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- PDB-8dus: Estrogen Receptor Alpha Ligand Binding Domain in Complex with (1'... -

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Basic information

Entry
Database: PDB / ID: 8dus
TitleEstrogen Receptor Alpha Ligand Binding Domain in Complex with (1'-(4-(2-(ethylamino)ethoxy)phenyl)-6'-hydroxy-1',4'-dihydro-2'H-spiro[cyclopropane-1,3'-isoquinolin]-2'-yl)(phenyl)methanone
ComponentsEstrogen receptor
KeywordsTRANSCRIPTION / Antiestrogen / breast cancer / alpha helical bundle / estrogen receptor
Function / homology
Function and homology information


regulation of epithelial cell apoptotic process / antral ovarian follicle growth / G protein-coupled estrogen receptor activity / regulation of branching involved in prostate gland morphogenesis / RUNX1 regulates transcription of genes involved in WNT signaling / RUNX1 regulates estrogen receptor mediated transcription / regulation of toll-like receptor signaling pathway / prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis / nuclear estrogen receptor activity / epithelial cell proliferation involved in mammary gland duct elongation ...regulation of epithelial cell apoptotic process / antral ovarian follicle growth / G protein-coupled estrogen receptor activity / regulation of branching involved in prostate gland morphogenesis / RUNX1 regulates transcription of genes involved in WNT signaling / RUNX1 regulates estrogen receptor mediated transcription / regulation of toll-like receptor signaling pathway / prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis / nuclear estrogen receptor activity / epithelial cell proliferation involved in mammary gland duct elongation / epithelial cell development / prostate epithelial cord elongation / negative regulation of smooth muscle cell apoptotic process / mammary gland branching involved in pregnancy / uterus development / vagina development / TFIIB-class transcription factor binding / androgen metabolic process / steroid hormone receptor signaling pathway / mammary gland alveolus development / estrogen receptor signaling pathway / cellular response to estrogen stimulus / estrogen response element binding / : / nuclear receptor-mediated steroid hormone signaling pathway / negative regulation of canonical NF-kappaB signal transduction / Nuclear signaling by ERBB4 / RNA polymerase II preinitiation complex assembly / protein localization to chromatin / 14-3-3 protein binding / TBP-class protein binding / nitric-oxide synthase regulator activity / steroid binding / TFAP2 (AP-2) family regulates transcription of growth factors and their receptors / ESR-mediated signaling / transcription corepressor binding / negative regulation of miRNA transcription / positive regulation of nitric-oxide synthase activity / cellular response to estradiol stimulus / transcription coregulator binding / stem cell differentiation / nuclear estrogen receptor binding / SUMOylation of intracellular receptors / euchromatin / negative regulation of DNA-binding transcription factor activity / beta-catenin binding / transcription coactivator binding / positive regulation of DNA-binding transcription factor activity / Nuclear Receptor transcription pathway / response to estrogen / Regulation of RUNX2 expression and activity / Constitutive Signaling by Aberrant PI3K in Cancer / nuclear receptor activity / male gonad development / positive regulation of nitric oxide biosynthetic process / sequence-specific double-stranded DNA binding / positive regulation of fibroblast proliferation / Ovarian tumor domain proteases / PIP3 activates AKT signaling / response to estradiol / phospholipase C-activating G protein-coupled receptor signaling pathway / positive regulation of cytosolic calcium ion concentration / ATPase binding / fibroblast proliferation / regulation of inflammatory response / PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling / DNA-binding transcription activator activity, RNA polymerase II-specific / Estrogen-dependent gene expression / transcription regulator complex / Extra-nuclear estrogen signaling / calmodulin binding / DNA-binding transcription factor activity, RNA polymerase II-specific / chromatin remodeling / RNA polymerase II cis-regulatory region sequence-specific DNA binding / DNA-binding transcription factor activity / negative regulation of gene expression / chromatin binding / regulation of DNA-templated transcription / chromatin / regulation of transcription by RNA polymerase II / protein kinase binding / positive regulation of DNA-templated transcription / Golgi apparatus / enzyme binding / negative regulation of transcription by RNA polymerase II / signal transduction / positive regulation of transcription by RNA polymerase II / protein-containing complex / zinc ion binding / nucleoplasm / identical protein binding / membrane / nucleus / plasma membrane / cytoplasm / cytosol
Similarity search - Function
Estrogen receptor / Oestrogen-type nuclear receptor final C-terminal domain / : / Oestrogen receptor / Oestrogen-type nuclear receptor final C-terminal / Estrogen receptor/oestrogen-related receptor / Nuclear hormone receptor / Nuclear hormones receptors DNA-binding region signature. / Zinc finger, nuclear hormone receptor-type / Zinc finger, C4 type (two domains) ...Estrogen receptor / Oestrogen-type nuclear receptor final C-terminal domain / : / Oestrogen receptor / Oestrogen-type nuclear receptor final C-terminal / Estrogen receptor/oestrogen-related receptor / Nuclear hormone receptor / Nuclear hormones receptors DNA-binding region signature. / Zinc finger, nuclear hormone receptor-type / Zinc finger, C4 type (two domains) / Nuclear hormone receptors DNA-binding domain profile. / c4 zinc finger in nuclear hormone receptors / Nuclear hormone receptor, ligand-binding domain / Nuclear hormone receptor-like domain superfamily / Ligand-binding domain of nuclear hormone receptor / Nuclear receptor (NR) ligand-binding (LBD) domain profile. / Ligand binding domain of hormone receptors / Zinc finger, NHR/GATA-type
Similarity search - Domain/homology
Chem-TWF / Estrogen receptor
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodX-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.9 Å
AuthorsHancock, G.R. / Young, K.S. / Hosfield, D.J. / Joiner, C. / Sullivan, E.A. / Yildz, Y. / Laine, M. / Greene, G.L. / Fanning, S.W.
Funding support1items
OrganizationGrant numberCountry
Not funded
CitationJournal: NPJ Breast Cancer / Year: 2022
Title: Unconventional isoquinoline-based SERMs elicit fulvestrant-like transcriptional programs in ER+ breast cancer cells.
Authors: Hancock, G.R. / Young, K.S. / Hosfield, D.J. / Joiner, C. / Sullivan, E.A. / Yildiz, Y. / Laine, M. / Greene, G.L. / Fanning, S.W.
History
DepositionJul 27, 2022Deposition site: RCSB / Processing site: RCSB
Revision 1.0Nov 9, 2022Provider: repository / Type: Initial release
Revision 1.1May 24, 2023Group: Database references / Category: citation / citation_author
Item: _citation.journal_abbrev / _citation.journal_id_CSD ..._citation.journal_abbrev / _citation.journal_id_CSD / _citation.journal_id_ISSN / _citation.journal_volume / _citation.page_first / _citation.page_last / _citation.pdbx_database_id_DOI / _citation.pdbx_database_id_PubMed / _citation.title / _citation.year / _citation_author.identifier_ORCID / _citation_author.name
Revision 1.2Oct 25, 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
A: Estrogen receptor
B: Estrogen receptor
E: Estrogen receptor
F: Estrogen receptor
G: Estrogen receptor
H: Estrogen receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)176,85312
Polymers174,1986
Non-polymers2,6556
Water8,809489
1
A: Estrogen receptor
B: Estrogen receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)58,9514
Polymers58,0662
Non-polymers8852
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2740 Å2
ΔGint-11 kcal/mol
Surface area20290 Å2
MethodPISA
2
E: Estrogen receptor
F: Estrogen receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)58,9514
Polymers58,0662
Non-polymers8852
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2780 Å2
ΔGint-12 kcal/mol
Surface area19990 Å2
MethodPISA
3
G: Estrogen receptor
H: Estrogen receptor
hetero molecules


Theoretical massNumber of molelcules
Total (without water)58,9514
Polymers58,0662
Non-polymers8852
Water362
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
Buried area2800 Å2
ΔGint-11 kcal/mol
Surface area20240 Å2
MethodPISA
Unit cell
Length a, b, c (Å)102.036, 57.672, 259.871
Angle α, β, γ (deg.)90.000, 100.080, 90.000
Int Tables number5
Space group name H-MC121

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Components

#1: Protein
Estrogen receptor / ER / ER-alpha / Estradiol receptor / Nuclear receptor subfamily 3 group A member 1


Mass: 29033.018 Da / Num. of mol.: 6 / Mutation: C381S, C417S, C530S, L536S
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: ESR1, ESR, NR3A1 / Production host: Escherichia coli (E. coli) / References: UniProt: P03372
#2: Chemical
ChemComp-TWF / [(1'R)-1'-{4-[2-(ethylamino)ethoxy]phenyl}-6'-hydroxy-1',4'-dihydro-2'H-spiro[cyclopropane-1,3'-isoquinolin]-2'-yl](phenyl)methanone


Mass: 442.549 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C28H30N2O3 / Feature type: SUBJECT OF INVESTIGATION
#3: Water ChemComp-HOH / water


Mass: 18.015 Da / Num. of mol.: 489 / 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: 2.16 Å3/Da / Density % sol: 43.08 %
Crystal growTemperature: 298 K / Method: vapor diffusion, hanging drop / Details: PEG 3,350, MgCl2, HEPES pH 8.0

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Data collection

DiffractionMean temperature: 100 K / Serial crystal experiment: N
Diffraction sourceSource: SYNCHROTRON / Site: APS / Beamline: 19-BM / Wavelength: 0.97 Å
DetectorType: ADSC QUANTUM 315r / Detector: CCD / Date: Sep 20, 2020
RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelengthWavelength: 0.97 Å / Relative weight: 1
ReflectionResolution: 1.9→50 Å / Num. obs: 102498 / % possible obs: 98.8 % / Redundancy: 3 % / Biso Wilson estimate: 17.82 Å2 / CC1/2: 0.993 / Rpim(I) all: 0.112 / Net I/σ(I): 748
Reflection shellResolution: 1.9→1.93 Å / Num. unique obs: 4967 / CC1/2: 0.516

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Processing

Software
NameVersionClassification
PHENIX1.18.2_3874refinement
PDB_EXTRACT3.27data extraction
HKL-3000data reduction
HKL-3000data scaling
PHENIXphasing
RefinementMethod to determine structure: MOLECULAR REPLACEMENT
Starting model: 5UFX

5ufx


Resolution: 1.9→49.91 Å / SU ML: 0.18 / Cross valid method: THROUGHOUT / σ(F): 1.96 / Phase error: 45.91 / Stereochemistry target values: ML
RfactorNum. reflection% reflection
Rfree0.3268 5051 5.08 %
Rwork0.2852 94455 -
obs0.2873 99506 84.45 %
Solvent computationShrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL
Displacement parametersBiso max: 96.93 Å2 / Biso mean: 25.5308 Å2 / Biso min: 0.04 Å2
Refinement stepCycle: final / Resolution: 1.9→49.91 Å
ProteinNucleic acidLigandSolventTotal
Num. atoms10598 0 198 489 11285
Biso mean--19.82 25.35 -
Num. residues----1366
LS refinement shell

Refine-ID: X-RAY DIFFRACTION / Rfactor Rfree error: 0 / Total num. of bins used: 30

Resolution (Å)Rfactor RfreeNum. reflection RfreeRfactor RworkNum. reflection RworkNum. reflection all% reflection obs (%)
1.9-1.920.40471260.34692563268969
1.92-1.940.3721720.34692945311780
1.94-1.970.37211560.34122963311980
1.97-1.990.39261530.32152989314282
1.99-2.020.38061450.31963144328983
2.02-2.050.36151420.32123047318983
2.05-2.080.32491570.31153048320582
2.08-2.110.34031890.30343072326184
2.11-2.140.36061920.2942981317381
2.14-2.170.31881810.26963106328784
2.17-2.210.33831560.27213004316082
2.21-2.250.3271680.2773144331284
2.25-2.30.30441730.26763003317682
2.3-2.340.29331560.26423151330783
2.34-2.390.33281570.27183008316582
2.39-2.450.3441550.26943156331184
2.45-2.510.29661670.27212995316281
2.51-2.580.32181490.27233138328785
2.58-2.650.33661590.28353146330583
2.65-2.740.28361660.2693071323783
2.74-2.840.29991710.27213126329784
2.84-2.950.33031810.2693149333084
2.95-3.090.31581810.26883174335585
3.09-3.250.37671470.28293248339586
3.25-3.450.32111790.28023287346688
3.45-3.720.32751850.27373403358891
3.72-4.090.29121950.25353517371294
4.09-4.680.312180.25793570378896
4.68-5.90.28892070.29743701390897
5.9-49.910.37231680.32593606377492
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)
12.4182-1.57480.19561.64130.24470.5220.047-0.1233-0.16650.19310.0220.2964-0.0342-0.1899-0.00820.34740.06760.23490.3007-0.03040.3591-4.546-7.147-22.688
21.05540.4791-0.23230.9550.15051.7577-0.02590.00280.0865-0.01520.00220.0356-0.0561-0.09280.01060.32230.13730.0740.43340.0620.04991.885-2.064-24.751
31.4427-0.3578-0.02131.2204-0.82162.26350.0682-0.00540.00780.0907-0.0985-0.0136-0.04610.08210.04080.24370.04280.08540.33050.03770.13869.825-4.397-26.605
40.42950.12780.11390.5461-0.00330.9942-0.0863-0.2371-0.15170.264-0.05280.0367-0.0161-0.12950.08230.42930.0274-0.01320.472-0.01090.115511.203-5.356-18.477
50.7818-0.16350.32912.07230.78921.75340.02770.141-0.0867-0.0286-0.0167-0.0820.06740.2258-0.0150.32340.0388-0.08780.4566-0.04940.060738.6024.684-27.216
60.2169-0.00390.00690.22870.03320.1866-0.0109-0.0013-0.0410.0239-0.0534-0.0052-0.01120.0056-0.05360.37690.0465-0.19440.3870.0279-0.416129.76512.034-25.266
70.50170.1753-0.26560.4024-0.27270.63260.0094-0.20350.04580.2962-0.02370.02060.0143-0.1339-0.00240.4481-0.0374-0.05060.5073-0.05020.022824.88410.503-8.969
80.3244-0.17670.19571.4198-0.81.9864-0.00230.0532-0.0222-0.06180.06220.0488-0.0802-0.07630.00860.36860.0389-0.01440.47640.11410.038728.296-3.44-29.716
90.1890.03540.13680.5009-0.42330.7951-0.1391-0.0881-0.00550.0685-0.01510.0797-0.064-0.0499-0.00750.35650.1242-0.10060.3615-0.1039-0.175923.3368.611-26.615
102.9311-0.99870.12462.5384-0.6591.63520.02-0.2359-0.25650.1462-0.02830.00690.18660.0432-0.01250.3589-0.11730.04720.37910.05490.39527.542-21.70168.533
110.25190.1001-0.03770.24660.00170.1468-0.01-0.0107-0.0104-0.0272-0.01340.04960.001-0.12910.0223-0.1791-0.454-0.00350.19190.04920.331516.233-3.26764.739
121.1650.2757-0.29790.3026-0.08460.79990.06130.07930.1757-0.04720.06570.0458-0.1060.0202-0.01390.0851-0.24110.07990.29730.00040.384516.5660.45547.962
130.9005-0.1999-0.23360.7894-0.61050.95270.0510.08260.2150.02110.0733-0.2017-0.17760.1394-0.03490.1536-0.2265-0.01690.2686-0.07280.400928.634-4.37858.895
140.36620.0936-0.03670.37340.01480.36150.0541-0.1050.00390.1052-0.0009-0.04080.05340.0882-0.0220.1485-0.18020.15080.1747-0.04240.523234.75-7.90264.549
152.35133.6248-2.70795.8288-3.59084.52090.0032-0.6170.0120.2728-0.06790.36740.16-0.22880.06260.2440.04490.15340.6841-0.0080.399215.0041.27576.243
160.8214-0.674-0.88261.86340.28832.4179-0.14990.2067-0.3548-0.32970.0282-0.47950.17610.30230.10720.3082-0.00480.20530.4124-0.04840.681958.418-3.81152.869
175.04450.0535-1.01442.4971-1.03151.08550.3871-0.56670.69370.5639-0.2088-0.1795-0.33450.0695-0.12920.2818-0.210.11570.374-0.06030.457356.15819.60767.862
180.92240.4340.03230.2666-0.12740.4303-0.02970.06480.0335-0.0337-0.0891-0.0118-0.04760.09770.0317-0.0359-0.27240.17810.2108-0.05680.484248.18412.46557.079
193.72512.3816-0.02691.7652-0.51511.1790.2799-0.44110.29690.4899-0.29550.154-0.1291-0.06670.04320.3225-0.29850.07690.4111-0.07680.494448.79714.07977.288
206.1799-0.9725-0.45474.95741.62981.80640.235-0.34630.10450.4452-0.12710.12690.0162-0.0248-0.08860.3481-0.26030.07330.4061-0.09790.190242.046.19675.056
210.77520.4499-0.22891.6944-0.67141.9181-0.14510.099-0.3727-0.21030.0065-0.25970.1479-0.08230.15980.1635-0.0570.04170.2574-0.11530.411447.282-3.52155.27
220.15020.0150.01560.4084-0.11680.17270.05210.02020.0934-0.04810.0295-0.0246-0.0748-0.01-0.0185-0.0134-0.29130.10670.35850.04630.37941.6298.53559.317
230.81290.51320.18161.10620.32651.0624-0.06680.05190.0613-0.07630.0769-0.07870.0040.11150.0120.182-0.0007-0.2590.0721-0.0238-0.198122.788-10.159109.728
240.81520.28170.55450.4076-0.01451.024-0.0354-0.00160.0144-0.0143-0.0576-0.0033-0.0088-0.0188-0.0264-0.0227-0.0986-0.14380.1214-0.0893-0.455521.232-5.023102.536
250.29450.1467-0.06950.3986-0.22280.8443-0.0481-0.04020.06660.04640.02910.009-0.06980.09150.044-0.1043-0.17590.1182-0.16420.2859-0.194517.814-0.807112.827
262.73851.9947-0.3164.6829-0.76473.18390.1034-0.0150.10280.1283-0.01320.0562-0.13450.0248-0.06670.087-0.03270.06650.04930.0259-0.054910.8210.127120.84
270.8070.27260.08520.6558-0.16411.8708-0.08360.068-0.0549-0.11780.09240.0589-0.0265-0.059-0.0860.0466-0.0850.0756-0.01280.02740.00467.682-8.461105.575
280.74520.3632-0.28380.9634-0.74552.5475-0.00580.0918-0.189-0.0780.08660.08630.0449-0.0701-0.02970.0007-0.1525-0.0355-0.0212-0.04960.10651.423-13.886100.082
291.24240.6765-0.25741.4034-0.46310.8108-0.0182-0.04290.12030.0374-0.0578-0.0101-0.08480.0551-0.0104-0.2361-0.0606-0.0488-0.0401-0.15710.03945.517-0.924111.771
300.5289-0.7342-0.82422.07912.57544.28470.04170.04660.0927-0.39730.0858-0.0261-0.20760.1072-0.11490.4001-0.0949-0.04280.62460.06750.180323.328-0.51992.391
311.08590.0544-0.13532.6017-1.08731.2735-0.0459-0.038-0.20480.0903-0.04040.01040.0842-0.04950.0239-0.00810.01320.06150.0392-0.00860.2159-19.54.847112.242
320.707-0.426-0.00610.840.17060.27760.09930.16320.1239-0.1658-0.10790.1119-0.0052-0.01620.0232-0.1340.24960.1415-0.1794-0.1726-0.0892-10.49912.898107.841
330.4263-0.3024-0.18910.99140.20960.93270.12510.167-0.0215-0.2282-0.0907-0.00250.00420.03940.01130.04350.15490.0653-0.0164-0.15740.2022-6.9343.405104.574
340.1506-0.3709-0.11941.03810.47490.6766-0.023-0.02520.02410.1759-0.1014-0.0262-0.0895-0.0440.0361-0.05080.01510.0731-0.0823-0.09220.0987-6.2793.089114.082
Refinement TLS group
IDRefine-IDRefine TLS-IDSelection detailsAuth asym-IDAuth seq-ID
1X-RAY DIFFRACTION1( CHAIN A AND RESID 308:363 )A308 - 363
2X-RAY DIFFRACTION2( CHAIN A AND RESID 364:420 )A364 - 420
3X-RAY DIFFRACTION3( CHAIN A AND RESID 421:465 )A421 - 465
4X-RAY DIFFRACTION4( CHAIN A AND RESID 466:548 )A466 - 548
5X-RAY DIFFRACTION5( CHAIN B AND RESID 306:341 )B306 - 341
6X-RAY DIFFRACTION6( CHAIN B AND RESID 342:405 )B342 - 405
7X-RAY DIFFRACTION7( CHAIN B AND RESID 406:437 )B406 - 437
8X-RAY DIFFRACTION8( CHAIN B AND RESID 438:496 )B438 - 496
9X-RAY DIFFRACTION9( CHAIN B AND RESID 497:549 )B497 - 549
10X-RAY DIFFRACTION10( CHAIN E AND RESID 309:321 )E309 - 321
11X-RAY DIFFRACTION11( CHAIN E AND RESID 322:394 )E322 - 394
12X-RAY DIFFRACTION12( CHAIN E AND RESID 395:420 )E395 - 420
13X-RAY DIFFRACTION13( CHAIN E AND RESID 421:465 )E421 - 465
14X-RAY DIFFRACTION14( CHAIN E AND RESID 466:526 )E466 - 526
15X-RAY DIFFRACTION15( CHAIN E AND RESID 527:548 )E527 - 548
16X-RAY DIFFRACTION16( CHAIN F AND RESID 306:321 )F306 - 321
17X-RAY DIFFRACTION17( CHAIN F AND RESID 322:341 )F322 - 341
18X-RAY DIFFRACTION18( CHAIN F AND RESID 342:394 )F342 - 394
19X-RAY DIFFRACTION19( CHAIN F AND RESID 395:420 )F395 - 420
20X-RAY DIFFRACTION20( CHAIN F AND RESID 421:438 )F421 - 438
21X-RAY DIFFRACTION21( CHAIN F AND RESID 439:496 )F439 - 496
22X-RAY DIFFRACTION22( CHAIN F AND RESID 497:548 )F497 - 548
23X-RAY DIFFRACTION23( CHAIN G AND RESID 308:341 )G308 - 341
24X-RAY DIFFRACTION24( CHAIN G AND RESID 342:371 )G342 - 371
25X-RAY DIFFRACTION25( CHAIN G AND RESID 372:420 )G372 - 420
26X-RAY DIFFRACTION26( CHAIN G AND RESID 421:438 )G421 - 438
27X-RAY DIFFRACTION27( CHAIN G AND RESID 439:465 )G439 - 465
28X-RAY DIFFRACTION28( CHAIN G AND RESID 466:496 )G466 - 496
29X-RAY DIFFRACTION29( CHAIN G AND RESID 497:528 )G497 - 528
30X-RAY DIFFRACTION30( CHAIN G AND RESID 529:549 )G529 - 549
31X-RAY DIFFRACTION31( CHAIN H AND RESID 306:342 )H306 - 342
32X-RAY DIFFRACTION32( CHAIN H AND RESID 343:420 )H343 - 420
33X-RAY DIFFRACTION33( CHAIN H AND RESID 421:465 )H421 - 465
34X-RAY DIFFRACTION34( CHAIN H AND RESID 466:549 )H466 - 549

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