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- PDB-6bl3: Crystal Complex of Cyclooxygenase-2 with indomethacin-butyldiamin... -

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Basic information

Entry
Database: PDB / ID: 6bl3
TitleCrystal Complex of Cyclooxygenase-2 with indomethacin-butyldiamine-dansyl conjugate
ComponentsProstaglandin G/H synthase 2Cyclooxygenase
KeywordsOXIDOREDUCTASE/INHIBITOR / cyclooxygenase-2 / fluorescent inhibitor complex / 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 / cellular response to homocysteine / hair cycle / 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 / cellular response to homocysteine / hair cycle / 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 / oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen / response to fatty acid / positive regulation of smooth muscle contraction / cyclooxygenase pathway / 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 / nuclear inner membrane / prostaglandin biosynthetic process / 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 / embryo implantation / positive regulation of brown fat cell differentiation / positive regulation of synaptic transmission, glutamatergic / learning / response to cytokine / caveola / positive regulation of smooth muscle cell proliferation / peroxidase activity / negative regulation of cysteine-type endopeptidase activity involved in apoptotic process / 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 / cellular response to heat / regulation of cell population proliferation / cellular response to hypoxia / angiogenesis / response to oxidative stress / response to lipopolysaccharide / neuron projection / response to xenobiotic stimulus / 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
PROTOPORPHYRIN IX CONTAINING FE / Chem-L7M / Prostaglandin G/H synthase 2
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.217 Å
AuthorsXu, S. / Uddin, M.J. / Banerjee, S. / Marnett, L.J.
CitationJournal: J.Biol.Chem. / Year: 2019
Title: Fluorescent indomethacin-dansyl conjugates utilize the membrane-binding domain of cyclooxygenase-2 to block the opening to the active site.
Authors: Xu, S. / Uddin, M.J. / Banerjee, S. / Duggan, K. / Musee, J. / Kiefer, J.R. / Ghebreselasie, K. / Rouzer, C.A. / Marnett, L.J.
History
DepositionNov 9, 2017Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 14, 2018Provider: repository / Type: Initial release
Revision 1.1Mar 13, 2019Group: Data collection / Category: diffrn_detector / Item: _diffrn_detector.detector / _diffrn_detector.type
Revision 1.2May 15, 2019Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.3Jun 12, 2019Group: Data collection / Database references / Category: citation / citation_author
Item: _citation.journal_volume / _citation.page_first ..._citation.journal_volume / _citation.page_first / _citation.page_last / _citation_author.identifier_ORCID
Revision 2.0Jul 29, 2020Group: Atomic model / Data collection ...Atomic model / Data collection / Derived calculations / Refinement description / 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 / pdbx_struct_conn_angle / refine_hist / 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_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_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 / _refine_hist.d_res_low / _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 2.1Oct 4, 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)279,66330
Polymers269,3314
Non-polymers10,33226
Water15,421856
1
A: Prostaglandin G/H synthase 2
B: Prostaglandin G/H synthase 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)139,83215
Polymers134,6652
Non-polymers5,16613
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11350 Å2
ΔGint-14 kcal/mol
Surface area41870 Å2
MethodPISA
2
C: Prostaglandin G/H synthase 2
D: Prostaglandin G/H synthase 2
hetero molecules


Theoretical massNumber of molelcules
Total (without water)139,83215
Polymers134,6652
Non-polymers5,16613
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area11310 Å2
ΔGint-17 kcal/mol
Surface area41890 Å2
MethodPISA
Unit cell
Length a, b, c (Å)215.474, 121.776, 134.800
Angle α, β, γ (deg.)90.00, 123.48, 90.00
Int Tables number5
Space group name H-MC121

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Components

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Protein , 1 types, 4 molecules ABCD

#1: Protein
Prostaglandin G/H synthase 2 / Cyclooxygenase / 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
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Ptgs2, Cox-2, Cox2, Pghs-b, Tis10 / Production host: Spodoptera frugiperda (fall armyworm)
References: UniProt: Q05769, prostaglandin-endoperoxide synthase

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Sugars , 3 types, 18 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
#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 / N-Acetylglucosamine


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
#6: Sugar
ChemComp-BOG / octyl beta-D-glucopyranoside / Beta-Octylglucoside / octyl beta-D-glucoside / octyl D-glucoside / octyl 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

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Non-polymers , 3 types, 864 molecules

#4: Chemical
ChemComp-HEM / PROTOPORPHYRIN IX CONTAINING FE / HEME / Heme B


Mass: 616.487 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C34H32FeN4O4
#5: Chemical
ChemComp-L7M / 2-[1-(4-chlorobenzene-1-carbonyl)-5-methoxy-2-methyl-1H-indol-3-yl]-N-[4-({[5-(dimethylamino)naphthalen-1-yl]sulfonyl}amino)butyl]acetamide


Mass: 661.210 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C35H37ClN4O5S
#7: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 856 / 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: 2.74 Å3/Da / Density % sol: 55.08 %
Crystal growTemperature: 291 K / Method: evaporation / pH: 6.7
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, VAPOR DIFFUSION, HANGING DROP, temperature 291K

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Data collection

DiffractionMean temperature: 100 K
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-C / Wavelength: 0.97918 Å
DetectorType: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Oct 19, 2017
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97918 Å / Relative weight: 1
ReflectionResolution: 2.217→103.3 Å / Num. obs: 141148 / % possible obs: 97.83 % / Observed criterion σ(F): 1.34 / Redundancy: 3.4 % / CC1/2: 0.989 / Rmerge(I) obs: 0.1535 / Rpim(I) all: 0.0977 / Rrim(I) all: 0.1826 / Net I/σ(I): 5.97
Reflection shellResolution: 2.217→2.296 Å / Rmerge(I) obs: 1.424 / Num. unique obs: 13090 / CC1/2: 0.458 / Rpim(I) all: 0.9065

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Processing

Software
NameVersionClassification
PHENIX(1.12_2829: ???)refinement
XDSdata reduction
Aimlessdata scaling
PHASERphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 3NT1

3nt1


Resolution: 2.217→112.436 Å / SU ML: 0.3 / Phase error: 25.86 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2287 4220 3 %
Rwork0.2047 --
obs0.2054 140568 97.79 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Refinement stepCycle: LAST / Resolution: 2.217→112.436 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms17896 0 700 856 19452
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00319164
X-RAY DIFFRACTIONf_angle_d0.78326089
X-RAY DIFFRACTIONf_dihedral_angle_d17.14211315
X-RAY DIFFRACTIONf_chiral_restr0.0492753
X-RAY DIFFRACTIONf_plane_restr0.0053320
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.2168-2.2420.40391150.33783722X-RAY DIFFRACTION80
2.242-2.26840.32961320.31634394X-RAY DIFFRACTION95
2.2684-2.29610.31481500.28924531X-RAY DIFFRACTION98
2.2961-2.32510.31051440.27854544X-RAY DIFFRACTION98
2.3251-2.35570.3231290.27274561X-RAY DIFFRACTION99
2.3557-2.3880.30961520.26234600X-RAY DIFFRACTION99
2.388-2.42210.30971410.25374574X-RAY DIFFRACTION99
2.4221-2.45830.26781430.24884584X-RAY DIFFRACTION99
2.4583-2.49670.27731350.23734608X-RAY DIFFRACTION99
2.4967-2.53760.24231420.23024540X-RAY DIFFRACTION99
2.5376-2.58140.25891460.22994558X-RAY DIFFRACTION98
2.5814-2.62830.25011440.22854593X-RAY DIFFRACTION99
2.6283-2.67890.24381430.23284561X-RAY DIFFRACTION99
2.6789-2.73360.27151420.23424581X-RAY DIFFRACTION99
2.7336-2.7930.28121420.23554632X-RAY DIFFRACTION99
2.793-2.8580.27791390.23114604X-RAY DIFFRACTION99
2.858-2.92950.28521420.23094605X-RAY DIFFRACTION99
2.9295-3.00870.2721430.22674584X-RAY DIFFRACTION99
3.0087-3.09720.25991450.22514557X-RAY DIFFRACTION98
3.0972-3.19720.28231370.21974548X-RAY DIFFRACTION98
3.1972-3.31150.26831380.22154593X-RAY DIFFRACTION99
3.3115-3.44410.23771470.20424582X-RAY DIFFRACTION99
3.4441-3.60090.21431380.18554572X-RAY DIFFRACTION99
3.6009-3.79070.20271430.17594608X-RAY DIFFRACTION99
3.7907-4.02820.18451450.17254561X-RAY DIFFRACTION98
4.0282-4.33920.18351410.16364559X-RAY DIFFRACTION98
4.3392-4.77590.14331500.15554579X-RAY DIFFRACTION98
4.7759-5.4670.16261360.16454576X-RAY DIFFRACTION98
5.467-6.88770.24431350.20054598X-RAY DIFFRACTION98
6.8877-112.58120.20421410.19624639X-RAY DIFFRACTION97
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)
10.58740.070.65820.9889-0.36171.8385-0.18240.01440.32060.2548-0.09280.1385-0.6470.06810.29060.50020.0124-0.09950.3119-0.04760.5164-42.7338-5.080623.5472
21.19090.2414-0.85270.5352-0.51122.69750.0191-0.09910.5910.175-0.04820.0681-0.5596-0.0880.10630.37050.0146-0.05640.3878-0.0360.4035-49.5776-16.611421.3087
30.77420.13960.37050.8501-0.04990.66320.00140.026-0.05830.0125-0.0459-0.16070.02880.09480.04250.25680.00340.01930.26740.02440.2026-40.1665-38.68920.1033
41.09910.06530.29290.5882-0.14250.8222-0.0164-0.17430.04150.1549-0.0229-0.0714-0.05410.03690.05570.2751-0.0046-0.01050.2551-0.0010.207-41.1983-30.038228.9457
51.0271-0.44050.52341.0582-0.77781.22170.0044-0.37370.00920.08660.13880.3452-0.2244-0.4381-0.16220.4030.07550.06950.5624-0.01260.427-80.9755-22.305114.7893
60.38060.01670.03941.9465-0.80910.5340.044-0.24310.26250.3665-0.05480.2291-0.1336-0.30210.02990.37130.00860.00440.4566-0.030.4182-68.5294-19.735810.0495
70.314-0.16810.36320.3570.02910.63920.1368-0.0859-0.148-0.0510.07070.2730.3369-0.3039-0.17720.3267-0.0726-0.03990.39060.11060.388-75.1009-39.58081.3829
80.67550.22350.12590.729-0.06860.61470.01370.15120.0561-0.1853-0.01350.02960.09350.0631-0.0030.3378-0.01170.00660.29620.05470.2527-57.2998-23.4384-13.221
91.2163-0.15970.18751.25140.04721.4307-0.26670.4495-0.0856-0.56420.2288-0.1095-0.03470.2393-0.0090.3865-0.02550.03940.33280.02250.2749-51.7341-20.8768-18.4671
100.94920.2480.50580.8851-0.28590.9531-0.06680.00880.0967-0.14380.06510.1735-0.0381-0.1424-0.01790.27970.0127-0.0180.25580.0270.2812-68.9457-18.9319-7.5073
111.95840.2059-0.01330.9591-0.22280.69630.1419-0.1736-0.6681-0.1242-0.0613-0.30650.18880.1997-0.19590.47690.0508-0.10940.3399-0.08120.589142.0109-57.240961.8715
122.36450.3345-1.21170.5697-0.43111.4678-0.01110.2092-0.4703-0.0442-0.1303-0.26270.3010.001-0.14950.38290.0415-0.05390.361-0.04740.417138.267-45.685155.7528
130.89720.28960.23860.9063-0.14290.57710.0112-0.0449-0.00880.18-0.0371-0.1379-0.0730.0380.01520.2789-0.0076-0.03670.2648-0.01050.271739.1987-23.65165.2833
141.01430.15220.41720.7281-0.10130.84990.00720.0774-0.10090.1005-0.0319-0.2971-0.03650.1955-0.02290.266-0.0003-0.04190.2994-0.01110.357647.5756-32.273862.2471
151.59720.6137-0.24990.3566-0.00410.6435-0.18890.6223-0.1931-0.30030.0546-0.0124-0.01120.2690.04950.4341-0.0380.05550.6743-0.04410.344927.823-34.360325.373
160.507-0.39270.57151.3303-0.19690.91370.01430.1813-0.3712-0.23180.2195-0.44170.40010.29780.10190.55450.0668-0.01180.5462-0.17560.445317.4959-58.599535.4308
170.79960.36010.41670.42340.1860.3788-0.2220.35080.3764-0.16310.1114-0.00190.0070.06590.05640.3322-0.0609-0.00690.41160.09280.258416.1591-23.94137.2561
180.63630.06540.2520.5843-0.34790.78540.0058-0.0510.12430.0831-0.04130.089-0.0221-0.1024-0.06860.2873-0.01410.03690.2805-0.01290.26332.9317-38.9655.992
191.53-0.02610.10411.4589-0.22721.01610.0251-0.0954-0.02090.15270.11780.12650.045-0.3406-0.00570.2804-0.00840.04560.2475-0.00080.2565-0.9312-41.581962.5877
201.26810.20160.34070.8134-0.19080.5382-0.00170.2156-0.0894-0.09220.10180.0540.077-0.0154-0.02420.2744-0.00680.01040.279-0.040.23145.8834-43.365343.3151
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection details
1X-RAY DIFFRACTION1chain 'A' and (resid 33 through 105A)
2X-RAY DIFFRACTION2chain 'A' and (resid 106 through 138 )
3X-RAY DIFFRACTION3chain 'A' and (resid 139 through 319 )
4X-RAY DIFFRACTION4chain 'A' and (resid 320 through 583 )
5X-RAY DIFFRACTION5chain 'B' and (resid 33 through 105A)
6X-RAY DIFFRACTION6chain 'B' and (resid 106 through 138 )
7X-RAY DIFFRACTION7chain 'B' and (resid 139 through 181 )
8X-RAY DIFFRACTION8chain 'B' and (resid 182 through 269 )
9X-RAY DIFFRACTION9chain 'B' and (resid 270 through 319 )
10X-RAY DIFFRACTION10chain 'B' and (resid 320 through 583 )
11X-RAY DIFFRACTION11chain 'C' and (resid 33 through 105A)
12X-RAY DIFFRACTION12chain 'C' and (resid 106 through 138 )
13X-RAY DIFFRACTION13chain 'C' and (resid 139 through 319 )
14X-RAY DIFFRACTION14chain 'C' and (resid 320 through 583 )
15X-RAY DIFFRACTION15chain 'D' and (resid 33 through 93 )
16X-RAY DIFFRACTION16chain 'D' and (resid 94 through 123 )
17X-RAY DIFFRACTION17chain 'D' and (resid 124 through 181 )
18X-RAY DIFFRACTION18chain 'D' and (resid 182 through 269 )
19X-RAY DIFFRACTION19chain 'D' and (resid 270 through 319 )
20X-RAY DIFFRACTION20chain 'D' and (resid 320 through 583 )

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