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- PDB-4z0l: The murine cyclooxygenase-2 complexed with a nido-dicarbaborate-c... -

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Basic information

Entry
Database: PDB / ID: 4z0l
TitleThe murine cyclooxygenase-2 complexed with a nido-dicarbaborate-containing indomethacin derivative
ComponentsProstaglandin G/H synthase 2
KeywordsOXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR / cyclooxygenase / indomethacin / OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR complex
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
Chem-4LA / PROTOPORPHYRIN IX CONTAINING FE / Chem-N1B / Prostaglandin G/H synthase 2
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.29 Å
AuthorsXu, S. / Neumann, W. / Banerjee, S. / Hey-Hawkins, E. / Marnett, L.J.
Funding support United States, Germany, 5items
OrganizationGrant numberCountry
National Institutes of Health/National Cancer Institute (NIH/NCI)CA89450 United States
German Research Foundation (DFG) Germany
the Fonds der Chemischen Industrie Germany
the Free State of SaxonyESF-NFG 100148835 Germany
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)P41 GM103403 United States
CitationJournal: Chemmedchem / Year: 2016
Title: nido-Dicarbaborate Induces Potent and Selective Inhibition of Cyclooxygenase-2.
Authors: Neumann, W. / Xu, S. / Sarosi, M.B. / Scholz, M.S. / Crews, B.C. / Ghebreselasie, K. / Banerjee, S. / Marnett, L.J. / Hey-Hawkins, E.
History
DepositionMar 26, 2015Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jun 10, 2015Provider: repository / Type: Initial release
Revision 1.1Jul 1, 2015Group: Database references
Revision 1.2Feb 3, 2016Group: Database references
Revision 1.3Aug 23, 2017Group: Data collection / Derived calculations / Refinement description
Category: diffrn_detector / pdbx_struct_oper_list / software
Item: _diffrn_detector.detector / _pdbx_struct_oper_list.symmetry_operation
Revision 1.4Sep 6, 2017Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.5Sep 27, 2017Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.6Dec 4, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Structure summary
Category: atom_site / atom_site_anisotrop ...atom_site / atom_site_anisotrop / 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_alt_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 / _atom_site_anisotrop.U[1][1] / _atom_site_anisotrop.U[1][2] / _atom_site_anisotrop.U[1][3] / _atom_site_anisotrop.U[2][2] / _atom_site_anisotrop.U[2][3] / _atom_site_anisotrop.U[3][3] / _atom_site_anisotrop.id / _atom_site_anisotrop.pdbx_auth_asym_id / _atom_site_anisotrop.pdbx_auth_atom_id / _atom_site_anisotrop.pdbx_auth_comp_id / _atom_site_anisotrop.pdbx_auth_seq_id / _atom_site_anisotrop.pdbx_label_asym_id / _atom_site_anisotrop.pdbx_label_atom_id / _atom_site_anisotrop.pdbx_label_comp_id / _atom_site_anisotrop.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 27, 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
C: Prostaglandin G/H synthase 2
D: Prostaglandin G/H synthase 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)279,77933
Polymers269,3314
Non-polymers10,44829
Water11,746652
1
A: Prostaglandin G/H synthase 2
B: Prostaglandin G/H synthase 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)139,74316
Polymers134,6652
Non-polymers5,07814
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area10870 Å2
ΔGint-22 kcal/mol
Surface area42350 Å2
MethodPISA
2
C: Prostaglandin G/H synthase 2
D: Prostaglandin G/H synthase 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)140,03517
Polymers134,6652
Non-polymers5,37015
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11310 Å2
ΔGint-18 kcal/mol
Surface area42220 Å2
MethodPISA
Unit cell
Length a, b, c (Å)180.944, 135.011, 124.195
Angle α, β, γ (deg.)90.00, 90.00, 90.00
Int Tables number18
Space group name H-MP21212

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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 / PGHS-2 / Prostaglandin-endoperoxide synthase 2 / TIS10 protein


Mass: 67332.711 Da / Num. of mol.: 4 / Fragment: UNP residues 18-604
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 / Cell line (production host): sf21 / Production host: Spodoptera frugiperda (fall armyworm)
References: UniProt: Q05769, prostaglandin-endoperoxide synthase

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Sugars , 3 types, 17 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
#4: 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
#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.: 5 / Source method: isolated from a natural source / Formula: C14H28O6 / Comment: detergent*YM
IdentifierTypeProgram
b-octylglucosideIUPAC CARBOHYDRATE SYMBOLPDB-CARE 1.0

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Non-polymers , 4 types, 664 molecules

#3: Chemical
ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME


Mass: 616.487 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C34H32FeN4O4
#5: Chemical
ChemComp-4LA / (R)-7-{[5-methoxy-2-methyl-3-(methoxycarbonylmethyl)-1H-indolyl]carbonyl}-7,8-dicarba-nido-dodeca-hydroundecaborate


Mass: 381.586 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Formula: C16H14B9NO4
#6: Chemical
ChemComp-N1B / (S)-7-{[5-methoxy-2-methyl-3-(methoxycarbonylmethyl)-1H-indolyl]carbonyl}-7,8-dicarba-nido-dodeca-hydroundecaborate


Mass: 381.586 Da / Num. of mol.: 4 / Source method: isolated from a natural source / Formula: C16H14B9NO4
#8: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 652 / Source method: isolated from a natural source / Formula: H2O

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Experimental details

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Experiment

ExperimentMethod: X-RAY DIFFRACTION

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Sample preparation

CrystalDensity Matthews: 2.88 Å3/Da / Density % sol: 56.32 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop / pH: 8
Details: mCOX-2 protein reconstituted with a 2-fold molar excess of heme in phosphtate buffer, pH 6.7, 100 mM NaCl, 1.2% (w/v) -OG, and 0.1% NaN3, and 10-fold molar excess of inhibitors from 25 mM ...Details: mCOX-2 protein reconstituted with a 2-fold molar excess of heme in phosphtate buffer, pH 6.7, 100 mM NaCl, 1.2% (w/v) -OG, and 0.1% NaN3, and 10-fold molar excess of inhibitors from 25 mM DMSO stocks were added to protein samples. Mixing 3 uL of the protein-inhibitor complex with 3 uL crystallization solution containing 50 mM EPPS, pH 8.0, 120 mM MgCl2, 22-26% PEG MME-550 against reservoir solutions comprised of 50 mM EPPS pH 8.0, 120 mM MgCl2, 22-26% PEG MME-550

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.97918 Å
DetectorType: PSI PILATUS 6M / Detector: PIXEL / Date: Feb 5, 2014
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97918 Å / Relative weight: 1
ReflectionResolution: 2.29→50 Å / Num. obs: 135815 / % possible obs: 98.7 % / Redundancy: 4.3 % / Rmerge(I) obs: 0.0609 / Net I/σ(I): 17.7
Reflection shellResolution: 2.29→2.37 Å / Redundancy: 4.8 % / Rmerge(I) obs: 0.1949 / Mean I/σ(I) obs: 5.7 / % possible all: 91

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Processing

Software
NameVersionClassification
PHENIX1.9_1692refinement
XDSdata reduction
XDSdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 3NT1

3nt1


Resolution: 2.29→49.6 Å / SU ML: 0.3 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 32.62 / Stereochemistry target values: ML
RfactorNum. reflection% reflectionSelection details
Rfree0.25 4042 2.99 %Random selection
Rwork0.21 ---
obs0.212 135407 98.4 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.29→49.6 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17860 0 736 652 19248
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00819332
X-RAY DIFFRACTIONf_angle_d0.94626757
X-RAY DIFFRACTIONf_dihedral_angle_d11.6847091
X-RAY DIFFRACTIONf_chiral_restr0.0292749
X-RAY DIFFRACTIONf_plane_restr0.0043312
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.29-2.31320.4107980.33683373X-RAY DIFFRACTION74
2.3132-2.34140.35961430.32114538X-RAY DIFFRACTION100
2.3414-2.3710.33631280.31214537X-RAY DIFFRACTION100
2.371-2.40220.32711300.29994551X-RAY DIFFRACTION100
2.4022-2.43510.3261540.28914543X-RAY DIFFRACTION99
2.4351-2.46990.36681360.27934485X-RAY DIFFRACTION99
2.4699-2.50680.31861500.27184556X-RAY DIFFRACTION99
2.5068-2.5460.30141360.25824537X-RAY DIFFRACTION99
2.546-2.58770.32661350.2614548X-RAY DIFFRACTION99
2.5877-2.63230.35681380.26544479X-RAY DIFFRACTION99
2.6323-2.68020.27031450.25114499X-RAY DIFFRACTION99
2.6802-2.73170.27321410.24614544X-RAY DIFFRACTION99
2.7317-2.78750.2451250.24234579X-RAY DIFFRACTION100
2.7875-2.84810.31611600.24954524X-RAY DIFFRACTION100
2.8481-2.91430.31961340.25444583X-RAY DIFFRACTION100
2.9143-2.98720.28571460.24954555X-RAY DIFFRACTION100
2.9872-3.0680.30531320.24454594X-RAY DIFFRACTION99
3.068-3.15820.26691420.24214546X-RAY DIFFRACTION100
3.1582-3.26010.27771400.23264587X-RAY DIFFRACTION100
3.2601-3.37660.25031460.2364577X-RAY DIFFRACTION99
3.3766-3.51180.26531310.22014523X-RAY DIFFRACTION99
3.5118-3.67160.29421440.20414609X-RAY DIFFRACTION100
3.6716-3.86510.20451330.1794616X-RAY DIFFRACTION99
3.8651-4.10710.19461510.16984598X-RAY DIFFRACTION99
4.1071-4.42410.17551490.16154604X-RAY DIFFRACTION100
4.4241-4.86890.19661360.1584610X-RAY DIFFRACTION99
4.8689-5.57270.20231460.16544606X-RAY DIFFRACTION98
5.5727-7.01780.2461480.19234720X-RAY DIFFRACTION100
7.0178-49.61350.20821450.18074744X-RAY DIFFRACTION96
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)
12.1553-0.82030.76780.96220.26441.3963-0.0224-0.56360.10660.4175-0.08480.2002-0.22-0.20.10350.4935-0.02020.06860.79330.02290.3456118.157937.157692.3182
24.09070.593-2.34052.7342-0.68282.39430.4466-0.1480.8175-0.0203-0.05910.3985-0.3914-0.1043-0.34320.59510.03230.1950.5051-0.11490.5786111.327764.371475.8878
33.2583-0.2104-0.10330.6607-0.51481.05650.0970.1726-0.0327-0.0635-0.10520.01250.0154-0.18420.00260.2897-0.00530.00770.43360.01450.2365113.389635.934866.5657
42.7080.61780.38930.90410.84281.1657-0.01120.40030.1612-0.2020.14880.09030.0132-0.2546-0.12560.35350.04780.02490.64970.15310.3037119.883246.058441.564
52.35520.444-0.881.1508-0.42211.36530.21760.3480.57120.1285-0.03890.0627-0.2698-0.1687-0.19780.36480.06830.04820.41930.11540.3567120.717353.282662.2392
63.28143.3764-1.05465.26810.13393.3463-0.26850.57480.1138-0.5990.30880.5373-0.0323-0.994-0.02810.42570.0994-0.02811.070.18010.522999.997147.581644.2181
72.83220.16410.07231.38040.60761.59380.1219-0.25830.02840.1703-0.0850.3112-0.0847-0.5194-0.03310.30470.00180.05280.58810.08620.2736102.016739.394573.147
86.7475-0.06272.38821.1894-0.23932.2470.17540.10570.7935-0.0572-0.16420.0374-0.1376-0.20110.03070.38490.08380.10730.3460.03280.4177121.277560.324455.5835
94.0145-1.10662.24122.306-0.44342.2565-0.25140.23120.90140.29140.0011-0.1209-0.44150.52090.23040.5416-0.09980.14960.38580.05420.7775146.399766.658462.8102
102.2807-0.04610.37490.79330.13093.17910.1233-0.39760.41880.2921-0.09230.0095-0.0441-0.2054-0.06610.4106-0.11090.04470.362-0.04980.4046147.67550.490478.728
112.41120.6737-0.41221.578-0.66621.3194-0.00450.0071-0.1752-0.1358-0.0653-0.16430.13140.13320.07250.27380.0080.0040.31720.02660.2036150.649728.114767.5353
121.4850.073-0.35960.3436-0.24010.83160.0702-0.23830.06660.0468-0.1166-0.1266-0.06550.29310.03890.3179-0.0568-0.01850.46220.04410.3286154.571837.409373.9823
133.1853-2.1854-0.63093.55490.99351.1463-0.23-0.96350.0360.46950.2789-0.25950.07560.1827-0.03720.42420.0224-0.02360.91280.01180.3834158.681929.821630.2529
142.7559-0.94051.55173.18990.28771.9777-0.044-0.312-0.80470.17460.01280.13660.30520.02540.05980.5020.06830.05360.42290.23090.5852165.36162.791413.5456
152.8972-0.6254-0.35190.98570.67650.8613-0.0384-0.23560.2004-0.03430.0216-0.0075-0.08910.27080.03060.2847-0.00720.00520.35710.07580.3033163.598831.30994.5525
164.48170.6123-1.02882.1269-0.83993.4148-0.060.43840.0222-0.19820.0765-0.0282-0.13790.1263-0.010.2561-0.00970.00290.3298-0.03810.2139157.125521.5885-20.6162
172.55310.4110.79510.44030.20071.16750.0306-0.022-0.27460.0535-0.01070.11920.19720.0622-0.03330.32010.02180.01280.29170.0410.385156.134414.1154-0.0383
184.36754.16022.74385.69330.04355.9224-0.12290.8404-0.3773-0.52130.3308-0.5382-0.08570.8621-0.18950.3480.01250.07020.6673-0.07490.413176.921619.8757-17.909
192.2006-0.0005-0.3171.0916-0.14611.81-0.0122-0.4692-0.01730.14860.0562-0.1410.02870.4255-0.04260.26330.0225-0.00930.49310.0210.3301174.9127.67511.1428
205.4717-0.4374-1.47071.17470.79211.8934-0.21760.0829-0.95570.0227-0.03870.13930.2990.25080.27390.38670.0670.03840.25720.0590.4466155.55517.1983-6.7971
213.7531-1.2198-1.59972.78610.05451.2352-0.38520.2011-0.87890.30060.08510.27820.4756-0.29340.24120.4257-0.04780.07440.2856-0.01380.6978130.24091.02030.2157
221.68080.1012-0.84790.022-0.10582.4974-0.0726-0.2118-0.40770.2008-0.17180.0739-0.1142-0.11830.30040.3848-0.01110.05760.33480.10340.4348129.03616.971716.388
233.7784-0.9394-0.49041.44210.52171.16440.04320.7109-0.4998-0.1877-0.11140.35920.0403-0.31080.0660.3569-0.01710.0210.4385-0.05670.4522119.57519.3904-8.9089
242.26820.69640.44080.85490.87660.97410.0474-0.02070.1219-0.0338-0.02780.0903-0.1866-0.0699-0.00210.26910.04390.01920.23130.00390.3644127.778141.95888.1037
255.7460.99911.88941.7161-0.13527.563-0.217-0.00520.5393-0.11170.00990.1805-0.4392-0.13220.2650.29030.03570.00720.1864-0.03440.4252128.932949.477610.8407
261.88770.10860.16210.70560.31491.0814-0.0352-0.16170.02360.034-0.04140.1967-0.0049-0.17970.07830.23960.00060.03710.29730.00970.3114121.578531.455411.1727
271.34060.1435-0.13980.81740.43151.4631-0.0154-0.2183-0.10060.0789-0.11380.19720.0953-0.22250.09740.2550.01660.01460.24460.05220.3429123.621228.123412.6907
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN A AND RESID 33:85 )A33 - 85
2X-RAY DIFFRACTION2( CHAIN A AND RESID 86:120 )A86 - 120
3X-RAY DIFFRACTION3( CHAIN A AND RESID 121:237 )A121 - 237
4X-RAY DIFFRACTION4( CHAIN A AND RESID 238:319 )A238 - 319
5X-RAY DIFFRACTION5( CHAIN A AND RESID 320:390 )A320 - 390
6X-RAY DIFFRACTION6( CHAIN A AND RESID 391:428 )A391 - 428
7X-RAY DIFFRACTION7( CHAIN A AND RESID 429:534 )A429 - 534
8X-RAY DIFFRACTION8( CHAIN A AND RESID 535:582 )A535 - 582
9X-RAY DIFFRACTION9( CHAIN B AND RESID 33:85 )B33 - 85
10X-RAY DIFFRACTION10( CHAIN B AND RESID 86:143 )B86 - 143
11X-RAY DIFFRACTION11( CHAIN B AND RESID 144:319 )B144 - 319
12X-RAY DIFFRACTION12( CHAIN B AND RESID 320:582 )B320 - 582
13X-RAY DIFFRACTION13( CHAIN C AND RESID 33:85 )C33 - 85
14X-RAY DIFFRACTION14( CHAIN C AND RESID 86:120 )C86 - 120
15X-RAY DIFFRACTION15( CHAIN C AND RESID 121:237 )C121 - 237
16X-RAY DIFFRACTION16( CHAIN C AND RESID 238:319 )C238 - 319
17X-RAY DIFFRACTION17( CHAIN C AND RESID 320:390 )C320 - 390
18X-RAY DIFFRACTION18( CHAIN C AND RESID 391:428 )C391 - 428
19X-RAY DIFFRACTION19( CHAIN C AND RESID 429:534 )C429 - 534
20X-RAY DIFFRACTION20( CHAIN C AND RESID 535:582 )C535 - 582
21X-RAY DIFFRACTION21( CHAIN D AND RESID 33:85 )D33 - 85
22X-RAY DIFFRACTION22( CHAIN D AND RESID 86:143 )D86 - 143
23X-RAY DIFFRACTION23( CHAIN D AND RESID 144:181 )D144 - 181
24X-RAY DIFFRACTION24( CHAIN D AND RESID 182:269 )D182 - 269
25X-RAY DIFFRACTION25( CHAIN D AND RESID 270:319 )D270 - 319
26X-RAY DIFFRACTION26( CHAIN D AND RESID 320:485 )D320 - 485
27X-RAY DIFFRACTION27( CHAIN D AND RESID 486:582 )D486 - 582

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