reduction
XDSdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 3NT1 chain A

3nt1


Resolution: 2.16→112.393 Å / SU ML: 0.31 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 24.52 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2241 4542 2.98 %RANDOM
Rwork0.176 ---
all0.1782 152390 --
obs0.1775 152330 98.08 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.16→112.393 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17896 0 528 1138 19562
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.01318996
X-RAY DIFFRACTIONf_angle_d1.45325778
X-RAY DIFFRACTIONf_dihedral_angle_d13.6397066
X-RAY DIFFRACTIONf_chiral_restr0.0512738
X-RAY DIFFRACTIONf_plane_restr0.0063316
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.1596-2.18420.33571310.30024644X-RAY DIFFRACTION93
2.1842-2.20990.3121710.28784920X-RAY DIFFRACTION98
2.2099-2.23680.31241430.27914849X-RAY DIFFRACTION97
2.2368-2.26510.30341510.27254807X-RAY DIFFRACTION97
2.2651-2.2950.33781410.27634869X-RAY DIFFRACTION96
2.295-2.32640.35041480.2614816X-RAY DIFFRACTION97
2.3264-2.35960.30081580.23644933X-RAY DIFFRACTION99
2.3596-2.39490.27711580.21364959X-RAY DIFFRACTION99
2.3949-2.43230.26821500.21434946X-RAY DIFFRACTION99
2.4323-2.47220.24181380.20564966X-RAY DIFFRACTION99
2.4722-2.51480.26511670.20494944X-RAY DIFFRACTION99
2.5148-2.56050.25071490.20494967X-RAY DIFFRACTION99
2.5605-2.60980.25441560.20344940X-RAY DIFFRACTION99
2.6098-2.66310.26481500.20454957X-RAY DIFFRACTION99
2.6631-2.7210.27091540.18974944X-RAY DIFFRACTION98
2.721-2.78430.28041490.19324887X-RAY DIFFRACTION97
2.7843-2.85390.28221540.19614841X-RAY DIFFRACTION97
2.8539-2.93110.24781530.18975020X-RAY DIFFRACTION99
2.9311-3.01730.24461490.19324972X-RAY DIFFRACTION99
3.0173-3.11470.23621590.18884963X-RAY DIFFRACTION99
3.1147-3.22610.24251460.1844988X-RAY DIFFRACTION99
3.2261-3.35520.25781510.18824973X-RAY DIFFRACTION99
3.3552-3.50790.22141580.16974942X-RAY DIFFRACTION99
3.5079-3.69290.24011430.15814846X-RAY DIFFRACTION96
3.6929-3.92430.18871570.14664981X-RAY DIFFRACTION99
3.9243-4.22730.1921520.14214982X-RAY DIFFRACTION99
4.2273-4.65270.16081500.13314991X-RAY DIFFRACTION99
4.6527-5.3260.16081420.13084941X-RAY DIFFRACTION98
5.326-6.710.19971610.15894947X-RAY DIFFRACTION98
6.71-112.54540.17071530.16055053X-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)
11.5215-0.20210.81342.7526-2.20392.75470.0968-0.37270.08490.1260.17810.3714-0.2561-0.6759-0.29510.33380.05790.12780.58330.05230.4701-81.5015-26.557318.5293
24.0332-0.60951.87213.36510.86771.5298-0.2705-0.24890.81670.36780.34040.3608-0.4875-0.00490.04140.43120.1160.06540.482-0.00820.558-74.5376-1.90085.049
31.6156-0.06660.68721.5258-0.64091.44530.0772-0.1995-0.2014-0.10340.1120.27270.3109-0.3656-0.15550.339-0.089-0.00950.36230.09070.3327-72.8147-36.82514.1322
41.08760.46170.28211.645-0.37841.368-0.05140.13920.1264-0.38380.2040.3650.0549-0.1133-0.05530.3816-0.0672-0.09320.33360.05780.2816-69.9769-22.7318-12.8525
530.875-0.02752.35-0.66981.7588-0.1820.4203-0.1722-0.54070.0285-0.21720.14440.23530.15460.3664-0.01380.05930.31430.03540.2254-49.8956-20.359-15.9213
61.8239-0.01630.58670.9128-0.36211.1354-0.0370.03610.1824-0.04040.04390.1152-0.0568-0.05860.0080.3088-0.0067-0.01930.27890.05220.2895-60.7574-12.4959-1.2627
72.41561.2443-0.54824.0832.63682.776-0.19370.26640.0833-1.02570.1780.5230.2631-0.2257-0.00010.6989-0.1172-0.14190.460.09240.3574-65.9225-17.8378-28.2246
81.7740.62720.22851.6513-0.29031.50250.0174-0.00440.0403-0.23940.1630.50080.1762-0.4635-0.19060.296-0.0671-0.0840.43340.11570.4258-81.9853-26.4657-4.1428
91.67980.7160.57531.7-0.48161.8619-0.21980.18960.3088-0.20410.01320.0978-0.2964-0.02470.12320.3530.0041-0.03590.24950.01610.306-56.6161-5.0794-6.7422
100.44730.59510.12472.0482-2.06693.7796-0.17820.00850.18170.3979-0.12670.0835-0.71290.15160.2320.4662-0.0134-0.07110.2824-0.02570.4897-42.9556-3.638423.5828
113.2511.8221-3.1461.1125-1.96383.26120.1451-0.11410.55150.2614-0.11070.1896-0.7817-0.1052-0.22910.41130.0602-0.02620.3612-0.01680.4119-49.6766-15.164421.7904
121.2879-0.01620.77721.1775-0.22041.4981-0.20090.27380.2679-0.0002-0.0338-0.369-0.15870.52180.20970.3001-0.0529-0.00250.44070.10430.3695-29.1046-17.494212.3582
131.26490.13020.4121.1628-0.13650.95270.03710.0094-0.08460.0385-0.034-0.13510.17490.0914-0.02410.2710.03420.00750.21980.0210.224-42.6634-40.185421.9615
142.5492-0.13211.02232.4165-0.08121.29650.1094-0.031-0.16790.0762-0.0657-0.12730.1360.013-0.02590.318-0.00370.02210.27160.03120.2092-50.2937-44.957923.4192
151.41640.02650.38660.8846-0.49231.69840.0448-0.28810.16670.3146-0.0167-0.0938-0.1251-0.05770.05550.32350.0023-0.01180.2079-0.03920.2306-48.1997-22.995227.8278
162.69730.4878-0.00162.3515-0.10611.3409-0.0046-0.3021-0.3380.2568-0.1098-0.31310.21110.27650.05510.43910.0319-0.12310.42920.06870.426-32.595-46.6235.2233
171.4686-0.02110.1731.1933-0.37021.4389-0.0391-0.15320.2810.2944-0.1084-0.3276-0.20720.33660.18380.3441-0.0564-0.1070.36490.02490.4062-29.5169-17.844426.9718
181.8589-0.12190.33611.7433-0.57321.50220.0432-0.37630.03710.14270.02140.11670.1287-0.2242-0.0430.27850.0040.06160.2941-0.01010.1738-56.8891-35.962732.2294
192.8653-2.5176-0.04552.39490.29311.1671-0.4058-0.6844-0.26430.54380.26590.04720.0265-0.26450.06940.40730.04920.08190.63960.05430.3389-102.3698-33.409286.9815
201.4371-0.2781.51074.4759-1.71652.4029-0.085-0.1367-0.45630.22780.50620.83530.4169-0.5215-0.35830.5448-0.06960.06560.58670.20390.4651-91.8954-57.629376.9844
212.0651-0.9691.3290.7733-0.12751.764-0.1448-0.44030.16310.1020.10970.08530.0126-0.17950.06750.25690.04680.02160.3603-0.06640.2636-97.5496-24.928569.2772
221.2025-0.30.26821.34190.37291.16370.04930.00250.074-0.15660.0244-0.1743-0.0510.0999-0.08050.2105-0.0010.03850.22180.00060.2416-78.2499-37.953356.9759
231.9431-0.62960.74131.40750.13610.95460.0698-0.1709-0.21780.0830.04680.04260.19240.0044-0.09290.24370.02040.03140.31530.04620.2256-88.7835-45.407469.794
241.71320.1005-0.00711.62110.56651.54280.1276-0.14990.0192-0.02760.193-0.57340.04460.2094-0.21210.32440.00670.04170.4017-0.06630.4437-60.9404-41.759861.4762
251.68-0.24030.20731.50470.3640.8524-0.1073-0.56160.15040.36910.1384-0.14480.0453-0.0955-0.05690.34240.0523-0.02480.4595-0.05360.2523-80.8336-32.93782.3847
262.4007-0.41090.60871.53090.44440.84510.15250.0008-0.4545-0.03680.0047-0.00910.10410.0744-0.17550.29880.0146-0.03960.2230.01940.3506-83.9984-54.440657.1864
273.098-0.8729-0.53630.82650.19620.29570.0899-0.0413-0.7357-0.0439-0.05090.4460.1663-0.0236-0.01150.5021-0.0444-0.14420.39070.03720.6292-115.5223-52.268452.5787
281.3767-0.31240.38680.6496-0.16560.81190.1770.571-0.2982-0.5575-0.13490.42070.2080.0973-0.06520.49260.0741-0.17140.399-0.08850.4244-108.7424-42.043534.5299
291.0709-0.18030.30821.02170.08840.82290.05750.0871-0.0748-0.2907-0.06270.3912-0.0262-0.18340.01950.31420.0234-0.09180.3107-0.010.409-119.5491-26.354848.4005
301.8307-0.69260.51291.75620.02411.7187-0.0057-0.4415-0.0292-0.05660.09470.4728-0.0312-0.42420.00510.2145-0.00180.03050.40710.030.3988-122.028-23.456166.1546
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 33 through 92 )
2X-RAY DIFFRACTION2chain 'A' and (resid 93 through 123 )
3X-RAY DIFFRACTION3chain 'A' and (resid 124 through 181 )
4X-RAY DIFFRACTION4chain 'A' and (resid 182 through 218 )
5X-RAY DIFFRACTION5chain 'A' and (resid 219 through 319 )
6X-RAY DIFFRACTION6chain 'A' and (resid 320 through 390 )
7X-RAY DIFFRACTION7chain 'A' and (resid 391 through 428 )
8X-RAY DIFFRACTION8chain 'A' and (resid 429 through 535 )
9X-RAY DIFFRACTION9chain 'A' and (resid 536 through 583 )
10X-RAY DIFFRACTION10chain 'B' and (resid 33 through 105A)
11X-RAY DIFFRACTION11chain 'B' and (resid 106 through 138 )
12X-RAY DIFFRACTION12chain 'B' and (resid 139 through 181 )
13X-RAY DIFFRACTION13chain 'B' and (resid 182 through 269 )
14X-RAY DIFFRACTION14chain 'B' and (resid 270 through 346 )
15X-RAY DIFFRACTION15chain 'B' and (resid 347 through 390 )
16X-RAY DIFFRACTION16chain 'B' and (resid 391 through 428 )
17X-RAY DIFFRACTION17chain 'B' and (resid 429 through 535 )
18X-RAY DIFFRACTION18chain 'B' and (resid 536 through 583 )
19X-RAY DIFFRACTION19chain 'C' and (resid 33 through 94 )
20X-RAY DIFFRACTION20chain 'C' and (resid 95 through 123 )
21X-RAY DIFFRACTION21chain 'C' and (resid 124 through 158 )
22X-RAY DIFFRACTION22chain 'C' and (resid 159 through 346 )
23X-RAY DIFFRACTION23chain 'C' and (resid 347 through 390 )
24X-RAY DIFFRACTION24chain 'C' and (resid 391 through 428 )
25X-RAY DIFFRACTION25chain 'C' and (resid 429 through 535 )
26X-RAY DIFFRACTION26chain 'C' and (resid 536 through 583 )
27X-RAY DIFFRACTION27chain 'D' and (resid 33 through 138 )
28X-RAY DIFFRACTION28chain 'D' and (resid 139 through 181 )
29X-RAY DIFFRACTION29chain 'D' and (resid 182 through 536 )
30X-RAY DIFFRACTION30chain 'D' and (resid 537 through 583 )

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