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- PDB-7jxm: EGFR kinase (T790M/V948R) in complex with osimertinib and EAI045 -

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Open data


ID or keywords:

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Basic information

Entry
Database: PDB / ID: 7jxm
TitleEGFR kinase (T790M/V948R) in complex with osimertinib and EAI045
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 / regulation of nitric-oxide synthase activity / 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 / regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / eyelid development in camera-type eye / protein insertion into membrane / cerebral cortex cell migration / ERBB2 Regulates Cell Motility / 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 / MAP kinase kinase kinase activity / Estrogen-dependent nuclear events downstream of ESR-membrane signaling / embryonic placenta development / positive regulation of bone resorption / positive regulation of G1/S transition of mitotic cell cycle / GAB1 signalosome / positive regulation of nitric oxide mediated signal transduction / 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 / cellular response to cadmium ion / GRB2 events in EGFR signaling / SHC1 events in EGFR signaling / positive regulation of DNA repair / EGFR Transactivation by Gastrin / 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 / ossification / positive regulation of synaptic transmission, glutamatergic / neurogenesis / cellular response to dexamethasone stimulus / basal plasma membrane / regulation of ERK1 and ERK2 cascade / neuron projection morphogenesis / positive regulation of superoxide anion generation / positive regulation of DNA replication / Signal transduction by L1 / epithelial cell proliferation / cellular response to estradiol stimulus / NOTCH3 Activation and Transmission of Signal to the Nucleus / positive regulation of epithelial cell proliferation / astrocyte activation / liver regeneration / positive regulation of protein localization to plasma membrane / EGFR downregulation / cell surface receptor protein tyrosine kinase signaling pathway / 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 / clathrin-coated endocytic vesicle membrane / lung development / Constitutive Signaling by EGFRvIII / Signaling by ERBB2 ECD mutants / epidermal growth factor receptor signaling pathway / Signaling by ERBB2 KD Mutants / negative regulation of protein catabolic process / receptor protein-tyrosine kinase / Downregulation of ERBB2 signaling / kinase binding / ruffle membrane
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
Chem-9LL / PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / Chem-YY3 / Epidermal growth factor receptor
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.192 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 Commun / Year: 2022
Title: Molecular basis for cooperative binding and synergy of ATP-site and allosteric EGFR inhibitors
Authors: Beyett, T.S. / To, C. / Heppner, D.E. / Rana, J.K. / Schmoker, A.M. / Jang, J. / De Clercq, D.J.H. / Gomez, G. / Scott, D.A. / Gray, N.S. / Janne, P.A. / Eck, M.J.
History
DepositionAug 27, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0Sep 8, 2021Provider: repository / Type: Initial release
Revision 1.1May 18, 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.journal_volume / _citation.page_first / _citation.pdbx_database_id_DOI / _citation.title / _citation.year
Revision 1.2Oct 18, 2023Group: Data collection / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_initial_refinement_model / struct_ncs_dom_lim
Item: _struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id ..._struct_ncs_dom_lim.beg_auth_comp_id / _struct_ncs_dom_lim.beg_label_asym_id / _struct_ncs_dom_lim.beg_label_comp_id / _struct_ncs_dom_lim.beg_label_seq_id / _struct_ncs_dom_lim.end_auth_comp_id / _struct_ncs_dom_lim.end_label_asym_id / _struct_ncs_dom_lim.end_label_comp_id / _struct_ncs_dom_lim.end_label_seq_id

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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
C: Epidermal growth factor receptor
B: Epidermal growth factor receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)153,75613
Polymers150,8984
Non-polymers2,8589
Water3,729207
1
C: Epidermal growth factor receptor
hetero molecules

D: Epidermal growth factor receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)76,8947
Polymers75,4492
Non-polymers1,4445
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation1_556x,y,z+11
Buried area5140 Å2
ΔGint-42 kcal/mol
Surface area26120 Å2
MethodPISA
2
A: Epidermal growth factor receptor
hetero molecules

B: Epidermal growth factor receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)76,8636
Polymers75,4492
Non-polymers1,4144
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation1_656x+1,y,z+11
Buried area4190 Å2
ΔGint-32 kcal/mol
Surface area26000 Å2
MethodPISA
Unit cell
Length a, b, c (Å)72.548, 103.224, 87.043
Angle α, β, γ (deg.)90.000, 101.550, 90.000
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 702 through 748 or resid 755...
21(chain B and (resid 702 through 748 or resid 755...
31(chain C and (resid 702 through 748 or resid 755...
41(chain D and (resid 702 through 748 or resid 755...

NCS domain segments:

Ens-ID: 1

Dom-IDComponent-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11ALAALAARGARG(chain A and (resid 702 through 748 or resid 755...AB702 - 74811 - 57
12ALAALALEULEU(chain A and (resid 702 through 748 or resid 755...AB755 - 85864 - 167
13VALVALLEULEU(chain A and (resid 702 through 748 or resid 755...AB876 - 907185 - 216
14THRTHRASPASP(chain A and (resid 702 through 748 or resid 755...AB909 - 1006218 - 315
21ALAALAARGARG(chain B and (resid 702 through 748 or resid 755...BD702 - 74811 - 57
22ALAALALEULEU(chain B and (resid 702 through 748 or resid 755...BD755 - 85864 - 167
23VALVALLEULEU(chain B and (resid 702 through 748 or resid 755...BD876 - 907185 - 216
24THRTHRARGARG(chain B and (resid 702 through 748 or resid 755...BD909 - 986218 - 295
25PROPROASPASP(chain B and (resid 702 through 748 or resid 755...BD990 - 1006299 - 315
31ALAALAARGARG(chain C and (resid 702 through 748 or resid 755...CC702 - 74811 - 57
32ALAALALEULEU(chain C and (resid 702 through 748 or resid 755...CC755 - 85864 - 167
33VALVALLEULEU(chain C and (resid 702 through 748 or resid 755...CC876 - 907185 - 216
34THRTHRARGARG(chain C and (resid 702 through 748 or resid 755...CC909 - 986218 - 295
35PROPROASPASP(chain C and (resid 702 through 748 or resid 755...CC990 - 1006299 - 315
41ALAALAARGARG(chain D and (resid 702 through 748 or resid 755...DA702 - 74811 - 57
42ALAALALEULEU(chain D and (resid 702 through 748 or resid 755...DA755 - 90764 - 216
43THRTHRARGARG(chain D and (resid 702 through 748 or resid 755...DA909 - 986218 - 295
44PROPROASPASP(chain D and (resid 702 through 748 or resid 755...DA990 - 1006299 - 315

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Components

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Protein , 1 types, 4 molecules DACB

#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

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Non-polymers , 5 types, 216 molecules

#2: Chemical ChemComp-ANP / PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER


Mass: 506.196 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: C10H17N6O12P3 / Comment: AMP-PNP, energy-carrying molecule analogue*YM
#3: Chemical ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 3 / Source method: obtained synthetically / Formula: Mg
#4: Chemical ChemComp-9LL / (2R)-2-(5-fluoro-2-hydroxyphenyl)-2-(1-oxo-1,3-dihydro-2H-isoindol-2-yl)-N-(1,3-thiazol-2-yl)acetamide


Mass: 383.396 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C19H14FN3O3S / Feature type: SUBJECT OF INVESTIGATION
#5: Chemical ChemComp-YY3 / N-(2-{[2-(dimethylamino)ethyl](methyl)amino}-4-methoxy-5-{[4-(1-methyl-1H-indol-3-yl)pyrimidin-2-yl]amino}phenyl)prop-2-enamide / Osimertinib / AZD 9291 / Osimertinib


Mass: 499.607 Da / Num. of mol.: 1 / Source method: obtained synthetically / Formula: C28H33N7O2 / Feature type: SUBJECT OF INVESTIGATION / Comment: medication, inhibitor*YM
#6: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 207 / Source method: isolated from a natural source / Formula: H2O

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Details

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: 2.12 Å3/Da / Density % sol: 41.87 %
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5.5 / Details: 0.1 M Bis-Tris pH 5.5, 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: Oct 18, 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: 2.19→49.909 Å / Num. obs: 120584 / % possible obs: 97.4 % / Redundancy: 3.442 % / Biso Wilson estimate: 42.21 Å2 / CC1/2: 0.973 / Rmerge(I) obs: 0.208 / Rrim(I) all: 0.247 / Χ2: 0.775 / Net I/σ(I): 8.95
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Rmerge(I) obsMean I/σ(I) obsNum. measured obsNum. possibleNum. unique obsCC1/2Rrim(I) all% possible all
2.19-2.323.2040.8121.56306741036695740.7020.97792.4
2.32-2.483.5540.6442.6234307977496520.8040.7698.8
2.48-2.683.5110.5483.9331541909189830.8470.64998.8
2.68-2.943.3360.4936.2327280839081780.8170.58997.5
2.94-3.283.6160.3849.8827134757775030.8840.45299
3.28-3.793.5240.27215.0823417671966450.8920.32298.9
3.79-4.633.380.1519.7218707568655350.9460.1897.3
4.63-6.523.5810.09921.615672442743770.9850.11698.9
6.52-49.9093.1580.05223.997718252824440.9950.06396.7

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Processing

Software
NameVersionClassification
XSCALEdata scaling
PHENIX1.11.1_2575refinement
PDB_EXTRACT3.25data extraction
xia2data reduction
PHASERphasing
Cootmodel building
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5D41

5d41


Resolution: 2.192→49.909 Å / SU ML: 0.36 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 30.29 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2705 3812 3.16 %
Rwork0.2266 116772 -
obs0.228 120584 94.92 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 117.08 Å2 / Biso mean: 51.8507 Å2 / Biso min: 23.25 Å2
Refinement stepCycle: final / Resolution: 2.192→49.909 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9359 0 187 207 9753
Biso mean--51.19 46.76 -
Num. residues----1159
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0099769
X-RAY DIFFRACTIONf_angle_d1.07113241
X-RAY DIFFRACTIONf_chiral_restr0.0611467
X-RAY DIFFRACTIONf_plane_restr0.0071643
X-RAY DIFFRACTIONf_dihedral_angle_d16.9765899
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A5584X-RAY DIFFRACTION11.436TORSIONAL
12B5584X-RAY DIFFRACTION11.436TORSIONAL
13C5584X-RAY DIFFRACTION11.436TORSIONAL
14D5584X-RAY DIFFRACTION11.436TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection Rwork% reflection obs (%)
2.192-2.21930.35771090.345315370
2.2193-2.24850.41331330.3218396587
2.2485-2.27930.3281320.3095419793
2.2793-2.31180.33721420.2989436995
2.3118-2.34630.32851420.2914438396
2.3463-2.3830.29941440.2804442196
2.383-2.42210.31481420.2889440497
2.4221-2.46380.32091460.2827436797
2.4638-2.50860.36421410.3084446097
2.5086-2.55690.30861440.2897440897
2.5569-2.60910.41881460.2908440397
2.6091-2.66580.38211420.2742437997
2.6658-2.72780.2721430.2631441596
2.7278-2.7960.29511420.2643435895
2.796-2.87160.34721360.2627420493
2.8716-2.95610.30871380.266427995
2.9561-3.05150.27641450.2568444497
3.0515-3.16050.29781450.2606448398
3.1605-3.2870.27451480.243446098
3.287-3.43660.29261430.2359442497
3.4366-3.61780.31981450.2347444797
3.6178-3.84430.29131430.2178440997
3.8443-4.1410.25231400.1893432595
4.141-4.55750.20951390.1675433495
4.5575-5.21640.19711510.1698448098
5.2164-6.56970.20171440.1876445498
6.5697-49.9090.19171470.1789434796
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)
19.12632.5804-1.824.1068-1.96064.0824-0.0021-0.0150.580.15360.0376-0.0522-0.58370.04720.08230.38110.0874-0.04990.31890.03960.3862-3.674-13.08221.774
21.54240.98820.95742.88230.7762.8098-0.16230.04460.6602-0.0716-0.11090.3563-0.4751-0.27420.28060.4350.04040.03890.40820.09420.50941.609-9.82323.703
34.4596-1.04661.17383.4956-0.34493.6070.1728-0.2216-0.35-0.0794-0.1140.1390.3323-0.2053-0.06630.2890.01730.01640.2926-0.0210.22085.915-28.20533.957
42.7259-0.51650.37792.04170.90265.9595-0.01850.02670.4728-0.11960.03670.0181-0.4802-0.1283-0.03880.30570.0090.01070.25780.05090.3518.002-18.71841.425
53.5196-0.5982-1.05194.39182.21484.7239-0.1919-0.3018-0.09810.60250.1008-0.31420.50310.40350.07720.3570.0127-0.02010.3420.09430.277911.622-27.39950.229
60.783-1.0491.98551.6153-0.03328.84250.1204-0.1812-0.2425-0.4342-0.1-0.2451.50760.3281-0.03390.55030.02560.03640.38780.03320.53518.347-39.528.087
73.6141-0.22910.12563.1687-0.40752.9681-0.0164-0.6218-0.31380.11740.05620.26610.712-0.5768-0.00350.4107-0.11020.00650.58160.11630.440312.739-37.17796.631
82.58230.3381-0.76125.31411.65294.7705-0.11150.0246-0.3833-0.0219-0.16960.35820.5688-0.63230.07480.4728-0.0888-0.11710.51320.09580.526712.235-37.23898.876
95.58420.2549-1.91036.64321.29683.6329-0.19620.6117-0.7073-0.57060.20470.21031.0667-0.2375-0.03870.6545-0.0377-0.06890.31330.02130.324921.906-42.40492.736
103.6150.6764-0.99761.15640.70365.1410.1441-0.0438-0.0514-0.1099-0.01830.17220.0468-0.3134-0.11670.23660.0012-0.01830.21150.02690.223925.711-25.66885.612
112.7628-0.23681.28813.96680.83545.19550.21840.0445-0.5476-0.35440.02490.24880.8057-0.3604-0.20720.4041-0.0332-0.05450.3022-0.00320.34324.166-32.47271.151
123.33660.14671.36594.58720.96295.5667-0.12450.5372-0.1123-0.61520.4314-0.55760.18220.5621-0.19960.39620.01380.07010.3201-0.0070.277133.743-25.33666.985
134.00840.1671.33077.6581.34276.2036-0.20250.2411-0.0023-0.6580.388-1.4462-0.49461.1105-0.15640.3251-0.05960.05960.3775-0.01460.3640.288-19.54478.904
141.71381.9642-3.05512.5938-4.15629.8920.0975-0.07370.43950.5417-0.0185-0.1272-1.10710.3156-0.30490.4925-0.0364-0.00950.4556-0.1070.626829.131-13.75392.475
154.8853-1.8048-0.47754.6569-1.53446.6216-0.3088-0.6634-1.03770.42820.5230.79660.5255-0.7078-0.08020.3798-0.1291-0.01090.41240.17160.6331-20.87-43.455100.196
164.2987-0.0657-2.26352.09210.0666.267-0.21850.2296-0.50730.2128-0.10810.37970.8926-1.04870.24360.4677-0.0477-0.04730.39110.03750.4867-22.316-40.24195.749
176.51620.5903-3.23872.0985-2.40985.706-0.50270.4727-1.41680.30840.3277-0.37680.9908-0.23940.34340.5315-0.0348-0.05160.3497-0.01610.593-10.55-45.38592.733
184.12941.3748-0.68933.4415-0.61315.01630.17530.1250.08250.05490.10820.1205-0.2157-0.3861-0.30280.3073-0.0097-0.02470.3118-0.01620.2331-11.393-26.36684.226
193.038-0.25970.86253.17330.71924.60790.2260.0713-0.78890.18880.046-0.10250.86320.1478-0.30920.3196-0.028-0.0460.32130.00440.4033-10.003-37.95378.254
203.07330.12470.92693.76630.55094.44850.03170.614-0.2156-0.53470.1189-0.46-0.05370.4579-0.17860.31110.02540.06490.4608-0.03120.2978-5.975-27.55568.935
212.60531.6479-3.44491.1641-0.25988.7922-0.0224-0.19030.1604-0.138-0.0963-0.4231-0.33030.68290.09940.42040.0356-0.01030.4137-0.02110.4181-9.256-14.65890.277
222.16870.72140.32412.63760.33651.39350.0731-0.20940.42510.0993-0.02680.3539-0.4882-0.23130.00190.44410.08660.06020.35340.02060.3584-34.387-9.35524.817
233.11580.3849-0.57042.80460.20164.99320.1055-0.2328-0.05660.32610.02370.01130.09810.1578-0.11390.27310.03820.03080.32570.04630.2314-27.241-25.81144.482
241.6357-1.7782.25982.8313-0.78085.303-0.2714-0.4162-0.09240.3208-0.3594-1.08210.15230.59390.34320.5252-0.0296-0.00610.45830.07780.5798-27.638-34.2623.023
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN D AND RESID 700:731 )D700 - 731
2X-RAY DIFFRACTION2( CHAIN D AND RESID 732:786 )D732 - 786
3X-RAY DIFFRACTION3( CHAIN D AND RESID 787:830 )D787 - 830
4X-RAY DIFFRACTION4( CHAIN D AND RESID 831:908 )D831 - 908
5X-RAY DIFFRACTION5( CHAIN D AND RESID 909:978 )D909 - 978
6X-RAY DIFFRACTION6( CHAIN D AND RESID 979:1007 )D979 - 1007
7X-RAY DIFFRACTION7( CHAIN A AND RESID 700:731 )A700 - 731
8X-RAY DIFFRACTION8( CHAIN A AND RESID 732:755 )A732 - 755
9X-RAY DIFFRACTION9( CHAIN A AND RESID 756:786 )A756 - 786
10X-RAY DIFFRACTION10( CHAIN A AND RESID 787:853 )A787 - 853
11X-RAY DIFFRACTION11( CHAIN A AND RESID 854:928 )A854 - 928
12X-RAY DIFFRACTION12( CHAIN A AND RESID 929:960 )A929 - 960
13X-RAY DIFFRACTION13( CHAIN A AND RESID 961:978 )A961 - 978
14X-RAY DIFFRACTION14( CHAIN A AND RESID 979:1007 )A979 - 1007
15X-RAY DIFFRACTION15( CHAIN C AND RESID 702:717 )C702 - 717
16X-RAY DIFFRACTION16( CHAIN C AND RESID 718:755 )C718 - 755
17X-RAY DIFFRACTION17( CHAIN C AND RESID 756:786 )C756 - 786
18X-RAY DIFFRACTION18( CHAIN C AND RESID 787:830 )C787 - 830
19X-RAY DIFFRACTION19( CHAIN C AND RESID 831:892 )C831 - 892
20X-RAY DIFFRACTION20( CHAIN C AND RESID 893:978 )C893 - 978
21X-RAY DIFFRACTION21( CHAIN C AND RESID 979:1006 )C979 - 1006
22X-RAY DIFFRACTION22( CHAIN B AND RESID 701:797 )B701 - 797
23X-RAY DIFFRACTION23( CHAIN B AND RESID 798:991 )B798 - 991
24X-RAY DIFFRACTION24( CHAIN B AND RESID 992:1012 )B992 - 1012

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