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- PDB-7jxl: EGFR kinase (T790M/V948R) in complex with AZ5104 -

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ID or keywords:

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Basic information

Entry
Database: PDB / ID: 7jxl
TitleEGFR kinase (T790M/V948R) in complex with AZ5104
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-VO7 / Epidermal growth factor receptor
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.4 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)152,8418
Polymers150,8984
Non-polymers1,9424
Water2,144119
1
B: Epidermal growth factor receptor
hetero molecules

D: Epidermal growth factor receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)76,4204
Polymers75,4492
Non-polymers9712
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation1_554x,y,z-11
Buried area3080 Å2
ΔGint-19 kcal/mol
Surface area26100 Å2
MethodPISA
2
A: Epidermal growth factor receptor
hetero molecules

C: Epidermal growth factor receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)76,4204
Polymers75,4492
Non-polymers9712
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
crystal symmetry operation1_554x,y,z-11
Buried area3170 Å2
ΔGint-19 kcal/mol
Surface area26160 Å2
MethodPISA
Unit cell
Length a, b, c (Å)71.054, 101.326, 86.952
Angle α, β, γ (deg.)90.000, 101.360, 90.000
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 701 through 860 or resid 877...
21(chain B and (resid 701 through 750 or resid 756...
31(chain C and (resid 701 through 749 or resid 755...
41(chain D and (resid 701 through 750 or resid 756...

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
11GLNGLNLYSLYS(chain A and (resid 701 through 860 or resid 877...AB701 - 86010 - 169
12PROPROLEULEU(chain A and (resid 701 through 860 or resid 877...AB877 - 907186 - 216
13THRTHRASPASP(chain A and (resid 701 through 860 or resid 877...AB909 - 984218 - 293
14SERSERGLUGLU(chain A and (resid 701 through 860 or resid 877...AB991 - 1005300 - 314
15VO7VO7VO7VO7(chain A and (resid 701 through 860 or resid 877...AF1101
21GLNGLNALAALA(chain B and (resid 701 through 750 or resid 756...BD701 - 75010 - 59
22ASNASNLYSLYS(chain B and (resid 701 through 750 or resid 756...BD756 - 86065 - 169
23PROPROLEULEU(chain B and (resid 701 through 750 or resid 756...BD877 - 907186 - 216
24THRTHRVO7VO7(chain B and (resid 701 through 750 or resid 756...BD - H909 - 1101218
31GLNGLNGLUGLU(chain C and (resid 701 through 749 or resid 755...CC701 - 74910 - 58
32ALAALALYSLYS(chain C and (resid 701 through 749 or resid 755...CC755 - 86064 - 169
33PROPROLEULEU(chain C and (resid 701 through 749 or resid 755...CC877 - 907186 - 216
34THRTHRASPASP(chain C and (resid 701 through 749 or resid 755...CC909 - 984218 - 293
35SERSERGLUGLU(chain C and (resid 701 through 749 or resid 755...CC991 - 1005300 - 314
36VO7VO7VO7VO7(chain C and (resid 701 through 749 or resid 755...CG1101
41GLNGLNALAALA(chain D and (resid 701 through 750 or resid 756...DA701 - 75010 - 59
42ASNASNLEULEU(chain D and (resid 701 through 750 or resid 756...DA756 - 90765 - 216
43THRTHRASPASP(chain D and (resid 701 through 750 or resid 756...DA909 - 984218 - 293
44SERSERGLUGLU(chain D and (resid 701 through 750 or resid 756...DA991 - 1005300 - 314
45VO7VO7VO7VO7(chain D and (resid 701 through 750 or resid 756...DE1101

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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-VO7 / N-(2-{[2-(dimethylamino)ethyl](methyl)amino}-5-{[4-(1H-indol-3-yl)pyrimidin-2-yl]amino}-4-methoxyphenyl)propanamide / AZ5104


Mass: 485.581 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C27H31N7O2 / Feature type: SUBJECT OF INVESTIGATION
#3: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 119 / 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: 2.03 Å3/Da / Density % sol: 39.52 % / Mosaicity: 0.136 °
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: Jul 25, 2019
RadiationMonochromator: Double Crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9792 Å / Relative weight: 1
ReflectionResolution: 2.4→65.23 Å / Num. obs: 47165 / % possible obs: 99.7 % / Redundancy: 7 % / Biso Wilson estimate: 39.81 Å2 / Rpim(I) all: 0.07 / Rrim(I) all: 0.186 / Net I/σ(I): 11.2 / Num. measured all: 330030
Reflection shell

Diffraction-ID: 1 / % possible all: 99.7

Resolution (Å)Redundancy (%)Mean I/σ(I) obsNum. measured allNum. unique obsRpim(I) allRrim(I) all
2.4-2.4471.81635923470.6031.603
6.51-65.266.732.91616524210.0270.071

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Processing

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

5d41


Resolution: 2.4→60.05 Å / SU ML: 0.31 / Cross valid method: THROUGHOUT / σ(F): 1.38 / Phase error: 26.95 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2393 2307 4.9 %
Rwork0.2089 44818 -
obs0.2104 47125 99.57 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 109.77 Å2 / Biso mean: 51.1253 Å2 / Biso min: 25.28 Å2
Refinement stepCycle: final / Resolution: 2.4→60.05 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9385 0 144 119 9648
Biso mean--50.63 45.49 -
Num. residues----1163
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A5485X-RAY DIFFRACTION10.928TORSIONAL
12B5485X-RAY DIFFRACTION10.928TORSIONAL
13C5485X-RAY DIFFRACTION10.928TORSIONAL
14D5485X-RAY DIFFRACTION10.928TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 16

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.4-2.450.32521630.268227702933100
2.45-2.510.3161440.252627912935100
2.51-2.570.27731440.255527922936100
2.57-2.640.31251230.247528402963100
2.64-2.720.32161360.255228022938100
2.72-2.810.30671490.247827772926100
2.81-2.910.3051520.2512771292399
2.91-3.020.28691650.23752744290999
3.02-3.160.29171290.2392786291598
3.16-3.330.30121300.217328132943100
3.33-3.540.2751450.221328232968100
3.54-3.810.19861420.203328002942100
3.81-4.190.21451380.18528282966100
4.19-4.80.20271620.16922779294199
4.8-6.050.19721390.195728292968100
6.05-60.050.16991460.18092873301999
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)
15.9838-0.8375-0.04824.5815-0.29736.0336-0.00610.0779-0.3213-0.1880.00610.1150.8282-0.52390.04810.502-0.14770.01570.3686-0.00260.419-1.413-34.211-23.716
23.4897-1.2251-2.18143.20570.96364.55440.04490.3116-0.3124-0.036-0.14840.23410.8216-0.80880.07660.4591-0.1875-0.00090.36970.02110.4533-2.78-34.566-21.533
38.27568.9791-1.07832.0493-1.45155.1564-0.6290.2658-0.6419-0.58390.5741-0.83150.91450.02640.0450.4629-0.01240.01180.2654-0.01410.400310.043-43.738-28.14
43.8940.0829-1.59392.3351-1.0655.57320.09650.14780.0530.039-0.0510.12750.0166-0.2485-0.01960.23240.0055-0.02320.1985-0.04770.2167.38-23.338-34.596
53.4781-0.2250.85383.4591.50833.65120.23990.1938-0.1778-0.1683-0.1076-0.17770.30760.1073-0.10890.30150.06710.03120.28340.05620.239212.208-23.257-50.753
60.41640.3468-2.4227-0.0338-0.72289.46230.13560.05490.14560.1949-0.114-0.4146-1.33860.1825-0.00390.5874-0.10630.05870.42180.00790.69197.388-6.796-31.239
73.7872-0.37942.4753.6429-0.47632.2809-0.0246-0.14090.3469-0.1505-0.13510.3138-0.6913-0.39550.29330.34970.0931-0.00360.4740.03540.4619-22.127-6.559-94.931
82.90940.53583.57472.0121-0.16752.1578-0.47880.03090.53270.1658-0.01940.6635-0.9937-0.69970.25990.46730.102-0.0050.35370.0180.4357-22.91-7.011-98.139
95.78750.0211.34174.44010.35014.8626-0.0201-0.16360.89640.1108-0.0834-0.0687-1.01740.08380.13350.4524-0.0395-0.04370.35210.05060.4837-12.549-2.703-92.023
105.0512-1.72281.57514.305-2.06798.0230.2249-0.2879-0.7048-0.29730.13220.49610.7206-0.5567-0.32710.2725-0.0442-0.05930.3364-0.00360.3542-16.963-25.857-84.403
112.85320.88620.31162.9724-0.50634.80410.0639-0.2270.40490.34030.00750.222-0.4795-0.1203-0.04210.22480.02430.01370.259-0.02630.2852-7.654-14.869-76.323
123.64041.67840.35274.8178-0.57375.87110.0322-0.69630.0690.5647-0.1362-0.3153-0.01780.51230.0030.38380.038-0.05310.4513-0.00750.2912-0.743-21.437-67.167
132.8358-1.25451.92244.6280.36096.82790.1420.2669-0.55660.23440.1571-0.44180.91910.527-0.33070.37460.0957-0.00010.34230.01340.343-0.647-32.329-80.629
148.5274-1.29247.2421.3549-0.68287.9076-0.3702-0.54340.60920.07150.1454-0.27760.73160.52640.2190.5060.0959-0.02290.5825-0.04690.3797-5.931-28.044-97.364
154.22610.0034-0.31012.97330.11778.64810.2141-0.3226-0.58970.0377-0.09590.07331.65160.3823-0.06280.47560.03-0.07470.30890.04120.3623-38.2-33.801-22.638
162.54210.1444-0.78721.2818-0.01297.697-0.03030.2878-0.19-0.09950.087-0.0130.57790.4052-0.08870.2570.0269-0.05920.3823-0.00890.3072-30.782-26.738-30.277
172.0072-1.12560.13294.40440.80446.64450.09310.1632-0.0202-0.4810.1544-0.2268-0.15710.6066-0.18420.3031-0.06190.02710.58530.03420.2904-26.121-20.751-49.129
181.20441.2099-0.7912.388-1.02345.1476-0.50130.26310.2978-0.3770.3077-0.3286-1.00740.10320.28810.7023-0.044-0.02210.5256-0.01080.4977-27.935-6.328-27.584
194.85751.05962.76665.61172.84927.7683-0.29250.40760.4647-0.5458-0.05510.4447-0.7449-0.5090.40290.37620.1359-0.01380.39970.03250.444412.982-4.95-99.847
203.48021.75312.90422.73852.44177.4922-0.03010.45670.8008-0.4482-0.32410.4878-1.3689-0.58150.32550.46960.03120.06550.53630.02380.494511.562-4.815-101.954
214.1969-0.5851.7123.3251-0.27666.16290.0126-0.0530.27360.12080.08490.06660.1116-0.0021-0.10.204-0.00860.07640.2939-0.02210.239223.69-10.83-89.851
223.2165-0.401-0.10814.98550.89538.5615-0.0901-0.2525-0.08320.54350.1184-0.13380.5620.35230.01420.25870.0263-0.02720.28130.00050.256428.059-13.431-72.718
232.1843-1.16483.84122.0018-1.56555.95720.45280.1369-0.4290.84210.0189-0.16860.69770.8171-0.44810.8970.0489-0.14660.4637-0.07710.637127.202-28.924-94.199
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 732:752 )D732 - 752
3X-RAY DIFFRACTION3( CHAIN D AND RESID 753:768 )D753 - 768
4X-RAY DIFFRACTION4( CHAIN D AND RESID 769:853 )D769 - 853
5X-RAY DIFFRACTION5( CHAIN D AND RESID 854:978 )D854 - 978
6X-RAY DIFFRACTION6( CHAIN D AND RESID 979:1007 )D979 - 1007
7X-RAY DIFFRACTION7( CHAIN A AND RESID 701:731 )A701 - 731
8X-RAY DIFFRACTION8( CHAIN A AND RESID 732:755 )A732 - 755
9X-RAY DIFFRACTION9( CHAIN A AND RESID 756:790 )A756 - 790
10X-RAY DIFFRACTION10( CHAIN A AND RESID 791:810 )A791 - 810
11X-RAY DIFFRACTION11( CHAIN A AND RESID 811:928 )A811 - 928
12X-RAY DIFFRACTION12( CHAIN A AND RESID 929:960 )A929 - 960
13X-RAY DIFFRACTION13( CHAIN A AND RESID 961:991 )A961 - 991
14X-RAY DIFFRACTION14( CHAIN A AND RESID 992:1013 )A992 - 1013
15X-RAY DIFFRACTION15( CHAIN C AND RESID 700:731 )C700 - 731
16X-RAY DIFFRACTION16( CHAIN C AND RESID 732:853 )C732 - 853
17X-RAY DIFFRACTION17( CHAIN C AND RESID 854:978 )C854 - 978
18X-RAY DIFFRACTION18( CHAIN C AND RESID 979:1007 )C979 - 1007
19X-RAY DIFFRACTION19( CHAIN B AND RESID 700:731 )B700 - 731
20X-RAY DIFFRACTION20( CHAIN B AND RESID 732:752 )B732 - 752
21X-RAY DIFFRACTION21( CHAIN B AND RESID 753:853 )B753 - 853
22X-RAY DIFFRACTION22( CHAIN B AND RESID 854:978 )B854 - 978
23X-RAY DIFFRACTION23( CHAIN B AND RESID 979:1005 )B979 - 1005

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