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- PDB-7ltx: EGFR (T790M/V948R) in complex with quinazolinone allosteric inhibitor -

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Open data


ID or keywords:

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Basic information

Entry
Database: PDB / ID: 7ltx
TitleEGFR (T790M/V948R) in complex with quinazolinone allosteric inhibitor
ComponentsEpidermal growth factor receptor
KeywordsTRANSFERASE/Inhibitor / EGFR / kinase / allosteric / inhibitor / quinazolinone / 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
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / Chem-YFA / Epidermal growth factor receptor
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.3 Å
AuthorsBeyett, T.S. / Eck, M.J.
Funding support United States, 2items
OrganizationGrant numberCountry
National Institutes of Health/National Cancer Institute (NIH/NCI)2R01CA201049-06 United States
National Institutes of Health/National Cancer Institute (NIH/NCI)1F32CA247198-01 United States
CitationJournal: Bioorg.Med.Chem.Lett. / Year: 2022
Title: Quinazolinones as allosteric fourth-generation EGFR inhibitors for the treatment of NSCLC.
Authors: Gero, T.W. / Heppner, D.E. / Beyett, T.S. / To, C. / Azevedo, S.C. / Jang, J. / Bunnell, T. / Feru, F. / Li, Z. / Shin, B.H. / Soroko, K.M. / Gokhale, P.C. / Gray, N.S. / Janne, P.A. / Eck, M.J. / Scott, D.A.
History
DepositionFeb 20, 2021Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 23, 2022Provider: repository / Type: Initial release
Revision 1.1Apr 13, 2022Group: Database references / Category: citation / citation_author
Item: _citation.country / _citation.journal_abbrev ..._citation.country / _citation.journal_abbrev / _citation.journal_id_ASTM / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.pdbx_database_id_DOI / _citation.title / _citation.year
Revision 1.2Apr 20, 2022Group: Database references / Category: citation / citation_author
Item: _citation.page_first / _citation.page_last ..._citation.page_first / _citation.page_last / _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.name
Revision 1.3May 18, 2022Group: Database references / Category: citation / citation_author / Item: _citation.journal_volume / _citation_author.name
Revision 1.4Oct 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
A: Epidermal growth factor receptor
B: Epidermal growth factor receptor
C: Epidermal growth factor receptor
D: Epidermal growth factor receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)155,23516
Polymers150,8984
Non-polymers4,33712
Water2,828157
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A: Epidermal growth factor receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,8094
Polymers37,7251
Non-polymers1,0843
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
B: Epidermal growth factor receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,8094
Polymers37,7251
Non-polymers1,0843
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
C: Epidermal growth factor receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,8094
Polymers37,7251
Non-polymers1,0843
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
D: Epidermal growth factor receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,8094
Polymers37,7251
Non-polymers1,0843
Water181
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)56.888, 73.488, 150.217
Angle α, β, γ (deg.)90.000, 99.630, 90.000
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 700 through 907 or resid 909 through 1007 or resid 1101 through 1201))
21(chain B and (resid 700 through 859 or resid 876...
31(chain C and (resid 700 through 907 or resid 909 through 1007 or resid 1101 through 1201))
41(chain D and (resid 700 through 859 or resid 876...

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
11ASNASNLEULEU(chain A and (resid 700 through 907 or resid 909 through 1007 or resid 1101 through 1201))AA700 - 9079 - 216
12THRTHRMETMET(chain A and (resid 700 through 907 or resid 909 through 1007 or resid 1101 through 1201))AA909 - 1007218 - 316
13ANPANPHOHHOH(chain A and (resid 700 through 907 or resid 909 through 1007 or resid 1101 through 1201))AE - Q1101 - 1201
21ASNASNALAALA(chain B and (resid 700 through 859 or resid 876...BB700 - 8599 - 168
22VALVALLEULEU(chain B and (resid 700 through 859 or resid 876...BB876 - 907185 - 216
23THRTHRMETMET(chain B and (resid 700 through 859 or resid 876...BB909 - 1007218 - 316
24ANPANPHOHHOH(chain B and (resid 700 through 859 or resid 876...BH - R1101 - 1201
31ASNASNLEULEU(chain C and (resid 700 through 907 or resid 909 through 1007 or resid 1101 through 1201))CC700 - 9079 - 216
32THRTHRMETMET(chain C and (resid 700 through 907 or resid 909 through 1007 or resid 1101 through 1201))CC909 - 1007218 - 316
33ANPANPHOHHOH(chain C and (resid 700 through 907 or resid 909 through 1007 or resid 1101 through 1201))CK - S1101 - 1201
41ASNASNALAALA(chain D and (resid 700 through 859 or resid 876...DD700 - 8599 - 168
42VALVALLEULEU(chain D and (resid 700 through 859 or resid 876...DD876 - 907185 - 216
43THRTHRMETMET(chain D and (resid 700 through 859 or resid 876...DD909 - 1007218 - 316
44ANPANPHOHHOH(chain D and (resid 700 through 859 or resid 876...DN - T1101 - 1201

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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-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
#3: Chemical
ChemComp-MG / MAGNESIUM ION


Mass: 24.305 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: Mg
#4: Chemical
ChemComp-YFA / (2R)-2-{5-fluoro-6-[4-(1-methylpiperidin-4-yl)phenyl]-4-oxoquinazolin-3(4H)-yl}-2-phenyl-N-(1,3-thiazol-2-yl)acetamide


Mass: 553.650 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C31H28FN5O2S / Feature type: SUBJECT OF INVESTIGATION
#5: Water ChemComp-HOH / water / Water


Mass: 18.015 Da / Num. of mol.: 157 / 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: 2.05 Å3/Da / Density % sol: 40.04 % / Mosaicity: 0.148 °
Crystal growTemperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5.5 / Details: 0.1 M Bis-Tris pH 5.5, 30% (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-C / Wavelength: 0.9793 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Jul 13, 2019
RadiationMonochromator: Double Crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9793 Å / Relative weight: 1
ReflectionResolution: 2.3→148.1 Å / Num. obs: 53925 / % possible obs: 98.9 % / Redundancy: 6.6 % / Biso Wilson estimate: 44.5 Å2 / Rpim(I) all: 0.051 / Rrim(I) all: 0.132 / Net I/σ(I): 8.5 / Num. measured all: 358220
Reflection shell

Diffraction-ID: 1

Resolution (Å)Redundancy (%)Mean I/σ(I) obsNum. measured allNum. unique obsRpim(I) allRrim(I) all% possible all
2.3-2.346.60.91793926990.461.18499.7
6.24-148.416.731.71891228030.0210.05399.1

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Processing

Software
NameVersionClassification
xia2data scaling
PHENIX1.19.1_4122refinement
PDB_EXTRACT3.27data extraction
xia2data reduction
PHASERphasing
Cootmodel building
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 6DUK

6duk


Resolution: 2.3→148.1 Å / SU ML: 0.29 / Cross valid method: THROUGHOUT / σ(F): 1.34 / Phase error: 23.62 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.216 2600 4.83 %
Rwork0.1859 51225 -
obs0.1874 53825 98.67 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 118.95 Å2 / Biso mean: 55.3065 Å2 / Biso min: 30 Å2
Refinement stepCycle: final / Resolution: 2.3→148.1 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9438 0 288 157 9883
Biso mean--48.23 48.67 -
Num. residues----1170
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A5942X-RAY DIFFRACTION11.043TORSIONAL
12B5942X-RAY DIFFRACTION11.043TORSIONAL
13C5942X-RAY DIFFRACTION11.043TORSIONAL
14D5942X-RAY DIFFRACTION11.043TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 19

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
2.3-2.340.311360.27542695283199
2.34-2.390.32951420.27552717285999
2.39-2.440.33941250.26842662278799
2.44-2.490.28991310.26032658278998
2.49-2.550.29631370.23932626276397
2.55-2.610.24071450.24012677282299
2.61-2.680.27081520.223626762828100
2.68-2.760.27491430.217827262869100
2.76-2.850.24721220.21422744286699
2.85-2.950.28761350.202926992834100
2.95-3.070.24761390.2022652279198
3.07-3.210.22031220.19692687280997
3.21-3.380.23251390.19622688282799
3.38-3.590.23071550.193927272882100
3.59-3.870.20381210.16562735285699
3.87-4.260.1731320.1562645277797
4.26-4.870.17251410.148927462887100
4.87-6.140.19831490.16672691284098
6.14-148.10.15571340.15532774290897
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)
13.2319-0.0356-0.73644.3260.12654.42050.0512-0.29490.4710.03730.1155-0.61-0.56990.695-0.14590.372-0.10990.04540.405-0.0720.419139.970612.726210.3954
24.00020.5556-0.39132.8157-0.34245.4588-0.0291-0.48250.31880.27040.0151-0.539-0.32730.8923-0.07570.2865-0.0075-0.02370.4484-0.11530.426241.30197.540813.5414
33.63871.1906-1.82144.2497-0.02125.657-0.0240.14140.2070.12080.32930.4886-0.032-0.8399-0.18580.21770.02450.01070.3690.02630.27921.29462.954515.8622
40.25280.3178-1.11711.5361-0.92514.1908-0.4374-0.5782-0.12050.79010.1934-0.15790.23481.0302-0.00930.63510.19520.01040.5829-0.01330.43229.0792.856932.8157
54.516-0.633-0.35844.06780.40916.1381-0.2192-0.3465-0.26610.58480.26370.64440.4162-1.1658-0.12260.51660.03550.18720.56790.13790.474414.3343-0.645429.0207
60.87340.5357-1.44590.36450.29776.5846-0.1427-0.0068-0.58880.0428-0.15110.68560.0378-0.93440.13670.497-0.03510.01320.7550.08150.615712.80172.33324.3167
74.4577-0.9285-1.95383.93130.80124.3868-0.2912-0.42340.5080.28070.3623-0.4711-0.61641.1322-0.10840.5169-0.1416-0.03470.6047-0.11250.459638.487349.242512.1983
82.3080.34690.13432.3837-0.45553.89760.0008-0.56940.16360.40350.0943-0.4825-0.43031.1836-0.05360.356-0.0313-0.07010.7705-0.15580.419640.10643.84814.4963
91.34930.7094-0.52853.0142-0.17455.81930.1025-0.20760.06270.07420.09940.01690.08020.1704-0.15380.29410.0762-0.00910.3964-0.01270.318222.99637.348421.2967
103.22230.2943-0.37442.89510.63175.0917-0.1243-0.3947-0.13810.30720.15410.26160.4119-0.5428-0.0990.38760.05410.05870.48040.09290.386314.376332.364229.4118
110.34320.6877-1.50930.5811-1.78535.86910.03040.7205-0.32940.13430.05270.41750.1675-1.0493-0.10620.50610.01370.00750.75730.00790.638611.966637.71625.1664
123.9034-0.3604-0.40893.3171-1.22714.67340.04870.09570.12140.12520.08310.6214-0.5796-0.5727-0.07190.45150.13280.02210.35340.04770.453334.259529.13362.79
132.5203-0.16150.84132.4106-0.54395.9996-0.03940.08440.0930.03710.24180.3001-0.683-0.8509-0.21970.44360.10960.00140.43680.10860.452732.971430.470264.1838
144.0304-1.1606-0.90881.85820.43622.83160.00380.03880.1493-0.18240.0827-0.01080.0891-0.026-0.0640.37770.00690.00790.19990.04880.257545.914719.492458.5634
150.8676-0.1715-1.80251.15880.11114.22910.02750.61870.3128-0.23240.11930.3001-0.2209-0.7808-0.26320.63330.03520.08090.48640.11810.434946.839819.064441.7878
163.750.21780.13731.9194-0.35844.74940.05880.347-0.0842-0.4625-0.1498-0.39830.56610.43770.10030.51670.07420.16980.35550.00870.446161.152915.156146.9707
172.7075-0.8907-4.4868-0.13840.77496.99370.2391-0.50380.19460.0268-0.1874-0.29150.01090.7180.06120.57840.0169-0.0090.51550.00080.639860.457918.158271.7604
184.1298-0.0482-1.2693.1726-0.57943.75250.00590.15480.3894-0.04330.1310.8662-0.1638-0.4219-0.07770.44520.06340.00810.27370.02110.574736.170365.110560.2976
193.1676-0.40580.36924.01340.57633.8848-0.04750.48490.168-0.544-0.03790.6984-0.4866-0.56940.0260.38450.0232-0.05820.42060.09390.516432.988961.204356.8609
203.1156-0.2311-1.01062.57750.78713.65870.01650.2250.2383-0.31640.10880.1297-0.24470.1806-0.12810.2956-0.0326-0.03640.22810.04480.257249.964154.068854.5188
214.77670.77010.4412.9640.24164.39150.07690.6887-0.1306-0.51210.0981-0.26170.3530.7903-0.15640.42530.05410.02980.4977-0.06610.309662.61848.140746.6962
221.1183-1.4112-2.20421.11841.90384.41710.0513-0.5887-0.00170.0936-0.033-0.01860.28330.846-0.0240.57080.007-0.00850.6122-0.03810.493561.59353.637870.7886
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'A' and (resid 700 through 731 )A700 - 731
2X-RAY DIFFRACTION2chain 'A' and (resid 732 through 790 )A732 - 790
3X-RAY DIFFRACTION3chain 'A' and (resid 791 through 853 )A791 - 853
4X-RAY DIFFRACTION4chain 'A' and (resid 854 through 892 )A854 - 892
5X-RAY DIFFRACTION5chain 'A' and (resid 893 through 978 )A893 - 978
6X-RAY DIFFRACTION6chain 'A' and (resid 979 through 1007 )A979 - 1007
7X-RAY DIFFRACTION7chain 'B' and (resid 700 through 731 )B700 - 731
8X-RAY DIFFRACTION8chain 'B' and (resid 732 through 791 )B732 - 791
9X-RAY DIFFRACTION9chain 'B' and (resid 792 through 892 )B792 - 892
10X-RAY DIFFRACTION10chain 'B' and (resid 893 through 978 )B893 - 978
11X-RAY DIFFRACTION11chain 'B' and (resid 979 through 1007 )B979 - 1007
12X-RAY DIFFRACTION12chain 'C' and (resid 700 through 731 )C700 - 731
13X-RAY DIFFRACTION13chain 'C' and (resid 732 through 752 )C732 - 752
14X-RAY DIFFRACTION14chain 'C' and (resid 753 through 853 )C753 - 853
15X-RAY DIFFRACTION15chain 'C' and (resid 854 through 892 )C854 - 892
16X-RAY DIFFRACTION16chain 'C' and (resid 893 through 978 )C893 - 978
17X-RAY DIFFRACTION17chain 'C' and (resid 979 through 1007 )C979 - 1007
18X-RAY DIFFRACTION18chain 'D' and (resid 700 through 731 )D700 - 731
19X-RAY DIFFRACTION19chain 'D' and (resid 732 through 768 )D732 - 768
20X-RAY DIFFRACTION20chain 'D' and (resid 769 through 892 )D769 - 892
21X-RAY DIFFRACTION21chain 'D' and (resid 893 through 978 )D893 - 978
22X-RAY DIFFRACTION22chain 'D' and (resid 979 through 1007 )D979 - 1007

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