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- PDB-3tzi: X-ray crystal structure of arachidonic acid bound in the cyclooxy... -

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Basic information

Entry
Database: PDB / ID: 3tzi
TitleX-ray crystal structure of arachidonic acid bound in the cyclooxygenase channel of G533V murine COX-2
ComponentsProstaglandin G/H synthase 2
KeywordsOXIDOREDUCTASE / N-glycosylation / Monotopic Membrane Protein
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) / oxidoreductase activity, acting on single donors with incorporation of molecular oxygen / 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 / Synthesis of Prostaglandins (PG) and Thromboxanes (TX) / oxidoreductase activity, acting on single donors with incorporation of molecular oxygen / 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 / positive regulation of prostaglandin biosynthetic process / positive regulation of fever generation / positive regulation of smooth muscle contraction / response to selenium ion / oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen / prostaglandin secretion / positive regulation of synaptic plasticity / cellular response to fluid shear stress / 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 / maintenance of blood-brain barrier / decidualization / negative regulation of calcium ion transport / negative regulation of cell cycle / nuclear outer membrane / oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen / positive regulation of vasoconstriction / positive regulation of vascular endothelial growth factor production / keratinocyte differentiation / positive regulation of brown fat cell differentiation / positive regulation of synaptic transmission, glutamatergic / response to cytokine / embryo implantation / 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 / response to oxidative stress / angiogenesis / 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 / endoplasmic reticulum membrane / negative regulation of apoptotic process / enzyme binding / endoplasmic reticulum / protein homodimerization activity / protein-containing complex / metal ion binding / cytoplasm / cytosol
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
ARACHIDONIC ACID / 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: 2.15 Å
AuthorsVecchio, A.J. / Malkowski, M.G.
CitationJournal: J.Biol.Chem. / Year: 2012
Title: Investigating Substrate Promiscuity in Cyclooxygenase-2: THE ROLE OF ARG-120 AND RESIDUES LINING THE HYDROPHOBIC GROOVE.
Authors: Vecchio, A.J. / Orlando, B.J. / Nandagiri, R. / Malkowski, M.G.
History
DepositionSep 27, 2011Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 25, 2012Provider: repository / Type: Initial release
Revision 1.1Jun 13, 2012Group: Database references
Revision 1.2Aug 1, 2012Group: Database references
Revision 1.3Nov 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 / pdbx_validate_close_contact / 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_label_asym_id / _pdbx_struct_conn_angle.ptnr2_auth_asym_id / _pdbx_struct_conn_angle.ptnr2_label_asym_id / _pdbx_struct_conn_angle.ptnr3_auth_asym_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 / _pdbx_validate_close_contact.auth_asym_id_2 / _pdbx_validate_close_contact.auth_seq_id_2 / _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_comp_id / _struct_ref_seq_dif.details
Description: Carbohydrate remediation / Provider: repository / Type: Remediation
Revision 2.1Sep 13, 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 27, 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)141,40523
Polymers136,3212
Non-polymers5,08321
Water14,700816
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area14630 Å2
ΔGint13 kcal/mol
Surface area41660 Å2
MethodPISA
Unit cell
Length a, b, c (Å)122.265, 133.508, 181.093
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-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: 68160.641 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 19-604 / Mutation: N580A, G533V
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Cox-2, Cox2, Pghs-b, Ptgs2, 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)][b-D-GlcpNAc]{[(4+1)][a-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)][a-D-Manp]{}}}}LINUCSPDB-CARE
#6: 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
#7: 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, 830 molecules

#4: Chemical ChemComp-ACD / ARACHIDONIC ACID


Mass: 304.467 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C20H32O2
#5: Chemical ChemComp-COH / PROTOPORPHYRIN IX CONTAINING CO


Mass: 619.575 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C34H32CoN4O4
#8: Chemical
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 8 / Source method: obtained synthetically / Formula: C2H6O2
#9: Chemical ChemComp-AKR / ACRYLIC ACID


Mass: 72.063 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H4O2
#10: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 816 / 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: 2.71 Å3/Da / Density % sol: 54.62 %
Crystal growTemperature: 296 K / Method: vapor diffusion, sitting drop / pH: 7.5
Details: 23-34% Polyacrylic acid 5100, 100mM HEPES pH 7.5, 20mM MgCl2, VAPOR DIFFUSION, SITTING DROP, temperature 296K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: CHESS / Beamline: A1 / Wavelength: 0.978 Å
DetectorType: ADSC QUANTUM 210 / Detector: CCD / Date: Sep 24, 2009
RadiationMonochromator: Horizontal focusing 5.05 asymmetric cut Si(111)
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.978 Å / Relative weight: 1
ReflectionResolution: 2.15→20 Å / Num. all: 80417 / Num. obs: 76377 / % possible obs: 99.98 % / Redundancy: 5.1 % / Rmerge(I) obs: 0.087 / Net I/σ(I): 12.7
Reflection shellResolution: 2.15→2.27 Å / Redundancy: 4.9 % / Rmerge(I) obs: 0.447 / Mean I/σ(I) obs: 3.3 / % possible all: 99.9

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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: 2.15→19.99 Å / Cor.coef. Fo:Fc: 0.962 / Cor.coef. Fo:Fc free: 0.943 / SU B: 9.872 / SU ML: 0.117 / Cross valid method: THROUGHOUT / ESU R: 0.197 / ESU R Free: 0.167 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.2096 4039 5 %RANDOM
Rwork0.16976 ---
obs0.17179 76377 99.98 %-
all-80417 --
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 29.812 Å2
Baniso -1Baniso -2Baniso -3
1-1.01 Å20 Å20 Å2
2--0.06 Å20 Å2
3----1.07 Å2
Refine analyzeLuzzati sigma a obs: 0.299 Å
Refinement stepCycle: LAST / Resolution: 2.15→19.99 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8869 0 343 816 10028
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.010.0229577
X-RAY DIFFRACTIONr_bond_other_d
X-RAY DIFFRACTIONr_angle_refined_deg1.2662.00313035
X-RAY DIFFRACTIONr_angle_other_deg
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.4451123
X-RAY DIFFRACTIONr_dihedral_angle_2_deg36.64323.956450
X-RAY DIFFRACTIONr_dihedral_angle_3_deg14.109151495
X-RAY DIFFRACTIONr_dihedral_angle_4_deg11.8681546
X-RAY DIFFRACTIONr_chiral_restr0.0860.21383
X-RAY DIFFRACTIONr_gen_planes_refined0.0050.0217392
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_it0.3421.55558
X-RAY DIFFRACTIONr_mcbond_other
X-RAY DIFFRACTIONr_mcangle_it0.66529037
X-RAY DIFFRACTIONr_scbond_it1.3934019
X-RAY DIFFRACTIONr_scangle_it2.3214.53988
X-RAY DIFFRACTIONr_rigid_bond_restr
X-RAY DIFFRACTIONr_sphericity_free
X-RAY DIFFRACTIONr_sphericity_bonded
LS refinement shellResolution: 2.15→2.205 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.272 311 -
Rwork0.233 5537 -
obs--99.93 %
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)
11.6217-1.27740.77144.5305-1.523.4836-0.00050.17630.0173-0.00290.0645-0.2769-0.28030.5423-0.0640.0809-0.07380.06230.26-0.06740.229959.523538.242630.2784
21.2725-1.20261.362920.9531.92232.03750.46940.2189-0.33290.0359-0.1851-0.28550.65870.2459-0.28430.29430.10470.09320.4549-0.10720.608466.830520.533728.0143
32.5069-3.2744-0.04665.2905-1.78333.6513-0.135-0.14090.0918-0.289-0.0077-0.41210.62390.46670.14280.32880.04920.26270.2416-0.17770.647750.06765.4217.0762
42.6349-1.7249-0.9716.17232.824711.5997-0.0960.0151-0.0760.5371-0.1532-0.94550.58310.56790.24920.27120.16760.04950.34150.00380.441746.35433.719929.4641
51.24280.55050.07561.09440.79414.2987-0.07140.15310.0413-0.12590.1197-0.1042-0.34210.2759-0.04830.0691-0.04060.03140.04930.00010.082142.591237.248424.2988
61.59331.41120.38131.49440.41883.4689-0.09340.15670.1381-0.14090.02670.1669-0.1509-0.17410.06670.02490.0265-0.00910.08110.00910.072928.581724.11521.9634
72.8733-0.0741.01091.274-0.2394.10060.00140.22450.21520.0414-0.00120.3005-0.0918-0.4521-0.00020.0231-0.01490.03620.1311-0.01380.122912.062819.562830.7525
81.55440.7268-0.48490.91640.10582.2647-0.04040.1389-0.22280.00220.0511-0.17150.28210.0938-0.01070.06620.00930.01770.0271-0.03330.082131.792914.162630.1344
94.8527-2.56131.62184.3263-3.42055.28650.1970.56080.0809-0.4343-0.160.26940.2427-0.8341-0.0370.1451-0.0271-0.02760.4531-0.04490.10113.448716.668611.4404
102.39721.25470.9361.87870.68212.1209-0.14880.25770.0852-0.2070.1576-0.0167-0.14420.1117-0.00870.1011-0.06320.04510.1238-0.00490.03340.48529.976314.4558
111.40720.8805-0.70551.9208-0.90633.4232-0.16090.3136-0.1665-0.31830.1194-0.23530.05910.17550.04150.0871-0.05640.05870.1709-0.05770.095244.602425.760412.4818
121.39550.43240.49491.9018-0.09053.26340.04690.1297-0.34780.07270.033-0.14370.5358-0.0072-0.07990.1391-0.01660.03530.0159-0.04340.126525.92585.736232.263
134.6086-0.1541-1.7620.6716-0.95733.2543-0.1312-0.0387-0.22620.07880.02460.00010.8234-0.15450.10660.7722-0.1181-0.00260.02150.01930.225627.01312.052956.9502
146.23241.33180.738511.41816.57993.8407-0.08060.4165-1.30480.60981.0173-1.75180.49170.69-0.93670.69480.2242-0.06010.38430.0280.710245.79690.136462.0155
152.4141.186-2.39622.4947-1.939910.2484-0.0295-0.3099-0.6232-0.0554-0.1443-0.42350.60630.60970.17380.23960.1773-0.09370.25980.03140.509860.003618.97164.1543
160.64950.22160.72651.22841.13085.37450.076-0.1146-0.08860.2762-0.13830.03060.4511-0.36430.06230.1384-0.06370.00740.04270.01110.086125.842719.232463.1009
170.93630.7269-0.9061.97840.44241.83430.0710.04150.0890.0796-0.04960.1409-0.0398-0.1693-0.02140.013-0.00990.02560.133-0.01370.070936.760136.232161.8254
181.3830.1504-0.28143.62882.65115.44810.0122-0.03160.3184-0.3548-0.05070.0183-0.8002-0.0520.03850.1385-0.0010.02540.0056-0.02580.155140.194755.401452.4732
191.36210.1181-0.42912.0623-0.57563.3920.0565-0.10810.16950.070.11510.0302-0.35390.0309-0.17170.043-0.00910.0210.0295-0.03670.084243.760845.886856.108
201.350.35730.02461.84250.55622.37730.036-0.155-0.1150.19210.0387-0.18820.15470.2253-0.07480.0487-0.0037-0.04240.05560.02710.06144.783129.895762.5972
214.14240.1709-2.06945.01570.31594.72390.147-0.31190.27820.28330.01640.2246-0.21340.0349-0.16340.1436-0.07550.06360.1426-0.07480.088641.205450.54274.4126
221.34340.78250.69352.68831.9522.53140.1-0.21890.04690.2827-0.10860.10220.3179-0.2080.00860.1749-0.06330.01340.10710.03330.035430.961425.260273.2397
230.89070.6233-0.38221.202-0.24751.56560.0839-0.27-0.19160.2196-0.0781-0.11130.44860.2394-0.00580.20830.0371-0.0420.11560.03390.114639.9520.5268.2161
241.59480.9504-0.87112.67050.97655.52310.0906-0.37730.0420.18260.1619-0.2687-0.01250.8117-0.25240.0155-0.0005-0.02940.1904-0.08020.158656.280642.768761.5522
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A33 - 68
2X-RAY DIFFRACTION2A69 - 82
3X-RAY DIFFRACTION3A83 - 102
4X-RAY DIFFRACTION4A103 - 122
5X-RAY DIFFRACTION5A123 - 185
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