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- PDB-7jxq: EGFR kinase (T790M/V948R) in complex with allosteric inhibitor JB... -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 7jxq
TitleEGFR kinase (T790M/V948R) in complex with allosteric inhibitor JBJ-09-063
ComponentsEpidermal growth factor receptor
KeywordsTRANSFERASE/TRANSFERASE Inhibitor / EGFR / ErbB1 / kinase / inhibitor / TRANSFERASE / TRANSFERASE-TRANSFERASE Inhibitor complex
Function / homology
Function and homology information


response to hydroxyisoflavone / multivesicular body, internal vesicle lumen / positive regulation of prolactin secretion / negative regulation of cardiocyte differentiation / positive regulation of protein kinase C activity / diterpenoid metabolic process / Shc-EGFR complex / ovulation cycle / Inhibition of Signaling by Overexpressed EGFR / epidermal growth factor receptor activity ...response to hydroxyisoflavone / multivesicular body, internal vesicle lumen / positive regulation of prolactin secretion / negative regulation of cardiocyte differentiation / positive regulation of protein kinase C activity / diterpenoid metabolic process / Shc-EGFR complex / ovulation cycle / Inhibition of Signaling by Overexpressed EGFR / epidermal growth factor receptor activity / EGFR interacts with phospholipase C-gamma / positive regulation of mucus secretion / response to UV-A / epidermal growth factor binding / PLCG1 events in ERBB2 signaling / tongue development / midgut development / ERBB2-EGFR signaling pathway / hydrogen peroxide metabolic process / PTK6 promotes HIF1A stabilization / digestive tract morphogenesis / morphogenesis of an epithelial fold / ERBB2 Activates PTK6 Signaling / intracellular vesicle / Signaling by EGFR / response to cobalamin / transmembrane receptor protein tyrosine kinase activator activity / protein tyrosine kinase activator activity / negative regulation of epidermal growth factor receptor signaling pathway / Signaling by ERBB4 / eyelid development in camera-type eye / regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / protein insertion into membrane / cerebral cortex cell migration / ERBB2 Regulates Cell Motility / Respiratory syncytial virus (RSV) attachment and entry / regulation of JNK cascade / : / PI3K events in ERBB2 signaling / positive regulation of cyclin-dependent protein serine/threonine kinase activity / negative regulation of mitotic cell cycle / hair follicle development / Estrogen-dependent nuclear events downstream of ESR-membrane signaling / MAP kinase kinase kinase activity / embryonic placenta development / positive regulation of bone resorption / positive regulation of G1/S transition of mitotic cell cycle / GAB1 signalosome / salivary gland morphogenesis / peptidyl-tyrosine autophosphorylation / regulation of peptidyl-tyrosine phosphorylation / positive regulation of phosphorylation / positive regulation of glial cell proliferation / positive regulation of vasoconstriction / Signaling by ERBB2 / cellular response to epidermal growth factor stimulus / GRB2 events in EGFR signaling / SHC1 events in EGFR signaling / cellular response to cadmium ion / EGFR Transactivation by Gastrin / positive regulation of DNA repair / GRB2 events in ERBB2 signaling / TFAP2 (AP-2) family regulates transcription of growth factors and their receptors / transmembrane receptor protein tyrosine kinase activity / SHC1 events in ERBB2 signaling / positive regulation of synaptic transmission, glutamatergic / cellular response to dexamethasone stimulus / ossification / neurogenesis / regulation of ERK1 and ERK2 cascade / basal plasma membrane / neuron projection morphogenesis / positive regulation of superoxide anion generation / positive regulation of DNA replication / epithelial cell proliferation / Signal transduction by L1 / cellular response to estradiol stimulus / positive regulation of epithelial cell proliferation / NOTCH3 Activation and Transmission of Signal to the Nucleus / astrocyte activation / liver regeneration / positive regulation of protein localization to plasma membrane / EGFR downregulation / cellular response to amino acid stimulus / positive regulation of smooth muscle cell proliferation / Signaling by ERBB2 TMD/JMD mutants / positive regulation of MAP kinase activity / lung development / clathrin-coated endocytic vesicle membrane / Constitutive Signaling by EGFRvIII / Signaling by ERBB2 ECD mutants / Signaling by ERBB2 KD Mutants / epidermal growth factor receptor signaling pathway / negative regulation of protein catabolic process / receptor protein-tyrosine kinase / Downregulation of ERBB2 signaling / kinase binding / ruffle membrane / positive regulation of miRNA transcription / cell-cell adhesion
Similarity search - Function
: / Epidermal growth factor receptor transmembrane-juxtamembrane segment / Tyrosine protein kinase, EGF/ERB/XmrK receptor / Growth factor receptor domain 4 / Growth factor receptor domain IV / Receptor L-domain / Furin-like cysteine-rich domain / Receptor L-domain superfamily / Furin-like cysteine rich region / Receptor L domain ...: / Epidermal growth factor receptor transmembrane-juxtamembrane segment / Tyrosine protein kinase, EGF/ERB/XmrK receptor / Growth factor receptor domain 4 / Growth factor receptor domain IV / Receptor L-domain / Furin-like cysteine-rich domain / Receptor L-domain superfamily / Furin-like cysteine rich region / Receptor L domain / Furin-like repeat / Furin-like repeats / Growth factor receptor cysteine-rich domain superfamily / Tyrosine-protein kinase, catalytic domain / Tyrosine kinase, catalytic domain / Tyrosine protein kinases specific active-site signature. / Tyrosine-protein kinase, active site / Protein tyrosine and serine/threonine kinase / Serine-threonine/tyrosine-protein kinase, catalytic domain / Protein kinase, ATP binding site / Protein kinases ATP-binding region signature. / Protein kinase domain profile. / Protein kinase domain / Protein kinase-like domain superfamily
Similarity search - Domain/homology
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / Chem-VNS / Epidermal growth factor receptor
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.83 Å
AuthorsBeyett, T.S. / Eck, M.J.
Funding support United States, 2items
OrganizationGrant numberCountry
National Institutes of Health/National Cancer Institute (NIH/NCI)5R01CA201049-05 United States
National Institutes of Health/National Cancer Institute (NIH/NCI)1F32CA247198-01 United States
CitationJournal: Nat Cancer / Year: 2022
Title: An allosteric inhibitor against the therapy-resistant mutant forms of EGFR in non-small cell lung cancer.
Authors: To, C. / Beyett, T.S. / Jang, J. / Feng, W.W. / Bahcall, M. / Haikala, H.M. / Shin, B.H. / Heppner, D.E. / Rana, J.K. / Leeper, B.A. / Soroko, K.M. / Poitras, M.J. / Gokhale, P.C. / ...Authors: To, C. / Beyett, T.S. / Jang, J. / Feng, W.W. / Bahcall, M. / Haikala, H.M. / Shin, B.H. / Heppner, D.E. / Rana, J.K. / Leeper, B.A. / Soroko, K.M. / Poitras, M.J. / Gokhale, P.C. / Kobayashi, Y. / Wahid, K. / Kurppa, K.J. / Gero, T.W. / Cameron, M.D. / Ogino, A. / Mushajiang, M. / Xu, C. / Zhang, Y. / Scott, D.A. / Eck, M.J. / Gray, N.S. / Janne, P.A.
History
DepositionAug 27, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 8, 2021Provider: repository / Type: Initial release
Revision 1.1Apr 27, 2022Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year
Revision 1.2May 11, 2022Group: 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 1.3Oct 18, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
D: Epidermal growth factor receptor
A: Epidermal growth factor receptor
B: Epidermal growth factor receptor
C: Epidermal growth factor receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)155,24716
Polymers150,8984
Non-polymers4,34912
Water9,746541
1
B: Epidermal growth factor receptor
hetero molecules

D: Epidermal growth factor receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)77,6238
Polymers75,4492
Non-polymers2,1746
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_544-x,y-1/2,-z-11
Buried area5070 Å2
ΔGint-44 kcal/mol
Surface area25930 Å2
MethodPISA
2
A: Epidermal growth factor receptor
hetero molecules

C: Epidermal growth factor receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)77,6238
Polymers75,4492
Non-polymers2,1746
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation2_655-x+1,y+1/2,-z1
Buried area5160 Å2
ΔGint-44 kcal/mol
Surface area25690 Å2
MethodPISA
Unit cell
Length a, b, c (Å)57.318, 74.598, 150.569
Angle α, β, γ (deg.)90.000, 98.690, 90.000
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 701 through 765 or resid 767...
21(chain B and (resid 701 through 765 or resid 767...
31(chain C and (resid 701 through 765 or resid 767...
41(chain D and (resid 701 through 765 or resid 767...

NCS domain segments:
Dom-IDComponent-IDEns-IDSelection detailsAuth asym-IDAuth seq-ID
111(chain A and (resid 701 through 765 or resid 767...A701 - 765
121(chain A and (resid 701 through 765 or resid 767...A767 - 862
131(chain A and (resid 701 through 765 or resid 767...A700 - 1201
141(chain A and (resid 701 through 765 or resid 767...A890 - 907
151(chain A and (resid 701 through 765 or resid 767...A909 - 1093
211(chain B and (resid 701 through 765 or resid 767...B701 - 765
221(chain B and (resid 701 through 765 or resid 767...B767 - 862
231(chain B and (resid 701 through 765 or resid 767...B876 - 888
241(chain B and (resid 701 through 765 or resid 767...B890 - 907
251(chain B and (resid 701 through 765 or resid 767...B909 - 1094
311(chain C and (resid 701 through 765 or resid 767...C701 - 765
321(chain C and (resid 701 through 765 or resid 767...C767 - 862
331(chain C and (resid 701 through 765 or resid 767...C876 - 888
341(chain C and (resid 701 through 765 or resid 767...C890 - 907
351(chain C and (resid 701 through 765 or resid 767...C909 - 1091
411(chain D and (resid 701 through 765 or resid 767...D701 - 765
421(chain D and (resid 701 through 765 or resid 767...D767 - 862
431(chain D and (resid 701 through 765 or resid 767...D700 - 1201
441(chain D and (resid 701 through 765 or resid 767...D890 - 907
451(chain D and (resid 701 through 765 or resid 767...D909 - 1092

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Components

#1: Protein
Epidermal growth factor receptor / Proto-oncogene c-ErbB-1 / Receptor tyrosine-protein kinase erbB-1


Mass: 37724.598 Da / Num. of mol.: 4 / Fragment: kinase domain / Mutation: T790M, V948R
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: EGFR, ERBB, ERBB1, HER1 / Plasmid: pTriEX / Cell line (production host): Sf9 / Production host: Spodoptera frugiperda (fall armyworm)
References: UniProt: P00533, receptor protein-tyrosine kinase
#2: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mg
#3: Chemical
ChemComp-ANP / PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER


Mass: 506.196 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C10H17N6O12P3 / Comment: AMP-PNP, energy-carrying molecule analogue*YM
#4: Chemical
ChemComp-VNS / (2R)-2-(5-fluoro-2-hydroxyphenyl)-2-{6-[4-(1-methylpiperidin-4-yl)phenyl]-1-oxo-1,3-dihydro-2H-isoindol-2-yl}-N-(1,3-thiazol-2-yl)acetamide


Mass: 556.650 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C31H29FN4O3S / Feature type: SUBJECT OF INVESTIGATION
#5: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 541 / Source method: isolated from a natural source / Formula: H2O
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: 2.11 Å3/Da / Density % sol: 41.67 % / Description: Plate
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5.7 / Details: 0.1 M Bis-Tris pH 5.7, 28% (w/v) PEG 3350

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 24-ID-E / Wavelength: 0.9792 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Nov 10, 2018
RadiationMonochromator: Double Crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9792 Å / Relative weight: 1
ReflectionResolution: 1.83→66.69 Å / Num. obs: 215143 / % possible obs: 99.5 % / Redundancy: 7 % / CC1/2: 0.999 / Rmerge(I) obs: 0.095 / Rpim(I) all: 0.038 / Rrim(I) all: 0.102 / Net I/σ(I): 9.3
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsNum. measured allNum. unique obsCC1/2Rpim(I) allRrim(I) allNet I/σ(I) obs% possible all
1.83-1.887.11.7945802781160.5130.7171.9350.999.6
8.18-66.6970.028915713120.9990.0120.03131.899.9

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Processing

Software
NameVersionClassification
PHENIX1.18.2_3874refinement
Aimless0.7.3data scaling
PDB_EXTRACT3.25data extraction
xia2data reduction
PHASERphasing
Cootmodel building
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5D41

5d41


Resolution: 1.83→66.69 Å / SU ML: 0.23 / Cross valid method: THROUGHOUT / σ(F): 1.33 / Phase error: 25.2 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.218 3902 1.81 %
Rwork0.184 211241 -
obs0.1846 215143 98.92 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 112.34 Å2 / Biso mean: 45.2554 Å2 / Biso min: 21.32 Å2
Refinement stepCycle: final / Resolution: 1.83→66.69 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9569 0 288 541 10398
Biso mean--35.9 45.39 -
Num. residues----1189
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A5801X-RAY DIFFRACTION12.098TORSIONAL
12B5801X-RAY DIFFRACTION12.098TORSIONAL
13C5801X-RAY DIFFRACTION12.098TORSIONAL
14D5801X-RAY DIFFRACTION12.098TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 28

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
1.83-1.850.35331130.34747560767398
1.85-1.880.33371320.32847476760898
1.88-1.90.3231620.30617500766299
1.9-1.930.28581300.29237549767998
1.93-1.950.29751560.27937480763699
1.95-1.980.26381330.26637561769499
1.98-2.010.30181340.27057538767299
2.01-2.050.31911310.25177626775799
2.05-2.080.30591450.24137472761799
2.08-2.120.25941440.23017576772099
2.12-2.160.28021370.22287486762399
2.16-2.210.28481390.20627670780999
2.21-2.250.23071320.21287539767199
2.25-2.310.24241430.20127553769699
2.31-2.360.24111380.20687525766399
2.36-2.430.2741350.19737532766799
2.43-2.50.25781370.20797384752196
2.5-2.580.26561470.19927333748097
2.58-2.670.28781350.20327562769799
2.67-2.780.20861500.192775617711100
2.78-2.90.21411340.195176377771100
2.9-3.060.28371470.186876047751100
3.06-3.250.2241420.186176697811100
3.25-3.50.21421420.168776117753100
3.5-3.850.19341340.154376097743100
3.85-4.410.18211420.134276357777100
4.41-5.560.14361470.14637400754798
5.56-66.690.15711410.15537593773499
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)
16.2790.0282-1.17772.1642-1.28555.83120.0719-0.02330.0088-0.0379-0.1773-0.55070.04360.77810.18520.2625-0.0145-0.0370.3099-0.07540.28725.567-9.912-65.52
25.51970.5368-6.89664.51470.95082.04370.4913-0.27410.2988-0.0801-0.08130.0974-0.65980.4204-0.25850.29610.0129-0.04910.2808-0.04470.216116.38-4.771-60.392
33.77780.53420.85633.73020.64292.06470.2869-0.46630.26470.20650.0282-0.438-0.46820.7252-0.18840.2652-0.0267-0.03970.3269-0.04730.298723.308-6.591-65.271
42.45030.5704-1.572.1674-0.53033.4794-0.0367-0.21810.04090.24040.0709-0.04420.04660.1834-0.01770.2730.0411-0.00720.18880.0050.227310.4-17.315-55.246
52.9868-0.02560.65612.69860.92215.8184-0.0495-0.2923-0.17430.33770.1550.37040.5547-0.5501-0.09220.3217-0.00460.09110.26770.08950.3157-4.903-21.622-46.901
66.67422.4409-6.57761.1239-1.68397.45530.14190.3309-0.0057-0.02120.24150.7680.2781-0.9452-0.29720.3926-0.0206-0.00690.45030.1070.5268-4.766-18.57-71.703
74.4812-1.1236-2.25553.88270.40796.79240.45850.24820.60640.1676-0.21520.9009-0.3986-1.0108-0.29240.23130.09510.05730.44840.1530.481313.38-26.753-8.061
83.3607-0.5462-2.21693.0593-0.12737.36140.45450.51750.8199-0.37480.089-0.0629-0.8397-0.3321-0.48270.35780.07390.12510.28650.14790.517621.932-21.518-14.153
93.1725-0.46210.17892.44830.84918.70010.24280.36580.5565-0.05060.16740.1152-0.9422-1.1614-0.26970.27820.10810.10940.39110.15860.51315.547-23.414-8.696
109.2902-4.14632.11524.2219-0.47325.46280.27630.6797-0.1692-0.3162-0.08330.41130.3415-0.8587-0.25410.2536-0.07320.00210.42260.07990.297416.734-36.85-16.796
114.7911-0.3793-1.89213.2240.8524.99020.24370.01030.97-0.25810.2847-0.3-0.52010.1364-0.43160.3121-0.03050.09080.18510.03070.365630.342-25.637-13.982
123.05490.529-1.89573.40161.11335.9290.07560.44450.2734-0.36370.19090.06270.0819-0.3249-0.22770.1986-0.0094-0.00140.23290.06570.258831.179-36.327-23.036
135.34440.3729-0.02973.32181.22286.95160.08780.1970.1726-0.27640.3245-0.66930.07490.9749-0.40670.28060.00160.11850.3522-0.09090.414744.009-36.914-27.115
148.1552-1.4228-0.20087.35291.26212.04730.24740.4153-0.493-0.8323-0.1157-0.2660.60710.4103-0.16770.43980.04770.02990.4879-0.1070.325536.921-36.020.19
155.5897-1.3072-1.82036.48061.05197.18730.1329-0.11050.25930.08040.255-0.8439-0.40840.5891-0.33780.2655-0.0536-0.08180.2417-0.1010.31919.662-44.921-60.777
163.39660.50620.82064.3654-1.49289.43570.1741-0.1591-0.06480.31240.1807-0.7375-0.99611.1406-0.1780.287-0.1034-0.06680.3373-0.10730.463321.478-44.143-62.739
176.60846.43526.85016.30996.68267.24290.2067-0.247-0.75771.03560.3617-1.13430.38870.7063-0.68880.51680.1335-0.17090.5048-0.07660.57225.845-56.585-51.723
183.17850.2367-1.27453.1864-0.53082.9644-0.1226-0.41830.15940.49210.2442-0.1329-0.0730.0212-0.09110.290.0654-0.03640.24-0.04340.18035.818-57.285-53.392
193.7128-0.6211-0.47563.46370.01796.5108-0.151-0.6473-0.21210.63350.36220.34410.2669-0.5251-0.23880.39340.05390.05890.43170.1370.291-6.955-63.628-46.299
208.13384.1153-7.3732.1031-3.09232.4044-0.10770.3697-0.07540.02420.25350.35030.2176-0.9037-0.23940.4354-0.0651-0.03530.73810.0510.3214-5.588-57.322-70.395
212.7536-0.3328-0.54636.45740.69145.59010.12110.01070.24510.0017-0.0030.6198-0.3313-0.8156-0.08090.25870.1111-0.01330.42390.13520.387918.976-61.567-12.079
222.9599-0.1164-0.18864.60671.58079.13860.0520.42490.5145-0.20470.02630.414-0.8302-1.51230.05660.35380.14550.06290.51440.18780.47817.744-60.041-10.07
239.5142-6.73732.00555.2802-6.84982.02750.53030.2699-0.3488-0.72490.30710.79870.3423-1.2069-0.65540.4388-0.0393-0.08580.77150.11470.448912.073-72.749-20.59
242.2741-0.9078-0.53182.54940.75063.03120.08210.10450.2464-0.21080.0499-0.0374-0.0582-0.1545-0.1370.22310.00360.00920.23780.09230.200332.519-72.608-15.786
252.6670.1802-0.76781.8515-0.2294.30670.12250.64750.4821-0.4517-0.01670.0742-0.179-0.4205-0.13020.32360.0530.03030.37120.12170.2633.788-73.383-32.482
263.82720.11-0.12932.30510.08725.31140.07570.2127-0.105-0.2193-0.0152-0.29910.4320.3964-0.03770.32840.06240.0520.2690.00960.311145.035-83.431-26.914
274.2166-3.0085-5.18612.00212.88622.4556-0.0647-0.30060.1487-0.12260.284-0.45040.10360.751-0.21680.3531-0.0091-0.02260.5554-0.00690.38445.165-73.841-5.066
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN D AND RESID 700:717 )D700 - 717
2X-RAY DIFFRACTION2( CHAIN D AND RESID 718:731 )D718 - 731
3X-RAY DIFFRACTION3( CHAIN D AND RESID 732:752 )D732 - 752
4X-RAY DIFFRACTION4( CHAIN D AND RESID 753:892 )D753 - 892
5X-RAY DIFFRACTION5( CHAIN D AND RESID 893:978 )D893 - 978
6X-RAY DIFFRACTION6( CHAIN D AND RESID 979:1007 )D979 - 1007
7X-RAY DIFFRACTION7( CHAIN A AND RESID 700:717 )A700 - 717
8X-RAY DIFFRACTION8( CHAIN A AND RESID 718:731 )A718 - 731
9X-RAY DIFFRACTION9( CHAIN A AND RESID 732:752 )A732 - 752
10X-RAY DIFFRACTION10( CHAIN A AND RESID 753:778 )A753 - 778
11X-RAY DIFFRACTION11( CHAIN A AND RESID 779:810 )A779 - 810
12X-RAY DIFFRACTION12( CHAIN A AND RESID 811:892 )A811 - 892
13X-RAY DIFFRACTION13( CHAIN A AND RESID 893:991 )A893 - 991
14X-RAY DIFFRACTION14( CHAIN A AND RESID 992:1007 )A992 - 1007
15X-RAY DIFFRACTION15( CHAIN B AND RESID 701:731 )B701 - 731
16X-RAY DIFFRACTION16( CHAIN B AND RESID 732:752 )B732 - 752
17X-RAY DIFFRACTION17( CHAIN B AND RESID 753:768 )B753 - 768
18X-RAY DIFFRACTION18( CHAIN B AND RESID 769:908 )B769 - 908
19X-RAY DIFFRACTION19( CHAIN B AND RESID 909:978 )B909 - 978
20X-RAY DIFFRACTION20( CHAIN B AND RESID 979:1007 )B979 - 1007
21X-RAY DIFFRACTION21( CHAIN C AND RESID 700:731 )C700 - 731
22X-RAY DIFFRACTION22( CHAIN C AND RESID 732:752 )C732 - 752
23X-RAY DIFFRACTION23( CHAIN C AND RESID 753:768 )C753 - 768
24X-RAY DIFFRACTION24( CHAIN C AND RESID 769:853 )C769 - 853
25X-RAY DIFFRACTION25( CHAIN C AND RESID 854:928 )C854 - 928
26X-RAY DIFFRACTION26( CHAIN C AND RESID 929:978 )C929 - 978
27X-RAY DIFFRACTION27( CHAIN C AND RESID 979:1007 )C979 - 1007

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