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- PDB-7ky0: Inactive conformation of EGFR (T790M/V948R) kinase in complex wit... -

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Basic information

Entry
Database: PDB / ID: 7ky0
TitleInactive conformation of EGFR (T790M/V948R) kinase in complex with BI-4020
ComponentsEpidermal growth factor receptor
KeywordsTRANSFERASE/TRANSFERASE INHIBITOR / EGFR / kinase / inhibitor / macrocycle / 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-XA4 / Epidermal growth factor receptor
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.1 Å
AuthorsBeyett, T.S. / Eck, M.J.
Funding support United States, 2items
OrganizationGrant numberCountry
National Institutes of Health/National Cancer Institute (NIH/NCI)5R01CA116020-14 United States
National Institutes of Health/National Cancer Institute (NIH/NCI) United States
CitationJournal: Chemmedchem / Year: 2024
Title: Structural Analysis of the Macrocyclic Inhibitor BI-4020 Binding to EGFR Kinase.
Authors: Beyett, T.S. / Rana, J.K. / Schaeffner, I.K. / Heppner, D.E. / Eck, M.J.
History
DepositionDec 6, 2020Deposition site: RCSB / Processing site: RCSB
Revision 1.0Jan 19, 2022Provider: repository / Type: Initial release
Revision 1.1Oct 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
Revision 1.2May 29, 2024Group: 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.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year

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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)153,0698
Polymers150,8984
Non-polymers2,1714
Water0
1
D: Epidermal growth factor receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,2672
Polymers37,7251
Non-polymers5431
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
2
A: Epidermal growth factor receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,2672
Polymers37,7251
Non-polymers5431
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
3
B: Epidermal growth factor receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,2672
Polymers37,7251
Non-polymers5431
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
4
C: Epidermal growth factor receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)38,2672
Polymers37,7251
Non-polymers5431
Water0
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Unit cell
Length a, b, c (Å)70.221, 100.729, 86.789
Angle α, β, γ (deg.)90.000, 101.070, 90.000
Int Tables number4
Space group name H-MP1211
Noncrystallographic symmetry (NCS)NCS domain:
IDEns-IDDetails
11(chain A and (resid 1101 through 747 or resid 756 through 1007))
21(chain B and (resid 1101 or resid 701 through 747...
31(chain C and (resid 1101 or resid 701 through 747...
41(chain D and (resid 1101 or resid 701 through 747...

NCS domain segments:

Ens-ID: 1

Dom-IDComponent-IDBeg auth comp-IDBeg label comp-IDEnd auth comp-IDEnd label comp-IDEnd label seq-IDSelection detailsAuth asym-IDLabel asym-IDAuth seq-IDLabel seq-ID
11XA4XA4LEULEU56(chain A and (resid 1101 through 747 or resid 756 through 1007))AF - B1101 - 747
12ASNASNMETMET(chain A and (resid 1101 through 747 or resid 756 through 1007))AB756 - 100765 - 316
21XA4XA4XA4XA4(chain B and (resid 1101 or resid 701 through 747...BG1101
22GLNGLNLEULEU(chain B and (resid 1101 or resid 701 through 747...BC701 - 74710 - 56
23ASNASNGLUGLU(chain B and (resid 1101 or resid 701 through 747...BC756 - 98565 - 294
24SERSERMETMET(chain B and (resid 1101 or resid 701 through 747...BC991 - 1007300 - 316
31XA4XA4XA4XA4(chain C and (resid 1101 or resid 701 through 747...CH1101
32GLNGLNLEULEU(chain C and (resid 1101 or resid 701 through 747...CD701 - 74710 - 56
33ASNASNGLUGLU(chain C and (resid 1101 or resid 701 through 747...CD756 - 98565 - 294
34SERSERMETMET(chain C and (resid 1101 or resid 701 through 747...CD991 - 1007300 - 316
41XA4XA4XA4XA4(chain D and (resid 1101 or resid 701 through 747...DE1101
42GLNGLNLEULEU(chain D and (resid 1101 or resid 701 through 747...DA701 - 74710 - 56
43ASNASNGLUGLU(chain D and (resid 1101 or resid 701 through 747...DA756 - 98565 - 294
44SERSERMETMET(chain D and (resid 1101 or resid 701 through 747...DA991 - 1007300 - 316

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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-XA4 / (20R)-10,15,20-trimethyl-2-[(4-methylpiperazin-1-yl)methyl]-18,19,20,21-tetrahydro-15H,17H-12,8-(metheno)pyrazolo[3',4':2,3][1,5,10,12]oxatriazacycloheptadecino[12,11-a]benzimidazol-7(6H)-one


Mass: 542.675 Da / Num. of mol.: 4 / Source method: obtained synthetically / Formula: C30H38N8O2 / 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: 2 Å3/Da / Density % sol: 38.38 % / Mosaicity: 0.351 °
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-C / Wavelength: 0.9788 Å
DetectorType: DECTRIS EIGER X 16M / Detector: PIXEL / Date: Aug 7, 2020
RadiationMonochromator: Double Crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.9788 Å / Relative weight: 1
ReflectionResolution: 3.1→68.92 Å / Num. obs: 21029 / % possible obs: 97.4 % / Redundancy: 4 % / Biso Wilson estimate: 35.58 Å2 / Rpim(I) all: 0.19 / Rrim(I) all: 0.372 / Net I/σ(I): 3 / Num. measured all: 83654
Reflection shell

Diffraction-ID: 1 / Redundancy: 3.7 %

Resolution (Å)Mean I/σ(I) obsNum. measured allNum. unique obsRpim(I) allRrim(I) all% possible all
3.1-3.160.6379210220.4540.91393.7
8.42-68.9311.5394910630.0530.10794.9

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Processing

Software
NameVersionClassification
xia2data scaling
PHENIX1.18.2_3874refinement
PDB_EXTRACT3.27data extraction
xia2data reduction
PHASERphasing
Cootmodel building
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5d41

5d41


Resolution: 3.1→68.92 Å / SU ML: 0.56 / Cross valid method: THROUGHOUT / σ(F): 1.35 / Phase error: 31.3 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.2925 1049 5.01 %
Rwork0.2376 19901 -
obs0.2404 20950 97.08 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 114.39 Å2 / Biso mean: 46.3299 Å2 / Biso min: 15.65 Å2
Refinement stepCycle: final / Resolution: 3.1→68.92 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms9331 0 160 0 9491
Biso mean--37.83 --
Num. residues----1156
Refine LS restraints
Refine-IDTypeDev idealNumber
X-RAY DIFFRACTIONf_bond_d0.0119694
X-RAY DIFFRACTIONf_angle_d1.33613119
X-RAY DIFFRACTIONf_dihedral_angle_d21.4173686
X-RAY DIFFRACTIONf_chiral_restr0.0661444
X-RAY DIFFRACTIONf_plane_restr0.0081630
Refine LS restraints NCS
Ens-IDDom-IDAuth asym-IDNumberRefine-IDRmsType
11A5681X-RAY DIFFRACTION10.245TORSIONAL
12B5681X-RAY DIFFRACTION10.245TORSIONAL
13C5681X-RAY DIFFRACTION10.245TORSIONAL
14D5681X-RAY DIFFRACTION10.245TORSIONAL
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 7

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
3.1-3.270.37031490.29722651280092
3.27-3.470.35091330.30762900303398
3.47-3.740.31391500.27942889303999
3.74-4.120.32261790.26352839301899
4.12-4.710.26691520.19622820297297
4.71-5.940.25051440.19962878302298
5.94-68.920.24061420.19342924306697
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)
11.43210.1958-0.89080.9843-0.50113.6499-0.0812-0.2294-0.5035-0.1786-0.17590.08770.47360.2820.26660.6684-0.1572-0.02330.08890.08140.4751-36.2812-32.1966-20.8016
20.24510.59870.24692.29870.97091.85370.19820.43440.0361-0.1195-0.16870.08140.4334-0.0725-0.11710.29320.0799-0.05190.35370.16650.3703-30.0986-39.5471-28.4018
31.00710.203-0.35471.7448-0.22290.9514-0.12170.22980.03020.41750.66570.0112-0.0112-0.2477-0.29950.32920.0762-0.02430.26930.12390.412-31.9294-23.2524-31.4491
41.52520.11840.54031.39650.05343.5882-0.0118-0.0875-0.26460.3112-0.0490.19320.4888-0.3402-0.01730.19810.06440.00790.16380.0440.2976-24.8713-24.928-44.2808
52.2338-0.2760.54813.28760.97044.017-0.08190.16920.4575-0.13730.0855-0.16530.42740.4647-0.16890.2061-0.1070.01120.3177-0.05750.21-17.93-15.2557-50.5931
60.29030.3531-0.69944.2711-0.80431.58830.0934-0.12140.02931.451-0.19630.5508-0.47260.12770.25980.46220.060.34730.55010.23090.6763-27.2563-5.4058-30.9656
72.5064-0.5184-0.73242.93240.84912.9344-0.3381-0.0010.2655-0.357-0.08670.145-0.4698-0.28790.40790.33450.0799-0.10560.25470.04760.3894-37.4119-1.1306-13.5346
84.1954-1.43660.59974.2985-0.77643.1590.1671-0.2957-0.41830.35310.41780.0332-0.2826-0.28150.11960.2750.24220.259-0.236-0.11380.4666-32.5119-12.4214-6.4053
91.7930.31930.28562.45850.12333.28130.20030.05280.04520.1906-0.21880.5031-0.4896-0.66440.06090.21620.00830.0130.3645-0.02730.2301-26.5066-9.57936.7967
100.9209-0.84221.08414.24690.84952.62340.02110.0758-0.22470.2797-0.0014-0.07370.66170.2027-0.03510.3444-0.05790.05070.3403-0.01480.3363-19.2515-20.27376.3529
112.60120.41231.3293.2893-0.51623.5314-0.02510.1022-0.22810.2532-0.3812-0.02541.28030.19890.35570.6647-0.06930.08770.32630.0050.3943-2.2328-32.1299-20.4795
122.980.4317-2.48095.0082-2.29514.44980.10440.2704-0.6524-1.23290.4219-0.0930.96910.2662-0.04580.76290.267-0.30310.513-0.00870.47167.0606-36.0427-27.233
131.75320.3619-0.23671.90420.67233.04320.02520.47180.2111-0.03040.38610.10450.27870.3269-0.28560.34190.04230.03670.64570.06910.38137.472-21.9804-38.6786
141.2805-0.17810.65722.54580.75340.8558-0.31670.83690.2522-0.46620.5255-0.3995-0.26980.4846-0.01920.3181-0.1744-0.0631.2090.13150.389511.6632-15.7522-50.3761
150.96660.1766-0.74811.8257-0.81752.6809-0.3687-0.32591.05750.7724-0.3348-0.4687-0.46620.71180.47870.45430.0477-0.1310.813-0.09390.57649.3646-6.1504-26.7395
162.57041.9195-1.34952.6739-0.99752.8340.6645-0.784-0.23720.1711-0.3856-0.0672-0.54960.913-0.13520.5072-0.1029-0.1050.60770.04020.3549-2.0818-4.9552-9.6138
173.73130.94392.41972.66850.75625.1186-0.2748-0.14650.69110.0289-0.42470.082-0.283-0.08770.61250.3792-0.0976-0.09360.27140.14330.3254-3.5262-5.6411-12.3383
184.3375-0.03981.35756.2039-1.16831.25860.2906-0.53571.0156-0.16170.01050.4392-0.5921-0.1622-0.33470.71980.01190.09510.4108-0.12680.26837.8303-1.3018-6.3758
193.6908-3.28591.04246.2665-0.81933.72430.4949-0.4042-0.15130.05170.04110.74340.0619-0.201-0.49780.3445-0.1747-0.01180.46650.0420.32541.9575-21.4518-0.335
202.2078-0.0648-0.43460.5903-0.84192.0720.2131-0.1702-0.1295-0.3429-0.0867-0.0673-0.0302-0.5601-0.0220.3612-0.0228-0.0240.33650.13250.25913.8153-16.9881.0497
210.76680.01270.10030.88320.42020.86870.47640.15110.4929-0.5598-0.8987-0.20890.3218-0.5430.4280.58810.10450.00360.4365-0.01210.384810.4501-4.780613.0344
220.9825-0.4048-0.93361.70890.0852.23420.1743-0.38530.15740.82470.01320.11640.23450.3421-0.09370.4398-0.14210.17680.4759-0.01140.265813.9972-18.326117.6918
235.36330.8519-3.32941.4134-0.88654.1504-0.7549-0.3606-0.75760.0651-0.3155-0.25251.06250.2181-0.15480.7319-0.1896-0.07740.66390.12260.168623.383-27.04346.1652
240.8843-0.28051.9890.1586-0.50054.64790.10840.1070.0607-0.48830.23210.2191.3050.2079-0.370.61350.0189-0.08490.60870.00020.702610.958-31.4265-6.4307
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1chain 'D' and (resid 700 through 739 )D700 - 739
2X-RAY DIFFRACTION2chain 'D' and (resid 740 through 768 )D740 - 768
3X-RAY DIFFRACTION3chain 'D' and (resid 769 through 810 )D769 - 810
4X-RAY DIFFRACTION4chain 'D' and (resid 811 through 928 )D811 - 928
5X-RAY DIFFRACTION5chain 'D' and (resid 929 through 978 )D929 - 978
6X-RAY DIFFRACTION6chain 'D' and (resid 979 through 1007 )D979 - 1007
7X-RAY DIFFRACTION7chain 'A' and (resid 701 through 768 )A701 - 768
8X-RAY DIFFRACTION8chain 'A' and (resid 769 through 810 )A769 - 810
9X-RAY DIFFRACTION9chain 'A' and (resid 811 through 928 )A811 - 928
10X-RAY DIFFRACTION10chain 'A' and (resid 929 through 1007 )A929 - 1007
11X-RAY DIFFRACTION11chain 'B' and (resid 700 through 754 )B700 - 754
12X-RAY DIFFRACTION12chain 'B' and (resid 755 through 786 )B755 - 786
13X-RAY DIFFRACTION13chain 'B' and (resid 787 through 908 )B787 - 908
14X-RAY DIFFRACTION14chain 'B' and (resid 909 through 978 )B909 - 978
15X-RAY DIFFRACTION15chain 'B' and (resid 979 through 1007 )B979 - 1007
16X-RAY DIFFRACTION16chain 'C' and (resid 700 through 731 )C700 - 731
17X-RAY DIFFRACTION17chain 'C' and (resid 732 through 755 )C732 - 755
18X-RAY DIFFRACTION18chain 'C' and (resid 756 through 786 )C756 - 786
19X-RAY DIFFRACTION19chain 'C' and (resid 787 through 810 )C787 - 810
20X-RAY DIFFRACTION20chain 'C' and (resid 811 through 853 )C811 - 853
21X-RAY DIFFRACTION21chain 'C' and (resid 854 through 892 )C854 - 892
22X-RAY DIFFRACTION22chain 'C' and (resid 893 through 960 )C893 - 960
23X-RAY DIFFRACTION23chain 'C' and (resid 961 through 978 )C961 - 978
24X-RAY DIFFRACTION24chain 'C' and (resid 979 through 1007 )C979 - 1007

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