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- PDB-8v8h: PI3Ka H1047R co-crystal structure with inhibitor in cryptic pocke... -

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Basic information

Entry
Database: PDB / ID: 8v8h
TitlePI3Ka H1047R co-crystal structure with inhibitor in cryptic pocket near H1047R (compound 4).
Components
  • Phosphatidylinositol 3-kinase regulatory subunit alpha
  • Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
KeywordsSIGNALING PROTEIN / H1047R / PI3K / PI3Ka
Function / homology
Function and homology information


perinuclear endoplasmic reticulum membrane / regulation of toll-like receptor 4 signaling pathway / response to muscle inactivity / phosphatidylinositol kinase activity / negative regulation of actin filament depolymerization / regulation of actin filament organization / response to L-leucine / positive regulation of focal adhesion disassembly / response to butyrate / 1-phosphatidylinositol-3-kinase regulator activity ...perinuclear endoplasmic reticulum membrane / regulation of toll-like receptor 4 signaling pathway / response to muscle inactivity / phosphatidylinositol kinase activity / negative regulation of actin filament depolymerization / regulation of actin filament organization / response to L-leucine / positive regulation of focal adhesion disassembly / response to butyrate / 1-phosphatidylinositol-3-kinase regulator activity / positive regulation of endoplasmic reticulum unfolded protein response / phosphatidylinositol 3-kinase regulator activity / IRS-mediated signalling / phosphatidylinositol 3-kinase activator activity / interleukin-18-mediated signaling pathway / T follicular helper cell differentiation / autosome genomic imprinting / phosphatidylinositol 3-kinase complex / myeloid leukocyte migration / PI3K events in ERBB4 signaling / cellular response to hydrostatic pressure / phosphatidylinositol 3-kinase regulatory subunit binding / regulation of cellular respiration / neurotrophin TRKA receptor binding / Activated NTRK2 signals through PI3K / cis-Golgi network / ErbB-3 class receptor binding / negative regulation of fibroblast apoptotic process / Activated NTRK3 signals through PI3K / transmembrane receptor protein tyrosine kinase adaptor activity / phosphatidylinositol 3-kinase complex, class IB / positive regulation of protein localization to membrane / vasculature development / 1-phosphatidylinositol-4-phosphate 3-kinase activity / Signaling by cytosolic FGFR1 fusion mutants / Co-stimulation by ICOS / RHOD GTPase cycle / cardiac muscle cell contraction / RHOF GTPase cycle / phosphatidylinositol 3-kinase complex, class IA / Nephrin family interactions / kinase activator activity / anoikis / Signaling by LTK in cancer / phosphatidylinositol-3-phosphate biosynthetic process / positive regulation of leukocyte migration / relaxation of cardiac muscle / Signaling by LTK / MET activates PI3K/AKT signaling / PI3K/AKT activation / negative regulation of stress fiber assembly / 1-phosphatidylinositol-4,5-bisphosphate 3-kinase activity / RND1 GTPase cycle / positive regulation of filopodium assembly / phosphatidylinositol-4,5-bisphosphate 3-kinase / RND2 GTPase cycle / vascular endothelial growth factor signaling pathway / RND3 GTPase cycle / phosphatidylinositol 3-kinase / insulin binding / growth hormone receptor signaling pathway / 1-phosphatidylinositol-3-kinase activity / Signaling by ALK / RHOB GTPase cycle / RHOV GTPase cycle / PI-3K cascade:FGFR3 / Erythropoietin activates Phosphoinositide-3-kinase (PI3K) / GP1b-IX-V activation signalling / negative regulation of macroautophagy / natural killer cell mediated cytotoxicity / PI-3K cascade:FGFR2 / response to dexamethasone / phosphatidylinositol-mediated signaling / PI-3K cascade:FGFR4 / PI-3K cascade:FGFR1 / RHOC GTPase cycle / RHOJ GTPase cycle / intracellular glucose homeostasis / phosphatidylinositol phosphate biosynthetic process / negative regulation of osteoclast differentiation / Synthesis of PIPs at the plasma membrane / RHOU GTPase cycle / CDC42 GTPase cycle / negative regulation of anoikis / RET signaling / PI3K events in ERBB2 signaling / insulin receptor substrate binding / Interleukin-3, Interleukin-5 and GM-CSF signaling / PI3K Cascade / T cell differentiation / intercalated disc / protein kinase activator activity / RHOG GTPase cycle / extrinsic apoptotic signaling pathway via death domain receptors / regulation of multicellular organism growth / negative regulation of cell-matrix adhesion / RHOA GTPase cycle / CD28 dependent PI3K/Akt signaling / positive regulation of TOR signaling / Role of LAT2/NTAL/LAB on calcium mobilization
Similarity search - Function
PI3Kalpha, catalytic domain / Phosphatidylinositol 3-kinase regulatory subunit alpha, SH3 domain / PIK3R1, inter-SH2 domain / PI3K p85 subunit, C-terminal SH2 domain / PI3K regulatory subunit p85-related , inter-SH2 domain / PI3K p85 subunit, N-terminal SH2 domain / Phosphatidylinositol 3-kinase regulatory subunit P85 inter-SH2 domain / PI3-kinase family, p85-binding domain / PI3-kinase family, p85-binding domain / Rho GTPase-activating protein domain ...PI3Kalpha, catalytic domain / Phosphatidylinositol 3-kinase regulatory subunit alpha, SH3 domain / PIK3R1, inter-SH2 domain / PI3K p85 subunit, C-terminal SH2 domain / PI3K regulatory subunit p85-related , inter-SH2 domain / PI3K p85 subunit, N-terminal SH2 domain / Phosphatidylinositol 3-kinase regulatory subunit P85 inter-SH2 domain / PI3-kinase family, p85-binding domain / PI3-kinase family, p85-binding domain / Rho GTPase-activating protein domain / RhoGAP domain / Rho GTPase-activating proteins domain profile. / GTPase-activator protein for Rho-like GTPases / 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. / Rho GTPase activation protein / 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 3/4-kinase, conserved site / Phosphatidylinositol 3- and 4-kinases signature 2. / Phosphatidylinositol 3-/4-kinase, catalytic domain superfamily / Phosphoinositide 3-kinase, catalytic domain / Phosphatidylinositol 3- and 4-kinase / Phosphatidylinositol 3- and 4-kinases catalytic domain profile. / Phosphatidylinositol 3-/4-kinase, catalytic domain / C2 domain superfamily / SH2 domain / Src homology 2 (SH2) domain profile. / Src homology 2 domains / SH2 domain / Src homology 3 domains / SH2 domain superfamily / SH3-like domain superfamily / Src homology 3 (SH3) domain profile. / SH3 domain / Armadillo-type fold / Ubiquitin-like domain superfamily / Protein kinase-like domain superfamily
Similarity search - Domain/homology
: / : / Phosphatidylinositol 3-kinase regulatory subunit alpha / Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.58 Å
AuthorsGunn, R.J. / Lawson, J.D.
Funding support United States, 1items
OrganizationGrant numberCountry
Not funded United States
CitationJournal: J.Med.Chem. / Year: 2024
Title: Discovery of Pyridopyrimidinones that Selectively Inhibit the H1047R PI3K alpha Mutant Protein.
Authors: Ketcham, J.M. / Harwood, S.J. / Aranda, R. / Aloiau, A.N. / Bobek, B.M. / Briere, D.M. / Burns, A.C. / Caddell Haatveit, K. / Calinisan, A. / Clarine, J. / Elliott, A. / Engstrom, L.D. / ...Authors: Ketcham, J.M. / Harwood, S.J. / Aranda, R. / Aloiau, A.N. / Bobek, B.M. / Briere, D.M. / Burns, A.C. / Caddell Haatveit, K. / Calinisan, A. / Clarine, J. / Elliott, A. / Engstrom, L.D. / Gunn, R.J. / Ivetac, A. / Jones, B. / Kuehler, J. / Lawson, J.D. / Nguyen, N. / Parker, C. / Pearson, K.E. / Rahbaek, L. / Saechao, B. / Wang, X. / Waters, A. / Waters, L. / Watkins, A.H. / Olson, P. / Smith, C.R. / Christensen, J.G. / Marx, M.A.
History
DepositionDec 5, 2023Deposition site: RCSB / Processing site: RCSB
Revision 1.0Mar 20, 2024Provider: repository / Type: Initial release
Revision 1.1Mar 27, 2024Group: Database references / Category: citation / citation_author
Item: _citation.pdbx_database_id_PubMed / _citation.title ..._citation.pdbx_database_id_PubMed / _citation.title / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.2Apr 10, 2024Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last

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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 alpha isoform
B: Phosphatidylinositol 3-kinase regulatory subunit alpha
C: Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
D: Phosphatidylinositol 3-kinase regulatory subunit alpha
hetero molecules


Theoretical massNumber of molelcules
Total (without water)318,6398
Polymers316,9554
Non-polymers1,6844
Water00
1
A: Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
B: Phosphatidylinositol 3-kinase regulatory subunit alpha
hetero molecules


Theoretical massNumber of molelcules
Total (without water)159,3194
Polymers158,4772
Non-polymers8422
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5700 Å2
ΔGint-14 kcal/mol
Surface area59670 Å2
MethodPISA
2
C: Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform
D: Phosphatidylinositol 3-kinase regulatory subunit alpha
hetero molecules


Theoretical massNumber of molelcules
Total (without water)159,3194
Polymers158,4772
Non-polymers8422
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area5530 Å2
ΔGint-17 kcal/mol
Surface area59110 Å2
MethodPISA
Unit cell
Length a, b, c (Å)233.850, 157.770, 121.900
Angle α, β, γ (deg.)90.000, 112.660, 90.000
Int Tables number5
Space group name H-MC121
Space group name HallC2y
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
d_1ens_1(chain "A" and (resid 2 through 409 or resid 416...
d_2ens_1(chain "C" and (resid 2 through 409 or resid 416...
d_1ens_2(chain "B" and (resid 326 through 331 or resid 333...
d_2ens_2(chain "D" and (resid 326 through 331 or resid 333...

NCS domain segments:
Dom-IDComponent-IDEns-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
d_11ens_1PROPROVALVALAA2 - 4096 - 413
d_12ens_1LYSLYSARGARGAA416 - 524420 - 528
d_13ens_1ASNASNLEULEUAA526 - 866530 - 870
d_14ens_1GLYGLYGLYGLYAA868 - 887872 - 891
d_15ens_1ILEILEASPASPAA889 - 939893 - 943
d_16ens_1GLUGLUGLUGLUAA950954
d_17ens_1VALVALTHRTHRAA952 - 974956 - 978
d_18ens_1GLUGLUMETMETAA976 - 1040980 - 1044
d_19ens_1GLNGLNALAALAAA1042 - 10461046 - 1050
d_110ens_1GLYGLYLYSLYSAA1049 - 10541053 - 1058
d_111ens_1ASPASPGLNGLNAA1056 - 10641060 - 1068
d_21ens_1PROPROVALVALCC2 - 4096 - 413
d_22ens_1LYSLYSARGARGCC416 - 524420 - 528
d_23ens_1ASNASNLEULEUCC526 - 866530 - 870
d_24ens_1GLYGLYGLYGLYCC868 - 887872 - 891
d_25ens_1ILEILEASPASPCC889 - 939893 - 943
d_26ens_1GLUGLUGLUGLUCC950954
d_27ens_1VALVALTHRTHRCC952 - 974956 - 978
d_28ens_1GLUGLUMETMETCC976 - 1040980 - 1044
d_29ens_1GLNGLNALAALACC1042 - 10461046 - 1050
d_210ens_1GLYGLYLYSLYSCC1049 - 10541053 - 1058
d_211ens_1ASPASPGLNGLNCC1056 - 10641060 - 1068
d_11ens_2METMETALAALABB326 - 3315 - 10
d_12ens_2TRPTRPSERSERBB333 - 39312 - 72
d_13ens_2PROPROILEILEBB395 - 53974 - 218
d_14ens_2SERSERARGARGBB541 - 577220 - 256
d_15ens_2TRPTRPTRPTRPBB583262
d_21ens_2METMETALAALADD326 - 3315 - 10
d_22ens_2TRPTRPSERSERDD333 - 39312 - 72
d_23ens_2PROPROILEILEDD395 - 53974 - 218
d_24ens_2SERSERARGARGDD541 - 577220 - 256
d_25ens_2TRPTRPTRPTRPDD583262

NCS ensembles :
ID
ens_1
ens_2

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Components

#1: Protein Phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit alpha isoform


Mass: 124810.422 Da / Num. of mol.: 2 / Mutation: H1047R
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PIK3CA / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: P42336
#2: Protein Phosphatidylinositol 3-kinase regulatory subunit alpha / PtdIns-3-kinase regulatory subunit alpha / Phosphatidylinositol 3-kinase 85 kDa regulatory subunit ...PtdIns-3-kinase regulatory subunit alpha / Phosphatidylinositol 3-kinase 85 kDa regulatory subunit alpha / PtdIns-3-kinase regulatory subunit p85-alpha


Mass: 33666.961 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: PIK3R1, GRB1 / Production host: Trichoplusia ni (cabbage looper) / References: UniProt: P27986
#3: Chemical ChemComp-YO4 / 2-({(1R)-1-[2-(4,4-dimethylpiperidin-1-yl)-3,6-dimethyl-4-oxo-4H-1-benzopyran-8-yl]ethyl}amino)benzoic acid


Mass: 448.554 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C27H32N2O4 / Feature type: SUBJECT OF INVESTIGATION
#4: Chemical ChemComp-YNZ / (2S)-N~1~-[(4P)-2-tert-butyl-4'-methyl[4,5'-bi-1,3-thiazol]-2'-yl]pyrrolidine-1,2-dicarboxamide


Mass: 393.527 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C17H23N5O2S2 / Feature type: SUBJECT OF INVESTIGATION
Has ligand of interestY

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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: 3.27 Å3/Da / Density % sol: 62.43 %
Crystal growTemperature: 291 K / Method: vapor diffusion, hanging drop
Details: 0.2 M Sodium acetate, 0.1 M Sodium citrate pH 5.5, 4% w/v PEG 4000.

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: CLSI / Beamline: 08ID-1 / Wavelength: 0.95371 Å
DetectorType: DECTRIS PILATUS3 S 6M / Detector: PIXEL / Date: Aug 12, 2022
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.95371 Å / Relative weight: 1
ReflectionResolution: 3.58→48.21 Å / Num. obs: 47973 / % possible obs: 99.54 % / Redundancy: 4.6 % / Biso Wilson estimate: 104.01 Å2 / CC1/2: 0.99 / Rpim(I) all: 0.08 / Net I/σ(I): 9.1
Reflection shellResolution: 3.58→3.71 Å / Num. unique obs: 4774 / CC1/2: 0.75 / Rpim(I) all: 0.4

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Processing

SoftwareName: PHENIX / Version: 1.20.1_4487 / Classification: refinement
RefinementMethod to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.58→48.21 Å / SU ML: 0.4945 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 30.4375
Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
RfactorNum. reflection% reflectionSelection details
Rfree0.2719 2353 4.91 %RANDOM
Rwork0.222 45565 --
obs0.2244 47918 99.54 %-
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso mean: 143.7 Å2
Refinement stepCycle: LAST / Resolution: 3.58→48.21 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms20726 0 118 0 20844
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.00421295
X-RAY DIFFRACTIONf_angle_d0.770828732
X-RAY DIFFRACTIONf_chiral_restr0.04593093
X-RAY DIFFRACTIONf_plane_restr0.00543670
X-RAY DIFFRACTIONf_dihedral_angle_d15.53828161
Refine LS restraints NCS
Ens-IDDom-IDAsym-IDAuth asym-IDRefine-IDTypeRms dev position (Å)
ens_1d_2AAX-RAY DIFFRACTIONTorsion NCS0.830597485796
ens_2d_2BBX-RAY DIFFRACTIONTorsion NCS1.16134251677
LS refinement shellResolution: 3.58→3.85 Å
RfactorNum. reflection% reflection
Rfree0.3869 128 -
Rwork0.3421 2643 -
obs--99.64 %
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)
11.71144971866-0.5187769470070.4953987429691.6974084826-0.3082854407011.44115704918-0.08705707548130.100349177026-0.150098475436-0.103790818319-0.02484219294860.2001279373050.09690336996470.1087996302680.1000311686160.972827536151-0.0257453821635-0.003419502376670.8111735596060.02615129234690.80303992391332.22663721230.022304662913.6228749582
20.717698874562-0.1939137387370.4944566785251.28867849833-0.3338249484472.23385587364-0.0224652295804-0.313519255783-0.1562230678960.209265928137-0.01160989218970.2407644634530.0939998690521-0.2007207905050.06483249668971.12690206954-0.02541817064810.2380922264210.975600586280.04886783112680.89277943158632.9738133639-4.8830176462739.4541344912
30.969228356124-0.117034205845-0.1076094210461.28365773070.3737623088382.217165527070.01091567121590.291094680298-0.206170404837-0.309919201453-0.06575484288730.4988075214890.0464317435745-0.04639308462240.05256545466191.09610285933-0.00261855606099-0.1687731115930.85291764217-0.1092057890930.99375704777826.4189658225-15.76393466440.0428082031735
41.614989258920.06344507544280.07698832111531.57041953020.1733969963871.020650378360.044540887952-0.0627076084704-0.214735229072-0.139864961103-0.0410515317688-0.1075814622640.2770768663650.238621181281-0.005902384717911.023831353950.120262269660.04733783671010.8044926871580.03426819823970.7259212094351.7156924977-7.772616427517.7421043921
50.8768741701380.0309099833221-0.3994003927010.0008952077954770.08322686829441.14093743981-0.1285345932680.662229760718-0.545868752156-1.2452784035-0.444332268146-0.433017616049-0.28536970164-0.3435295267210.5067330357813.12815614280.2977847676250.2405204297252.25920742017-0.09185194298692.6610882838941.8341820976-38.0255756127-12.8954305211
60.38060105566-0.836273741782-0.8245472461441.471661626071.144244789780.3731083215120.3429249016270.1084585911480.0619489105872-1.06323776777-0.118360717958-0.323467091173-0.3046006057140.0640013757533-0.1812168946771.653468788050.1375217939160.04955803967751.1247572556-0.1152539889591.311147492940.626931142215.1267500932-8.91748203748
71.75127531774-0.155169759895-0.1081257914451.69325315740.5133532591961.47807259645-0.140853213402-0.126183951681-0.1958160623420.06891793483660.406722041938-0.9277480517310.1785256377860.389043017217-0.2362069899260.7293670254190.0795391287967-0.07542680095261.05937912401-0.2538554006381.3651246493363.6237421207-29.404392023991.224501874
81.663978927460.0562140219012-1.033161303851.728429925270.7876662083481.952802176950.169014528478-0.3397208424520.0347347478210.250815943790.0546486363398-0.0856723090111-0.4877886245610.265590637901-0.1871438733060.9851323339460.01540347137520.0002342608349410.963825464972-0.03795099004980.78399108110641.43954479724.30749258805108.845909892
91.285775516610.2392527537680.05299563513741.1718506881-0.170468626207-0.00223098536857-0.449716301961-0.0376909856513-0.324235153022-0.3292235148080.283100041328-0.567017336066-0.1529331357550.2104916540690.224786261831.1314486902-0.2124601744910.2340755213021.1631216623-0.1919941855941.3008980057364.51166630244.9799111155593.3414340229
100.792950851104-0.5682548245420.1705292549091.04362156078-0.8188471130790.8216427079260.551893232146-0.162487222725-0.0143614627459-0.963823657211-0.701044894584-1.06772228657-0.3186070719490.5388909599280.4743091235451.80419785432-0.7059987763180.7585136223072.11725586223-0.3121420715212.3277108240884.988124343416.582320628472.3677000584
110.878106366601-0.541612564495-0.01373325774731.90040124946-0.106367007771.3550390881-0.1555578803420.05423396138120.142532861996-0.5816709099230.389513646305-0.680541527315-0.7124059483040.573631066265-0.173764710231.6668409847-0.4186407041920.3999838682911.4754860813-0.1721409108731.7968497122374.999239527922.30846725284.489331611
121.212015363920.5638585388090.3834622353661.522949022830.4192027797091.562748719960.06118727912090.09488919696520.101037719602-0.4363719359720.177550574624-0.444449196592-0.4724541397620.328972053212-0.228352345480.929517440782-0.1450886331120.225746051990.835719667231-0.0801098749830.85894761971351.6621581551.5480919037388.212111211
134.388055552610.0414737210908-0.4339944376632.33828573201-0.2633958825112.870228552880.3561089212361.14552042368-0.0203499961304-0.00918499104227-0.0976297936732-0.0509121741755-0.702470063334-1.06561149562-0.2182649392121.312074899190.2480564479530.1890271744891.13357681170.1830093289720.77405115640429.740781813410.302597511772.3565244318
140.623793341030.5727548297730.3080654426661.66082639057-0.05072913683241.84401206718-0.2596531601610.5500234270330.283661532857-0.625321882890.131455867727-0.0215341215579-1.331391231880.1189958622020.07845038558162.11499215741-0.09965643583390.3900820648990.977327969410.0727119639571.1276496459439.923410241522.100724067372.1969017688
150.01246432185180.0188729876185-0.01744726761410.00117672823899-0.005674612256880.006420823795580.6596629605840.6494939246790.1942146394580.0752460314198-0.2616434293760.288242084875-0.6022194189970.308260481159-0.3121176438353.112057652310.1180243284850.1810583649232.580402536620.3793036570313.0879604463369.304664977539.062469997265.4237513988
160.5692636523610.3022462525420.2583896914230.9053358038020.4006152731641.20092497148-0.1721799333510.257014544470.110329274625-1.388092430430.0340540636458-0.6927418704790.07934030870660.4242981280850.1095189077061.5586668268-0.09721742108110.2629458931591.70784103751-0.2438303906351.6095810136771.9311728931-13.199060364168.4384346461
Refinement TLS group

Refine-ID: X-RAY DIFFRACTION

IDRefine TLS-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11chain 'A' and (resid 2 through 121 )AA2 - 1211 - 120
22chain 'A' and (resid 122 through 264 )AA122 - 264121 - 263
33chain 'A' and (resid 265 through 602 )AA265 - 602264 - 558
44chain 'A' and (resid 603 through 1064 )AA603 - 1064559 - 1020
55chain 'B' and (resid 326 through 428 )BC326 - 4281 - 89
66chain 'B' and (resid 429 through 587 )BC429 - 58790 - 239
77chain 'C' and (resid 2 through 121 )CD2 - 1211 - 120
88chain 'C' and (resid 122 through 270 )CD122 - 270121 - 269
99chain 'C' and (resid 271 through 354 )CD271 - 354270 - 340
1010chain 'C' and (resid 355 through 418 )CD355 - 418341 - 399
1111chain 'C' and (resid 419 through 576 )CD419 - 576400 - 532
1212chain 'C' and (resid 577 through 853 )CD577 - 853533 - 809
1313chain 'C' and (resid 854 through 963 )CD854 - 963810 - 911
1414chain 'C' and (resid 964 through 1064 )CD964 - 1064912 - 1012
1515chain 'D' and (resid 326 through 428 )DF326 - 4281 - 89
1616chain 'D' and (resid 429 through 587 )DF429 - 58790 - 239

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