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- PDB-3qh0: X-ray crystal structure of palmitic acid bound to the cyclooxygen... -

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Basic information

Entry
Database: PDB / ID: 3qh0
TitleX-ray crystal structure of palmitic acid bound to the cyclooxygenase channel of cyclooxygenase-2
ComponentsProstaglandin G/H synthase 2
KeywordsOXIDOREDUCTASE / Biological Dimer / 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 / 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 / regulation of neuroinflammatory response / positive regulation of synaptic plasticity / positive regulation of smooth muscle contraction / oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen / cyclooxygenase pathway / response to fatty acid / response to fructose / positive regulation of fever generation / prostaglandin secretion / response to vitamin D / cellular response to fluid shear stress / nuclear outer membrane / response to angiotensin / response to manganese ion / prostaglandin biosynthetic process / nuclear inner membrane / negative regulation of smooth muscle contraction / cellular response to ATP / positive regulation of cell migration involved in sprouting angiogenesis / 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 / keratinocyte differentiation / positive regulation of vasoconstriction / positive regulation of brown fat cell differentiation / embryo implantation / positive regulation of synaptic transmission, glutamatergic / learning / response to cytokine / caveola / 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 / peroxidase activity / cellular response to mechanical stimulus / positive regulation of nitric oxide biosynthetic process / positive regulation of peptidyl-serine phosphorylation / response to estradiol / cellular response to heat / regulation of cell population proliferation / cellular response to hypoxia / angiogenesis / response to oxidative stress / response to lipopolysaccharide / response to xenobiotic stimulus / neuron projection / positive regulation of apoptotic process / 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 / 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 CO / PALMITIC ACID / Prostaglandin G/H synthase 2
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.1 Å
AuthorsVecchio, A.J. / Malkowski, M.G.
CitationJournal: J.Biol.Chem. / Year: 2011
Title: Human cyclooxygenase-2 is a sequence homodimer that functions as a conformational heterodimer.
Authors: Dong, L. / Vecchio, A.J. / Sharma, N.P. / Jurban, B.J. / Malkowski, M.G. / Smith, W.L.
History
DepositionJan 25, 2011Deposition 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_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.occupancy / _atom_site.type_symbol / _chem_comp.mon_nstd_flag / _chem_comp.name / _chem_comp.type / _pdbx_struct_assembly_gen.asym_id_list / _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

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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)145,41937
Polymers139,7582
Non-polymers5,66235
Water13,565753
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area16450 Å2
ΔGint46 kcal/mol
Surface area41330 Å2
MethodPISA
Unit cell
Length a, b, c (Å)121.906, 130.888, 179.968
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: 69878.773 Da / Num. of mol.: 2 / Fragment: UNP Residue 1-608 / Mutation: N580A
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 , 6 types, 7 molecules

#2: Polysaccharide 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetylamino-2-deoxy-alpha-L-idopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAcb1-4LIdopNAca1-ROHGlycam Condensed SequenceGMML 1.0
WURCS=2.0/2,2,1/[a2121h-1a_1-5_2*NCC/3=O][a2122h-1b_1-5_2*NCC/3=O]/1-2/a4-b1WURCSPDB2Glycan 1.1.0
[][L-1-deoxy-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)][a-D-Manp]{}}}}LINUCSPDB-CARE
#4: Polysaccharide 2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose


Type: oligosaccharide / Mass: 424.401 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
DescriptorTypeProgram
DGlcpNAca1-4DGlcpNAcb1-Glycam Condensed SequenceGMML 1.0
WURCS=2.0/2,2,1/[a2122h-1b_1-5_2*NCC/3=O][a2122h-1a_1-5_2*NCC/3=O]/1-2/a4-b1WURCSPDB2Glycan 1.1.0
[]{[(4+1)][b-D-GlcpNAc]{[(4+1)][a-D-GlcpNAc]{}}}LINUCSPDB-CARE
#5: 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.: 1
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
#10: 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
#11: 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, 781 molecules

#6: Chemical...
ChemComp-EDO / 1,2-ETHANEDIOL / ETHYLENE GLYCOL


Mass: 62.068 Da / Num. of mol.: 23 / Source method: obtained synthetically / Formula: C2H6O2
#7: Chemical ChemComp-PLM / PALMITIC ACID


Mass: 256.424 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C16H32O2
#8: Chemical ChemComp-AKR / ACRYLIC ACID


Mass: 72.063 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C3H4O2
#9: Chemical ChemComp-COH / PROTOPORPHYRIN IX CONTAINING CO


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


Mass: 18.015 Da / Num. of mol.: 753 / 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: 2.57 Å3/Da / Density % sol: 52.11 %
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: 0.9769 Å
DetectorType: ADSC QUANTUM 210 / Detector: CCD / Date: Nov 5, 2009
RadiationMonochromator: Si (111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9769 Å / Relative weight: 1
ReflectionResolution: 2.1→20 Å / Num. all: 82053 / Num. obs: 77928 / % possible obs: 98 % / Redundancy: 5.6 % / Biso Wilson estimate: 24.9 Å2 / Rmerge(I) obs: 0.096 / Net I/σ(I): 13.5
Reflection shellResolution: 2.1→2.21 Å / Redundancy: 5.4 % / Rmerge(I) obs: 0.562 / Mean I/σ(I) obs: 2.9 / Num. unique all: 11717 / % possible all: 96.8

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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: 2.1→20 Å / Cor.coef. Fo:Fc: 0.961 / Cor.coef. Fo:Fc free: 0.943 / SU B: 7.901 / SU ML: 0.097 / Cross valid method: THROUGHOUT / ESU R: 0.177 / ESU R Free: 0.154 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
RfactorNum. reflection% reflectionSelection details
Rfree0.19894 4122 5 %RANDOM
Rwork0.15947 ---
all0.211 82053 --
obs0.16145 77928 97.9 %-
Solvent computationIon probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK
Displacement parametersBiso mean: 28.188 Å2
Baniso -1Baniso -2Baniso -3
1-0 Å20 Å20 Å2
2---0.05 Å20 Å2
3---0.05 Å2
Refine analyzeLuzzati sigma a obs: 0.257 Å
Refinement stepCycle: LAST / Resolution: 2.1→20 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms8833 0 377 753 9963
Refine LS restraints
Refine-IDTypeDev idealDev ideal targetNumber
X-RAY DIFFRACTIONr_bond_refined_d0.0110.0229570
X-RAY DIFFRACTIONr_angle_refined_deg1.3292.00113009
X-RAY DIFFRACTIONr_dihedral_angle_1_deg5.69251129
X-RAY DIFFRACTIONr_dihedral_angle_2_deg37.36123.924446
X-RAY DIFFRACTIONr_dihedral_angle_3_deg13.632151482
X-RAY DIFFRACTIONr_dihedral_angle_4_deg14.881546
X-RAY DIFFRACTIONr_chiral_restr0.0930.21380
X-RAY DIFFRACTIONr_gen_planes_refined0.0060.0217344
X-RAY DIFFRACTIONr_mcbond_it0.5021.55565
X-RAY DIFFRACTIONr_mcangle_it0.9729044
X-RAY DIFFRACTIONr_scbond_it1.84134005
X-RAY DIFFRACTIONr_scangle_it3.0634.53952
LS refinement shellResolution: 2.1→2.154 Å / Total num. of bins used: 20
RfactorNum. reflection% reflection
Rfree0.276 310 -
Rwork0.211 5576 -
obs--96.52 %
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)
11.0567-0.06870.17043.88691.05621.985-0.0529-0.25150.03050.05060.16270.0524-0.1368-0.5552-0.10970.05940.06640.04950.27530.07580.14891.339437.127359.892
24.9645-3.23544.10299.9081-5.11414.17430.2881-0.3324-0.8992-0.43320.54220.77470.352-0.4681-0.83030.2147-0.14280.04090.50970.16540.4432-3.520118.197863.7919
31.8541-0.2957-1.29774.1887-0.73356.7349-0.109-0.0229-0.42380.09140.05430.26390.9159-0.75270.05470.1581-0.16140.00690.22940.05790.336713.25722.37466.6624
40.5823-0.30630.19250.6588-0.49911.6769-0.1028-0.15320.03510.11440.15550.032-0.1028-0.1831-0.05260.07110.06640.0060.10590.00740.06618.308835.462566.3008
50.8995-0.83270.13791.0728-0.29551.6292-0.0628-0.12610.07050.08340.0895-0.1018-0.0349-0.0293-0.02660.02850.0067-0.0110.0418-0.00940.062933.229322.866.6822
62.1833-0.05240.8621.7125-0.36592.26380.12390.05270.0733-0.0476-0.0058-0.1649-0.020.26-0.1180.02030.00460.02960.0472-0.0080.131951.567119.013955.7902
75.35350.5336-1.08883.4482-1.21874.8179-0.0794-0.39010.51180.11020.0015-0.292-0.33540.26220.07790.0492-0.01160.02620.0532-0.06360.229550.612826.873765.6095
81.3031-0.3199-0.03340.7833-0.25151.18760.0521-0.0525-0.1195-0.03860.0030.08370.1689-0.0251-0.0550.0659-0.0039-0.02820.0040.01160.092633.89049.419756.2276
91.8318-0.95551.58891.4795-1.37254.0377-0.1121-0.34290.03690.22930.1652-0.0143-0.0742-0.0985-0.05310.0760.03790.0120.0863-0.01080.023431.968922.137473.5913
103.1558-0.9282-0.75871.03570.29911.6793-0.0588-0.30080.15690.18160.1935-0.1337-0.03640.179-0.13470.09670.0486-0.03540.1573-0.02830.031841.912118.000779.9808
110.6755-0.5657-0.13550.85060.30261.0947-0.0796-0.2153-0.07060.13790.12090.11-0.0283-0.1927-0.04130.05670.03560.02780.13620.04420.062918.253224.726371.4308
121.3668-0.51510.22082.96470.84773.7331-0.0961-0.148-0.40130.05510.05020.24060.3826-0.20770.04580.1187-0.0034-0.00650.0350.03810.154638.00552.994864.4858
132.9754-0.1115-1.1250.3923-0.02972.3630.10840.0284-0.0427-0.2478-0.03950.01170.52750.0547-0.0690.31030.063-0.06180.0534-0.04560.160134.40971.909933.1464
1415.94842.04241.52082.4515-0.36072.5035-0.2384-0.052-0.4182-0.08160.14680.35550.3138-0.34710.09160.3346-0.0522-0.070.1334-0.05270.264418.7895-3.701830.1323
152.3969-1.2917-0.66232.17822.39045.21920.03650.1937-0.47120.1566-0.38660.42770.6574-0.74840.35010.2704-0.1501-0.05430.1863-0.0860.39042.195416.672925.0434
160.5947-0.10480.27980.5184-0.15241.50080.13990.112-0.1026-0.2033-0.16040.01050.20960.12350.02050.13080.10240.00040.0822-0.00360.051534.334819.327426.3919
170.7912-0.81360.11861.0323-0.15281.25030.04040.08010.0558-0.0845-0.0641-0.06290.01160.13890.02370.06250.02690.00480.05670.02010.08224.252134.779528.0386
181.6692-0.37810.70732.6959-1.04462.8517-0.1123-0.01420.25880.18090.0748-0.1658-0.31570.10790.03750.0665-0.011-0.02260.01410.00080.09921.692552.708238.8209
191.34720.88240.13287.71155.22329.1587-0.49890.26130.2689-1.1470.4025-0.6736-1.33881.12410.09650.4071-0.2397-0.0260.33250.090.369431.59254.507529.0998
200.7768-0.21740.14361.22240.08761.23140.00940.0169-0.0581-0.04750.01450.1130.0042-0.0954-0.02390.01210.0128-0.01660.05530.02030.070811.986237.619736.1886
210.6783-0.74950.38593.0221-1.59342.13550.20830.23580.0589-0.3966-0.2078-0.05240.0470.3079-0.00050.09850.04660.02980.15970.02140.048224.366940.559917.9436
222.86391.85390.633211.70412.27564.460.0690.20820.0596-0.16940.0581-0.0235-0.11690.0316-0.12720.10740.0439-0.00140.12850.02170.090812.866449.750416.7382
231.169-0.32950.81641.434-0.36720.97580.20360.2538-0.0309-0.2803-0.1890.02890.19010.2156-0.01470.17530.120.01080.1387-0.01210.009830.55725.450816.8981
240.8854-0.48270.01450.7145-0.26880.65360.11770.1463-0.1451-0.1968-0.07870.12830.2014-0.0269-0.0390.10510.0169-0.06350.0607-0.01210.076217.03325.590123.7865
Refinement TLS group
IDRefine-IDRefine TLS-IDAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1A33 - 68
2X-RAY DIFFRACTION2A69 - 86
3X-RAY DIFFRACTION3A87 - 120
4X-RAY DIFFRACTION4A121 - 186
5X-RAY DIFFRACTION5A187 - 235
6X-RAY DIFFRACTION6A236 - 268
7X-RAY DIFFRACTION7A269 - 296
8X-RAY DIFFRACTION8A297 - 375
9X-RAY DIFFRACTION9A376 - 400
10X-RAY DIFFRACTION10A401 - 445
11X-RAY DIFFRACTION11A446 - 553
12X-RAY DIFFRACTION12A554 - 584
13X-RAY DIFFRACTION13B33 - 66
14X-RAY DIFFRACTION14B67 - 81
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