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- PDB-3mdl: X-ray crystal structure of 1-arachidonoyl glycerol bound to the c... -

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Basic information

Entry
Database: PDB / ID: 3mdl
TitleX-ray crystal structure of 1-arachidonoyl glycerol bound to the cyclooxygenase channel of cyclooxygenase-2
ComponentsProstaglandin G/H synthase 2
KeywordsOXIDOREDUCTASE / COX-2 / Cyclooxygenase-2 / Endocannabinoid
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 salvage ...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 salvage / Synthesis of Prostaglandins (PG) and Thromboxanes (TX) / positive regulation of fibroblast growth factor production / prostaglandin-endoperoxide synthase / prostaglandin-endoperoxide synthase activity / cyclooxygenase pathway / positive regulation of transforming growth factor beta production / cellular response to lead ion / negative regulation of synaptic transmission, dopaminergic / 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 / response to fatty acid / response to fructose / positive regulation of smooth muscle contraction / oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen / positive regulation of fever generation / response to vitamin D / prostaglandin secretion / cellular response to fluid shear stress / response to selenium ion / response to nematode / nuclear outer membrane / response to angiotensin / nuclear inner membrane / response to manganese ion / prostaglandin biosynthetic process / negative regulation of smooth muscle contraction / 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 / negative regulation of cell cycle / decidualization / response to tumor necrosis factor / positive regulation of vascular endothelial growth factor production / 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 / positive regulation of smooth muscle cell proliferation / peroxidase activity / caveola / regulation of blood pressure / memory / positive regulation of protein import into nucleus / cellular response to mechanical stimulus / positive regulation of nitric oxide biosynthetic process / response to estradiol / regulation of cell population proliferation / cellular response to heat / cellular response to lipopolysaccharide / angiogenesis / cellular response to hypoxia / response to oxidative stress / neuron projection / positive regulation of apoptotic process / response to xenobiotic stimulus / negative regulation of cell population proliferation / heme binding / endoplasmic reticulum membrane / negative regulation of apoptotic process / enzyme binding / 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
Chem-1AG / ACRYLIC ACID / PROTOPORPHYRIN IX CONTAINING CO / Prostaglandin G/H synthase 2
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.2 Å
AuthorsVecchio, A.J. / Malkowski, M.G.
CitationJournal: J.Biol.Chem. / Year: 2011
Title: The structural basis of endocannabinoid oxygenation by cyclooxygenase-2.
Authors: Vecchio, A.J. / Malkowski, M.G.
History
DepositionMar 30, 2010Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 13, 2011Provider: repository / Type: Initial release
Revision 1.1Jul 13, 2011Group: Version format compliance
Revision 1.2Nov 8, 2017Group: Refinement description / Category: software / Item: _software.classification / _software.name
Revision 2.0Jul 29, 2020Group: Advisory / Atomic model ...Advisory / Atomic model / Data collection / Database references / Derived calculations / Structure summary
Category: atom_site / chem_comp ...atom_site / chem_comp / database_PDB_caveat / 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_validate_chiral / 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_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 / _pdbx_validate_chiral.auth_asym_id / _pdbx_validate_chiral.auth_seq_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_seq_id / _struct_conn.ptnr1_label_asym_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_comp_id / _struct_ref_seq_dif.details
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Oct 6, 2021Group: Database references / Structure summary / Category: chem_comp / database_2 / struct_ref_seq_dif
Item: _chem_comp.pdbx_synonyms / _database_2.pdbx_DOI ..._chem_comp.pdbx_synonyms / _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details
Revision 2.2Sep 6, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model
Revision 2.3Oct 30, 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
hetero molecules


Theoretical massNumber of molelcules
Total (without water)140,14721
Polymers134,9202
Non-polymers5,22719
Water17,294960
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11490 Å2
ΔGint-25 kcal/mol
Surface area41280 Å2
MethodPISA
Unit cell
Length a, b, c (Å)118.958, 131.773, 179.858
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number23
Space group name H-MI222
DetailsAsymmetric Unit contains the COX-2 Biological Dimer.

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Components

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Protein , 1 types, 2 molecules AB

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


Mass: 67459.844 Da / Num. of mol.: 2 / Fragment: UNP residues 20 to 599 / Mutation: N580A
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Ptgs2, Cox-2, Cox2, Pghs-b, Tis10 / Plasmid: pFastBac1 / Production host: Spodoptera frugiperda (fall armyworm) / Strain (production host): SF21
References: UniProt: Q05769, prostaglandin-endoperoxide synthase

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Sugars , 4 types, 7 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.: 3
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)][a-L-IdopNAc]{[(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: isolated from a genetically manipulated source
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)][b-D-Manp]{}}}}LINUCSPDB-CARE
#8: 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.: 2
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
#9: 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.: 1
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 , 5 types, 972 molecules

#4: Chemical ChemComp-1AG / (2S)-2,3-dihydroxypropyl (5Z,8Z,11Z,14Z)-icosa-5,8,11,14-tetraenoate


Mass: 378.545 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C23H38O4
#5: Chemical
ChemComp-AKR / ACRYLIC ACID


Mass: 72.063 Da / Num. of mol.: 5 / Source method: obtained synthetically / Formula: C3H4O2
#6: Chemical ChemComp-GOL / GLYCEROL / GLYCERIN / PROPANE-1,2,3-TRIOL


Mass: 92.094 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C3H8O3
#7: Chemical ChemComp-COH / PROTOPORPHYRIN IX CONTAINING CO


Mass: 619.575 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C34H32CoN4O4
#10: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 960 / 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: 2.61 Å3/Da / Density % sol: 52.91 %
Crystal growTemperature: 296 K / Method: vapor diffusion, sitting drop / pH: 7.5
Details: 23-34% Polyacrylic Acid Sodium Salt, 0.1M Hepes pH 7.5, 0.02M Magnesium chloride, VAPOR DIFFUSION, SITTING DROP, temperature 296K

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Data collection

DiffractionMean temperature: 77 K
Diffraction sourceSource: SYNCHROTRON / Site: CHESS / Beamline: A1 / Wavelength: 0.9777 Å
DetectorType: ADSC QUANTUM 210 / Detector: CCD / Date: May 7, 2007
RadiationMonochromator: Horizontal focusing 5.05 asymmetric cut Si(111)
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9777 Å / Relative weight: 1
ReflectionResolution: 2.2→20 Å / Num. all: 71165 / Num. obs: 67549 / % possible obs: 99.2 % / Redundancy: 4.5 % / Rmerge(I) obs: 0.086 / Net I/σ(I): 11.4
Reflection shellResolution: 2.2→2.32 Å / Redundancy: 3.6 % / Rmerge(I) obs: 0.417 / Mean I/σ(I) obs: 2.8 / % possible all: 95.9

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Processing

Software
NameVersionClassification
Adxvdata processing
PHASERphasing
REFMAC5.5.0088refinement
MOSFLMdata reduction
SCALAdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB entry 1CVU

1cvu


Resolution: 2.2→19.97 Å / Cor.coef. Fo:Fc: 0.956 / Cor.coef. Fo:Fc free: 0.93 / SU B: 10.851 / SU ML: 0.125 / Cross valid method: THROUGHOUT / ESU R: 0.233 / ESU R Free: 0.189 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.21466 3597 5.1 %RANDOM
Rwork0.1651 ---
obs0.1676 67549 99.24 %-
all-71165 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK
Displacement parametersBiso mean: 28.169 Å2
Baniso -1Baniso -2Baniso -3
1--0.02 Å20 Å20 Å2
2--0.08 Å20 Å2
3----0.06 Å2
Refine analyzeLuzzati sigma a obs: 0.259 Å
Refinement stepCycle: LAST / Resolution: 2.2→19.97 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8906 0 354 960 10220
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0080.0229605
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.1272.00813054
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.22151113
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.59723.946446
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.612151528
X-RAY DIFFRACTIONr_dihedral_angle_4_deg12.711546
X-RAY DIFFRACTIONr_chiral_restr0.0790.21383
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0217363
X-RAY DIFFRACTIONr_gen_planes_other
X-RAY DIFFRACTIONr_nbd_refined
X-RAY DIFFRACTIONr_nbd_other
X-RAY DIFFRACTIONr_nbtor_refined
X-RAY DIFFRACTIONr_nbtor_other
X-RAY DIFFRACTIONr_xyhbond_nbd_refined
X-RAY DIFFRACTIONr_xyhbond_nbd_other
X-RAY DIFFRACTIONr_metal_ion_refined
X-RAY DIFFRACTIONr_metal_ion_other
X-RAY DIFFRACTIONr_symmetry_vdw_refined
X-RAY DIFFRACTIONr_symmetry_vdw_other
X-RAY DIFFRACTIONr_symmetry_hbond_refined
X-RAY DIFFRACTIONr_symmetry_hbond_other
X-RAY DIFFRACTIONr_symmetry_metal_ion_refined
X-RAY DIFFRACTIONr_symmetry_metal_ion_other
X-RAY DIFFRACTIONr_mcbond_it0.3281.55553
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it0.66829014
X-RAY DIFFRACTIONr_scbond_it1.28834052
X-RAY DIFFRACTIONr_scangle_it2.2374.54036
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.2→2.256 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.285 229 -
Rwork0.225 4546 -
obs--91.69 %
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)
11.341.2029-0.00392.0080.35892.7309-0.0756-0.03130.08380.03910.19190.2162-0.218-0.4567-0.11630.05020.07160.04060.18310.06880.14780.794438.008559.2429
22.4547-3.01991.84573.9107-2.80782.89850.0997-0.2022-0.6007-0.19950.42350.75280.3053-0.5686-0.52320.054-0.0984-0.01030.23910.13110.3922-1.020417.308866.266
31.908-0.5772-4.01076.4798-2.600110.7451-0.29470.2448-0.2261-0.1493-0.03970.27440.739-0.51370.33440.0893-0.09880.01750.13350.00680.23613.29192.320864.7852
40.4753-0.1943-0.18220.7346-0.41551.4008-0.0412-0.06690.0890.12430.09960.0072-0.135-0.1004-0.05840.08990.0270.00250.0835-0.01360.094617.568736.624366.1563
50.8765-0.75110.55520.9814-0.61331.425-0.0662-0.07120.0880.11780.0206-0.1006-0.13830.0910.04570.06660.0085-0.01340.06860.00120.109631.487123.42867.2984
61.8969-0.28380.85691.0826-0.15732.13090.0160.03860.0728-0.0634-0.0033-0.0627-0.02380.2122-0.01270.00620.00620.01430.08010.02260.128850.057219.571456.1051
71.44430.1286-0.0810.77090.36962.9760.0692-0.20210.11490.0502-0.0475-0.0772-0.05080.1309-0.02170.02220.01490.00620.10370.03060.130246.287818.595562.916
80.4878-0.2228-0.28920.4647-0.15021.0978-0.058-0.1021-0.09030.0320.06210.05350.11520.0213-0.00410.0792-0.0022-0.00460.060.02590.11328.792513.997361.142
94.2694-1.1034-1.05761.25340.60271.8958-0.0997-0.42980.09550.14120.1617-0.1657-0.03510.3632-0.0620.08980.0222-0.0260.125-0.00690.026640.367218.427780.0507
101.65480.12350.36741.2491-0.03552.2864-0.1204-0.2340.05650.270.17080.0889-0.066-0.2129-0.05030.10360.08240.03860.10430.00260.052114.411531.577476.8399
110.6801-0.286-0.51810.76420.60761.8301-0.0415-0.0921-0.09660.0166-0.00910.1555-0.0327-0.14950.05060.08530.01770.00410.05770.03460.087319.465620.175966.2711
120.9657-0.6403-0.10892.69770.36193.1549-0.0314-0.0447-0.21210.08830.03020.06130.4086-0.060.00120.1122-0.01210.02190.04240.04910.14736.57653.535664.7406
135.62390.8908-1.45050.4212-0.23163.44910.0655-0.1149-0.3505-0.1938-0.07490.01620.58990.27360.00940.30010.0766-0.02840.0341-0.02270.119833.23251.777833.5452
147.2498-6.75245.89696.723-5.86085.10940.4829-0.3633-1.0806-0.89890.56691.20270.7744-0.4925-1.04980.5001-0.277-0.2410.1890.05870.468414.24211.02927.2664
154.5453-2.4241-1.15752.56592.354610.9226-0.06830.1347-0.64630.0681-0.21080.35850.7305-0.66280.27910.1695-0.1259-0.02470.10590.00210.23470.686919.069525.9556
160.6102-0.25350.1770.8508-0.37441.78260.07810.0709-0.041-0.1489-0.0737-0.04550.27520.1681-0.00450.11550.03160.01240.0686-0.00620.085834.177719.352526.7035
170.8099-0.6668-0.45110.8505-0.17131.25080.0469-0.02950.1149-0.03360.0218-0.1111-0.04090.0529-0.06870.048-0.01330.01240.10550.02180.154924.078935.877329.6002
181.9447-0.84381.27780.7843-0.75023.7267-0.05620.15630.27750.08990.04850.04-0.4830.19290.00760.0815-0.00960.01090.05170.06390.169220.368954.853737.7259
191.9598-0.6681-0.24782.67720.76343.36130.1117-0.00020.211-0.2620.1198-0.4331-0.47430.5014-0.23150.0944-0.06430.05360.11610.01510.145928.313750.229127.9276
200.9119-0.4613-0.35281.13990.1861.234-0.01730.05940.0433-0.00430.01080.0892-0.1071-0.21860.00650.04550.0051-0.00610.10590.05110.12819.976542.206537.5449
211.03050.0476-0.21691.1974-0.67411.93690.09120.1227-0.0536-0.2037-0.01830.13850.1031-0.0519-0.07290.0791-0.0156-0.02430.0553-0.01450.099416.226629.374127.4792
224.0160.591-0.14584.33840.0692.68740.16470.27720.0807-0.2764-0.0502-0.1552-0.34190.0203-0.11440.06990.0240.03690.09740.07080.064719.814750.126715.9849
230.8835-0.36820.36250.9511-0.41871.47130.09080.1966-0.0656-0.2084-0.06040.03660.28850.0154-0.03040.13540.0265-0.00680.0635-0.02770.025626.480119.696215.5314
241.365-0.2126-0.21270.8816-0.80532.28490.02890.05410.0187-0.03540.07430.12270.0559-0.2624-0.10310.0087-0.0172-0.00620.10820.03490.12446.909737.484535.3803
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A33 - 67
2X-RAY DIFFRACTION2A68 - 92
3X-RAY DIFFRACTION3A93 - 122
4X-RAY DIFFRACTION4A123 - 186
5X-RAY DIFFRACTION5A187 - 233
6X-RAY DIFFRACTION6A234 - 271
7X-RAY DIFFRACTION7A272 - 320
8X-RAY DIFFRACTION8A321 - 400
9X-RAY DIFFRACTION9A401 - 445
10X-RAY DIFFRACTION10A446 - 493
11X-RAY DIFFRACTION11A494 - 553
12X-RAY DIFFRACTION12A554 - 584
13X-RAY DIFFRACTION13B33 - 67
14X-RAY DIFFRACTION14B68 - 89
15X-RAY DIFFRACTION15B90 - 122
16X-RAY DIFFRACTION16B123 - 188
17X-RAY DIFFRACTION17B189 - 240
18X-RAY DIFFRACTION18B241 - 269
19X-RAY DIFFRACTION19B270 - 302
20X-RAY DIFFRACTION20B303 - 356
21X-RAY DIFFRACTION21B357 - 401
22X-RAY DIFFRACTION22B402 - 429
23X-RAY DIFFRACTION23B430 - 531
24X-RAY DIFFRACTION24B532 - 583

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