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- PDB-4rry: Crystal Structure of Apo Murine H90W Cyclooxygenase-2 -

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Basic information

Entry
Database: PDB / ID: 4rry
TitleCrystal Structure of Apo Murine H90W Cyclooxygenase-2
ComponentsProstaglandin G/H synthase 2
KeywordsOXIDOREDUCTASE / prostaglandin-endoperoxide synthase / 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 / 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 / positive regulation of synaptic plasticity / regulation of neuroinflammatory response / response to fructose / cyclooxygenase pathway / positive regulation of smooth muscle contraction / oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen / response to fatty acid / positive regulation of fever generation / response to vitamin D / cellular response to fluid shear stress / prostaglandin secretion / nuclear outer membrane / response to angiotensin / nuclear inner membrane / response to manganese ion / negative regulation of smooth muscle contraction / prostaglandin biosynthetic process / positive regulation of cell migration involved in sprouting angiogenesis / cellular response to ATP / 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 / positive regulation of vasoconstriction / keratinocyte differentiation / positive regulation of brown fat cell differentiation / embryo implantation / positive regulation of synaptic transmission, glutamatergic / : / learning / response to cytokine / positive regulation of smooth muscle cell proliferation / peroxidase activity / caveola / memory / regulation of blood pressure / positive regulation of protein import into nucleus / cellular response to mechanical stimulus / positive regulation of nitric oxide biosynthetic process / positive regulation of peptidyl-serine phosphorylation / response to estradiol / regulation of cell population proliferation / cellular response to heat / cellular response to hypoxia / angiogenesis / response to oxidative stress / response to lipopolysaccharide / neuron projection / positive regulation of apoptotic process / response to xenobiotic stimulus / 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 ...: / 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
Prostaglandin G/H synthase 2
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.429 Å
AuthorsXu, S. / Blobaum, A.L. / Banerjee, S. / Marnett, L.J.
CitationJournal: J.Biol.Chem. / Year: 2015
Title: Action at a Distance: MUTATIONS OF PERIPHERAL RESIDUES TRANSFORM RAPID REVERSIBLE INHIBITORS TO SLOW, TIGHT BINDERS OF CYCLOOXYGENASE-2.
Authors: Blobaum, A.L. / Xu, S. / Rowlinson, S.W. / Duggan, K.C. / Banerjee, S. / Kudalkar, S.N. / Birmingham, W.R. / Ghebreselasie, K. / Marnett, L.J.
History
DepositionNov 6, 2014Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 8, 2015Provider: repository / Type: Initial release
Revision 1.1May 6, 2015Group: Database references
Revision 1.2Jun 3, 2015Group: Database references
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Database references / Derived calculations / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / entity / pdbx_branch_scheme / pdbx_chem_comp_identifier / pdbx_entity_branch / pdbx_entity_branch_descriptor / pdbx_entity_branch_link / pdbx_entity_branch_list / pdbx_entity_nonpoly / pdbx_nonpoly_scheme / pdbx_struct_assembly_gen / struct_asym / struct_conn / struct_ref_seq_dif / 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_entity_nonpoly.entity_id / _pdbx_entity_nonpoly.name / _pdbx_struct_assembly_gen.asym_id_list / _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_seq_id / _struct_conn.ptnr2_label_asym_id / _struct_ref_seq_dif.details
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 6, 2024Group: Structure summary / Category: pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: 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)274,74522
Polymers269,5234
Non-polymers5,22118
Water13,277737
1
A: Prostaglandin G/H synthase 2
B: Prostaglandin G/H synthase 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)137,37211
Polymers134,7622
Non-polymers2,6119
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area9600 Å2
ΔGint23 kcal/mol
Surface area42000 Å2
MethodPISA
2
C: Prostaglandin G/H synthase 2
D: Prostaglandin G/H synthase 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)137,37211
Polymers134,7622
Non-polymers2,6119
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area9660 Å2
ΔGint23 kcal/mol
Surface area42160 Å2
MethodPISA
Unit cell
Length a, b, c (Å)181.195, 134.465, 121.887
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21212

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Components

#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: 67380.773 Da / Num. of mol.: 4 / Mutation: H90W
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) / Strain (production host): baculovirus
References: UniProt: Q05769, prostaglandin-endoperoxide synthase
#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
#4: 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.: 6
Source method: isolated from a genetically manipulated source
Formula: C14H28O6 / Comment: detergent*YM
IdentifierTypeProgram
b-octylglucosideIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 737 / Source method: isolated from a natural source / Formula: H2O
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: 2.75 Å3/Da / Density % sol: 55.35 %
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-E / Wavelength: 0.97918 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Oct 5, 2012
RadiationMonochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97918 Å / Relative weight: 1
ReflectionResolution: 2.429→49.364 Å / Num. all: 112545 / Num. obs: 112512 / % possible obs: 99.8 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 5.2 % / Biso Wilson estimate: 38.6 Å2 / Rmerge(I) obs: 0.107 / Net I/σ(I): 17.1
Reflection shellResolution: 2.43→2.52 Å / Redundancy: 6.9 % / Rmerge(I) obs: 0.235 / Num. unique all: 4642 / % possible all: 99.62

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Processing

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

3nt1


Resolution: 2.429→49.364 Å / SU ML: 0.32 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 32.39 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.2585 3362 3 %RANDOM
Rwork0.2086 ---
all0.215 112240 --
obs0.2101 112189 99.58 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.429→49.364 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17912 0 344 737 18993
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00418804
X-RAY DIFFRACTIONf_angle_d0.83225490
X-RAY DIFFRACTIONf_dihedral_angle_d15.136942
X-RAY DIFFRACTIONf_chiral_restr0.0332754
X-RAY DIFFRACTIONf_plane_restr0.0043272
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.4287-2.46340.32471340.27284441X-RAY DIFFRACTION99
2.4634-2.50020.32921580.2674459X-RAY DIFFRACTION100
2.5002-2.53930.33391480.26274507X-RAY DIFFRACTION100
2.5393-2.58090.32171270.26244493X-RAY DIFFRACTION100
2.5809-2.62540.28741360.25984488X-RAY DIFFRACTION100
2.6254-2.67310.37221240.25054509X-RAY DIFFRACTION100
2.6731-2.72450.28651380.25264491X-RAY DIFFRACTION100
2.7245-2.78010.34161390.25134465X-RAY DIFFRACTION99
2.7801-2.84060.3391420.24544525X-RAY DIFFRACTION99
2.8406-2.90670.28991310.24764487X-RAY DIFFRACTION100
2.9067-2.97930.29041290.24624538X-RAY DIFFRACTION100
2.9793-3.05990.33421330.24824496X-RAY DIFFRACTION100
3.0599-3.14990.31381360.25134503X-RAY DIFFRACTION100
3.1499-3.25160.29271440.23374548X-RAY DIFFRACTION100
3.2516-3.36780.27861590.234542X-RAY DIFFRACTION100
3.3678-3.50260.31021310.2224499X-RAY DIFFRACTION100
3.5026-3.66190.24341290.20764524X-RAY DIFFRACTION99
3.6619-3.85490.22451520.19094544X-RAY DIFFRACTION100
3.8549-4.09630.19611520.17354552X-RAY DIFFRACTION100
4.0963-4.41240.22511460.16124552X-RAY DIFFRACTION100
4.4124-4.85610.2111340.15914586X-RAY DIFFRACTION100
4.8561-5.5580.20531450.1674614X-RAY DIFFRACTION100
5.558-6.99930.24271420.20084662X-RAY DIFFRACTION100
6.9993-49.37420.22581530.18934802X-RAY DIFFRACTION99
Refinement TLS params.

Method: refined / Refine-ID: X-RAY DIFFRACTION

IDL11 (°2)L12 (°2)L13 (°2)L22 (°2)L23 (°2)L33 (°2)S11 (Å °)S12 (Å °)S13 (Å °)S21 (Å °)S22 (Å °)S23 (Å °)S31 (Å °)S32 (Å °)S33 (Å °)T11 (Å2)T12 (Å2)T13 (Å2)T22 (Å2)T23 (Å2)T33 (Å2)Origin x (Å)Origin y (Å)Origin z (Å)
14.1945-1.37961.16120.6644-1.15062.6673-0.2315-0.87980.10920.52330.1971-0.035-0.6153-0.16880.0470.48890.00380.03640.7243-0.0320.333226.424-27.7033-32.0708
24.2074-0.3636-0.47754.6370.45641.84930.2163-0.75430.7229-0.0259-0.2517-0.0928-0.0505-0.2513-0.05130.3803-0.03970.08270.5138-0.15540.399823.9508-3.5327-47.2224
33.2292-0.35380.25450.98260.05510.6750.0224-0.5026-0.5130.0381-0.0077-0.02550.1196-0.1750.00270.3374-0.0161-0.03520.34980.04930.337124.5738-38.2455-48.3952
40.73320.15960.43690.69-0.78371.49870.29570.1773-0.2158-0.0045-0.20350.13210.1347-0.2995-0.05960.2706-0.0418-0.04720.331-0.02030.311416.2524-24.3373-63.6009
51.88110.35170.33230.6307-0.33271.70190.0890.2555-0.1096-0.0907-0.05010.00250.1604-0.0122-0.05060.33450.0510.00240.3039-0.02710.337130.155-22.1159-78.501
62.00140.2571-0.64980.9581-0.23581.35420.07010.04580.30050.01190.00710.0866-0.1915-0.1754-0.08850.29530.0446-0.00880.23510.01420.265530.7138-14.1656-60.2784
74.19841.2243-1.9833.83451.12795.2484-0.20550.5788-0.2041-0.20890.01140.738-0.0658-0.91760.18350.31490.0435-0.04280.53380.02250.3719.646-19.4308-78.1159
81.7594-0.13510.72391.27240.0661.19660.0403-0.345-0.02860.0902-0.05940.19110.0938-0.31610.02430.2733-0.01180.01530.45050.0230.32212.2311-27.9146-49.311
92.87810.41941.3212.1873-0.19383.1017-0.03870.0690.3538-0.0826-0.01940.0283-0.1319-0.18390.08820.30140.03030.05520.1818-0.03090.306630.5458-6.8117-67.2402
102.151-0.50151.32332.1458-1.95992.1307-0.331-0.18840.66860.4881-0.0863-0.2629-0.5398-0.03540.30830.4627-0.0256-0.00640.3298-0.09290.592160.1563-5.4188-51.9064
111.2250.1560.92520.7492-1.5595.34480.0297-0.25910.48880.22850.03080.0347-0.3751-0.19560.07420.3283-0.00860.02290.3405-0.03390.538453.6671-16.7905-49.3521
122.0162-0.4490.34730.20490.15550.36250.10580.41420.1767-0.0423-0.1778-0.1637-0.14410.23340.04420.3231-0.03170.02660.3690.14080.355964.0004-19.2737-69.1955
131.1880.06480.06540.5742-0.63590.62860.07290.0659-0.0845-0.104-0.02530.05670.14820.0736-0.07390.31430.02630.01130.24060.00250.287959.2159-41.8701-53.0993
142.33640.19450.07132.0482-0.01490.8620.0527-0.0311-0.2931-0.1831-0.0732-0.08270.0886-0.06990.04920.32810.0082-0.01830.23780.06110.306954.1508-46.5841-47.1229
153.6253-1.02910.20340.6771-0.07961.1550.0198-0.46450.0110.08830.0701-0.1365-0.04790.1094-0.00610.3098-0.0418-0.030.22590.01740.349758.6023-24.4591-45.3418
163.42511.6112-2.34125.24250.83743.9819-0.0377-0.1076-0.2427-0.2809-0.0757-0.58050.28070.55190.16140.37340.0494-0.0110.4890.08160.404975.3404-48.2888-48.8818
171.498-0.64860.19991.5108-0.171.6371-0.05390.14160.3075-0.0947-0.0307-0.2229-0.14250.17580.06390.283-0.04250.01330.26610.03840.364772.798-19.5592-57.4781
184.5983-1.71360.24262.7811-0.70111.9181-0.1915-0.7502-0.01540.16270.1842-0.18640.0731-0.07750.02150.3186-0.0025-0.02810.3194-0.00260.262554.4604-37.4041-36.3298
192.3572-1.0316-1.14140.4440.67782.4251-0.5574-1.0477-0.00070.40780.5651-0.23910.54340.4248-0.01360.59280.183-0.06031.15880.00980.475470.1559-40.859628.5481
203.8364-1.92181.01913.8917-0.59540.979-0.1728-0.9353-0.77220.37350.21860.16770.60310.7487-0.0010.72670.24050.01820.9230.2590.562771.5022-64.351513.6081
213.5004-0.46180.32411.5001-0.76683.0157-0.0745-0.63010.32150.11870.1465-0.04610.1230.6214-0.07030.31060.0097-0.00460.5825-0.04770.31763.1741-31.641812.1324
221.5834-0.0986-0.25260.8850.46621.6635-0.0452-0.03610.00780.00250.0957-0.0958-0.03180.3559-0.05570.2820.04140.03210.43290.00150.298270.4068-44.1354-9.7718
232.7698-0.3283-0.75851.2665-0.05790.98040.0474-0.4003-0.41320.0645-0.1881-0.07720.30850.46560.10140.41460.1657-0.04410.65580.03790.313369.8955-51.95386.6569
244.41541.31912.6042.655-0.25175.4364-0.11050.3928-0.0417-0.30950.4652-0.79060.01181.6165-0.24720.4230.03330.06420.8632-0.10980.57586.9109-48.1065-17.0467
250.8005-0.5656-0.34561.3041-0.15150.64-0.1242-0.59710.10060.24330.2553-0.43340.0290.6283-0.13830.42490.1026-0.06741.0409-0.12390.494484.2317-40.037211.8473
262.7454-0.1319-0.94542.38811.23873.4483-0.3714-0.174-0.77340.21130.10590.04580.51210.6150.25740.45850.10510.04340.37290.090.409265.7003-60.584-6.522
271.7491-0.1175-0.78910.77840.83771.1287-0.2521-0.1598-0.64890.4218-0.07980.12940.6207-0.1560.37030.5317-0.00580.12280.43880.08210.620837.9461-58.13959.3751
282.363-0.0822-0.16491.2582-0.05821.26390.07250.7486-0.3235-0.2742-0.28520.26070.1533-0.44890.25260.40190.00670.00270.6847-0.1760.506432.4745-47.4846-8.6522
291.6619-0.3264-0.29541.00560.70191.4348-0.02050.0555-0.121-0.024-0.11660.2130.0073-0.26520.1310.28610.00910.01580.3955-0.02230.303132.8678-32.23049.2201
305.7683-2.4743-0.852.90341.14182.335-0.3438-0.8808-0.08270.18880.24420.18620.04010.30680.09550.38490.02880.02580.43930.05980.32541.9055-29.925324.6883
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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