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- PDB-4ezk: Potent and Selective Inhibitors of PI3K-delta: Obtaining Isoform ... -

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Basic information

Entry
Database: PDB / ID: 4ezk
TitlePotent and Selective Inhibitors of PI3K-delta: Obtaining Isoform Selectivity from the Affinity Pocket and Tryptophan Shelf
ComponentsPhosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
KeywordsTRANSFERASE/TRANSFERASE INHIBITOR / kinase p110 / p110-gamma / lipid kinase / cytoplasmic / TRANSFERASE-TRANSFERASE INHIBITOR complex
Function / homology
Function and homology information


negative regulation of triglyceride catabolic process / secretory granule localization / natural killer cell chemotaxis / neutrophil extravasation / phosphatidylinositol-4-phosphate 3-kinase / positive regulation of acute inflammatory response / respiratory burst involved in defense response / negative regulation of cardiac muscle contraction / regulation of calcium ion transmembrane transport / T cell chemotaxis ...negative regulation of triglyceride catabolic process / secretory granule localization / natural killer cell chemotaxis / neutrophil extravasation / phosphatidylinositol-4-phosphate 3-kinase / positive regulation of acute inflammatory response / respiratory burst involved in defense response / negative regulation of cardiac muscle contraction / regulation of calcium ion transmembrane transport / T cell chemotaxis / negative regulation of fibroblast apoptotic process / phosphatidylinositol 3-kinase complex, class IB / sphingosine-1-phosphate receptor signaling pathway / phosphatidylinositol 3-kinase complex, class IA / dendritic cell chemotaxis / 1-phosphatidylinositol-4-phosphate 3-kinase activity / 1-phosphatidylinositol-4,5-bisphosphate 3-kinase activity / phosphatidylinositol-4,5-bisphosphate 3-kinase / phosphatidylinositol 3-kinase / phosphatidylinositol-3-phosphate biosynthetic process / 1-phosphatidylinositol-3-kinase activity / Erythropoietin activates Phosphoinositide-3-kinase (PI3K) / mast cell degranulation / hepatocyte apoptotic process / positive regulation of Rac protein signal transduction / regulation of cell adhesion mediated by integrin / Synthesis of PIPs at the plasma membrane / phosphatidylinositol-mediated signaling / phosphatidylinositol phosphate biosynthetic process / regulation of angiogenesis / phosphorylation / T cell proliferation / cellular response to cAMP / GPVI-mediated activation cascade / ephrin receptor binding / neutrophil chemotaxis / phosphatidylinositol 3-kinase/protein kinase B signal transduction / positive regulation of endothelial cell migration / T cell activation / positive regulation of cytokine production / positive regulation of MAP kinase activity / platelet aggregation / endocytosis / G beta:gamma signalling through PI3Kgamma / kinase activity / phospholipase C-activating G protein-coupled receptor signaling pathway / positive regulation of cytosolic calcium ion concentration / angiogenesis / adaptive immune response / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / non-specific serine/threonine protein kinase / protein kinase activity / inflammatory response / immune response / G protein-coupled receptor signaling pathway / innate immune response / protein serine kinase activity / protein serine/threonine kinase activity / ATP binding / identical protein binding / membrane / plasma membrane / cytosol / cytoplasm
Similarity search - Function
PIK3 catalytic subunit gamma, adaptor-binding domain / PIK3 catalytic subunit gamma adaptor-binding domain / Phosphatidylinositol 3-/4-kinase, catalytic domain / Phosphatidylinositol 3-kinase, accessory domain (PIK) / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 4 / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 4 / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, Domain 5 / C2 domain / Phosphatidylinositol 3-kinase, adaptor-binding domain / Phosphatidylinositol 3-kinase adaptor-binding (PI3K ABD) domain profile. ...PIK3 catalytic subunit gamma, adaptor-binding domain / PIK3 catalytic subunit gamma adaptor-binding domain / Phosphatidylinositol 3-/4-kinase, catalytic domain / Phosphatidylinositol 3-kinase, accessory domain (PIK) / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 4 / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 4 / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, Domain 5 / C2 domain / Phosphatidylinositol 3-kinase, adaptor-binding domain / Phosphatidylinositol 3-kinase adaptor-binding (PI3K ABD) domain profile. / PI3-kinase family, Ras-binding domain / Phosphatidylinositol 3-kinase Ras-binding (PI3K RBD) domain / PI3-kinase family, ras-binding domain / Phosphatidylinositol 3-kinase Ras-binding (PI3K RBD) domain profile. / C2 phosphatidylinositol 3-kinase-type domain / Phosphoinositide 3-kinase C2 / C2 phosphatidylinositol 3-kinase (PI3K)-type domain profile. / Phosphoinositide 3-kinase, region postulated to contain C2 domain / Phosphoinositide 3-kinase family, accessory domain (PIK domain) / Phosphoinositide 3-kinase family, accessory domain (PIK domain) / Phosphoinositide 3-kinase, accessory (PIK) domain superfamily / Phosphoinositide 3-kinase, accessory (PIK) domain / Phosphatidylinositol kinase / PIK helical domain profile. / Phosphatidylinositol 3- and 4-kinases signature 1. / Phosphatidylinositol 3- and 4-kinases signature 2. / Phosphatidylinositol 3/4-kinase, conserved site / Phosphatidylinositol 3-/4-kinase, catalytic domain superfamily / Phosphoinositide 3-kinase, catalytic domain / Phosphatidylinositol 3- and 4-kinases catalytic domain profile. / Phosphatidylinositol 3-/4-kinase, catalytic domain / Phosphatidylinositol 3- and 4-kinase / Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1 / C2 domain superfamily / Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat / Ubiquitin-like (UB roll) / Alpha Horseshoe / Armadillo-type fold / Ubiquitin-like domain superfamily / Roll / Protein kinase-like domain superfamily / Immunoglobulin-like / Sandwich / 2-Layer Sandwich / Orthogonal Bundle / Mainly Beta / Mainly Alpha / Alpha Beta
Similarity search - Domain/homology
Chem-0SD / Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 2.803 Å
AuthorsMurray, J.M.
CitationJournal: Bioorg.Med.Chem.Lett. / Year: 2012
Title: Potent and selective inhibitors of PI3K-delta: obtaining isoform selectivity from the affinity pocket and tryptophan shelf
Authors: Sutherlin, D.P. / Baker, S. / Bisconte, A. / Blaney, P.M. / Brown, A. / Chan, B.K. / Chantry, D. / Castanedo, G. / DePledge, P. / Goldsmith, P. / Goldstein, D.M. / Hancox, T. / Kaur, J. / ...Authors: Sutherlin, D.P. / Baker, S. / Bisconte, A. / Blaney, P.M. / Brown, A. / Chan, B.K. / Chantry, D. / Castanedo, G. / DePledge, P. / Goldsmith, P. / Goldstein, D.M. / Hancox, T. / Kaur, J. / Knowles, D. / Kondru, R. / Lesnick, J. / Lucas, M.C. / Lewis, C. / Murray, J. / Nadin, A.J. / Nonomiya, J. / Pang, J. / Pegg, N. / Price, S. / Reif, K. / Safina, B.S. / Salphati, L. / Staben, S. / Seward, E.M. / Shuttleworth, S. / Sohal, S. / Sweeney, Z.K. / Ultsch, M. / Waszkowycz, B. / Wei, B.
History
DepositionMay 2, 2012Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 17, 2013Provider: repository / Type: Initial release
Revision 1.1Sep 13, 2023Group: Data collection / Database references ...Data collection / Database references / Derived calculations / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / pdbx_initial_refinement_model / struct_ref_seq_dif / struct_site
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _struct_ref_seq_dif.details / _struct_site.pdbx_auth_asym_id / _struct_site.pdbx_auth_comp_id / _struct_site.pdbx_auth_seq_id

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform
hetero molecules


Theoretical massNumber of molelcules
Total (without water)111,1872
Polymers110,6991
Non-polymers4881
Water21612
1


  • Idetical with deposited unit
  • defined by author&software
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA
Unit cell
Length a, b, c (Å)140.730, 67.190, 106.020
Angle α, β, γ (deg.)90.00, 96.76, 90.00
Int Tables number5
Space group name H-MC121

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Components

#1: Protein Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit gamma isoform / PI3-kinase subunit gamma / PI3K-gamma / PI3Kgamma / PtdIns-3-kinase subunit gamma / ...PI3-kinase subunit gamma / PI3K-gamma / PI3Kgamma / PtdIns-3-kinase subunit gamma / Phosphatidylinositol 4 / 5-bisphosphate 3-kinase 110 kDa catalytic subunit gamma / PtdIns-3-kinase subunit p110-gamma / p110gamma / Phosphoinositide-3-kinase catalytic gamma polypeptide / Serine/threonine protein kinase PIK3CG / p120-PI3K


Mass: 110699.023 Da / Num. of mol.: 1 / Fragment: UNP residues 144-1102 / Mutation: K802T
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PIK3CG / Cell line (production host): Sf9 / Production host: Spodoptera frugiperda (fall armyworm)
References: UniProt: P48736, phosphatidylinositol-4,5-bisphosphate 3-kinase, non-specific serine/threonine protein kinase
#2: Chemical ChemComp-0SD / 2-(1-{[2-(2H-indazol-4-yl)-4-(morpholin-4-yl)pyrido[3,2-d]pyrimidin-6-yl]methyl}piperidin-4-yl)propan-2-ol


Mass: 487.597 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C27H33N7O2
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 12 / 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: 2.25 Å3/Da / Density % sol: 45.28 %
Crystal growTemperature: 289 K / Method: vapor diffusion, hanging drop / pH: 8.5
Details: PEG 3350, 0.2M NH4SO4, 0.1M Tris-HCl 8.5, vapor diffusion, hanging drop, temperature 289K

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Data collection

Diffraction sourceSource: SYNCHROTRON / Site: ALS / Beamline: 5.0.2 / Wavelength: 1 Å
DetectorType: ADSC QUANTUM 315 / Detector: CCD / Date: Dec 1, 2011
RadiationProtocol: SINGLE / Scattering type: x-ray
Radiation wavelengthWavelength: 1 Å / Relative weight: 1
ReflectionResolution: 2.8→34.392 Å / % possible obs: 95.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.2 % / Biso Wilson estimate: 85 Å2 / Rsym value: 0.046 / Net I/σ(I): 22.5
Reflection shell
Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsRsym valueDiffraction-ID% possible all
2.8-2.953.20.3312.10.331191
2.95-3.133.20.2133.40.213192.5
3.13-3.353.10.1453.80.145194.7
3.35-3.623.10.08280.082197.5
3.62-3.963.20.05911.10.059198.2
3.96-4.433.30.04514.10.045198.6
4.43-5.123.20.04114.20.041197.9
5.12-6.2730.068.70.06194.9
6.27-8.863.40.02718.90.027199.5
8.86-34.3923.40.018320.018196.8

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Phasing

PhasingMethod: molecular replacement

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Processing

Software
NameVersionClassificationNB
SCALA3.3.20data scaling
PHASERphasing
PHENIX1.8_1066refinement
PDB_EXTRACT3.11data extraction
XSCALEdata scaling
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: PDB ENTRY 1E8X

1e8x


Resolution: 2.803→34.392 Å / Occupancy max: 1 / Occupancy min: 0.1 / SU ML: 0.42 / σ(F): 1.34 / Phase error: 30.18 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2533 1202 5.16 %
Rwork0.2432 --
obs0.2437 23292 95.51 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 120.2513 Å2
Baniso -1Baniso -2Baniso -3
1--11.2848 Å20 Å27.946 Å2
2--0.4702 Å20 Å2
3---10.8146 Å2
Refinement stepCycle: LAST / Resolution: 2.803→34.392 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms6818 0 36 12 6866
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0097005
X-RAY DIFFRACTIONf_angle_d1.4639482
X-RAY DIFFRACTIONf_dihedral_angle_d19.2052635
X-RAY DIFFRACTIONf_chiral_restr0.0941064
X-RAY DIFFRACTIONf_plane_restr0.0061225
LS refinement shell
Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkRefine-ID% reflection obs (%)
2.8029-2.91510.38291360.35042281X-RAY DIFFRACTION91
2.9151-3.04770.32861340.32342355X-RAY DIFFRACTION92
3.0477-3.20820.33191280.3192372X-RAY DIFFRACTION93
3.2082-3.40910.35531180.30972452X-RAY DIFFRACTION96
3.4091-3.6720.30871420.27722481X-RAY DIFFRACTION98
3.672-4.0410.26481270.25062535X-RAY DIFFRACTION98
4.041-4.62460.20981530.21872525X-RAY DIFFRACTION99
4.6246-5.82190.22481350.21152490X-RAY DIFFRACTION97
5.8219-34.39460.19981290.20212599X-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)
11.0835-0.36250.14725.25121.91294.82670.33622.2953-2.8145-1.1769-0.37510.35571.92320.4689-0.6131.14780.2177-0.2051.6592-0.85231.728427.0745-37.94733.8396
25.0575-1.2515-0.73630.79931.02171.52990.65482.416-1.8291-0.4682-0.1361-0.1990.44521.4014-0.57290.97040.2025-0.02781.5485-0.7291.0742.5006-33.07926.0641
33.50421.21611.25082.8157-0.93642.03730.68390.9782-2.05690.0218-0.01460.2671.52210.4465-0.15471.07490.5435-0.28380.2526-0.67211.809836.5006-42.328216.7985
46.3073-1.07061.6680.7073-0.38664.15430.3531-0.6529-1.36810.5581-0.07440.05530.6613-0.8251-0.57850.8532-0.1878-0.03180.95960.47831.345417.7827-35.84132.4349
51.94562.6199-0.64466.56420.60297.4404-0.4331-2.846-0.22240.86090.12850.7768-0.2079-2.4531-0.04751.96610.14720.41032.0914-0.48481.840912.7584-19.641248.4595
63.5624-1.2931-0.54431.5375-1.29992.18440.5439-2.2078-1.3920.3941-0.04641.14650.7365-1.8055-0.30340.9301-0.2160.47672.35440.7391.7015-0.7808-31.92940.1186
72.36130.3797-0.45780.64311.03412.21020.4273-1.0716-2.34090.5343-0.18330.92831.9213-1.5939-0.27291.1304-0.5724-0.06611.6750.30731.95021.5771-38.765429.8596
87.95-1.9363.94512.4778-0.58488.84460.4815-1.0728-1.85330.57510.13410.69691.2597-1.2872-0.45190.683-0.24940.04531.07750.26761.2399.9123-32.333631.7202
97.134-1.40971.83254.2192-0.72377.16670.1232-1.6684-0.99720.73440.48160.297-0.3157-0.9996-0.1790.9955-0.13790.30541.70550.6161.173811.8601-25.190638.8325
108.44125.6757.73013.82085.22877.3552-0.0727-1.8421-0.13520.09750.18280.8217-0.5194-1.94310.08210.89740.2460.04551.78180.19251.854.3185-20.126736.2238
117.2898-1.99910.4852.62011.19583.74520.2098-0.5338-2.7250.2733-0.16470.88360.6747-1.9837-0.37320.9067-0.2098-0.06071.63480.27771.83843.5988-36.922425.8723
123.233-0.35993.3953.5758-1.37393.84410.38761.0352-2.8027-0.27370.11070.24421.7222-0.0186-0.59781.3146-0.0765-0.32770.9641-0.08681.908118.3151-44.382714.5951
133.0683-0.4996-0.83541.8149-1.09193.28740.07560.6772-1.01670.11330.1107-0.37870.97561.96740.4011-0.24510.7540.44563.1074-0.75410.995367.7046-30.785312.6048
147.8020.0701-1.18661.88482.51676.04540.00421.89262.0385-0.5151-0.94290.001-0.94710.6442-0.21591.1905-0.70170.21022.71680.48531.972259.835-7.78042.584
152.89610.1422-0.47050.1897-0.31954.18940.36482.3285-0.0732-0.32770.3892-0.2161-0.02292.7221-0.0060.49470.02770.21142.3884-0.18160.832664.8756-24.221916.1701
162.00720.9950.36874.6363-1.19158.755-0.24152.23561.1065-0.5772-0.0901-0.7485-0.41842.3469-0.1670.6571-0.17320.13522.3034-0.28710.886159.426-19.304214.9545
176.7905-0.46651.45881.09190.63666.15680.25891.8038-0.4398-0.6055-0.517-0.367-0.35731.48-0.16570.71960.50080.36011.8304-0.10220.50855.2771-23.218314.241
185.1585-2.262-1.52692.4893-1.46473.49950.85431.5324-2.0458-0.0438-0.06190.04621.44941.564-0.72690.86730.505-0.00631.1101-0.60152.042752.4103-41.921617.4965
191.4539-0.6231-0.50413.9968-2.64683.98230.16951.367-0.6714-0.4-0.6708-0.23130.98361.1066-0.58720.84640.43310.09952.9034-0.89780.417857.876-31.69688.4078
209.520.22342.40467.79214.51287.4902-0.22741.92031.8287-0.5517-0.0486-0.5184-1.56071.6940.02481.0086-0.16930.27091.42020.14581.095249.5509-13.830411.5373
216.70080.21563.46525.00821.42189.1893-0.16830.93070.7646-0.16270.0431-0.6748-1.36071.7941-0.03930.8733-0.15540.27511.4776-0.21330.789548.8505-18.507520.6866
227.4448-0.62931.07975.87740.98224.61590.37042.2017-0.9211-0.5298-0.0481-0.2170.50811.7565-0.24530.57710.124-0.15641.3097-0.25530.530348.4887-25.336811.2581
235.92613.6256-2.4469.6825-4.19611.98620.40343.3591-0.0061-1.2361-0.2538-0.5139-0.22582.1618-0.15241.1466-0.07480.02592.405-0.3311.066747.6972-20.69930.1257
244.257-4.24982.84754.8279-1.80263.75290.57722.70320.1062-0.41-0.1342-0.2061-0.09371.8215-0.32240.7623-0.1340.07032.6032-0.27860.931257.1972-21.49084.3995
251.49880.10780.67292.3133-1.47841.31170.0951.1893-0.7085-0.1486-0.0226-0.1460.85411.58510.3670.81610.93460.73042.9477-0.47750.568365.0247-34.651510.3311
268.8303-2.76062.82835.1857-0.84246.7084-0.3075-1.7578-1.31520.63320.3937-0.77510.44350.8014-0.3720.68640.07760.1311.3159-0.02971.035256.4281-27.069954.8948
277.5825-1.45851.98143.3636-0.21745.1811-0.0813-0.53770.18380.50170.63-0.01470.23620.3859-0.30980.6243-0.02590.06430.84240.03090.753955.8473-26.277645.1388
288.9393-1.3680.41544.43120.326.58680.34720.0482-1.5588-0.27590.2045-0.14060.71131.2357-0.52940.66240.2225-0.09540.9115-0.00670.808655.5718-33.755938.0794
297.7082-0.78331.23392.5941-0.0775.84020.0554-1.1138-1.17210.55230.2749-0.04070.5104-0.049-0.50420.81930.0716-0.02960.76640.2670.974843.7204-31.513838.8373
302.06520.36961.02591.8675-1.16334.88610.2636-0.3101-2.19530.6780.0920.18330.93010.1025-0.41610.90120.0813-0.06060.69520.16890.982739.3865-35.063234.6809
316.6992-0.42962.65032.0481-0.16514.28860.26770.3088-1.2644-0.05750.10810.47590.43450.3131-0.38390.51060.0856-0.01510.3877-0.10870.644232.9074-29.872521.5461
327.9099-0.61541.57479.9249-2.65757.3920.73511.73540.1809-1.09680.1330.4802-0.3448-0.5025-0.02760.5780.14870.18550.8641-0.14340.954120.2066-20.23497.7745
337.1312-0.75092.14263.89350.14765.86630.2480.80520.3362-0.603-0.53870.8051-0.8326-0.47290.13170.8520.28590.0280.95380.05850.774812.6957-13.498711.9514
345.7269-1.19841.35812.63360.23674.1325-0.3593-0.25661.4560.4188-0.09260.0063-1.0665-0.75310.3350.77860.2204-0.00050.4081-0.07210.891120.1907-4.673731.4163
356.295-2.77691.37163.67380.47576.3469-0.7225-1.58092.43570.9064-0.59310.1578-1.7663-0.37010.35331.7990.3262-0.38570.8906-0.48141.698323.96697.04340.8659
367.2326-0.96671.46043.43430.10163.6698-0.3639-1.21970.50980.69210.01710.0942-1.2453-0.80970.14690.93520.2292-0.04790.6574-0.01060.54831.8627-10.470241.8619
375.6122-0.74894.66521.7322-0.29989.3153-0.35971.19140.74970.07260.0782-0.348-0.97061.4640.25482.1927-0.3330.11031.96980.12972.073346.9559-11.181225.2611
385.2377-2.60161.90934.6512-1.683.4112-0.9667-0.84792.0738-0.0017-0.1575-0.6637-1.9807-0.13780.29821.4571-0.1213-0.32410.3502-0.33741.493135.40671.483239.1695
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1(CHAIN A AND RESID 143:158 )A143 - 158
2X-RAY DIFFRACTION2(CHAIN A AND RESID 159:171 )A159 - 171
3X-RAY DIFFRACTION3(CHAIN A AND RESID 172:188 )A172 - 188
4X-RAY DIFFRACTION4(CHAIN A AND RESID 189:208 )A189 - 208
5X-RAY DIFFRACTION5(CHAIN A AND RESID 209:214 )A209 - 214
6X-RAY DIFFRACTION6(CHAIN A AND RESID 215:251 )A215 - 251
7X-RAY DIFFRACTION7(CHAIN A AND RESID 267:274 )A267 - 274
8X-RAY DIFFRACTION8(CHAIN A AND RESID 275:286 )A275 - 286
9X-RAY DIFFRACTION9(CHAIN A AND RESID 287:298 )A287 - 298
10X-RAY DIFFRACTION10(CHAIN A AND RESID 299:304 )A299 - 304
11X-RAY DIFFRACTION11(CHAIN A AND RESID 305:312 )A305 - 312
12X-RAY DIFFRACTION12(CHAIN A AND RESID 313:320 )A313 - 320
13X-RAY DIFFRACTION13(CHAIN A AND RESID 357:369 )A357 - 369
14X-RAY DIFFRACTION14(CHAIN A AND RESID 370:381 )A370 - 381
15X-RAY DIFFRACTION15(CHAIN A AND RESID 382:427 )A382 - 427
16X-RAY DIFFRACTION16(CHAIN A AND RESID 428:435 )A428 - 435
17X-RAY DIFFRACTION17(CHAIN A AND RESID 460:469 )A460 - 469
18X-RAY DIFFRACTION18(CHAIN A AND RESID 470:474 )A470 - 474
19X-RAY DIFFRACTION19(CHAIN A AND RESID 475:484 )A475 - 484
20X-RAY DIFFRACTION20(CHAIN A AND RESID 485:489 )A485 - 489
21X-RAY DIFFRACTION21(CHAIN A AND RESID 497:502 )A497 - 502
22X-RAY DIFFRACTION22(CHAIN A AND RESID 503:507 )A503 - 507
23X-RAY DIFFRACTION23(CHAIN A AND RESID 508:512 )A508 - 512
24X-RAY DIFFRACTION24(CHAIN A AND RESID 513:517 )A513 - 517
25X-RAY DIFFRACTION25(CHAIN A AND RESID 518:522 )A518 - 522
26X-RAY DIFFRACTION26(CHAIN A AND RESID 544:560 )A544 - 560
27X-RAY DIFFRACTION27(CHAIN A AND RESID 561:585 )A561 - 585
28X-RAY DIFFRACTION28(CHAIN A AND RESID 586:612 )A586 - 612
29X-RAY DIFFRACTION29(CHAIN A AND RESID 613:637 )A613 - 637
30X-RAY DIFFRACTION30(CHAIN A AND RESID 638:652 )A638 - 652
31X-RAY DIFFRACTION31(CHAIN A AND RESID 653:725 )A653 - 725
32X-RAY DIFFRACTION32(CHAIN A AND RESID 726:753 )A726 - 753
33X-RAY DIFFRACTION33(CHAIN A AND RESID 760:837 )A760 - 837
34X-RAY DIFFRACTION34(CHAIN A AND RESID 838:967 )A838 - 967
35X-RAY DIFFRACTION35(CHAIN A AND RESID 981:1003 )A981 - 1003
36X-RAY DIFFRACTION36(CHAIN A AND RESID 1004:1038 )A1004 - 1038
37X-RAY DIFFRACTION37(CHAIN A AND RESID 1039:1045 )A1039 - 1045
38X-RAY DIFFRACTION38(CHAIN A AND RESID 1046:1091 )A1046 - 1091

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